Database Repository Iso.m/z Exp.m/z Theo.m/z z Theo.MM(Da) IPMD(ppm) Protein ID Proteion Name Accession Number Sequence Seq.Length Function PTMs P_Score PTM Score Proteoform Score Seq.Coverage uniprot_mouse_length brain_HCD 614.25354 618.969971 618.975426 21 12971.47405 -8.813430462 4EBP2_MOUSE Eukaryotic translation initiation factor 4E-binding protein 2 {ECO:0000250|UniProtKB:Q13542}; Short=4E-BP2 {ECO:0000250|UniProtKB:Q13542}; Short=eIF4E-binding protein 2 {ECO:0000250|UniProtKB:Q13542};AltName: Full=Phosphorylated heat- and acid-stable protein regulated by insulin 2 {ECO:0000303|PubMed:8939971}; Short=PHAS-II {ECO:0000303|PubMed:8939971} P70445 MSASAGGSHQPSQSRAIPTRTVAISDAAQLPQDYCTTPGGTLFSTTPGGTRIIYDRKFLLDRRNSPMAQTPPCHLPNIPGVTSPGALIEDSKVEVNNLNNLNNHDRKHAVGDEAQFEMDI 120 "FUNCTION: Repressor of translation initiation involved in synaptic plasticity, learning and memory formation (PubMed:16237163, PubMed:17029989). Regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form of EIF4EBP2 competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. In contrast, hyperphosphorylated form dissociates from EIF4E, allowing interaction between EIF4G1/EIF4G3 and EIF4E, leading to initiation of translation (PubMed:17029989, PubMed:20347422, PubMed:23172145). EIF4EBP2 is enriched in brain and acts as a regulator of synapse activity and neuronal stem cell renewal via its ability to repress translation initiation (PubMed:20347422, PubMed:24139800, PubMed:23172145). Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways (PubMed:8939971). {ECO:0000250|UniProtKB:Q13542, ECO:0000269|PubMed:16237163, ECO:0000269|PubMed:17029989, ECO:0000269|PubMed:20347422, ECO:0000269|PubMed:23172145, ECO:0000269|PubMed:24139800, ECO:0000269|PubMed:8939971}." T37P 595.8 "T,3;" 78 100 uniprot_mouse_length brain_HCD 544.7461548 545.66748 545.669637 25 13609.72967 -3.952082183 ADX_MOUSE "Adrenodoxin, mitochondrial;AltName: Full=Adrenal ferredoxin;AltName: Full=Ferredoxin-1;Flags: Precursor" P46656 SSSEDKITVHFKNRDGETLTTKGKIGDSLLDVVIENNLDIDGFGACEGTLACSTCHLIFEDHIYEKLDAITDEENDMLDLAFGLTDRSRLGCQVCLTKAMDNMTVRVPEAVADVRQSVDMSKNS 124 "FUNCTION: Essential for the synthesis of various steroid hormones, participates in the reduction of mitochondrial cytochrome P450 for steroidogenesis. Transfers electrons from adrenodoxin reductase to CYP11A1, a cytochrome P450 that catalyzes cholesterol side-chain cleavage (By similarity). {ECO:0000250}." null 2415.48 null null 100 uniprot_mouse_length brain_HCD 592.4051514 592.988586 592.986391 33 19524.52861 3.702320685 ARPC4_MOUSE Actin-related protein 2/3 complex subunit 4;AltName: Full=Arp2/3 complex 20 kDa subunit; Short=p20-ARC P59999 TATLRPYLSAVRATLQAALCLENFSSQVVERHNKPEVEVRSSKELLLQPVTISRNEKEKVLIEGSINSVRVSIAVKQADEIEKILCHKFMRFMMMRAENFFILRRKPVEGYDISFLITNFHTEQMYKHKLVDFVIHFMEEIDKEISEMKLSVNARARIVAEEFLKNF 167 FUNCTION: Functions as actin-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the mother actin filament (By similarity). {ECO:0000250}. null 762.94 null null 100 uniprot_mouse_length brain_HCD 540.6661377 540.959839 540.951846 30 16190.53911 14.77556135 ARPC5_MOUSE Actin-related protein 2/3 complex subunit 5;AltName: Full=Arp2/3 complex 16 kDa subunit; Short=p16-ARC Q9CPW4 SKNTVSSARFRKVDVDEYDENKFVDEEDGGDGQAGPDEGEVDSCLRQGNMTAALQAALKNPPINTKSQAVKDRAGSIVLKVLISFKANDIEKAVQSLDKNGVDLLMKYIYKGFESPSDNSSAVLLQWHEKALAAGGVGSIVRVLTARKTV 150 FUNCTION: Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. {ECO:0000250}. S1Ac 1934.59 "S,127;" 151 100 uniprot_mouse_length brain_HCD 623.8604126 626.903687 626.897732 28 17515.11587 9.498396841 ATRAP_MOUSE Type-1 angiotensin II receptor-associated protein;AltName: Full=AT1 receptor-associated protein Q9WVK0 MELPAVNLKVILLVHWLLTTWGCLVFSSSYAWGNFTILALGVWAVAQRDSIDAIGMFLGGLVATIFLDIIYISIFYSSVATGDTGRFGAGMAILSLLLKPFSCCLVYHMHRERGGELPLRPDFFGPSQEHSAYQTIDSSSDAAADPFASLENKGQAVPRGY 161 "FUNCTION: Appears to be a negative regulator of type-1 angiotensin II receptor-mediated signaling by regulating receptor internalisation as well as mechanism of receptor desensitization such as phosphorylation. Induces also a decrease in angiotensin II-stimulated transcriptional activity. May play a role of negative regulator in cardiomyocyte hypertrophy induced by angiotensin II through an inhibition of p38 mitogen-activated protein kinase pathway. {ECO:0000269|PubMed:10358057, ECO:0000269|PubMed:15757644}." null 3728.98 null null 100 uniprot_mouse_length brain_HCD 614.25354 613.781738 613.782924 19 11636.86613 -1.931821013 B2MG_MOUSE Beta-2-microglobulin;Flags: Precursor P01887 IQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEIQMLKNGKKIPKVEMSDMSFSKDWSFYILAHTEFTPTETDTYACRVKHASMAEPKTVYWDRDM 99 FUNCTION: Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system. null 461.16 null null 100 uniprot_mouse_length brain_HCD 656.4720459 655.894165 655.897404 27 17672.21101 -4.938212772 BTG2_MOUSE Protein BTG2;AltName: Full=BTG family member 2;AltName: Full=NGF-inducible protein TIS21 Q04211 MSHGKRTDMLPEIAAAVGFLSSLLRTRGCVSEQRLKVFSRALQDALTDHYKHHWFPEKPSKGSGYRCIRINHKMDPIISKVASQIGLSQPQLHRLLPSELTLWVDPYEVSYRIGEDGSICVLYEEAPVAASYGLLTCKNQMMLGRSSPSKNYVMAVSS 158 FUNCTION: Anti-proliferative protein; the function is mediated by association with deadenylase subunits of the CCR4-NOT complex. Activates mRNA deadenylation in a CNOT6 and CNOT7-dependent manner. In vitro can inhibit deadenylase activity of CNOT7 and CNOT8. Involved in cell cycle regulation. Could be involved in the growth arrest and differentiation of the neuronal precursors. Modulates transcription regulation mediated by ESR1. Involved in mitochondrial depolarization and neurite outgrowth (By similarity). {ECO:0000250}. null 1536.91 null null 100 uniprot_mouse_length brain_HCD 542.0778809 542.866272 542.86398 22 11914.9978 4.222001718 CASP3_MOUSE Caspase-3; Short=CASP-3; EC=3.4.22.56;AltName: Full=Apopain;AltName: Full=Cysteine protease CPP32; Short=CPP-32;AltName: Full=LICE;AltName: Full=Protein Yama;AltName: Full=SREBP cleavage activity 1; Short=SCA-1;Contains: Caspase-3 subunit p17;Contains: Caspase-3 subunit p12;Flags: Precursor P70677 SGTDEEMACQKIPVEADFLYAYSTAPGYYSWRNSKDGSWFIQSLCSMLKLYAHKLEFMHILTRVNRKVATEFESFSLDSTFHAKKQIPCIVSMLTKELYFYH 102 "FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop- helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Triggers cell adhesion in sympathetic neurons through RET cleavage (By similarity). Cleaves IL-1 beta between an Asp and an Ala, releasing the mature cytokine which is involved in a variety of inflammatory processes. {ECO:0000250}." null 604.88 null null 100 uniprot_mouse_length brain_HCD 660.8756104 659.197327 659.198423 28 18419.53449 -1.663140878 CBLN3_MOUSE Cerebellin-3;Flags: Precursor Q9JHG0 QEGSEPVLLEGECLVVCEPGRPTAGGPGGAALGEAPPGRVAFAAVRSHHHEPAGETGNGTSGAIYFDQVLVNEGEGFDRTSGCFVAPVRGVYSFRFHVVKVYNRQTVQVSLMLNTWPVISAFANDPDVTREAATSSVLLPLDPGDRVSLRLRRGNLLGGWKYSSFSGFLIFPL 173 FUNCTION: May be involved in synaptic functions in the CNS. null 5783.33 null null 100 uniprot_mouse_length brain_HCD 658.1266479 653.516968 653.508452 34 22173.26224 13.03085432 CBX5_MOUSE Chromobox protein homolog 5;AltName: Full=Heterochromatin protein 1 homolog alpha; Short=HP1 alpha Q61686 MGKKTKRTADSSSSEDEEEYVVEKVLDRRMVKGQVEYLLKWKGFSEEHNTWEPEKNLDCPELISEFMKKYKKMKEGENNKPREKSEGNKRKSSFSNSADDIKSKKKREQSNDIARGFERGLEPEKIIGATDSCGDLMFLMKWKDTDEADLVLAKEANVKCPQIVIAFYEERLTWHAYPEDAENKEKESAKS 191 "FUNCTION: Component of heterochromatin that recognizes and binds histone H3 tails methylated at 'Lys-9' (H3K9me), leading to epigenetic repression. In contrast, it is excluded from chromatin when 'Tyr-41' of histone H3 is phosphorylated (H3Y41ph). Can interact with lamin-B receptor (LBR). This interaction can contribute to the association of the heterochromatin with the inner nuclear membrane. Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins (By similarity). {ECO:0000250}." null 2362.76 null null 100 uniprot_mouse_length brain_HCD 542.0778809 540.725403 540.724612 35 18881.34248 1.462541215 CCD12_MOUSE Coiled-coil domain-containing protein 12 Q8R344 MAAAPAGVGRLEEEALRRKERLKALREKTGRKDREDGEPQTKQLREEGEEVGKHRGLRLRNYVPEDEDLKRRRVPQAKPVAVEEKVKEQLEAAKPEPVIEEVDLANLAPRKPDWDLKRDVAKKLEKLEKRTQRAIAELIRERLKGQEDSLASAVDATTGQEACDSD 166 "-------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License--------------------------------------------------" null 1464.03 null null 100 uniprot_mouse_length brain_HCD 575.8931885 575.893188 575.888324 33 18961.29315 8.446909513 CCD12_MOUSE Coiled-coil domain-containing protein 12 Q8R344 MAAAPAGVGRLEEEALRRKERLKALREKTGRKDREDGEPQTKQLREEGEEVGKHRGLRLRNYVPEDEDLKRRRVPQAKPVAVEEKVKEQLEAAKPEPVIEEVDLANLAPRKPDWDLKRDVAKKLEKLEKRTQRAIAELIRERLKGQEDSLASAVDATTGQEACDSD 166 "-------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License--------------------------------------------------" S165P 1696.55 "S,125;" 161 100 uniprot_mouse_length brain_HCD 544.1306152 544.28363 544.287666 30 16290.61416 -7.41451471 CD3Z_MOUSE T-cell surface glycoprotein CD3 zeta chain;AltName: Full=T-cell receptor T3 zeta chain;AltName: CD_antigen=CD247;Flags: Precursor P24161 QSFGLLDPKLCYLLDGILFIYGVIITALYLRAKFSRSAETAANLQDPNQLYNELNLGRREEYDVLEKKRARDPEMGGKQQRRRNPQEGVYNALQKDKMAEAYSEIGTKGERRRGKGHDGLYQGLSTATKDTYDALHMQTLAPR 143 FUNCTION: Probable role in assembly and expression of the TCR complex as well as signal transduction upon antigen triggering. null 6577.1 null null 100 uniprot_mouse_length brain_HCD 575.8931885 575.453369 575.454184 35 20094.87319 -1.416028239 CENPR_MOUSE Centromere protein R; Short=CENP-R;AltName: Full=Nuclear receptor-interacting factor 3 Q9CQ82 MPVKRSLKLDDQFEKNSFSPSKIVRKKSITAYSPTTGTYQLSPFSSPATPKEQEHRNGPSNETRKRSNLSSPVRQESTVKDRDGFMVLLSKIEISSEKTMEIMKNLSSIQALEGNRQLEDLIGVSLVPCSLKSEARKTKELMTKVIKQKLFEKKKSRITPKDHHLDSFEFLKAILN 176 "FUNCTION: Transcription coregulator that can have both coactivator and corepressor functions. Involved in the coactivation of nuclear receptors for retinoid X (RXRs) and thyroid hormone (TRs) in a ligand-dependent fashion. In contrast, it does not coactivate nuclear receptors for retinoic acid, vitamin D, progesterone receptor, nor glucocorticoid. Acts as a coactivator for estrogen receptor alpha. Acts as a transcriptional corepressor via its interaction with the NFKB1 NF-kappa-B subunit, possibly by interfering with the transactivation domain of NFKB1. Induces apoptosis in breast cancer cells, but not in other cancer cells, via a caspase-2 mediated pathway that involves mitochondrial membrane permeabilization but does not require other caspases. May also act as an inhibitor of cyclin A-associated kinase. Also acts a component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex (By similarity). {ECO:0000250}." S17P 1638.93 "S,26;" 166 100 uniprot_mouse_length brain_HCD 616.8864136 616.854492 616.848957 32 19696.14433 8.973327161 CETN2_MOUSE Centrin-2;AltName: Full=Caltractin isoform 1 Q9R1K9 ASNFKKTTMASSAQRKRMSPKPELTEDQKQEIREAFDLFDADGTGTIDIKELKVAMRALGFEPKKEEIKKMISEIDKEGTGKMNFSDFLTVMTQKMSEKDTKEEILKAFKLFDDDETGKISFKNLKRVAKELGENLTDEELQEMIDEADRDGDGEVNEQEFLRIMKKTSLY 171 FUNCTION: Plays a fundamental role in microtubule organizing center structure and function. Required for centriole duplication and correct spindle formation. Has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CCP110 (By similarity). {ECO:0000250}. A1Ac 8710.87 "A,347;" 284 100 uniprot_mouse_length brain_HCD 614.25354 611.350037 611.348043 31 18910.76946 3.261024741 CGBP1_MOUSE CGG triplet repeat-binding protein 1; Short=CGG-binding protein 1;AltName: Full=20 kDa CGG-binding protein;AltName: Full=p20-CGGBP DNA-binding protein Q8BHG9 MERFVVTAPPARNRSKTALYVTPLDRVTEFGGELHEDGGKLFCTSCNVVLNHVRKSAISDHLKSKTHTKRKAEFEEQNVRKKQRPLTASLQCNSPAQTEKASVIQDFVKMCLEANIPLEKADHPAVRAFLSRHVKNGGSIPKSDQLRRAYLPDGYENENQLLSSQDC 167 FUNCTION: Binds to nonmethylated 5'-d(CGG)(n)-3' trinucleotide repeats in the FMR1 promoter. May play a role in regulating FMR1 promoter (By similarity). {ECO:0000250}. S56PS164P 1461.44 "S,95;S,46;" 138 100 uniprot_mouse_length brain_HCD 623.8604126 623.250671 623.246956 30 18657.38868 5.961339535 CIB3_MOUSE Calcium and integrin-binding family member 3 Q0P523 MRLFYRYQDLAPQLVPLDYTTSPKVKVPYELIGSMPELKDNPFRQRIAQVFSQDGDGHMTLENFLDMFSVMSEMAPRDLKAYYAFKIYDFNNDNYICAWDLEQTVTRLTRGELSAEEVTLVCEKVLDEADGDQDGRLSLEDFQNMILRAPDFLSTFHIRI 160 SUBUNIT: Interacts with ITGA2B (via C-terminus cytoplasmic tail region); the interaction is stabilized/increased in a calcium and magnesium-dependent manner. {ECO:0000269|PubMed:18989529}. null 4040.55 null null 100 uniprot_mouse_length brain_HCD 542.6298218 541.3573 541.355305 29 15662.28887 3.684834468 CISD3_MOUSE "CDGSH iron-sulfur domain-containing protein 3, mitochondrial;AltName: Full=Melanoma nuclear protein 13;Flags: Precursor" B1AR13 GFRRLSFPTDFIFLFPNHICLPALSKPYQRREISSWLARWFPKDPAKPVVAQKTPIRLELVAGKTYRWCVCGRSKNQPFCDGSHFFQRTGLSPLKFKAQETRTVALCTCKATQRPPYCDGTHKSEQVQKAEVGSPL 136 COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601; Evidence={ECO:0000250}; Note=Binds 2 [2Fe-2S] clusters per subunit. {ECO:0000250}; K64AcK95AcK123Ac 1130.65 "K,30;K,0;K,6;" 102 100 uniprot_mouse_length brain_HCD 627.0341187 628.923584 628.918204 23 14435.10595 8.554346719 CK052_MOUSE Uncharacterized protein C11orf52 homolog Q9D8L0 MGNRLCCGGTWSCPSTFQKKSKTGSHPRPTLSILKQQQLWQNGTKDYETTAPTYEQVLYPPASQKKTSNSTSEESDLHYADIHVLRQIRPHSLHTVKCLHSESATEYATLRFPQATPQYDSNNGTLV 127 "ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9D8L0-1; Sequence=Displayed; Name=2; IsoId=Q9D8L0-2; Sequence=VSP_021875;-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" T30PS63P 1516.55 "T,13;S,34;" 119 100 uniprot_mouse_length brain_HCD 547.168335 543.245422 543.238587 26 14091.19047 12.58261737 CK098_MOUSE Uncharacterized protein C11orf98 homolog {ECO:0000250|UniProtKB:E9PRG8} Q9D937 MAPPGGKINRPRTELKKKLFKRRRVLSRDRRRKRQVVGAVIDEGLTTKHHLKKRASSARANITLSGKKRRKLLQQIRLAQKEKAAMEVEAPSKSTRTSQPQPKQQKKIKAPQDVAMEDLEDKS 123 "-------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License--------------------------------------------------" null 1654.09 null null 100 uniprot_mouse_length brain_HCD 540.1045532 540.543762 540.545612 45 24266.52752 -3.422084886 CLD15_MOUSE Claudin-15 Q9Z0S5 MSVAVETFGFFMSALGLLMLGLTLSNSYWRVSTVHGNVITTNTIFENLWYSCATDSLGVSNCWDFPSMLALSGYVQGCRALMITAILLGFLGLFLGMVGLRCTNVGNMDLSKKAKLLAIAGTLHILAGACGMVAISWYAVNITTDFFNPLYAGTKYELGPALYLGWSASLLSILGGICVFSTCCCSSKEEPATRAGLPYKPSTVVIPRATSDESDISFGKYGKNAYV 227 "FUNCTION: Claudins function as major constituents of the tight junction complexes that regulate the permeability of epithelia. While some claudin family members function as impermeable barriers, others mediate the permeability to ions and small molecules. Often, several claudin family members are coexpressed and interact with each other, and this determines the overall permeability. CLDN15 forms tight junctions that mediate the paracellular transport of small monovalent cations along a concentration gradient, due to selective permeability for Na(+), Li(+) and K(+) ions, but selects against Cl(-) ions. Plays an important role in paracellular Na(+) transport in the intestine and in Na(+) homeostasis. Required for normal Na(+)-dependent intestinal nutrient uptake. {ECO:0000269|PubMed:18242218, ECO:0000269|PubMed:20727355, ECO:0000269|PubMed:23089202}." null 770.99 null null 100 uniprot_mouse_length brain_HCD 622.7888794 627.006226 627.000158 30 18769.98294 9.677168116 COF2_MOUSE "Cofilin-2;AltName: Full=Cofilin, muscle isoform" P45591 ASGVTVNDEVIKVFNDMKVRKSSTQEEIKKRKKAVLFCLSDDKRQIIVEEAKQILVGDIGDTVEDPYTSFVKLLPLNDCRYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKFTGIKHEWQVNGLDDIKDRSTLGEKLGGSVVVSLEGKPL 165 FUNCTION: Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is the major component of intranuclear and cytoplasmic actin rods. A1AcS2PT5P 1441.37 "A,93;S,0;T,2;" 144 100 uniprot_mouse_length brain_HCD 627.0341187 624.12323 624.126886 20 12456.5286 -5.857814514 COXM1_MOUSE COX assembly mitochondrial protein homolog; Short=Cmc1p Q9CPZ8 ALDPAEQHLRHVEKDVLIPKIIREKARERCSEQVEDFTRCCKDSGILMVLKCRKENSALKDCLTAYYNDPAFYEECKLEYLKEREEFRKTGVPTKKRLQKLPTNM 105 FUNCTION: Required for mitochondrial cytochrome c oxidase (COX) assembly and respiration. {ECO:0000250}. A1Ac 1067.34 "A,50;" 90 100 uniprot_mouse_length brain_HCD 522.0480347 520.231995 520.234525 28 14531.55456 -4.863904589 CQ100_MOUSE Uncharacterized protein C17orf100 homolog Q8BGJ3 MGRMASPLRSKSSAPRVESTRHKETSTVRVETSSHREETSSHRVETSSRQVRTSSRQVETSQRHREGPSLTPSTKRLPQFLEVSSQHVETSSQCTETSSRHVRASSSLRVETTVHRVESPARQSARMAR 129 "-------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License--------------------------------------------------" null 434.88 null null 100 uniprot_mouse_length brain_HCD 640.3203735 642.650452 642.648061 19 12185.3024 3.720014579 CS025_MOUSE UPF0449 protein C19orf25 homolog Q9D7E4 MNSKAKKRVVLPTRPAPPTVEQILEDVRGAPAQDPVFTALAPEDPPDPSPRAEDSEIQQEQIYQQSRAYVAMNERLRQAGEALRQKFDGLRQAGQRLEQDISQVTSATS 109 "SIMILARITY: Belongs to the UPF0449 family. {ECO:0000305}.-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" Y63P 687.77 "Y,57;" 82 100 uniprot_mouse_length brain_HCD 522.0480347 523.347656 523.355463 40 20882.19758 -14.91672592 CSRP3_MOUSE "Cysteine and glycine-rich protein 3;AltName: Full=Cysteine-rich protein 3; Short=CRP3;AltName: Full=LIM domain protein, cardiac;AltName: Full=Muscle LIM protein" P50462 MPNWGGGAKCGACEKTVYHAEEIQCNGRSFHKTCFHCMACRKALDSTTVAAHESEIYCKVCYGRRYGPKGIGFGQGAGCLSTDTGEHLGLQFQQSPKPARAATTSNPSKFSAKFGESEKCPRCGKSVYAAEKVMGGGKPWHKTCFRCAICGKSLESTNVTDKDGELYCKVCYAKNFGPTGIGFGGLTQQVEKKE 194 "FUNCTION: Positive regulator of myogenesis. Plays a crucial and specific role in the organization of cytosolic structures in cardiomyocytes. Could play a role in mechanical stretch sensing. May be a scaffold protein that promotes the assembly of interacting proteins at Z-line structures. It is essential for calcineurin anchorage to the Z line. Required for stress-induced calcineurin-NFAT activation. {ECO:0000269|PubMed:15665106, ECO:0000269|PubMed:9039266}." null 652.01 null null 100 uniprot_mouse_length brain_HCD 614.25354 611.779541 611.777085 21 12820.30792 4.01455969 CTL2A_MOUSE Protein CTLA-2-alpha;AltName: Full=Cytotoxic T-lymphocyte-associated protein 2-alpha;Flags: Precursor P12399 AAPPPDPSLDNEWKEWKTKFAKAYNLNEERHRRLVWEENKKKIEAHNADYEQGKTSFYMGLNQFSDLTPEEFKTNCYGNSLNRGEMAPDLPEYEDLGKNSYLTPGRAQPE 110 "FUNCTION: Not known, expressed in activated T-cell." null 573.3 null null 100 uniprot_mouse_length brain_HCD 627.0341187 626.121582 626.116719 20 12496.32494 7.766972359 CV039_MOUSE UPF0545 protein C22orf39 homolog Q3U595 MAVAGSWQPPRPCEVYRAEWELCRSVGHVLHHYYVHGKRPDCRQWLRDLTNCREWEESRSAEAQRSLCESEQVRVQAAQKHTLVWALRQRPPTDWNLPLPQEKDK 105 "SIMILARITY: Belongs to the UPF0545 family. {ECO:0000305}.-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" null 1112.52 null null 100 uniprot_mouse_length brain_HCD 925.3269043 920.928955 920.929087 19 17469.63434 -0.143248679 DBND1_MOUSE Dysbindin domain-containing protein 1 Q9CZ00 MESPEGAGPGEIVKDVKVPQAALNVSAHETGDMCRTPVAEEEEEVGIPIPAPGFLQVTERRQPLSSVSSLEVHFDLLDLTELTDMSDQELAEVFADSDDENLATESPAGLHPLSRASCLRSPSWTKTRAEQNREKQPPSDPERQGTIVDTFLTVEEPKED 160 ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9CZ00-1; Sequence=Displayed; Name=2; IsoId=Q9CZ00-2; Sequence=VSP_026215; null 4170.16 null null 100 uniprot_mouse_length brain_HCD 575.8931885 574.114807 574.110871 30 17184.30804 6.856043153 DBND2_MOUSE Dysbindin domain-containing protein 2 Q9CRD4 MDPNPRAALERQQLRLRERQKFFEDILQPETEFVFPLSHLHLESQRPPIGSISSMEVNVDTLEQVEFIDLADQDGADVFLPCEESSPAPQMSGVDDHPEELSLLVPTSDRTTSRTSSLSSDSSNLRSPNPSDGGGDTPLAQSDEEDGDDGGAEPGPCS 158 FUNCTION: May modulate the activity of casein kinase-1. Inhibits CSNK1D autophosphorylation (in vitro) (By similarity). {ECO:0000250}. null 1542.14 null null 100 uniprot_mouse_length brain_HCD 614.25354 609.815369 609.813089 42 25556.12198 3.738280442 DHPR_MOUSE Dihydropteridine reductase; EC=1.5.1.34;AltName: Full=HDHPR;AltName: Full=Quinoid dihydropteridine reductase Q8BVI4 MAASGEARRVLVYGGRGALGSRCVQAFRARNWWVASIDVVENEEASASVVVKMTDSFTEQADQVTADVGKLLGDQKVDAILCVAGGWAGGNAKSKSLFKNCDMMWKQSMWTSTISSHLATKHLKEGGLLTLAGAKAALDGTPGMIGYGMAKGAVHQLCQSLAGKNSGMPPGAAAIAVLPVTLDTPMNRKSMPEADFSSWTPLEFLVETFHDWITGNKRPNSGSLIQVVTTDGKTELTPAYF 241 "FUNCTION: The product of this enzyme, tetrahydrobiopterin (BH-4), is an essential cofactor for phenylalanine, tyrosine, and tryptophan hydroxylases. {ECO:0000250}." null 2520.13 null null 100 uniprot_mouse_length brain_HCD 887.7693481 883.520081 883.518194 15 13230.76061 2.135288689 DNLZ_MOUSE DNL-type zinc finger protein;AltName: Full=Hsp70-escort protein 1; Short=HEP1;AltName: Full=mtHsp70-escort protein;Flags: Precursor Q9D113 SSAPGSGRAAALGRVEADHYQLVYTCKVCGTRSSKRISKLAYHQGVVIVTCPGCQNHHIIADNLSWFSDLKGKRNIEEILAARGEEVRRVSGDGALELILEAAVPPDTPEGDEDPPNPGKMGQS 124 "FUNCTION: May function as a co-chaperone towards HSPA9/mortalin which, by itself, is prone to self-aggregation. {ECO:0000250}." null 375.73 null null 100 uniprot_mouse_length brain_HCD 543.168396 539.453857 539.451521 35 18835.78266 4.331106289 DNPH1_MOUSE 2'-deoxynucleoside 5'-phosphate N-hydrolase 1 {ECO:0000255|HAMAP-Rule:MF_03036}; EC=3.2.2.- {ECO:0000255|HAMAP-Rule:MF_03036};AltName: Full=c-Myc-responsive protein Rcl {ECO:0000255|HAMAP-Rule:MF_03036} Q80VJ3 AASGELVPCSVYFCGSIRGGREDQALYSRIVSRLRRYGKVLTEHVADAELEPRGEEAAGGDQFIHERDLAWLRQADVVVAEVTQPSLGVGYELGRAVALGKPILCLFRPQSGRVLSAMIRGAADGSRFQVWDYAEEEVETMLHRYFEAYLPQGTASSSNPSACLNPTVLEKI 172 FUNCTION: Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5- phosphate and a purine or pyrimidine base. Deoxyribonucleoside 5'- monophosphates containing purine bases are preferred to those containing pyrimidine bases. {ECO:0000255|HAMAP-Rule:MF_03036}. null 2189.85 null null 100 uniprot_mouse_length brain_HCD 627.0341187 628.036377 628.043077 32 20053.35598 -10.66813268 EMC4_MOUSE ER membrane protein complex subunit 4;AltName: Full=Transmembrane protein 85 Q9CZX9 TTQGGLVANRGRRFKWAIELSGPGGGSRGRSDRGSGQGDSLYPVGYLDKQVPDTSVQETDRILVEKRCWDIALGPLKQIPMNLFIMYMAGNTISIFPTMMVCMMAWRPIQALMAISATFKMLESSSQKFLQGLVYLIGNLMGLALAVYKCQSMGLLPTHASDWLAFIEPPERMEFSGGGLLL 182 FUNCTION: May mediate anti-apoptotic activity. {ECO:0000250}. S35P 3418.81 "S,226;" 232 100 uniprot_mouse_length brain_HCD 614.25354 615.220093 615.215365 29 17802.227 7.684745386 EMP1_MOUSE Epithelial membrane protein 1; Short=EMP-1;AltName: Full=Tumor-associated membrane protein P47801 MLVLLAGLFVVHIATAIMLFVSTIANVWMVADYANASVGLWKNCTGGNCDGSLSYGNEDAIKAVQAFMILSIIFSIISLVVFVFQLFTMEKGNRFFLSGSTMLVCWLCILVGVSIYTHHYAHSEGNFNSSSHQGYCFILTWICFCFSFIIGILYMVLRKK 160 SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. null 1361.67 null null 100 uniprot_mouse_length brain_HCD 614.25354 610.849365 610.853638 29 17675.73549 -6.994745319 F162B_MOUSE Protein FAM162B Q9CX19 MLWVSRSVLRLGLGFTTHRAPQIISRWPRWGPRVACHPCSSSGQNPSGFEPPEKVHRIPAQYKPSKFDKKILLWTGRFKSIEDIPPLVPPEMIAVSRNKARVKACYIMIGLTIVACFAVIVSAKRAVERHESLTSWNLAKKAKWREEAALAAQSKSK 157 SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. null 1057.91 null null 100 uniprot_mouse_length brain_HCD 577.3182983 573.182068 573.185151 20 11437.69566 -5.378940646 F19A4_MOUSE Protein FAM19A4;AltName: Full=Chemokine-like protein TAFA-4;Flags: Precursor Q7TPG5 QHLRGHAGHHLIKPGTCEVVAVHRCCNKNRIEERSQTVKCSCFPGQVAGTTRAQPSCVEAAIVIEKWWCHMNPCLEGEDCKVLPDSSGWSCSSGNKVKTTKVTR 104 SUBCELLULAR LOCATION: Secreted {ECO:0000250}. null 1119.67 null null 100 uniprot_mouse_length brain_HCD 950.9771729 946.462769 946.467344 16 15119.46452 -4.834234738 FABP5_MOUSE "Fatty acid-binding protein, epidermal;AltName: Full=Epidermal-type fatty acid-binding protein; Short=E-FABP;AltName: Full=Fatty acid-binding protein 5;AltName: Full=Keratinocyte lipid-binding protein;AltName: Full=Psoriasis-associated fatty acid-binding protein homolog; Short=PA-FABP" Q05816 ASLKDLEGKWRLMESHGFEEYMKELGVGLALRKMAAMAKPDCIITCDGNNITVKTESTVKTTVFSCNLGEKFDETTADGRKTETVCTFQDGALVQHQQWDGKESTITRKLKDGKMIVECVMNNATCTRVYEKVQ 134 FUNCTION: High specificity for fatty acids. Highest affinity for C18 chain length (By similarity). {ECO:0000250}. A1AcY130P 661.6 "A,53;Y,65;" 96 100 uniprot_mouse_length brain_HCD 623.8604126 621.535583 621.526403 24 14884.61932 14.77088672 FABP7_MOUSE "Fatty acid-binding protein, brain;AltName: Full=Brain lipid-binding protein; Short=BLBP;AltName: Full=Brain-type fatty acid-binding protein; Short=B-FABP;AltName: Full=Fatty acid-binding protein 7" P51880 MVDAFCATWKLTDSQNFDEYMKALGVGFATRQVGNVTKPTVIISQEGGKVVIRTQCTFKNTEINFQLGEEFEETSIDDRNCKSVVRLDGDKLIHVQKWDGKETNCTREIKDGKMVVTLTFGDIVAVRCYEKA 132 "FUNCTION: B-FABP could be involved in the transport of a so far unknown hydrophobic ligand with potential morphogenic activity during CNS development. It is required for the establishment of the radial glial fiber system in developing brain, a system that is necessary for the migration of immature neurons to establish cortical layers." null 2510.64 null null 100 uniprot_mouse_length brain_HCD 614.25354 613.781738 613.786449 28 17149.00182 -7.67484971 FUND1_MOUSE FUN14 domain-containing protein 1 Q9DB70 MASRNPPPQDYESDDESYEVLDLTEYARRHHWWNRVFGHSSGPMVEKYSVATQIVMGGVTGWCAGFLFQKVGKLAATAVGGGFLLLQVASHSGYVQIDWKRVEKDVNKAKRQIKKRANKAAPEINNIIEEATDFIKQNIVISSGFVGGFLLGLAS 155 "FUNCTION: Acts as an activator of hypoxia-induced mitophagy, an important mechanism for mitochondrial quality control. {ECO:0000250}." null 1054.08 null null 100 uniprot_mouse_length brain_HCD 658.1266479 655.946472 655.940855 28 18328.32455 8.563528138 GA45A_MOUSE Growth arrest and DNA damage-inducible protein GADD45 alpha;AltName: Full=DNA damage-inducible transcript 1 protein; Short=DDIT-1 P48316 MTLEEFSAAEQKTERMDTVGDALEEVLSKARSQRTITVGVYEAAKLLNVDPDNVVLCLLAADEDDDRDVALQIHFTLIRAFCCENDINILRVSNPGRLAELLLLENDAGPAESGGAAQTPDLHCVLVTNPHSSQWKDPALSQLICFCRESRYMDQWVPVINLPER 165 "FUNCTION: Might affect PCNA interaction with some CDK (cell division protein kinase) complexes; stimulates DNA excision repair in vitro and inhibits entry of cells into S phase. In T-cells, functions as a regulator of p38 MAPKs by inhibiting p88 phosphorylation and activity. {ECO:0000269|PubMed:15735649}." null 1257.44 null null 100 uniprot_mouse_length brain_HCD 544.1309204 539.809082 539.815183 25 13463.36607 -11.30195841 GALA_MOUSE Galanin peptides;Contains: Galanin;Contains: Galanin message-associated peptide; Short=GMAP;Flags: Precursor P47212 MARGSVILLGWLLLVVTLSATLGLGMPAKEKRGWTLNSAGYLLGPHAIDNHRSFSDKHGLTGKRELQLEVEERRPGSVDVPLPESNIVRTIMEFLSFLHLKEAGALDSLPGIPLATSSEDLEKS 124 "FUNCTION: Contracts smooth muscle of the gastrointestinal and genitourinary tract, regulates growth hormone release, modulates insulin release, and may be involved in the control of adrenal secretion." null 918.1 null null 100 uniprot_mouse_length brain_HCD 640.3203735 639.483643 639.493226 12 7658.91656 -14.98596308 GBG12_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12;Flags: Precursor Q9DAS9 SSKTASTNSIAQARRTVQQLRLEASIERIKVSKASADLMSYCEEHARSDPLLMGIPTSENPFKDKKTC 68 "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction." S1AcS25PC68Me 342.72 "S,32;S,9;C,28;" 48 100 uniprot_mouse_length brain_HCD 616.8864136 620.582092 620.575617 12 7431.90512 10.43432094 GBG2_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2;AltName: Full=G gamma-I;Flags: Precursor P63213 ASNNTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASENPFREKKFFC 67 "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction." C67Me 1844.02 "C,69;" 91 100 uniprot_mouse_length brain_HCD 592.4051514 592.434937 592.429738 30 17733.87432 8.774919799 GLPA_MOUSE Glycophorin-A;AltName: CD_antigen=CD235a P14220 MTESTAAVTTSGHSLTTTFHIPSSQHYQEEHSPSLSGSDSLLQITTPVVASTVGNPNQHSATMSTPAIHVSTYHTAPTEVSAAFEEQPVSPHIGGMPSPIQHDFPALVMILIILGVMAGIIGTILLISYCISRMTKKSSVDIQSPEGGDNSVPLSSIEQTPNEESSNV 168 FUNCTION: Glycophorin A is the major intrinsic membrane sialoglycoprotein of the erythrocyte. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane (By similarity). {ECO:0000250}. S155P 819.55 "S,10;" 114 100 uniprot_mouse_length brain_HCD 616.8864136 615.580872 615.581057 29 17813.83283 -0.301208048 GLPA_MOUSE Glycophorin-A;AltName: CD_antigen=CD235a P14220 MTESTAAVTTSGHSLTTTFHIPSSQHYQEEHSPSLSGSDSLLQITTPVVASTVGNPNQHSATMSTPAIHVSTYHTAPTEVSAAFEEQPVSPHIGGMPSPIQHDFPALVMILIILGVMAGIIGTILLISYCISRMTKKSSVDIQSPEGGDNSVPLSSIEQTPNEESSNV 168 FUNCTION: Glycophorin A is the major intrinsic membrane sialoglycoprotein of the erythrocyte. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane (By similarity). {ECO:0000250}. S155PS165P 7531.42 "S,23;S,3;" 264 100 uniprot_mouse_length brain_HCD 627.0341187 625.093689 625.088274 34 21207.97579 8.662720241 H12_MOUSE Histone H1.2;AltName: Full=H1 VAR.1;AltName: Full=H1c P15864 SEAAPAAPAAAPPAEKAPAKKKAAKKPAGVRRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGILVQTKGTGASGSFKLNKKAASGEAKPQAKKAGAAKAKKPAGAAKKPKKATGAATPKKAAKKTPKKAKKPAAAAVTKKVAKSPKKAKVTKPKKVKSASKAVKPKAAKPKVAKAKKVAAKKK 211 "FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250}." S1AcK16Ac 3793.24 "S,2;K,0;" 269 100 uniprot_mouse_length brain_HCD 540.6661377 540.79718 540.798568 26 14027.74909 -2.566249803 H2B1P_MOUSE Histone H2B type 1-P Q8CGP2 PEPVKSVPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S14PS36PK46Me 1119.9 "S,5;S,0;K,24;" 107 100 uniprot_mouse_length brain_HCD 614.25354 609.815369 609.816574 38 23123.00196 -1.976574117 HSPB1_MOUSE Heat shock protein beta-1; Short=HspB1;AltName: Full=Growth-related 25 kDa protein;AltName: Full=Heat shock 25 kDa protein; Short=HSP 25;AltName: Full=Heat shock 27 kDa protein; Short=HSP 27;AltName: Full=p25 P14602 MTERRVPFSLLRSPSWEPFRDWYPAHSRLFDQAFGVPRLPDEWSQWFSAAGWPGYVRPLPAATAEGPAAVTLAAPAFSRALNRQLSSGVSEIRQTADRWRVSLDVNHFAPEELTVKTKEGVVEITGKHEERQDEHGYISRCFTRKYTLPPGVDPTLVSSSLSPEGTLTVEAPLPKAVTQSAEITIPVTFEARAQIGGPEAGKSEQSGAK 209 FUNCTION: Involved in stress resistance and actin organization. S15PK127Ac 2180.36 "S,9;K,213;" 224 100 uniprot_mouse_length brain_HCD 592.4051514 592.153137 592.158536 21 12408.3194 -9.117141172 MIF_MOUSE Macrophage migration inhibitory factor; Short=MIF; EC=5.3.2.1;AltName: Full=Delayed early response protein 6; Short=DER6;AltName: Full=Glycosylation-inhibiting factor; Short=GIF;AltName: Full=L-dopachrome isomerase;AltName: Full=L-dopachrome tautomerase; EC=5.3.3.12;AltName: Full=Phenylpyruvate tautomerase P34884 PMFIVNTNVPRASVPEGFLSELTQQLAQATGKPAQYIAVHVVPDQLMTFSGTNDPCALCSLHSIGKIGGAQNRNYSKLLCGLLSDRLHISPDRVYINYYDMNAANVGWNGSTFA 114 "FUNCTION: Pro-inflammatory cytokine. Involved in the innate immune response to bacterial pathogens. The expression of MIF at sites of inflammation suggests a role as mediator in regulating the function of macrophages in host defense. Counteracts the anti- inflammatory activity of glucocorticoids. Has phenylpyruvate tautomerase and dopachrome tautomerase activity (in vitro), but the physiological substrate is not known. It is not clear whether the tautomerase activity has any physiological relevance, and whether it is important for cytokine activity (By similarity). {ECO:0000250}." K77Ac 366.24 "K,44;" 54 100 uniprot_mouse_length brain_HCD 760.3514404 763.077698 763.068384 16 12187.08424 12.20566086 4EBP1_MOUSE Eukaryotic translation initiation factor 4E-binding protein 1; Short=4E-BP1; Short=eIF4E-binding protein 1;AltName: Full=Phosphorylated heat- and acid-stable protein regulated by insulin 1; Short=PHAS-I Q60876 SAGSSCSQTPSRAIPTRRVALGDGVQLPPGDYSTTPGGTLFSTTPGGTRIIYDRKFLMECRNSPVAKTPPKDLPAIPGVTSPTSDEPPMQASQSQLPSSPEDKRAGGEESQFEMDI 116 "FUNCTION: Repressor of translation initiation that regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. In contrast, hyperphosphorylated form dissociates from EIF4E, allowing interaction between EIF4G1/EIF4G3 and EIF4E, leading to initiation of translation (By similarity). Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways (PubMed:7629182). {ECO:0000250|UniProtKB:Q13541, ECO:0000269|PubMed:7629182}." null 432.77 null null 100 uniprot_mouse_length brain_HCD 643.0522461 644.95929 644.954115 19 12229.11826 8.023130113 4EBP1_MOUSE Eukaryotic translation initiation factor 4E-binding protein 1; Short=4E-BP1; Short=eIF4E-binding protein 1;AltName: Full=Phosphorylated heat- and acid-stable protein regulated by insulin 1; Short=PHAS-I Q60876 SAGSSCSQTPSRAIPTRRVALGDGVQLPPGDYSTTPGGTLFSTTPGGTRIIYDRKFLMECRNSPVAKTPPKDLPAIPGVTSPTSDEPPMQASQSQLPSSPEDKRAGGEESQFEMDI 116 "FUNCTION: Repressor of translation initiation that regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. In contrast, hyperphosphorylated form dissociates from EIF4E, allowing interaction between EIF4G1/EIF4G3 and EIF4E, leading to initiation of translation (By similarity). Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways (PubMed:7629182). {ECO:0000250|UniProtKB:Q13541, ECO:0000269|PubMed:7629182}." S1Ac 2645.48 "S,84;" 118 100 uniprot_mouse_length brain_HCD 588.9731445 592.308228 592.313049 32 18911.99966 -8.140055239 AARD_MOUSE Alanine and arginine-rich domain-containing protein Q811W1 MGLGDYSHCRQRMSRGLYGVSGRAALWSPVFHPVHRMPCGTWRIGIEVPEHVRASSPVLEHLRRQLERAFQRAAARGRARRAREAVAAVAAAAAAAREERSRTRMECALARLRAELLELRFQNHQLARTLLDLNMKMQQLKKRQDQELASKPQSPQDKEMNSECGSA 167 "TISSUE SPECIFICITY: Preferrentially expressed in testis both in embryo and adult. Expressed at much lower level in other tissues. {ECO:0000269|PubMed:12617826, ECO:0000269|PubMed:17486547}." null 9401.12 null null 100 uniprot_mouse_length brain_HCD 669.9186401 667.354675 667.351132 15 9990.25856 5.309488212 ACBP_MOUSE Acyl-CoA-binding protein; Short=ACBP;AltName: Full=Diazepam-binding inhibitor; Short=DBI;AltName: Full=Endozepine; Short=EP P31786 SQAEFDKAAEEVKRLKTQPTDEEMLFIYSHFKQATVGDVNTDRPGLLDLKGKAKWDSWNKLKGTSKESAMKTYVEKVDELKKKYGI 86 FUNCTION: Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA receptor. S1AcK7AcK50Ac 1730.21 "S,2;K,0;K,0;" 75 100 uniprot_mouse_length brain_HCD 784.5089111 781.148804 781.142012 12 9356.69654 8.694591807 ADIG_MOUSE Adipogenin;AltName: Full=Small adipocyte factor 1; Short=SMAF-1 Q8R400 MKYPLVPLVSDLTLSFLVFWLCLPVALLLFLTIVWLHFLLSQESKEDDSDLCFNWEPWSKRPSECGCEETFPGEEDGLHW 80 FUNCTION: Plays a role in stimulating adipocyte differentiation and development. {ECO:0000269|PubMed:16132694}. null 705.34 null null 100 uniprot_mouse_length brain_HCD 542.6281128 540.55481 540.562055 30 16178.84697 -13.40351144 ADM2_MOUSE ADM2;AltName: Full=Intermedin;Contains: Adrenomedullin-2; Short=AM2; AltName: Full=Intermedin-long; Short=IMDL;Contains: Intermedin-short; Short=IMDS;Flags: Precursor Q7TNK8 MAQLLMVTVTLGCISLLYLLPGTLSGSLGKGLRHSRPREPPAKIPSSNLQPGHPSLQPVVWKSRRHAPQPQGRGNRALAMVHLPQGGGSRHPGPQRPTGSRRPHAQLLRVGCVLGTCQVQNLSHRLWQLVRPAGRRDSAPVDPSSPHSYG 150 "FUNCTION: IMDL and IMDS may play a role as physiological regulators of gastrointestinal, cardiovascular bioactivities mediated by the CALCRL/RAMPs receptor complexes. Activates the cAMP-dependent pathway. {ECO:0000269|PubMed:14615490, ECO:0000269|PubMed:14706825}." null 757.35 null null 100 uniprot_mouse_length brain_HCD 604.3099365 603.508301 603.504233 15 9033.55862 6.740269625 AKA7A_MOUSE A-kinase anchor protein 7 isoform alpha; Short=AKAP-7 isoform alpha;AltName: Full=A-kinase anchor protein 18; Short=AKAP-18;AltName: Full=A-kinase anchor protein 9 kDa; Short=AKAP 9;AltName: Full=Protein kinase A-anchoring protein 7 isoform alpha; Short=PRKA7 isoform alpha O55074 GQLCCFPFARDEGKICEKDRREPEDAELVRLSKRLVENAVLKAVQQYLEETQNKKQPGEGNSTKAEEGDRNGDGSDNNRK 80 "FUNCTION: Targets the cAMP-dependent protein kinase (PKA) to the plasma membrane, and permits functional coupling to the L-type calcium channel. The membrane-associated form reduces epithelial sodium channel (ENaC) activity, whereas the free cytoplasmic form may negatively regulate ENaC channel feedback inhibition by intracellular sodium (By similarity). {ECO:0000250}." null 841.41 null null 100 uniprot_mouse_length brain_HCD 614.5807495 613.930359 613.92222 23 14090.19942 13.25719522 ANG2_MOUSE Angiogenin-2;AltName: Full=Angiogenin-related protein;Flags: Precursor Q64438 QDDSRYTKFLTQHYDAKPKGRDDRYCESMMVKRKLTSFCKDVNTFIHDTKNNIKAICGKKGSPYGRNLRISKSHFQVTTCTHKGRSPRPPCRYRASKGFRYIIIGCENGWPVHFDESFISP 121 FUNCTION: Has ribonuclease activity (in vitro). Seems to lack angiogenic activity. {ECO:0000269|PubMed:8633065}. null 2460.42 null null 100 uniprot_mouse_length brain_HCD 761.5108643 759.643066 759.645296 11 8342.09527 -2.935045819 APC13_MOUSE Anaphase-promoting complex subunit 13; Short=APC13;AltName: Full=Cyclosome subunit 13 Q8R034 MDSEVQRDGRILDLIDDAWREDKLPYEDVAIPLSELPEPEQDNGGTTESVKEQEMKWTDLALQGLHENVPPAGN 74 "FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). {ECO:0000250}." null 398.63 null null 100 uniprot_mouse_length brain_HCD 620.2070923 619.407043 619.412011 14 8653.76406 -8.019771784 APEL_MOUSE Apelin;AltName: Full=APJ endogenous ligand;Contains: Apelin-36;Contains: Apelin-31;Contains: Apelin-28;Contains: Apelin-13;Flags: Precursor Q9R0R4 MNLRLCVQALLLLWLSLTAVCGVPLMLPPDGTGLEEGSMRYLVKPRTSRTGPGAWQGGRRKFRRQRPRLSHKGPMPF 77 FUNCTION: Endogenous ligand for APJ. Has an inhibitory effect on cytokine production in response to T-cell receptor/CD3 cross- linking. The oral intake of apelin in the colostrum and the milk might therefore modulate immune responses in neonates. May also have a role in the central control of body fluid homeostasis by influencing AVP release and drinking behavior. null 224.19 null null 100 uniprot_mouse_length brain_HCD 526.0170898 525.901611 525.906957 13 6821.78968 -10.16467229 APOC1_MOUSE Apolipoprotein C-I; Short=Apo-CI; Short=ApoC-I;AltName: Full=Apolipoprotein C1;Contains: Truncated apolipoprotein C-I;Flags: Precursor P34928 DLSGTLESIPDKLKEFGNTLEDKARAAIEHIKQKEILTKTRAWFSEAFGKVKEKLKTTFS 60 "FUNCTION: Inhibitor of lipoprotein binding to the low density lipoprotein (LDL) receptor, LDL receptor-related protein, and very low density lipoprotein (VLDL) receptor. Associates with high density lipoproteins (HDL) and the triacylglycerol-rich lipoproteins in the plasma and makes up about 10% of the protein of the VLDL and 2% of that of HDL. Appears to interfere directly with fatty acid uptake and is also the major plasma inhibitor of cholesteryl ester transfer protein (CETP). Modulates the interaction of APOE with beta-migrating VLDL and inhibits binding of beta-VLDL to the LDL receptor-related protein (By similarity). Binds free fatty acids and reduces their intracellular esterification. {ECO:0000250|UniProtKB:P02654, ECO:0000250|UniProtKB:P33047, ECO:0000269|PubMed:17339654}." null 1105 null null 100 uniprot_mouse_length brain_HCD 880.9211426 878.378296 878.382703 14 12277.34721 -5.017290923 ARP19_MOUSE cAMP-regulated phosphoprotein 19; Short=ARPP-19 P56212 SAEVPEAASAEEQKEMEDKVTSPEKAEEAKLKARYPHLGQKPGGSDFLRKRLQKGQKYFDSGDYNMAKAKMKNKQLPAAAPDKTEVTGDHIPTPQDLPQRKPSLVASKLAG 111 "FUNCTION: Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-62 during mitosis, specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, an essential condition to keep cyclin-B1-CDK1 activity high during M phase. May indirectly enhance GAP-43 expression by binding to the NGF-regulatory region of its mRNA (By similarity). {ECO:0000250}." S1AcS61P 1535.41 "S,63;S,34;" 101 100 uniprot_mouse_length brain_HCD 542.0480347 537.645264 537.647664 38 20381.58875 -4.46450024 ARPC3_MOUSE Actin-related protein 2/3 complex subunit 3;AltName: Full=Arp2/3 complex 21 kDa subunit; Short=p21-ARC Q9JM76 PAYHSSLMDPDTKLIGNMALLPLRSQFKGPAPRETKDTDIVDEAIYYFKANVFFKNYEIKNEADRTLIYITLYISECLKKLQKCNSKSQGEKEMYTLGITNFPIPGEPGFPLNAIYAKPASKQEDEMMRAYLQQLRQETGLRLCEKVFDPQSDKPSKWWTCFVKRQFMNKSLSGPGQ 177 FUNCTION: Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. {ECO:0000250}. null 3075.06 null null 100 uniprot_mouse_length brain_HCD 728.9130249 729.146118 729.147919 13 9461.91742 -2.469781358 ATIF1_MOUSE "ATPase inhibitor, mitochondrial;AltName: Full=Inhibitor of F(1)F(o)-ATPase; Short=IF(1); Short=IF1;Flags: Precursor" O35143 VSDSSDSMDTGAGSIREAGGAFGKREKAEEDRYFREKTKEQLAALRKHHEDEIDHHSKEIERLQKQIERHKKKIQQLKNNH 81 "FUNCTION: Endogenous F(1)F(o)-ATPase inhibitor limiting ATP depletion when the mitochondrial membrane potential falls below a threshold and the F(1)F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix. Required to avoid the consumption of cellular ATP when the F(1)F(o)-ATP synthase enzyme acts as an ATP hydrolase (By similarity). Indirectly acts as a regulator of heme synthesis in erythroid tissues: regulates heme synthesis by modulating the mitochondrial pH and redox potential, allowing FECH to efficiently catalyze the incorporation of iron into protoporphyrin IX to produce heme. {ECO:0000250, ECO:0000269|PubMed:23135403}." null 3069.97 null null 100 uniprot_mouse_length brain_HCD 693.7456665 692.28064 692.28086 13 8982.64541 -0.318297927 ATP5J_MOUSE "ATP synthase-coupling factor 6, mitochondrial; Short=ATPase subunit F6;Flags: Precursor" P97450 NKELDPVQKLFVDKIREYKSKRQASGGPVDIGPEYQQDLDRELYKLKQMYGKGEMDTFPTFKFDDPKFEVIDKPQS 76 "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. Also involved in the restoration of oligomycin-sensitive ATPase activity to depleted F1-F0 complexes." K9Ac 1743.14 "K,1;" 77 100 uniprot_mouse_length brain_HCD_6 749.9708862 753.3974 753.387829 12 9024.64816 12.70381864 ATP5J_MOUSE "ATP synthase-coupling factor 6, mitochondrial; Short=ATPase subunit F6;Flags: Precursor" P97450 NKELDPVQKLFVDKIREYKSKRQASGGPVDIGPEYQQDLDRELYKLKQMYGKGEMDTFPTFKFDDPKFEVIDKPQS 76 "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. Also involved in the restoration of oligomycin-sensitive ATPase activity to depleted F1-F0 complexes." K9AcK14Ac 1196.39 "K,0;K,0;" 71 100 uniprot_mouse_length brain_HCD 876.4707642 876.16864 876.174909 13 11371.2624 -7.154808038 ATP5L_MOUSE "ATP synthase subunit g, mitochondrial; Short=ATPase subunit g" Q9CPQ8 AKFIRNFAEKAPSMVAAAVTYSKPRLATFWHYAKVELVPPTPAEIPTAIQSVKKIIQSAKTGSFKHLTVKEAVLNGLVATEVWMWFYIGEIIGKRGIVGYDV 102 "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane." A1AcK10Ac 1437.37 "A,2;K,0;" 102 100 uniprot_mouse_length brain_HCD_6 876.4707642 879.400757 879.406492 13 11413.27297 -6.521630343 ATP5L_MOUSE "ATP synthase subunit g, mitochondrial; Short=ATPase subunit g" Q9CPQ8 AKFIRNFAEKAPSMVAAAVTYSKPRLATFWHYAKVELVPPTPAEIPTAIQSVKKIIQSAKTGSFKHLTVKEAVLNGLVATEVWMWFYIGEIIGKRGIVGYDV 102 "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane." A1AcK10AcK23Ac 1098.86 "A,2;K,0;K,0;" 87 100 uniprot_mouse_length brain_HCD 614.5835571 609.839294 609.841965 34 20689.60288 -4.379112228 B2CL2_MOUSE Bcl-2-like protein 2; Short=Bcl2-L-2;AltName: Full=Apoptosis regulator Bcl-W;AltName: Full=c98 P70345 ATPASTPDTRALVADFVGYKLRQKGYVCGAGPGEGPAADPLHQAMRAAGDEFETRFRRTFSDLAAQLHVTPGSAQQRFTQVSDELFQGGPNWGRLVAFFVFGAALCAESVNKEMEPLVGQVQDWMVAYLETRLADWIHSSGGWAEFTALYGDGALEEARRLREGNWASVRTVLTGAVALGALVTVGAFFASK 192 "FUNCTION: Promotes cell survival. Blocks dexamethasone-induced apoptosis. Mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX. {ECO:0000269|PubMed:11784036, ECO:0000269|PubMed:14746907, ECO:0000269|PubMed:8761287}." A1Ac 3619.24 "A,182;" 220 100 uniprot_mouse_length brain_HCD 707.4125366 708.210999 708.210812 20 14137.20274 0.263389309 BATF_MOUSE Basic leucine zipper transcriptional factor ATF-like;AltName: Full=B-cell-activating transcription factor; Short=B-ATF O35284 MPHSSDSSDSSFSRSPPPGKQDSSDDVRKVQRREKNRIAAQKSRQRQTQKADTLHLESEDLEKQNAALRKEIKQLTEELKYFTSVLSSHEPLCSVLASGTPSPPEVVYSAHAFHQPHISSPRFQP 125 "FUNCTION: AP-1 family transcription factor that controls the differentiation of lineage-specific cells in the immune system: specifically mediates the differentiation of T-helper 17 cells (Th17), follicular T-helper cells (TfH), CD8(+) dendritic cells and class-switch recombination (CSR) in B-cells. Acts via the formation of a heterodimer with JUNB that recognizes and binds DNA sequence 5'-TGA[CG]TCA-3'. The BATF-JUNB heterodimer also forms a complex with IRF4 (or IRF8) in immune cells, leading to recognition of AICE sequence (5'-TGAnTCA/GAAA-3'), an immune- specific regulatory element, followed by cooperative binding of BATF and IRF4 (or IRF8) and activation of genes. Controls differentiation of T-helper cells producing interleukin-17 (Th17 cells) by binding to Th17-associated gene promoters: regulates expression of the transcription factor RORC itself and RORC target genes such as IL17 (IL17A or IL17B). Also involved in differentiation of follicular T-helper cells (TfH) by directing expression of BCL6 and MAF. In B-cells, involved in class-switch recombination (CSR) by controlling the expression of both AICDA and of germline transcripts of the intervening heavy-chain region and constant heavy-chain region (I(H)-C(H)). Following infection, can participate in CD8(+) dendritic cell differentiation via interaction with IRF4 and IRF8 to mediate cooperative gene activation. Regulates effector CD8(+) T-cell differentiation by regulating expression of SIRT1. Following DNA damage, part of a differentiation checkpoint that limits self-renewal of hematopoietic stem cells (HSCs): up-regulated by STAT3, leading to differentiation of HSCs, thereby restricting self-renewal of HSCs. {ECO:0000269|PubMed:11466704, ECO:0000269|PubMed:12594265, ECO:0000269|PubMed:19578362, ECO:0000269|PubMed:20421391, ECO:0000269|PubMed:21572431, ECO:0000269|PubMed:22001828, ECO:0000269|PubMed:22385964, ECO:0000269|PubMed:22983707, ECO:0000269|PubMed:22992523, ECO:0000269|PubMed:22992524, ECO:0000269|PubMed:23021777}." S43P 2149.63 "S,3;" 125 100 uniprot_mouse_length brain_HCD 858.5696411 855.376953 855.373253 24 20493.9333 4.325743162 BETAT_MOUSE Angiopoietin-like protein 8 {ECO:0000305};AltName: Full=Betatrophin {ECO:0000303|PubMed:23623304};AltName: Full=Lipasin {ECO:0000303|PubMed:22809513};AltName: Full=Refeeding-induced fat and liver protein {ECO:0000303|PubMed:22569073};Flags: Precursor Q8R1L8 VRPAPVAPLGGPEPAQYEELTLLFHGALQLGQALNGVYRATEARLTEAGHSLGLYDRALEFLGTEVRQGQDATQELRTSLSEIQVEEDALHLRAEATARSLGEVARAQQALRDTVRRLQVQLRGAWLGQAHQEFETLKARADKQSHLLWALTGHVQRQQREMAEQQQWLRQIQQRLHTAALPA 183 "FUNCTION: Hormone that acts as a blood lipid regulator by regulating serum triglyceride levels (PubMed:22569073, PubMed:22809513, PubMed:23150577, PubMed:24043787). May be involved in the metabolic transition between fasting and refeeding: required to direct fatty acids to adipose tissue for storage in the fed state (PubMed:24043787). According to a report, may act by promoting ANGPTL3 cleavage (PubMed:23150577). According to another study, not required for cleavage of ANGPTL3 (PubMed:24043787). {ECO:0000269|PubMed:22569073, ECO:0000269|PubMed:22809513, ECO:0000269|PubMed:23150577, ECO:0000269|PubMed:24043787}." null 1170.59 null null 100 uniprot_mouse_length brain_HCD 544.7453613 541.995605 541.990357 38 20546.61043 9.683693967 BL1S3_MOUSE Biogenesis of lysosome-related organelles complex 1 subunit 3; Short=BLOC-1 subunit 3;AltName: Full=Reduced pigmentation protein Q5U5M8 MESSQGRRRRPGTVVPGEAAETDSELSASSSEEELYLGPSGPTRGRPTGLRVAGEAAETDSEPEPEPTVVPVDLPPLVVQRDPAETWGTEETPAMAPARSLLQLRLAESQTRLDHDVAAAVSGVYRRAGRDVAALAGRLAAAQATGLAAAHSVRLARGDLCALAERLDIVAGCRLLPDIRGVPGMEPEQDPGPRA 195 "FUNCTION: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking. {ECO:0000269|PubMed:16760431, ECO:0000269|PubMed:19546860, ECO:0000269|PubMed:21998198}." T59PS61P 1516.21 "T,0;S,1;" 162 100 uniprot_mouse_length brain_HCD 547.2439575 543.051392 543.044359 44 23836.9212 12.95032615 C1QBP_MOUSE "Complement component 1 Q subcomponent-binding protein, mitochondrial;AltName: Full=GC1q-R protein;AltName: Full=Glycoprotein gC1qBP; Short=C1qBP;Flags: Precursor" O35658 LHTEGDKAFVEFLTDEIKEEKKIQKHKSLPKMSGDWELEVNGTEAKLLRKVAGEKITVTFNINNSIPPTFDGEEEPSQGQKAEEQEPERTSTPNFVVEVTKTDGKKTLVLDCHYPEDEIGHEDEAESDIFSIKEVSFQATGDSEWRDTNYTLNTDSLDWALYDHLMDFLADRGVDNTFADELVELSTALEHQEYITFLEDLKSFVKNQ 208 "FUNCTION: Is believed to be a multifunctional and multicompartmental protein involved in inflammation and infection processes, ribosome biogenesis, regulation of apoptosis, transcriptional regulation and pre-mRNA splicing. At the cell surface is thought to act as an endothelial receptor for plasma proteins of the complement and kallikrein-kinin cascades. Putative receptor for C1q; specifically binds to the globular ""heads"" of C1q thus inhibiting C1; may perform the receptor function through a complex with C1qR/CD93. In complex with cytokeratin-1/KRT1 is a high affinity receptor for kininogen-1/HMWK. Can also bind other plasma proteins, such as coagulation factor XII leading to its autoactivation. May function to bind initially fluid kininogen-1 to the cell membrane. The secreted form may enhance both extrinsic and intrinsic coagulation pathways. It is postulated that the cell surface form requires docking with transmembrane proteins for downstream signaling which might be specific for a cell-type or response. By acting as C1q receptor is involved in chemotaxis of immature dendritic cells and neutrophils and is proposed to signal through CD209/DC-SIGN on immature dendritic cells, through integrin alpha-4/beta-1 during trophoblast invasion of the decidua, and through integrin beta-1 during endothelial cell adhesion and spreading. Signaling involved in inhibition of innate immune response is implicating the PI3K-AKT/PKB pathway. In mitochondrial translation may be involved in formation of functional 55S mitoribosomes; the function seems to involve its RNA-binding activity. May be involved in the nucleolar ribosome maturation process; the function may involve the exchange of FBL for RRP1 in the association with pre-ribosome particles. Involved in regulation of RNA splicing by inhibiting the RNA-binding capacity of SRSF1 and its phosphorylation. Is required for the nuclear translocation of splicing factor U2AF1L4. Involved in regulation of CDKN2A- and HRK-mediated apoptosis. Stabilizes mitochondrial CDKN2A isoform smARF. May be involved in regulation of FOXC1 transcriptional activity and NFY/CCAAT-binding factor complex-mediated transcription. In infection processes acts as an attachment site for microbial proteins. May play a role in antibacterial defense. Involved in regulation of antiviral response by inhibiting DDX58- and IFIH1-mediated signaling pathways probably involving its association with MAVS after viral infection. {ECO:0000269|PubMed:17486078, ECO:0000269|PubMed:18166172, ECO:0000269|PubMed:18460468, ECO:0000269|PubMed:22904065}." K18AcK21Ac 11230.25 "K,4;K,6;" 359 100 uniprot_mouse_length brain_HCD 929.2563477 924.666199 924.667757 23 21232.33526 -1.68522101 C209C_MOUSE CD209 antigen-like protein C;AltName: Full=DC-SIGN-related protein 2; Short=DC-SIGNR2;AltName: CD_antigen=CD209 Q91ZW9 MRMHTRLQFLKRVSNVAYSHGQEQAKKEKVYKEMTQLKSQINRLCRPCPWDWTVFQGNCYFFSKFQQNWNDSVNACRKLDAQLVVIKSDDEQSFLQQTSKEKGYAWMGLSDLKHEGRWHWVDGSHLLFSFMKYWNKGEPNNEWEEDCAEFRGDGWNDAPCTIKKYWICKKSAMSCTEK 178 FUNCTION: Probable pathogen-recognition receptor. May recognize in a calcium-dependent manner high mannose N-linked oligosaccharides in a variety of pathogen antigens. null 1831.02 null null 100 uniprot_mouse_length brain_HCD 544.1305542 541.743286 541.741638 28 15132.75144 3.042285652 CALC_MOUSE Calcitonin;Flags: Precursor P70160 MGFLKFSPFLVVSILLLYQACSLQAVPLRSILESSPGMATLSEEEVRLLAALVQDYMQMKARELEQEEEQEAEGSSLDSPRSKRCGNLSTCMLGTYTQDLNKFHTFPQTSIGVEAPGKKRDVAKDLETNHQSHFGN 136 FUNCTION: Causes a rapid but short-lived drop in the level of calcium and phosphate in blood by promoting the incorporation of those ions in the bones. null 2699.08 null null 100 uniprot_mouse_length brain_HCD 644.0369873 645.15033 645.155069 26 16739.01498 -7.346156582 CALM_MOUSE Calmodulin; Short=CaM P62204 ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK 148 "FUNCTION: Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis (By similarity). {ECO:0000250}." A1Ac 3699.1 "A,3;" 178 100 uniprot_mouse_length brain_HCD 968.5040283 964.48407 964.485066 19 18296.1964 -1.032857653 CAV2_MOUSE Caveolin-2 Q9WVC3 MGLETEKADVQLFMADDAYSHHSGVDYADPEKYVDSSHDRDPHQLNSHLKLGFEDLIAEPETTHSFDKVWICSHALFEISKYVMYKFLTVFLAIPLAFIAGILFATLSCLHIWILMPFVKTCLMVLPSVQTIWKSVTDVVIGPLCTSVGRSFSSVSMQLSHD 162 "FUNCTION: May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Acts as an accessory protein in conjunction with CAV1 in targeting to lipid rafts and driving caveolae formation. The Ser-36 phosphorylated form has a role in modulating mitosis in endothelial cells. Positive regulator of cellular mitogenesis of the MAPK signaling pathway. Required for the insulin-stimulated nuclear translocation and activation of MAPK1 and STAT3, and the subsequent regulation of cell cycle progression (By similarity). {ECO:0000250}." Y19P 1152.27 "Y,0;" 104 100 uniprot_mouse_length brain_HCD 642.4260864 643.835754 643.840752 29 18632.36244 -7.762176366 CB068_MOUSE UPF0561 protein C2orf68 homolog Q149G0 MEAAQDHGPGLCCKPGGRLDMSHGFVHHIRRNQLDRDDYDKKVKQAAKEKARRRHTPAPTRPRKPDLQVYLPRHRDGSTHPVNPDCEEASESSSSGSSELEPPGRQLFCLDYEADSGEVTSVIVYQDDDPGRVSEAVSAHTPLDPAMREALRSRIQEELAKRQSRH 166 SIMILARITY: Belongs to the UPF0561 family. {ECO:0000305}. null 5936.1 null null 100 uniprot_mouse_length brain_HCD 544.1303101 546.28241 546.281028 49 26704.73906 2.529225615 CB5D1_MOUSE Cytochrome b5 domain-containing protein 1 Q5NCY3 MPRRGLVAGPDLDNFQRRYFTPSEVAEHNQLEDLWVSYLGFVYNLTPLVEEFKGDLLLKPILEVAGQDISHWFDPQTRDIRKHIDPLTGCMRYRTPRGRFVHIPPPLPRSDWANDFGVPWWKGANYQVGRLSARTRNIRIINTLATQEHTLQVGAQESMWEILHRYLPYNAHAASYTWKYDGKNLNMDQTLEENGIRDEEEEFDYLNMDGKLHTPAILLYFNDDLTEL 228 "ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q5NCY3-1; Sequence=Displayed; Name=2; IsoId=Q5NCY3-2; Sequence=VSP_029825, VSP_029826;" null 2074.19 null null 100 uniprot_mouse_length brain_HCD 876.4707642 878.478638 878.47774 13 11402.20216 1.021875993 CC126_MOUSE Coiled-coil domain-containing protein 126;Flags: Precursor Q8BIS8 QPRRQSSVKLREQILDLSKRYVKALAEESRSTADVDSGASMAGYADLKRTIAVLLDDILQRLVKLESKVDYIVVNGSATNTTNGTNGNLVPVTTNKRTSVSGSVR 105 SUBCELLULAR LOCATION: Secreted {ECO:0000305}. null 1410.63 null null 100 uniprot_mouse_length brain_HCD 883.0892944 883.623474 883.631613 13 11469.20314 -9.210714948 CC167_MOUSE Coiled-coil domain-containing protein 167 Q9D162 MTKKKRENLGVAQEIDGLEEKLSRCRKDLEAVTSQLYRAELSPEDRRSLEKEKHTLMNKASKYEKELKLLRHENRKNTLLSVAIFTVFALLYAYWTM 97 SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. null 361.83 null null 100 uniprot_mouse_length brain_HCD 544.1303101 542.900574 542.893509 39 21122.82325 13.01310543 CCD53_MOUSE WASH complex subunit CCDC53;AltName: Full=Coiled-coil domain-containing protein 53 Q9CR27 MDEDGLPLMGSGIDLTKVPAIQQKRTVAFLNQFVVHTVQFLNRFSAVCEEKLADLSLRIQQIETTLNILDAKLSSIPGLEDVTVEVSPLNVTAVTNGSHSETTSEQTQQNSTQDSGAQESEAPSENVLTVAKDPRYARYLKMVQVGVPVMAIRDKMISEGLDPELLEKPDAPVPNGESERAVEESSDSDSSFSD 194 "FUNCTION: Acts at least in part as component of the WASH core complex whose assembly at the surface of endosomes seems to inhibit WASH nucleation-promoting factor (NPF) activity in recruiting and activating the Arp2/3 complex to induce actin polymerization, and which is involved in regulation of the fission of tubules that serve as transport intermediates during endosome sorting. {ECO:0000250|UniProtKB:Q9Y3C0}." M1Ac 1550.16 "M,120;" 167 100 uniprot_mouse_length brain_HCD 726.0477905 723.507141 723.510151 23 16608.71626 -4.160116779 CCD58_MOUSE Coiled-coil domain-containing protein 58 Q8R3Q6 AAPSGSVNCEEFAEFQELLKVMRTIDDRIVHELNTTVPTASFAGKIDASQTCKQLYESLMAAHVSRDRVIKNCIAQTSAVVKSLREEREKNLDDLTLLKRLRKEQTKLKWMQSELNVEEVVNDRSWKVFNERCRVHFKPPKNE 143 "SIMILARITY: Belongs to the CCDC58 family. {ECO:0000305}.-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" A1AcK99Ac 5876.27 "A,92;K,147;" 206 100 uniprot_mouse_length brain_HCD 1024.295898 1024.993774 1024.985485 9 9211.86461 8.087347757 CCL19_MOUSE C-C motif chemokine 19;AltName: Full=Epstein-Barr virus-induced molecule 1 ligand chemokine; Short=EBI1 ligand chemokine; Short=ELC;AltName: Full=Small-inducible cytokine A19;Flags: Precursor O70460 GANDAEDCCLSVTQRPIPGNIVKAFRYLLNEDGCRVPAVVFTTLRGYQLCAPPDQPWVDRIIRRLKKSSAKNKGNSTRRSPVS 83 FUNCTION: Strongly chemotactic for naive (L-selectinhi) CD4 T- cells and for CD8 T-cells and weakly attractive for resting B- cells and memory (L-selectinlo) CD4 T-cells. May play a role in promoting encounters between recirculating T-cells and dendritic cells and in the migration of activated B-cells into the T-zone of secondary lymphoid tissues. Binds to chemokine receptor CCR7. Binds to atypical chemokine receptor ACKR4 and mediates the recruitment of beta-arrestin (ARRB1/2) to ACKR4. null 651.88 null null 100 uniprot_mouse_length brain_HCD 999.5317993 997.251282 997.260826 11 10953.86234 -9.57047692 CCL27_MOUSE C-C motif chemokine 27;AltName: Full=CC chemokine ILC;AltName: Full=Cutaneous T-cell-attracting chemokine; Short=CTACK;AltName: Full=ESkine;AltName: Full=IL-11 R-alpha-locus chemokine; Short=ALP; Short=mILC;AltName: Full=Skinkine;AltName: Full=Small-inducible cytokine A27;Flags: Precursor Q9Z1X0 LPLPSSTSCCTQLYRQPLPSRLLRRIVHMELQEADGDCHLQAVVLHLARRSVCVHPQNRSLARWLERQGKRLQGTVPSLNLVLQKKMYSHPQQQN 95 FUNCTION: Chemotactic factor that attracts skin-associated memory T-lymphocytes. May play a role in mediating homing of lymphocytes to cutaneous sites. May play a role in cell migration during embryogenesis. Nuclear forms may facilitate cellular migration by inducing cytoskeletal relaxation. Binds to CCR10. null 392.04 null null 100 uniprot_mouse_length brain_HCD 750.7243652 749.135986 749.145981 12 8973.74749 -13.34142094 CCL8_MOUSE C-C motif chemokine 8;AltName: Full=Monocyte chemoattractant protein 2;AltName: Full=Monocyte chemotactic protein 2; Short=MCP-2;AltName: Full=Small-inducible cytokine A8;Flags: Precursor Q9Z121 EKLTGPDKAPVTCCFHVLKLKIPLRVLKSYERINNIQCPMEAVVFQTKQGMSLCVDPTQKWVSEYMEILDQKSQILQP 78 FUNCTION: Chemotactic factor that attracts monocytes. This protein can bind heparin (By similarity). {ECO:0000250}. null 1512.17 null null 100 uniprot_mouse_length brain_HCD 712.6341553 709.745361 709.745907 11 7793.20259 -0.768827082 CD24_MOUSE Signal transducer CD24;AltName: Full=Lymphocyte antigen 52; Short=Ly-52;AltName: Full=M1/69-J11D heat stable antigen; Short=HSA;AltName: Full=Nectadrin;AltName: Full=R13-Ag;AltName: Full=X62 heat stable antigen;AltName: CD_antigen=CD24;Flags: Precursor P24807 MGRAMVARLGLGLLLLALLLPTQIYCNQTSVAPFPGNQNISASPNPSNATTRGGGSSLQSTAGLLALSLSLLHLYC 76 FUNCTION: May have a specific role to play in early thymocyte development. null 1125.81 null null 100 uniprot_mouse_length brain_HCD 614.4029541 616.009033 616.004091 16 9836.06 8.023003738 CDC26_MOUSE Anaphase-promoting complex subunit CDC26;AltName: Full=Cell division cycle protein 26 homolog Q99JP4 MLRRKPTRLELKLDDIEEFESIRKDLEARKKQKEDVEGVGTSDGEGAAGLSSDPKSREQMINDRIGYKPQLKSNNRTSQFGNFEF 85 "FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. May recruit the E2 ubiquitin-conjugating enzymes to the complex (By similarity). {ECO:0000250}." S42P 231.22 "S,24;" 32 100 uniprot_mouse_length brain_HCD 713.2910156 716.716003 716.720041 25 17883.98387 -5.633415839 CDN1A_MOUSE Cyclin-dependent kinase inhibitor 1;AltName: Full=CDK-interacting protein 1;AltName: Full=Melanoma differentiation-associated protein;AltName: Full=p21 P39689 SNPGDVRPVPHRSKVCRCLFGPVDSEQLRRDCDALMAGCLQEARERWNFDFVTETPLEGNFVWERVRSLGLPKVYLSPGSRSRDDLGGDKRPSTSSALLQGPAPEDHVALSLSCTLVSERPEDSPGGPGTSQGRKRRQTSLTDFYHSKRRLVFCKRKP 158 "FUNCTION: May be the important intermediate by which p53/TP53 mediates its role as an inhibitor of cellular proliferation in response to DNA damage. Binds to and inhibits cyclin-dependent kinase activity, preventing phosphorylation of critical cyclin- dependent kinase substrates and blocking cell cycle progression. Functions in the nuclear localization and assembly of cyclin D- CDK4 complex and promotes its kinase activity towards RB1. At higher stoichiometric ratios, inhibits the kinase activity of the cyclin D-CDK4 complex (By similarity). {ECO:0000250}." S77PS111PS124P 5234.15 "S,46;S,0;S,0;" 200 100 uniprot_mouse_length brain_HCD 543.1710205 542.289978 542.293875 41 22181.02476 -7.186090118 CDN1B_MOUSE Cyclin-dependent kinase inhibitor 1B;AltName: Full=Cyclin-dependent kinase inhibitor p27;AltName: Full=p27Kip1 P46414 MSNVRVSNGSPSLERMDARQAEHPKPSACRNLFGPVNHEELTRDLEKHCRDMEEASQRKWNFDFQNHKPLEGRYEWQEVERGSLPEFYYRPPRPPKSACKVLAQESQDVSGSRQAVPLIGSQANSEDRHLVDQMPDSSDNPAGLAEQCPGMRKRPAAEDSSSQNKRANRTEENVSDGSPNAGTVEQTPKKPGLRRQT 197 "FUNCTION: Important regulator of cell cycle progression. Involved in G1 arrest. Potent inhibitor of cyclin E- and cyclin A-CDK2 complexes. Forms a complex with cyclin type D-CDK4 complexes and is involved in the assembly, stability, and modulation of cyclin D-CDK4 complex activation. Acts either as an inhibitor or an activator of cyclin type D-CDK4 complexes depending on its phosphorylation state and/or stoichometry. {ECO:0000269|PubMed:12093740, ECO:0000269|PubMed:15528185, ECO:0000269|PubMed:20228253, ECO:0000269|PubMed:9399644}." null 2891.62 null null 100 uniprot_mouse_length brain_HCD_6 615.4825439 619.689575 619.693781 36 22260.95201 -6.786908012 CDN1B_MOUSE Cyclin-dependent kinase inhibitor 1B;AltName: Full=Cyclin-dependent kinase inhibitor p27;AltName: Full=p27Kip1 P46414 MSNVRVSNGSPSLERMDARQAEHPKPSACRNLFGPVNHEELTRDLEKHCRDMEEASQRKWNFDFQNHKPLEGRYEWQEVERGSLPEFYYRPPRPPKSACKVLAQESQDVSGSRQAVPLIGSQANSEDRHLVDQMPDSSDNPAGLAEQCPGMRKRPAAEDSSSQNKRANRTEENVSDGSPNAGTVEQTPKKPGLRRQT 197 "FUNCTION: Important regulator of cell cycle progression. Involved in G1 arrest. Potent inhibitor of cyclin E- and cyclin A-CDK2 complexes. Forms a complex with cyclin type D-CDK4 complexes and is involved in the assembly, stability, and modulation of cyclin D-CDK4 complex activation. Acts either as an inhibitor or an activator of cyclin type D-CDK4 complexes depending on its phosphorylation state and/or stoichometry. {ECO:0000269|PubMed:12093740, ECO:0000269|PubMed:15528185, ECO:0000269|PubMed:20228253, ECO:0000269|PubMed:9399644}." S10P 2732.57 "S,31;" 213 100 uniprot_mouse_length brain_HCD 780.6083984 784.488464 784.477633 23 18010.96876 13.80709279 CDN2A_MOUSE Cyclin-dependent kinase inhibitor 2A {ECO:0000312|MGI:MGI:104738};AltName: Full=Cyclin-dependent kinase 4 inhibitor A; Short=CDK4I;AltName: Full=p16-INK4a; Short=p16-INK4 P51480 MESAADRLARAAAQGRVHDVRALLEAGVSPNAPNSFGRTPIQVMMMGNVHVAALLLNYGADSNCEDPTTFSRPVHDAAREGFLDTLVVLHGSGARLDVRDAWGRLPLDLAQERGHQDIVRYLRSAGCSLCSAGWSLCTAGNVAQTDGHSFSSSTPRALELRGQSQEQS 168 FUNCTION: Acts as a negative regulator of the proliferation of normal cells by interacting strongly with CDK4 and CDK6. This inhibits their ability to interact with cyclins D and to phosphorylate the retinoblastoma protein. S152P 1702.84 "S,5;" 147 100 uniprot_mouse_length brain_HCD 713.2910156 715.219177 715.223073 13 9280.89526 -5.44690748 CEBOS_MOUSE Protein CEBPZOS {ECO:0000305} Q8BTE5 MARIMEPLARKIFKGVLAAELVGVAGAYCLFKKMHSSQDFRQTMSKKFPFILEVYYKSIEQSGMYGVREKDEEKWLTSKN 80 "SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250|UniProtKB:A8MTT3}; Single-pass membrane protein {ECO:0000255}.-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" null 1884.29 null null 100 uniprot_mouse_length brain_HCD 651.0525513 649.913086 649.910503 15 9728.65085 3.974297212 CENPW_MOUSE Centromere protein W; Short=CENP-W;AltName: Full=Cancer-up-regulated gene 2 protein Q3URR0 MAPSTTVTRRVKRKAPRAFLKRTLKQKKPHLGLGRCCDLLIHLNCLLFIQRLAEESRTNACESKSRVIKKDHVLAAGKVILKKSRG 86 "FUNCTION: Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation (By similarity). The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres (By similarity). Part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere, as opposed to nucleosomes containing CENPA. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA, and plays an important role in kinetochore assembly. CENPW has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins, with most further proteins binding downstream. Required for normal chromosome organization and normal progress through mitosis (By similarity). {ECO:0000250}." null 664.43 null null 100 uniprot_mouse_length brain_HCD 644.0369873 641.559387 641.559672 14 8963.83002 -0.443907217 CENPX_MOUSE Centromere protein X; Short=CENP-X;AltName: Full=FANCM-interacting histone fold protein 2;AltName: Full=Fanconi anemia-associated polypeptide of 10 kDa;AltName: Full=Immediate-early-response protein D9;AltName: Full=Retinoic acid-inducible gene D9 protein;AltName: Full=Stimulated by retinoic acid gene 13 protein homolog Q8C4X1 MEGNSGFRKELVSRLLHLHFRDCKTKVSGDALQLMAEFLRIFVLEAAVRGVWQAQAEDLDVVEVDQLEKVLPQLLLDF 78 "FUNCTION: DNA-binding component of the FA core complex involved in DNA damage repair and genome maintenance. Recruited to forks stalled by DNA interstrand cross-links, and required for cellular resistance to such lesions. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA, and plays an important role in kinetochore assembly. Component of the APITD1/CENPS complex that is essential for the stable assembly of the outer kinetochore. Plays an important role in mitotic progression and chromosome segregation (By similarity). {ECO:0000250}." M1Ac 959.03 "M,46;" 63 100 uniprot_mouse_length brain_HCD 876.4707642 873.471375 873.480164 14 12208.71175 -10.06260777 CH004_MOUSE Uncharacterized protein C8orf4 homolog Q9D915 MKAKPSHQATSMSSSLRVSPSIHGYHFDTAARKKAVGNIFENIDQESLQRLFRNSGDKKAEERAKIIFAIDQDLEEKTRALMALKKRTKDKLLQFLKLRKYSIKVH 106 FUNCTION: May decrease apoptosis. {ECO:0000250}. null 1054.26 null null 100 uniprot_mouse_length brain_HCD 778.3515015 777.639526 777.640107 14 10867.95258 -0.746660064 CH10_MOUSE "10 kDa heat shock protein, mitochondrial; Short=Hsp10;AltName: Full=10 kDa chaperonin;AltName: Full=Chaperonin 10; Short=CPN10" Q64433 AGQAFRKFLPLFDRVLVERSAAETVTKGGIMLPEKSQGKVLQATVVAVGSGGKGKSGEIEPVSVKVGDKVLLPEYGGTKVVLDDKDYFLFRDSDILGKYVD 101 "FUNCTION: Eukaryotic CPN10 homolog which is essential for mitochondrial protein biogenesis, together with CPN60. Binds to CPN60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter." A1Ac 3840.4 "A,3;" 148 100 uniprot_mouse_length brain_HCD 545.3996582 540.848572 540.854614 47 25360.14264 -11.1716208 CHM2A_MOUSE Charged multivesicular body protein 2a;AltName: Full=Chromatin-modifying protein 2a; Short=CHMP2a;AltName: Full=Vacuolar protein sorting-associated protein 2; Short=mVps2 Q9DB34 MDLLFGRRKTPEELLRQNQRALNRAMRELDRERQKLETQEKKIIADIKKMAKQGQMDAVRIMAKDLVRTRRYVRKFVLMRANIQAVSLKIQTLKSNNSMAQAMKGVTKAMGTMNRQLKLPQIQKIMMEFERQAEIMDMKEEMMNDAIDDAMGDEEDEEESDAVVSQVLDELGLSLTDELSNLPSTGGSLSVAAGGKKAEATASALADADADLEERLKNLRRD 222 "FUNCTION: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4 (By similarity). {ECO:0000250}." S184PT185PS188P 1962.95 "S,2;T,0;S,0;" 202 100 uniprot_mouse_length brain_HCD 588.9731445 587.649353 587.643787 24 14072.4376 9.471770938 CHRC1_MOUSE Chromatin accessibility complex protein 1; Short=CHRAC-1;AltName: Full=DNA polymerase epsilon subunit p15;AltName: Full=NF-YC-like protein;AltName: Full=YC-like protein 1; Short=YCL1 Q9JKP8 ADAAVGKEKCGDQRLVSLPLSRIRVIMKSSPEVSSINQEALVLTAKATELFVQYLATCSYRHGSGKAKKALTYSDLASTAEDSETLQFLADILPKKILASKYLKMLKEKREEEEDNEDDGSDLGEALA 128 "FUNCTION: Forms a complex with DNA polymerase epsilon subunit POLE3 and binds naked DNA, which is then incorporated into chromatin, aided by the nucleosome remodeling activity of ISWI/SNF2H and ACF1. {ECO:0000250}." A1AcK101Ac 5728.86 "A,122;K,164;" 182 100 uniprot_mouse_length brain_HCD 615.968689 613.710205 613.70461 26 15922.30433 9.116891146 CHSP1_MOUSE Calcium-regulated heat stable protein 1;AltName: Full=Calcium-regulated heat-stable protein of 24 kDa; Short=CRHSP-24 Q9CR86 SSEPPPPPLQPPTHQTSVGLLDTPRTRDRSPSPLRGNVVPSPLPTRRTRTFSATVRASQGPVYKGVCKCFCRSKGHGFITPADGGPDIFLHISDVEGEYVPVEGDEVTYKMCSIPPKNEKLQAVEVVITHLAPGTKHETWSGHVISN 147 FUNCTION: Binds mRNA and regulates the stability of target mRNA. {ECO:0000269|PubMed:21078874}. null 2820.79 null null 100 uniprot_mouse_length brain_HCD_6 684.4483032 680.496094 680.488971 23 15620.23137 10.46710572 CISD3_MOUSE "CDGSH iron-sulfur domain-containing protein 3, mitochondrial;AltName: Full=Melanoma nuclear protein 13;Flags: Precursor" B1AR13 GFRRLSFPTDFIFLFPNHICLPALSKPYQRREISSWLARWFPKDPAKPVVAQKTPIRLELVAGKTYRWCVCGRSKNQPFCDGSHFFQRTGLSPLKFKAQETRTVALCTCKATQRPPYCDGTHKSEQVQKAEVGSPL 136 COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601; Evidence={ECO:0000250}; Note=Binds 2 [2Fe-2S] clusters per subunit. {ECO:0000250}; K64AcK95Ac 1838.23 "K,29;K,0;" 123 100 uniprot_mouse_length brain_HCD 543.1710205 542.289978 542.28398 18 9738.10377 11.06067589 CKS2_MOUSE Cyclin-dependent kinases regulatory subunit 2; Short=CKS-2 P56390 AHKQIYYSDKYFDEHYEYRHVMLPRELSKQVPKTHLMSEEEWRRLGVQQSLGWVHYMIHEPEPHILLFRRPLPKEQQK 78 FUNCTION: Binds to the catalytic subunit of the cyclin dependent kinases and is essential for their biological function. null 583.43 null null 100 uniprot_mouse_length brain_HCD 858.5696411 854.934814 854.936983 27 23043.27236 -2.536499085 CLD9_MOUSE Claudin-9 Q9Z0S7 MASTGLELLGMTLAVLGWLGTLVSCALPLWKVTAFIGNSIVVAQVVWEGLWMSCVVQSTGQMQCKVYDSLLALPQDLQAARALCVVALLLALLGLLVAITGAQCTTCVEDEGAKARIVLTAGVLLLLSGILVLIPVCWTAHAIIQDFYNPLVAEALKRELGASLYLGWAAAALLMLGGGLLCCTCPPSHFERPRGPRLGYSIPSRSGASGLDKRDYV 217 "FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium- independent cell-adhesion activity. {ECO:0000250}." S201PS206P 1776.6 "S,4;S,0;" 159 100 uniprot_mouse_length brain_HCD 910.3096313 913.479126 913.481538 20 18239.61102 -2.64047311 CLDN2_MOUSE Claudin domain-containing protein 2 Q9D9H2 MGVKKSLQTGGNLLNLLSSILTVLSTTTNYWTRQQGGHSGLWQECTHGKCSNIPCQNTVAVSAACMVLAATFSIVALGIGIRIQCREAESRRSQNTIVLLFLSGLLLLIALAVYTSKNAWKPEVFFSWSYFFGWLALPFLFIAGFCFLLADMILQSTEAISGFPVCL 167 SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. null 2274.88 null null 100 uniprot_mouse_length brain_HCD 703.1317749 706.673523 706.665467 13 9169.64659 11.39994749 CNBP1_MOUSE Beta-catenin-interacting protein 1;AltName: Full=Inhibitor of beta-catenin and Tcf-4 Q9JJN6 MNREGAPGKSPEEMYIQQKVRVLLMLRKMGSNLTASEEEFLRTYAGVVSSQLSQLPQHSIDQGAEDVVMAFSRSETEDRRQ 81 "FUNCTION: Prevents the interaction between CTNNB1 and TCF family members, and acts as negative regulator of the Wnt signaling pathway." null 1453.95 null null 100 uniprot_mouse_length brain_HCD 1182.540527 1185.712158 1185.717193 11 13024.87665 -4.246203821 COX20_MOUSE Cytochrome c oxidase protein 20 homolog Q9D7J4 AAAPEPHETEKKPFKLLGILDVENTPCARESILYGSLGSIVTGLGHFLVTSRIRRSCDVGVGGFILVTLGCWFHCRYNFAKQRIQERIAREGIKNKILYESTHLDPERKMKTNNSS 116 SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305}; Multi- pass membrane protein {ECO:0000305}. null 239.46 null null 100 uniprot_mouse_length brain_HCD 1044.915161 1044.308594 1044.293625 12 12513.51222 14.33385175 COX5A_MOUSE "Cytochrome c oxidase subunit 5A, mitochondrial;AltName: Full=Cytochrome c oxidase polypeptide Va;Flags: Precursor" P12787 SHGSHETDEEFDARWVTYFNKPDIDAWELRKGMNTLVGYDLVPEPKIIDAALRACRRLNDFASAVRILEVVKDKAGPHKEIYPYVIQELRPTLNELGISTPEELGLDKV 109 "FUNCTION: This is the heme A-containing chain of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport." K46AcK72Ac 478.27 "K,10;K,11;" 51 100 uniprot_mouse_length brain_HCD 705.0968018 701.90332 701.909941 9 6306.18926 -9.432388848 COX7B_MOUSE "Cytochrome c oxidase subunit 7B, mitochondrial;AltName: Full=Cytochrome c oxidase polypeptide VIIb;Flags: Precursor" P56393 SHQKRAPSFHDKYGNAILAGGAIFCVSTWTYTATQIGIEWNMSPVGRVTPKEWRDQ 56 "FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. Plays a role in proper central nervous system (CNS) development in vertebrates (By similarity). {ECO:0000250}." null 499.92 null null 100 uniprot_mouse_length brain_HCD_6 961.1241455 956.428284 956.420953 13 12414.46329 7.664712262 COXM1_MOUSE COX assembly mitochondrial protein homolog; Short=Cmc1p Q9CPZ8 ALDPAEQHLRHVEKDVLIPKIIREKARERCSEQVEDFTRCCKDSGILMVLKCRKENSALKDCLTAYYNDPAFYEECKLEYLKEREEFRKTGVPTKKRLQKLPTNM 105 FUNCTION: Required for mitochondrial cytochrome c oxidase (COX) assembly and respiration. {ECO:0000250}. null 519.67 null null 100 uniprot_mouse_length brain_HCD 728.9130249 725.4422 725.44092 13 9413.72822 1.764040318 COXM2_MOUSE COX assembly mitochondrial protein 2 homolog Q8K199 MHPDLSPHLHTEECNVLINLLKECHKNHNILKFFGHCNDLDREMRKCLKNEYSERRTRSREHGAAMRRRLSDPPEEAGR 79 FUNCTION: May be involved in cytochrome c oxidase biogenesis. {ECO:0000250}. null 1171.17 null null 100 uniprot_mouse_length brain_HCD 542.0480347 545.592712 545.591936 49 26671.97879 1.423045856 CR025_MOUSE Uncharacterized protein C18orf25 homolog Q8BH50 MKMEEAVGKVEELIESAAPPKASEQETAKEEDGSVELESQVQKDGVADSTVLSSMPCLLMELRRDSSESQLASTESDKPTTGRVYESDSSNHCMLSPSSSGHLADSDTLSSVEENEPSQAETTVEGDTSGVSGATVGRKSRRSRSESETSTMAAKKNRQSSDKQNGRVTKVKGHRSQKHKERIRLLRQKREAAARKKYNLLQDSSTSDSDLTCDSSTSSSDDDDEVSGSSKTITAEIPGRGCFLN 245 "ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q8BH50-1; Sequence=Displayed; Name=2; IsoId=Q8BH50-2; Sequence=VSP_014754, VSP_014755; Note=No experimental confirmation available.;-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" S66PS143PS145P 4476.43 "S,80;S,0;S,2;" 323 100 uniprot_mouse_length brain_HCD 546.4417725 542.66864 542.668172 43 23278.70225 0.862657408 CRBB2_MOUSE Beta-crystallin B2;AltName: Full=Beta-B2 crystallin;AltName: Full=Beta-crystallin Bp P62696 ASDHQTQAGKPQPLNPKIIIFEQENFQGHSHELSGPCPNLKETGMEKAGSVLVQAGPWVGYEQANCKGEQFVFEKGEYPRWDSWTSSRRTDSLSSLRPIKVDSQEHKIILYENPNFTGKKMEIVDDDVPSFHAHGYQEKVSSVRVQSGTWVGYQYPGYRGLQYLLEKGDYKDNSDFGAPHPQVQSVRRIRDMQWHQRGAFHPSS 204 FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens. A1Ac 1710 "A,125;" 172 100 uniprot_mouse_length brain_HCD 632.9466553 633.452087 633.455079 36 22755.35783 -4.722667408 CRIP2_MOUSE Cysteine-rich protein 2; Short=CRP-2;AltName: Full=Heart LIM protein Q9DCT8 MASKCPKCDKTVYFAEKVSSLGKDWHKFCLKCERCNKTLTPGGHAEHDGKPFCHKPCYATLFGPKGVNIGGAGSYIYEKPQTEAPQVTGPIEVPVVRTEERKTSGPPKGPSKASSVTTFTGEPNMCPRCNKRVYFAEKVTSLGKDWHRPCLRCERCSKTLTPGGHAEHDGQPYCHKPCYGILFGPKGVNTGAVGSYIYDKDPEGTVQP 208 SUBUNIT: Interacts with TGFB1I1. {ECO:0000269|PubMed:15713747}. K23Ac 2880.37 "K,74;" 209 100 uniprot_mouse_length brain_HCD 644.0369873 647.119507 647.129114 35 22602.49253 -14.84582266 CRYAA_MOUSE Alpha-crystallin A chain P24622 MDVTIQHPWFKRALGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISELMTHMWFVMHQPHAGNPKNNPVKVRSDRDKFVIFLDVKHFSPEDLTVKVLEDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFSGPKVQSGLDAGHSERAIPVSREEKPSSAPSS 196 "FUNCTION: Contributes to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions (By similarity). {ECO:0000250}." M1AcK93AcK122Ac 5909.85 "M,72;K,0;K,32;" 264 100 uniprot_mouse_length brain_HCD 644.0369873 642.021851 642.017761 16 10251.27608 6.36989533 CS024_MOUSE Uncharacterized membrane protein C19orf24 homolog;Flags: Precursor Q9DAZ5 ENSSLPGPPYNHTNGRLPDRDTGSAVLRLFYVITGLCGLISLYFLIRAFRLKKSQRRRYGLLTNTEEHEEMASQDSEEETVFETRNLR 88 "SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" S73P 1105 "S,5;" 80 100 uniprot_mouse_length brain_HCD 857.7901611 861.890686 861.888668 11 9465.77084 2.341410476 CSEN4_MOUSE Calsenilin isoform 4 P0C092 MRQLPAGPSSLACSGCKAGRLVTVPFSSRDAEDQGSREGIGWQPPGRSWAHTTEQEGKHQVAKATVHPPGPDALLLNQVDPVQCCPTRL 89 "FUNCTION: Unknown for isoform 4. Csen is involved in calcium- dependent transcriptional repression, regulation of potassium channels, and perhaps in processing of PSEN2 and apoptosis." null 932.15 null null 100 uniprot_mouse_length brain_HCD 544.1303101 545.971741 545.976724 38 20697.09385 -9.127270678 CSRP1_MOUSE Cysteine and glycine-rich protein 1;AltName: Full=Cysteine-rich protein 1; Short=CRP; Short=CRP1 P97315 MPNWGGGKKCGVCQKTVYFAEEVQCEGNSFHKSCFLCMVCKKNLDSTTVAVHGEEIYCKSCYGKKYGPKGYGYGQGAGTLSTDKGESLGIKHEEAPGHRPTTNPNASKFAQKIGGSERCPRCSQAVYAAEKVIGAGKSWHKSCFRCAKCGKGLESTTLADKDGEIYCKGCYAKNFGPKGFGFGQGAGALVHSE 193 FUNCTION: Could play a role in neuronal development. {ECO:0000250}. K84AcK112AcK131Ac 1130.45 "K,15;K,0;K,0;" 144 100 uniprot_mouse_length brain_HCD 651.0525513 646.237549 646.241449 22 14188.29982 -6.035162061 CST8_MOUSE Cystatin-8;AltName: Full=Cystatin-related epididymal spermatogenic protein;AltName: Full=Cystatin-related epididymal-specific protein;Flags: Precursor P32766 VGVDQSKNEVKAQNYFGSINISNANVKQCVWFAMKEYNKESEDKYVFLVDKILHAKLQITDRMEYQIDVQISRSNCKKPLNNTENCIPQKKPELEKKMSCSFLVGALPWNGEFNLLSKECKDV 123 FUNCTION: Performs a specialized role during sperm development and maturation. null 1866.92 null null 100 uniprot_mouse_length brain_HCD 757.0575562 755.810059 755.817359 12 9053.80336 -9.658955518 CTXN1_MOUSE Cortexin-1 Q8K129 MSSAWTLSPEPLPPSTGPPVGAGLDVEQRTVFAFVLCLLVVLVLLMVRCVRILLDPYSRMPASSWTDHKEALERGQFDYALV 82 FUNCTION: May mediate extracellular or intracellular signaling of cortical neurons during forebrain development. {ECO:0000250}. null 1422.35 null null 100 uniprot_mouse_length brain_HCD 683.6676025 680.356995 680.358375 13 8827.6536 -2.028888222 CTXN3_MOUSE Cortexin-3 Q8BXZ0 MDGGQPVPSPLVPLGNGSDYSMSLEQKTTFVFVILLFIFLGILIVRCFRILLDPYRSMPTSTWADGLEGLEKGQFDHALA 80 SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. null 2385.08 null null 100 uniprot_mouse_length brain_HCD 788.9657593 786.066711 786.064628 12 9416.77028 2.650451002 CX6A2_MOUSE "Cytochrome c oxidase subunit 6A2, mitochondrial;AltName: Full=Cytochrome c oxidase polypeptide VIa-heart; Short=COXVIAH;Flags: Precursor" P43023 ASAAKGDHGGAGANTWRLLTFVLALPGVALCSLNCWMHAGHHERPEFIPYHHLRIRTKPFAWGDGNHTLFHNPHVNPLPTGYEHP 85 "FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport." null 1543.23 null null 100 uniprot_mouse_length brain_HCD 836.0684814 836.332458 836.330633 12 10018.96037 2.182744505 CX6B1_MOUSE Cytochrome c oxidase subunit 6B1;AltName: Full=Cytochrome c oxidase subunit VIb isoform 1; Short=COX VIb-1 P56391 AEDIKTKIKNYKTAPFDSRFPNQNQTKNCWQNYLDFHRCEKAMTAKGGDVSVCEWYRRVYKSLCPVSWVSAWDDRIAEGTFPGKI 85 FUNCTION: Connects the two COX monomers into the physiological dimeric form. {ECO:0000250}. A1AcK61Ac 381.11 "A,13;K,17;" 37 100 uniprot_mouse_length brain_HCD 758.6699829 761.41864 761.420628 16 12160.72091 -2.610729481 CXCL9_MOUSE C-X-C motif chemokine 9;AltName: Full=Gamma-interferon-induced monokine;AltName: Full=Monokine induced by interferon-gamma; Short=MIG; Short=MuMIG;AltName: Full=Protein m119;AltName: Full=Small-inducible cytokine B9;Flags: Precursor P18340 TLVIRNARCSCISTSRGTIHYKSLKDLKQFAPSPNCNKTEIIATLKNGDQTCLDPDSANVKKLMKEWEKKISQKKKQKRGKKHQKNMKNRKPKTPQSRRRSRKTT 105 "FUNCTION: May be a cytokine that affects the growth, movement, or activation state of cells that participate in immune and inflammatory response." null 306.4 null null 100 uniprot_mouse_length brain_HCD 642.4260864 638.493408 638.484228 24 15291.60503 14.37812043 CYB5B_MOUSE Cytochrome b5 type B;AltName: Full=Cytochrome b5 outer mitochondrial membrane isoform;Flags: Precursor Q9CQX2 KVEGSEPSVTYYRLEEVAKRNSAEETWMVIHGRVYDITRFLSEHPGGEEVLLEQAGADATESFEDVGHSPDAREMLKQYYIGDVHPSDLKPKGDDKDPSKNNSCQSSWAYWFVPIVGAILIGFLYRHFWADSKSS 135 FUNCTION: Cytochrome b5 is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases. {ECO:0000250}. null 3630.17 null null 100 uniprot_mouse_length brain_HCD 689.0536499 685.353943 685.356885 17 11628.05681 -4.292842125 CYC_MOUSE "Cytochrome c, somatic" P62897 GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAAGFSYTDANKNKGITWGEDTLMEYLENPKKYIPGTKMIFAGIKKKGERADLIAYLKKATNE 104 "FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. {ECO:0000269|PubMed:12062423}." Y48PY97P 3324.6 "Y,57;Y,29;" 127 100 uniprot_mouse_length brain_HCD 921.4906006 919.567383 919.559887 12 11017.71059 8.151521838 DAP1_MOUSE Death-associated protein 1; Short=DAP-1 Q91XC8 SSPPEGKLETKAGHPPAVKAGGMRIVQKHPHTGDGKEERDKDDQEWESTSPPKPTVFISGVIARGDKDFPPAAAQVAHQKPHASMDKHVSPRTQHIQQPRK 101 FUNCTION: Negative regulator of autophagy. Involved in mediating interferon-gamma-induced cell death (By similarity). {ECO:0000250}. null 489.65 null null 100 uniprot_mouse_length brain_HCD 739.6512451 741.442139 741.450884 15 11101.75518 -11.79488529 DAP1_MOUSE Death-associated protein 1; Short=DAP-1 Q91XC8 SSPPEGKLETKAGHPPAVKAGGMRIVQKHPHTGDGKEERDKDDQEWESTSPPKPTVFISGVIARGDKDFPPAAAQVAHQKPHASMDKHVSPRTQHIQQPRK 101 FUNCTION: Negative regulator of autophagy. Involved in mediating interferon-gamma-induced cell death (By similarity). {ECO:0000250}. S1AcK28Ac 155.39 "S,0;K,6;" 28 100 uniprot_mouse_length brain_HCD 907.9122314 909.649109 909.654219 13 11806.49538 -5.617643688 DAPL1_MOUSE Death-associated protein-like 1;AltName: Full=Early epithelial differentiation-associated protein Q9D757 MANEVQVLPSPLKGRYAPAVKAGGMRISKKQEMGVLERHTKKTGLEKTSAITNVAKIQMLDALTDTLDKLNHKFPATVHTAHQKPTPALEKAAPMKRAYIIQQPRKC 107 FUNCTION: May play a role in the early stages of epithelial differentiation or in apoptosis. {ECO:0000269|PubMed:15920738}. null 1350.19 null null 100 uniprot_mouse_length brain_HCD 542.12677 540.512146 540.510154 40 21568.38194 3.685399948 DDT4L_MOUSE DNA damage-inducible transcript 4-like protein;AltName: Full=HIF-1 responsive protein RTP801-like;AltName: Full=Soleus muscle atrophied after hindlimb suspension protein 1 Q8VHZ5 MVATGSLSSKNPASISELLDGGYHPGSLLSDFDYWDYVVPEPNLNEVVFEETTCQNLVKMLENCLSRSKQTKLGCSKVLVPEKLTQRIAQDVLRLSSTEPCGLRGCVMHVNLEIENVCKKLDRIVCDASVVPTFELTLVFKQESCPWTSLKDFFFSRGRFSSGLKRTLILSSGFRLVKKKLYSLIGTTVIEEC 193 FUNCTION: Inhibits cell growth by regulating the TOR signaling pathway upstream of the TSC1-TSC2 complex and downstream of AKT1. {ECO:0000250}. null 3194.17 null null 100 uniprot_mouse_length brain_HCD 654.769104 651.082642 651.09063 16 10396.4414 -12.26925726 DEXI_MOUSE Dexamethasone-induced protein;AltName: Full=Protein MYLE Q9WUQ7 MPGARVAAHLDALGPLVSYVQPPLLPSMFYVGLFFVNVLILYYAFLMEYIVLNVGLVFLPEDLDQALVDLGVLSDPGSGLYDADSELDVFDGYLE 95 "SIMILARITY: Belongs to the DEXI family. {ECO:0000305}.-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" null 1094.78 null null 100 uniprot_mouse_length brain_HCD 732.2070313 734.635437 734.627593 12 8799.52735 10.67753484 DFB20_MOUSE "Beta-defensin 20; Short=BD-20; Short=mBD-20;AltName: Full=Defensin, beta 20;Flags: Precursor" Q30KP3 KRCFSNVEGYCRKKCRLVEISEMGCLHGKYCCVNELENKKHKKHSVVEETVKLQDKSKVQDYMILPTVTYYTISI 75 FUNCTION: Has antibacterial activity. {ECO:0000250}. null 1071.84 null null 100 uniprot_mouse_length brain_HCD 543.1710205 540.647339 540.651823 35 18877.79323 -8.293938209 DNPH1_MOUSE 2'-deoxynucleoside 5'-phosphate N-hydrolase 1 {ECO:0000255|HAMAP-Rule:MF_03036}; EC=3.2.2.- {ECO:0000255|HAMAP-Rule:MF_03036};AltName: Full=c-Myc-responsive protein Rcl {ECO:0000255|HAMAP-Rule:MF_03036} Q80VJ3 AASGELVPCSVYFCGSIRGGREDQALYSRIVSRLRRYGKVLTEHVADAELEPRGEEAAGGDQFIHERDLAWLRQADVVVAEVTQPSLGVGYELGRAVALGKPILCLFRPQSGRVLSAMIRGAADGSRFQVWDYAEEEVETMLHRYFEAYLPQGTASSSNPSACLNPTVLEKI 172 FUNCTION: Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5- phosphate and a purine or pyrimidine base. Deoxyribonucleoside 5'- monophosphates containing purine bases are preferred to those containing pyrimidine bases. {ECO:0000255|HAMAP-Rule:MF_03036}. A1Ac 2656.31 "A,174;" 196 100 uniprot_mouse_length brain_HCD 658.4674683 653.618652 653.611126 29 18915.70206 11.5150178 DNPH1_MOUSE 2'-deoxynucleoside 5'-phosphate N-hydrolase 1 {ECO:0000255|HAMAP-Rule:MF_03036}; EC=3.2.2.- {ECO:0000255|HAMAP-Rule:MF_03036};AltName: Full=c-Myc-responsive protein Rcl {ECO:0000255|HAMAP-Rule:MF_03036} Q80VJ3 AASGELVPCSVYFCGSIRGGREDQALYSRIVSRLRRYGKVLTEHVADAELEPRGEEAAGGDQFIHERDLAWLRQADVVVAEVTQPSLGVGYELGRAVALGKPILCLFRPQSGRVLSAMIRGAADGSRFQVWDYAEEEVETMLHRYFEAYLPQGTASSSNPSACLNPTVLEKI 172 FUNCTION: Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5- phosphate and a purine or pyrimidine base. Deoxyribonucleoside 5'- monophosphates containing purine bases are preferred to those containing pyrimidine bases. {ECO:0000255|HAMAP-Rule:MF_03036}. S16P 3344.35 "S,46;" 195 100 uniprot_mouse_length brain_HCD 978.0792236 976.141296 976.134463 17 16569.27006 7.000456369 DPOE3_MOUSE DNA polymerase epsilon subunit 3; EC=2.7.7.7;AltName: Full=DNA polymerase II subunit 3;AltName: Full=DNA polymerase epsilon subunit p17;AltName: Full=NF-YB-like protein;AltName: Full=YB-like protein 1; Short=YBL1 Q9JKP7 AERPEDLNLPNAVITRIIKEALPDGVNISKEARSAISRAASVFVLYATSCANNFAMKGKRKTLNASDVLSAMEEMEFQRFITPLKEALEAYRRDEKGKKEASEQKKKDKDKKDSEEQDKSREVEEEDEERLDEDDQNEEEEIDN 144 "FUNCTION: Forms a complex with DNA polymerase epsilon subunit CHRAC1 and binds naked DNA, which is then incorporated into chromatin, aided by the nucleosome-remodeling activity of ISWI/SNF2H and ACF1. {ECO:0000250}." T82P 1657.56 "T,34;" 124 100 uniprot_mouse_length brain_HCD 615.4825439 614.414917 614.418162 20 12262.35234 -5.281432115 DPOE4_MOUSE DNA polymerase epsilon subunit 4; EC=2.7.7.7;AltName: Full=DNA polymerase II subunit 4;AltName: Full=DNA polymerase epsilon subunit p12 Q9CQ36 AAAAAAGSGTPREEEAPGGEAAASQAQAPTSAPGGVRLSRLPLARVKALVKADPDVTLAGQEAIFILARAAELFVETIAKDAYCCAQQGKRKTLQRRDLDNAIEAVDEFAFLEGTLD 117 FUNCTION: May play a role in allowing polymerase epsilon to carry out its replication and/or repair function. T10PS24P 1039.5 "T,2;S,10;" 97 100 uniprot_mouse_length brain_HCD 544.1305542 540.718506 540.710856 21 11328.91951 14.14778211 DPY30_MOUSE Protein dpy-30 homolog;AltName: Full=Dpy-30-like protein; Short=Dpy-30L Q99LT0 MESEQMLEGQTQVAENPHSEYGLTDSVERIVENEKINAEKSSKQKVDLQSLPTRAYLDQTVVPILLQGLAVLAKERPPNPIEFLASYLLKNKAQFEDRN 99 "FUNCTION: As part of the MLL1/MLL complex, involved in the methylation of histone H3 at 'Lys-4', particularly trimethylation. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. May play some role in histone H3 acetylation. In embryonic stem (ES) cells, plays a crucial role in the differentiation potential, particularly along the neural lineage, regulating gene induction and histone H3 'Lys- 4' methylation at key developmental loci, including that mediated by retinoic acid. Does not affect ES cell self-renewal. May also play an indirect or direct role in endosomal transport. {ECO:0000269|PubMed:21335234}." M1AcS19P 1247.65 "M,10;S,100;" 102 100 uniprot_mouse_length brain_HCD 628.1668091 629.312317 629.306349 27 16955.25395 9.483289881 DSCR6_MOUSE Protein ripply3;AltName: Full=Down syndrome critical region protein 6 Q924S9 MRPEAAGVREARGRLCHCPGDDPGRLPLPRGPESSIPAPWRPWMSPPPGDAELTRTERPCESWGDQHTSGSKGAFGFQHPVRLYLPVSKRQEYLQSSGEKVLASFPVQATIHFYNDDSESGSEEEQEEEAQPNHLQCLEAEVRDSAQEERAE 152 FUNCTION: Acts as a transcriptional corepressor. Negative regulator of the transcriptional activity of TBX1. Plays a role in the development of the pharyngeal apparatus and derivatives. {ECO:0000269|PubMed:21177346}. null 2016.71 null null 100 uniprot_mouse_length brain_HCD 614.5835571 618.016235 618.015994 21 12950.32438 0.390526402 DYLT3_MOUSE Dynein light chain Tctex-type 3;AltName: Full=Protein 91/23;AltName: Full=T-complex-associated testis-expressed 1-like P56387 MEGYQRPCDEVGFNADEAHNIVKECVDGVLGGNDYNENNINQWTASIVEQSITHLVKLGKAYKYIVTCAVVQRSPYGFHTASSCFWDTTSDGTCTIRWENRTMNCIVNVFAVAIVL 116 FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Probably binds BUB3 as part of transport cargo. Required for the efficient progression through mitosis. null 1229.66 null null 100 uniprot_mouse_length brain_HCD 542.0480347 543.676697 543.682952 31 16814.15396 -11.50527644 EFNA4_MOUSE Ephrin-A4;AltName: Full=EPH-related receptor tyrosine kinase ligand 4; Short=LERK-4;Flags: Precursor O08542 LRHPIYWNSSNPRLLRGDAVVELGFNDYLDIFCPHYESPGPPEGPETFALYMVDWSGYEACTAEGANAFQRWNCSMPFAPFSPVRFSEKIQRYTPFPLGFEFLPGETYYYISVPTPESPGRCLRLQVSVCCKESGSSHESAHPVGSPGES 150 "FUNCTION: Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. May play a role in the interaction between activated B-lymphocytes and dendritic cells in tonsils (By similarity). {ECO:0000250}." null 1885.14 null null 100 uniprot_mouse_length brain_HCD 908.5949707 913.269104 913.264753 14 12765.69535 4.764230626 EIF1B_MOUSE Eukaryotic translation initiation factor 1b; Short=eIF1b Q9CXU9 STIQNLQSFDPFADATKGDDLLPAGTEDYIHIRIQQRNGRKTLTTVQGIADDYDKKKLVKAFKKKFACNGTVIEHPEYGEVIQLQGDQRKNICQFLLEVGIVKEEQLKVHGF 112 FUNCTION: Probably involved in translation. S8P 544.33 "S,47;" 64 100 uniprot_mouse_length brain_HCD 707.4125366 708.516663 708.513378 19 13436.74338 4.635900688 ENSA_MOUSE Alpha-endosulfine;AltName: Full=ARPP-19e P60840 SQKQEEENPAEETGEEKQDTQEKEGILPEKAEEAKLKAKYPSLGQKPGGSDFLMKRLQKGQKYFDSGDYNMAKAKMKNKQLPSAGADKNLVTGDHIPTPQDLPQRKSSLVTSKLAGGQVE 120 "FUNCTION: Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-67 during mitosis, specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, an essential condition to keep cyclin-B1-CDK1 activity high during M phase. Also acts as a stimulator of insulin secretion by interacting with sulfonylurea receptor (ABCC8), thereby preventing sulfonylurea from binding to its receptor and reducing K(ATP) channel currents (By similarity). {ECO:0000250}." S1PS66PS107P 1740.12 "S,17;S,0;S,0;" 102 100 uniprot_mouse_length brain_HCD 547.2439575 546.022766 546.025687 29 15796.72721 -5.34935771 ERG28_MOUSE Probable ergosterol biosynthetic protein 28 Q9ERY9 MSRFLNVLRSWLVMVSIIAMGNTLQSFRDHTFLYEKLYTGKPNLVNGLQARTFGIWTLLSSVIRCLCAIDIHNKTLYHITLWTFLLALGHFLSELFVFGTAAPTVGVLAPLMVASFSILGMLVGLRYLEAEPVSRQKKRN 140 SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. null 6029.35 null null 100 uniprot_mouse_length brain_HCD 642.47229 639.277771 639.26988 19 12121.11793 12.34376332 ERH_MOUSE Enhancer of rudimentary homolog; Short=Mer P84089 SHTILLVQPTKRPEGRTYADYESVNECMEGVCKMYEEHLKRMNPNSPSITYDISQLFDFIDDLADLSCLVYRADTQTYQPYNKDWIKEKIYVLLRRQAQQAGK 103 FUNCTION: May have a role in the cell cycle. null 857.62 null null 100 uniprot_mouse_length brain_HCD 524.0151367 522.346497 522.346002 28 14590.67536 0.946847548 FABP4_MOUSE "Fatty acid-binding protein, adipocyte;AltName: Full=3T3-L1 lipid-binding protein;AltName: Full=Adipocyte lipid-binding protein; Short=ALBP;AltName: Full=Adipocyte-type fatty acid-binding protein; Short=A-FABP; Short=AFABP;AltName: Full=Fatty acid-binding protein 4;AltName: Full=Myelin P2 protein homolog;AltName: Full=P15;AltName: Full=P2 adipocyte protein;AltName: Full=Protein 422" P04117 CDAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDLVTIRSESTFKNTEISFKLGVEFDEITADDRKVKSIITLDGGALVQVQKWDGKSTTIKRKRDGDKLVVECVMKGVTSTRVYERA 131 "FUNCTION: Lipid transport protein in adipocytes. Binds both long chain fatty acids and retinoic acid. Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus. {ECO:0000269|PubMed:12077340, ECO:0000269|PubMed:16574478, ECO:0000269|PubMed:17516629}." Y19P 295.02 "Y,31;" 52 100 uniprot_mouse_length brain_HCD_6 658.4674683 655.244812 655.241996 23 15039.55292 4.297666719 FABP5_MOUSE "Fatty acid-binding protein, epidermal;AltName: Full=Epidermal-type fatty acid-binding protein; Short=E-FABP;AltName: Full=Fatty acid-binding protein 5;AltName: Full=Keratinocyte lipid-binding protein;AltName: Full=Psoriasis-associated fatty acid-binding protein homolog; Short=PA-FABP" Q05816 ASLKDLEGKWRLMESHGFEEYMKELGVGLALRKMAAMAKPDCIITCDGNNITVKTESTVKTTVFSCNLGEKFDETTADGRKTETVCTFQDGALVQHQQWDGKESTITRKLKDGKMIVECVMNNATCTRVYEKVQ 134 FUNCTION: High specificity for fatty acids. Highest affinity for C18 chain length (By similarity). {ECO:0000250}. A1Ac 2097.45 "A,79;" 118 100 uniprot_mouse_length brain_HCD 614.5835571 616.276855 616.283631 24 14759.79301 -10.99417688 FABPH_MOUSE "Fatty acid-binding protein, heart;AltName: Full=Fatty acid-binding protein 3;AltName: Full=Heart-type fatty acid-binding protein; Short=H-FABP;AltName: Full=Mammary-derived growth inhibitor; Short=MDGI" P11404 ADAFVGTWKLVDSKNFDDYMKSLGVGFATRQVASMTKPTTIIEKNGDTITIKTQSTFKNTEINFQLGIEFDEVTADDRKVKSLVTLDGGKLIHVQKWNGQETTLTRELVDGKLILTLTHGSVVSTRTYEKEA 132 FUNCTION: FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. Y19P 1997.56 "Y,111;" 139 100 uniprot_mouse_length brain_HCD 589.015564 591.30957 591.308691 25 14749.70275 1.487061688 FBP12_MOUSE Fatty acid-binding protein 12 Q9DAK4 MVDQLQGTWKSVSCDNFENYMKELGVGRASRKLGCLAKPTVTISTDGDLITIKTKSIFKNKEISFKLGEEFEETTPSGRKSKSTVILDNDSLVQVQDWDGKEATICRRLVDGKMVVESAVNNVTCTRTYQRV 132 FUNCTION: May play a role in lipid transport. {ECO:0000250}. null 3720.75 null null 100 uniprot_mouse_length brain_HCD 628.1668091 623.38446 623.376115 27 16795.13742 13.38750237 FUCM_MOUSE Fucose mutarotase; EC=5.1.3.29 Q8R2K1 MVALKGIPKVLSPELLFALARMGHGDEIVLADANFPTSSICQCGPVEIRADGLDIPQLLEAVLRLLPLDTYVESPAAVMDLVPSDKEKGLQTPIWKRYESLLLEADCKKTLMKLERFEFYERAKKAFAVVATGEMALYGNIILKKGTLDLGPS 153 "FUNCTION: Involved in the interconversion between alpha- and beta- L-fucoses. L-Fucose (6-deoxy-L-galactose) exists as alpha-L-fucose (29.5%) and beta-L-fucose (70.5%), the beta-form is metabolized through the salvage pathway. GDP-L-fucose formed either by the de novo or salvage pathways is transported into the endoplasmic reticulum, where it serves as a substrate for N- and O- glycosylations by fucosyltransferases. Fucosylated structures expressed on cell surfaces or secreted in biological fluids are believed to play a critical role in cell-cell adhesion and recognition processes. {ECO:0000269|PubMed:17602138}." null 1829.65 null null 100 uniprot_mouse_length brain_HCD 604.3099365 607.17157 607.168855 14 8482.35964 4.471283723 FXYD7_MOUSE FXYD domain-containing ion transport regulator 7 P59648 MATPTQSPTNVPEETDPFFYDYATVQTVGMTLATIMFVLGIIIILSKKVKCRKADSRSESPTCKSCKSELPSSAPGGGGV 80 SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. null 879.87 null null 100 uniprot_mouse_length brain_HCD 526.0170898 524.126465 524.125591 13 6797.63043 1.667241144 GBG10_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-10;Flags: Precursor Q9CXP8 SSGASVSALQRLVEQLKLEAGVERIKVSQAAAELQQYCIQNACKDALLLGVPAGSNPFREPRSC 64 "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction. Interacts with beta-1 and beta-2, but not with beta-3 (By similarity). {ECO:0000250}." null 1262.08 null null 100 uniprot_mouse_length brain_HCD 623.7414551 624.339539 624.331209 11 6853.64101 13.34159513 GBG10_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-10;Flags: Precursor Q9CXP8 SSGASVSALQRLVEQLKLEAGVERIKVSQAAAELQQYCIQNACKDALLLGVPAGSNPFREPRSC 64 "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction. Interacts with beta-1 and beta-2, but not with beta-3 (By similarity). {ECO:0000250}." S1AcC64Me 277.31 "S,18;C,18;" 32 100 uniprot_mouse_length brain_HCD 526.977478 527.123413 527.13009 13 6836.68896 -12.66653942 GBG5_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-5;Flags: Precursor Q80SZ7 SGSSSVAAMKKVVQQLRLEAGLNRVKVSQAAADLKQFCLQNAQHDPLLTGVSSSTNPFRPQKVC 64 "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction." null 400.11 null null 100 uniprot_mouse_length brain_HCD 692.213623 689.160828 689.16783 10 6878.67606 -10.16060671 GBG5_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-5;Flags: Precursor Q80SZ7 SGSSSVAAMKKVVQQLRLEAGLNRVKVSQAAADLKQFCLQNAQHDPLLTGVSSSTNPFRPQKVC 64 "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction." S1Ac 243.76 "S,19;" 32 100 uniprot_mouse_length brain_HCD 690.2684326 690.567322 690.569396 10 6892.69171 -3.003641152 GBG5_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-5;Flags: Precursor Q80SZ7 SGSSSVAAMKKVVQQLRLEAGLNRVKVSQAAADLKQFCLQNAQHDPLLTGVSSSTNPFRPQKVC 64 "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction." S1AcC64Me 485.5 "S,22;C,22;" 38 100 uniprot_mouse_length brain_HCD 542.12677 538.778381 538.784232 14 7525.97723 -10.85898955 GBG8_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-8;AltName: Full=Gamma-9;Flags: Precursor P63078 MSNNMAKIAEARKTVEQLKLEVNIDRMKVSQAAAELLAFCETHAKDDPLVTPVPAAENPFRDKRLFC 67 "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction. This subunit may have a very specific role in the development and turnover of olfactory and vomeronasal neurons." C67Me 343.69 "C,29;" 48 100 uniprot_mouse_length brain_HCD 621.5100098 617.189514 617.182189 37 22786.71419 11.86871606 GDIR2_MOUSE Rho GDP-dissociation inhibitor 2; Short=Rho GDI 2;AltName: Full=D4;AltName: Full=Rho-GDI beta Q61599 TEKDAQPQLEEADDDLDSKLNYKPPPQKSLKELQEMDKDDESLTKYKKTLLGDVPVVADPTVPNVTVTRLSLVCDSAPGPITMDLTGDLEALKKDTFVLKEGIEYRVKINFKVNKDIVSGLKYVQHTYRTGMRVDKATFMVGSYGPRPEEYEFLTPVEEAPKGMLARGTYHNKSFFTDDDKQDHLTWEWNLAIKKDWTE 199 "FUNCTION: Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them." Y22P 2955.47 "Y,94;" 224 100 uniprot_mouse_length brain_HCD 787.7772217 788.656494 788.653095 12 9447.8325 4.310058055 GFRP_MOUSE GTP cyclohydrolase 1 feedback regulatory protein; Short=GFRP;AltName: Full=GTP cyclohydrolase I feedback regulatory protein;AltName: Full=p35 P99025 PYLLISTQIRMEVGPTMVGDEHSDPELMQHLGASKRSVLGNNFYEYYVNDPPRIVLDKLECKGFRVLSMTGVGQTLVWCLHKE 83 FUNCTION: Mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase 1. This inhibition is reversed by L-phenylalanine (By similarity). {ECO:0000250}. null 1124.06 null null 100 uniprot_mouse_length brain_HCD 544.7453613 548.47406 548.468116 26 14227.15677 10.83756452 GLCM1_MOUSE Glycosylation-dependent cell adhesion molecule 1; Short=GlyCAM-1;AltName: Full=Endothelial ligand FOR L-selectin;AltName: Full=MC26;AltName: Full=SGP50;AltName: Full=Sulfated 50 kDa glycoprotein;Flags: Precursor Q02596 LPGSKDELQMKTQPTDAIPAAQSTPTSYTSEESTSSKDLSKEPSIFREELISKDNVVIESTKPENQEAQDGLRSGSSQLEETTRPTTSAATTSEENLTKSSQTVEEELGKIIEGFVTGAEDIISGASRITKS 132 FUNCTION: Adhesion molecule that accomplishes cell binding by presenting carbohydrate(s) to the lectin domain of L-selectin. S35P 815.1 "S,1;" 87 100 uniprot_mouse_length brain_HCD 634.3192139 632.95813 632.954891 22 13895.99347 5.117083158 H2A1H_MOUSE Histone H2A type 1-H Q8CGP6 SGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAK 127 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1AcK5Ac 802.78 "S,0;K,4;" 86 100 uniprot_mouse_length brain_HCD 695.1759644 698.741089 698.748168 20 13947.94924 -10.13116476 H2A1H_MOUSE Histone H2A type 1-H Q8CGP6 SGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAK 127 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1AcQ104MeT120P 903.13 "S,0;Q,72;T,0;" 98 100 uniprot_mouse_length brain_HCD 780.6083984 777.062683 777.053521 18 13961.94925 11.79082936 H2A1H_MOUSE Histone H2A type 1-H Q8CGP6 SGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAK 127 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1AcR3dMeT120P 785.6 "S,0;R,57;T,0;" 88 100 uniprot_mouse_length brain_HCD 779.637085 779.167358 779.162174 18 13999.90502 6.653811761 H2A1H_MOUSE Histone H2A type 1-H Q8CGP6 SGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAK 127 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1PR3dMeT120P 160.79 "S,21;R,24;T,0;" 42 100 uniprot_mouse_length brain_HCD 588.9731445 588.583984 588.589805 24 14095.14119 -9.889102649 H2A1K_MOUSE Histone H2A type 1-K Q8CGP7 SGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTETHHKAKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1AcK5Ac 5274.77 "S,2;K,0;" 184 100 uniprot_mouse_length brain_HCD 634.3192139 636.915344 636.906835 22 13982.93662 13.36025587 H2A2B_MOUSE Histone H2A type 2-B;AltName: Full=H2a-613A Q64522 SGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYMAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEELNKLLGGVTIAQGGVLPNIQAVLLPKKTESHKPGKNK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1PR3dMe 894.59 "S,58;R,64;" 99 100 uniprot_mouse_length brain_HCD 779.637085 778.220459 778.225329 18 13983.04184 -6.257847751 H2A3_MOUSE Histone H2A type 3 Q8BFU2 SGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." null 178.04 null null 100 uniprot_mouse_length brain_HCD 614.5835571 611.092041 611.093131 23 14025.12789 -1.783663274 H2A3_MOUSE Histone H2A type 3 Q8BFU2 SGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." R3dMeQ104Me 1645.52 "R,77;Q,108;" 119 100 uniprot_mouse_length brain_HCD 588.9731445 588.583984 588.589805 24 14095.14119 -9.889102649 H2A3_MOUSE Histone H2A type 3 Q8BFU2 SGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1AcR3dMeK5Ac 5644.04 "S,2;R,185;K,7;" 184 100 uniprot_mouse_length brain_HCD 544.1305542 541.743286 541.738205 26 14052.17953 9.379314151 H2AJ_MOUSE Histone H2A.J; Short=H2a/j Q8R1M2 MSGRGKQGGKVRAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESQKVKSK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." Q105Me 1638.24 "Q,122;" 137 100 uniprot_mouse_length brain_HCD 707.4125366 705.360229 705.357067 20 14080.12752 4.48353371 H2AJ_MOUSE Histone H2A.J; Short=H2a/j Q8R1M2 MSGRGKQGGKVRAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESQKVKSK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." K6Ac 1707.61 "K,0;" 105 100 uniprot_mouse_length brain_HCD 747.9404297 746.5979 746.592837 18 13414.65959 6.781997327 H2AZ_MOUSE Histone H2A.Z; Short=H2A/z P0C0S6 AGGKAGKDSGKAKTKAVSRSQRAGLQFPVGRIHRHLKSRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGKKGQQKTV 127 "FUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. May be involved in the formation of constitutive heterochromatin. May be required for chromosome segregation during cell division. Essential for early development. {ECO:0000269|PubMed:11516949, ECO:0000269|PubMed:15195148, ECO:0000269|PubMed:15546624}." null 890.76 null null 100 uniprot_mouse_length brain_HCD 544.1708984 542.876892 542.870302 25 13540.74602 12.13934492 H2AZ_MOUSE Histone H2A.Z; Short=H2A/z P0C0S6 AGGKAGKDSGKAKTKAVSRSQRAGLQFPVGRIHRHLKSRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGKKGQQKTV 127 "FUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. May be involved in the formation of constitutive heterochromatin. May be required for chromosome segregation during cell division. Essential for early development. {ECO:0000269|PubMed:11516949, ECO:0000269|PubMed:15195148, ECO:0000269|PubMed:15546624}." A1AcK4AcK7Ac 2874.37 "A,2;K,0;K,0;" 169 100 uniprot_mouse_length brain_HCD 617.6983643 617.916687 617.911861 23 14181.95937 7.810194339 H2B1A_MOUSE "Histone H2B type 1-A;AltName: Full=Histone H2B, testis;AltName: Full=Testis-specific histone H2B" P70696 PEVAVKGATISKKGFKKAVTKTQKKEGRKRKRCRKESYSIYIYKVLKQVHPDTGISSKAMSIMNSFVTDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 126 "FUNCTION: Variant histone specifically required to direct the transformation of dissociating nucleosomes to protamine in male germ cells. Entirely replaces classical histone H2B prior nucleosome to protamine transition and probably acts as a nucleosome dissociating factor that creates a more dynamic chromatin, facilitating the large-scale exchange of histones. Also expressed maternally and is present in the female pronucleus, suggesting a similar role in protamine replacement by nucleosomes at fertilization. Also found in fat cells, its function and the presence of post-translational modifications specific to such cells are still unclear. Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. {ECO:0000269|PubMed:23884607}." P1AcK47MeK58dMe 1391.04 "P,0;K,28;K,21;" 77 100 uniprot_mouse_length brain_HCD 617.6983643 617.916687 617.913443 23 14181.99576 5.249945207 H2B1A_MOUSE "Histone H2B type 1-A;AltName: Full=Histone H2B, testis;AltName: Full=Testis-specific histone H2B" P70696 PEVAVKGATISKKGFKKAVTKTQKKEGRKRKRCRKESYSIYIYKVLKQVHPDTGISSKAMSIMNSFVTDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 126 "FUNCTION: Variant histone specifically required to direct the transformation of dissociating nucleosomes to protamine in male germ cells. Entirely replaces classical histone H2B prior nucleosome to protamine transition and probably acts as a nucleosome dissociating factor that creates a more dynamic chromatin, facilitating the large-scale exchange of histones. Also expressed maternally and is present in the female pronucleus, suggesting a similar role in protamine replacement by nucleosomes at fertilization. Also found in fat cells, its function and the presence of post-translational modifications specific to such cells are still unclear. Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. {ECO:0000269|PubMed:23884607}." K47MeK58dMeK86tMe 1313.97 "K,30;K,19;K,83;" 68 100 uniprot_mouse_length brain_HCD 683.6676025 679.127625 679.137722 21 14233.87876 -14.86810106 H2B1A_MOUSE "Histone H2B type 1-A;AltName: Full=Histone H2B, testis;AltName: Full=Testis-specific histone H2B" P70696 PEVAVKGATISKKGFKKAVTKTQKKEGRKRKRCRKESYSIYIYKVLKQVHPDTGISSKAMSIMNSFVTDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 126 "FUNCTION: Variant histone specifically required to direct the transformation of dissociating nucleosomes to protamine in male germ cells. Entirely replaces classical histone H2B prior nucleosome to protamine transition and probably acts as a nucleosome dissociating factor that creates a more dynamic chromatin, facilitating the large-scale exchange of histones. Also expressed maternally and is present in the female pronucleus, suggesting a similar role in protamine replacement by nucleosomes at fertilization. Also found in fat cells, its function and the presence of post-translational modifications specific to such cells are still unclear. Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. {ECO:0000269|PubMed:23884607}." P1AcS37PK47Me 5993.92 "P,1;S,144;K,61;" 184 100 uniprot_mouse_length brain_HCD 604.9911499 607.210693 607.205938 23 13935.72291 7.831542937 H2B1B_MOUSE Histone H2B type 1-B;AltName: Full=h2B-143 Q64475 PEPSKSAPAPKKGSKKAISKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S14PK46MeK57dMe 967.05 "S,5;K,19;K,13;" 83 100 uniprot_mouse_length brain_HCD 998.8571777 997.191101 997.191759 14 13939.67094 -0.659778599 H2B1B_MOUSE Histone H2B type 1-B;AltName: Full=h2B-143 Q64475 PEPSKSAPAPKKGSKKAISKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." P1AcK5AcK11Ac 278.31 "P,0;K,0;K,0;" 33 100 uniprot_mouse_length brain_HCD 998.8571777 997.191101 997.194359 14 13939.70732 -3.267092069 H2B1B_MOUSE Histone H2B type 1-B;AltName: Full=h2B-143 Q64475 PEPSKSAPAPKKGSKKAISKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." P1AcK5AcK85tMe 353.98 "P,0;K,0;K,40;" 40 100 uniprot_mouse_length brain_HCD 702.5175171 699.838867 699.833698 20 13969.6603 7.386308368 H2B1C_MOUSE Histone H2B type 1-C/E/G Q6ZWY9 PEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S14PS36PK85tMe 1534.98 "S,4;S,0;K,117;" 116 100 uniprot_mouse_length brain_HCD 702.5175171 699.838867 699.833698 20 13969.6603 7.386308368 H2B1H_MOUSE Histone H2B type 1-H;AltName: Full=h2B-221 Q64478 PEPAKSAPAPKKGSKKALTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S14PS36PK57dMe 1385.84 "S,5;S,0;K,15;" 107 100 uniprot_mouse_length brain_HCD 702.5175171 699.838867 699.833698 20 13969.6603 7.386308368 H2B1K_MOUSE Histone H2B type 1-K Q8CGP1 PEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S14PS36PK57dMe 1585.04 "S,4;S,0;K,21;" 122 100 uniprot_mouse_length brain_HCD 998.2001343 997.0672 997.055583 14 13937.76444 11.65101247 H2B1P_MOUSE Histone H2B type 1-P Q8CGP2 PEPVKSVPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." P1AcK46MeK57dMe 744.93 "P,0;K,17;K,10;" 68 100 uniprot_mouse_length brain_HCD 544.1305542 539.338989 539.340131 26 13989.82971 -2.116924223 H2B1P_MOUSE Histone H2B type 1-P Q8CGP2 PEPVKSVPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S14PK46MeK85tMe 1638.74 "S,15;K,38;K,114;" 131 100 uniprot_mouse_length brain_HCD 998.8571777 997.191101 997.192558 14 13939.68218 -1.461027531 H2B3A_MOUSE Histone H2B type 3-A Q9D2U9 PEPSRSTPAPKKGSKKAITKAQKKDGKKRKRGRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREVQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." P1AcK11Ac 330.45 "P,0;K,0;" 21 100 uniprot_mouse_length brain_HCD 998.8571777 997.191101 997.195158 14 13939.71856 -4.068336823 H2B3A_MOUSE Histone H2B type 3-A Q9D2U9 PEPSRSTPAPKKGSKKAITKAQKKDGKKRKRGRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREVQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." P1AcK46MeK57dMe 261.19 "P,0;K,10;K,7;" 15 100 uniprot_mouse_length brain_HCD 854.546936 850.797424 850.787846 22 18685.31194 11.25817259 MUP6_MOUSE "Major urinary protein 6; Short=MUP 6;AltName: Full=Alpha-2U-globulin;AltName: Full=Group 1, BS6;AltName: Allergen=Mus m 1;Flags: Precursor" P02762 EEASSTGRNFNVEKINGEWHTIILASDKREKIEDNGNFRLFLEQIHVLENSLVLKFHTVRDEECSELSMVADKTEKAGEYSVTYDGFNTFTIPKTDYDNFLMAHLINEKDGETFQLMGLYGREPDLSSDIKERFAQLCEEHGILRENIIDLSNANRCLQARE 162 FUNCTION: Binds pheromones that are released from drying urine of males. These pheromones affect the sexual behavior of females. null 1030.1 null null 100 uniprot_mouse_length brain_HCD 726.1279907 722.594238 722.597842 26 18751.52399 -4.987170651 PPIF_MOUSE "Peptidyl-prolyl cis-trans isomerase F, mitochondrial; Short=PPIase F; EC=5.2.1.8;AltName: Full=Cyclophilin D; Short=CyP-D; Short=CypD;AltName: Full=Cyclophilin F;AltName: Full=Rotamase F;Flags: Precursor" Q99KR7 CSDGGARGANSSSGNPLVYLDVGADGQPLGRVVLELKADVVPKTAENFRALCTGEKGFGYKGSTFHRVIPAFMCQAGDFTNHNGTGGRSIYGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSKSGKTSKKIVITDCGQLS 177 "FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in activating oxidative stress- induced necrosis. Involved in modulation of mitochondrial membrane F(1)F(0) ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels. Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis. {ECO:0000269|PubMed:15800626, ECO:0000269|PubMed:15800627, ECO:0000269|PubMed:16103352, ECO:0000269|PubMed:18684715, ECO:0000269|PubMed:19801635, ECO:0000269|PubMed:21281446, ECO:0000269|PubMed:22726440}." K37Ac 7015.4 "K,125;" 242 100 uniprot_mouse_length brain_HCD 622.7885742 620.747192 620.753433 20 12389.05874 -10.05329468 4EBP1_MOUSE Eukaryotic translation initiation factor 4E-binding protein 1; Short=4E-BP1; Short=eIF4E-binding protein 1;AltName: Full=Phosphorylated heat- and acid-stable protein regulated by insulin 1; Short=PHAS-I Q60876 SAGSSCSQTPSRAIPTRRVALGDGVQLPPGDYSTTPGGTLFSTTPGGTRIIYDRKFLMECRNSPVAKTPPKDLPAIPGVTSPTSDEPPMQASQSQLPSSPEDKRAGGEESQFEMDI 116 "FUNCTION: Repressor of translation initiation that regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. In contrast, hyperphosphorylated form dissociates from EIF4E, allowing interaction between EIF4G1/EIF4G3 and EIF4E, leading to initiation of translation (By similarity). Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways (PubMed:7629182). {ECO:0000250|UniProtKB:Q13541, ECO:0000269|PubMed:7629182}." S1AcT35PT39P 480.61 "S,38;T,1;T,0;" 67 100 uniprot_mouse_length brain_HCD 649.0530396 650.656555 650.656 27 17530.69515 0.853255455 A14EL_MOUSE ARL14 effector protein-like Q3UKZ7 MTEPSQKNNSTQQELTNHLFPEKSSQIGQKQLQQIERQLKCLAFQNPGPQVADFNPETRQQKKKARMSKMNEYFSVKYKVMKKYDKSGRLICNDVDLCDCLEKNCLGCFYPCPKCNSNKCGPECRCNRRWVYDAIVTESGEVINTLPFSVPD 152 "-------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License--------------------------------------------------" null 3142.87 null null 100 uniprot_mouse_length brain_HCD 697.6692505 698.045837 698.047884 19 13236.89718 -2.9318872 AAMDC_MOUSE Mth938 domain-containing protein;AltName: Full=LI2 Q8R0P4 MASPKIASLSWGQMKVQGSTLTYKDCKVWPGGSRAWDWRETGTEHSPGVQPADVKEVAEKGVQTLVIGRGMSEALKVPPSTVEYLEKQGIDVRVLQTEQAVKEYNALVAQGVRVGGVFHSTC 122 FUNCTION: May play a role in preadipocyte differentiation and adipogenesis. {ECO:0000269|PubMed:22279136}. null 2416.75 null null 100 uniprot_mouse_length brain_HCD 646.1055908 649.002319 648.996024 14 9067.93873 9.7001148 ABRAL_MOUSE Costars family protein ABRACL;AltName: Full=ABRA C-terminal-like protein Q4KML4 MNVEHEVNLLVEEIHRLGSKNADGKLSVKFGVLFQDDRCANLFEALVGTLKAAKRRKIVTYAGELLLQGVHDDVDIVLLQD 81 SIMILARITY: Belongs to the costars family. {ECO:0000305}. M1Ac 661.7 "M,40;" 60 100 uniprot_mouse_length brain_HCD 629.6715088 631.947632 631.947134 16 10090.14649 0.787780988 ACPM_MOUSE "Acyl carrier protein, mitochondrial; Short=ACP;AltName: Full=CI-SDAP;AltName: Full=NADH-ubiquinone oxidoreductase 9.6 kDa subunit;Flags: Precursor" Q9CR21 SDAPPLTLDGIKDRVLYVLKLYDKIDPEKLSVNSHFMKDLGLDSLDQVEIIMAMEDEFGFEIPDIDAEKLMCPQEIVDYIADKKDVYE 88 "FUNCTION: Carrier of the growing fatty acid chain in fatty acid biosynthesis in mitochondria. Accessory and non-catalytic subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which functions in the transfer of electrons from NADH to the respiratory chain (By similarity). {ECO:0000250}." null 271.14 null null 100 uniprot_mouse_length brain_HCD 921.8252563 922.55957 922.556875 11 10132.11795 2.921567844 ACPM_MOUSE "Acyl carrier protein, mitochondrial; Short=ACP;AltName: Full=CI-SDAP;AltName: Full=NADH-ubiquinone oxidoreductase 9.6 kDa subunit;Flags: Precursor" Q9CR21 SDAPPLTLDGIKDRVLYVLKLYDKIDPEKLSVNSHFMKDLGLDSLDQVEIIMAMEDEFGFEIPDIDAEKLMCPQEIVDYIADKKDVYE 88 "FUNCTION: Carrier of the growing fatty acid chain in fatty acid biosynthesis in mitochondria. Accessory and non-catalytic subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which functions in the transfer of electrons from NADH to the respiratory chain (By similarity). {ECO:0000250}." K20Ac 565.65 "K,39;" 48 100 uniprot_mouse_length brain_HCD 739.8943481 740.772522 740.772796 23 17005.75733 -0.369920906 AGR3_MOUSE Anterior gradient protein 3 homolog;Flags: Precursor Q8R3W7 IAIKKEKRPPQTLSRGWGDDITWVQTYEEGLFHARKSNKPLMVIHHLEDCQYCQALKKEFAKNEEIQEMAQNDFIMLNLMHETTDKNLSPDGQYVPRIMFVDPSLTVRADITGRYSNRLYTYEPQDLPMLVDNMKKALRLIQSEL 145 SUBUNIT: Interacts with LYPD3 and DAG1 (alphaDAG1). {ECO:0000250}. null 1831.07 null null 100 uniprot_mouse_length brain_HCD 685.5714722 688.785767 688.779686 20 13748.58138 8.828079117 ANFB_MOUSE Natriuretic peptides B;AltName: Full=Gamma-brain natriuretic peptide;Contains: Brain natriuretic peptide; Short=BNP;Flags: Precursor P40753 MDLLKVLSQMILFLLFLYLSPLGGHSYPLGSPSQSPEQFKMQKLLELIREKSEEMAQRQLLKDQGLTKEHPKRVLRSQGSTLRVQQRPQNSKVTHISSCFGHKIDRIGSVSRLGCNALKLL 121 "FUNCTION: Cardiac hormone which may function as a paracrine antifibrotic factor in the heart. Also plays a key role in cardiovascular homeostasis through natriuresis, diuresis, vasorelaxation, and inhibition of renin and aldosterone secretion. Specifically binds and stimulates the cGMP production of the NPR1 receptor. Binds the clearance receptor NPR3." null 1189.36 null null 100 uniprot_mouse_length brain_HCD 577.2947388 576.361511 576.361683 30 17251.83441 -0.298023856 ANR37_MOUSE Ankyrin repeat domain-containing protein 37 Q569N2 MLLLSCNLEEDDLKSLLETGASVNAPPDPQEQSPAHLAAGGGLACFLLWQLQTGADLNQQDVLGETPLHKAAKVGSLDCLSLLVASDVQIGVCNKNGQTAEDLAWSYGFPECARFLTMIKCMQTARSSGEQQERDPRAPVLRQKRSFRTVESGVMKRKC 159 SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. null 1360.73 null null 100 uniprot_mouse_length brain_HCD 547.239502 546.361633 546.364749 18 9811.56161 -5.70259927 APC11_MOUSE Anaphase-promoting complex subunit 11; Short=APC11;AltName: Full=Cyclosome subunit 11 Q9CPX9 MKVKIKCWNGVATWLWVANDENCGICRMAFNGCCPDCKVPGDDCPLVWGQCSHCFHMHCILKWLNAQQVQQHCPMCRQEWKFKE 84 "FUNCTION: Together with the cullin protein ANAPC2, constitutes the catalytic component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. May recruit the E2 ubiquitin-conjugating enzymes to the complex (By similarity). {ECO:0000250|UniProtKB:Q9NYG5}." null 953.34 null null 100 uniprot_mouse_length brain_HCD 640.3217773 639.339844 639.340998 34 21691.56921 -1.805374602 ARL14_MOUSE ADP-ribosylation factor-like protein 14;AltName: Full=ADP-ribosylation factor 7 Q3SXC5 GLLNSKNPQSKQAHILLLGLDSAGKSTLLYRLKFAETLATIPTIGFNVEMVQLQSSLTLTVWDVGGQEKMRTVWDCYCENAQGLMYVVDCSEGKKRLEDSRKEFKHILKNEHIKNTPVVILANKQDLPGALSAEDITRMFKVKKLCSNRNWYVQPCCAVTGEGLDDGFRKLTEFLKSYRRTRETLAIFKQK 191 FUNCTION: GTPase that recruits MYO1E to MHC class II-containing vesicles via the effector protein ARL14EP and hence controls the movement of these vesicles along the actin cytoskeleton in dendritic cells. {ECO:0000250}. null 2291.43 null null 100 uniprot_mouse_length brain_HCD 873.6409302 869.662415 869.670066 14 12155.37032 -8.798105762 ARP19_MOUSE cAMP-regulated phosphoprotein 19; Short=ARPP-19 P56212 SAEVPEAASAEEQKEMEDKVTSPEKAEEAKLKARYPHLGQKPGGSDFLRKRLQKGQKYFDSGDYNMAKAKMKNKQLPAAAPDKTEVTGDHIPTPQDLPQRKPSLVASKLAG 111 "FUNCTION: Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-62 during mitosis, specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, an essential condition to keep cyclin-B1-CDK1 activity high during M phase. May indirectly enhance GAP-43 expression by binding to the NGF-regulatory region of its mRNA (By similarity). {ECO:0000250}." null 1265.09 null null 100 uniprot_mouse_length brain_HCD 682.949707 681.069336 681.076585 18 12235.36793 -10.64353504 ARP19_MOUSE cAMP-regulated phosphoprotein 19; Short=ARPP-19 P56212 SAEVPEAASAEEQKEMEDKVTSPEKAEEAKLKARYPHLGQKPGGSDFLRKRLQKGQKYFDSGDYNMAKAKMKNKQLPAAAPDKTEVTGDHIPTPQDLPQRKPSLVASKLAG 111 "FUNCTION: Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-62 during mitosis, specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, an essential condition to keep cyclin-B1-CDK1 activity high during M phase. May indirectly enhance GAP-43 expression by binding to the NGF-regulatory region of its mRNA (By similarity). {ECO:0000250}." S61P 1894.47 "S,45;" 103 100 uniprot_mouse_length brain_HCD 587.9829712 587.726929 587.731825 21 12315.35771 -8.330821736 ARP19_MOUSE cAMP-regulated phosphoprotein 19; Short=ARPP-19 P56212 SAEVPEAASAEEQKEMEDKVTSPEKAEEAKLKARYPHLGQKPGGSDFLRKRLQKGQKYFDSGDYNMAKAKMKNKQLPAAAPDKTEVTGDHIPTPQDLPQRKPSLVASKLAG 111 "FUNCTION: Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-62 during mitosis, specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, an essential condition to keep cyclin-B1-CDK1 activity high during M phase. May indirectly enhance GAP-43 expression by binding to the NGF-regulatory region of its mRNA (By similarity). {ECO:0000250}." S61PS103P 292.56 "S,18;S,5;" 47 100 uniprot_mouse_length brain_HCD 773.6815186 772.829285 772.818274 22 16970.98361 14.24742186 ARP5L_MOUSE Actin-related protein 2/3 complex subunit 5-like protein;AltName: Full=Arp2/3 complex 16 kDa subunit 2; Short=ARC16-2 Q9D898 MARNTLSSRFRRVDIDEFDENKFVDEHEEAAAAAGEPGPDPCEVDGLLRQGDMLRAFHAALRNSPINTKNQAVKERAQGVVLKVLTNFKSSEIEQAVQSLDRNGIDLLMKYIYKGFEKPTENSSAVLLQWHEKALAVGGLGSIIRVLTARKTV 153 FUNCTION: May function as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. {ECO:0000250}. null 602.86 null null 100 uniprot_mouse_length brain_HCD 637.3640137 638.223755 638.220902 19 12101.18883 4.470055436 ARTN_MOUSE Artemin;Flags: Precursor Q9Z0L2 AGTRSSRARTTDARGCRLRSQLVPVSALGLGHSSDELIRFRFCSGSCRRARSQHDLSLASLLGAGALRSPPGSRPISQPCCRPTRYEAVSFMDVNSTWRTVDHLSATACGCLG 113 "FUNCTION: Ligand for the GFR-alpha-3-RET receptor complex but can also activate the GFR-alpha-1-RET receptor complex. Supports the survival of sensory and sympathetic peripheral neurons in culture and also supports the survival of dopaminergic neurons of the ventral mid-brain (By similarity). Strong attractant of gut hematopoietic cells thus promoting the formation Peyer's patch- like structures, a major component of the gut-associated lymphoid tissue. {ECO:0000250, ECO:0000269|PubMed:17322904}." null 566.94 null null 100 uniprot_mouse_length brain_HCD 633.7541504 638.261108 638.259612 26 16559.73341 2.344498084 ATOH7_MOUSE Protein atonal homolog 7;AltName: Full=Helix-loop-helix protein mATH-5; Short=mATH5 Q9Z2E5 MKSACKPHGPPAGARGAPPCAGAAERAVSCAGPGRLESAARRRLAANARERRRMQGLNTAFDRLRRVVPQWGQDKKLSKYETLQMALSYIIALTRILAEAERDWVGLRCEQRGRDHPYLPFPGARLQVDPEPYGQRLFGFQPEPFPMAS 149 "FUNCTION: Transcription factor involved in the differentiation of most retinal ganglion cells, including those constituting the retino-hypothalamic tract. {ECO:0000269|PubMed:11156601, ECO:0000269|PubMed:11493566, ECO:0000269|PubMed:12451142, ECO:0000269|PubMed:9806930}." null 2725.61 null null 100 uniprot_mouse_length brain_HCD 645.9365845 644.363159 644.356431 9 5788.20747 10.44170488 ATP5E_MOUSE "ATP synthase subunit epsilon, mitochondrial; Short=ATPase subunit epsilon" P56382 VAYWRQAGLSYIRFSQICAKAVRDALKTEFKANAEKTSGSSIKIVKVSKKE 51 "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits (By similarity). {ECO:0000250}." K20AcK31Ac 129.18 "K,5;K,0;" 24 100 uniprot_mouse_length brain_HCD 602.7141724 604.28009 604.285339 31 18691.82362 -8.68574435 ATP5H_MOUSE "ATP synthase subunit d, mitochondrial; Short=ATPase subunit d" Q9DCX2 AGRKLALKTIDWVSFVEVMPQNQKAIGNALKSWNETFHARLASLSEKPPAIDWAYYRANVAKPGLVDDFEKKYNALKIPVPEDKYTALVDQEEKEDVKSCAEFVSGSQLRIQEYEKQLEKMRNIIPFDQMTIDDLNEIFPETKLDKKKYPYWPHQPIENL 160 "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements." A1AcK84Ac 3618.78 "A,46;K,0;" 200 100 uniprot_mouse_length brain_HCD 699.5198364 698.748047 698.744026 13 9066.66654 5.754432024 ATP5J_MOUSE "ATP synthase-coupling factor 6, mitochondrial; Short=ATPase subunit F6;Flags: Precursor" P97450 NKELDPVQKLFVDKIREYKSKRQASGGPVDIGPEYQQDLDRELYKLKQMYGKGEMDTFPTFKFDDPKFEVIDKPQS 76 "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. Also involved in the restoration of oligomycin-sensitive ATPase activity to depleted F1-F0 complexes." K9AcK14AcK47Ac 737.39 "K,1;K,0;K,0;" 49 100 uniprot_mouse_length brain_HCD 543.2492676 538.72522 538.729172 21 11287.30383 -7.33629 ATP5L_MOUSE "ATP synthase subunit g, mitochondrial; Short=ATPase subunit g" Q9CPQ8 AKFIRNFAEKAPSMVAAAVTYSKPRLATFWHYAKVELVPPTPAEIPTAIQSVKKIIQSAKTGSFKHLTVKEAVLNGLVATEVWMWFYIGEIIGKRGIVGYDV 102 "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane." null 869.56 null null 100 uniprot_mouse_length brain_HCD 734.6984253 730.465271 730.465068 14 10207.50357 0.277899797 ATPK_MOUSE "ATP synthase subunit f, mitochondrial" P56135 ASLVPLKEKKLMEVKLGELPSWIMMRDFTPSGIAGAFRRGYDRYYNKYINVRKGSISGISMVLAAYVVFSYCISYKELKHERRRKYH 87 "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane." null 776.87 null null 100 uniprot_mouse_length brain_HCD 547.2453003 543.441589 543.440229 41 22228.02405 2.503229235 BAD_MOUSE Bcl2-associated agonist of cell death; Short=BAD;AltName: Full=Bcl-2-binding component 6;AltName: Full=Bcl-xL/Bcl-2-associated death promoter;AltName: Full=Bcl2 antagonist of cell death Q61337 MGTPKQPSLAPAHALGLRKSDPGIRSLGSDAGGRRWRPAAQSMFQIPEFEPSEQEDASATDRGLGPSLTEDQPGPYLAPGLLGSNIHQQGRAATNSHHGGAGAMETRSRHSSYPAGTEEDEGMEEELSPFRGRSRSAPPNLWAAQRYGRELRRMSDEFEGSFKGLPRPKSAGTATQMRQSAGWTRIIQSWWDRNLGKGGSTPSQ 204 "FUNCTION: Promotes cell death. Successfully competes for the binding to Bcl-X(L), Bcl-2 and Bcl-W, thereby affecting the level of heterodimerization of these proteins with BAX. Can reverse the death repressor activity of Bcl-X(L), but not that of Bcl-2. Appears to act as a link between growth factor receptor signaling and the apoptotic pathways." S112PS128P 2316.67 "S,22;S,0;" 230 100 uniprot_mouse_length brain_HCD 998.0165405 998.119751 998.107678 10 9966.0696 12.09586584 BAF_MOUSE "Barrier-to-autointegration factor;AltName: Full=Breakpoint cluster region protein 1;AltName: Full=LAP2-binding protein 1;Contains: Barrier-to-autointegration factor, N-terminally processed" O54962 TTSQKHRDFVAEPMGEKPVGSLAGIGDVLSKRLEERGFDKAYVVLGQFLVLKKDEDLFREWLKDTCGANAKQSRDCFGCLREWCDAFL 88 "FUNCTION: Plays fundamental roles in nuclear assembly, chromatin organization, gene expression and gonad development. May potently compress chromatin structure and be involved in membrane recruitment and chromatin decondensation during nuclear assembly. Contains 2 non-specific dsDNA-binding sites which may promote DNA cross-bridging (By similarity). {ECO:0000250}." null 391.35 null null 100 uniprot_mouse_length brain_HCD 682.7322998 679.203064 679.203942 15 10168.05192 -1.292741549 BAF_MOUSE "Barrier-to-autointegration factor;AltName: Full=Breakpoint cluster region protein 1;AltName: Full=LAP2-binding protein 1;Contains: Barrier-to-autointegration factor, N-terminally processed" O54962 TTSQKHRDFVAEPMGEKPVGSLAGIGDVLSKRLEERGFDKAYVVLGQFLVLKKDEDLFREWLKDTCGANAKQSRDCFGCLREWCDAFL 88 "FUNCTION: Plays fundamental roles in nuclear assembly, chromatin organization, gene expression and gonad development. May potently compress chromatin structure and be involved in membrane recruitment and chromatin decondensation during nuclear assembly. Contains 2 non-specific dsDNA-binding sites which may promote DNA cross-bridging (By similarity). {ECO:0000250}." T1AcT2PS3P 297.48 "T,21;T,0;S,0;" 36 100 uniprot_mouse_length brain_HCD 620.0751953 621.54126 621.536474 29 17986.53919 7.699895059 BAP18_MOUSE Chromatin complexes subunit BAP18;AltName: Full=BPTF-associated protein of 18 kDa Q9DCT6 MTSASTKVGEIFSAAGAAFTKLGELTMQLHPVSDSSPAGAKWTETEIEMLRAAVKRFGDDLNHISCVIKERTVAQIKTTVKRKVYEDSGIPLPAESPKKGPKKMTSGVLSPPNAPPPSSSSVPEAGVPPIKKQKADVTLSALNDSDANSDLVDVEGLGETPPAKKLNFDQA 171 FUNCTION: Component of chromatin complexes such as the MLL1/MLL and NURF complexes. {ECO:0000250}. null 2364.64 null null 100 uniprot_mouse_length brain_HCD 545.1296387 541.445251 541.43981 25 13503.98425 10.04999031 BDNF_MOUSE Brain-derived neurotrophic factor; Short=BDNF;Flags: Precursor P21237 HSDPARRGELSVCDSISEWVTAADKKTAVDMSGGTVTVLEKVPVSKGQLKQYFYETKCNPMGYTKEGCRGIDKRHWNSQCRTTQSYVRALTMDSKKRIGWRFIRIDTSCVCTLTIKRGR 119 "FUNCTION: During development, promotes the survival and differentiation of selected neuronal populations of the peripheral and central nervous systems. Participates in axonal growth, pathfinding and in the modulation of dendritic growth and morphology. Major regulator of synaptic transmission and plasticity at adult synapses in many regions of the CNS." null 1618.96 null null 100 uniprot_mouse_length brain_HCD 542.6288452 541.321289 541.328346 23 12421.54241 -13.0363347 BET1L_MOUSE BET1-like protein;AltName: Full=Golgi SNARE with a size of 15 kDa; Short=GOS-15; Short=GS15;AltName: Full=Vesicle transport protein GOS15 O35153 MADWTRAQSSGAVEDILDRENKRMADSLASKVTRLKSLALDIDRDTEDQNRYLDGMDSDFTSVTGLLTGSVKRFSTMARSGRDNRKLLCGMAVVLIVAFFILSYLLSRTRT 111 FUNCTION: Vesicle SNARE required for targeting and fusion of retrograde transport vesicles with the Golgi complex. Required for the integrity of the Golgi complex (By similarity). {ECO:0000250|UniProtKB:O35152}. null 691.31 null null 100 uniprot_mouse_length brain_HCD 544.1309814 539.889648 539.88598 38 20466.64411 6.794837495 BL1S3_MOUSE Biogenesis of lysosome-related organelles complex 1 subunit 3; Short=BLOC-1 subunit 3;AltName: Full=Reduced pigmentation protein Q5U5M8 MESSQGRRRRPGTVVPGEAAETDSELSASSSEEELYLGPSGPTRGRPTGLRVAGEAAETDSEPEPEPTVVPVDLPPLVVQRDPAETWGTEETPAMAPARSLLQLRLAESQTRLDHDVAAAVSGVYRRAGRDVAALAGRLAAAQATGLAAAHSVRLARGDLCALAERLDIVAGCRLLPDIRGVPGMEPEQDPGPRA 195 "FUNCTION: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking. {ECO:0000269|PubMed:16760431, ECO:0000269|PubMed:19546860, ECO:0000269|PubMed:21998198}." T59P 2545.98 "T,3;" 209 100 uniprot_mouse_length brain_HCD 579.3068237 581.884155 581.884252 17 9870.02598 -0.166229902 BLCAP_MOUSE Bladder cancer-associated protein;AltName: Full=Bladder cancer 10 kDa protein; Short=Bc10 P62951 MYCLQWLLPVLLIPKPLNPALWFSHSMFMGFYLLSFLLERKPCTICALVFLAALFLICYSCWGNCFLYHCSDSPLPESAHDPGVVGT 87 FUNCTION: May regulate cell proliferation and coordinate apoptosis and cell cycle progression via a novel mechanism independent of both p53/TP53 and NF-kappa-B. {ECO:0000250}. null 372.11 null null 100 uniprot_mouse_length brain_HCD 614.1868286 613.092773 613.085064 30 18353.53335 12.57482518 BOD1_MOUSE Biorientation of chromosomes in cell division protein 1;AltName: Full=Biorientation defective protein 1;AltName: Full=Protein FAM44B Q5SQY2 MADGAGAGAAGQASGPSGGSSGAGGPVNPASLPPGDPQLIALIVEQLKSRGLFDSFRRDCLADVDTKPAYQNLRQKVDNFVSTHLDKQEWNPAMNKNQLRNGLRQSVVQSGMLEAGVDRIISQVVDPKLNHIFRPQIERAIHEFLAAQKKEAVPAPPPEPESQDPPAPSQDAS 173 FUNCTION: Required for proper chromosome biorientation through the detection or correction of syntelic attachments in mitotic spindles. {ECO:0000250}. null 1749.07 null null 100 uniprot_mouse_length brain_HCD 600.9500122 604.314026 604.317794 17 10251.39477 -6.23533037 BOLA2_MOUSE BolA-like protein 2 Q8BGS2 MELSADYLREKLRQDLEAEHVEVEDTTLNRCATSFRVLVVSAKFEGKPLLQRHRLVNECLAEELPHIHAFEQKTLTPEQWTRQRRE 86 ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q8BGS2-1; Sequence=Displayed; Note=No experimental confirmation available.; Name=2; IsoId=Q8BGS2-2; Sequence=VSP_010094; Note=No experimental confirmation available.; M1Ac 1192.25 "M,69;" 86 100 uniprot_mouse_length brain_HCD 627.0343628 624.425293 624.431966 37 23054.95587 -10.68656253 BORG1_MOUSE Cdc42 effector protein 2;AltName: Full=Binder of Rho GTPases 1 Q8JZX9 STKVPIYLKRGSRKGKKEKLRDLLSSDMISPPLGDFRHTIHIGSGGGDDMFGDISFLQGKFHLLPGTAVEEAEEDGSFDLPFQFTRTTTVCGRELPDGLSPLLKNAISLPVIGGPQALTLPTAQAPPKPPRLHLESPQPSPQPSPQGAGNVDVWRIPEAGSPHNGMSPEPEAEEPFLSHASSLLSLHVDLGPSILDDVLQIMDHDLGRVQIPT 213 FUNCTION: Probably involved in the organization of the actin cytoskeleton. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation in fibroblasts in a CDC42-dependent manner (By similarity). {ECO:0000250}. S1AcS30PS140P 3928.4 "S,241;S,114;S,138;" 267 100 uniprot_mouse_length brain_HCD 547.2453003 546.131226 546.131513 49 26697.41111 -0.526272621 BPIA1_MOUSE BPI fold-containing family A member 1;AltName: Full=Palate lung and nasal epithelium clone protein;Flags: Precursor P97361 QLAGLPLPLGQGPPLPLNQGPPLPLNQGQLLPLAQGLPLAVSPALPSNPTDLLAGKFTDALSGGLLSGGLLGILENIPLLDVIKSGGGNSNGLVGGLLGKLTSSVPLLNNILDIKITDPQLLELGLVQSPDGHRLYVTIPLGLTLNVNMPVVGSLLQLAVKLNITAEVLAVKDNQGRIHLVLGDCTHSPGSLKISLLNGVTPVQSFLDNLTGILTKVLPELIQGKVCPLVNGILSGLDVTLVHNIAELLIHGLQFVIKV 259 "FUNCTION: Plays a role in the innate immune responses of the upper airways. Reduces the surface tension in secretions from airway epithelia and inhibits the formation of biofilm by pathogenic Gram-negative bacteria, such as P.aeruginosa and K.pneumoniae. Binds bacterial lipopolysaccharide (LPS). Negatively regulates proteolytic cleavage of SCNN1G, an event that is required for activation of the epithelial sodium channel (ENaC), and thereby contributes to airway surface liquid homeostasis and proper clearance of mucus (By similarity). Plays a role in the airway inflammatory response after exposure to irritants. May attract macrophages and neutrophils. May be associated with tumor progression. {ECO:0000250, ECO:0000269|PubMed:23499554}." null 2986.12 null null 100 uniprot_mouse_length brain_HCD 790.402832 786.006653 786.010007 22 17261.20132 -4.267334943 BT3L4_MOUSE Transcription factor BTF3 homolog 4;AltName: Full=Basic transcription factor 3-like 4 Q9CQH7 MNQEKLAKLQAQVRIGGKGTARRKKKVVHRTATADDKKLQSSLKKLAVNNIAGIEEVNMIKDDGTVIHFNNPKVQASLSANTFAITGHAEAKPITEMLPGILSQLGADSLTSLRKLAEQFPRQVLDSKAPKPEDIDEEDDDVPDLVENFDEASKNEAN 158 SIMILARITY: Belongs to the NAC-beta family. {ECO:0000305}. null 2319.03 null null 100 uniprot_mouse_length brain_HCD 526.9035034 523.424438 523.419146 34 17752.23207 10.11135455 BTG2_MOUSE Protein BTG2;AltName: Full=BTG family member 2;AltName: Full=NGF-inducible protein TIS21 Q04211 MSHGKRTDMLPEIAAAVGFLSSLLRTRGCVSEQRLKVFSRALQDALTDHYKHHWFPEKPSKGSGYRCIRINHKMDPIISKVASQIGLSQPQLHRLLPSELTLWVDPYEVSYRIGEDGSICVLYEEAPVAASYGLLTCKNQMMLGRSSPSKNYVMAVSS 158 FUNCTION: Anti-proliferative protein; the function is mediated by association with deadenylase subunits of the CCR4-NOT complex. Activates mRNA deadenylation in a CNOT6 and CNOT7-dependent manner. In vitro can inhibit deadenylase activity of CNOT7 and CNOT8. Involved in cell cycle regulation. Could be involved in the growth arrest and differentiation of the neuronal precursors. Modulates transcription regulation mediated by ESR1. Involved in mitochondrial depolarization and neurite outgrowth (By similarity). {ECO:0000250}. S147P 826.81 "S,0;" 100 100 uniprot_mouse_length brain_HCD 614.5784302 616.102783 616.106794 25 15369.65552 -6.509905286 C16L2_MOUSE CD164 sialomucin-like 2 protein;Flags: Precursor Q9D6W7 GKGARGFGRGALLRLNVWPTTQGGCKHLGHCEHCVDRAHNFSICVWQQCGPEEPGHCVAQAEVVKEGCSIYNHSESCPASHHHSTEEPKPSTTGSPPIPEDHSPGFDGASFIGGIVLVLSLQATAFFVLRFLKAKDSTYQTLI 143 SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. null 3556.87 null null 100 uniprot_mouse_length brain_HCD 665.3878784 661.427795 661.433115 20 13201.65044 -8.042521191 C2AIL_MOUSE CDKN2AIP N-terminal-like protein;AltName: Full=CDKN2A-interacting protein N-terminal-like protein Q9D211 MVGGEASAAVEKLVSGVRQAADFAEQFRSYSESEKQWKARMEFILRHLPDYRDPPDGGGRLDQLLSLSMVWANHLFLGCSYNKDLLDKVMEMADGIEVEDLPQFTTRSELMRKHQS 116 "SIMILARITY: Belongs to the CARF family. {ECO:0000305}.-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" null 956.37 null null 100 uniprot_mouse_length brain_HCD 757.310791 757.310791 757.300206 12 9071.599 13.97730456 C42S1_MOUSE CDC42 small effector protein 1 Q8BHL7 MSEFWHKLGCCVVEKPQPKKKRRRIDRTMIGEPMNFVHLTHIGSGEMGAGDGLAMTGAVQEQMRSKGNHRDRPWSNSRAL 80 "FUNCTION: Probably involved in the organization of the actin cytoskeleton by acting downstream of CDC42, inducing actin filament assembly. Alters CDC42-induced cell shape changes. In activated T-cells, may play a role in CDC42-mediated F-actin accumulation at the immunological synapse. May play a role in early contractile events in phagocytosis in macrophages (By similarity). {ECO:0000250}." null 1392.61 null null 100 uniprot_mouse_length brain_HCD 782.1282349 778.125793 778.133337 31 24079.10915 -9.694409184 CABP2_MOUSE Calcium-binding protein 2; Short=CaBP2 Q9JLK4 GNCAKTPWHRGSKERWQWPGSPLGGSRPSPGPRTEEQEGTQGYSVLGSLVGPACIFLRPSIAATQLDRELRPEEIEELQIAFQEFDRDRDGYIGYRELGACMRTLGYMPTEMELIEISQQISGGKVDFEDFVELMGPKLLAETADMIGVRELRDAFREFDTNGDGCISVGELRAALKALLGERLSQREVDEILQDIDLNGDGLVDFEEFVRMMSR 215 "SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus {ECO:0000250}." null 1293.53 null null 100 uniprot_mouse_length brain_HCD 614.5784302 612.491882 612.49511 23 14057.37548 -5.269716817 CALCA_MOUSE Calcitonin gene-related peptide 1;AltName: Full=Alpha-type CGRP;AltName: Full=Calcitonin gene-related peptide I; Short=CGRP-I;Flags: Precursor Q99JA0 MGFLKFSPFLVVSILLLYQACSLQAVPLRSILESSPGMATLSEEEVRLLAALVQDYMQMKARELEQEEEQEAEGSSVTAQKRSCNTATCVTHRLAGLLSRSGGVVKDNFVPTNVGSEAFGRRRRDLQA 128 "FUNCTION: CGRP induces vasodilation. It dilates a variety of vessels including the coronary, cerebral and systemic vasculature. Its abundance in the CNS also points toward a neurotransmitter or neuromodulator role. It also elevates platelet cAMP (By similarity). {ECO:0000250}." null 3170.62 null null 100 uniprot_mouse_length brain_HCD 544.1309814 540.126892 540.124494 38 20475.70612 4.439883528 CAV1_MOUSE Caveolin-1 P49817 SGGKYVDSEGHLYTVPIREQGNIYKPNNKAMADEVTEKQVYDAHTKEIDLVNRDPKHLNDDVVKIDFEDVIAEPEGTHSFDGIWKASFTTFTVTKYWFYRLLSTIFGIPMALIWGIYFAILSFLHIWAVVPCIKSFLIEIQCISRVYSIYVHTFCDPLFEAIGKIFSNIRISTQKEI 177 FUNCTION: Involved in the costimulatory signal essential for T- cell receptor (TCR)-mediated T-cell activation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. May act as a scaffolding protein within caveolar membranes. Interacts directly with G- protein alpha subunits and can functionally regulate their activity. Forms a stable heterooligomeric complex with CAV2 that targets to lipid rafts and drives caveolae formation. Recruits CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling through the Wnt pathway. {ECO:0000269|PubMed:10816572}. Y5P 2443.05 "Y,0;" 182 100 uniprot_mouse_length brain_HCD 782.1282349 778.125793 778.12073 14 10874.68259 6.507289725 CCKN_MOUSE Cholecystokinin; Short=CCK;Contains: Cholecystokinin-33; Short=CCK33;Contains: Cholecystokinin-12; Short=CCK12;Contains: Cholecystokinin-8; Short=CCK8;Flags: Precursor P09240 QPVVPAEATDPVEQRAQEAPRRQLRAVLRTDGEPRARLGALLARYIQQVRKAPSGRMSVLKNLQSLDPSHRISDRDYMGWMDFGRRSAEDYEYPS 95 "FUNCTION: This peptide hormone induces gall bladder contraction and the release of pancreatic enzymes in the gut. Its function in the brain is not clear. Binding to CCK-A receptors stimulates amylase release from the pancreas, binding to CCK-B receptors stimulates gastric acid secretion." null 233.46 null null 100 uniprot_mouse_length brain_HCD 604.8995361 603.759888 603.764149 14 8434.69361 -7.057896191 CCL11_MOUSE Eotaxin;AltName: Full=C-C motif chemokine 11;AltName: Full=Eosinophil chemotactic protein;AltName: Full=Small-inducible cytokine A11;Flags: Precursor P48298 HPGSIPTSCCFIMTSKKIPNTLLKSYKRITNNRCTLKAIVFKTRLGKEICADPKKKWVQDATKHLDQKLQTPKP 74 "FUNCTION: In response to the presence of allergens, this protein directly promotes the accumulation of eosinophils (a prominent feature of allergic inflammatory reactions), but not lymphocytes, macrophages or neutrophils." null 929.64 null null 100 uniprot_mouse_length brain_HCD 544.1309814 544.995667 544.990175 19 10330.80592 10.07633561 CCL24_MOUSE C-C motif chemokine 24;AltName: Full=Eosinophil chemotactic protein 2;AltName: Full=Eotaxin-2;AltName: Full=Small-inducible cytokine A24;Flags: Precursor Q9JKC0 VTIPSSCCTSFISKKIPENRVVSYQLANGSICPKAGVIFITKKGHKICTDPKLLWVQRHIQKLDAKKNQPSKGAKAVRTKFAVQRRRGNSTEV 93 "FUNCTION: Chemotactic for resting T-lymphocytes, and eosinophils. Has lower chemotactic activity for neutrophils but none for monocytes and activated lymphocytes. Binds to CCR3 (By similarity). {ECO:0000250}." null 794.33 null null 100 uniprot_mouse_length brain_HCD 790.402832 789.680664 789.690884 10 7883.90632 -12.94169365 CCL3_MOUSE C-C motif chemokine 3;AltName: Full=Heparin-binding chemotaxis protein;AltName: Full=L2G25B;AltName: Full=Macrophage inflammatory protein 1-alpha; Short=MIP-1-alpha;AltName: Full=SIS-alpha;AltName: Full=Small-inducible cytokine A3;AltName: Full=TY-5;Flags: Precursor P10855 APYGADTPTACCFSYSRKIPRQFIVDYFETSSLCSQPGVIFLTKRNRQICADSKETWVQEYITDLELNA 69 "FUNCTION: Monokine with inflammatory, pyrogenic and chemokinetic properties. Has a potent chemotactic activity for eosinophils. Binding to a high-affinity receptor activates calcium release in neutrophils." null 372.26 null null 100 uniprot_mouse_length brain_HCD 824.1838989 828.300476 828.311553 9 7442.80103 -13.37289784 CD003_MOUSE Uncharacterized protein C4orf3 homolog Q99M08 MEVSQAASGTDGVRERRGSFEAGRRNQDEAPQSGMNGLPKHSYWLDLWLFILFDLALFVFVYLLP 65 "SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" M1Ac 217.62 "M,12;" 27 100 uniprot_mouse_length brain_HCD 544.1309814 541.584961 541.582855 23 12427.39582 3.888486278 CDKA1_MOUSE Cyclin-dependent kinase 2-associated protein 1; Short=CDK2-associated protein 1;AltName: Full=Deleted in oral cancer 1; Short=DOC-1;AltName: Full=Putative oral cancer suppressor O35207 MSYKPNLTAHMPAAALNAGSVHSPSTSMATSSQYRQLLSDYGPPSLGYTQGTGNSQVPQSKYAELLAIIEELGKEIRPTYAGSKSAMERLKRGIIHARSLVRECLAETERNARS 114 FUNCTION: specific inhibitor of the cell-cycle kinase CDK2. {ECO:0000269|PubMed:10938106}. S45P 729.08 "S,73;" 85 100 uniprot_mouse_length brain_HCD 697.6692505 695.830994 695.83121 19 13194.78083 -0.310919736 CDKA2_MOUSE Cyclin-dependent kinase 2-associated protein 2; Short=CDK2-associated protein 2;AltName: Full=DOC-1-related protein; Short=DOC-1R Q9CPY4 MSYKPIAPAPSSTPGSSTPGPGTPVPTAGSVPSPSGSVPGAAAPFRPLFNDFGPPSMGYVQAMKPPGSQGSQSTYTDLLSVIEEMGKEIRPTYAGSKSAMERLKRGIIHARALVRECLAETERNART 127 "SIMILARITY: Belongs to the CDK2AP family. {ECO:0000305}.-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" null 2685.31 null null 100 uniprot_mouse_length brain_HCD 660.946228 659.33667 659.336836 27 17766.07743 -0.251886617 CDN1A_MOUSE Cyclin-dependent kinase inhibitor 1;AltName: Full=CDK-interacting protein 1;AltName: Full=Melanoma differentiation-associated protein;AltName: Full=p21 P39689 SNPGDVRPVPHRSKVCRCLFGPVDSEQLRRDCDALMAGCLQEARERWNFDFVTETPLEGNFVWERVRSLGLPKVYLSPGSRSRDDLGGDKRPSTSSALLQGPAPEDHVALSLSCTLVSERPEDSPGGPGTSQGRKRRQTSLTDFYHSKRRLVFCKRKP 158 "FUNCTION: May be the important intermediate by which p53/TP53 mediates its role as an inhibitor of cellular proliferation in response to DNA damage. Binds to and inhibits cyclin-dependent kinase activity, preventing phosphorylation of critical cyclin- dependent kinase substrates and blocking cell cycle progression. Functions in the nuclear localization and assembly of cyclin D- CDK4 complex and promotes its kinase activity towards RB1. At higher stoichiometric ratios, inhibits the kinase activity of the cyclin D-CDK4 complex (By similarity). {ECO:0000250}." S1AcS77P 7416.6 "S,291;S,65;" 261 100 uniprot_mouse_length brain_HCD 692.2106934 695.823792 695.822941 26 18056.37835 1.222299318 CDN2C_MOUSE Cyclin-dependent kinase 4 inhibitor C;AltName: Full=Cyclin-dependent kinase 6 inhibitor;AltName: Full=p18-INK4c;AltName: Full=p18-INK6 Q60772 MAEPWGNELASAAARGDLEQLTSLLQNNVNVNAQNGFGRTALQVMKLGNPEIARRLLLRGANPNLKDGTGFAVIHDAARAGFLDTVQALLEFQADVNIEDNEGNLPLHLAAKEGHLPVVEFLMKHTACNVGHRNHKGDTAFDLARFYGRNEVISLMEANGVGGATSLQ 168 "FUNCTION: Interacts strongly with CDK6, weakly with CDK4. Inhibits cell growth and proliferation with a correlated dependence on endogenous retinoblastoma protein RB." null 4167.65 null null 100 uniprot_mouse_length brain_HCD 616.8856812 615.080627 615.082392 29 17799.37229 -2.868816628 CDN2D_MOUSE Cyclin-dependent kinase 4 inhibitor D;AltName: Full=p19-INK4d Q60773 MLLEEVCVGDRLSGAAARGDVQEVRRLLHRELVHPDALNRFGKTALQVMMFGSPAVALELLKQGASPNVQDASGTSPVHDAARTGFLDTLKVLVEHGADVNALDSTGSLPIHLAIREGHSSVVSFLAPESDLHHRDASGLTPLELARQRGAQNLMDILQGHMMIPM 166 "FUNCTION: Interacts strongly with CDK4 and CDK6 and inhibits them. {ECO:0000269|PubMed:7739547, ECO:0000269|PubMed:7739548}." null 7778.98 null null 100 uniprot_mouse_length brain_HCD 960.0300293 963.781311 963.774453 21 20207.24218 7.115809238 CE024_MOUSE UPF0461 protein C5orf24 homolog Q80X32 MMHPVAGSNPAFCGPGKPSCLNEDAMRAADQFDLYSSQQNKYSHTVSHKPMVCQRQDPLNETHLQPTSGRNIEIKDELKKKKNLNRSGKRGRPSGTTKSAGYRTSTGRPLGTTKAAGFKTSPGRPLGTTKAAGYKVSPGRPPGSIKALSRLADLGYGCGTAAFPYPMMHSRVVHGLQETSGEVKPPSE 188 SIMILARITY: Belongs to the UPF0461 family. {ECO:0000305}. S37P 1847.97 "S,111;" 154 100 uniprot_mouse_length brain_HCD 616.8856812 617.452881 617.447824 31 19099.86174 8.189937965 CETN4_MOUSE Centrin-4;AltName: Full=Centrin4 {ECO:0000303|PubMed:12802058} Q8K4K1 ASSQRITLDQWKKKAAKVELNDTQKQEIKEAFDLFDIDGSGTIDLKELKIAMRALGFEPKKEEVKQLIAEIDKEGTGTICFEDFFAIMSVKMSEKDEKEEILKAFKLFDDDATGSISLNNIKRVAKELGENLTEDELQEMLDEADRDGDGEINEEEFLKMMKKTSLY 167 FUNCTION: Ca(2+)-binding protein that may be involved in basal body assembly or in a subsequent step of ciliogenesis. {ECO:0000269|PubMed:12802058}. A1Ac 8387.58 "A,342;" 281 100 uniprot_mouse_length brain_HCD 777.1407471 780.639343 780.640863 14 10909.96314 -1.946782898 CH10_MOUSE "10 kDa heat shock protein, mitochondrial; Short=Hsp10;AltName: Full=10 kDa chaperonin;AltName: Full=Chaperonin 10; Short=CPN10" Q64433 AGQAFRKFLPLFDRVLVERSAAETVTKGGIMLPEKSQGKVLQATVVAVGSGGKGKSGEIEPVSVKVGDKVLLPEYGGTKVVLDDKDYFLFRDSDILGKYVD 101 "FUNCTION: Eukaryotic CPN10 homolog which is essential for mitochondrial protein biogenesis, together with CPN60. Binds to CPN60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter." A1AcK7Ac 2341.23 "A,2;K,0;" 124 100 uniprot_mouse_length brain_HCD 787.0587769 786.345581 786.352743 14 10989.92947 -9.107802289 CH10_MOUSE "10 kDa heat shock protein, mitochondrial; Short=Hsp10;AltName: Full=10 kDa chaperonin;AltName: Full=Chaperonin 10; Short=CPN10" Q64433 AGQAFRKFLPLFDRVLVERSAAETVTKGGIMLPEKSQGKVLQATVVAVGSGGKGKSGEIEPVSVKVGDKVLLPEYGGTKVVLDDKDYFLFRDSDILGKYVD 101 "FUNCTION: Eukaryotic CPN10 homolog which is essential for mitochondrial protein biogenesis, together with CPN60. Binds to CPN60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter." A1AcK7AcT78P 1351.74 "A,0;K,0;T,82;" 97 100 uniprot_mouse_length brain_HCD 724.6809692 722.550781 722.555612 27 19470.9803 -6.685644565 CI009_MOUSE "Uncharacterized protein C9orf9 homolog;AltName: Full=Acrosome and sperm tail protein {ECO:0000303|PubMed:24256100, ECO:0000303|Ref.4}; Short=MAST {ECO:0000303|PubMed:24256100, ECO:0000303|Ref.4}" Q7TPM5 MNEVKESLRSIEQKYKLFQQQQFTFIAALEHCRENAHDKIRPISSIEQVQSYMEHYCNNSTHRRILIMFMDICSELSKLCQHFEALHSGTPVTNSLLEKCKTLVSQSNDLSSLRAKYPHEVVNHLSCDEARNHYGGVVSLIPIVLDFMKEWIAHSEKLPRKVLQHGTT 168 SUBUNIT: Interacts with CABP1 AND CALR. {ECO:0000269|PubMed:24256100}. null 1594.65 null null 100 uniprot_mouse_length brain_HCD 1015.345215 1015.896179 1015.910661 9 9130.19121 -14.2549944 CI016_MOUSE UPF0184 protein C9orf16 homolog P58686 MSGPNGDLGMPVDAGTEGENDSFGEAEYAAINSMLDQINSCLDHLEEKNDHLHARLQELLESNRQTRLEFQQQLGEAPGDASP 83 "SIMILARITY: Belongs to the UPF0184 (EST00098) family. {ECO:0000305}.-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" S82P 605.11 "S,29;" 50 100 uniprot_mouse_length brain_HCD 658.0570679 653.561584 653.55956 37 24132.6784 3.097610042 CINP_MOUSE Cyclin-dependent kinase 2-interacting protein Q9D0V8 MEAKTLGIATPRKPVLSVSARKLKDNAADWHNLILKWDSLSDKGFTTASSIANLKVSLLSKEKVELESSSPASMEEEEKTNLDYDKGLEALCEELQAILDGLTKIQMKMEKLSSTTKGICELENYHYREESSRPPLFHTWPTAFFYEVSRRLSEAYKKELLLKHTIGAELAHTADRNLSLTYLSMWLHQPYIESNSKLQLESMLLETGHRAL 212 "FUNCTION: Interacts with the components of the replication complex and 2 kinases, CDK2 and CDC7, thereby providing a functional and physical link between CDK2 and CDC7 during firing of the origins of replication. Regulates ATR-mediated checkpoint signaling (By similarity). {ECO:0000250}." M1Ac 3451.51 "M,226;" 261 100 uniprot_mouse_length brain_HCD 544.1309814 542.409546 542.412885 48 25974.79 -6.156014458 CJ011_MOUSE Leucine-rich repeat-containing protein C10orf11 homolog Q9D9B4 MAGLMVSGTQVSYVGQSCREIPEHLGRDFGHFAKRLDLSFNLLRSLEGLSAFRSLEELILDNNLLGDDLVLPGLPHLHTLTLNKNQITDLEYLLDHLAEVTPSLEYLSLLGNVACPNELVNLEKDEEDYKRYRCFVLHKLPKLKFLDAQKVTRQEREEALVRGAFMKVVKPKASSEEEKAAAPENQPQYTPLPSGSRDLTSHRGVLGKGRYFYYGRNSEGNRFIRDDQL 229 FUNCTION: Required for melanocyte differentiation. {ECO:0000250}. null 5464.44 null null 100 uniprot_mouse_length brain_HCD 881.8521118 882.239075 882.235645 13 11451.05542 3.887518092 CJ032_MOUSE UPF0693 protein C10orf32 homolog Q9CRC6 ATGTPDSQARFGQSVKGLLTEKVNTCGTDVIALTKQVLKGSRSSELLGQAARNMVLQEDAILHSEDSLRKMAIITTHLQYQQEAIQKNVEQSPDLQDQLSHLLK 104 "SIMILARITY: Belongs to the UPF0693 family. {ECO:0000305}.-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" A1Ac 854.04 "A,40;" 76 100 uniprot_mouse_length brain_HCD 614.1868286 617.250183 617.243998 14 8623.41125 10.02051942 CK2N2_MOUSE Calcium/calmodulin-dependent protein kinase II inhibitor 2;AltName: Full=CaM-KII inhibitory protein; Short=CaM-KIIN Q78WH7 MSEILPYGEDKMGRFGADPEGSDLSFSCRLQDTNSFFAGNQAKRPPKLGQIGRAKRVVIEDDRIDDVLKGMGEKPPSGV 79 FUNCTION: Potent and specific cellular inhibitor of CaM-kinase II (CAMK2). Traps Ca(2+)/calmodulin on CAMK2 (By similarity). {ECO:0000250}. null 334.87 null null 100 uniprot_mouse_length brain_HCD 649.0530396 653.337341 653.339918 15 9780.09087 -3.943875669 CKS2_MOUSE Cyclin-dependent kinases regulatory subunit 2; Short=CKS-2 P56390 AHKQIYYSDKYFDEHYEYRHVMLPRELSKQVPKTHLMSEEEWRRLGVQQSLGWVHYMIHEPEPHILLFRRPLPKEQQK 78 FUNCTION: Binds to the catalytic subunit of the cyclin dependent kinases and is essential for their biological function. A1Ac 945.93 "A,0;" 55 100 uniprot_mouse_length brain_HCD 637.3640137 641.537964 641.529404 35 22404.50436 13.34290702 CLD4_MOUSE Claudin-4;AltName: Full=Clostridium perfringens enterotoxin receptor; Short=CPE-R; Short=CPE-receptor O35054 MASMGLQVLGISLAVLGWLGIILSCALPMWRVTAFIGSNIVTAQTSWEGLWMNCVVQSTGQMQCKMYDSMLALPQDLQAARALMVISIIVGALGMLLSVVGGKCTNCMEDETVKAKIMITAGAVFIVASMLIMVPVSWTAHNVIRDFYNPMVASGQKREMGASLYVGWAASGLLLLGGGLLCCSCPPRSNDKPYSAKYSAARSVPASNYV 210 "FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium- independent cell-adhesion activity. {ECO:0000250}." Y209P 2715.02 "Y,152;" 202 100 uniprot_mouse_length brain_HCD 730.3717651 734.349915 734.355055 32 23454.33694 -6.999950751 CLD6_MOUSE Claudin-6;AltName: Full=Skullin Q9Z262 MASTGLQILGIVLTLLGWVNALVSCALPMWKVTAFIGNSIVVAQMVWEGLWMSCVVQSTGQMQCKVYDSLLALPQDLQAARALCVVTLLIVLLGLLVYLAGAKCTTCVEDRNSKSRLVLISGIIFVISGVLTLIPVCWTAHSIIQDFYNPLVADAQKRELGASLYLGWAASGLLLLGGGLLCCACSSGGTQGPRHYMACYSTSVPHSRGPSEYPTKNYV 219 "FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium- independent cell-adhesion activity. {ECO:0000250}." S201P 2547.98 "S,2;" 213 100 uniprot_mouse_length brain_HCD 525.9760742 528.538513 528.532223 25 13182.2944 11.90123009 CO040_MOUSE UPF0235 protein C15orf40 homolog Q9CRC3 MPKKAGATSKGKNQTKEPETAPPAAGPVATDPKGFVTIAIHAKPGSRQNAVTDLSTEAVGVAIAAPPSEGEANAELCRYLSKVLDLRKSDVVLDKGGKSREKVVKLLASTTPEEVLEKLKTEAEKK 126 "SIMILARITY: Belongs to the UPF0235 family. {ECO:0000305}.-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" null 316.73 null null 100 uniprot_mouse_length brain_HCD 1045.76355 1045.76355 1045.763587 8 8354.10543 -0.035567611 COA5_MOUSE Cytochrome c oxidase assembly factor 5 Q99M07 MPRYYEDKPEGGACAGVKEDLGACLLQSACVLQEGKSPRQCLKEGNCRALQYSFFECKRSMLDARSRFRGRKGY 74 FUNCTION: Involved in an early step of the mitochondrial complex IV assembly process. {ECO:0000250}. null 247.45 null null 100 uniprot_mouse_length brain_HCD 650.3551025 646.165222 646.161818 18 11606.90236 5.268290193 CORT_MOUSE Cortistatin;Contains: Cortistatin-14;Flags: Precursor P56469 MMGGRGTGGKWPSAFGLLLLWGVAASALPLESGPTGQDSVQEATEGRSGLLTFLAWWHEWASQASSSTPVGGGTPGLSKSQERPPPQQPPHLDKKPCKNFFWKTFSSCK 109 SUBCELLULAR LOCATION: Secreted. null 266.04 null null 100 uniprot_mouse_length brain_HCD 876.0230103 872.598694 872.595399 15 13066.91849 3.775916834 COX20_MOUSE Cytochrome c oxidase protein 20 homolog Q9D7J4 AAAPEPHETEKKPFKLLGILDVENTPCARESILYGSLGSIVTGLGHFLVTSRIRRSCDVGVGGFILVTLGCWFHCRYNFAKQRIQERIAREGIKNKILYESTHLDPERKMKTNNSS 116 SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305}; Multi- pass membrane protein {ECO:0000305}. A1Ac 1040.4 "A,57;" 99 100 uniprot_mouse_length brain_HCD 652.1968384 652.430847 652.432248 13 8464.61435 -2.147091956 COX6C_MOUSE Cytochrome c oxidase subunit 6C;AltName: Full=Cytochrome c oxidase polypeptide VIc Q9CPQ1 MSSGALLPKPQMRGLLAKRLRVHIAGAFIVALGVAAAYKFGVAEPRKKAYAEFYRNYDSMKDFEEMRKAGIFQSAK 76 "FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. {ECO:0000250}." null 1165.69 null null 100 uniprot_mouse_length brain_HCD 658.0910645 655.552429 655.55291 10 6542.527 -0.73342788 COX7R_MOUSE "Cytochrome c oxidase subunit 7A-related protein, mitochondrial;AltName: Full=Cytochrome c oxidase subunit VIIa-related protein;AltName: Full=Silica-induced gene 81 protein; Short=SIG-81;AltName: Full=Supercomplex assembly factor I {ECO:0000303|PubMed:23812712};Flags: Precursor" Q61387 GKNKVPELQKFFQKADGFHLKRGLPDQMLYRTTMALTLGGTIYCLIALYMASQPRNK 57 "FUNCTION: Involved in the regulation of oxidative phosphorylation and energy metabolism (PubMed:23857330, PubMed:23812712). Necessary for the assembly of mitochondrial respiratory supercomplex (PubMed:23857330, PubMed:23812712). {ECO:0000269|PubMed:23812712, ECO:0000269|PubMed:23857330}." K14Ac 245.11 "K,24;" 34 100 uniprot_mouse_length brain_HCD 642.4732666 644.536804 644.539251 13 8362.00621 -3.79620136 CP074_MOUSE Uncharacterized protein C16orf74 homolog Q8K1L6 MGLKPSCLKGFKMCVSSSNNNHDEAPVLNDKHLSVPNIIITPPTPTGMGLSRDSNKQVWMDELGSYQDDGELEPEA 76 "SEQUENCE CAUTION: Sequence=AAH27666.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; Sequence=BAE43181.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" T44P 320.65 "T,1;" 44 100 uniprot_mouse_length brain_HCD 1008.396545 1003.606995 1003.604184 18 18036.85651 2.800535262 CPLX4_MOUSE Complexin-4;AltName: Full=Complexin IV; Short=CPX IV;Flags: Precursor Q80WM3 MAFFVKNMISNQVKNLGFGGGSEEKKEEGGTSDPAAAKGMTREEYEEYQKQMIEEKMERDAAFTQKKAERACLRVHLRDKYRLPKSEMDETQIQLAGDDVDLPEDLRKMVDEDQDEEEEKDSILGQLQNLQNMDLDTIKEKAQATFTEIKQSAEQKC 157 FUNCTION: Positively regulates a late step in synaptic vesicle exocytosis. {ECO:0000269|PubMed:15911881}. C157Me 1369.52 "C,83;" 126 100 uniprot_mouse_length brain_HCD 777.1407471 778.851624 778.86087 18 13994.4841 -11.87177993 CRBL2_MOUSE cAMP-responsive element-binding protein-like 2 Q32M00 MDDSKVVGGKVKKPGKRGRKPAKIDLKAKLERSRQSARECRARKKLRYQYLEELVSSRERAICALREELEMYKQWCMAMDQGKIPSEIRALLTGEEQSKPQQNSSRHPKAGKTDANTNSLVGN 123 FUNCTION: Probable regulator of CREB1 transcriptional activity which is involved in adipose cells differentiation. May also play a regulatory role in the cell cycle. {ECO:0000269|PubMed:21728997}. null 2401.68 null null 100 uniprot_mouse_length brain_HCD 827.7537842 826.18457 826.186646 26 21442.82695 -2.512371157 CREG1_MOUSE Protein CREG1;AltName: Full=Cellular repressor of E1A-stimulated genes 1;Flags: Precursor O88668 RGGRDHGDWDVDRRLPPLPPREDGPRVARFVTHVSDWGSLATISTIKEVRGWPFADIISISDGPPGEGTGEPYMYLSPLQQAVSDLQENPEATLTMSLAQTVYCRNHGFDPQSPLCVHIMMSGTVTKVNKTEEDYARDSLFVRHPEMKHWPSSHNWFFAKLKISRIWVLDYFGGPKVVTPEEYFNVTLQ 189 FUNCTION: May contribute to the transcriptional control of cell growth and differentiation. Antagonizes transcriptional activation and cellular transformation by the adenovirus E1A protein. The transcriptional control activity of cell growth requires interaction with IGF2R (By similarity). {ECO:0000250}. null 1628.37 null null 100 uniprot_mouse_length brain_HCD 998.0165405 1001.802063 1001.805802 21 21004.89973 -3.732271975 CRGA_MOUSE Gamma-crystallin A;AltName: Full=Gamma-A-crystallin;AltName: Full=Gamma-crystallin 4 P04345 GKITFYEDRGFQGRCYECSSDCPNLQTYFSRCNSIRVDSGCWMLYERPNYQGYQYFLRRGDYPDYQQWMGFSDSIRSCRSIPYTSSHRIRLYERDDYRGLVSELMDDCSCIHDRFRLHEIYSMHVLEGCWVLYEMPNYRGRQYLLRPGDYRRYHDWGAMDAKVGSLRRVMDLY 173 FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens. null 1255.72 null null 100 uniprot_mouse_length brain_HCD 614.1868286 613.52179 613.51922 30 18366.5583 4.188215621 CS043_MOUSE Uncharacterized protein C19orf43 homolog Q9D735 MAARGRRAEPPGREAPGPAGSGRSRWAESGPGTSPESGDDEVSGSSPVSSGVNLFANDGSFLELFKRKMEEEQRQRQEEPPPGPQRPDPPASAAAGPGNPKRKGGPGPTLSFVGKRRGGNKLALKTGIVAKKQKTEDEVLTSKGDAWAKYMAEVKKYKAHQCGDDDKTRPLVK 173 "-------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License--------------------------------------------------" null 1764.07 null null 100 uniprot_mouse_length brain_HCD 683.7625122 683.131287 683.13199 27 18408.5454 -1.029638366 CS043_MOUSE Uncharacterized protein C19orf43 homolog Q9D735 MAARGRRAEPPGREAPGPAGSGRSRWAESGPGTSPESGDDEVSGSSPVSSGVNLFANDGSFLELFKRKMEEEQRQRQEEPPPGPQRPDPPASAAAGPGNPKRKGGPGPTLSFVGKRRGGNKLALKTGIVAKKQKTEDEVLTSKGDAWAKYMAEVKKYKAHQCGDDDKTRPLVK 173 "-------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License--------------------------------------------------" K143Ac 7950.78 "K,359;" 269 100 uniprot_mouse_length brain_HCD 634.3200073 637.071655 637.073522 20 12715.46008 -2.930158762 CST12_MOUSE Cystatin-12;AltName: Full=Cystatin TE-1;Flags: Precursor Q9DAN8 KFLEIDKNEEEFAISVEHVVFHFNENQDDDFAYKFLRVRRSLRQKYTLKYLVDLEMGRTLCGKYDEDIDNCPLQEGPGERKVRCTYIVETEAWVTKFTILNSTCVQT 107 FUNCTION: May play a specialized role in spermatogenesis. {ECO:0000269|PubMed:12444065}. null 503.72 null null 100 uniprot_mouse_length brain_HCD 734.6552734 737.376831 737.38378 9 6624.45189 -9.423783789 CX7A1_MOUSE "Cytochrome c oxidase subunit 7A1, mitochondrial;AltName: Full=Cytochrome c oxidase subunit VIIa-heart; Short=Cytochrome c oxidase subunit VIIa-H;AltName: Full=Cytochrome c oxidase subunit VIIa-muscle; Short=Cytochrome c oxidase subunit VIIa-M;Flags: Precursor" P56392 LENRVAEKQKLFQADNDLPVHLKGGGMDNVLYRLTMTLTLGGTAYCLYCLGWASFPHKK 59 "FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport." null 677.01 null null 100 uniprot_mouse_length brain_HCD 629.6715088 630.140198 630.132639 15 9431.98346 11.99549656 CXL14_MOUSE C-X-C motif chemokine 14;AltName: Full=B-cell and monocyte-activating chemokine;AltName: Full=Chemokine BRAK;AltName: Full=Kidney-expressed chemokine CXC;AltName: Full=MIP-2G;AltName: Full=Small-inducible cytokine B14;Flags: Precursor Q9WUQ5 SKCKCSRKGPKIRYSDVKKLEMKPKYPHCEEKMVIVTTKSMSRYRGQEHCLHPKLQSTKRFIKWYNAWNEKRRVYEE 77 "FUNCTION: Chemotactic for CESS B-cells and THP-1 monocytes, but not T-cells. {ECO:0000269|PubMed:10784614}." null 290.89 null null 100 uniprot_mouse_length brain_HCD 1008.396545 1011.108398 1011.109716 15 15143.62893 -1.303085589 CYB5_MOUSE Cytochrome b5 P56395 AGQSDKDVKYYTLEEIQKHKDSKSTWVILHHKVYDLTKFLEEHPGGEEVLREQAGGDATENFEDVGHSTDARELSKTYIIGELHPDDRSKIAKPSDTLITTVESNSSWWTNWVIPAISALAVALMYRLYMAED 133 "FUNCTION: Cytochrome b5 is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases. It is also involved in several steps of the sterol biosynthesis pathway, particularly in the C-5 double bond introduction during the C-5 desaturation." A1Ac 817.43 "A,0;" 85 100 uniprot_mouse_length brain_HCD 642.4702148 645.237854 645.22884 18 11590.10887 13.97024334 CYC_MOUSE "Cytochrome c, somatic" P62897 GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAAGFSYTDANKNKGITWGEDTLMEYLENPKKYIPGTKMIFAGIKKKGERADLIAYLKKATNE 104 "FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. {ECO:0000269|PubMed:12062423}." G1AcY48P 874.34 "G,52;Y,36;" 79 100 uniprot_mouse_length brain_HCD 732.2000122 728.50708 728.505756 16 11634.08209 1.817525962 CYT3_MOUSE Stefin-3 P35173 MSQENLKIKGGLSEARPATPEIQMIADKVRPLLEEQTNEKYEKFEAVEYKSQVVAGQNLFIKIDVGNGCFLHMKVFRGLSGEDDLKLKGYQTNKTKTDELTSM 103 FUNCTION: This is an intracellular thiol proteinase inhibitor. null 610.98 null null 100 uniprot_mouse_length brain_HCD 813.9421387 815.365356 815.373723 14 11395.22384 -10.26100603 CYTM1_MOUSE Cysteine-rich and transmembrane domain-containing protein 1 Q8K353 MNPENPPPYPGPGPTAPYPPYPQQPMGPMGPMGAPPPQGYPYPPPQGYPYQGYPQYGWQGGPQEPPKTTVYVVEDQRRDDLGPSTCLTACWTALCCCCLWDMLT 104 SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. null 2007.62 null null 100 uniprot_mouse_length brain_HCD 699.5198364 694.929688 694.919766 16 11097.70819 14.27718779 DAP1_MOUSE Death-associated protein 1; Short=DAP-1 Q91XC8 SSPPEGKLETKAGHPPAVKAGGMRIVQKHPHTGDGKEERDKDDQEWESTSPPKPTVFISGVIARGDKDFPPAAAQVAHQKPHASMDKHVSPRTQHIQQPRK 101 FUNCTION: Negative regulator of autophagy. Involved in mediating interferon-gamma-induced cell death (By similarity). {ECO:0000250}. S2P 813.8 "S,10;" 59 100 uniprot_mouse_length brain_HCD 697.6692505 697.545227 697.545427 16 11139.71876 -0.286646878 DAP1_MOUSE Death-associated protein 1; Short=DAP-1 Q91XC8 SSPPEGKLETKAGHPPAVKAGGMRIVQKHPHTGDGKEERDKDDQEWESTSPPKPTVFISGVIARGDKDFPPAAAQVAHQKPHASMDKHVSPRTQHIQQPRK 101 FUNCTION: Negative regulator of autophagy. Involved in mediating interferon-gamma-induced cell death (By similarity). {ECO:0000250}. S1AcS2P 2019.09 "S,8;S,28;" 117 100 uniprot_mouse_length brain_HCD 617.6973267 622.263184 622.261012 18 11177.69017 3.489843824 DAP1_MOUSE Death-associated protein 1; Short=DAP-1 Q91XC8 SSPPEGKLETKAGHPPAVKAGGMRIVQKHPHTGDGKEERDKDDQEWESTSPPKPTVFISGVIARGDKDFPPAAAQVAHQKPHASMDKHVSPRTQHIQQPRK 101 FUNCTION: Negative regulator of autophagy. Involved in mediating interferon-gamma-induced cell death (By similarity). {ECO:0000250}. S2PS48P 695.23 "S,10;S,0;" 62 100 uniprot_mouse_length brain_HCD 732.2000122 734.939514 734.936851 16 11737.98131 3.623658485 DDA1_MOUSE DET1- and DDB1-associated protein 1 Q9D9Z5 ADFLKGLPVYNKSNFSRFHADSVCKASNRRPSVYLPTREYPSEQIIVTEKTNILLRYLHQQWDKKNAAKKRDQEQVEAEGESSAPPRKVARTDSPDMPEDT 101 FUNCTION: May be involved in ubiquitination and subsequent proteasomal degradation of target proteins. Component of the DDD- E2 complexes which may provide a platform for interaction with CUL4A and WD repeat proteins (By similarity). {ECO:0000250}. A1AcS32P 599.21 "A,45;S,37;" 72 100 uniprot_mouse_length brain_HCD 614.1868286 613.819519 613.816896 30 18374.48508 4.273331324 DESI1_MOUSE Desumoylating isopeptidase 1; Short=DeSI-1; EC=3.4.-.-;AltName: Full=PPPDE peptidase domain-containing protein 2;AltName: Full=Protein FAM152B Q9CQT7 MEPPNLYPVKLYVYDLSKGLARRLSPIMLGKQLEGIWHTSIVVHKDEFFFGSSGISSCTPGGTLLGPPDSVVDVGNTEVTEEIFLEYLSSLGESLFRGEAYNLFEHNCNTFSNEVAQFLTGRKIPSYITDLPSEVLSTPFGQALRPFLDSIQIQPPGGNSVGRPNGQS 168 "FUNCTION: Protease which deconjugates SUMO1, SUMO2 and SUMO3 from some substrate proteins. Has isopeptidase but not SUMO-processing activity. Desumoylates ZBTB46. {ECO:0000269|PubMed:22370726, ECO:0000269|PubMed:22498933}." null 1547.74 null null 100 uniprot_mouse_length brain_HCD 847.5718994 844.913086 844.9104 6 5061.46391 3.178961343 DFB13_MOUSE "Beta-defensin 13; Short=BD-13; Short=mBD-13;AltName: Full=Defensin, beta 13;Flags: Precursor" Q8R2I4 TLYRRFLCKKMNGQCEAECFTFEQKIGTCQANFLCCRKRKEH 42 FUNCTION: Has antibacterial activity. {ECO:0000250}. null 214.58 null null 100 uniprot_mouse_length brain_HCD 785.2276001 781.059631 781.05839 6 4678.35218 1.589314797 DFB35_MOUSE "Beta-defensin 35; Short=BD-35; Short=mBD-35;AltName: Full=Defensin, beta 35;Flags: Precursor" Q8R2I3 EIAVCETCRLGRGKCRRACIESEKIVGWCKLNFFCCRERI 40 FUNCTION: Has antibacterial activity. {ECO:0000250}. null 223.69 null null 100 uniprot_mouse_length brain_HCD 596.9086304 597.811951 597.804176 10 5966.0426 13.00540195 DFB40_MOUSE "Beta-defensin 40; Short=BD-40; Short=mBD-40;AltName: Full=Defensin, beta 40;Flags: Precursor" Q70KL2 LDTIKCLQGNNNCHIQKCPWFLLQVSTCYKGKGRCCQKRRWFARSHVYHV 50 FUNCTION: Has antibacterial activity. {ECO:0000250}. null 757.05 null null 100 uniprot_mouse_length brain_HCD 541.6662598 542.934265 542.936576 35 18957.75955 -4.256230623 DNPH1_MOUSE 2'-deoxynucleoside 5'-phosphate N-hydrolase 1 {ECO:0000255|HAMAP-Rule:MF_03036}; EC=3.2.2.- {ECO:0000255|HAMAP-Rule:MF_03036};AltName: Full=c-Myc-responsive protein Rcl {ECO:0000255|HAMAP-Rule:MF_03036} Q80VJ3 AASGELVPCSVYFCGSIRGGREDQALYSRIVSRLRRYGKVLTEHVADAELEPRGEEAAGGDQFIHERDLAWLRQADVVVAEVTQPSLGVGYELGRAVALGKPILCLFRPQSGRVLSAMIRGAADGSRFQVWDYAEEEVETMLHRYFEAYLPQGTASSSNPSACLNPTVLEKI 172 FUNCTION: Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5- phosphate and a purine or pyrimidine base. Deoxyribonucleoside 5'- monophosphates containing purine bases are preferred to those containing pyrimidine bases. {ECO:0000255|HAMAP-Rule:MF_03036}. A1AcS16P 354.54 "A,41;S,14;" 70 100 uniprot_mouse_length brain_HCD 544.1309814 542.165894 542.166306 24 12980.97858 -0.760735789 DOPD_MOUSE D-dopachrome decarboxylase; EC=4.1.1.84;AltName: Full=D-dopachrome tautomerase O35215 PFVELETNLPASRIPAGLENRLCAATATILDKPEDRVSVTIRPGMTLLMNKSTEPCAHLLVSSIGVVGTAEQNRTHSASFFKFLTEELSLDQDRIVIRFFPLEAWQIGKKGTVMTFL 117 "FUNCTION: Tautomerization of D-dopachrome with decarboxylation to give 5,6-dihydroxyindole (DHI). {ECO:0000250}." P1Ac 967.88 "P,8;" 95 100 uniprot_mouse_length brain_HCD 663.7713013 664.235046 664.231234 14 9281.23303 5.7395475 DPH3_MOUSE DPH3 homolog;AltName: Full=CSL-type zinc finger-containing protein 2;AltName: Full=DelGEF-interacting protein 1; Short=DelGIP1 Q8K0W9 MAVFHDEVEIEDFQYDEDSETYFYPCPCGDNFAITKEDLENGEDVATCPSCSLIIKVIYDKDQFMCGETVPAPSTNKELVKC 82 "FUNCTION: Essential for the first step in the synthesis of diphthamide, a post-translational modification of histidine which occurs in elongation factor 2." null 1758.73 null null 100 uniprot_mouse_length brain_HCD 581.7600098 579.597778 579.592809 21 12144.43806 8.573812917 DPOE4_MOUSE DNA polymerase epsilon subunit 4; EC=2.7.7.7;AltName: Full=DNA polymerase II subunit 4;AltName: Full=DNA polymerase epsilon subunit p12 Q9CQ36 AAAAAAGSGTPREEEAPGGEAAASQAQAPTSAPGGVRLSRLPLARVKALVKADPDVTLAGQEAIFILARAAELFVETIAKDAYCCAQQGKRKTLQRRDLDNAIEAVDEFAFLEGTLD 117 FUNCTION: May play a role in allowing polymerase epsilon to carry out its replication and/or repair function. A1Ac 801.71 "A,49;" 87 100 uniprot_mouse_length brain_HCD 545.1296387 542.703613 542.71136 21 11370.93007 -14.27410465 DPY30_MOUSE Protein dpy-30 homolog;AltName: Full=Dpy-30-like protein; Short=Dpy-30L Q99LT0 MESEQMLEGQTQVAENPHSEYGLTDSVERIVENEKINAEKSSKQKVDLQSLPTRAYLDQTVVPILLQGLAVLAKERPPNPIEFLASYLLKNKAQFEDRN 99 "FUNCTION: As part of the MLL1/MLL complex, involved in the methylation of histone H3 at 'Lys-4', particularly trimethylation. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. May play some role in histone H3 acetylation. In embryonic stem (ES) cells, plays a crucial role in the differentiation potential, particularly along the neural lineage, regulating gene induction and histone H3 'Lys- 4' methylation at key developmental loci, including that mediated by retinoic acid. Does not affect ES cell self-renewal. May also play an indirect or direct role in endosomal transport. {ECO:0000269|PubMed:21335234}." M1AcS19PK35Ac 923.81 "M,3;S,66;K,35;" 85 100 uniprot_mouse_length brain_HCD 544.1309814 543.630615 543.638137 30 16271.12715 -13.83597859 EDF1_MOUSE Endothelial differentiation-related factor 1; Short=EDF-1;AltName: Full=Multiprotein-bridging factor 1; Short=MBF1 Q9JMG1 AESDWDTVTVLRKKGPTAAQAKSKQAILAAQRRGEDVETSKKWAAGQNKQHSITKNTAKLDRETEELHHDRVTLEVGKVIQRGRQSKGLTQKDLATKINEKPQVIADYESGRAIPNNQVLGKIERAIGLKLRGKDIGKPIEKGPKAK 147 "FUNCTION: Transcriptional coactivator stimulating NR5A1 and ligand-dependent NR1H3/LXRA and PPARG transcriptional activities. Enhances the DNA-binding activity of ATF1, ATF2, CREB1 and NR5A1. Regulates nitric oxid synthase activity probably by sequestering calmodulin in the cytoplasm. Might function in endothelial cells differentiation, hormone-induced cardiomyocytes hypertrophy and lipid metabolism (By similarity). {ECO:0000250}." A1Ac 1367.38 "A,89;" 125 100 uniprot_mouse_length brain_HCD 705.7966919 704.143372 704.150511 18 12650.69804 -10.13905104 EIF1_MOUSE Eukaryotic translation initiation factor 1; Short=eIF1;AltName: Full=Protein translation factor SUI1 homolog P48024 SAIQNLHSFDPFADASKGDDLLPAGTEDYIHIRIQQRNGRKTLTTVQGIADDYDKKKLVKAFKKKFACNGTVIEHPEYGEVIQLQGDQRKNICQFLIEIGLAKDDQLKVHGF 112 FUNCTION: Necessary for scanning and involved in initiation site selection. Promotes the assembly of 48S ribosomal complexes at the authentic initiation codon of a conventional capped mRNA (By similarity). {ECO:0000250}. S1Ac 1569.86 "S,63;" 93 100 uniprot_mouse_length brain_HCD 1104.149414 1104.731689 1104.734253 12 13238.80022 -2.320509994 ENSA_MOUSE Alpha-endosulfine;AltName: Full=ARPP-19e P60840 SQKQEEENPAEETGEEKQDTQEKEGILPEKAEEAKLKAKYPSLGQKPGGSDFLMKRLQKGQKYFDSGDYNMAKAKMKNKQLPSAGADKNLVTGDHIPTPQDLPQRKSSLVTSKLAGGQVE 120 "FUNCTION: Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-67 during mitosis, specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, an essential condition to keep cyclin-B1-CDK1 activity high during M phase. Also acts as a stimulator of insulin secretion by interacting with sulfonylurea receptor (ABCC8), thereby preventing sulfonylurea from binding to its receptor and reducing K(ATP) channel currents (By similarity). {ECO:0000250}." S1Ac 1122.67 "S,38;" 60 100 uniprot_mouse_length brain_HCD 575.8942261 580.487427 580.483522 21 12163.14413 6.726733257 ERH_MOUSE Enhancer of rudimentary homolog; Short=Mer P84089 SHTILLVQPTKRPEGRTYADYESVNECMEGVCKMYEEHLKRMNPNSPSITYDISQLFDFIDDLADLSCLVYRADTQTYQPYNKDWIKEKIYVLLRRQAQQAGK 103 FUNCTION: May have a role in the cell cycle. S1Ac 325.09 "S,28;" 49 100 uniprot_mouse_length brain_HCD 658.9058838 654.750549 654.756111 28 18295.15166 -8.494282833 F163B_MOUSE Protein FAM163B Q8BUM6 MTAGTVVITGGILATVILLCIIAVLCYCRLQYYCCKKDESEEDEEEPDFAVHSHLPPLHSNRNLVLTNGPALYPAATTSFSQKSPQARALCRSCSHYEPPTFFLQEPEDEDFEGVRNGGGRVAYKSISQEDVELPSASFGGLQALNPNRLSAMREAFSRSRSVSTDV 167 SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. null 4371.53 null null 100 uniprot_mouse_length brain_HCD 946.5032349 949.497437 949.49317 17 16116.36779 4.493474595 F183B_MOUSE Protein FAM183B Q5NC57 MAGRVGQMKNQDEVHQNQILRELFLKELRAQKLYTQYHVNPLRKVHTITRKPMSWHDNLEEPEDAKFLNLIHHAAQGPKKKYSETQTEAQEIGWDPNPLINPDRQDHRLNHFRVYHDITLYKAKLWSLGEDDHQK 135 ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q5NC57-1; Sequence=Displayed; Name=2; IsoId=Q5NC57-2; Sequence=VSP_034207; Note=No experimental confirmation available.; null 805.32 null null 100 uniprot_mouse_length brain_HCD 627.3538208 624.495667 624.486763 18 11217.75352 14.25731406 F195B_MOUSE Protein FAM195B Q3UGS4 MTSSPVSRVVYNGKRNSSPRSPTNSSEIFTPAHEENVRFIYEAWQGVERDLRSQLSSGERCLVEEYVEKVPNPSLKTFKPIDLSDLKRRNTQDAKKS 97 SIMILARITY: Belongs to the FAM195 family. {ECO:0000305}. S21PK79Ac 774.47 "S,4;K,58;" 74 100 uniprot_mouse_length brain_HCD 666.4799805 662.38739 662.384595 17 11237.53095 4.219809367 F19A2_MOUSE Protein FAM19A2;AltName: Full=Chemokine-like protein TAFA-2;Flags: Precursor Q7TPG7 ANHHKAHHVRTGTCEVVALHRCCNKNKIEERSQTVKCSCFPGQVAGTTRAAPSCVDASIVEQKWWCHMQPCLEGEECKVLPDRKGWSCSSGNKVKTTRVTH 101 SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. null 505.62 null null 100 uniprot_mouse_length brain_HCD 673.015625 668.583374 668.582962 22 14679.81104 0.616263741 FABPH_MOUSE "Fatty acid-binding protein, heart;AltName: Full=Fatty acid-binding protein 3;AltName: Full=Heart-type fatty acid-binding protein; Short=H-FABP;AltName: Full=Mammary-derived growth inhibitor; Short=MDGI" P11404 ADAFVGTWKLVDSKNFDDYMKSLGVGFATRQVASMTKPTTIIEKNGDTITIKTQSTFKNTEINFQLGIEFDEVTADDRKVKSLVTLDGGKLIHVQKWNGQETTLTRELVDGKLILTLTHGSVVSTRTYEKEA 132 FUNCTION: FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. null 2137.4 null null 100 uniprot_mouse_length brain_HCD 589.0108032 593.350342 593.353022 25 14801.8114 -4.517046388 FABPH_MOUSE "Fatty acid-binding protein, heart;AltName: Full=Fatty acid-binding protein 3;AltName: Full=Heart-type fatty acid-binding protein; Short=H-FABP;AltName: Full=Mammary-derived growth inhibitor; Short=MDGI" P11404 ADAFVGTWKLVDSKNFDDYMKSLGVGFATRQVASMTKPTTIIEKNGDTITIKTQSTFKNTEINFQLGIEFDEVTADDRKVKSLVTLDGGKLIHVQKWNGQETTLTRELVDGKLILTLTHGSVVSTRTYEKEA 132 FUNCTION: FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. A1AcY19P 2294.74 "A,103;Y,126;" 139 100 uniprot_mouse_length brain_HCD 798.2349243 801.490906 801.479534 18 14401.61878 14.18846176 FABPL_MOUSE "Fatty acid-binding protein, liver;AltName: Full=14 kDa selenium-binding protein;AltName: Full=Fatty acid-binding protein 1;AltName: Full=Liver-type fatty acid-binding protein; Short=L-FABP" P12710 MNFSGKYQLQSQENFEPFMKAIGLPEDLIQKGKDIKGVSEIVHEGKKIKLTITYGPKVVRNEFTLGEECELETMTGEKVKAVVKLEGDNKMVTTFKGIKSVTELNGDTITNTMTLGDIVYKRVSKRI 127 "FUNCTION: Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport. Also seems to bind selenium." M1AcS11PK84Ac 915.97 "M,22;S,10;K,48;" 85 100 uniprot_mouse_length brain_HCD 658.0570679 654.341431 654.347377 31 20242.74649 -9.087429929 FACOS_MOUSE FANCD2 opposite strand protein;AltName: Full=Fanconi anemia group D2 protein opposite strand transcript protein Q9D4K4 MAGYQLWSPWTPLDESFQWLRHTTPTPSSKHPFRASPCFPHTPSDLEVQLCLQEVTLVLDRPLVEPGESPKLPCHKSELRAVSNKKGVVRKPQPVRLSGVDSVFGRVITAQPPKWTGTFRVSDKSAFCKIISREHQWPTGLKEPQVQMTVTMCKQMLRSILLLYATYKKCTFALQHSK 178 "-------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License--------------------------------------------------" null 2209.75 null null 100 uniprot_mouse_length brain_HCD 633.7541504 632.803955 632.805981 25 15787.13352 -3.201489771 FGF1_MOUSE Fibroblast growth factor 1; Short=FGF-1;AltName: Full=Acidic fibroblast growth factor; Short=aFGF;AltName: Full=Heparin-binding growth factor 1; Short=HBGF-1;Flags: Precursor P61148 FNLPLGNYKKPKLLYCSNGGHFLRILPDGTVDGTRDRSDQHIQLQLSAESAGEVYIKGTETGQYLAMDTEGLLYGSQTPNEECLFLERLEENHYNTYTSKKHAEKNWFVGLKKNGSCKRGPRTHYGQKAILFLPLPVSSD 140 "FUNCTION: Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as potent mitogen in vitro (By similarity). {ECO:0000250}." null 2632.7 null null 100 uniprot_mouse_length brain_HCD 614.1868286 613.52179 613.514475 27 16529.87511 11.92237686 FGF22_MOUSE Fibroblast growth factor 22; Short=FGF-22;Flags: Precursor Q9ESS2 GYPHLEGDVRWRRLFSSTHFFLRVDLGGRVQGTRWRHGQDSIVEIRSVRVGTVVIKAVYSGFYVAMNRRGRLYGSRVYSVDCRFRERIEENGYNTYASRRWRHRGRPMFLALDSQGIPRQGRRTRRHQLSTHFLPVLVSS 140 "FUNCTION: Plays a role in the fasting response, glucose homeostasis, lipolysis and lipogenesis. Can stimulate cell proliferation (in vitro). May be involved in hair development." null 1234.31 null null 100 uniprot_mouse_length brain_HCD 544.1309814 539.877014 539.878755 33 17772.98002 -3.224501478 GA45B_MOUSE Growth arrest and DNA damage-inducible protein GADD45 beta;AltName: Full=Myeloid differentiation primary response protein MyD118;AltName: Full=Negative growth regulatory protein MyD118 P22339 MTLEELVASDNAVQKMQAVTAAVEQLLVAAQRQDRLTVGVYEAAKLMNVDPDSVVLCLLAIDEEEEDDIALQIHFTLIQSFCCDNDIDIVRVSGMQRLAQLLGEPAETLGTTEARDLHCLLVTNCHTDSWKSQGLVEVASYCEESRGNNQWVPYISLEER 160 FUNCTION: Involved in the regulation of growth and apoptosis. Mediates activation of stress-responsive MTK1/MEKK4 MAPKKK (By similarity). {ECO:0000250}. null 1553.65 null null 100 uniprot_mouse_length brain_HCD 575.8942261 580.487427 580.491574 20 11583.82188 -7.144362422 GAST_MOUSE Gastrin;Contains: Gastrin-71; Short=G71;Contains: Big gastrin; AltName: Full=Gastrin-34; Short=G34;Contains: Gastrin;Flags: Precursor P48757 MPRLCVYMLVLVLALATFSEASWKPRSQLQDASSGPGTNEDLEQRQFNKLGSASHHRRQLGPQGPQHFIADLSKKQRPRMEEEEEAYGWMDFGRRSAEEDQ 101 FUNCTION: Gastrin stimulates the stomach mucosa to produce and secrete hydrochloric acid and the pancreas to secrete its digestive enzymes. It also stimulates smooth muscle contraction and increases blood circulation and water secretion in the stomach and intestine. null 289.46 null null 100 uniprot_mouse_length brain_HCD 756.1401978 753.593689 753.591049 10 7522.90838 3.503179672 GBG12_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12;Flags: Precursor Q9DAS9 SSKTASTNSIAQARRTVQQLRLEASIERIKVSKASADLMSYCEEHARSDPLLMGIPTSENPFKDKKTC 68 "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction." null 147.78 null null 100 uniprot_mouse_length brain_HCD 946.5032349 948.754211 948.740138 8 7578.91896 14.83380456 GBG12_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12;Flags: Precursor Q9DAS9 SSKTASTNSIAQARRTVQQLRLEASIERIKVSKASADLMSYCEEHARSDPLLMGIPTSENPFKDKKTC 68 "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction." S1AcC68Me 150.87 "S,9;C,18;" 24 100 uniprot_mouse_length brain_HCD 544.1309814 544.284912 544.27915 14 7602.906 10.58668034 GBG12_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12;Flags: Precursor Q9DAS9 SSKTASTNSIAQARRTVQQLRLEASIERIKVSKASADLMSYCEEHARSDPLLMGIPTSENPFKDKKTC 68 "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction." S25P 313.18 "S,9;" 38 100 uniprot_mouse_length brain_HCD 572.9716187 572.138123 572.141585 12 6850.69679 -6.051721282 GBG5_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-5;Flags: Precursor Q80SZ7 SGSSSVAAMKKVVQQLRLEAGLNRVKVSQAAADLKQFCLQNAQHDPLLTGVSSSTNPFRPQKVC 64 "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction." C64Me 828.46 "C,26;" 45 100 uniprot_mouse_length brain_HCD 542.1262207 537.785217 537.783113 14 7511.96158 3.912888124 GBG8_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-8;AltName: Full=Gamma-9;Flags: Precursor P63078 MSNNMAKIAEARKTVEQLKLEVNIDRMKVSQAAAELLAFCETHAKDDPLVTPVPAAENPFRDKRLFC 67 "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction. This subunit may have a very specific role in the development and turnover of olfactory and vomeronasal neurons." null 513.71 null null 100 uniprot_mouse_length brain_HCD 634.6201782 632.722351 632.725708 29 18310.02636 -5.305499269 GKN1_MOUSE Gastrokine-1;AltName: Full=18 kDa antrum mucosa protein; Short=AMP-18;AltName: Full=Protein CA11 homolog;Flags: Precursor Q9CR36 FAYTVNINGNDGNVDGSGQQSVSINGVHNVANIDNNNGWDSWNSLWDYENSFAATRLFSKKSCIVHRMNKDAMPSLQDLDTMVKEQKGKGPGGAPPKDLMYSVNPTRVEDLNTFGPKIAGMCRGIPTYVAEEIPGPNQPLYSKKCYTADILWILRMSFCGTSVETY 166 FUNCTION: Has mitogenic activity and may be involved in maintaining the integrity of the gastric mucosal epithelium. {ECO:0000269|PubMed:12851218}. null 2475.48 null null 100 uniprot_mouse_length brain_HCD 790.9173584 795.502991 795.494962 13 10323.42656 10.09273853 GLPC_MOUSE Glycophorin-C;AltName: CD_antigen=CD236 Q78HU7 MSSPVSKPPPELLEPNPGKSYGIMEIAIIAAVITAVALVLVCLLFLMLRYLYRHKGTYHTNEAKGTEFAESADAALQSDPALQDAGDTSKKEYFI 95 SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Note=Linked to the membrane via band 4.1. {ECO:0000250}. null 466.55 null null 100 uniprot_mouse_length brain_HCD 954.2340698 954.499878 954.486502 11 10483.34359 14.01374421 GLPC_MOUSE Glycophorin-C;AltName: CD_antigen=CD236 Q78HU7 MSSPVSKPPPELLEPNPGKSYGIMEIAIIAAVITAVALVLVCLLFLMLRYLYRHKGTYHTNEAKGTEFAESADAALQSDPALQDAGDTSKKEYFI 95 SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Note=Linked to the membrane via band 4.1. {ECO:0000250}. S71PS89P 161 "S,1;S,0;" 27 100 uniprot_mouse_length brain_HCD 634.3200073 633.225403 633.216589 29 18324.2613 13.91914265 GOG7B_MOUSE Golgin subfamily A member 7B Q9D428 MATEVHNLQELRRSASLATKVFIQRDYSDGTICQFQTKFPPELDSRIERQLFEETVKTLNGFYAEAEKIGGSSYLEGCLACATAYFIFLCMETHYEKVLKKISRYIQEQNEKVFAPRGLLLTDPVERGMRVIEISIYEDRCSSGSSSSGSSSGSGSSSAGGGGAGAR 167 FUNCTION: May be involved in protein transport from Golgi to cell surface. {ECO:0000250}. null 1300.59 null null 100 uniprot_mouse_length brain_HCD 683.7625122 679.763245 679.75734 12 8142.08578 8.686377563 GON1_MOUSE Progonadoliberin-1;AltName: Full=Progonadoliberin I;Contains: Gonadoliberin-1; AltName: Full=Gonadoliberin I; AltName: Full=Gonadotropin-releasing hormone I; Short=GnRH-I; AltName: Full=Luliberin I; AltName: Full=Luteinizing hormone-releasing hormone I; Short=LH-RH I;Contains: Prolactin release-inhibiting factor 1; AltName: Full=Prolactin release-inhibiting factor I;Flags: Precursor P13562 QHWSYGLRPGGKRNTEHLVESFQEMGKEVDQMAEPQHFECTVHWPRSPLRDLRGALESLIEEEARQKKM 69 FUNCTION: Stimulates the secretion of gonadotropins; it stimulates the secretion of both luteinizing and follicle-stimulating hormones. null 1636.04 null null 100 uniprot_mouse_length brain_HCD 634.3200073 629.94104 629.938173 19 11943.81768 4.551302311 GPHA2_MOUSE Glycoprotein hormone alpha-2;AltName: Full=Putative secreted protein Zsig51;AltName: Full=Thyrostimulin subunit alpha;Flags: Precursor Q925Q5 HSPETAIPGCHLHPFNVTVRSDRLGTCQGSHVAQACVGHCESSAFPSRYSVLVASGYRHNITSSSQCCTISSLRKVRVWLQCVGNQRGELEIFTARACQCDMCRFSRY 108 "FUNCTION: Stimulates the thyroid. Binds and activates THSR, leads to increased cAMP production (By similarity). {ECO:0000250}." null 407.28 null null 100 uniprot_mouse_length brain_HCD 679.0958252 679.367126 679.370312 11 7459.07172 -4.688952549 GROA_MOUSE Growth-regulated alpha protein;AltName: Full=C-X-C motif chemokine 1;AltName: Full=Platelet-derived growth factor-inducible protein KC;AltName: Full=Secretory protein N51;Contains: KC(5-72); AltName: Full=Hematopoietic synergistic factor; Short=HSF; AltName: Full=KC-T;Flags: Precursor P12850 NELRCQCLQTMAGIHLKNIQSLKVLPSGPHCTQTEVIATLKNGREACLDPEAPLVQKIVQKMLKGVPK 68 "FUNCTION: Has chemotactic activity for neutrophils. Contributes to neutrophil activation during inflammation (By similarity). Hematoregulatory chemokine, which, in vitro, suppresses hematopoietic progenitor cell proliferation. KC(5-72) shows a highly enhanced hematopoietic activity. {ECO:0000250, ECO:0000269|PubMed:10725737}." null 522.95 null null 100 uniprot_mouse_length brain_HCD 732.2000122 727.697754 727.691559 16 11621.05604 8.513093458 GUC2B_MOUSE Guanylate cyclase activator 2B;Contains: Uroguanylin; Short=UGN;Flags: Precursor O09051 MSRSQLWAAVVLLLLLQSAQGVYIKYHGFQVQLESVKKLNELEEKEMSNPQPRRSGLLPAVCHNPALPLDLQPVCASQEAASTFKALRTIATDECELCINVACTGC 106 FUNCTION: Endogenous activator of intestinal guanylate cyclase. It stimulates this enzyme through the same receptor binding region as the heat-stable enterotoxins. May be a potent physiological regulator of intestinal fluid and electrolyte transport. May be an autocrine/paracrine regulator of intestinal salt and water transport (By similarity). {ECO:0000250}. null 560.65 null null 100 uniprot_mouse_length brain_HCD 627.0343628 622.615173 622.617064 34 21123.95465 -3.036634017 H12_MOUSE Histone H1.2;AltName: Full=H1 VAR.1;AltName: Full=H1c P15864 SEAAPAAPAAAPPAEKAPAKKKAAKKPAGVRRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGILVQTKGTGASGSFKLNKKAASGEAKPQAKKAGAAKAKKPAGAAKKPKKATGAATPKKAAKKTPKKAKKPAAAAVTKKVAKSPKKAKVTKPKKVKSASKAVKPKAAKPKVAKAKKVAAKKK 211 "FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250}." null 2899.5 null null 100 uniprot_mouse_length brain_HCD 526.9035034 529.731506 529.726069 40 21138.01722 10.26445171 H12_MOUSE Histone H1.2;AltName: Full=H1 VAR.1;AltName: Full=H1c P15864 SEAAPAAPAAAPPAEKAPAKKKAAKKPAGVRRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGILVQTKGTGASGSFKLNKKAASGEAKPQAKKAGAAKAKKPAGAAKKPKKATGAATPKKAAKKTPKKAKKPAAAAVTKKVAKSPKKAKVTKPKKVKSASKAVKPKAAKPKVAKAKKVAAKKK 211 "FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250}." K25Me 1224.38 "K,0;" 168 100 uniprot_mouse_length brain_HCD 685.5714722 688.785767 688.788946 32 21998.22081 -4.615925467 H14_MOUSE Histone H1.4;AltName: Full=H1 VAR.2;AltName: Full=H1e P43274 SETAPAAPAAPAPAEKTPVKKKARKAAGGAKRKTSGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEAKPKAKRAGAAKAKKPAGAAKKPKKAAGTATAKKSTKKTPKKAKKPAAAAGAKKAKSPKKAKATKAKKAPKSPAKAKTVKPKAAKPKTSKPKAAKPKKTAAKKK 218 "FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation. {ECO:0000269|PubMed:12808097, ECO:0000269|PubMed:16377562}." S1AcK16AcT17P 2665.27 "S,2;K,0;T,0;" 217 100 uniprot_mouse_length brain_HCD 526.9035034 525.679688 525.672229 27 14159.13606 14.1884992 H2A1F_MOUSE Histone H2A type 1-F Q8CGP5 SGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKPKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1AcQ104MeT120P 488.3 "S,1;Q,51;T,0;" 78 100 uniprot_mouse_length brain_HCD 658.0570679 659.054932 659.046601 21 13811.96453 12.64044244 H2A1H_MOUSE Histone H2A type 1-H Q8CGP6 SGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAK 127 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." null 918.8 null null 100 uniprot_mouse_length brain_HCD 581.7600098 581.296021 581.291655 24 13919.98561 7.510012874 H2A1H_MOUSE Histone H2A type 1-H Q8CGP6 SGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAK 127 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1PR3dMe 1939.68 "S,88;R,100;" 129 100 uniprot_mouse_length brain_HCD 542.1262207 540.165344 540.159608 26 14011.13569 10.61952467 H2A1K_MOUSE Histone H2A type 1-K Q8CGP7 SGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTETHHKAKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." null 962.54 null null 100 uniprot_mouse_length brain_HCD 676.8241577 674.347656 674.339238 21 14133.10988 12.48370186 H2A1K_MOUSE Histone H2A type 1-K Q8CGP7 SGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTETHHKAKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1PR3dMeQ104Me 1361.64 "S,59;R,68;Q,88;" 108 100 uniprot_mouse_length brain_HCD 525.3856812 525.751465 525.746883 27 14161.15172 8.71492328 H2A1K_MOUSE Histone H2A type 1-K Q8CGP7 SGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTETHHKAKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1AcR3dMeT120P 2194 "S,0;R,133;T,124;" 152 100 uniprot_mouse_length brain_HCD 744.5848999 741.515381 741.520697 19 14062.87949 -7.169241056 H2A2B_MOUSE Histone H2A type 2-B;AltName: Full=H2a-613A Q64522 SGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYMAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEELNKLLGGVTIAQGGVLPNIQAVLLPKKTESHKPGKNK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1PR3dMeT120P 151.54 "S,7;R,7;T,0;" 14 100 uniprot_mouse_length brain_HCD 542.1262207 540.165344 540.159608 26 14011.13569 10.61952467 H2A3_MOUSE Histone H2A type 3 Q8BFU2 SGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." R3dMe 995.15 "R,67;" 110 100 uniprot_mouse_length brain_HCD 621.0681763 616.890747 616.896676 22 13543.7157 -9.610895824 H2AV_MOUSE Histone H2A.V;AltName: Full=H2A.F/Z Q3THW5 MAGGKAGKDSGKAKAKAVSRSQRAGLQFPVGRIHRHLKTRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGKKGQQKTA 128 "FUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. May be involved in the formation of constitutive heterochromatin. May be required for chromosome segregation during cell division (By similarity). {ECO:0000250}." K5Ac 1049.88 "K,1;" 89 100 uniprot_mouse_length brain_HCD 802.9099731 802.976929 802.982879 17 13627.69774 -7.410231548 H2AV_MOUSE Histone H2A.V;AltName: Full=H2A.F/Z Q3THW5 MAGGKAGKDSGKAKAKAVSRSQRAGLQFPVGRIHRHLKTRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGKKGQQKTA 128 "FUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. May be involved in the formation of constitutive heterochromatin. May be required for chromosome segregation during cell division (By similarity). {ECO:0000250}." K5AcK8AcK12Ac 316.33 "K,0;K,0;K,1;" 54 100 uniprot_mouse_length brain_HCD 627.8303833 630.302368 630.308557 22 13837.77459 -9.818740153 H2B1C_MOUSE Histone H2B type 1-C/E/G Q6ZWY9 PEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." K46MeK57dMeR79dMe 669.28 "K,18;K,8;R,10;" 86 100 uniprot_mouse_length brain_HCD 697.6692505 695.830994 695.833561 20 13889.65758 -3.689600215 H2B1C_MOUSE Histone H2B type 1-C/E/G Q6ZWY9 PEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." P1AcS14P 2384.73 "P,1;S,9;" 70 100 uniprot_mouse_length brain_HCD 697.6692505 695.830994 695.835381 20 13889.69396 -6.30515173 H2B1C_MOUSE Histone H2B type 1-C/E/G Q6ZWY9 PEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S14PK46MeK57dMe 2342.56 "S,10;K,40;K,25;" 71 100 uniprot_mouse_length brain_HCD 773.3856201 775.931152 775.923722 18 13941.61337 9.576126544 H2B1C_MOUSE Histone H2B type 1-C/E/G Q6ZWY9 PEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S14PS36PK46Me 513.45 "S,1;S,0;K,17;" 69 100 uniprot_mouse_length brain_HCD 735.46875 736.607544 736.612091 19 13969.61609 -6.172929746 H2B1C_MOUSE Histone H2B type 1-C/E/G Q6ZWY9 PEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." P1AcS14PS36P 175.27 "P,0;S,1;S,0;" 18 100 uniprot_mouse_length brain_HCD 633.1381226 632.760315 632.759205 22 13891.68887 1.754129213 H2B1F_MOUSE Histone H2B type 1-F/J/L;AltName: Full=H2B 291A P10853 PEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S14PK46Me 854.51 "S,7;K,20;" 86 100 uniprot_mouse_length brain_HCD 627.8303833 630.302368 630.308557 22 13837.77459 -9.818740153 H2B1H_MOUSE Histone H2B type 1-H;AltName: Full=h2B-221 Q64478 PEPAKSAPAPKKGSKKALTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." K46MeK57dMeR86Me 589.05 "K,11;K,7;R,0;" 77 100 uniprot_mouse_length brain_HCD 697.6692505 695.830994 695.835381 20 13889.69396 -6.30515173 H2B1H_MOUSE Histone H2B type 1-H;AltName: Full=h2B-221 Q64478 PEPAKSAPAPKKGSKKALTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S14PK46MeR86Me 2105.22 "S,9;K,36;R,0;" 143 100 uniprot_mouse_length brain_HCD 773.3856201 775.931152 775.923722 18 13941.61337 9.576126544 H2B1H_MOUSE Histone H2B type 1-H;AltName: Full=h2B-221 Q64478 PEPAKSAPAPKKGSKKALTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S14PS36P 449.89 "S,2;S,0;" 66 100 uniprot_mouse_length brain_HCD 627.8303833 630.302368 630.308557 22 13837.77459 -9.818740153 H2B1K_MOUSE Histone H2B type 1-K Q8CGP1 PEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." K46MeK57dMeR86Me 658.75 "K,23;K,11;R,0;" 82 100 uniprot_mouse_length brain_HCD 697.6692505 695.830994 695.835381 20 13889.69396 -6.30515173 H2B1K_MOUSE Histone H2B type 1-K Q8CGP1 PEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S14PK46MeR86Me 2293.47 "S,10;K,40;R,0;" 148 100 uniprot_mouse_length brain_HCD 773.3856201 775.931152 775.923722 18 13941.61337 9.576126544 H2B1K_MOUSE Histone H2B type 1-K Q8CGP1 PEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S14PS36P 481.55 "S,1;S,0;" 60 100 uniprot_mouse_length brain_HCD 697.6692505 695.830994 695.835381 20 13889.69396 -6.30515173 H2B2B_MOUSE Histone H2B type 2-B;AltName: Full=H2b 616 Q64525 PDPAKSAPAPKKGSKKAVTKVQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S14PK46MeR86Me 2206.1 "S,10;K,36;R,0;" 145 100 uniprot_mouse_length brain_HCD 773.3856201 775.931152 775.923722 18 13941.61337 9.576126544 H2B2B_MOUSE Histone H2B type 2-B;AltName: Full=H2b 616 Q64525 PDPAKSAPAPKKGSKKAVTKVQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S14PS36P 431.02 "S,1;S,0;" 63 100 uniprot_mouse_length brain_HCD 998.2073975 994.186951 994.191803 14 13897.67161 -4.880664266 H2B3A_MOUSE Histone H2B type 3-A Q9D2U9 PEPSRSTPAPKKGSKKAITKAQKKDGKKRKRGRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREVQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." P1Ac 911.57 "P,0;" 81 100 uniprot_mouse_length brain_HCD 610.8279419 607.521851 607.52689 19 11518.00175 -8.294964627 IFM1_MOUSE Interferon-induced transmembrane protein 1;AltName: Full=Dispanin subfamily A member 2a; Short=DSPA2a;AltName: Full=Fragilis protein 2;AltName: Full=Mouse ifitm-like protein 2; Short=Mil-2 Q9D103 MPKEQQEVVVLGSPHISTSATATTINMPEISTPDHVVWSLFNTLFMNFCCLGFVAYAYSVKSRDRKMVGDTTGAQAFASTAKCLNISSLFFTILTAIVVIVVCAIR 106 "FUNCTION: IFN-induced antiviral protein which inhibits the entry of viruses to the host cell cytoplasm, permitting endocytosis, but preventing subsequent viral fusion and release of viral contents into the cytosol. Active against multiple viruses, including influenza A virus, SARS coronavirus (SARS-CoV), Marburg virus (MARV), Ebola virus (EBOV), Dengue virus (DNV) and West Nile virus (WNV). Can inhibit: influenza virus hemagglutinin protein-mediated viral entry, MARV and EBOV GP1,2-mediated viral entry and SARS-CoV S protein-mediated viral entry. Also implicated in cell adhesion and control of cell growth and migration. Plays a key role in the antiproliferative action of IFN-gamma either by inhibiting the ERK activation or by arresting cell growth in G1 phase in a p53- dependent manner. Acts as a positive regulator of osteoblast differentiation. {ECO:0000269|PubMed:18505827, ECO:0000269|PubMed:21253575}." null 911.96 null null 100 uniprot_mouse_length brain_HCD 658.0557861 655.420166 655.427464 22 14390.39162 -11.13469419 ADXL_MOUSE "Adrenodoxin-like protein, mitochondrial;AltName: Full=Ferredoxin-1-like protein;Flags: Precursor" Q9CPW2 AGEEAADSPELPRDVVNVVFVDRSGKRIPVRGKVGDNVLYLAQRHGVDLEGACEASLACSTCHVYVSEAHLDLLPPPEEREDDMLDMAPLLQENSRLGCQIVLTPELEGVEFALPKITRNFYVDGHIPKPH 131 FUNCTION: Essential for heme A and Fe/S protein biosynthesis. {ECO:0000250}. null 4633.12 null null 100 uniprot_mouse_length brain_HCD 683.9489746 682.027588 682.032812 13 8849.42149 -7.659615906 APOA2_MOUSE Apolipoprotein A-II; Short=Apo-AII; Short=ApoA-II;AltName: Full=Apolipoprotein A2;Contains: Proapolipoprotein A-II; Short=ProapoA-II;Flags: Precursor P09813 QADGPDMQSLFTQYFQSMTDYGKDLMEKAKTSEIQSQAKAYFEKTHEQLTPLVRSAGTSLVNFFSSLMNLEEKPAPAAK 79 "FUNCTION: May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism." null 1525.07 null null 100 uniprot_mouse_length brain_HCD 859.6881714 856.57251 856.570212 25 21377.23085 2.682518716 ARL8A_MOUSE ADP-ribosylation factor-like protein 8A;AltName: Full=ADP-ribosylation factor-like protein 10B;AltName: Full=Novel small G protein indispensable for equal chromosome segregation 2 Q8VEH3 MIALFNKLLDWFKALFWKEEMELTLVGLQYSGKTTFVNVIASGQFNEDMIPTVGFNMRKITKGNVTIKLWDIGGQPRFRSMWERYCRGVSAIVYMVDAADQEKIEASKNELHNLLDKPQLQGIPVLVLGNKRDLAGALDEKELIEKMNLSAIQDREICCYSISCKEKDNIDITLQWLIQHSKSRRS 186 "FUNCTION: May play a role in lysosomes motility. Alternatively, may play a role in chromosome segregation (By similarity). {ECO:0000250}." null 3281.31 null null 100 uniprot_mouse_length brain_HCD 656.1260986 651.700806 651.70333 19 12357.35264 -3.873443362 ARP19_MOUSE cAMP-regulated phosphoprotein 19; Short=ARPP-19 P56212 SAEVPEAASAEEQKEMEDKVTSPEKAEEAKLKARYPHLGQKPGGSDFLRKRLQKGQKYFDSGDYNMAKAKMKNKQLPAAAPDKTEVTGDHIPTPQDLPQRKPSLVASKLAG 111 "FUNCTION: Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-62 during mitosis, specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, an essential condition to keep cyclin-B1-CDK1 activity high during M phase. May indirectly enhance GAP-43 expression by binding to the NGF-regulatory region of its mRNA (By similarity). {ECO:0000250}." S1AcS61PS103P 3753.62 "S,132;S,69;S,43;" 150 100 uniprot_mouse_length brain_HCD 788.4238892 790.736206 790.735335 15 11840.0228 1.10157552 ASIP_MOUSE Agouti-signaling protein; Short=ASP;AltName: Full=Agouti coat color protein;AltName: Full=Agouti switch protein;Flags: Precursor Q03288 HLALEETLGDDRSLRSNSSMNSLDFSSVSIVALNKKSKKISRKEAEKRKRSSKKKASMKKVARPPPPSPCVATRDSCKPPAPACCDPCASCQCRFFGSACTCRVLNPNC 109 "FUNCTION: Involved in the regulation of melanogenesis. The binding of ASP to MC1R precludes alpha-MSH initiated signaling and thus blocks production of cAMP, leading to a down-regulation of eumelanogenesis (brown/black pigment) and thus increasing synthesis of pheomelanin (yellow/red pigment). Causes hair follicle melanocytes to synthesize phaeomelanin instead of black or brown pigment eumelanin and produces hairs with a subapical yellow band on an otherwise black or brown background when expressed during the mid-portion of hair growth." null 407.52 null null 100 uniprot_mouse_length brain_HCD 656.1260986 652.069031 652.062489 34 22124.09926 10.03241534 BAD_MOUSE Bcl2-associated agonist of cell death; Short=BAD;AltName: Full=Bcl-2-binding component 6;AltName: Full=Bcl-xL/Bcl-2-associated death promoter;AltName: Full=Bcl2 antagonist of cell death Q61337 MGTPKQPSLAPAHALGLRKSDPGIRSLGSDAGGRRWRPAAQSMFQIPEFEPSEQEDASATDRGLGPSLTEDQPGPYLAPGLLGSNIHQQGRAATNSHHGGAGAMETRSRHSSYPAGTEEDEGMEEELSPFRGRSRSAPPNLWAAQRYGRELRRMSDEFEGSFKGLPRPKSAGTATQMRQSAGWTRIIQSWWDRNLGKGGSTPSQ 204 "FUNCTION: Promotes cell death. Successfully competes for the binding to Bcl-X(L), Bcl-2 and Bcl-W, thereby affecting the level of heterodimerization of these proteins with BAX. Can reverse the death repressor activity of Bcl-X(L), but not that of Bcl-2. Appears to act as a link between growth factor receptor signaling and the apoptotic pathways." R131dMeR133dMe 9438.24 "R,8;R,1;" 343 100 uniprot_mouse_length brain_HCD 541.0147095 538.419495 538.423482 19 10206.03896 -7.405641149 BAF_MOUSE "Barrier-to-autointegration factor;AltName: Full=Breakpoint cluster region protein 1;AltName: Full=LAP2-binding protein 1;Contains: Barrier-to-autointegration factor, N-terminally processed" O54962 TTSQKHRDFVAEPMGEKPVGSLAGIGDVLSKRLEERGFDKAYVVLGQFLVLKKDEDLFREWLKDTCGANAKQSRDCFGCLREWCDAFL 88 "FUNCTION: Plays fundamental roles in nuclear assembly, chromatin organization, gene expression and gonad development. May potently compress chromatin structure and be involved in membrane recruitment and chromatin decondensation during nuclear assembly. Contains 2 non-specific dsDNA-binding sites which may promote DNA cross-bridging (By similarity). {ECO:0000250}." T1PT2PS3P 1962.29 "T,0;T,0;S,1;" 108 100 uniprot_mouse_length brain_HCD 614.2867432 611.452393 611.459029 39 23794.87151 -10.85342036 C1QBP_MOUSE "Complement component 1 Q subcomponent-binding protein, mitochondrial;AltName: Full=GC1q-R protein;AltName: Full=Glycoprotein gC1qBP; Short=C1qBP;Flags: Precursor" O35658 LHTEGDKAFVEFLTDEIKEEKKIQKHKSLPKMSGDWELEVNGTEAKLLRKVAGEKITVTFNINNSIPPTFDGEEEPSQGQKAEEQEPERTSTPNFVVEVTKTDGKKTLVLDCHYPEDEIGHEDEAESDIFSIKEVSFQATGDSEWRDTNYTLNTDSLDWALYDHLMDFLADRGVDNTFADELVELSTALEHQEYITFLEDLKSFVKNQ 208 "FUNCTION: Is believed to be a multifunctional and multicompartmental protein involved in inflammation and infection processes, ribosome biogenesis, regulation of apoptosis, transcriptional regulation and pre-mRNA splicing. At the cell surface is thought to act as an endothelial receptor for plasma proteins of the complement and kallikrein-kinin cascades. Putative receptor for C1q; specifically binds to the globular ""heads"" of C1q thus inhibiting C1; may perform the receptor function through a complex with C1qR/CD93. In complex with cytokeratin-1/KRT1 is a high affinity receptor for kininogen-1/HMWK. Can also bind other plasma proteins, such as coagulation factor XII leading to its autoactivation. May function to bind initially fluid kininogen-1 to the cell membrane. The secreted form may enhance both extrinsic and intrinsic coagulation pathways. It is postulated that the cell surface form requires docking with transmembrane proteins for downstream signaling which might be specific for a cell-type or response. By acting as C1q receptor is involved in chemotaxis of immature dendritic cells and neutrophils and is proposed to signal through CD209/DC-SIGN on immature dendritic cells, through integrin alpha-4/beta-1 during trophoblast invasion of the decidua, and through integrin beta-1 during endothelial cell adhesion and spreading. Signaling involved in inhibition of innate immune response is implicating the PI3K-AKT/PKB pathway. In mitochondrial translation may be involved in formation of functional 55S mitoribosomes; the function seems to involve its RNA-binding activity. May be involved in the nucleolar ribosome maturation process; the function may involve the exchange of FBL for RRP1 in the association with pre-ribosome particles. Involved in regulation of RNA splicing by inhibiting the RNA-binding capacity of SRSF1 and its phosphorylation. Is required for the nuclear translocation of splicing factor U2AF1L4. Involved in regulation of CDKN2A- and HRK-mediated apoptosis. Stabilizes mitochondrial CDKN2A isoform smARF. May be involved in regulation of FOXC1 transcriptional activity and NFY/CCAAT-binding factor complex-mediated transcription. In infection processes acts as an attachment site for microbial proteins. May play a role in antibacterial defense. Involved in regulation of antiviral response by inhibiting DDX58- and IFIH1-mediated signaling pathways probably involving its association with MAVS after viral infection. {ECO:0000269|PubMed:17486078, ECO:0000269|PubMed:18166172, ECO:0000269|PubMed:18460468, ECO:0000269|PubMed:22904065}." K18Ac 9607.04 "K,6;" 342 100 uniprot_mouse_length brain_HCD 791.125061 792.570496 792.568816 29 22942.46824 2.119191968 C1QC_MOUSE Complement C1q subcomponent subunit C;Flags: Precursor Q02105 SAGCYGIPGMPGMPGAPGKDGHDGLQGPKGEPGIPAVPGTRGPKGQKGEPGMPGHRGKNGPRGTSGLPGDPGPRGPPGEPGVEGRYKQKHQSVFTVTRQTTQYPEANALVRFNSVVTNPQGHYNPSTGKFTCEVPGLYYFVYYTSHTANLCVHLNLNLARVASFCDHMFNSKQVSSGGVLLRLQRGDEVWLSVNDYNGMVGIEGSNSVFSGFLLFPD 217 "FUNCTION: C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes." null 4338.97 null null 100 uniprot_mouse_length brain_HCD 658.0557861 658.62793 658.628941 30 19717.84767 -1.535481418 CABP5_MOUSE Calcium-binding protein 5; Short=CaBP5 Q9JLK3 MQFPMGPACIFLRKGIAEKQRERPLGQDELDELREAFLEFDKDQDGFISYKDLGNLMRTMGYMPTEMELTELGQQIRMNLGGRVDFEDFVELMTPKLLAETAGMIGVQEMRDAFKEFDANGDGEITLAELQQAMQRLLGEKLTPREIAEVVQEADINGDGTVDFEEFVKMMSR 173 FUNCTION: Inhibits calcium-dependent inactivation of L-type calcium channel and shifts voltage dependence of activation to more depolarized membrane potentials. Involved in the transmission of light signals. {ECO:0000269|PubMed:18586882}. null 8201.43 null null 100 uniprot_mouse_length brain_HCD 656.1260986 653.933167 653.925041 12 7832.09824 12.42574209 CCD23_MOUSE Coiled-coil domain-containing protein 23 Q99LQ4 MDPPARKEKSKVKEPAFRVEKAKQKSAQQELKQRQRAEIYALNRVMTELEQQQFDEFCKQMQPPGE 66 "SIMILARITY: Belongs to the CCDC23 family. {ECO:0000305}.-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" null 1104.79 null null 100 uniprot_mouse_length brain_HCD 541.0147095 540.135742 540.139189 22 11855.05141 -6.381341273 CD046_MOUSE Uncharacterized protein C4orf46 homolog Q3UUX7 MADSEEFRASSPPPPPPSSPSSGASSSSLSMPVSLGWRDPSRSPGPTVDPLEQVELQIGDAAFSLTKLLEATSAVSAQVEELALKCTENARFLKTWRDLLKEGYDSLKPDN 111 "SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q504U0}.-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" null 3156.42 null null 100 uniprot_mouse_length brain_HCD 544.1687012 543.977478 543.977779 26 14110.409 -0.553281159 CHRC1_MOUSE Chromatin accessibility complex protein 1; Short=CHRAC-1;AltName: Full=DNA polymerase epsilon subunit p15;AltName: Full=NF-YC-like protein;AltName: Full=YC-like protein 1; Short=YCL1 Q9JKP8 ADAAVGKEKCGDQRLVSLPLSRIRVIMKSSPEVSSINQEALVLTAKATELFVQYLATCSYRHGSGKAKKALTYSDLASTAEDSETLQFLADILPKKILASKYLKMLKEKREEEEDNEDDGSDLGEALA 128 "FUNCTION: Forms a complex with DNA polymerase epsilon subunit POLE3 and binds naked DNA, which is then incorporated into chromatin, aided by the nucleosome remodeling activity of ISWI/SNF2H and ACF1. {ECO:0000250}." A1AcS121P 6201.06 "A,146;S,254;" 200 100 uniprot_mouse_length brain_HCD 656.1260986 658.48645 658.491421 29 19057.23027 -7.548776687 CK088_MOUSE UPF0722 protein C11orf88 homolog Q80Y73 METGPRGCPSGRKESQEICSPGLLVFTGCSEQDANLAKQFWLGASMYPTTESQLVLTRGSSQRLPVARNSKVVLREKSSVQPFPFDQDKDAIIFAKAQRIQESEERAKYLQKAKTRDEILQLLRKQREERISKELISLPYKPKDKVPKSKEVLSESGLRDQEEVKALE 168 "SIMILARITY: Belongs to the UPF0722 family. {ECO:0000305}.-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" null 7205.05 null null 100 uniprot_mouse_length brain_HCD 550.2826538 545.762451 545.764455 42 22867.08046 -3.671598813 CLD1_MOUSE Claudin-1 O88551 MANAGLQLLGFILASLGWIGSIVSTALPQWKIYSYAGDNIVTAQAIYEGLWMSCVSQSTGQIQCKVFDSLLNLNSTLQATRALMVIGILLGLIAIFVSTIGMKCMRCLEDDEVQKMWMAVIGGIIFLISGLATLVATAWYGNRIVQEFYDPLTPINARYEFGQALFTGWAAASLCLLGGVLLSCSCPRKTTSYPTPRPYPKPTPSSGKDYV 211 "FUNCTION: Claudins function as major constituents of the tight junction complexes that regulate the permeability of epithelia. While some claudin family members play essential roles in the formation of impermeable barriers, others mediate the permeability to ions and small molecules. Often, several claudin family members are coexpressed and interact with each other, and this determines the overall permeability. CLDN1 is required to prevent the paracellular diffusion of small molecules through tight junctions in the epidermis and is required for the normal barrier function of the skin. Required for normal water homeostasis and to prevent excessive water loss through the skin, probably via an indirect effect on the expression levels of other proteins, since CLDN1 itself seems to be dispensable for water barrier formation in keratinocyte tight junctions. {ECO:0000269|PubMed:10508613, ECO:0000269|PubMed:11889141, ECO:0000269|PubMed:23407391}." null 8166.35 null null 100 uniprot_mouse_length brain_HCD 614.2867432 613.186646 613.190345 16 9790.03816 -6.033187276 COMD6_MOUSE COMM domain-containing protein 6 Q3V4B5 MEESGFREPVLDAKSEVTGQLIDFQWKLGMAVSSDSCRSLKYPYVAVMLKVADHSGQVSSKSIEMTIPQFQNFYKQFKEIAAVIETV 87 FUNCTION: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes. Inhibits TNF-induced NFKB1 activation. {ECO:0000250|UniProtKB:Q7Z4G1}. null 1999.68 null null 100 uniprot_mouse_length brain_HCD 656.1260986 656.838257 656.845524 30 19664.34183 -11.06373386 CTF2_MOUSE Cardiotrophin-2; Short=CT-2;AltName: Full=Neuropoietin; Short=Np;Flags: Precursor P83714 APISPSEPIGQAYSLALYMQKNTSALLQTYLQHQGSPFSDPGFSAPELQLSTLPSAAVSFKTWHAMEDAERLSRAQGAFLALTQHLQLVGDDQSYLNPGSPILLAQLGAARLRAQGLLGNMAAIMTALGLPIPPEEDTLGFVPFGASAFERKCRGYIVTREYGHWTDRAVRDLALLKAKYSA 182 FUNCTION: Increases the platelet count associated with splenomegaly. May have an important role in neuronal precursor development and maturation. null 7196.47 null null 100 uniprot_mouse_length brain_HCD 541.0147095 541.255676 541.258499 22 11879.67546 -5.215124518 EMC6_MOUSE ER membrane protein complex subunit 6;AltName: Full=Transmembrane protein 93 Q9CQW0 AAVVAKREGPPFISEAAVRGNAAVLDYCRTSVSALSGATAGILGLTGLYGFIFYLLASVLLSLLLILKAGRRWNKYFKSRRPLFTGGLIGGLFTYVLFWTFLYGMVHVY 109 SUBUNIT: Component of the ER membrane protein complex (EMC). {ECO:0000250}. null 3067.21 null null 100 uniprot_mouse_length brain_HCD 544.1687012 543.168457 543.168071 22 11921.68604 0.710703133 EMC6_MOUSE ER membrane protein complex subunit 6;AltName: Full=Transmembrane protein 93 Q9CQW0 AAVVAKREGPPFISEAAVRGNAAVLDYCRTSVSALSGATAGILGLTGLYGFIFYLLASVLLSLLLILKAGRRWNKYFKSRRPLFTGGLIGGLFTYVLFWTFLYGMVHVY 109 SUBUNIT: Component of the ER membrane protein complex (EMC). {ECO:0000250}. A1Ac 4586.7 "A,178;" 177 100 uniprot_mouse_length brain_HCD 750.7142944 746.385498 746.381846 15 11175.71949 4.893000673 F195B_MOUSE Protein FAM195B Q3UGS4 MTSSPVSRVVYNGKRNSSPRSPTNSSEIFTPAHEENVRFIYEAWQGVERDLRSQLSSGERCLVEEYVEKVPNPSLKTFKPIDLSDLKRRNTQDAKKS 97 SIMILARITY: Belongs to the FAM195 family. {ECO:0000305}. S21P 547.92 "S,4;" 61 100 uniprot_mouse_length brain_HCD 541.0147095 542.547791 542.548009 37 20026.25416 -0.402678938 FAP20_MOUSE Fanconi anemia-associated protein of 20 kDa Q3UN58 MEEERRLRGRLSRRRPPAGGGPPNCRPWFLSEGSKSEPWAALLRSTVSGTADWTPNRQPLPPLPAFPSQESLPDPESTVPPEAFTVGSKTFSWTPLPPALRGSGSSRHLFCEPEGSLGSPTPSLKGCPALNSGRTPSAQECVPVQSPLALLSCPLCQKAFDPKLTQLDVDSHLAQCLAECTEDVVW 186 FUNCTION: Component of the Fanconi anemia (FA) complex required to recruit the FA complex to DNA interstrand cross-links (ICLs) and promote ICLs repair. Following DNA damage recognizes and binds 'Lys-63'-linked ubiquitin generated by RNF8 at ICLs and recruits other components of the FA complex. Promotes translesion synthesis via interaction with REV1 (By similarity). {ECO:0000250}. null 8719.94 null null 100 uniprot_mouse_length brain_HCD 544.1687012 539.366394 539.373924 32 17218.94702 -13.96055074 FXYD5_MOUSE FXYD domain-containing ion transport regulator 5;AltName: Full=EF-8;AltName: Full=Ion channel homolog RIC;AltName: Full=Oncoprotein-induced protein 2;Flags: Precursor P97808 QTPKKPTSIFTADQTSATTRDNVPDPDQTSPGVQTTPLIWTREEATGSQTAAQTETQQLTKMATSNPVSDPGPHTSSKKGTPAVSRIEPLSPSKNFMPPSYIEHPLDSNENNPFYYDDTTLRKRGLLVAAVLFITGIIILTSGKCRQLSQFCLNRHR 157 FUNCTION: Involved in down-regulation of E-cadherin which results in reduced cell adhesion. Promotes metastasis (By similarity). {ECO:0000250}. null 9196.41 null null 100 uniprot_mouse_length brain_HCD 683.9489746 683.865417 683.860847 12 8191.32769 6.68334865 GBG11_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-11;Flags: Precursor P61953 MPALHIEDLPEKEKLKMEVEQLRKEVKLQRQQVSKCSEEIKNYIEERSGEDPLVKGIPEDKNPFKEKGSC 70 "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction (By similarity). {ECO:0000250}." C70Me 1472.84 "C,65;" 89 100 uniprot_mouse_length brain_HCD 541.0147095 539.474548 539.472862 15 8073.08934 3.125903011 GBG4_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-4;Flags: Precursor P50153 MKEGMSNNSTTSISQARKAVEQLKMEACMDRVKVSQAASDLLAYCEAHVREDPLIIPVPASENPFREKKFFC 72 "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction. {ECO:0000305}." null 1599.76 null null 100 uniprot_mouse_length brain_HCD 614.2867432 615.320374 615.315416 29 17805.12819 8.056900619 GPIX_MOUSE Platelet glycoprotein IX; Short=GP-IX; Short=GPIX;AltName: Full=Glycoprotein 9;AltName: CD_antigen=CD42a;Flags: Precursor O88186 TQACPRPCTCQSLETMGLKVNCEGQGLTALPVIPAHTRQLLLANNSLRSVPPGAFDHLPQLWDLDVTHNPWHCDCSLTYLRLWLEDHMPEALMHVYCASPDLATRRPLGQLTGYELGSCGWKLPPSWAYPGVWWDVSLVAVAVLGLILLAGLLNTFTESRN 161 FUNCTION: The GPIb-V-IX complex functions as the vWF receptor and mediates vWF-dependent platelet adhesion to blood vessels. The adhesion of platelets to injured vascular surfaces in the arterial circulation is a critical initiating event in hemostasis. GP-IX may provide for membrane insertion and orientation of GP-Ib (By similarity). {ECO:0000250}. null 7118.5 null null 100 uniprot_mouse_length brain_HCD 544.1687012 540.939087 540.938719 29 15650.207 0.680140004 GRP_MOUSE Gastrin-releasing peptide; Short=GRP;Contains: Neuromedin-C; AltName: Full=GRP-10;Flags: Precursor Q8R1I2 MRGSELSLLLLALVLCQAPRGPAAPVSTGAGGGTVLAKMYPRGSHWAVGHLMGKKSTDESPSLYAADRDGLKEQLRGYVRWEEAARDLLDLLEAAGNQSHQPPQHPPLSLQPTWDPEDGSYFNDVQTAKLVDSLLQVLKEKGGTAS 146 "FUNCTION: GRP stimulates gastrin release as well as other gastrointestinal hormones. Operates as a negative feedback regulating fear and established a causal relationship between GRP- receptor gene expression, long-term potentiation, and amygdala- dependent memory for fear. {ECO:0000269|PubMed:12526815}." null 8239.06 null null 100 uniprot_mouse_length brain_HCD 683.9489746 681.072266 681.069716 23 15633.58876 3.743559492 GSKIP_MOUSE GSK3-beta interaction protein; Short=GSKIP Q8BGR8 METDYNPVELSSMSGFEEGSELNGFEGADMKDMQLEAEAVVNDVLFAVNHMFVSKSMPCADDVAYINVETKERNRYCLELTEAGLRVVGYAFDQVEDHLQTPYHETVYSLLDTLSPAYREAFGNALLQRLEALKRDGQS 139 SUBUNIT: Interacts with GSK3B. {ECO:0000250}. null 5678.98 null null 100 uniprot_mouse_length brain_HCD 614.2867432 614.562256 614.568345 23 14105.05784 -9.907995872 H2A3_MOUSE Histone H2A type 3 Q8BFU2 SGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1AcT120P 3581.2 "S,2;T,0;" 185 100 uniprot_mouse_length brain_HCD 544.1687012 544.670044 544.670437 25 13585.74972 -0.721637638 H2AV_MOUSE Histone H2A.V;AltName: Full=H2A.F/Z Q3THW5 MAGGKAGKDSGKAKAKAVSRSQRAGLQFPVGRIHRHLKTRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGKKGQQKTA 128 "FUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. May be involved in the formation of constitutive heterochromatin. May be required for chromosome segregation during cell division (By similarity). {ECO:0000250}." K5AcK8Ac 5210 "K,2;K,0;" 201 100 uniprot_mouse_length brain_HCD 541.0147095 540.490051 540.490615 26 14019.74234 -1.042997701 H2B3A_MOUSE Histone H2B type 3-A Q9D2U9 PEPSRSTPAPKKGSKKAITKAQKKDGKKRKRGRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREVQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." P1AcK11AcS14P 3786.95 "P,6;K,0;S,36;" 195 100 uniprot_mouse_length brain_HCD 762.9417725 766.56073 766.556785 13 9948.23235 5.146364295 ACBP_MOUSE Acyl-CoA-binding protein; Short=ACBP;AltName: Full=Diazepam-binding inhibitor; Short=DBI;AltName: Full=Endozepine; Short=EP P31786 SQAEFDKAAEEVKRLKTQPTDEEMLFIYSHFKQATVGDVNTDRPGLLDLKGKAKWDSWNKLKGTSKESAMKTYVEKVDELKKKYGI 86 FUNCTION: Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA receptor. S1AcK7Ac 2625.47 "S,5;K,0;" 116 100 uniprot_mouse_length brain_HCD 807.2472534 803.996399 803.996382 21 16853.90644 0.021052061 AIF1_MOUSE Allograft inflammatory factor 1; Short=AIF-1;AltName: Full=Ionized calcium-binding adapter molecule 1 O70200 SQSRDLQGGKAFGLLKAQQEERLEGINKQFLDDPKYSNDEDLPSKLEAFKVKYMEFDLNGNGDIDIMSLKRMLEKLGVPKTHLELKRLIREVSSGSEETFSYSDFLRMMLGKRSAILRMILMYEEKNKEHKRPTGPPAKKAISELP 146 "FUNCTION: Actin-binding protein that enhances membrane ruffling and RAC activation. Enhances the actin-bundling activity of LCP1. Binds calcium. Plays a role in RAC signaling and in phagocytosis. May play a role in macrophage activation and function. Promotes the proliferation of vascular smooth muscle cells and of T- lymphocytes. Enhances lymphocyte migration. Plays a role in vascular inflammation. {ECO:0000269|PubMed:10934045, ECO:0000269|PubMed:11500035, ECO:0000269|PubMed:11722645, ECO:0000269|PubMed:11916959, ECO:0000269|PubMed:14756805}." S1AcK10Ac 2821.28 "S,0;K,9;" 161 100 uniprot_mouse_length brain_HCD 544.784668 541.592896 541.599001 44 23773.32905 -11.27308613 ALRF2_MOUSE Aly/REF export factor 2;AltName: Full=Alyref;AltName: Full=RNA and export factor-binding protein 2 Q9JJW6 MADKMDMSLDDIIKLNRNQRRVNRGGGPRRNRPAIARGGRNRPAPYSRPKPLPDKWQHDLFDSGCGGGEGVETGAKLLVSNLDFGVSDADIQELFAEFGTLKKAAVDYDRSGRSLGTADVHFERRADALKAMKQYKGVPLDGRPMDIQLVASQIDPQRRPAQSGNRGGMTRSRGSGGFGGRGSQGRGRGTGRNSKQQQLSAEELDAQLDAYNARMDTS 218 "FUNCTION: Export adapter involved in spliced and unspliced mRNA nuclear export. Binds mRNA which is transferred to the NXF1-NXT1 heterodimer for export (TAP/NFX1 pathway); enhances NXF1-NXT1 RNA- binding activity. {ECO:0000269|PubMed:10786854, ECO:0000269|PubMed:11158589, ECO:0000269|PubMed:18364396}." R24dMeR32dMe 10764.74 "R,12;R,0;" 356 100 uniprot_mouse_length brain_HCD 544.1685791 544.362915 544.364786 14 7604.10431 -3.436961732 AT5G3_MOUSE "ATP synthase F(0) complex subunit C3, mitochondrial;AltName: Full=ATP synthase lipid-binding protein;AltName: Full=ATP synthase proteolipid P3;AltName: Full=ATPase protein 9;AltName: Full=ATPase subunit c;Flags: Precursor" P56384 DIDTAAKFIGAGAATVGVAGSGAGIGTVFGSLIIGYARNPSLKQQLFSYAILGFALSEAMGLFCLMVAFLILFAM 75 "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element." null 1956.48 null null 100 uniprot_mouse_length brain_HCD 614.25354 612.481262 612.480208 12 7334.76049 1.721209955 ATOX1_MOUSE Copper transport protein ATOX1;AltName: Full=Metal transport protein ATX1 O08997 MPKHEFSVDMTCEGCAEAVSRVLNKLGGVEFNIDLPNKKVCIDSEHSSDTLLATLNKTGKAVSYLGPK 68 FUNCTION: Binds and deliver cytosolic copper to the copper ATPase proteins. May be important in cellular antioxidant defense (By similarity). {ECO:0000250}. null 931.31 null null 100 uniprot_mouse_length brain_HCD 542.0512085 538.601074 538.600398 19 10209.39985 1.255511048 BOLA2_MOUSE BolA-like protein 2 Q8BGS2 MELSADYLREKLRQDLEAEHVEVEDTTLNRCATSFRVLVVSAKFEGKPLLQRHRLVNECLAEELPHIHAFEQKTLTPEQWTRQRRE 86 ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q8BGS2-1; Sequence=Displayed; Note=No experimental confirmation available.; Name=2; IsoId=Q8BGS2-2; Sequence=VSP_010094; Note=No experimental confirmation available.; null 3307.48 null null 100 uniprot_mouse_length brain_HCD 544.1685791 545.286255 545.284715 24 13055.82083 2.823997758 C10_MOUSE Protein C10 O35127 ASASAQPAALSAEQAKVVLAEVIQAFSAPENAVRMDEARDNACNDMGKMLQFVLPVATQIQQEVIKAYGFSCDGEGVLKFARLVKSYEAQDPEIASLSGKLKALFLPPMTLPPHGPASGSSVAAS 125 "FUNCTION: In brain, may be required for corpus callusum development. {ECO:0000250}." null 5476.19 null null 100 uniprot_mouse_length brain_HCD 527.0862427 523.197998 523.20433 28 14614.70874 -12.10225673 CALCB_MOUSE Calcitonin gene-related peptide 2;AltName: Full=Beta-type CGRP;AltName: Full=Calcitonin gene-related peptide II; Short=CGRP-II;Flags: Precursor Q99MP3 MDFWKFFPFLALSTIWVLCLASSLQAAPFRSALESSLDLGTLGDQEKHLLLAALMQDYEQMKARKLEQEEQETKGSRVTAQKRSCNTATCVTHRLADLLSRSGGVLKDNFVPTDVGSEAFGRRRRRDLQA 130 "FUNCTION: CGRP induces vasodilation. It dilates a variety of vessels including the coronary, cerebral and systemic vasculature. Its abundance in the CNS also points toward a neurotransmitter or neuromodulator role (By similarity). {ECO:0000250}." null 1786.23 null null 100 uniprot_mouse_length brain_HCD 544.784668 541.559387 541.56178 21 11345.78839 -4.418319492 CASP6_MOUSE Caspase-6; Short=CASP-6; EC=3.4.22.59;AltName: Full=Apoptotic protease Mch-2;Contains: Caspase-6 subunit p18;Contains: Caspase-6 subunit p11;Flags: Precursor O08738 ASVYTLPAGADFLMCYSVAEGYYSHRETVNGSWYIQDLCEMLARYGSSLEFTELLTLVNRKVSQRRVDFCKDPDAIGKKQVPCFASMLTKKLHFCPKPSK 100 "FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. Cleaves poly(ADP-ribose) polymerase in vitro, as well as lamins. Overexpression promotes programmed cell death (By similarity). {ECO:0000250}." null 3051.62 null null 100 uniprot_mouse_length brain_HCD 543.9406738 544.131348 544.125477 34 18456.24638 10.78915893 CAV2_MOUSE Caveolin-2 Q9WVC3 MGLETEKADVQLFMADDAYSHHSGVDYADPEKYVDSSHDRDPHQLNSHLKLGFEDLIAEPETTHSFDKVWICSHALFEISKYVMYKFLTVFLAIPLAFIAGILFATLSCLHIWILMPFVKTCLMVLPSVQTIWKSVTDVVIGPLCTSVGRSFSSVSMQLSHD 162 "FUNCTION: May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Acts as an accessory protein in conjunction with CAV1 in targeting to lipid rafts and driving caveolae formation. The Ser-36 phosphorylated form has a role in modulating mitosis in endothelial cells. Positive regulator of cellular mitogenesis of the MAPK signaling pathway. Required for the insulin-stimulated nuclear translocation and activation of MAPK1 and STAT3, and the subsequent regulation of cell cycle progression (By similarity). {ECO:0000250}." Y19PS23PY27P 3445.26 "Y,3;S,0;Y,0;" 213 100 uniprot_mouse_length brain_HCD 755.0835571 754.548889 754.544798 13 9792.07622 5.422024202 CB082_MOUSE Uncharacterized protein C2orf82 homolog;Flags: Precursor Q9CXL7 AEGPQEPDPTLWNEPIELPSGEGPLESTSHNQEFAVSGPPFPTSAPAPEDSTPPARVDQDGGSLGPGAIAAIVIAALLATCVVLALVVVALRKFSAS 97 "SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" null 887.21 null null 100 uniprot_mouse_length brain_HCD 543.9406738 546.473328 546.47754 27 14720.88024 -7.708209346 CC014_MOUSE Uncharacterized protein C3orf14 homolog Q8BGD0 MASLFTQEIHLSKRHEEILSQRLMLLQKMKNKFGDENTERASLLQATETASRRNLRLLKDIDAAEEAFQTKLIPHPQPSMLSLETRYWASVEEHIPKWELFLLGRAPYPIGAENQNEVPFVQTEAKL 127 "ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q8BGD0-1; Sequence=Displayed; Name=2; IsoId=Q8BGD0-2; Sequence=VSP_014596; Note=No experimental confirmation available.;-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" null 2066.02 null null 100 uniprot_mouse_length brain_HCD 718.8442993 721.66333 721.657582 11 7924.23096 7.965104599 CC179_MOUSE Coiled-coil domain-containing protein 179 J3QM76 MCLRVKDEEPAQVYPEGPRRHHPSDVSTRQSVEKRINYMQNLQKEKRKLGKRFARPNPIPDTGILWT 67 "-------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License--------------------------------------------------" null 531.27 null null 100 uniprot_mouse_length brain_HCD 545.2867432 545.472717 545.475073 26 14149.34134 -4.31864802 CCL25_MOUSE C-C motif chemokine 25;AltName: Full=Chemokine TECK;AltName: Full=Small-inducible cytokine A25;AltName: Full=Thymus-expressed chemokine;Flags: Precursor O35903 QGAFEDCCLGYQHRIKWNVLRHARNYHQQEVSGSCNLRAVRFYFRQKVVCGNPEDMNVKRAMRILTARKRLVHWKSASDSQTERKKSNHMKSKVENPNSTSVRSATLGHPRMVMMPRKTNN 121 "FUNCTION: Potentially involved in T-cell development. Recombinant protein shows chemotactic activity on thymocytes, macrophages, THP-1 cells, and dendritics cells but is inactive on peripheral blood lymphocytes and neutrophils. Binds to CCR9. Binds to atypical chemokine receptor ACKR4 and mediates the recruitment of beta-arrestin (ARRB1/2) to ACKR4." null 5816.96 null null 100 uniprot_mouse_length brain_HCD 589.013855 590.182007 590.18607 23 13544.26784 -6.88454755 CD036_MOUSE Uncharacterized protein C4orf36 homolog Q9DAA3 MAYGLPRRNTVQTILKGSCYKVQEPWDLAELTKTWYTNLTNIRLPFLGEIVFGSPMNLLASQTKQECQFPSMQSMALEKEYEAKRLTKLKCQENVCKEIQASLREKKVGLRRPLQPK 117 "-------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License--------------------------------------------------" null 6190.24 null null 100 uniprot_mouse_length brain_HCD 680.9090576 682.354614 682.351707 28 19067.82695 4.260644156 CD3E_MOUSE T-cell surface glycoprotein CD3 epsilon chain;AltName: Full=T-cell surface antigen T3/Leu-4 epsilon chain;AltName: CD_antigen=CD3e;Flags: Precursor P22646 DDAENIEYKVSISGTSVELTCPLDSDENLKWEKNGQELPQKHDKHLVLQDFSEVEDSGYYVCYTPASNKNTYLYLKARVCEYCVEVDLTAVAIIIIVDICITLGLLMVIYYWSKNRKAKAKPVTRGTGAGSRPRGQNKERPPPVPNPDYEPIRKGQRDLYSGLNQRAV 168 FUNCTION: The CD3 complex mediates signal transduction. Y149P 8715.91 "Y,25;" 269 100 uniprot_mouse_length brain_HCD 610.8439331 613.529968 613.537241 27 16530.48971 -11.85378457 CD3Z_MOUSE T-cell surface glycoprotein CD3 zeta chain;AltName: Full=T-cell receptor T3 zeta chain;AltName: CD_antigen=CD247;Flags: Precursor P24161 QSFGLLDPKLCYLLDGILFIYGVIITALYLRAKFSRSAETAANLQDPNQLYNELNLGRREEYDVLEKKRARDPEMGGKQQRRRNPQEGVYNALQKDKMAEAYSEIGTKGERRRGKGHDGLYQGLSTATKDTYDALHMQTLAPR 143 FUNCTION: Probable role in assembly and expression of the TCR complex as well as signal transduction upon antigen triggering. S37PY51PY62P 1175.51 "S,4;Y,0;Y,0;" 117 100 uniprot_mouse_length brain_HCD 822.0374756 822.037476 822.037399 27 22155.98275 0.093166001 CG050_MOUSE Uncharacterized protein C7orf50 homolog Q9CXL3 MAKHKRKGLEGTGKESKRQKITPAEETPRTSEAGPDKETASTLVQEASPELSPEERRVLERKLKKERKKEEKKRLREAGIAATQTAKVQTLPAKPSAATLALEYLQGWAQKQESWRFQKTRQTWLLLHMYDEDKVPDEHFPTLLDYLEGLRGSARELTVRKAEALMQKLDEAEPEDSGGSPGKVQRLRQVLQLLS 195 "SEQUENCE CAUTION: Sequence=BAB29235.1; Type=Frameshift; Positions=180; Evidence={ECO:0000305};-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" null 4605.16 null null 100 uniprot_mouse_length brain_HCD 753.0847778 755.790955 755.801629 21 15842.81919 -14.12329604 CH059_MOUSE Uncharacterized protein C8orf59 homolog Q0VG62 MLAAAAPRALFCQLLVLYRFLVGDRTPGVPRPETLRPPLSRTMAKNKLKGQKSRNVFHIASHKTFKAKNKAKPVTTNLKKINIMNHEKVNRMNRAFVNIQKELANFSKSLSLKSVQKELKHHENEPANVDEATRLMAQL 139 "CAUTION: It is uncertain whether Met-1 or Met-43 is the initiator. {ECO:0000305}.-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" K63Ac 962.57 "K,74;" 95 100 uniprot_mouse_length brain_HCD 777.2106323 774.635132 774.639351 14 10825.94201 -5.446617264 CH10_MOUSE "10 kDa heat shock protein, mitochondrial; Short=Hsp10;AltName: Full=10 kDa chaperonin;AltName: Full=Chaperonin 10; Short=CPN10" Q64433 AGQAFRKFLPLFDRVLVERSAAETVTKGGIMLPEKSQGKVLQATVVAVGSGGKGKSGEIEPVSVKVGDKVLLPEYGGTKVVLDDKDYFLFRDSDILGKYVD 101 "FUNCTION: Eukaryotic CPN10 homolog which is essential for mitochondrial protein biogenesis, together with CPN60. Binds to CPN60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter." null 2858.13 null null 100 uniprot_mouse_length brain_HCD 544.784668 545.284546 545.286214 25 13600.14507 -3.059130269 CHCH1_MOUSE "Coiled-coil-helix-coiled-coil-helix domain-containing protein 1;AltName: Full=28S ribosomal protein S37, mitochondrial; Short=MRP-S37" Q9CQA6 MATPSLRGRLARFANPGKPILKPNKPLILANRVGNRRREKGEATCITEMSMMMACWKQNEFRDEACRKEIQDFFDCSSRAQEARKMRSIQESLGQSESLSPHKMTKLLQRFPNKSHLI 118 SUBUNIT: Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. {ECO:0000250}. null 4624.2 null null 100 uniprot_mouse_length brain_HCD 543.9406738 545.974609 545.972788 33 17975.08347 3.336017912 CI040_MOUSE Uncharacterized protein C9orf40 homolog Q8VCE4 MAKRRAAEPLTFRVPWKRLLLSDFPEEPPLWVPPSGTARPLKRQGDAGIMAEPASAPRKRRGGGDDRQELQGCSREPGEPPPGEQEEPRAAGGGDRVESAGSPQVADGVHSQQPEEFWQYNTFQYWRNPLPPLDLAALEDVSANSLTETLEDKNEGVEIDMES 163 "-------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License--------------------------------------------------" null 3054.83 null null 100 uniprot_mouse_length brain_HCD 803.4020996 801.48761 801.483699 15 12001.24541 4.87952941 CISD1_MOUSE CDGSH iron-sulfur domain-containing protein 1;AltName: Full=MitoNEET Q91WS0 GLSSNSAVRVEWIAAVTFAAGTAALGYLAYKKFYAKENRTKAMVNLQIQKDNPKVVHAFDMEDLGDKAVYCRCWRSKKFPFCDGAHIKHNEETGDNVGPLIIKKKET 107 FUNCTION: Plays a key role in regulating maximal capacity for electron transport and oxidative phosphorylation. May be involved in Fe-S cluster shuttling and/or in redox reactions (By similarity). {ECO:0000250}. K54Ac 1577.45 "K,3;" 94 100 uniprot_mouse_length brain_HCD 802.5785522 799.882263 799.876802 13 10380.39033 6.827530915 CJ053_MOUSE UPF0728 protein C10orf53 homolog Q3KNL4 MPAQAVVTLRYGPYSAVGLSVEHRTYRLQGLQAVLAKDGHQIILEQIEDWNLVELVVNEETVFQCDIQELEFGGDGKLDPLCEEARIAVLNAF 93 "SIMILARITY: Belongs to the UPF0728 family. {ECO:0000305}.-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" null 1620.87 null null 100 uniprot_mouse_length brain_HCD 654.727356 651.889343 651.879772 30 19515.37107 14.68255671 CK001_MOUSE UPF0686 protein C11orf1 homolog Q9D131 MAVSCSLNHSTYLQRQNLVCYLRNPHYGSLIYADGHGEVWTDWNDMSKFLQYGWRCTTNENSYSNRTLVGNWNQERYDLKNIVKPKPLPSQFGHAFETTYDANYSRKKPQSTHRFKREPHWFPGHQPELDPPHYKCTAKSTYMTNYSEPQPTHYSCCVYDPSVSQS 166 SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. null 2421.27 null null 100 uniprot_mouse_length brain_HCD 714.2255859 717.397461 717.391086 7 5013.73973 8.88627922 CL073_MOUSE Uncharacterized protein C12orf73 homolog;Flags: Precursor Q8BTC1 QVVHWYYRPDLTIPEIPPKPGELKTELLGLKERRHEPHVSQQ 42 "SUBCELLULAR LOCATION: Secreted {ECO:0000305}.-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" null 216.3 null null 100 uniprot_mouse_length brain_HCD 804.9081421 800.053284 800.061934 13 10382.79778 -10.8120487 CN142_MOUSE Uncharacterized protein C14orf142 homolog P0C8B4 MELSGEYVGCDGEPQRLRVSCEASGDADPLQSLSAGVVRMKELVAEFFGTLVEQDAQGLAEDPDDALDGDDEDDAEDENNSGRTNSDGPSAKRPKPAS 98 "-------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License--------------------------------------------------" M1Ac 1351.45 "M,57;" 90 100 uniprot_mouse_length brain_HCD 783.3365479 780.841614 780.846512 16 12471.53294 -6.27297477 COX5A_MOUSE "Cytochrome c oxidase subunit 5A, mitochondrial;AltName: Full=Cytochrome c oxidase polypeptide Va;Flags: Precursor" P12787 SHGSHETDEEFDARWVTYFNKPDIDAWELRKGMNTLVGYDLVPEPKIIDAALRACRRLNDFASAVRILEVVKDKAGPHKEIYPYVIQELRPTLNELGISTPEELGLDKV 109 "FUNCTION: This is the heme A-containing chain of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport." K46Ac 2222.8 "K,17;" 106 100 uniprot_mouse_length brain_HCD 543.9406738 543.162903 543.168208 20 10838.35768 -9.767081156 COX5B_MOUSE "Cytochrome c oxidase subunit 5B, mitochondrial;AltName: Full=Cytochrome c oxidase polypeptide Vb;Flags: Precursor" P19536 ASGGGVPTDEEQATGLEREIMIAAQKGLDPYNMLPPKAASGTKEDPNLVPSISNKRIVGCICEEDNCTVIWFWLHKGESQRCPNCGTHYKLVPHQMAH 98 "FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport." K37AcK55AcK90Ac 1007.89 "K,10;K,0;K,14;" 89 100 uniprot_mouse_length brain_HCD 785.8417969 784.554932 784.5562 7 5482.89314 -1.616658405 COX7C_MOUSE "Cytochrome c oxidase subunit 7C, mitochondrial;AltName: Full=Cytochrome c oxidase polypeptide VIIc;Flags: Precursor" P17665 SHYEEGPGKNLPFSVENKWRLLAMMTVYFGSGFAAPFFIVRHQLLKK 47 "FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport." K9Ac 633.16 "K,28;" 44 100 uniprot_mouse_length brain_HCD 614.5771484 614.539856 614.536592 23 14104.32874 5.311249279 CSF2_MOUSE Granulocyte-macrophage colony-stimulating factor; Short=GM-CSF;AltName: Full=Colony-stimulating factor; Short=CSF;Flags: Precursor P01587 APTRSPITVTRPWKHVEAIKEALNLLDDMPVTLNEEVEVVSNEFSFKKLTCVQTRLKIFEQGLRGNFTKLKGALNMTASYYQTYCPPTPETDCETQVTTYADFIDSLKTFLTDIPFECKKPGQK 124 "FUNCTION: Cytokine that stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes." null 6088.81 null null 100 uniprot_mouse_length brain_HCD 658.1777954 653.690918 653.700266 15 9785.49708 -14.30017966 CXL13_MOUSE C-X-C motif chemokine 13;AltName: Full=B lymphocyte chemoattractant;AltName: Full=CXC chemokine BLC;AltName: Full=Small-inducible cytokine B13;Flags: Precursor O55038 ILEAHYTNLKCRCSGVISTVVGLNIIDRIQVTPPGNGCPKTEVVIWTKMKKVICVNPRAKWLQRLLRHVQSKSLSSTPQAPVSKRRAA 88 "FUNCTION: Strongly chemotactic for B-lymphocytes, weakly for spleen monocytes and macrophages but no chemotactic activity for granulocytes. Binds to BLR1/CXCR5. May play a role in directing the migration of B-lymphocytes to follicles in secondary lymphoid organs." null 585.47 null null 100 uniprot_mouse_length brain_HCD 527.0862427 522.554443 522.55334 22 11468.16326 2.111477031 CYC_MOUSE "Cytochrome c, somatic" P62897 GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAAGFSYTDANKNKGITWGEDTLMEYLENPKKYIPGTKMIFAGIKKKGERADLIAYLKKATNE 104 "FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. {ECO:0000269|PubMed:12062423}." null 990.58 null null 100 uniprot_mouse_length brain_HCD 887.8051758 884.191711 884.1887 14 12358.63079 3.405863229 DAD1_MOUSE Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1; Short=Oligosaccharyl transferase subunit DAD1; EC=2.4.99.18;AltName: Full=Defender against cell death 1; Short=DAD-1 P61804 SASVVSVISRFLEEYLSSTPQRLKLLDAYLLYILLTGALQFGYCLLVGTFPFNSFLSGFISCVGSFILAVCLRIQINPQNKADFQGISPERAFADFLFASTILHLVVMNFVG 112 FUNCTION: Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER) (By similarity). Loss of the DAD1 protein triggers apoptosis. {ECO:0000250}. null 263.82 null null 100 uniprot_mouse_length brain_HCD 592.4359741 591.770935 591.774559 19 11219.70855 -6.123854686 DAP1_MOUSE Death-associated protein 1; Short=DAP-1 Q91XC8 SSPPEGKLETKAGHPPAVKAGGMRIVQKHPHTGDGKEERDKDDQEWESTSPPKPTVFISGVIARGDKDFPPAAAQVAHQKPHASMDKHVSPRTQHIQQPRK 101 FUNCTION: Negative regulator of autophagy. Involved in mediating interferon-gamma-induced cell death (By similarity). {ECO:0000250}. S1AcS2PS48P 2632.59 "S,11;S,31;S,0;" 133 100 uniprot_mouse_length brain_HCD 543.9406738 541.591919 541.595521 19 10266.30854 -6.650820673 DEFA4_MOUSE Alpha-defensin 4;AltName: Full=Defensin-related cryptdin-4;Flags: Precursor P28311 MKTLVLLSALVLLAFQVQADPIQNTDEETKTEEQPGEEDQAVSISFGGQEGSALHEKSLRGLLCYCRKGHCKRGERVRGTCGIRFLYCCPRR 92 FUNCTION: Probably contributes to the antimicrobial barrier function of the small bowel mucosa. null 1279.64 null null 100 uniprot_mouse_length brain_HCD 907.1617432 908.173401 908.174918 11 9973.91877 -1.670516399 DFAR2_MOUSE Alpha-defensin-related sequence 2;AltName: Full=CRS4C1;AltName: Full=Cryptdin-related protein 4C-1;AltName: Full=Defensin-related cryptdin-related sequence 2;Flags: Precursor P17534 MKKLVLLFALVLLAFQVQADSIQNTDEETKTEEQPGEKDQAVSVSFGDPQGSALQDAALGWGRRCPQCPRCPSCPSCPRCPRCPRCKCNPK 91 "FUNCTION: Apparent precursor of a secreted, cationic, proline- and cysteine-rich peptide that contains Cys-Pro-Xaa repeats. Unlike cryptdin, the proposed mature peptide region lacks the structural motif characteristic of defensins. It may have microbicidal activities." null 1541.45 null null 100 uniprot_mouse_length brain_HCD 547.206604 545.973145 545.972476 10 5447.72633 1.224477935 DFB17_MOUSE "Beta-defensin 17; Short=BD-17; Short=mBD-17;AltName: Full=Defensin, beta 17;Flags: Precursor" Q30KP6 KKSYPEYGSLDLRKECKMRRGHCKLQCSEKELRISFCIRPGTHCCM 46 FUNCTION: Has antibacterial activity. {ECO:0000250}. null 1069.23 null null 100 uniprot_mouse_length brain_HCD 544.784668 542.050964 542.0564 9 4867.50945 -10.02782096 DFB33_MOUSE "Beta-defensin 33; Short=BD-33; Short=mBD-33;AltName: Full=Defensin, beta 33;Flags: Precursor" Q30KN3 RKRNSKFRPCEKMGGICKSQKTHGCSILPAECKSRYKHCCRL 42 FUNCTION: Has antibacterial activity. {ECO:0000250}. null 751.38 null null 100 uniprot_mouse_length brain_HCD 762.0786743 760.655884 760.6476 21 15944.58341 10.89044265 DJC15_MOUSE DnaJ homolog subfamily C member 15 Q78YY6 MATGGGVTSREGLRYAEYLPPSAQRSDADIDHTAGRRLLAVGLGVAAVAFAGRYAFQIWKPLEQVITATARKISSPSFSSYYKGGFEQKMSKREASLILGVSPSAGKAKIRTAHKRIMILNHPDKGGSPYLASKINEAKDLLEASSKAN 149 "FUNCTION: Acts as an import component of the TIM23 translocase complex. Stimulates the ATPase activity of HSPA9 (By similarity). Negative regulator of the mitochondrial respiratory chain. Prevents mitochondrial hyperpolarization state and restricts mitochondrial generation of ATP. {ECO:0000250, ECO:0000269|PubMed:23530063}." null 2251.07 null null 100 uniprot_mouse_length brain_HCD 777.2106323 776.567566 776.560332 14 10852.83658 9.315332847 DLRB1_MOUSE "Dynein light chain roadblock-type 1;AltName: Full=Dynein light chain 2A, cytoplasmic" P62627 AEVEETLKRLQSQKGVQGIIVVNTEGIPIKSTMDNPTTTQYANLMHNFILKARSTVREIDPQNDLTFLRIRSKKNEIMVAPDKDYFLIVIQNPTE 95 FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. null 1526.6 null null 100 uniprot_mouse_length brain_HCD 545.2867432 544.784607 544.786777 17 9240.36873 -3.983331641 DPM2_MOUSE Dolichol phosphate-mannose biosynthesis regulatory protein;AltName: Full=Dolichol-phosphate mannose synthase subunit 2; Short=DPM synthase subunit 2 Q9Z324 ATGTDQAVGFGLVAVSLIIFTYYTTWVILLPFIDSQHVIHKYFLPRAYAVLLPLAAGLLLLLFVGLFITYVMLKSQKITKKAQ 83 FUNCTION: Regulates the biosynthesis of dolichol phosphate- mannose. Regulatory subunit of the dolichol-phosphate mannose (DPM) synthase complex; essential for the ER localization and stable expression of DPM1. When associated with the GPI-GlcNAc transferase (GPI-GnT) complex enhances but is not essential for its activity (By similarity). {ECO:0000250}. null 1954.38 null null 100 uniprot_mouse_length brain_HCD 960.1845093 964.606628 964.603683 22 21187.25576 3.053500646 EFNA5_MOUSE Ephrin-A5;AltName: Full=AL-1;AltName: Full=EPH-related receptor tyrosine kinase ligand 7; Short=LERK-7;Flags: Precursor O08543 QDPGSKVVADRYAVYWNSSNPRFQRGDYHIDVCINDYLDVFCPHYEDSVPEDKTERYVLYMVNFDGYSACDHTSKGFKRWECNRPHSPNGPLKFSEKFQLFTPFSLGFEFRPGREYFYISSAIPDNGRRSCLKLKVFVRPTNSCMKTIGVHDRVFDVNDKVENSLEPADDTVHESAEPSRGEN 183 "FUNCTION: Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Induces compartmentalized signaling within a caveolae-like membrane microdomain when bound to the extracellular domain of its cognate receptor. This signaling event requires the activity of the Fyn tyrosine kinase. Activates the EPHA3 receptor to regulate cell-cell adhesion and cytoskeletal organization. With the receptor EPHA2 may regulate lens fiber cells shape and interactions and be important for lens transparency maintenance. May function actively to stimulate axon fasciculation. The interaction of EFNA5 with EPHA5 also mediates communication between pancreatic islet cells to regulate glucose-stimulated insulin secretion. Cognate/functional ligand for EPHA7, their interaction regulates brain development modulating cell-cell adhesion and repulsion. {ECO:0000269|PubMed:11089974, ECO:0000269|PubMed:17448994, ECO:0000269|PubMed:18948590, ECO:0000269|PubMed:9053851}." null 2842.21 null null 100 uniprot_mouse_length brain_HCD 773.3865356 777.637146 777.637621 17 13196.82876 -0.61082938 ENSA_MOUSE Alpha-endosulfine;AltName: Full=ARPP-19e P60840 SQKQEEENPAEETGEEKQDTQEKEGILPEKAEEAKLKAKYPSLGQKPGGSDFLMKRLQKGQKYFDSGDYNMAKAKMKNKQLPSAGADKNLVTGDHIPTPQDLPQRKSSLVTSKLAGGQVE 120 "FUNCTION: Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-67 during mitosis, specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, an essential condition to keep cyclin-B1-CDK1 activity high during M phase. Also acts as a stimulator of insulin secretion by interacting with sulfonylurea receptor (ABCC8), thereby preventing sulfonylurea from binding to its receptor and reducing K(ATP) channel currents (By similarity). {ECO:0000250}." null 587.75 null null 100 uniprot_mouse_length brain_HCD 545.2867432 542.431335 542.438442 51 27599.32994 -13.10111937 ETFB_MOUSE Electron transfer flavoprotein subunit beta; Short=Beta-ETF Q9DCW4 AELRALVAVKRVIDFAVKIRVKPDKSGVVTDGVKHSMNPFCEIAVEEAVRLKEKKLVKEIIAVSCGPSQCQETIRTALAMGADRGIHVEIPGAQAESLGPLQVARVLAKLAEKEKVDLLFLGKQAIDDDCNQTGQMTAGLLDWPQGTFASQVTLEGDKVKVEREIDGGLETLRLKLPAVVTADLRLNEPRYATLPNIMKAKKKKIEVVKAGDLGVDLTSKVSVISVEEPPQRSAGVKVETTEDLVAKLKEVGRI 254 "FUNCTION: The electron transfer flavoprotein serves as a specific electron acceptor for several dehydrogenases, including five acyl- CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (By similarity). {ECO:0000250}." A1AcS222P 14980.74 "A,9;S,23;" 450 100 uniprot_mouse_length brain_HCD 544.1685791 542.476074 542.471716 29 15693.66733 8.034001813 F136A_MOUSE Protein FAM136A Q9CR98 AEVQQLRVQEAVDAMVKSVERENIRKMQGLMFRCSANCCEDTQASMQQVHQCIERCHAPLAQAQALVTSELERFQDRLARCTMHCNDKAKDSMDAGTKELQVKRQLDSCVTKCVDDHMHLIPTMTKKMKESLSSIGK 137 SUBCELLULAR LOCATION: Mitochondrion. T123PT125P 6810.93 "T,4;T,2;" 219 100 uniprot_mouse_length brain_HCD 542.0512085 541.574036 541.568119 33 17828.73008 10.92502369 F163A_MOUSE Protein FAM163A Q8CAA5 MTAGTVVITGGILATVILLCIIAVLCYCRLQYYCCKKGTDGEDAEEEEEEEEHGLSIHPRVPACNACSSHVLDGRGGLAPLTSESCSQPCGVASHCTTCSPYRTPFYIRTADMVPNGGGGERLSFAPTHYKEGGTPSLKLAAPQNYPVTWPSSGHEAFTNPRAISTDV 168 SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. null 9189.52 null null 100 uniprot_mouse_length brain_HCD 708.5971069 709.135376 709.133295 25 17694.31645 2.934535125 F219A_MOUSE Protein FAM219A Q9D772 MMEEIDRFQDPAAASISDRDCDAREEKQRELARKGSLKNGSMGSPVNQQPKKNNVMARTRLVVPNKGYSSLDQSPDEKPLVALDTDSDDDFDMSRYSSSGYSSAEQINQDLNIQLLKDGYRLDEIPDDEDLDLIPPKSVNPTCMCCQATSSTACHIQ 157 "SIMILARITY: Belongs to the FAM219 family. {ECO:0000305}.-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" S74PT85PS87P 7420.41 "S,25;T,0;S,0;" 243 100 uniprot_mouse_length brain_HCD 542.0512085 543.209717 543.210771 27 14632.6781 -1.940688921 FABP4_MOUSE "Fatty acid-binding protein, adipocyte;AltName: Full=3T3-L1 lipid-binding protein;AltName: Full=Adipocyte lipid-binding protein; Short=ALBP;AltName: Full=Adipocyte-type fatty acid-binding protein; Short=A-FABP; Short=AFABP;AltName: Full=Fatty acid-binding protein 4;AltName: Full=Myelin P2 protein homolog;AltName: Full=P15;AltName: Full=P2 adipocyte protein;AltName: Full=Protein 422" P04117 CDAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDLVTIRSESTFKNTEISFKLGVEFDEITADDRKVKSIITLDGGALVQVQKWDGKSTTIKRKRDGDKLVVECVMKGVTSTRVYERA 131 "FUNCTION: Lipid transport protein in adipocytes. Binds both long chain fatty acids and retinoic acid. Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus. {ECO:0000269|PubMed:12077340, ECO:0000269|PubMed:16574478, ECO:0000269|PubMed:17516629}." C1AcY19P 5501.62 "C,205;Y,241;" 212 100 uniprot_mouse_length brain_HCD 627.7249756 626.929016 626.925623 23 14389.27659 5.412305953 FABP6_MOUSE Gastrotropin; Short=GT;AltName: Full=Fatty acid-binding protein 6;AltName: Full=Ileal lipid-binding protein; Short=ILBP P51162 AFSGKYEFESEKNYDEFMKRLGLPGDVIERGRNFKIITEVQQDGQDFTWSQSYSGGNIMSNKFTIGKECEMQTMGGKKFKATVKMEGGKVVAEFPNYHQTSEVVGDKLVEISTIGDVTYERVSKRLA 127 FUNCTION: Ileal protein which stimulates gastric acid and pepsinogen secretion. Seems to be able to bind to bile salts and bilirubins. A1Ac 1460.27 "A,85;" 117 100 uniprot_mouse_length brain_HCD 547.206604 546.516907 546.513883 27 14721.86072 5.532774876 FABPH_MOUSE "Fatty acid-binding protein, heart;AltName: Full=Fatty acid-binding protein 3;AltName: Full=Heart-type fatty acid-binding protein; Short=H-FABP;AltName: Full=Mammary-derived growth inhibitor; Short=MDGI" P11404 ADAFVGTWKLVDSKNFDDYMKSLGVGFATRQVASMTKPTTIIEKNGDTITIKTQSTFKNTEINFQLGIEFDEVTADDRKVKSLVTLDGGKLIHVQKWNGQETTLTRELVDGKLILTLTHGSVVSTRTYEKEA 132 FUNCTION: FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. A1Ac 5427.59 "A,249;" 213 100 uniprot_mouse_length brain_HCD 887.9955444 885.523987 885.518861 17 15028.80426 5.788489248 FABPI_MOUSE "Fatty acid-binding protein, intestinal;AltName: Full=Fatty acid-binding protein 2;AltName: Full=Intestinal-type fatty acid-binding protein; Short=I-FABP" P55050 AFDGTWKVDRNENYEKFMEKMGINVMKRKLGAHDNLKLTITQDGNKFTVKESSNFRNIDVVFELGVNFPYSLADGTELTGAWTIEGNKLIGKFTRVDNGKELIAVREVSGNELIQTYTYEGVEAKRFFKKE 131 "FUNCTION: FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. FABP2 is probably involved in triglyceride-rich lipoprotein synthesis. Binds saturated long-chain fatty acids with a high affinity, but binds with a lower affinity to unsaturated long- chain fatty acids. FABP2 may also help maintain energy homeostasis by functioning as a lipid sensor. {ECO:0000269|PubMed:11023988}." A1Ac 1828.84 "A,86;" 133 100 uniprot_mouse_length brain_HCD 796.4220581 800.426086 800.416618 10 7991.16315 11.82937182 FCERG_MOUSE High affinity immunoglobulin epsilon receptor subunit gamma;AltName: Full=Fc receptor gamma-chain; Short=FcRgamma;AltName: Full=Fc-epsilon RI-gamma;AltName: Full=IgE Fc receptor subunit gamma; Short=FceRI gamma;Flags: Precursor P20491 LGEPQLCYILDAVLFLYGIVLTLLYCRLKIQVRKAAIASREKADAVYTGLNTRSQETYETLKHEKPPQ 68 "FUNCTION: Associates with a variety of FcR alpha chains to form a functional signaling complex. Regulates several aspects of the immune response. The gamma subunit has a critical role in allowing the IgE Fc receptor to reach the cell surface. Also involved in collagen-mediated platelet activation and in neutrophil activation mediated by integrin. {ECO:0000269|PubMed:17086186, ECO:0000269|PubMed:9171347}." Y47PY58PT60P 455.53 "Y,6;Y,0;T,0;" 49 100 uniprot_mouse_length brain_HCD 543.9406738 539.686401 539.692941 21 11306.54407 -12.11732138 FCOR_MOUSE Foxo1-corepressor; Short=FCoR; EC=2.3.1.-;AltName: Full=Foxo1 CoRepressor P0DJI6 MGGPTRRHQEEGSAECLGGPSTRAAPGPGLRDFHFTTAGPSKADRLGDAAQIHRERMRPVQCGDGSGERVFLQSPGSIGTLYIRLDLNSQRSTCCCLLNAGTKGMC 106 "FUNCTION: Regulator of adipocytes that acts by repressing FOXO1 transcriptional activity. Acts by promoting acetylation of FOXO1, both by preventing the interaction between FOXO1 and SIRT1 deacetylase, and by mediating acetyltransferase activity in vitro. Regulates insulin sensitivity and energy metabolism. {ECO:0000269|PubMed:22510882}." T93P 1130.67 "T,88;" 105 100 uniprot_mouse_length brain_HCD 614.25354 611.581177 611.58375 31 18918.07489 -4.20750582 FGF6_MOUSE Fibroblast growth factor 6; Short=FGF-6;AltName: Full=Heparin secretory-transforming protein 2; Short=HST-2; Short=HSTF-2;AltName: Full=Heparin-binding growth factor 6; Short=HBGF-6;Flags: Precursor P21658 SPAGARANGTLLDSRGWGTLLSRSRAGLAGEISGVNWESGYLVGIKRQRRLYCNVGIGFHLQVPPDGRISGTHEENPYSLLEISTVERGVVSLFGVKSALFIAMNSKGRLYTTPSFHDECKFRETLLPNNYNAYESDLYRGTYIALSKYGRVKRGSKVSPIMTVTHFLPRI 171 "FUNCTION: Plays an important role in the regulation of cell proliferation, cell differentiation, angiogenesis and myogenesis, and is required for normal muscle regeneration. {ECO:0000250}." null 5771.94 null null 100 uniprot_mouse_length brain_HCD 656.1295776 655.166992 655.161453 26 16999.17935 8.454690786 FIS1_MOUSE Mitochondrial fission 1 protein;AltName: Full=FIS1 homolog;AltName: Full=Tetratricopeptide repeat protein 11; Short=TPR repeat protein 11 Q9CQ92 MEAVLNELVSVEDLKNFERKFQSEQAAGSVSKSTQFEYAWCLVRSKYNEDIRRGIVLLEELLPKGSKEEQRDYVFYLAVGNYRLKEYEKALKYVRGLLQTEPQNNQAKELERLIDKAMKKDGLVGMAIVGGMALGVAGLAGLIGLAVSKSKS 152 "FUNCTION: Involved in the fragmentation of the mitochondrial network and its perinuclear clustering. Plays a minor role in the recruitment and association of the fission mediator dynamin- related protein 1 (DNM1L) to the mitochondrial surface and mitochondrial fission. May be not essential for the assembly of functional fission complexes and the subsequent membrane scission event. Can induce cytochrome c release from the mitochondrion to the cytosol, ultimately leading to apoptosis. Also mediates peroxisomal fission. {ECO:0000269|PubMed:23283981}." null 1256.36 null null 100 uniprot_mouse_length brain_HCD 708.65802 711.390198 711.382251 13 9230.96354 11.17086334 FM25C_MOUSE Protein FAM25C Q8CF02 MLGGLGKLAAEGLAHRTEKATEGAVHAVEEVVSEVVGHAKEVGEKAINDALKKAQESGDRVVKEVTEKVTHTITDAVTHAAEGLGRLGQ 89 "SIMILARITY: Belongs to the FAM25 family. {ECO:0000305}.-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" null 1256.02 null null 100 uniprot_mouse_length brain_HCD 544.784668 539.950745 539.950654 40 21546.00094 0.167846646 FTMT_MOUSE "Ferritin, mitochondrial; EC=1.16.3.1;Flags: Precursor" Q9D5H4 ASVASSQDSTRPSRVRQNFHPDSEAAINRQINLELYASYVYLSMAYYFSRDDVALYNFSKYFLRQSLEEREHAEKLMKLQNQRGGRICLQDIKKPDKDDWECGLRAMECALLLEKNVNQSLLDLHTLASEKGDPHLCDFLETHYLHEQVKSIKELGDHVHNLVTMGAPAAGLAEYLFDKHTLGSESKH 188 "FUNCTION: Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation (By similarity). {ECO:0000250}." null 10194.31 null null 100 uniprot_mouse_length brain_HCD 572.0013428 575.603577 575.600084 30 17228.98377 6.067859011 FUND1_MOUSE FUN14 domain-containing protein 1 Q9DB70 MASRNPPPQDYESDDESYEVLDLTEYARRHHWWNRVFGHSSGPMVEKYSVATQIVMGGVTGWCAGFLFQKVGKLAATAVGGGFLLLQVASHSGYVQIDWKRVEKDVNKAKRQIKKRANKAAPEINNIIEEATDFIKQNIVISSGFVGGFLLGLAS 155 "FUNCTION: Acts as an activator of hypoxia-induced mitophagy, an important mechanism for mitochondrial quality control. {ECO:0000250}." S13P 1012.37 "S,2;" 112 100 uniprot_mouse_length brain_HCD 592.4359741 594.470581 594.468233 29 17201.56139 3.949840474 GA45G_MOUSE Growth arrest and DNA damage-inducible protein GADD45 gamma;AltName: Full=Cytokine-responsive protein CR6 Q9Z111 MTLEEVRGQDTVPESTARMQGAGKALHELLLSAHGQGCLTAGVYESAKVLNVDPDNVTFCVLAADEEDEGDIALQIHFTLIQAFCCENDIDIVRVGDVQRLAAIVGADEEGGAPGDLHCILISNPNEDTWKDPALEKLSLFCEESRSFNDWVPSITLPE 159 FUNCTION: Involved in the regulation of growth and apoptosis. Mediates activation of stress-responsive MTK1/MEKK4 MAPKKK. null 6176.68 null null 100 uniprot_mouse_length brain_HCD 547.206604 543.018005 543.013836 25 13543.3324 7.678204159 GALA_MOUSE Galanin peptides;Contains: Galanin;Contains: Galanin message-associated peptide; Short=GMAP;Flags: Precursor P47212 MARGSVILLGWLLLVVTLSATLGLGMPAKEKRGWTLNSAGYLLGPHAIDNHRSFSDKHGLTGKRELQLEVEERRPGSVDVPLPESNIVRTIMEFLSFLHLKEAGALDSLPGIPLATSSEDLEKS 124 "FUNCTION: Contracts smooth muscle of the gastrointestinal and genitourinary tract, regulates growth hormone release, modulates insulin release, and may be involved in the control of adrenal secretion." S118P 4859.97 "S,222;" 184 100 uniprot_mouse_length brain_HCD 959.1802979 963.477051 963.480397 8 7696.84105 -3.473053277 GBG12_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12;Flags: Precursor Q9DAS9 SSKTASTNSIAQARRTVQQLRLEASIERIKVSKASADLMSYCEEHARSDPLLMGIPTSENPFKDKKTC 68 "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction." S25PS48PC68Me 205.65 "S,10;S,5;C,16;" 33 100 uniprot_mouse_length brain_HCD 668.0958252 668.262085 668.254993 12 8003.05656 10.61265686 GBG3_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-3;Flags: Precursor P63216 MKGETPVNSTMSIGQARKMVEQLKIEASLCRIKVSKAAADLMTYCDAHACEDPLITPVPTSENPFREKKFFC 72 "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction." null 578.63 null null 100 uniprot_mouse_length brain_HCD 544.784668 543.368042 543.364564 13 7047.73703 6.400844696 GBG7_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-7;Flags: Precursor Q61016 SGTNNVAQARKLVEQLRIEAGIERIKVSKASSDLMGYCEQHARNDPLLVGVPASENPFKDKKPC 64 "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction. Plays a role in the regulation of adenylyl cyclase signaling in certain regions of the brain. Plays a role in the formation or stabilzation of a G protein heterotrimer (G(olf) subunit alpha-beta-gamma-7) that is required for adenylyl cyclase activity in the striatum. {ECO:0000269|PubMed:12488442}." S1Ac 1230.1 "S,61;" 74 100 uniprot_mouse_length brain_HCD 592.4359741 592.113831 592.119031 31 18314.66984 -8.782750294 GKN2_MOUSE Gastrokine-2;AltName: Full=Blottin;Flags: Precursor Q9CQS6 EEIFNIFVPSKNGGNIQETVTIDNQQNTATINIHSGSCSSTTIFDYKHGYIASRVLSRRACYVIKMDHKAIPALDKLQRFLYEKQTMNAIDSPEYTWVRYNPLKSLITKVDWFLFGSPIRQLCKHMPLYEGEVATKPKEVSTGACAKVGLLGILGVSICGGIHL 164 "SUBUNIT: Heterodimer with TFF1; disulfide linked (By similarity). Interacts with TFF2. {ECO:0000250, ECO:0000269|PubMed:16888721}." null 7101.04 null null 100 uniprot_mouse_length brain_HCD 543.9406738 545.400085 545.392488 26 14147.19044 13.93024177 GLCM1_MOUSE Glycosylation-dependent cell adhesion molecule 1; Short=GlyCAM-1;AltName: Full=Endothelial ligand FOR L-selectin;AltName: Full=MC26;AltName: Full=SGP50;AltName: Full=Sulfated 50 kDa glycoprotein;Flags: Precursor Q02596 LPGSKDELQMKTQPTDAIPAAQSTPTSYTSEESTSSKDLSKEPSIFREELISKDNVVIESTKPENQEAQDGLRSGSSQLEETTRPTTSAATTSEENLTKSSQTVEEELGKIIEGFVTGAEDIISGASRITKS 132 FUNCTION: Adhesion molecule that accomplishes cell binding by presenting carbohydrate(s) to the lectin domain of L-selectin. null 2283.47 null null 100 uniprot_mouse_length brain_HCD 845.4489136 843.006836 843.003938 17 14307.05274 3.437632221 GLCM1_MOUSE Glycosylation-dependent cell adhesion molecule 1; Short=GlyCAM-1;AltName: Full=Endothelial ligand FOR L-selectin;AltName: Full=MC26;AltName: Full=SGP50;AltName: Full=Sulfated 50 kDa glycoprotein;Flags: Precursor Q02596 LPGSKDELQMKTQPTDAIPAAQSTPTSYTSEESTSSKDLSKEPSIFREELISKDNVVIESTKPENQEAQDGLRSGSSQLEETTRPTTSAATTSEENLTKSSQTVEEELGKIIEGFVTGAEDIISGASRITKS 132 FUNCTION: Adhesion molecule that accomplishes cell binding by presenting carbohydrate(s) to the lectin domain of L-selectin. S35PS40P 1254.45 "S,4;S,0;" 100 100 uniprot_mouse_length brain_HCD 614.25354 609.413452 609.41079 22 13378.02391 4.36839728 GLRX5_MOUSE "Glutaredoxin-related protein 5, mitochondrial;AltName: Full=Monothiol glutaredoxin-5;Flags: Precursor" Q80Y14 ASSGGQAEQLDALVKKDKVVVFLKGTPEQPQCGFSNAVVQILRLHGVRDYAAYNVLDDPELRQGIKDYSNWPTIPQVYLNGEFVGGCDILLQMHQNGDLVEELKKLGIRSALVDEKDQDSK 121 FUNCTION: Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters. Required for normal iron homeostasis. Required for normal regulation of hemoglobin synthesis by the iron-sulfur protein ACO1. May protect cells against apoptosis due to reactive oxygen species and oxidative stress. {ECO:0000269|PubMed:19442627}. null 3276.64 null null 100 uniprot_mouse_length brain_HCD 544.1685791 543.042297 543.040338 47 25462.86852 3.608135794 GSTA1_MOUSE "Glutathione S-transferase A1; EC=2.5.1.18;AltName: Full=GST class-alpha member 1;AltName: Full=Glutathione S-transferase Ya;AltName: Full=Glutathione S-transferase Ya1;Contains: Glutathione S-transferase A1, N-terminally processed" P13745 AGKPVLHYFNARGRMECIRWLLAAAGVEFEEKFIQSPEDLEKLKKDGNLMFDQVPMVEIDGMKLAQTRAILNYIATKYDLYGKDMKERALIDMYSEGILDLTEMIGQLVLCPPDQREAKTALAKDRTKNRYLPAFEKVLKSHGQDYLVGNRLTRVDIHLLEVLLYVEEFDASLLTPFPLLKAFKSRISSLPNVKKFLQPGSQRKPPMDAKQIQEARKAFKIQ 222 FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. null 14647.84 null null 100 uniprot_mouse_length brain_HCD 893.4779663 891.385376 891.398597 14 12459.57141 -14.83177501 GUC2A_MOUSE Guanylin;AltName: Full=Guanylate cyclase activator 2A;Flags: Precursor P33680 MNACVLSVLCLLGALAVLVEGVTVQDGDLSFPLESVKKLKGLREVQEPRLVSHKKFAPRLLQPVAPQLCSSHSALPEALRPVCEKPNAEEILQRLEAIAQDPNTCEICAYAACTGC 116 FUNCTION: Endogenous activator of intestinal guanylate cyclase. It stimulates this enzyme through the same receptor binding region as the heat-stable enterotoxins. null 1042.52 null null 100 uniprot_mouse_length brain_HCD 960.328064 964.864746 964.860374 22 21193.90269 4.531322736 H12_MOUSE Histone H1.2;AltName: Full=H1 VAR.1;AltName: Full=H1c P15864 SEAAPAAPAAAPPAEKAPAKKKAAKKPAGVRRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGILVQTKGTGASGSFKLNKKAASGEAKPQAKKAGAAKAKKPAGAAKKPKKATGAATPKKAAKKTPKKAKKPAAAAVTKKVAKSPKKAKVTKPKKVKSASKAVKPKAAKPKVAKAKKVAAKKK 211 "FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250}." S1AcK25MeK26Me 1157.24 "S,3;K,1;K,0;" 144 100 uniprot_mouse_length brain_HCD 544.784668 541.23938 541.237735 26 14039.16699 3.039113325 H2A1K_MOUSE Histone H2A type 1-K Q8CGP7 SGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTETHHKAKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." R3dMe 3725.09 "R,185;" 179 100 uniprot_mouse_length brain_HCD 589.013855 586.8479 586.839364 24 14053.13063 14.54638381 H2A1K_MOUSE Histone H2A type 1-K Q8CGP7 SGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTETHHKAKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1Ac 5976.15 "S,0;" 200 100 uniprot_mouse_length brain_HCD 544.784668 542.859009 542.853527 26 14081.17756 10.09809974 H2A1K_MOUSE Histone H2A type 1-K Q8CGP7 SGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTETHHKAKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1AcR3dMe 4127.56 "S,1;R,193;" 177 100 uniprot_mouse_length brain_HCD 545.2867432 543.399048 543.392591 26 14095.19322 11.88247994 H2A1K_MOUSE Histone H2A type 1-K Q8CGP7 SGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTETHHKAKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1AcR3dMeQ104Me 4742 "S,1;R,219;Q,239;" 200 100 uniprot_mouse_length brain_HCD 876.5581665 878.881165 878.879158 16 14039.05241 2.283079264 H2A3_MOUSE Histone H2A type 3 Q8BFU2 SGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1AcQ104Me 1781.15 "S,0;Q,96;" 122 100 uniprot_mouse_length brain_HCD 589.013855 586.8479 586.839364 24 14053.13063 14.54638381 H2A3_MOUSE Histone H2A type 3 Q8BFU2 SGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1AcR3dMe 5607.41 "S,0;R,182;" 186 100 uniprot_mouse_length brain_HCD 544.1685791 541.205383 541.199142 26 14038.16389 11.53235528 H2AJ_MOUSE Histone H2A.J; Short=H2a/j Q8R1M2 MSGRGKQGGKVRAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESQKVKSK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." null 5172.45 null null 100 uniprot_mouse_length brain_HCD 547.206604 544.972961 544.969789 26 14136.20066 5.821287428 H2AJ_MOUSE Histone H2A.J; Short=H2a/j Q8R1M2 MSGRGKQGGKVRAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESQKVKSK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." K6AcK10AcQ105Me 4938.41 "K,4;K,6;Q,240;" 196 100 uniprot_mouse_length brain_HCD 544.1685791 540.090759 540.094892 28 15087.64271 -7.651845476 H2AX_MOUSE Histone H2AX; Short=H2a/x;AltName: Full=Histone H2A.X P27661 SGRGKTGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGHYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGGVTIAQGGVLPNIQAVLLPKKSSATVGPKAPAVGKKASQASQEY 142 "FUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Required for checkpoint-mediated arrest of cell cycle progression in response to low doses of ionizing radiation and for efficient repair of DNA double strand breaks (DSBs) specifically when modified by C- terminal phosphorylation. {ECO:0000269|PubMed:11740565, ECO:0000269|PubMed:11934988, ECO:0000269|PubMed:12034884, ECO:0000269|PubMed:12447390, ECO:0000269|PubMed:12660252, ECO:0000269|PubMed:12689589, ECO:0000269|PubMed:12792649, ECO:0000269|PubMed:12914700, ECO:0000269|PubMed:12914701, ECO:0000269|PubMed:14530383, ECO:0000269|PubMed:15574327, ECO:0000269|PubMed:15580272, ECO:0000269|PubMed:15589157, ECO:0000269|PubMed:15610743, ECO:0000269|PubMed:15632067}." S1AcK5Ac 6335.39 "S,2;K,0;" 227 100 uniprot_mouse_length brain_HCD 544.784668 541.592896 541.59527 28 15129.65327 -4.38425577 H2AX_MOUSE Histone H2AX; Short=H2a/x;AltName: Full=Histone H2A.X P27661 SGRGKTGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGHYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGGVTIAQGGVLPNIQAVLLPKKSSATVGPKAPAVGKKASQASQEY 142 "FUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Required for checkpoint-mediated arrest of cell cycle progression in response to low doses of ionizing radiation and for efficient repair of DNA double strand breaks (DSBs) specifically when modified by C- terminal phosphorylation. {ECO:0000269|PubMed:11740565, ECO:0000269|PubMed:11934988, ECO:0000269|PubMed:12034884, ECO:0000269|PubMed:12447390, ECO:0000269|PubMed:12660252, ECO:0000269|PubMed:12689589, ECO:0000269|PubMed:12792649, ECO:0000269|PubMed:12914700, ECO:0000269|PubMed:12914701, ECO:0000269|PubMed:14530383, ECO:0000269|PubMed:15574327, ECO:0000269|PubMed:15580272, ECO:0000269|PubMed:15589157, ECO:0000269|PubMed:15610743, ECO:0000269|PubMed:15632067}." S1AcK5AcK9Ac 5501.83 "S,1;K,0;K,0;" 214 100 uniprot_mouse_length brain_HCD 712.520752 711.84668 711.847213 20 14209.93084 -0.749195179 H2B1A_MOUSE "Histone H2B type 1-A;AltName: Full=Histone H2B, testis;AltName: Full=Testis-specific histone H2B" P70696 PEVAVKGATISKKGFKKAVTKTQKKEGRKRKRCRKESYSIYIYKVLKQVHPDTGISSKAMSIMNSFVTDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 126 "FUNCTION: Variant histone specifically required to direct the transformation of dissociating nucleosomes to protamine in male germ cells. Entirely replaces classical histone H2B prior nucleosome to protamine transition and probably acts as a nucleosome dissociating factor that creates a more dynamic chromatin, facilitating the large-scale exchange of histones. Also expressed maternally and is present in the female pronucleus, suggesting a similar role in protamine replacement by nucleosomes at fertilization. Also found in fat cells, its function and the presence of post-translational modifications specific to such cells are still unclear. Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. {ECO:0000269|PubMed:23884607}." P1AcK6AcK58dMe 1701.53 "P,0;K,0;K,11;" 84 100 uniprot_mouse_length brain_HCD 712.520752 711.84668 711.849033 20 14209.96722 -3.305915146 H2B1A_MOUSE "Histone H2B type 1-A;AltName: Full=Histone H2B, testis;AltName: Full=Testis-specific histone H2B" P70696 PEVAVKGATISKKGFKKAVTKTQKKEGRKRKRCRKESYSIYIYKVLKQVHPDTGISSKAMSIMNSFVTDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 126 "FUNCTION: Variant histone specifically required to direct the transformation of dissociating nucleosomes to protamine in male germ cells. Entirely replaces classical histone H2B prior nucleosome to protamine transition and probably acts as a nucleosome dissociating factor that creates a more dynamic chromatin, facilitating the large-scale exchange of histones. Also expressed maternally and is present in the female pronucleus, suggesting a similar role in protamine replacement by nucleosomes at fertilization. Also found in fat cells, its function and the presence of post-translational modifications specific to such cells are still unclear. Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. {ECO:0000269|PubMed:23884607}." P1AcK58dMeK86tMe 1860.42 "P,0;K,19;K,117;" 75 100 uniprot_mouse_length brain_HCD 603.3545532 604.600769 604.596323 23 13875.70177 7.353738023 H2B1C_MOUSE Histone H2B type 1-C/E/G Q6ZWY9 PEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S14PK46MeR86Me 291.77 "S,3;K,10;R,0;" 56 100 uniprot_mouse_length brain_HCD 984.005127 988.049194 988.048117 14 13811.65998 1.090367887 H2B1F_MOUSE Histone H2B type 1-F/J/L;AltName: Full=H2B 291A P10853 PEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." K46Me 215.7 "K,7;" 36 100 uniprot_mouse_length brain_HCD 771.4325562 774.147766 774.154341 18 13909.76442 -8.492992121 H2B1F_MOUSE Histone H2B type 1-F/J/L;AltName: Full=H2B 291A P10853 PEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." P1AcK57dMeK85tMe 564.28 "P,1;K,13;K,56;" 77 100 uniprot_mouse_length brain_HCD 603.3545532 604.600769 604.596323 23 13875.70177 7.353738023 H2B1H_MOUSE Histone H2B type 1-H;AltName: Full=h2B-221 Q64478 PEPAKSAPAPKKGSKKALTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S14PK46Me 308.97 "S,6;K,9;" 51 100 uniprot_mouse_length brain_HCD 603.3545532 604.600769 604.596323 23 13875.70177 7.353738023 H2B1K_MOUSE Histone H2B type 1-K Q8CGP1 PEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S14PK46Me 308.97 "S,3;K,11;" 53 100 uniprot_mouse_length brain_HCD 771.4325562 774.147766 774.154341 18 13909.76442 -8.492992121 H2B1P_MOUSE Histone H2B type 1-P Q8CGP2 PEPVKSVPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." P1AcK46Me 583.4 "P,1;K,19;" 54 100 uniprot_mouse_length brain_HCD 771.4325562 774.147766 774.156363 18 13909.80082 -11.10484539 H2B1P_MOUSE Histone H2B type 1-P Q8CGP2 PEPVKSVPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." K46MeK57dMeR86Me 548.41 "K,16;K,11;R,0;" 46 100 uniprot_mouse_length brain_HCD 603.3545532 604.600769 604.596323 23 13875.70177 7.353738023 H2B2B_MOUSE Histone H2B type 2-B;AltName: Full=H2b 616 Q64525 PDPAKSAPAPKKGSKKAVTKVQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S14PK46Me 298.64 "S,6;K,9;" 51 100 uniprot_mouse_length brain_HCD 744.7387085 745.184753 745.184997 9 6694.66241 -0.326874578 68MP_MOUSE 6.8 kDa mitochondrial proteolipid P56379 MFQTLIQKVWVPMKPYYTQVYQEIWVGVGLMSLIVYKIRSADKRSKALKGPAPAHGHH 58 "SUBUNIT: Component of an ATP synthase complex composed of ATP5F1, ATP5G1, ATP5E, ATP5H, ATP5I, ATP5J, ATP5J2, MT-ATP6, MT-ATP8, ATP5A1, ATP5B, ATP5D, ATP5C1, ATP5O, ATP5L, USMG5 and MP68. {ECO:0000250}." null 1562.42 null null 100 uniprot_mouse_length brain_HCD 915.7252808 913.029541 913.017172 11 10028.18304 13.54740744 ACBP_MOUSE Acyl-CoA-binding protein; Short=ACBP;AltName: Full=Diazepam-binding inhibitor; Short=DBI;AltName: Full=Endozepine; Short=EP P31786 SQAEFDKAAEEVKRLKTQPTDEEMLFIYSHFKQATVGDVNTDRPGLLDLKGKAKWDSWNKLKGTSKESAMKTYVEKVDELKKKYGI 86 FUNCTION: Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA receptor. S1AcK7AcY28P 973.1 "S,1;K,0;Y,59;" 76 100 uniprot_mouse_length brain_HCD 632.9086304 635.019592 635.020746 9 5704.18634 -1.816814413 ATP5E_MOUSE "ATP synthase subunit epsilon, mitochondrial; Short=ATPase subunit epsilon" P56382 VAYWRQAGLSYIRFSQICAKAVRDALKTEFKANAEKTSGSSIKIVKVSKKE 51 "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits (By similarity). {ECO:0000250}." null 346.48 null null 100 uniprot_mouse_length brain_HCD 895.1591797 895.461853 895.461714 10 8940.61138 0.15525772 ATP5J_MOUSE "ATP synthase-coupling factor 6, mitochondrial; Short=ATPase subunit F6;Flags: Precursor" P97450 NKELDPVQKLFVDKIREYKSKRQASGGPVDIGPEYQQDLDRELYKLKQMYGKGEMDTFPTFKFDDPKFEVIDKPQS 76 "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. Also involved in the restoration of oligomycin-sensitive ATPase activity to depleted F1-F0 complexes." null 1783.9 null null 100 uniprot_mouse_length brain_HCD 960.3287354 964.478149 964.475752 23 22147.91696 2.4857173 BAD_MOUSE Bcl2-associated agonist of cell death; Short=BAD;AltName: Full=Bcl-2-binding component 6;AltName: Full=Bcl-xL/Bcl-2-associated death promoter;AltName: Full=Bcl2 antagonist of cell death Q61337 MGTPKQPSLAPAHALGLRKSDPGIRSLGSDAGGRRWRPAAQSMFQIPEFEPSEQEDASATDRGLGPSLTEDQPGPYLAPGLLGSNIHQQGRAATNSHHGGAGAMETRSRHSSYPAGTEEDEGMEEELSPFRGRSRSAPPNLWAAQRYGRELRRMSDEFEGSFKGLPRPKSAGTATQMRQSAGWTRIIQSWWDRNLGKGGSTPSQ 204 "FUNCTION: Promotes cell death. Successfully competes for the binding to Bcl-X(L), Bcl-2 and Bcl-W, thereby affecting the level of heterodimerization of these proteins with BAX. Can reverse the death repressor activity of Bcl-X(L), but not that of Bcl-2. Appears to act as a link between growth factor receptor signaling and the apoptotic pathways." S112P 2069.56 "S,15;" 179 100 uniprot_mouse_length brain_HCD 911.2014771 911.271301 911.281381 11 10008.08798 -11.0610517 BAF_MOUSE "Barrier-to-autointegration factor;AltName: Full=Breakpoint cluster region protein 1;AltName: Full=LAP2-binding protein 1;Contains: Barrier-to-autointegration factor, N-terminally processed" O54962 TTSQKHRDFVAEPMGEKPVGSLAGIGDVLSKRLEERGFDKAYVVLGQFLVLKKDEDLFREWLKDTCGANAKQSRDCFGCLREWCDAFL 88 "FUNCTION: Plays fundamental roles in nuclear assembly, chromatin organization, gene expression and gonad development. May potently compress chromatin structure and be involved in membrane recruitment and chromatin decondensation during nuclear assembly. Contains 2 non-specific dsDNA-binding sites which may promote DNA cross-bridging (By similarity). {ECO:0000250}." T1Ac 312.51 "T,20;" 33 100 uniprot_mouse_length brain_HCD 642.4682007 640.286865 640.284798 22 14057.25204 3.228616986 BATF_MOUSE Basic leucine zipper transcriptional factor ATF-like;AltName: Full=B-cell-activating transcription factor; Short=B-ATF O35284 MPHSSDSSDSSFSRSPPPGKQDSSDDVRKVQRREKNRIAAQKSRQRQTQKADTLHLESEDLEKQNAALRKEIKQLTEELKYFTSVLSSHEPLCSVLASGTPSPPEVVYSAHAFHQPHISSPRFQP 125 "FUNCTION: AP-1 family transcription factor that controls the differentiation of lineage-specific cells in the immune system: specifically mediates the differentiation of T-helper 17 cells (Th17), follicular T-helper cells (TfH), CD8(+) dendritic cells and class-switch recombination (CSR) in B-cells. Acts via the formation of a heterodimer with JUNB that recognizes and binds DNA sequence 5'-TGA[CG]TCA-3'. The BATF-JUNB heterodimer also forms a complex with IRF4 (or IRF8) in immune cells, leading to recognition of AICE sequence (5'-TGAnTCA/GAAA-3'), an immune- specific regulatory element, followed by cooperative binding of BATF and IRF4 (or IRF8) and activation of genes. Controls differentiation of T-helper cells producing interleukin-17 (Th17 cells) by binding to Th17-associated gene promoters: regulates expression of the transcription factor RORC itself and RORC target genes such as IL17 (IL17A or IL17B). Also involved in differentiation of follicular T-helper cells (TfH) by directing expression of BCL6 and MAF. In B-cells, involved in class-switch recombination (CSR) by controlling the expression of both AICDA and of germline transcripts of the intervening heavy-chain region and constant heavy-chain region (I(H)-C(H)). Following infection, can participate in CD8(+) dendritic cell differentiation via interaction with IRF4 and IRF8 to mediate cooperative gene activation. Regulates effector CD8(+) T-cell differentiation by regulating expression of SIRT1. Following DNA damage, part of a differentiation checkpoint that limits self-renewal of hematopoietic stem cells (HSCs): up-regulated by STAT3, leading to differentiation of HSCs, thereby restricting self-renewal of HSCs. {ECO:0000269|PubMed:11466704, ECO:0000269|PubMed:12594265, ECO:0000269|PubMed:19578362, ECO:0000269|PubMed:20421391, ECO:0000269|PubMed:21572431, ECO:0000269|PubMed:22001828, ECO:0000269|PubMed:22385964, ECO:0000269|PubMed:22983707, ECO:0000269|PubMed:22992523, ECO:0000269|PubMed:22992524, ECO:0000269|PubMed:23021777}." null 6667.22 null null 100 uniprot_mouse_length brain_HCD 960.3287354 963.992981 963.990044 24 23098.73296 3.04666739 BL1S4_MOUSE Biogenesis of lysosome-related organelles complex 1 subunit 4; Short=BLOC-1 subunit 4;AltName: Full=Protein cappuccino homolog Q8VED2 MEEGPAVGTLSREVSTEEAEPLGAAWSGDSGHVSQSHSSASGPWDDDGPEDAPGRDLPLLRRAASGYASSLLPSAGPRPEVEALDASLEELLAKVDEFVGMLDMIRGDSSHVVGEGVPRIHAKAAEMRRIYGRIDKLEAFVRMIGSSVARMEEQVAKAEAELGTFPRAFRRLLHTISVPALFRSAPSGPQRAAYEPPVLFRTEDHFPGCGDRPQL 215 "FUNCTION: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking. {ECO:0000269|PubMed:16760431, ECO:0000269|PubMed:19546860, ECO:0000269|PubMed:21998198}." null 2148.87 null null 100 uniprot_mouse_length brain_HCD 672.4346313 674.732239 674.732365 11 7408.05321 -0.187082279 CASPE_MOUSE "Caspase-14; Short=CASP-14; EC=3.4.22.-;AltName: Full=Mini-ICE; Short=MICE;Contains: Caspase-14 subunit p17, mature form;Contains: Caspase-14 subunit p10, mature form;Contains: Caspase-14 subunit p20, intermediate form;Contains: Caspase-14 subunit p8, intermediate form;Flags: Precursor" O89094 RHDEKGSGFIQTLTDVFIHKKGSILELTEEITRLMANTEVMQEGKPRKVNPEVQSTLRKKLYLQ 64 "FUNCTION: Non-apoptotic caspase which is involved in epidermal differentiation. Seems to play a role in keratinocyte differentiation and is required for cornification (PubMed:18156206). Regulates maturation of the epidermis by proteolytically processing filaggrin (PubMed:21654840). In vitro is equally active on the synthetic caspase substrates WEHD-ACF and IETD-AFC. Involved in processing of prosaposin in the epidermis (PubMed:24872419). May be involved in retinal pigment epithelium cell barrier function (By similarity). {ECO:0000250|UniProtKB:P31944, ECO:0000269|PubMed:11175259, ECO:0000269|PubMed:17515931, ECO:0000269|PubMed:18156206, ECO:0000269|PubMed:21654840, ECO:0000269|PubMed:24872419}." null 413.95 null null 100 uniprot_mouse_length brain_HCD 718.6751709 716.894958 716.902286 11 7871.92286 -10.22106366 CCL5_MOUSE C-C motif chemokine 5;AltName: Full=MuRantes;AltName: Full=SIS-delta;AltName: Full=Small-inducible cytokine A5;AltName: Full=T-cell-specific protein RANTES;Flags: Precursor P30882 SPYGSDTTPCCFAYLSLALPRAHVKEYFYTSSKCSNLAVVFVTRRNRQVCANPEKKWVQEYINYLEMS 68 "FUNCTION: Chemoattractant for blood monocytes, memory T-helper cells and eosinophils. Causes the release of histamine from basophils and activates eosinophils. May activate several chemokine receptors including CCR1, CCR3, CCR4 and CCR5. May also be an agonist of the G protein-coupled receptor GPR75. Together with GPR75, may play a role in neuron survival through activation of a downstream signaling pathway involving the PI3, Akt and MAP kinases. By activating GPR75 may also play a role in insulin secretion by islet cells. {ECO:0000250|UniProtKB:P13501}." null 525.33 null null 100 uniprot_mouse_length brain_HCD 642.4682007 639.059753 639.064757 22 14030.41138 -7.829538363 CHRC1_MOUSE Chromatin accessibility complex protein 1; Short=CHRAC-1;AltName: Full=DNA polymerase epsilon subunit p15;AltName: Full=NF-YC-like protein;AltName: Full=YC-like protein 1; Short=YCL1 Q9JKP8 ADAAVGKEKCGDQRLVSLPLSRIRVIMKSSPEVSSINQEALVLTAKATELFVQYLATCSYRHGSGKAKKALTYSDLASTAEDSETLQFLADILPKKILASKYLKMLKEKREEEEDNEDDGSDLGEALA 128 "FUNCTION: Forms a complex with DNA polymerase epsilon subunit POLE3 and binds naked DNA, which is then incorporated into chromatin, aided by the nucleosome remodeling activity of ISWI/SNF2H and ACF1. {ECO:0000250}." A1Ac 6039.72 "A,116;" 189 100 uniprot_mouse_length brain_HCD 642.4682007 640.790161 640.790018 22 14068.36715 0.223369292 CHRC1_MOUSE Chromatin accessibility complex protein 1; Short=CHRAC-1;AltName: Full=DNA polymerase epsilon subunit p15;AltName: Full=NF-YC-like protein;AltName: Full=YC-like protein 1; Short=YCL1 Q9JKP8 ADAAVGKEKCGDQRLVSLPLSRIRVIMKSSPEVSSINQEALVLTAKATELFVQYLATCSYRHGSGKAKKALTYSDLASTAEDSETLQFLADILPKKILASKYLKMLKEKREEEEDNEDDGSDLGEALA 128 "FUNCTION: Forms a complex with DNA polymerase epsilon subunit POLE3 and binds naked DNA, which is then incorporated into chromatin, aided by the nucleosome remodeling activity of ISWI/SNF2H and ACF1. {ECO:0000250}." S121P 6202.76 "S,184;" 178 100 uniprot_mouse_length brain_HCD 676.8179932 675.256409 675.256845 21 14152.38047 -0.646137239 CHRC1_MOUSE Chromatin accessibility complex protein 1; Short=CHRAC-1;AltName: Full=DNA polymerase epsilon subunit p15;AltName: Full=NF-YC-like protein;AltName: Full=YC-like protein 1; Short=YCL1 Q9JKP8 ADAAVGKEKCGDQRLVSLPLSRIRVIMKSSPEVSSINQEALVLTAKATELFVQYLATCSYRHGSGKAKKALTYSDLASTAEDSETLQFLADILPKKILASKYLKMLKEKREEEEDNEDDGSDLGEALA 128 "FUNCTION: Forms a complex with DNA polymerase epsilon subunit POLE3 and binds naked DNA, which is then incorporated into chromatin, aided by the nucleosome remodeling activity of ISWI/SNF2H and ACF1. {ECO:0000250}." A1AcK101AcS121P 5353.45 "A,102;K,143;S,159;" 178 100 uniprot_mouse_length brain_HCD 646.5813599 646.297302 646.290212 25 16124.23975 10.97068463 CHSP1_MOUSE Calcium-regulated heat stable protein 1;AltName: Full=Calcium-regulated heat-stable protein of 24 kDa; Short=CRHSP-24 Q9CR86 SSEPPPPPLQPPTHQTSVGLLDTPRTRDRSPSPLRGNVVPSPLPTRRTRTFSATVRASQGPVYKGVCKCFCRSKGHGFITPADGGPDIFLHISDVEGEYVPVEGDEVTYKMCSIPPKNEKLQAVEVVITHLAPGTKHETWSGHVISN 147 FUNCTION: Binds mRNA and regulates the stability of target mRNA. {ECO:0000269|PubMed:21078874}. S1AcS30PS32P 1978.41 "S,109;S,0;S,0;" 149 100 uniprot_mouse_length brain_HCD 1104.231079 1100.197754 1100.204126 11 12085.23526 -5.791737733 CISD1_MOUSE CDGSH iron-sulfur domain-containing protein 1;AltName: Full=MitoNEET Q91WS0 GLSSNSAVRVEWIAAVTFAAGTAALGYLAYKKFYAKENRTKAMVNLQIQKDNPKVVHAFDMEDLGDKAVYCRCWRSKKFPFCDGAHIKHNEETGDNVGPLIIKKKET 107 FUNCTION: Plays a key role in regulating maximal capacity for electron transport and oxidative phosphorylation. May be involved in Fe-S cluster shuttling and/or in redox reactions (By similarity). {ECO:0000250}. K54AcK67AcK103Ac 1016.01 "K,2;K,0;K,4;" 65 100 uniprot_mouse_length brain_HCD 646.1047974 650.195496 650.189918 22 14275.16548 8.578425033 CK052_MOUSE Uncharacterized protein C11orf52 homolog Q9D8L0 MGNRLCCGGTWSCPSTFQKKSKTGSHPRPTLSILKQQQLWQNGTKDYETTAPTYEQVLYPPASQKKTSNSTSEESDLHYADIHVLRQIRPHSLHTVKCLHSESATEYATLRFPQATPQYDSNNGTLV 127 "ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9D8L0-1; Sequence=Displayed; Name=2; IsoId=Q9D8L0-2; Sequence=VSP_021875;-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" null 5936.89 null null 100 uniprot_mouse_length brain_HCD 547.2418823 546.948792 546.951823 18 9822.12491 -5.542528549 CKS2_MOUSE Cyclin-dependent kinases regulatory subunit 2; Short=CKS-2 P56390 AHKQIYYSDKYFDEHYEYRHVMLPRELSKQVPKTHLMSEEEWRRLGVQQSLGWVHYMIHEPEPHILLFRRPLPKEQQK 78 FUNCTION: Binds to the catalytic subunit of the cyclin dependent kinases and is essential for their biological function. A1AcK3Ac 397.11 "A,0;K,4;" 52 100 uniprot_mouse_length brain_HCD 748.7203369 753.304382 753.313183 12 9023.75285 -11.68262547 CNCG_MOUSE "Retinal cone rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma; Short=GMP-PDE gamma; EC=3.1.4.35" P61249 MSDSPSLSPPAPSQGPTTPRKGPPKFKQRQTRQFKSKPPKKGVKGFGDDIPGMEGLGTDITVICPWEAFSHLELHELAQFGII 83 FUNCTION: Participates in processes of transmission and amplification of the visual signal. cGMP-PDEs are the effector molecules in G-protein-mediated phototransduction in vertebrate rods and cones. null 1501.18 null null 100 uniprot_mouse_length brain_HCD 805.1765137 804.012939 804.015141 12 9632.1763 -2.738190816 CNRG_MOUSE "Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma; Short=GMP-PDE gamma; EC=3.1.4.35" P09174 MNLEPPKGEIRSATRVIGGPVTPRKGPPKFKQRQTRQFKSKPPKKGVQGFGDDIPGMEGLGTDITVICPWEAFNHLELHELAQYGII 87 FUNCTION: Participates in processes of transmission and amplification of the visual signal. cGMP-PDEs are the effector molecules in G-protein-mediated phototransduction in vertebrate rods and cones. null 1609.64 null null 100 uniprot_mouse_length brain_HCD 695.5459595 698.363831 698.373827 17 11849.34428 -14.31387204 COA3_MOUSE "Cytochrome c oxidase assembly factor 3 homolog, mitochondrial;AltName: Full=Coiled-coil domain-containing protein 56" Q9D2R6 AAPGAGDPLNAKNGNAPFAQRIDPSREKLTPAQLQFMRQVQLAQWQKTLPQRRTRNIMTGLGIGALVLAIYGYTFYSVAQERFLDELEDEAKAARARALERERASGP 107 "FUNCTION: Component of some MITRAC complex, a cytochrome c oxidase (COX) assembly intermediate complex that regulates COX assembly. MITRAC complexes regulate both translation of mitochondrial encoded components and assembly of nuclear-encoded components imported in mitochondrion. Required for efficient translation of MT-CO1 and mitochondrial respiratory chain complex IV assembly (By similarity). {ECO:0000250}." null 905.15 null null 100 uniprot_mouse_length brain_HCD 822.7684326 820.762451 820.75207 12 9832.01744 12.64836515 COMD6_MOUSE COMM domain-containing protein 6 Q3V4B5 MEESGFREPVLDAKSEVTGQLIDFQWKLGMAVSSDSCRSLKYPYVAVMLKVADHSGQVSSKSIEMTIPQFQNFYKQFKEIAAVIETV 87 FUNCTION: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes. Inhibits TNF-induced NFKB1 activation. {ECO:0000250|UniProtKB:Q7Z4G1}. M1Ac 455.88 "M,21;" 45 100 uniprot_mouse_length brain_HCD 646.8552246 650.684753 650.690507 13 8441.97253 -8.842271355 CP074_MOUSE Uncharacterized protein C16orf74 homolog Q8K1L6 MGLKPSCLKGFKMCVSSSNNNHDEAPVLNDKHLSVPNIIITPPTPTGMGLSRDSNKQVWMDELGSYQDDGELEPEA 76 "SEQUENCE CAUTION: Sequence=AAH27666.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; Sequence=BAE43181.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" T44PT46P 228.1 "T,1;T,0;" 32 100 uniprot_mouse_length brain_HCD 962.3794556 962.885071 962.886594 10 9614.86027 -1.581909259 CX6A1_MOUSE "Cytochrome c oxidase subunit 6A1, mitochondrial;AltName: Full=Cytochrome c oxidase polypeptide VIa-liver;Flags: Precursor" P43024 SSGAHGEEGSARMWKALTYFVALPGVGVSMLNVFLKSRHEEHERPPFVAYPHLRIRTKPFPWGDGNHTLFHNPHVNPLPTGYEDE 85 "FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport." null 2490.68 null null 100 uniprot_mouse_length brain_HCD 659.5177002 655.040283 655.032135 12 7845.38323 12.43939448 CXCL2_MOUSE C-X-C motif chemokine 2;AltName: Full=Macrophage inflammatory protein 2; Short=MIP2;Flags: Precursor P10889 AVVASELRCQCLKTLPRVDFKNIQSLSVTPPGPHCAQTEVIATLKGGQKVCLDPEAPLVQKIIQKILNKGKAN 73 FUNCTION: Chemotactic for human polymorphonuclear leukocytes but does not induce chemokinesis or an oxidative burst. null 677.58 null null 100 uniprot_mouse_length brain_HCD 640.5415039 636.141296 636.149912 17 10792.53992 -13.54336945 CYTA_MOUSE "Cystatin-A;AltName: Full=Cystatin-A1;AltName: Full=Stefin-A;Contains: Cystatin-A, N-terminally processed" P56567 IPGGLTEARPATAEVQEIADRVKAQLEEETNEKYEIFKAVEYKTQVVAGVNYFIKMDVGGGCFTHIKVFKDLSGKNNLELTGYQTNKTEDDELTYF 96 FUNCTION: This is an intracellular thiol proteinase inhibitor. {ECO:0000250}. null 475.53 null null 100 uniprot_mouse_length brain_HCD 714.3890991 713.77533 713.77487 10 7124.7474 0.643886277 DEFB4_MOUSE "Beta-defensin 4; Short=BD-4; Short=mBD-4;AltName: Full=Defensin, beta 4;Flags: Precursor" P82019 MRIHYLLFTFLLVLLSPLAAFTQIINNPITCMTNGAICWGPCPTAFRQIGNCGHFKVRCCKIR 63 FUNCTION: Has bactericidal activity. {ECO:0000250}. null 551.96 null null 100 uniprot_mouse_length brain_HCD 960.3249512 964.652771 964.654906 11 10595.19758 -2.213230755 DFA20_MOUSE Alpha-defensin 20;AltName: Full=Cryptdin-4;AltName: Full=Defensin-related cryptdin-20;Flags: Precursor Q45VN2 MKTLVLLSALVLLAFQVQADPIQNTDEETNTEEQPGEEDQAVSVSFGDPEGSALHEKSSRDLICYCRKGGCNRGEQVYGTCSGRLLFCCRRRHRH 95 FUNCTION: May have microbicidal activities. {ECO:0000250}. null 692.14 null null 100 uniprot_mouse_length brain_HCD 869.8977661 870.795349 870.805721 11 9562.85719 -11.91066923 DFB19_MOUSE "Beta-defensin 19; Short=BD-19; Short=mBD-19;AltName: Full=Defensin, beta 19;AltName: Full=Testis-specific beta-defensin-like protein;Flags: Precursor" Q8K3I8 MRLALLLLAILVATELVVSGKNPILQCMGNRGFCRSSCKKSEQAYFYCRTFQMCCLQSYVRISLTGVDDNTNWSYEKHWPRIP 83 FUNCTION: Has antibacterial activity. {ECO:0000250}. null 638.88 null null 100 uniprot_mouse_length brain_HCD 727.3667603 727.811707 727.817317 9 6538.35444 -7.70860613 DFB29_MOUSE "Beta-defensin 29; Short=BD-29; Short=mBD-29;AltName: Full=Defensin, beta 29;Flags: Precursor" Q8BGW9 GLFGFRSSKRQEPWIACELYQGLCRNACQKYEIQYLSCPKTRKCCLKYPRKITSF 55 FUNCTION: Has antibacterial activity. {ECO:0000250}. null 939.02 null null 100 uniprot_mouse_length brain_HCD 1090.382935 1090.982422 1090.982395 10 10894.81586 0.024633761 DLRB1_MOUSE "Dynein light chain roadblock-type 1;AltName: Full=Dynein light chain 2A, cytoplasmic" P62627 AEVEETLKRLQSQKGVQGIIVVNTEGIPIKSTMDNPTTTQYANLMHNFILKARSTVREIDPQNDLTFLRIRSKKNEIMVAPDKDYFLIVIQNPTE 95 FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. A1Ac 2417.12 "A,94;" 112 100 uniprot_mouse_length brain_HCD 630.1522827 628.559509 628.552709 18 11290.9403 10.81894525 DPY30_MOUSE Protein dpy-30 homolog;AltName: Full=Dpy-30-like protein; Short=Dpy-30L Q99LT0 MESEQMLEGQTQVAENPHSEYGLTDSVERIVENEKINAEKSSKQKVDLQSLPTRAYLDQTVVPILLQGLAVLAKERPPNPIEFLASYLLKNKAQFEDRN 99 "FUNCTION: As part of the MLL1/MLL complex, involved in the methylation of histone H3 at 'Lys-4', particularly trimethylation. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. May play some role in histone H3 acetylation. In embryonic stem (ES) cells, plays a crucial role in the differentiation potential, particularly along the neural lineage, regulating gene induction and histone H3 'Lys- 4' methylation at key developmental loci, including that mediated by retinoic acid. Does not affect ES cell self-renewal. May also play an indirect or direct role in endosomal transport. {ECO:0000269|PubMed:21335234}." M1AcK35Ac 1821.47 "M,9;K,44;" 101 100 uniprot_mouse_length brain_HCD 737.1600342 741.265381 741.268016 18 13318.81348 -3.554909382 ENSA_MOUSE Alpha-endosulfine;AltName: Full=ARPP-19e P60840 SQKQEEENPAEETGEEKQDTQEKEGILPEKAEEAKLKAKYPSLGQKPGGSDFLMKRLQKGQKYFDSGDYNMAKAKMKNKQLPSAGADKNLVTGDHIPTPQDLPQRKSSLVTSKLAGGQVE 120 "FUNCTION: Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-67 during mitosis, specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, an essential condition to keep cyclin-B1-CDK1 activity high during M phase. Also acts as a stimulator of insulin secretion by interacting with sulfonylurea receptor (ABCC8), thereby preventing sulfonylurea from binding to its receptor and reducing K(ATP) channel currents (By similarity). {ECO:0000250}." S1AcS66P 1647.47 "S,90;S,0;" 119 100 uniprot_mouse_length brain_HCD 780.4085693 779.789978 779.795253 23 17903.27186 -6.764561128 F195A_MOUSE Protein FAM195A Q9CQB2 MYTITKGPSKLVAQRRTGPTQQQVESRLGELLKCRQPVPPTALPAHLQPSAQTQGPWPLASSGPRLVFNRVNGRRPLTTSPSLEGTQETYTVAHEENVRFVSEAWQQVERQLDGGPADESGPRPVQYVESTPDPRLQNFVPIDLDEWWAQQFLAKITNCS 160 "SIMILARITY: Belongs to the FAM195 family. {ECO:0000305}.-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" M1Ac 3011.92 "M,127;" 198 100 uniprot_mouse_length brain_HCD 741.9328003 743.846802 743.851462 15 11137.76373 -6.265017178 F195B_MOUSE Protein FAM195B Q3UGS4 MTSSPVSRVVYNGKRNSSPRSPTNSSEIFTPAHEENVRFIYEAWQGVERDLRSQLSSGERCLVEEYVEKVPNPSLKTFKPIDLSDLKRRNTQDAKKS 97 SIMILARITY: Belongs to the FAM195 family. {ECO:0000305}. K79Ac 1812.91 "K,94;" 91 100 uniprot_mouse_length brain_HCD 780.5516968 784.421387 784.423352 10 7831.23049 -2.505383407 FCERG_MOUSE High affinity immunoglobulin epsilon receptor subunit gamma;AltName: Full=Fc receptor gamma-chain; Short=FcRgamma;AltName: Full=Fc-epsilon RI-gamma;AltName: Full=IgE Fc receptor subunit gamma; Short=FceRI gamma;Flags: Precursor P20491 LGEPQLCYILDAVLFLYGIVLTLLYCRLKIQVRKAAIASREKADAVYTGLNTRSQETYETLKHEKPPQ 68 "FUNCTION: Associates with a variety of FcR alpha chains to form a functional signaling complex. Regulates several aspects of the immune response. The gamma subunit has a critical role in allowing the IgE Fc receptor to reach the cell surface. Also involved in collagen-mediated platelet activation and in neutrophil activation mediated by integrin. {ECO:0000269|PubMed:17086186, ECO:0000269|PubMed:9171347}." Y47P 320.58 "Y,9;" 34 100 uniprot_mouse_length brain_HCD 718.9760742 720.476929 720.473425 11 7911.20464 4.863067555 FCERG_MOUSE High affinity immunoglobulin epsilon receptor subunit gamma;AltName: Full=Fc receptor gamma-chain; Short=FcRgamma;AltName: Full=Fc-epsilon RI-gamma;AltName: Full=IgE Fc receptor subunit gamma; Short=FceRI gamma;Flags: Precursor P20491 LGEPQLCYILDAVLFLYGIVLTLLYCRLKIQVRKAAIASREKADAVYTGLNTRSQETYETLKHEKPPQ 68 "FUNCTION: Associates with a variety of FcR alpha chains to form a functional signaling complex. Regulates several aspects of the immune response. The gamma subunit has a critical role in allowing the IgE Fc receptor to reach the cell surface. Also involved in collagen-mediated platelet activation and in neutrophil activation mediated by integrin. {ECO:0000269|PubMed:17086186, ECO:0000269|PubMed:9171347}." Y47PY58P 1142.76 "Y,14;Y,0;" 69 100 uniprot_mouse_length brain_HCD 726.505249 726.169189 726.169244 9 6524.52282 -0.075115926 GALP_MOUSE Galanin-like peptide;Flags: Precursor Q810H5 APAHRGRGGWTLNSAGYLLGPVLPVSSKADQGRKRDSALEILDLWKIIDGLPYSHSPRMT 60 "FUNCTION: Isoform 1: Hypothalamic neuropeptide which binds to the G-protein-coupled galanin receptors (GALR1, GALR2 and GALR3). Involved in a large number of putative physiological functions in CNS homeostatic processes, including the regulation of gonadotropin-releasing hormone secretion." null 822.87 null null 100 uniprot_mouse_length brain_HCD 780.4085693 778.982239 778.983914 15 11663.74911 -2.150532814 GAST_MOUSE Gastrin;Contains: Gastrin-71; Short=G71;Contains: Big gastrin; AltName: Full=Gastrin-34; Short=G34;Contains: Gastrin;Flags: Precursor P48757 MPRLCVYMLVLVLALATFSEASWKPRSQLQDASSGPGTNEDLEQRQFNKLGSASHHRRQLGPQGPQHFIADLSKKQRPRMEEEEEAYGWMDFGRRSAEEDQ 101 FUNCTION: Gastrin stimulates the stomach mucosa to produce and secrete hydrochloric acid and the pancreas to secrete its digestive enzymes. It also stimulates smooth muscle contraction and increases blood circulation and water secretion in the stomach and intestine. S96P 871.56 "S,54;" 76 100 uniprot_mouse_length brain_HCD 861.3758545 865.946411 865.952301 8 6916.61619 -6.801606948 GBG5_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-5;Flags: Precursor Q80SZ7 SGSSSVAAMKKVVQQLRLEAGLNRVKVSQAAADLKQFCLQNAQHDPLLTGVSSSTNPFRPQKVC 64 "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction." S1P 281.22 "S,18;" 33 100 uniprot_mouse_length brain_HCD 589.0175781 586.220825 586.228049 12 7019.7343 -12.3225163 GBG7_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-7;Flags: Precursor Q61016 SGTNNVAQARKLVEQLRIEAGIERIKVSKASSDLMGYCEQHARNDPLLVGVPASENPFKDKKPC 64 "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction. Plays a role in the regulation of adenylyl cyclase signaling in certain regions of the brain. Plays a role in the formation or stabilzation of a G protein heterotrimer (G(olf) subunit alpha-beta-gamma-7) that is required for adenylyl cyclase activity in the striatum. {ECO:0000269|PubMed:12488442}." C64Me 1165.1 "C,50;" 62 100 uniprot_mouse_length brain_HCD 659.5933228 663.058167 663.049342 21 13896.02204 13.30897016 H2A1H_MOUSE Histone H2A type 1-H Q8CGP6 SGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAK 127 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1AcR3dMeQ104Me 571.82 "S,0;R,44;Q,55;" 67 100 uniprot_mouse_length brain_HCD 642.4682007 643.288818 643.2805 22 14123.15685 12.93115426 H2A1K_MOUSE Histone H2A type 1-K Q8CGP7 SGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTETHHKAKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1AcR3dMeK5Ac 5460.79 "S,0;R,196;K,0;" 180 100 uniprot_mouse_length brain_HCD 547.2418823 544.85791 544.851027 26 14133.11259 12.63309769 H2A1K_MOUSE Histone H2A type 1-K Q8CGP7 SGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTETHHKAKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1AcT120P 1907.17 "S,2;T,129;" 156 100 uniprot_mouse_length brain_HCD 714.3093872 710.111145 710.104518 20 14175.07624 9.332456509 H2A1K_MOUSE Histone H2A type 1-K Q8CGP7 SGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTETHHKAKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1AcK5AcT120P 1994.13 "S,2;K,0;T,89;" 127 100 uniprot_mouse_length brain_HCD 596.5247192 592.334534 592.33677 24 14185.06837 -3.775400595 H2A1K_MOUSE Histone H2A type 1-K Q8CGP7 SGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTETHHKAKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1PQ104MeT120P 1034.3 "S,59;Q,79;T,68;" 102 100 uniprot_mouse_length brain_HCD 876.7404175 877.989746 877.994627 16 14024.90027 -5.559152756 H2A2B_MOUSE Histone H2A type 2-B;AltName: Full=H2a-613A Q64522 SGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYMAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEELNKLLGGVTIAQGGVLPNIQAVLLPKKTESHKPGKNK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1AcR3dMeT120P 1873.27 "S,0;R,80;T,0;" 114 100 uniprot_mouse_length brain_HCD 547.2418823 544.85791 544.851027 26 14133.11259 12.63309769 H2A3_MOUSE Histone H2A type 3 Q8BFU2 SGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1AcR3dMeT120P 1827.39 "S,2;R,101;T,0;" 140 100 uniprot_mouse_length brain_HCD 684.2012939 685.20282 685.209068 22 15045.58521 -9.118641409 H2AX_MOUSE Histone H2AX; Short=H2a/x;AltName: Full=Histone H2A.X P27661 SGRGKTGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGHYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGGVTIAQGGVLPNIQAVLLPKKSSATVGPKAPAVGKKASQASQEY 142 "FUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Required for checkpoint-mediated arrest of cell cycle progression in response to low doses of ionizing radiation and for efficient repair of DNA double strand breaks (DSBs) specifically when modified by C- terminal phosphorylation. {ECO:0000269|PubMed:11740565, ECO:0000269|PubMed:11934988, ECO:0000269|PubMed:12034884, ECO:0000269|PubMed:12447390, ECO:0000269|PubMed:12660252, ECO:0000269|PubMed:12689589, ECO:0000269|PubMed:12792649, ECO:0000269|PubMed:12914700, ECO:0000269|PubMed:12914701, ECO:0000269|PubMed:14530383, ECO:0000269|PubMed:15574327, ECO:0000269|PubMed:15580272, ECO:0000269|PubMed:15589157, ECO:0000269|PubMed:15610743, ECO:0000269|PubMed:15632067}." S1Ac 5023 "S,1;" 191 100 uniprot_mouse_length brain_HCD 547.2418823 542.808655 542.806017 28 15163.55424 4.859535587 H2AX_MOUSE Histone H2AX; Short=H2a/x;AltName: Full=Histone H2A.X P27661 SGRGKTGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGHYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGGVTIAQGGVLPNIQAVLLPKKSSATVGPKAPAVGKKASQASQEY 142 "FUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Required for checkpoint-mediated arrest of cell cycle progression in response to low doses of ionizing radiation and for efficient repair of DNA double strand breaks (DSBs) specifically when modified by C- terminal phosphorylation. {ECO:0000269|PubMed:11740565, ECO:0000269|PubMed:11934988, ECO:0000269|PubMed:12034884, ECO:0000269|PubMed:12447390, ECO:0000269|PubMed:12660252, ECO:0000269|PubMed:12689589, ECO:0000269|PubMed:12792649, ECO:0000269|PubMed:12914700, ECO:0000269|PubMed:12914701, ECO:0000269|PubMed:14530383, ECO:0000269|PubMed:15574327, ECO:0000269|PubMed:15580272, ECO:0000269|PubMed:15589157, ECO:0000269|PubMed:15610743, ECO:0000269|PubMed:15632067}." S1PS139P 1709.83 "S,117;S,0;" 146 100 uniprot_mouse_length brain_HCD 733.921814 732.614929 732.613596 19 13893.64469 1.819784981 H2B1B_MOUSE Histone H2B type 1-B;AltName: Full=h2B-143 Q64475 PEPSKSAPAPKKGSKKAISKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S14P 453.56 "S,2;" 61 100 uniprot_mouse_length brain_HCD 816.6824951 812.928589 812.923658 17 13795.68852 6.06559686 H2B1C_MOUSE Histone H2B type 1-C/E/G Q6ZWY9 PEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." K46MeR86Me 946.16 "K,18;R,0;" 89 100 uniprot_mouse_length brain_HCD 740.5254517 736.721924 736.718178 19 13971.63174 5.084479027 H2B1F_MOUSE Histone H2B type 1-F/J/L;AltName: Full=H2B 291A P10853 PEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S14PS36PK46Me 1206.73 "S,7;S,0;K,22;" 110 100 uniprot_mouse_length brain_HCD 556.5960083 557.119263 557.126004 18 10005.26078 -12.10014366 ACBD7_MOUSE Acyl-CoA-binding domain-containing protein 7 Q9D258 MSLQADFDQAAQDVRKLKSRPEDEELKELYGLYKQSVIGDINIACPAMLDLKGKAKWEAWNLQKGLSKEDAMCAYISKARELIEKYGI 88 FUNCTION: Binds medium- and long-chain acyl-CoA esters. {ECO:0000250}. null 788.67 null null 100 uniprot_mouse_length brain_HCD 762.9404297 766.233459 766.244875 13 9944.17755 -14.89801461 ACBP_MOUSE Acyl-CoA-binding protein; Short=ACBP;AltName: Full=Diazepam-binding inhibitor; Short=DBI;AltName: Full=Endozepine; Short=EP P31786 SQAEFDKAAEEVKRLKTQPTDEEMLFIYSHFKQATVGDVNTDRPGLLDLKGKAKWDSWNKLKGTSKESAMKTYVEKVDELKKKYGI 86 FUNCTION: Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA receptor. Y28P 981.85 "Y,38;" 71 100 uniprot_mouse_length brain_HCD 626.2931519 627.809753 627.810243 16 10023.9558 -0.779824854 AF1Q_MOUSE Protein AF1q P97783 MRDPVSSQYSSFLFWRMPIPELDLSELEGLGLSDTPTYESKDSSSVGKMNGQASGTEQKNPEGDPLLEYSTFNFWRAPIASIHSVDLDLL 90 TISSUE SPECIFICITY: Detected in embryonic brain cortex. {ECO:0000269|PubMed:15530661}. null 727.83 null null 100 uniprot_mouse_length brain_HCD 743.7529907 741.016785 741.016138 18 13313.27831 0.872677308 ANFC_MOUSE C-type natriuretic peptide;Contains: CNP-22;Contains: CNP-29;Contains: CNP-53;Flags: Precursor Q61839 MHLSQLIACALLLALLSLRPSEAKPGTPPKVPRTPPGEELADSQAAGGNQKKGDKTPGSGGANLKGDRSRLLRDLRVDTKSRAAWARLLHEHPNARKYKGGNKKGLSKGCFGLKLDRIGSMSGLGC 126 "FUNCTION: Hormone which plays a role in endochondral ossification through regulation of cartilaginous growth plate chondrocytes proliferation and differentiation. May also be vasoactive and natriuretic. Specifically binds and stimulates the cGMP production of the NPR2 receptor. Binds the clearance receptor NPR3. {ECO:0000269|PubMed:11259675, ECO:0000269|PubMed:12890708}." null 1096.3 null null 100 uniprot_mouse_length brain_HCD 585.0100098 587.094177 587.100971 34 19916.41021 -11.57169591 ARL5C_MOUSE ADP-ribosylation factor-like protein 5C;AltName: Full=ADP-ribosylation factor-like protein 12 Q6P068 GQLIAKLMRIFGSQEHKVIIVGLDNAGKTTILYQFLTNEVVHTCSTIGSNVEEIVLRKTHFLMWDLGGQEALRSTWDTYYSNAEFVILVIDSTDRNRLLTTREELYKMLAHEALQNASVLIFANKQDVKDSMTTAEISQFLTLSAIKDHPWHIQGCCALTGEGLPAGLQWMQAQATAN 178 FUNCTION: Binds and exchanges GTP and GDP. {ECO:0000250}. null 8798.75 null null 100 uniprot_mouse_length brain_HCD 679.3267822 678.96759 678.967933 18 12197.41216 -0.504689474 ARP19_MOUSE cAMP-regulated phosphoprotein 19; Short=ARPP-19 P56212 SAEVPEAASAEEQKEMEDKVTSPEKAEEAKLKARYPHLGQKPGGSDFLRKRLQKGQKYFDSGDYNMAKAKMKNKQLPAAAPDKTEVTGDHIPTPQDLPQRKPSLVASKLAG 111 "FUNCTION: Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-62 during mitosis, specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, an essential condition to keep cyclin-B1-CDK1 activity high during M phase. May indirectly enhance GAP-43 expression by binding to the NGF-regulatory region of its mRNA (By similarity). {ECO:0000250}." S1Ac 1524.68 "S,73;" 116 100 uniprot_mouse_length brain_HCD 734.6556396 736.728271 736.731806 22 16177.08365 -4.79756079 AT7L1_MOUSE Ataxin-7-like protein 1;AltName: Full=Ataxin-7-like protein 4 Q9CZ05 MTSERSRIPCLSAAAAEGTGKKQQEGTAMATLHRKVPSPEAFLGKPWSSWIDAAKLHCSDNVDLEEAGKEGGKSREVMRLNKEDMHLFGHYPAHDDFYLVVCSACNQVVKPQVFQSHCGRKQDSKRNASISWSGAESRQALEQRQV 146 ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9CZ05-1; Sequence=Displayed; Name=2; IsoId=Q9CZ05-2; Sequence=VSP_021186; Note=No experimental confirmation available.; null 3149.28 null null 100 uniprot_mouse_length brain_HCD 642.9816284 639.68988 639.688588 9 5746.1969 2.02031288 ATP5E_MOUSE "ATP synthase subunit epsilon, mitochondrial; Short=ATPase subunit epsilon" P56382 VAYWRQAGLSYIRFSQICAKAVRDALKTEFKANAEKTSGSSIKIVKVSKKE 51 "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits (By similarity). {ECO:0000250}." K20Ac 330.2 "K,5;" 30 100 uniprot_mouse_length brain_HCD 581.7000122 584.229797 584.222627 10 5830.22585 12.27334059 ATP5E_MOUSE "ATP synthase subunit epsilon, mitochondrial; Short=ATPase subunit epsilon" P56382 VAYWRQAGLSYIRFSQICAKAVRDALKTEFKANAEKTSGSSIKIVKVSKKE 51 "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits (By similarity). {ECO:0000250}." K20AcK31AcK36Ac 273.16 "K,4;K,0;K,0;" 28 100 uniprot_mouse_length brain_HCD 838.4515381 840.265076 840.270576 18 15099.85624 -6.545887198 ATPD_MOUSE "ATP synthase subunit delta, mitochondrial;AltName: Full=F-ATPase delta subunit;Flags: Precursor" Q9D3D9 AEAAAAPAPAAGPGQMSFTFASPTQVFFDSANVKQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHTEDGTTTKYFVSSGSVTVNADSSVQLLAEEAVTLDMLDLGAARANLEKAQSELSGAADEAARAEIQIRIEANEALVKALE 146 "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP turnover in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits." K114AcK143Ac 1551.68 "K,22;K,4;" 109 100 uniprot_mouse_length brain_HCD 685.5707397 687.089783 687.088522 32 21943.80708 1.834865237 BASP1_MOUSE Brain acid soluble protein 1;AltName: Full=22 kDa neuronal tissue-enriched acidic protein;AltName: Full=Neuronal axonal membrane protein NAP-22 Q91XV3 GGKLSKKKKGYNVNDEKAKDKDKKAEGAGTEEEGTPKESEPQAAADATEVKESTEEKPKDAADGEAKAEEKEADKAAAAKEEAPKAEPEKSEGAAEEQPEPAPAPEQEAAAPGPAAGGEAPKAGEASAESTGAADGAAPEEGEAKKTEAPAAAGPEAKSDAAPAASDSKPSSAEPAPSSKETPAASEAPSSAAKAPAPAAPAAAEPQAEAPAAAASSEQSVAVKE 225 "SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. Cell projection, growth cone. Note=Associated with the membranes of growth cones that form the tips of elongating axons." null 2614.88 null null 100 uniprot_mouse_length brain_HCD 642.46875 639.103516 639.112396 33 21046.68529 -13.89485645 BNIP3_MOUSE BCL2/adenovirus E1B 19 kDa protein-interacting protein 3 O55003 MSQSGEENLQGSWVELHFSNGNGSSVPASVSIYNGDMEKILLDAQHESGRSSSKSSHCDSPPRSQTPQDTNRAEIDSHSFGEKNSTLSEEDYIERRREVESILKKNSDWIWDWSSRPENIPPKEFLFKHPKRTATLSMRNTSVMKKGGIFSADFLKVFLPSLLLSHLLAIGLGIYIGRRLTTSTSTF 187 "FUNCTION: Apoptosis-inducing protein that can overcome BCL2 suppression. May play a role in repartitioning calcium between the two major intracellular calcium stores in association with BCL2 (By similarity). Involved in mitochondrial quality control via its interaction with SPATA18/MIEAP: in response to mitochondrial damage, participates in mitochondrial protein catabolic process (also named MALM) leading to the degradation of damaged proteins inside mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane may play a critical role in the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix (By similarity). The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix (By similarity). Plays an important role in the calprotectin (S100A8/A9)-induced cell death pathway (By similarity). {ECO:0000250}." S48P 4342.67 "S,4;" 223 100 uniprot_mouse_length brain_HCD 783.6868286 785.50824 785.501558 11 8625.51172 8.506343527 BRK1_MOUSE Protein BRICK1; Short=BRK1 Q91VR8 AGQEDPVQREIHQDWANREYIEIITSSIKKISDFLNSFDMSCRSRLATLNEKLTALERRIEYIEARVTKGETLT 74 FUNCTION: Involved in regulation of actin and microtubule organization. Part of a WAVE complex that activates the Arp2/3 complex (By similarity). {ECO:0000250}. null 459.83 null null 100 uniprot_mouse_length brain_HCD 723.3877563 723.632629 723.627962 12 8667.5301 6.449991952 BRK1_MOUSE Protein BRICK1; Short=BRK1 Q91VR8 AGQEDPVQREIHQDWANREYIEIITSSIKKISDFLNSFDMSCRSRLATLNEKLTALERRIEYIEARVTKGETLT 74 FUNCTION: Involved in regulation of actin and microtubule organization. Part of a WAVE complex that activates the Arp2/3 complex (By similarity). {ECO:0000250}. A1Ac 1711.66 "A,56;" 76 100 uniprot_mouse_length brain_HCD 774.8407593 775.091309 775.089314 22 17020.94715 2.573372789 BST2_MOUSE Bone marrow stromal antigen 2; Short=BST-2;AltName: Full=HM1.24 antigen;AltName: CD_antigen=CD317;Flags: Precursor Q8R2Q8 MAPSFYHYLPVPMDEMGGKQGWGSHRQWLGAAILVVLFGVTLVILTIYFAVTANSVACRDGLRAQAECRNTTHLLQRQLTRTQDSLLQAETQANSCNLTVVTLQESLEKKVSQALEQQARIKELENEVTKLNQELENLRIQKETSSTVQVNS 152 "FUNCTION: IFN-induced antiviral host restriction factor which efficiently blocks the release of diverse mammalian enveloped viruses by directly tethering nascent virions to the membranes of infected cells. Acts as a direct physical tether, holding virions to the cell membrane and linking virions to each other. The tethered virions can be internalized by endocytosis and subsequently degraded or they can remain on the cell surface. In either case, their spread as cell-free virions is restricted. Its target viruses belong to diverse families, including retroviridae: human immunodeficiency virus type 1 (HIV-1), mouse mammary tumor virus (MMTV) and murine leukemia virus (MLV), filoviridae: ebola virus (EBOV), arenaviridae: lassa virus (LASV), and rhabdoviridae: vesicular stomatitis virus (VSV). Can inhibit cell surface proteolytic activity of MMP14 causing decreased activation of MMP15 which results in inhibition of cell growth and migration. Can stimulate signaling by LILRA4/ILT7 and consequently provide negative feedback to the production of IFN by plasmacytoid dendritic cells in response to viral infection. Plays a role in the organization of the subapical actin cytoskeleton in polarized epithelial cells. {ECO:0000269|PubMed:16920966, ECO:0000269|PubMed:19179289, ECO:0000269|PubMed:20686043, ECO:0000269|PubMed:20702620, ECO:0000269|PubMed:21919738, ECO:0000269|PubMed:22025715, ECO:0000269|PubMed:22284121, ECO:0000269|PubMed:22327075}." null 1769.33 null null 100 uniprot_mouse_length brain_HCD 653.0498657 654.556641 654.552824 31 20250.11563 5.830889212 CA052_MOUSE UPF0690 protein C1orf52 homolog Q9CWU4 MAAEEKDPLSYFAAYGSSSSDSSDENSEPEDAGRKEAASAPTTGGRGKQAEKRLPGPDELFRSVTRPAFLYNPLNKQIDWERHVVKAPEEPPKEFKIWKSNCVPPPETYTTEKKPPPPELDMAIKWSNIYEDNGDDAPQNAKKARLLPEGEETVESDDDKDERASKIRRVEPGEAAKKKK 180 SIMILARITY: Belongs to the UPF0690 family. {ECO:0000305}. Y130PS156P 3095.38 "Y,29;S,15;" 188 100 uniprot_mouse_length brain_HCD 718.986145 718.682556 718.675464 20 14346.49598 9.868365763 CA162_MOUSE Transmembrane protein C1orf162 homolog Q3U7U4 MGSTSSTPKSTICTFSTTAPVTSSTPYFFNPKKEHIILAFFAGVLLTLLIVALIFLIVKSCRKCHSSAQTQDPPSEPPTKLSSLSKESLTYASMTFKPPEENSNDLTRNHSSGLEPTIYSQIKVTDSDLPLP 132 "SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" null 1224.69 null null 100 uniprot_mouse_length brain_HCD 1047.529053 1050.372681 1050.372762 16 16780.94734 -0.077435307 CALM_MOUSE Calmodulin; Short=CaM P62204 ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK 148 "FUNCTION: Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis (By similarity). {ECO:0000250}." A1AcK21Ac 668.87 "A,2;K,0;" 64 100 uniprot_mouse_length brain_HCD 1047.529053 1050.372681 1050.375037 16 16780.98372 -2.243328197 CALM_MOUSE Calmodulin; Short=CaM P62204 ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK 148 "FUNCTION: Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis (By similarity). {ECO:0000250}." A1AcK115tMe 564.91 "A,2;K,52;" 61 100 uniprot_mouse_length brain_HCD 771.9551392 774.773987 774.768971 11 8507.45448 6.473951067 CCL7_MOUSE C-C motif chemokine 7;AltName: Full=Intercrine/chemokine MARC;AltName: Full=Monocyte chemoattractant protein 3;AltName: Full=Monocyte chemotactic protein 3; Short=MCP-3;AltName: Full=Protein FIC;AltName: Full=Small-inducible cytokine A7;Flags: Precursor Q03366 QPDGPNASTCCYVKKQKIPKRNLKSYRRITSSRCPWEAVIFKTKKGMEVCAEAHQKWVEEAIAYLDMKTPTPKP 74 "FUNCTION: Chemotactic factor that attracts monocytes and eosinophils, but not neutrophils. Augments monocyte anti-tumor activity (By similarity). {ECO:0000250}." null 1012.84 null null 100 uniprot_mouse_length brain_HCD 630.4925537 634.026733 634.020436 26 16450.51554 9.932484948 CD3Z_MOUSE T-cell surface glycoprotein CD3 zeta chain;AltName: Full=T-cell receptor T3 zeta chain;AltName: CD_antigen=CD247;Flags: Precursor P24161 QSFGLLDPKLCYLLDGILFIYGVIITALYLRAKFSRSAETAANLQDPNQLYNELNLGRREEYDVLEKKRARDPEMGGKQQRRRNPQEGVYNALQKDKMAEAYSEIGTKGERRRGKGHDGLYQGLSTATKDTYDALHMQTLAPR 143 FUNCTION: Probable role in assembly and expression of the TCR complex as well as signal transduction upon antigen triggering. S37PY51P 1477.18 "S,5;Y,0;" 131 100 uniprot_mouse_length brain_HCD 562.8214111 557.945374 557.946043 14 7794.24193 -1.199873809 CD52_MOUSE CAMPATH-1 antigen;AltName: Full=Lymphocyte differentiation antigen B7;AltName: CD_antigen=CD52;Flags: Precursor Q64389 MKSFLLFLTIILLVVIQIQTGSLGQATTAASGTNKNSTSTKKTPLKSGASSIIDAGACSFLFFANTLMCLFYLS 74 "FUNCTION: May play a role in carrying and orienting carbohydrate, as well as having a more specific role." null 625.46 null null 100 uniprot_mouse_length brain_HCD 617.6969604 619.6203 619.62297 29 17931.04935 -4.308599197 CDN2A_MOUSE Cyclin-dependent kinase inhibitor 2A {ECO:0000312|MGI:MGI:104738};AltName: Full=Cyclin-dependent kinase 4 inhibitor A; Short=CDK4I;AltName: Full=p16-INK4a; Short=p16-INK4 P51480 MESAADRLARAAAQGRVHDVRALLEAGVSPNAPNSFGRTPIQVMMMGNVHVAALLLNYGADSNCEDPTTFSRPVHDAAREGFLDTLVVLHGSGARLDVRDAWGRLPLDLAQERGHQDIVRYLRSAGCSLCSAGWSLCTAGNVAQTDGHSFSSSTPRALELRGQSQEQS 168 FUNCTION: Acts as a negative regulator of the proliferation of normal cells by interacting strongly with CDK4 and CDK6. This inhibits their ability to interact with cyclins D and to phosphorylate the retinoblastoma protein. null 1908.67 null null 100 uniprot_mouse_length brain_HCD 626.3452759 625.732117 625.724846 36 22478.06869 11.61964283 CH046_MOUSE Uncharacterized protein C8orf46 homolog Q8BG31 MHQIYSCSDENIEVFTTVIPSKVSSSSRRRVKSSHHLLAKNVVIESDLYPPPRPLELLPQRCERRDTGDRRWLQTGRLQTARPPGAHPTKTPSRPVGISEPKTSNLCGNRAYGKSLIPPVARISVKAPAGAEVAAKGSEHGAVLGRGSRHLKKIAEEYPALPQGAEASLPLTGSTSCGVPGILRKMWTRHKKKSEYVGATNSAFEAD 207 "-------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License--------------------------------------------------" null 1686.48 null null 100 uniprot_mouse_length brain_HCD 547.2434082 548.656128 548.648737 20 10947.96582 13.47115046 CH10_MOUSE "10 kDa heat shock protein, mitochondrial; Short=Hsp10;AltName: Full=10 kDa chaperonin;AltName: Full=Chaperonin 10; Short=CPN10" Q64433 AGQAFRKFLPLFDRVLVERSAAETVTKGGIMLPEKSQGKVLQATVVAVGSGGKGKSGEIEPVSVKVGDKVLLPEYGGTKVVLDDKDYFLFRDSDILGKYVD 101 "FUNCTION: Eukaryotic CPN10 homolog which is essential for mitochondrial protein biogenesis, together with CPN60. Binds to CPN60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter." A1AcT78P 1104.5 "A,1;T,88;" 95 100 uniprot_mouse_length brain_HCD 581.7000122 581.008728 581.001126 27 15652.01677 13.08435905 CHCH2_MOUSE Coiled-coil-helix-coiled-coil-helix domain-containing protein 2 Q9D1L0 MPRGSRSRTSRVTPPASRAPQMRAAPRRAPAAQPPAAAAPSAVGSPAAAPRQPGLMAQMATTAAGVAVGSAVGHTLGHAITGGFSGGGSAEPAKPDITYQEPQGAQLQNQQSFGPCSLEIKQFLECAQNQSDVKLCEGFNEVLRQCRIANGLM 153 "FUNCTION: Transcription factor. Binds to the oxygen responsive element of COX4I2 and activates its transcription under hypoxia conditions (4% oxygen), as well as normoxia conditions (20% oxygen). {ECO:0000250|UniProtKB:Q9Y6H1}." null 3023.81 null null 100 uniprot_mouse_length brain_HCD 581.7000122 578.508362 578.508375 28 16162.21896 -0.022788942 CHSP1_MOUSE Calcium-regulated heat stable protein 1;AltName: Full=Calcium-regulated heat-stable protein of 24 kDa; Short=CRHSP-24 Q9CR86 SSEPPPPPLQPPTHQTSVGLLDTPRTRDRSPSPLRGNVVPSPLPTRRTRTFSATVRASQGPVYKGVCKCFCRSKGHGFITPADGGPDIFLHISDVEGEYVPVEGDEVTYKMCSIPPKNEKLQAVEVVITHLAPGTKHETWSGHVISN 147 FUNCTION: Binds mRNA and regulates the stability of target mRNA. {ECO:0000269|PubMed:21078874}. S30PS32PS41P 2974.37 "S,2;S,0;S,0;" 185 100 uniprot_mouse_length brain_HCD 644.1920776 647.733276 647.73348 14 9050.26398 -0.31437747 CI016_MOUSE UPF0184 protein C9orf16 homolog P58686 MSGPNGDLGMPVDAGTEGENDSFGEAEYAAINSMLDQINSCLDHLEEKNDHLHARLQELLESNRQTRLEFQQQLGEAPGDASP 83 "SIMILARITY: Belongs to the UPF0184 (EST00098) family. {ECO:0000305}.-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" null 617.77 null null 100 uniprot_mouse_length brain_HCD 818.9362793 816.296936 816.290044 14 11409.05266 8.443120441 CJ032_MOUSE UPF0693 protein C10orf32 homolog Q9CRC6 ATGTPDSQARFGQSVKGLLTEKVNTCGTDVIALTKQVLKGSRSSELLGQAARNMVLQEDAILHSEDSLRKMAIITTHLQYQQEAIQKNVEQSPDLQDQLSHLLK 104 "SIMILARITY: Belongs to the UPF0693 family. {ECO:0000305}.-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" null 771.26 null null 100 uniprot_mouse_length brain_HCD 589.0150146 587.138977 587.14684 24 14060.51063 -13.39179347 CK086_MOUSE Uncharacterized protein C11orf86 homolog Q8VC23 MGTSLRSQSFREPRPSYGRLHESQGRSLDGRLHRALSLRLGREKSRSQVPDGTEGLEVSVQERLPGTLGDKEQLIQGQRGGGSRRWLRQYQQHVKRRWRSFVASFPSVTLSQPASPETLLDTNN 124 "-------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License--------------------------------------------------" null 1803.82 null null 100 uniprot_mouse_length brain_HCD 626.3452759 623.446716 623.44965 38 23640.06082 -4.70557872 CLC2L_MOUSE C-type lectin domain family 2 member L P0C7M9 MEPAREPPARARPPPPAARPAPAAPRPRSPAEAEARGPEGLLRRSGSGYEGSTSWKAALEDTTTRLLLGAIAVLLFAILVVMSILASKGCIKCETPCPEDWLLYGRKCYYFSEEPRDWNTGRQYCHTHEAALAVIQSQKELEFMFKFTRREPWIGLRRVGDDFHWVNGDPFDPDTFTISGMGECVFVEPTRLVSTECLTTRPWVCSKMAYT 211 SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. null 1671.52 null null 100 uniprot_mouse_length brain_HCD 892.3828735 889.253052 889.251284 14 12429.50673 1.987917076 COX5A_MOUSE "Cytochrome c oxidase subunit 5A, mitochondrial;AltName: Full=Cytochrome c oxidase polypeptide Va;Flags: Precursor" P12787 SHGSHETDEEFDARWVTYFNKPDIDAWELRKGMNTLVGYDLVPEPKIIDAALRACRRLNDFASAVRILEVVKDKAGPHKEIYPYVIQELRPTLNELGISTPEELGLDKV 109 "FUNCTION: This is the heme A-containing chain of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport." null 751.62 null null 100 uniprot_mouse_length brain_HCD 1298.562744 1301.702026 1301.695883 5 6500.47734 4.719510346 COX7R_MOUSE "Cytochrome c oxidase subunit 7A-related protein, mitochondrial;AltName: Full=Cytochrome c oxidase subunit VIIa-related protein;AltName: Full=Silica-induced gene 81 protein; Short=SIG-81;AltName: Full=Supercomplex assembly factor I {ECO:0000303|PubMed:23812712};Flags: Precursor" Q61387 GKNKVPELQKFFQKADGFHLKRGLPDQMLYRTTMALTLGGTIYCLIALYMASQPRNK 57 "FUNCTION: Involved in the regulation of oxidative phosphorylation and energy metabolism (PubMed:23857330, PubMed:23812712). Necessary for the assembly of mitochondrial respiratory supercomplex (PubMed:23857330, PubMed:23812712). {ECO:0000269|PubMed:23812712, ECO:0000269|PubMed:23857330}." null 173.66 null null 100 uniprot_mouse_length brain_HCD 585.0100098 582.820374 582.821457 8 4653.57385 -1.85899958 COX8B_MOUSE "Cytochrome c oxidase subunit 8B, mitochondrial;AltName: Full=Cytochrome c oxidase polypeptide VIII-heart;AltName: Full=Cytochrome c oxidase subunit 8-1;AltName: Full=Cytochrome c oxidase subunit 8H;Flags: Precursor" P48772 VSAKPAKTPTSAVEQAVGISAIVVGFMVPAGWVLAHLESYKKSSAA 46 "FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport." null 458.82 null null 100 uniprot_mouse_length brain_HCD 633.8427734 630.469849 630.465231 24 15099.15438 7.324167274 CRTP1_MOUSE Cysteine-rich tail protein 1 Q9D1E4 MDPHEMVVKNPYAHISIPRAHLRSDLGQQLEEVPSSSSSSETQPLPAGTCIPEPVGLLQTTEAPGPKGIKGIKGTAPEHGQQTWQSPCNPYSSGQRPSGLTYAGLPPVGRGDDIAHHCCCCPCCSCCHCPRFCRCHSCCVIS 142 "SIMILARITY: Belongs to the CYSRT1 family. {ECO:0000305}.-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" null 969.08 null null 100 uniprot_mouse_length brain_HCD 626.3452759 630.129089 630.122993 36 22636.4013 9.674865917 CRYAA_MOUSE Alpha-crystallin A chain P24622 MDVTIQHPWFKRALGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISELMTHMWFVMHQPHAGNPKNNPVKVRSDRDKFVIFLDVKHFSPEDLTVKVLEDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFSGPKVQSGLDAGHSERAIPVSREEKPSSAPSS 196 "FUNCTION: Contributes to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions (By similarity). {ECO:0000250}." S45PS145P 1615.6 "S,71;S,57;" 172 100 uniprot_mouse_length brain_HCD 778.1201172 774.481079 774.48673 26 20099.62992 -7.296314086 CRYAB_MOUSE Alpha-crystallin B chain;AltName: Full=Alpha(B)-crystallin;AltName: Full=P23 P23927 MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFSTATSLSPFYLRPPSFLRAPSWIDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVAAAPKK 175 "FUNCTION: May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions." M1Ac 1927.02 "M,39;" 163 100 uniprot_mouse_length brain_HCD 626.3452759 630.653503 630.645552 32 20137.63262 12.60837874 CRYAB_MOUSE Alpha-crystallin B chain;AltName: Full=Alpha(B)-crystallin;AltName: Full=P23 P23927 MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFSTATSLSPFYLRPPSFLRAPSWIDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVAAAPKK 175 "FUNCTION: May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions." S19P 1294.54 "S,4;" 141 100 uniprot_mouse_length brain_HCD 848.3656616 843.867004 843.856726 24 20217.53639 12.18026024 CRYAB_MOUSE Alpha-crystallin B chain;AltName: Full=Alpha(B)-crystallin;AltName: Full=P23 P23927 MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFSTATSLSPFYLRPPSFLRAPSWIDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVAAAPKK 175 "FUNCTION: May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions." S19PS45P 2325.68 "S,10;S,0;" 160 100 uniprot_mouse_length brain_HCD 855.7393188 856.100952 856.100512 15 12819.49569 0.51413173 CST14_MOUSE Cystatin-14;AltName: Full=Cystatin SC;Flags: Precursor Q8VII3 INKEFLDVTKDLDYFVASVEFAVAQFNDNNPEENTYKLLEVGRAQKKTWTMIFLMDLEMGRTICKKHDENIHNCPLLQGSREKKVHCVFQVDARPWFSHFTILTSTCVPT 110 FUNCTION: May play a specialized role in spermatogenesis. {ECO:0000269|PubMed:12444065}. null 244.44 null null 100 uniprot_mouse_length brain_HCD 637.3490601 634.818787 634.81818 20 12669.35168 0.955582422 CST9_MOUSE Cystatin-9;AltName: Full=Testatin;Flags: Precursor Q9Z0H6 NKETNRSVHFIPTVEFAVNTFNQESQDEYAYRMEHIMSSWREKVNFPTVYSMRLQLRRTICKKFEESLDICPFQESHGLNNTFTCLFTVGTYPWITKFKLFRSVCS 106 FUNCTION: Could play an essential role in tissue reorganization during early testis development. null 396.6 null null 100 uniprot_mouse_length brain_HCD 646.1085205 645.557495 645.556453 23 14816.78189 1.614292883 CT024_MOUSE Uncharacterized protein C20orf24 homolog Q9CQT9 MSGGRRKEEPPQPQLANGALKVSVWSKVLRSDAAWDDKDEFLDVIYWFRQIIALVLGVIWGVLPLRGFLGIAGFCLINAGVLYLYFSNYLQIDEEEYGGTWELTKEGFMTSFALFMVIWIIFYTAIHYD 129 "-------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License--------------------------------------------------" null 2177.87 null null 100 uniprot_mouse_length brain_HCD 916.1668091 918.472534 918.460487 11 10087.05897 13.11670982 CTRB1_MOUSE Chymotrypsinogen B; EC=3.4.21.1;Contains: Chymotrypsin B chain A;Contains: Chymotrypsin B chain B;Contains: Chymotrypsin B chain C;Flags: Precursor Q9CR35 LKTPDKLQQAALPIVSEAKCKESWGSKITDVMICAGASGVSSCMGDSGGPLVCQKDGVWTLAGIVSWGSGFCSTSTPAVYARVTALMPWVQEILEAN 97 "CATALYTIC ACTIVITY: Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa. {ECO:0000255|PROSITE-ProRule:PRU10078, ECO:0000255|PROSITE-ProRule:PRU10079}." null 219.75 null null 100 uniprot_mouse_length brain_HCD 992.1782227 995.002625 994.993078 10 9934.9236 9.594550887 CX6B1_MOUSE Cytochrome c oxidase subunit 6B1;AltName: Full=Cytochrome c oxidase subunit VIb isoform 1; Short=COX VIb-1 P56391 AEDIKTKIKNYKTAPFDSRFPNQNQTKNCWQNYLDFHRCEKAMTAKGGDVSVCEWYRRVYKSLCPVSWVSAWDDRIAEGTFPGKI 85 FUNCTION: Connects the two COX monomers into the physiological dimeric form. {ECO:0000250}. null 276.45 null null 100 uniprot_mouse_length brain_HCD 908.821228 911.933777 911.938036 13 11836.18364 -4.670431941 CYT2_MOUSE Stefin-2 P35174 MTEYTRKIKGGLSEARPATSEIQEIADKVRPLLEEKTNEKYEKFKAIEYKVQVVQGLNYFIKMNVGRGCYLHINVLSGISSENDLELTGYQTNKAKNDELTYF 103 FUNCTION: This is an intracellular thiol proteinase inhibitor. null 1207.62 null null 100 uniprot_mouse_length brain_HCD 811.0509644 815.711731 815.71286 12 9771.54976 -1.384118143 DAR10_MOUSE Alpha-defensin-related sequence 10;AltName: Full=CRS4C-4;AltName: Full=Cryptdin-related protein 4C-4;AltName: Full=Defensin-related cryptdin-related sequence 10;Flags: Precursor Q64263 MKKLVLLSAFVLLAFQVQADSIQNTDEETKTEEQPGEENQAMSVSFGDPEGSALQDAAVGMARPCPPCPSCPSCPWCPMCPRCPSCKCNPK 91 "FUNCTION: Apparent precursor of a secreted, cationic, proline- and cysteine-rich peptide that contains Cys-Pro-Xaa repeats. Unlike cryptdin, the proposed mature peptide region lacks the structural motif characteristic of defensins. It may have microbicidal activities (By similarity). {ECO:0000250}." null 535.38 null null 100 uniprot_mouse_length brain_HCD 723.3877563 718.830139 718.829171 26 18653.53696 1.346857077 DCTP1_MOUSE dCTP pyrophosphatase 1; EC=3.6.1.12;AltName: Full=Deoxycytidine-triphosphatase 1; Short=dCTPase 1;AltName: Full=RS21-C6;AltName: Full=XTP3-transactivated gene A protein homolog Q9QY93 STAGDGERGTVGQEDSAAARPFRFSPEPTLEDIRRLHAEFAAERDWEQFHQPRNLLLALVGEVGELAELFQWKSDTEPGPQAWPPKERAALQEELSDVLIYLVALAARCHVDLPQAVISKMDTNRQRYPVHLSRGSACKYTDLPRGTISENQAVGAGDPASELRDQAST 169 "FUNCTION: Hydrolyzes deoxynucleoside triphosphates (dNTPs) to the corresponding nucleoside monophosphates. Has a strong preference for modified dCTP. Activity is highest with 5-iodo-dCTP, followed by 5-bromo-dCTP, unmodified dCTP, 5-methyl-dCTP and 5-chloro-dCTP. Hydrolyzes 2-chloro-dATP and 2-hydroxy-dATP with lower efficiency, and has even lower activity with unmodified dATP, dTTP and dUTP (in vitro). Does not hydrolyze ATP, UTP, ITP, GTP, dADP, dCDP or dGTP. May protect DNA or RNA against the incorporation of non- canonical nucleotide triphosphates. May protect cells against inappropriate methylation of CpG islands by DNA methyltransferases. {ECO:0000269|PubMed:17320107, ECO:0000269|PubMed:19220460}." null 8284.2 null null 100 uniprot_mouse_length brain_HCD 725.3961182 726.6073 726.605519 8 5802.84528 2.450854888 DFB12_MOUSE "Beta-defensin 12; Short=BD-12; Short=mBD-12;AltName: Full=Defensin, beta 12;Flags: Precursor" Q8K4N3 GLEYSQSFPGGEIAVCETCRLGRGKCRRTCIESEKIAGWCKLNFFCCRERI 51 FUNCTION: Has antibacterial activity. {ECO:0000250}. null 333.82 null null 100 uniprot_mouse_length brain_HCD 734.6556396 731.319824 731.322885 15 10949.8353 -4.185266608 DHSD_MOUSE "Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial; Short=CybS;AltName: Full=CII-4;AltName: Full=QPs3;AltName: Full=Succinate dehydrogenase complex subunit D;AltName: Full=Succinate-ubiquinone oxidoreductase cytochrome b small subunit;AltName: Full=Succinate-ubiquinone reductase membrane anchor subunit;Flags: Precursor" Q9CXV1 SGSKAASLHWTSERVVSVLLLGLIPAGYLNPCSVVDYSLAAALTLHSHWGLGQVVTDYVHGDTLPKAARAGLLALSALTFAGLCYFNYHDVGICRAVAMLWKL 103 FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). {ECO:0000250}. null 1263.89 null null 100 uniprot_mouse_length brain_HCD 671.4799805 672.483521 672.489473 16 10738.8239 -8.851428054 DLRB2_MOUSE "Dynein light chain roadblock-type 2;AltName: Full=Dynein light chain 2B, cytoplasmic" Q9DAJ5 TEVEETLKRIQSHKGVIGTMVVNAEGIPIRTTLDNSTTVQYAGLLHQLTMKAKSTVRDIDPQNDLTFLRIRSKKHEIMVAPDKEYLLIVIQNPCE 95 FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. null 808.36 null null 100 uniprot_mouse_length brain_HCD 620.0737915 615.451599 615.442426 31 19037.69459 14.90492158 DNPH1_MOUSE 2'-deoxynucleoside 5'-phosphate N-hydrolase 1 {ECO:0000255|HAMAP-Rule:MF_03036}; EC=3.2.2.- {ECO:0000255|HAMAP-Rule:MF_03036};AltName: Full=c-Myc-responsive protein Rcl {ECO:0000255|HAMAP-Rule:MF_03036} Q80VJ3 AASGELVPCSVYFCGSIRGGREDQALYSRIVSRLRRYGKVLTEHVADAELEPRGEEAAGGDQFIHERDLAWLRQADVVVAEVTQPSLGVGYELGRAVALGKPILCLFRPQSGRVLSAMIRGAADGSRFQVWDYAEEEVETMLHRYFEAYLPQGTASSSNPSACLNPTVLEKI 172 FUNCTION: Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5- phosphate and a purine or pyrimidine base. Deoxyribonucleoside 5'- monophosphates containing purine bases are preferred to those containing pyrimidine bases. {ECO:0000255|HAMAP-Rule:MF_03036}. A1AcS16PS86P 5554.54 "A,218;S,63;S,0;" 231 100 uniprot_mouse_length brain_HCD 722.0322876 725.169189 725.169927 14 10133.37156 -1.017067652 DPM3_MOUSE Dolichol-phosphate mannosyltransferase subunit 3;AltName: Full=Dolichol-phosphate mannose synthase subunit 3; Short=DPM synthase subunit 3;AltName: Full=Dolichyl-phosphate beta-D-mannosyltransferase subunit 3;AltName: Full=Mannose-P-dolichol synthase subunit 3; Short=MPD synthase subunit 3 Q9D1Q4 MTKLTQWLWGLALLGSAWAALTMGALGLELPFPCREVLWPLPAYLLVSAGCYALGTVGYRVATFHDCEDAARELQSQIVEARADLARRGLRF 92 FUNCTION: Stabilizer subunit of the dolichol-phosphate mannose (DPM) synthase complex; tethers catalytic subunit DPM1 to the ER. {ECO:0000250}. null 636.64 null null 100 uniprot_mouse_length brain_HCD 645.1993408 648.91864 648.914001 19 12304.35509 7.149077862 DPOE4_MOUSE DNA polymerase epsilon subunit 4; EC=2.7.7.7;AltName: Full=DNA polymerase II subunit 4;AltName: Full=DNA polymerase epsilon subunit p12 Q9CQ36 AAAAAAGSGTPREEEAPGGEAAASQAQAPTSAPGGVRLSRLPLARVKALVKADPDVTLAGQEAIFILARAAELFVETIAKDAYCCAQQGKRKTLQRRDLDNAIEAVDEFAFLEGTLD 117 FUNCTION: May play a role in allowing polymerase epsilon to carry out its replication and/or repair function. A1AcT10PS24P 1093.95 "A,60;T,3;S,13;" 94 100 uniprot_mouse_length brain_HCD 939.3522949 938.825317 938.824272 12 11248.8828 1.113502115 DPY30_MOUSE Protein dpy-30 homolog;AltName: Full=Dpy-30-like protein; Short=Dpy-30L Q99LT0 MESEQMLEGQTQVAENPHSEYGLTDSVERIVENEKINAEKSSKQKVDLQSLPTRAYLDQTVVPILLQGLAVLAKERPPNPIEFLASYLLKNKAQFEDRN 99 "FUNCTION: As part of the MLL1/MLL complex, involved in the methylation of histone H3 at 'Lys-4', particularly trimethylation. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. May play some role in histone H3 acetylation. In embryonic stem (ES) cells, plays a crucial role in the differentiation potential, particularly along the neural lineage, regulating gene induction and histone H3 'Lys- 4' methylation at key developmental loci, including that mediated by retinoic acid. Does not affect ES cell self-renewal. May also play an indirect or direct role in endosomal transport. {ECO:0000269|PubMed:21335234}." M1Ac 1382.06 "M,12;" 95 100 uniprot_mouse_length brain_HCD 644.1920776 640.94043 640.940986 33 21106.02853 -0.867962125 DUS18_MOUSE Dual specificity protein phosphatase 18; EC=3.1.3.16; EC=3.1.3.48 Q8VE01 MTSPWSAFPVQIPQPSIRGLSQITKSLFISNGVAANNKLLLSSNQITTVINVSVEVANTFYEDIQYVQVPVVDAPVARLSNFFDSVADRIHSVEMQKGRTLLHCAAGVSRSAALCLAYLMKYHAMSLVDAHTWTKSCRPIIRPNSGFWEQLIHYELQLFGKNTMQMMDSPMGRIPDIYEKETRLMIPL 188 "FUNCTION: Can dephosphorylate single and diphosphorylated synthetic MAPK peptides, with preference for the phosphotyrosine and diphosphorylated forms over phosphothreonine. {ECO:0000250}." null 4381.43 null null 100 uniprot_mouse_length brain_HCD 1049.289917 1049.719849 1049.717754 10 10482.17037 1.995424774 DYL1_MOUSE "Dynein light chain 1, cytoplasmic;AltName: Full=8 kDa dynein light chain; Short=DLC8;AltName: Full=Dynein light chain LC8-type 1;AltName: Full=Protein inhibitor of neuronal nitric oxide synthase; Short=PIN; Short=mPIN" P63168 MCDRKAVIKNADMSEEMQQDSVECATQALEKYNIEKDIAAHIKKEFDKKYNPTWHCIVGRNFGSYVTHETKHFIYFYLGQVAILLFKSG 89 FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures (By similarity). {ECO:0000250}. K36AcS88P 198.47 "K,28;S,16;" 32 100 uniprot_mouse_length brain_HCD 747.1469727 749.120789 749.127025 20 14954.52746 -8.324924309 ECP3_MOUSE Eosinophil cationic-type ribonuclease 3;AltName: Full=MR-3;Flags: Precursor O35290 LGQTPSRWFAIQHINNNTNLRCNVEMLRINRFRRTCKGLNTFLHTSFANAVGVCGNPSGLCSDNISRNCHNSSSRVHITVCNITSRRRIPYTQCRYQPRRSVEYYTVACNPRTSLDSPMYPVVPVHLDGTF 131 "SIMILARITY: Belongs to the pancreatic ribonuclease family. {ECO:0000305}.-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" null 1058.75 null null 100 uniprot_mouse_length brain_HCD 587.8200073 592.513611 592.506776 33 19509.7027 11.53546275 EIF1A_MOUSE Probable RNA-binding protein EIF1AD;AltName: Full=Eukaryotic translation initiation factor 1A domain-containing protein Q3THJ3 MSQASKRKHVVQEVLGEHMVPSDHQQIVKVLRTPGNNLHEVETAQGQRFLVSMPSKYRKNIWIKRGDFLIVDPIEEGEKVKAEISFVLCKNHVRSLQKEGHWPEAFSEVAEKQNNMNRESQPELPAEPQLSGEGSSSEDDSDLFVNTNHRQYHESEEESEEDEEEEEEAA 170 FUNCTION: Plays a role into cellular response to oxidative stress. Decreases cell proliferation (By similarity). {ECO:0000250}. null 2238.46 null null 100 uniprot_mouse_length brain_HCD 671.4799805 670.112915 670.104826 15 10031.56431 12.07130399 ESP22_MOUSE Exocrine gland-secreted peptide 22;Flags: Precursor A8R0V4 LTQTQKESIFSAEHKSDLKSYLEMLVCRRLRDVPESVIHISKVSKEILPDDLLSTYLLELLVCFDKDKLVQSKGIVFNTIKRLLTNT 87 FUNCTION: Pheromone produced by juveniles which activates a small number of vomeronasal organ sensory neurons and exhibits a powerful inhibitory effect on adult male mating behavior. {ECO:0000269|PubMed:24089208}. null 742.45 null null 100 uniprot_mouse_length brain_HCD 642.46875 646.098816 646.100921 24 15474.4059 -3.258131915 F107B_MOUSE Protein FAM107B Q3TGF2 AEPDYIEDDNPELIRPQKLINPVKSSRNHQDLHRELLMNQKRGLAPQNKPELQKVMEKRRRDQVIKQKEEEAQKKKSDLEIELLKRQQKLEQLELEKQKLQEEQENAPEFVKVKGNLRRTGQEVAQAQES 130 SIMILARITY: Belongs to the FAM107 family. {ECO:0000305}. A1Ac 2044.47 "A,15;" 131 100 uniprot_mouse_length brain_HCD 618.0603027 617.233765 617.236406 22 13550.18804 -4.279319134 F174B_MOUSE Membrane protein FAM174B;Flags: Precursor Q8K064 RRAESASASQPEAEHQPPPGPGNATQLGSGMAGGGSSNSSVDAVVTRISSLLRDLPTLKATVIVACAFSALLIACLLLRVFRLGKRLKKTRKYDIITTPAERVEMAPLNEEDDEDEDSTVFDIKYR 126 SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. null 2086.41 null null 100 uniprot_mouse_length brain_HCD 642.9816284 643.587341 643.582009 28 17983.27727 8.285359937 F195A_MOUSE Protein FAM195A Q9CQB2 MYTITKGPSKLVAQRRTGPTQQQVESRLGELLKCRQPVPPTALPAHLQPSAQTQGPWPLASSGPRLVFNRVNGRRPLTTSPSLEGTQETYTVAHEENVRFVSEAWQQVERQLDGGPADESGPRPVQYVESTPDPRLQNFVPIDLDEWWAQQFLAKITNCS 160 "SIMILARITY: Belongs to the FAM195 family. {ECO:0000305}.-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" M1AcS61P 3493.25 "M,149;S,21;" 174 100 uniprot_mouse_length brain_HCD 1201.876953 1201.384766 1201.377488 12 14397.51706 6.057733787 FABPL_MOUSE "Fatty acid-binding protein, liver;AltName: Full=14 kDa selenium-binding protein;AltName: Full=Fatty acid-binding protein 1;AltName: Full=Liver-type fatty acid-binding protein; Short=L-FABP" P12710 MNFSGKYQLQSQENFEPFMKAIGLPEDLIQKGKDIKGVSEIVHEGKKIKLTITYGPKVVRNEFTLGEECELETMTGEKVKAVVKLEGDNKMVTTFKGIKSVTELNGDTITNTMTLGDIVYKRVSKRI 127 "FUNCTION: Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport. Also seems to bind selenium." S11PT51P 1172.03 "S,8;T,23;" 79 100 uniprot_mouse_length brain_HCD 841.7944946 843.224182 843.228137 14 11785.18323 -4.690155511 FKB1A_MOUSE Peptidyl-prolyl cis-trans isomerase FKBP1A; Short=PPIase FKBP1A; EC=5.2.1.8;AltName: Full=12 kDa FK506-binding protein; Short=12 kDa FKBP; Short=FKBP-12;AltName: Full=Calstabin-1;AltName: Full=FK506-binding protein 1A; Short=FKBP-1A;AltName: Full=Immunophilin FKBP12;AltName: Full=Rotamase P26883 GVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFTLGKQEVIRGWEEGVAQMSVGQRAKLIISSDYAYGATGHPGIIPPHATLVFDVELLKLE 107 "FUNCTION: Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruites SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). {ECO:0000250}." null 715.12 null null 100 uniprot_mouse_length brain_HCD 1134.995361 1130.526489 1130.522735 11 12417.7406 3.320815846 FSHB_MOUSE Follitropin subunit beta;AltName: Full=Follicle-stimulating hormone beta subunit; Short=FSH-B; Short=FSH-beta;AltName: Full=Follitropin beta chain;Flags: Precursor Q60687 SCELTNITISVEKEECRFCISINTTWCAGYCYTRDLVYKDPARPNTQKVCTFKELVYETVRLPGCARHSDSLYTYPVATECHCGKCDSDSTDCTVRGLGPSYCSFSEMKE 110 FUNCTION: Stimulates development of follicle and spermatogenesis in the reproductive organs. null 209.3 null null 100 uniprot_mouse_length brain_HCD 722.0473633 719.385071 719.377737 12 8616.52726 10.19464518 FXYD6_MOUSE FXYD domain-containing ion transport regulator 6;AltName: Full=PLM-like protein;AltName: Full=Phosphohippolin;Flags: Precursor Q9D164 SAAEKEKEKDPFYYDYQTLRIGGLVFAVVLFSVGILLILSRRCKCSFNQKPRAPGDEEAQVENLITTNAAEPQKAEN 77 SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. null 1119.13 null null 100 uniprot_mouse_length brain_HCD 646.1085205 643.243225 643.249032 11 7061.73703 -9.027456016 GBG7_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-7;Flags: Precursor Q61016 SGTNNVAQARKLVEQLRIEAGIERIKVSKASSDLMGYCEQHARNDPLLVGVPASENPFKDKKPC 64 "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction. Plays a role in the regulation of adenylyl cyclase signaling in certain regions of the brain. Plays a role in the formation or stabilzation of a G protein heterotrimer (G(olf) subunit alpha-beta-gamma-7) that is required for adenylyl cyclase activity in the striatum. {ECO:0000269|PubMed:12488442}." S1AcC64Me 743.16 "S,38;C,40;" 58 100 uniprot_mouse_length brain_HCD 627.3529053 626.171997 626.168656 12 7499.02126 5.335735477 GBGT2_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-T2;AltName: Full=G gamma-C;AltName: Full=G-gamma-8;Flags: Precursor Q61017 MAQDLSEKELLRMEVEQLKKEVKNPRDLISKTGKEIKDYVEAQAGTDPLLKGIPEDKNPFKEKGTC 66 "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction." null 360.88 null null 100 uniprot_mouse_length brain_HCD 577.9400024 578.533081 578.538782 24 13853.9176 -9.854041751 GCSH_MOUSE "Glycine cleavage system H protein, mitochondrial;AltName: Full=Lipoic acid-containing protein;Flags: Precursor" Q91WK5 SVRKFTEKHEWITTEEGIGTVGISNFAQEALGDVVYCSLPEVGTKLKKQEEFGALESVKAASELYSPLSGEVTEVNEALAENPGLVNKSCYEDGWLIKMTLSDPSEMDELMSEEAYEKYVKSIEE 125 FUNCTION: The glycine cleavage system catalyzes the degradation of glycine. The H protein (GCSH) shuttles the methylamine group of glycine from the P protein (GLDC) to the T protein (GCST) (By similarity). {ECO:0000250}. null 299 null null 100 uniprot_mouse_length brain_HCD 745.3182983 744.462219 744.457761 14 10403.40072 5.988571165 GLPC_MOUSE Glycophorin-C;AltName: CD_antigen=CD236 Q78HU7 MSSPVSKPPPELLEPNPGKSYGIMEIAIIAAVITAVALVLVCLLFLMLRYLYRHKGTYHTNEAKGTEFAESADAALQSDPALQDAGDTSKKEYFI 95 SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Note=Linked to the membrane via band 4.1. {ECO:0000250}. S71P 514.93 "S,12;" 50 100 uniprot_mouse_length brain_HCD 626.3452759 629.765503 629.768029 27 16967.72066 -4.01111234 GREM2_MOUSE "Gremlin-2;AltName: Full=Cysteine knot superfamily 1, BMP antagonist 2;AltName: Full=Protein related to DAN and cerberus; Short=PRDC;Flags: Precursor" O88273 RKNRPAGAIPSPYKDGSSNNSERWHHQIKEVLASSQEALVVTERKYLKSDWCKTQPLRQTVSEEGCRSRTILNRFCYGQCNSFYIPRHVKKEEDSFQSCAFCKPQRVTSVIVELECPGLDPPFRIKKIQKVKHCRCMSVNLSDSDKQ 147 "FUNCTION: Cytokine that inhibits the activity of BMP2 and BMP4 in a dose-dependent manner, and thereby modulates signaling by BMP family members. Contributes to the regulation of embryonic morphogenesis via BMP family members. Antagonizes BMP4-induced suppression of progesterone production in granulosa cells. {ECO:0000269|PubMed:15039429, ECO:0000269|PubMed:23063586, ECO:0000269|PubMed:23850456}." null 816.35 null null 100 uniprot_mouse_length brain_HCD 685.5707397 689.289673 689.287095 31 21325.87443 3.739880786 H12_MOUSE Histone H1.2;AltName: Full=H1 VAR.1;AltName: Full=H1c P15864 SEAAPAAPAAAPPAEKAPAKKKAAKKPAGVRRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGILVQTKGTGASGSFKLNKKAASGEAKPQAKKAGAAKAKKPAGAAKKPKKATGAATPKKAAKKTPKKAKKPAAAAVTKKVAKSPKKAKVTKPKKVKSASKAVKPKAAKPKVAKAKKVAAKKK 211 "FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250}." S1AcS35PS103P 2360.18 "S,2;S,0;S,0;" 215 100 uniprot_mouse_length brain_HCD 672.4362793 675.111206 675.102021 21 14149.12828 13.60543207 H2A1F_MOUSE Histone H2A type 1-F Q8CGP5 SGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKPKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1AcK5AcK9Ac 833.85 "S,1;K,0;K,2;" 86 100 uniprot_mouse_length brain_HCD 788.8314209 790.898499 790.891734 18 14211.0371 8.553048243 H2A1F_MOUSE Histone H2A type 1-F Q8CGP5 SGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKPKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1PR3dMeT120P 525.35 "S,32;R,35;T,0;" 60 100 uniprot_mouse_length brain_HCD 626.2931519 629.775269 629.772823 22 13825.988 3.883233125 H2A1H_MOUSE Histone H2A type 1-H Q8CGP6 SGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAK 127 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." Q104Me 2096.58 "Q,111;" 131 100 uniprot_mouse_length brain_HCD 614.5828857 611.0979 611.093131 23 14025.12789 7.804687016 H2A1K_MOUSE Histone H2A type 1-K Q8CGP7 SGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTETHHKAKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." Q104Me 1642.57 "Q,103;" 118 100 uniprot_mouse_length brain_HCD 614.5828857 612.319641 612.311883 23 14053.15919 12.67019879 H2A1K_MOUSE Histone H2A type 1-K Q8CGP7 SGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTETHHKAKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." R3dMeQ104Me 1671.41 "R,86;Q,110;" 111 100 uniprot_mouse_length brain_HCD 673.0150146 671.206543 671.196997 21 14067.12282 14.22230551 H2A1K_MOUSE Histone H2A type 1-K Q8CGP7 SGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTETHHKAKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1AcQ104Me 963.1 "S,0;Q,71;" 95 100 uniprot_mouse_length brain_HCD 644.1920776 641.822144 641.822039 22 14091.07075 0.162902925 H2A1K_MOUSE Histone H2A type 1-K Q8CGP7 SGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTETHHKAKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1P 1897.49 "S,76;" 125 100 uniprot_mouse_length brain_HCD 614.5828857 611.0979 611.091548 23 14025.09151 10.3951538 H2A3_MOUSE Histone H2A type 3 Q8BFU2 SGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1Ac 1529.58 "S,0;" 92 100 uniprot_mouse_length brain_HCD 673.0150146 671.206543 671.196997 21 14067.12282 14.22230551 H2A3_MOUSE Histone H2A type 3 Q8BFU2 SGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1AcR3dMeQ104Me 942.32 "S,0;R,55;Q,65;" 90 100 uniprot_mouse_length brain_HCD 646.1085205 641.376587 641.369274 22 14081.1099 11.40203368 H2A3_MOUSE Histone H2A type 3 Q8BFU2 SGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1AcK5AcQ104Me 1760.51 "S,0;K,6;Q,99;" 121 100 uniprot_mouse_length brain_HCD 626.2931519 629.775269 629.773787 24 15083.55664 2.352518822 H2AX_MOUSE Histone H2AX; Short=H2a/x;AltName: Full=Histone H2A.X P27661 SGRGKTGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGHYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGGVTIAQGGVLPNIQAVLLPKKSSATVGPKAPAVGKKASQASQEY 142 "FUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Required for checkpoint-mediated arrest of cell cycle progression in response to low doses of ionizing radiation and for efficient repair of DNA double strand breaks (DSBs) specifically when modified by C- terminal phosphorylation. {ECO:0000269|PubMed:11740565, ECO:0000269|PubMed:11934988, ECO:0000269|PubMed:12034884, ECO:0000269|PubMed:12447390, ECO:0000269|PubMed:12660252, ECO:0000269|PubMed:12689589, ECO:0000269|PubMed:12792649, ECO:0000269|PubMed:12914700, ECO:0000269|PubMed:12914701, ECO:0000269|PubMed:14530383, ECO:0000269|PubMed:15574327, ECO:0000269|PubMed:15580272, ECO:0000269|PubMed:15589157, ECO:0000269|PubMed:15610743, ECO:0000269|PubMed:15632067}." S1P 2754.35 "S,104;" 151 100 uniprot_mouse_length brain_HCD 617.6956787 619.570557 619.562111 23 14219.91515 13.63162865 H2B1A_MOUSE "Histone H2B type 1-A;AltName: Full=Histone H2B, testis;AltName: Full=Testis-specific histone H2B" P70696 PEVAVKGATISKKGFKKAVTKTQKKEGRKRKRCRKESYSIYIYKVLKQVHPDTGISSKAMSIMNSFVTDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 126 "FUNCTION: Variant histone specifically required to direct the transformation of dissociating nucleosomes to protamine in male germ cells. Entirely replaces classical histone H2B prior nucleosome to protamine transition and probably acts as a nucleosome dissociating factor that creates a more dynamic chromatin, facilitating the large-scale exchange of histones. Also expressed maternally and is present in the female pronucleus, suggesting a similar role in protamine replacement by nucleosomes at fertilization. Also found in fat cells, its function and the presence of post-translational modifications specific to such cells are still unclear. Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. {ECO:0000269|PubMed:23884607}." S37PK47MeK58dMe 685.81 "S,41;K,20;K,14;" 68 100 uniprot_mouse_length brain_HCD 958.3848267 953.861755 953.854444 15 14285.80326 7.665080495 H2B1A_MOUSE "Histone H2B type 1-A;AltName: Full=Histone H2B, testis;AltName: Full=Testis-specific histone H2B" P70696 PEVAVKGATISKKGFKKAVTKTQKKEGRKRKRCRKESYSIYIYKVLKQVHPDTGISSKAMSIMNSFVTDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 126 "FUNCTION: Variant histone specifically required to direct the transformation of dissociating nucleosomes to protamine in male germ cells. Entirely replaces classical histone H2B prior nucleosome to protamine transition and probably acts as a nucleosome dissociating factor that creates a more dynamic chromatin, facilitating the large-scale exchange of histones. Also expressed maternally and is present in the female pronucleus, suggesting a similar role in protamine replacement by nucleosomes at fertilization. Also found in fat cells, its function and the presence of post-translational modifications specific to such cells are still unclear. Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. {ECO:0000269|PubMed:23884607}." S37PK58dMeT116P 429.98 "S,24;K,5;T,16;" 52 100 uniprot_mouse_length brain_HCD 770.0769043 768.817749 768.815787 18 13813.67052 2.552007218 H2B1B_MOUSE Histone H2B type 1-B;AltName: Full=h2B-143 Q64475 PEPSKSAPAPKKGSKKAISKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." null 3727.84 null null 100 uniprot_mouse_length brain_HCD 627.6242065 629.671021 629.669827 22 13823.72255 1.895450221 H2B1C_MOUSE Histone H2B type 1-C/E/G Q6ZWY9 PEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." P1AcK46Me 764.33 "P,0;K,15;" 74 100 uniprot_mouse_length brain_HCD 777.2108765 780.356323 780.366296 18 14021.57968 -12.77958551 H2B1H_MOUSE Histone H2B type 1-H;AltName: Full=h2B-221 Q64478 PEPAKSAPAPKKGSKKALTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S14PS36PT115P 2322.94 "S,3;S,0;T,41;" 121 100 uniprot_mouse_length brain_HCD 777.2108765 780.356323 780.366296 18 14021.57968 -12.77958551 H2B1K_MOUSE Histone H2B type 1-K Q8CGP1 PEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S14PS36PT115P 2499.49 "S,7;S,0;T,66;" 144 100 uniprot_mouse_length brain_HCD 777.2108765 780.356323 780.366296 18 14021.57968 -12.77958551 H2B2B_MOUSE Histone H2B type 2-B;AltName: Full=H2b 616 Q64525 PDPAKSAPAPKKGSKKAVTKVQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S14PS36PT115P 2340.53 "S,5;S,0;T,41;" 120 100 uniprot_mouse_length brain_HCD 666.3599854 665.08252 665.085321 21 13938.77804 -4.212194528 H2B2E_MOUSE Histone H2B type 2-E;AltName: Full=H2b 613 Q64524 PELAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIANEASRLAHYNKRSTITSREIQTSVRLLLPGELAKHAVSEGTKAVTKYTSAK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." P1AcK5Ac 1082.95 "P,0;K,0;" 36 100 uniprot_mouse_length brain_HCD 666.3599854 665.08252 665.087054 21 13938.81444 -6.817857486 H2B2E_MOUSE Histone H2B type 2-E;AltName: Full=H2b 613 Q64524 PELAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIANEASRLAHYNKRSTITSREIQTSVRLLLPGELAKHAVSEGTKAVTKYTSAK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." P1AcK46MeK57dMe 1279.2 "P,0;K,28;K,18;" 46 100 uniprot_mouse_length brain_ETD 960.3352661 964.780884 964.78295 12 11559.38582 -2.141632932 APR_MOUSE Phorbol-12-myristate-13-acetate-induced protein 1;AltName: Full=Protein Noxa Q9JM54 MPGRKARRNAPVNPTRAELPPEFAAQLRKIGDKVYCTWSAPDITVVLAQMPGKSQKSRMRSPSPTRVPADLKDECAQLRRIGDKVNLRQKLLNLISKLFNLVT 103 "FUNCTION: Promotes activation of caspases and apoptosis. Promotes mitochondrial membrane changes and efflux of apoptogenic proteins from the mitochondria. Contributes to p53/TP53-dependent apoptosis after radiation exposure. Promotes proteasomal degradation of MCL1. Competes with BIM/BCL2L11 for binding to MCL1 and can displace BIM/BCL2L11 from its binding site on MCL1 (By similarity). Competes with BAK1 for binding to MCL1 and can displace BAK1 from its binding site on MCL1. {ECO:0000250, ECO:0000269|PubMed:10807576, ECO:0000269|PubMed:15694340, ECO:0000269|PubMed:15901672, ECO:0000269|PubMed:16822983, ECO:0000269|PubMed:17389404}." null 165.96 null null 100 uniprot_mouse_length brain_ETD 654.1795044 655.991028 655.995604 23 15057.88477 -6.975912553 ATPD_MOUSE "ATP synthase subunit delta, mitochondrial;AltName: Full=F-ATPase delta subunit;Flags: Precursor" Q9D3D9 AEAAAAPAPAAGPGQMSFTFASPTQVFFDSANVKQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHTEDGTTTKYFVSSGSVTVNADSSVQLLAEEAVTLDMLDLGAARANLEKAQSELSGAADEAARAEIQIRIEANEALVKALE 146 "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP turnover in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits." K114Ac 302.15 "K,11;" 46 100 uniprot_mouse_length brain_ETD 649.6040039 646.627502 646.626989 30 19357.78803 0.794030276 BTG1_MOUSE Protein BTG1;AltName: Full=B-cell translocation gene 1 protein P62325 MHPFYTRAATMIGEIAAAVSFISKFLRTKGLTSERQLQTFSQSLQELLAEHYKHHWFPEKPCKGSGYRCIRINHKMDPLIGQAAQRIGLSSQELFRLLPSELTLWVDPYEVSYRIGEDGSICVLYEASPAGGSTQNSTNVQMVDSRISCKEELLLGRTSPSKNYNMMTVSG 171 FUNCTION: Anti-proliferative protein. {ECO:0000250}. S159PS161P 329.56 "S,0;S,0;" 55 100 uniprot_mouse_length brain_ETD 543.0888672 542.701538 542.697895 42 22739.28471 6.712917023 C99L2_MOUSE CD99 antigen-like protein 2;AltName: Full=MIC2-like protein 1;AltName: CD_antigen=CD99;Flags: Precursor Q8BIF0 DTDGFNLEDALKETSSVKQRWDHFSTTTRRPVTTRAPANPAERWDHVATTTTRRPGTTRAPSNPMELDGFDLEDALDDRNDLDGPKKPSAGEAGGWSDKDLEDIVEGGGYKPDKNKGGGGYGSNDDPGSGISTETGTIAGVASALAMALIGAVSSYISYQQKKFCFSIQQGLNADYVKGENLEAVVCEEPQVTYSKQETQSAEPPPPEPPRI 212 "FUNCTION: Plays a role in a late step of leukocyte extravasation helping cells to overcome the endothelial basement membrane. Acts at the same site as, but independently of, PECAM1. Homophilic adhesion molecule, but these interactions may not be required for cell aggregation. {ECO:0000269|PubMed:17344467, ECO:0000269|PubMed:18163232, ECO:0000269|PubMed:20479283}." null 1187.74 null null 100 uniprot_mouse_length brain_ETD 623.7411499 627.67334 627.669134 31 19416.72226 6.70073375 EFNA1_MOUSE "Ephrin-A1;AltName: Full=EPH-related receptor tyrosine kinase ligand 1; Short=LERK-1;AltName: Full=Immediate early response protein B61;Contains: Ephrin-A1, secreted form;Flags: Precursor" P52793 ADRHIVFWNSSNPKFREEDYTVHVQLNDYLDIICPHYEDDSVADAAMERYTLYMVEHQEYVACQPQSKDQVRWNCNRPSAKHGPEKLSEKFQRFTPFILGKEFKEGHSYYYISKPIYHQESQCLKLKVTVNGKITHNPQAHVNPQEKRLQADDPEVQVLHSIGYS 165 "FUNCTION: Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. Plays an important role in angiogenesis and tumor neovascularization. The recruitment of VAV2, VAV3 and PI3-kinase p85 subunit by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly. Exerts anti-oncogenic effects in tumor cells through activation and down-regulation of EPHA2. Activates EPHA2 by inducing tyrosine phosphorylation which leads to its internalization and degradation. Acts as a negative regulator in the tumorigenesis of gliomas by down-regulating EPHA2 and FAK. Can evoke collapse of embryonic neuronal growth cone and regulates dendritic spine morphogenesis. {ECO:0000269|PubMed:16782872, ECO:0000269|PubMed:17143272, ECO:0000269|PubMed:18387945}." null 2074.41 null null 100 uniprot_mouse_length brain__ETD_4 543.0888672 539.716797 539.714256 29 15613.70099 4.707815241 F136A_MOUSE Protein FAM136A Q9CR98 AEVQQLRVQEAVDAMVKSVERENIRKMQGLMFRCSANCCEDTQASMQQVHQCIERCHAPLAQAQALVTSELERFQDRLARCTMHCNDKAKDSMDAGTKELQVKRQLDSCVTKCVDDHMHLIPTMTKKMKESLSSIGK 137 SUBCELLULAR LOCATION: Mitochondrion. T123P 630.66 "T,3;" 92 100 uniprot_mouse_length brain__ETD_4 589.0163574 585.063965 585.060077 12 7005.71864 6.645204318 GBG7_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-7;Flags: Precursor Q61016 SGTNNVAQARKLVEQLRIEAGIERIKVSKASSDLMGYCEQHARNDPLLVGVPASENPFKDKKPC 64 "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction. Plays a role in the regulation of adenylyl cyclase signaling in certain regions of the brain. Plays a role in the formation or stabilzation of a G protein heterotrimer (G(olf) subunit alpha-beta-gamma-7) that is required for adenylyl cyclase activity in the striatum. {ECO:0000269|PubMed:12488442}." null 635.77 null null 100 uniprot_mouse_length brain_ETD 543.0888672 538.441162 538.441018 22 11817.69461 0.267641896 GPHB5_MOUSE Glycoprotein hormone beta-5;AltName: Full=Thyrostimulin subunit beta;Flags: Precursor Q812B2 SSSGNLHTFVGCAVREFTFMAKKPGCRGLRITTDACWGRCETWEKPILEPPYIEAYHRVCTYNETRQVTVKLPNCAPGVDPFYTYPMAVRCDCGACSTATTECETI 106 "FUNCTION: Stimulates the thyroid. Binds and activates THSR, leading to increased cAMP production (By similarity). {ECO:0000250}." null 287.32 null null 100 uniprot_mouse_length brain_ETD 764.4804688 760.093079 760.093619 13 9864.21122 -0.71094758 ACBP_MOUSE Acyl-CoA-binding protein; Short=ACBP;AltName: Full=Diazepam-binding inhibitor; Short=DBI;AltName: Full=Endozepine; Short=EP P31786 SQAEFDKAAEEVKRLKTQPTDEEMLFIYSHFKQATVGDVNTDRPGLLDLKGKAKWDSWNKLKGTSKESAMKTYVEKVDELKKKYGI 86 FUNCTION: Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA receptor. null 5071.77 null null 100 uniprot_mouse_length brain_ETD 676.1279907 676.293213 676.294214 12 8100.52739 -1.480286766 ATP5I_MOUSE "ATP synthase subunit e, mitochondrial; Short=ATPase subunit e" Q06185 VPPVQVSPLIKFGRYSALIIGMAYGAKRYSYLKPRAEEERRIAAEEKKRLDELKRIERELAEAQDDSILK 70 "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane." null 2357.69 null null 100 uniprot_mouse_length brain_ETD 1008.895203 1011.899841 1011.888073 11 11114.76199 11.63004971 BID_MOUSE BH3-interacting domain death agonist;AltName: Full=p22 BID; Short=BID;Contains: BH3-interacting domain death agonist p15; AltName: Full=p15 BID;Contains: BH3-interacting domain death agonist p13; AltName: Full=p13 BID;Contains: BH3-interacting domain death agonist p11; AltName: Full=p11 BID P70444 HNIQPTLVRQLAAQFMNGSLSEEDKRNCLAKALDEVKTAFPRDMENDKAMLIMTMLLAKKVASHAPSLLRDVFHTTVNFINQNLFSYVRNLVRNEMD 97 FUNCTION: Induces caspases and apoptosis. Counters the protective effect of Bcl-2. The major proteolytic product p15 BID allows the release of cytochrome c. {ECO:0000269|PubMed:9873064}. null 261.77 null null 100 uniprot_mouse_length brain_ETD 708.6588745 706.178833 706.181825 28 19734.0688 -4.236858103 CETN2_MOUSE Centrin-2;AltName: Full=Caltractin isoform 1 Q9R1K9 ASNFKKTTMASSAQRKRMSPKPELTEDQKQEIREAFDLFDADGTGTIDIKELKVAMRALGFEPKKEEIKKMISEIDKEGTGKMNFSDFLTVMTQKMSEKDTKEEILKAFKLFDDDETGKISFKNLKRVAKELGENLTDEELQEMIDEADRDGDGEVNEQEFLRIMKKTSLY 171 FUNCTION: Plays a fundamental role in microtubule organizing center structure and function. Required for centriole duplication and correct spindle formation. Has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CCP110 (By similarity). {ECO:0000250}. S19P 1694.69 "S,3;" 147 100 uniprot_mouse_length brain_ETD 680.9863892 681.361389 681.36133 8 5440.8904 0.086826407 COX7C_MOUSE "Cytochrome c oxidase subunit 7C, mitochondrial;AltName: Full=Cytochrome c oxidase polypeptide VIIc;Flags: Precursor" P17665 SHYEEGPGKNLPFSVENKWRLLAMMTVYFGSGFAAPFFIVRHQLLKK 47 "FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport." null 2648.74 null null 100 uniprot_mouse_length brain_ETD 802.1567993 801.567139 801.556513 13 10402.22751 13.25629784 DYL1_MOUSE "Dynein light chain 1, cytoplasmic;AltName: Full=8 kDa dynein light chain; Short=DLC8;AltName: Full=Dynein light chain LC8-type 1;AltName: Full=Protein inhibitor of neuronal nitric oxide synthase; Short=PIN; Short=mPIN" P63168 MCDRKAVIKNADMSEEMQQDSVECATQALEKYNIEKDIAAHIKKEFDKKYNPTWHCIVGRNFGSYVTHETKHFIYFYLGQVAILLFKSG 89 FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures (By similarity). {ECO:0000250}. K36Ac 309.11 "K,30;" 32 100 uniprot_mouse_length brain_ETD 779.1547241 783.764282 783.76005 16 12518.15112 5.399900853 DYLT1_MOUSE Dynein light chain Tctex-type 1;AltName: Full=Activator of G-protein signaling 2; Short=AGS2;AltName: Full=T-complex testis-specific protein 1;AltName: Full=TCTEX-1 P51807 MEDFQASEETAFVVDEVSSIVKEAIESAIGGNAYQHSKVNQWTTNVLEQTLSQLTKLGRPFKYIVTCVIMQKNGAGLHSASSCFWDSSTDGSCTVRWENKTMYCIVSTFGLSI 113 FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Binds to transport cargos and is involved in apical cargo transport such as rhodopsin-bearing vesicles in polarized epithelia. Is involved in intracellular targeting of D-type retrovirus gag polyproteins to the cytoplasmic assembly site (By similarity). May also be a accessory component of axonemal dynein. Plays an important role in male germ cell development and function. Candidate for involvement in male sterility. {ECO:0000250}. M1Ac 397.94 "M,30;" 61 100 uniprot_mouse_length brain_ETD 845.0955811 845.262817 845.25209 12 10126.0179 12.69134136 BAF_MOUSE "Barrier-to-autointegration factor;AltName: Full=Breakpoint cluster region protein 1;AltName: Full=LAP2-binding protein 1;Contains: Barrier-to-autointegration factor, N-terminally processed" O54962 TTSQKHRDFVAEPMGEKPVGSLAGIGDVLSKRLEERGFDKAYVVLGQFLVLKKDEDLFREWLKDTCGANAKQSRDCFGCLREWCDAFL 88 "FUNCTION: Plays fundamental roles in nuclear assembly, chromatin organization, gene expression and gonad development. May potently compress chromatin structure and be involved in membrane recruitment and chromatin decondensation during nuclear assembly. Contains 2 non-specific dsDNA-binding sites which may promote DNA cross-bridging (By similarity). {ECO:0000250}." T1PT2P 380.54 "T,0;T,0;" 40 100 uniprot_mouse_length brain_ETD 845.0955811 847.013062 847.004525 10 8456.04175 10.07848622 CRIP1_MOUSE Cysteine-rich protein 1; Short=CRP-1;AltName: Full=Cysteine-rich intestinal protein; Short=CRIP P63254 PKCPKCDKEVYFAERVTSLGKDWHRPCLKCEKCGKTLTSGGHAEHEGKPYCNHPCYSAMFGPKGFGRGGAESHTFK 76 FUNCTION: Seems to have a role in zinc absorption and may function as an intracellular zinc transport protein. K8Ac 206.65 "K,0;" 26 100 uniprot_mouse_length brain_ETD 1104.914429 1103.415894 1103.413102 6 6611.47609 2.52992708 CX7A2_MOUSE "Cytochrome c oxidase subunit 7A2, mitochondrial;AltName: Full=Cytochrome c oxidase subunit VIIa-liver/heart; Short=Cytochrome c oxidase subunit VIIa-L;Flags: Precursor" P48771 FENKVPEKQKLFQEDNGMPVHLKGGASDALLYRATMALTLGGTAYAIYLLAMAAFPKKQN 60 "FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport." K10Ac 141 "K,2;" 20 100 uniprot_mouse_length brain_ETD 762.3217163 759.769531 759.773924 13 9859.05501 -5.78165407 DBIL5_MOUSE Diazepam-binding inhibitor-like 5;AltName: Full=Endozepine-like peptide; Short=ELP O09035 MSQVEFEMACASLKQLKGPVSDQEKLLVYSFYKQATQGDCNIPVPPATDVRAKAKYEAWMVNKGMSKMDAMRIYIAKVEELKKKEPC 87 FUNCTION: May be involved in the energy metabolism of the mature sperm. null 290.42 null null 100 uniprot_mouse_length brain_ETD 941.7801514 944.351929 944.342047 14 13199.77633 10.46412258 GHRL_MOUSE Appetite-regulating hormone;AltName: Full=Growth hormone secretagogue;AltName: Full=Growth hormone-releasing peptide;AltName: Full=Motilin-related peptide;AltName: Full=Protein M46;Contains: Ghrelin;Contains: Obestatin;Flags: Precursor Q9EQX0 MLSSGTICSLLLLSMLWMDMAMAGSSFLSPEHQKAQQRKESKKPPAKLQPRALEGWLHPEDRGQAEETEEELEIRFNAPFDVGIKLSGAQYQQHGRALGKFLQDILWEEVKEAPADK 117 "FUNCTION: Ghrelin is the ligand for growth hormone secretagogue receptor type 1 (GHSR). Induces the release of growth hormone from the pituitary. Has an appetite-stimulating effect, induces adiposity and stimulates gastric acid secretion. Involved in growth regulation." null 392.52 null null 100 uniprot_mouse_length brain_ETD 887.1710815 888.876282 888.877223 16 14199.02145 -1.058933331 H2A1K_MOUSE Histone H2A type 1-K Q8CGP7 SGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTETHHKAKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1PR3dMeT120P 626.76 "S,43;R,50;T,45;" 77 100 uniprot_mouse_length brain_ETD 876.5638428 879.001648 879.001029 16 14041.00268 0.704150733 H2A2A_MOUSE Histone H2A type 2-A;AltName: Full=H2a-614;AltName: Full=H2a-615;AltName: Full=Histone H2A.2 Q6GSS7 SGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYMAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKKTESHHKAKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1AcK5Ac 333.67 "S,0;K,1;" 47 100 uniprot_mouse_length brain_ETD 779.0856323 776.50177 776.492306 18 13951.84775 12.1881691 H2B1P_MOUSE Histone H2B type 1-P Q8CGP2 PEPVKSVPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." K57dMeR79dMeK85tMe 473.58 "K,10;R,6;K,58;" 58 100 uniprot_mouse_length brain_ETD 796.4230347 792.25708 792.248642 19 15025.70998 10.65079532 IFM3_MOUSE Interferon-induced transmembrane protein 3;AltName: Full=Dispanin subfamily A member 2b; Short=DSPA2b;AltName: Full=Fragilis protein;AltName: Full=Interferon-inducible protein 15;AltName: Full=Mouse ifitm-like protein 1; Short=Mil-1 Q9CQW9 MNHTSQAFITAASGGQPPNYERIKEEYEVAEMGAPHGSASVRTTVINMPREVSVPDHVVWSLFNTLFMNFCCLGFIAYAYSVKSRDRKMVGDVTGAQAYASTAKCLNISTLVLSILMVVITIVSVIIIVLNAQNLHT 137 "FUNCTION: IFN-induced antiviral protein which inhibits the entry of viruses to the host cell cytoplasm, permitting endocytosis, but preventing subsequent viral fusion and release of viral contents into the cytosol. Active against multiple viruses, including influenza A virus, SARS coronavirus (SARS-CoV), Marburg virus (MARV) and Ebola virus (EBOV), Dengue virus (DNV), West Nile virus (WNV) and human immunodeficiency virus type 1 (HIV-1). Can inhibit: influenza virus hemagglutinin protein-mediated viral entry, MARV and EBOV GP1,2-mediated viral entry and SARS-CoV S protein-mediated viral entry. Plays a critical role in the structural stability and function of vacuolar ATPase (v-ATPase). Establishes physical contact with the v-ATPase of endosomes which is critical for proper clathrin localization and is also required for the function of the v-ATPase to lower the pH in phagocytic endosomes thus establishing an antiviral state. Involved in initiating germ cell competence and specification, and in the demarcation of PGCs from their somatic neighbors. {ECO:0000269|PubMed:12124616, ECO:0000269|PubMed:18505827, ECO:0000269|PubMed:21253575, ECO:0000269|PubMed:22467717}." Y27P 161.25 "Y,20;" 32 100 uniprot_mouse_length brain_ETD 767.0212402 769.572937 769.584315 10 7682.84104 -14.78458963 GBG12_MOUSE Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12;Flags: Precursor Q9DAS9 SSKTASTNSIAQARRTVQQLRLEASIERIKVSKASADLMSYCEEHARSDPLLMGIPTSENPFKDKKTC 68 "FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction." S25PS48P 151.12 "S,8;S,6;" 30 100 uniprot_mouse_length brain_ETD 764.555481 763.326233 763.325202 13 9906.22179 1.350551709 ACBP_MOUSE Acyl-CoA-binding protein; Short=ACBP;AltName: Full=Diazepam-binding inhibitor; Short=DBI;AltName: Full=Endozepine; Short=EP P31786 SQAEFDKAAEEVKRLKTQPTDEEMLFIYSHFKQATVGDVNTDRPGLLDLKGKAKWDSWNKLKGTSKESAMKTYVEKVDELKKKYGI 86 FUNCTION: Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA receptor. S1Ac 6600.02 "S,1;" 152 100 uniprot_mouse_length brain_ETD 633.8651733 629.196655 629.193127 16 10046.08284 5.607615986 BAF_MOUSE "Barrier-to-autointegration factor;AltName: Full=Breakpoint cluster region protein 1;AltName: Full=LAP2-binding protein 1;Contains: Barrier-to-autointegration factor, N-terminally processed" O54962 TTSQKHRDFVAEPMGEKPVGSLAGIGDVLSKRLEERGFDKAYVVLGQFLVLKKDEDLFREWLKDTCGANAKQSRDCFGCLREWCDAFL 88 "FUNCTION: Plays fundamental roles in nuclear assembly, chromatin organization, gene expression and gonad development. May potently compress chromatin structure and be involved in membrane recruitment and chromatin decondensation during nuclear assembly. Contains 2 non-specific dsDNA-binding sites which may promote DNA cross-bridging (By similarity). {ECO:0000250}." T1P 140.08 "T,0;" 15 100 uniprot_mouse_length brain_ETD 610.843811 611.67981 611.683701 33 20141.5366 -6.361833217 CHAC2_MOUSE Putative glutathione-specific gamma-glutamylcyclotransferase 2 {ECO:0000250|UniProtKB:Q9BUX1}; Short=Gamma-GCG 2 {ECO:0000250|UniProtKB:Q9BUX1}; EC=2.3.2.- {ECO:0000250|UniProtKB:Q9BUX1};AltName: Full=Cation transport regulator-like protein 2 {ECO:0000250|UniProtKB:Q9BUX1} Q9CQG1 MWVFGYGSLIWKVDFPYQDKLVGYITNYSRRFWQGSTDHRGVPGKPGRVVTLVEDPGGSVWGVAYKLPVGKEEEVKTYLDFREKGGYRTTTVIFYPKDSTTKPFSVLLYIGTCDNPNYLGPAPLEDIAEQIFNAAGPSGRNTEYLFELADSVRKLVPEDADEHLFSLEKLVKERLEGK 178 "FUNCTION: Catalyzes the cleavage glutathione into 5-oxoproline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides. {ECO:0000250|UniProtKB:P32656}." null 728.89 null null 100 uniprot_mouse_length brain_ETD 522.1417847 521.235291 521.230759 23 11959.2974 8.693898557 CISD1_MOUSE CDGSH iron-sulfur domain-containing protein 1;AltName: Full=MitoNEET Q91WS0 GLSSNSAVRVEWIAAVTFAAGTAALGYLAYKKFYAKENRTKAMVNLQIQKDNPKVVHAFDMEDLGDKAVYCRCWRSKKFPFCDGAHIKHNEETGDNVGPLIIKKKET 107 FUNCTION: Plays a key role in regulating maximal capacity for electron transport and oxidative phosphorylation. May be involved in Fe-S cluster shuttling and/or in redox reactions (By similarity). {ECO:0000250}. null 1184.61 null null 100 uniprot_mouse_length brain_ETD 576.3630981 575.488525 575.48672 25 14355.15527 3.137154277 CK052_MOUSE Uncharacterized protein C11orf52 homolog Q9D8L0 MGNRLCCGGTWSCPSTFQKKSKTGSHPRPTLSILKQQQLWQNGTKDYETTAPTYEQVLYPPASQKKTSNSTSEESDLHYADIHVLRQIRPHSLHTVKCLHSESATEYATLRFPQATPQYDSNNGTLV 127 "ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9D8L0-1; Sequence=Displayed; Name=2; IsoId=Q9D8L0-2; Sequence=VSP_021875;-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" T30P 1510.33 "T,18;" 124 100 uniprot_mouse_length brain_ETD 907.807312 908.450134 908.449926 11 9976.94199 0.22926673 CX6B1_MOUSE Cytochrome c oxidase subunit 6B1;AltName: Full=Cytochrome c oxidase subunit VIb isoform 1; Short=COX VIb-1 P56391 AEDIKTKIKNYKTAPFDSRFPNQNQTKNCWQNYLDFHRCEKAMTAKGGDVSVCEWYRRVYKSLCPVSWVSAWDDRIAEGTFPGKI 85 FUNCTION: Connects the two COX monomers into the physiological dimeric form. {ECO:0000250}. A1Ac 2309.87 "A,52;" 97 100 uniprot_mouse_length brain_ETD 764.555481 764.048828 764.041277 10 7627.41029 9.883137505 CXCL5_MOUSE C-X-C motif chemokine 5;AltName: Full=Cytokine LIX;AltName: Full=Small-inducible cytokine B5;Contains: GCP-2(1-78);Contains: GCP-2(9-78);Flags: Precursor P50228 TELRCVCLTVTPKINPKLIANLEVIPAGPQCPTVEVIAKLKNQKEVCLDPEAPVIKKIIQKILGSDKKKA 70 "FUNCTION: May participate in the recruitment of inflammatory cells by injured or infected tissue. GCP-2(1-78) and, more potent, GCP- 2(9-78) attract neutrophils and are involved in neutrophil activation. {ECO:0000269|PubMed:10570306}." null 859.57 null null 100 uniprot_mouse_length brain_ETD 871.0635376 871.063538 871.076143 10 8696.75773 -14.47106828 CXL10_MOUSE C-X-C motif chemokine 10;AltName: Full=10 kDa interferon gamma-induced protein; Short=Gamma-IP10; Short=IP-10;AltName: Full=C7;AltName: Full=Interferon-gamma induced protein CRG-2;AltName: Full=Small-inducible cytokine B10;Flags: Precursor P17515 IPLARTVRCNCIHIDDGPVRMRAIGKLEIIPASLSCPRVEIIATMKKNDEQRCLNPESKTIKNLMKAFSQKRSKRAP 77 "FUNCTION: In addition to its role as a proinflammatory cytokine, may participate in T-cell effector function and perhaps T-cell development." null 453.33 null null 100 uniprot_mouse_length brain_ETD 650.3547974 646.055481 646.05307 23 14828.20827 3.731825051 CYYR1_MOUSE Cysteine and tyrosine-rich protein 1;AltName: Full=Proline-rich domain-containing protein;Flags: Precursor Q8VIH7 QCGKECHSYCCDGSTPYCCSYYAYIGNILSGTAIAGIVFGIVFIMGVIAGIAICICMCMKNNRGTRVGVIRAAHINAISYPMAPPPYTYDHEMEYRTDLPPPYSAAPQASAQRSPPPPYPGNPRKYSSSQNRIRDN 136 SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. null 122.77 null null 100 uniprot_mouse_length brain_ETD 614.2211914 613.066833 613.066838 36 22022.38055 -0.007346517 DENR_MOUSE Density-regulated protein; Short=DRP Q9CQJ6 ATDISESSGADCKGDTKNSAKLDADYPLRVLYCGVCSLPTEYCEYMPDVAKCRQWLEKNFPNEFAKLTVENSPKQETGITEGQGPVGEEEEKKKQKRGGRGQIKQKKKTVPQKVTIAKIPRAKKKYVTRVCGLATFEIDLKEAQRFFAQKFSCGASVTGEDEIIIQGDFTDDIIDVIQEKWPEVDDDSIEDLGEVKK 197 FUNCTION: May be involved in the translation of target mRNAs by scanning and recognition of the initiation codon. Involved in translation initiation; promotes recruitment of aminoacetyled initiator tRNA to P site of 40S ribosomes. Can promote release of deacylated tRNA and mRNA from recycled 40S subunits following ABCE1-mediated dissociation of post-termination ribosomal complexes into subunits (By similarity). {ECO:0000250}. null 467.9 null null 100 uniprot_mouse_length brain_ETD 610.843811 613.57196 613.570679 27 16531.39248 2.088511173 DPOE3_MOUSE DNA polymerase epsilon subunit 3; EC=2.7.7.7;AltName: Full=DNA polymerase II subunit 3;AltName: Full=DNA polymerase epsilon subunit p17;AltName: Full=NF-YB-like protein;AltName: Full=YB-like protein 1; Short=YBL1 Q9JKP7 AERPEDLNLPNAVITRIIKEALPDGVNISKEARSAISRAASVFVLYATSCANNFAMKGKRKTLNASDVLSAMEEMEFQRFITPLKEALEAYRRDEKGKKEASEQKKKDKDKKDSEEQDKSREVEEEDEERLDEDDQNEEEEIDN 144 "FUNCTION: Forms a complex with DNA polymerase epsilon subunit CHRAC1 and binds naked DNA, which is then incorporated into chromatin, aided by the nucleosome-remodeling activity of ISWI/SNF2H and ACF1. {ECO:0000250}." A1Ac 424.68 "A,33;" 62 100 uniprot_mouse_length brain_ETD 576.3630981 574.335571 574.333 33 18909.96997 4.477000386 EID1_MOUSE EP300-interacting inhibitor of differentiation 1;AltName: Full=CREBBP/EP300 inhibitory protein 1;AltName: Full=E1A-like inhibitor of differentiation 1; Short=EID-1 Q9DCR4 MAEMAELCELYEESNELQMDVLPGEGYMEVGRGARGPAPEEGPMEEEAGPAAARAQRGLFPEAGADLEGDEFDDWEDDYEFPEEERWSGAMHRVSAALEEANKVFLRTARAGDALDGGFQARCEKSPFDQLAFIEELFSLMVVNRLTEELGCDEIIDRELMLTREEETT 169 FUNCTION: Interacts with RB1 and EP300 and acts as a repressor of MYOD1 transactivation. Inhibits EP300 and CBP histone acetyltransferase activity. May be involved in coupling cell cycle exit to the transcriptional activation of genes required for cellular differentiation. May act as a candidate coinhibitory factor for NR0B2 that can be directly linked to transcription inhibitory mechanisms. {ECO:0000269|PubMed:11964378}. null 3272 null null 100 uniprot_mouse_length brain_ETD 547.2382813 544.772583 544.77007 26 14131.00807 4.612969674 H2A2A_MOUSE Histone H2A type 2-A;AltName: Full=H2a-614;AltName: Full=H2a-615;AltName: Full=Histone H2A.2 Q6GSS7 SGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYMAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKKTESHHKAKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1PQ104MeT120P 115.64 "S,12;Q,21;T,0;" 27 100 uniprot_mouse_length brain_ETD 610.843811 611.011414 611.020454 25 15243.49712 -14.79561891 H2AX_MOUSE Histone H2AX; Short=H2a/x;AltName: Full=Histone H2A.X P27661 SGRGKTGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGHYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGGVTIAQGGVLPNIQAVLLPKKSSATVGPKAPAVGKKASQASQEY 142 "FUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Required for checkpoint-mediated arrest of cell cycle progression in response to low doses of ionizing radiation and for efficient repair of DNA double strand breaks (DSBs) specifically when modified by C- terminal phosphorylation. {ECO:0000269|PubMed:11740565, ECO:0000269|PubMed:11934988, ECO:0000269|PubMed:12034884, ECO:0000269|PubMed:12447390, ECO:0000269|PubMed:12660252, ECO:0000269|PubMed:12689589, ECO:0000269|PubMed:12792649, ECO:0000269|PubMed:12914700, ECO:0000269|PubMed:12914701, ECO:0000269|PubMed:14530383, ECO:0000269|PubMed:15574327, ECO:0000269|PubMed:15580272, ECO:0000269|PubMed:15589157, ECO:0000269|PubMed:15610743, ECO:0000269|PubMed:15632067}." S1PS139PY142P 763.96 "S,58;S,0;Y,0;" 87 100 uniprot_mouse_length brain_ETD 614.2211914 616.68866 616.693108 23 14153.92808 -7.213202116 H2B1A_MOUSE "Histone H2B type 1-A;AltName: Full=Histone H2B, testis;AltName: Full=Testis-specific histone H2B" P70696 PEVAVKGATISKKGFKKAVTKTQKKEGRKRKRCRKESYSIYIYKVLKQVHPDTGISSKAMSIMNSFVTDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 126 "FUNCTION: Variant histone specifically required to direct the transformation of dissociating nucleosomes to protamine in male germ cells. Entirely replaces classical histone H2B prior nucleosome to protamine transition and probably acts as a nucleosome dissociating factor that creates a more dynamic chromatin, facilitating the large-scale exchange of histones. Also expressed maternally and is present in the female pronucleus, suggesting a similar role in protamine replacement by nucleosomes at fertilization. Also found in fat cells, its function and the presence of post-translational modifications specific to such cells are still unclear. Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. {ECO:0000269|PubMed:23884607}." P1AcK47Me 145.28 "P,0;K,6;" 26 100 uniprot_mouse_length brain_ETD 695.769165 692.745056 692.735773 20 13827.70182 13.40071165 H2B1B_MOUSE Histone H2B type 1-B;AltName: Full=h2B-143 Q64475 PEPSKSAPAPKKGSKKAISKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." K46Me 268.84 "K,5;" 38 100 uniprot_mouse_length brain_ETD 621.9711914 622.789124 622.783347 21 13051.44037 9.275352631 4EBP2_MOUSE Eukaryotic translation initiation factor 4E-binding protein 2 {ECO:0000250|UniProtKB:Q13542}; Short=4E-BP2 {ECO:0000250|UniProtKB:Q13542}; Short=eIF4E-binding protein 2 {ECO:0000250|UniProtKB:Q13542};AltName: Full=Phosphorylated heat- and acid-stable protein regulated by insulin 2 {ECO:0000303|PubMed:8939971}; Short=PHAS-II {ECO:0000303|PubMed:8939971} P70445 MSASAGGSHQPSQSRAIPTRTVAISDAAQLPQDYCTTPGGTLFSTTPGGTRIIYDRKFLLDRRNSPMAQTPPCHLPNIPGVTSPGALIEDSKVEVNNLNNLNNHDRKHAVGDEAQFEMDI 120 "FUNCTION: Repressor of translation initiation involved in synaptic plasticity, learning and memory formation (PubMed:16237163, PubMed:17029989). Regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form of EIF4EBP2 competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. In contrast, hyperphosphorylated form dissociates from EIF4E, allowing interaction between EIF4G1/EIF4G3 and EIF4E, leading to initiation of translation (PubMed:17029989, PubMed:20347422, PubMed:23172145). EIF4EBP2 is enriched in brain and acts as a regulator of synapse activity and neuronal stem cell renewal via its ability to repress translation initiation (PubMed:20347422, PubMed:24139800, PubMed:23172145). Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways (PubMed:8939971). {ECO:0000250|UniProtKB:Q13542, ECO:0000269|PubMed:16237163, ECO:0000269|PubMed:17029989, ECO:0000269|PubMed:20347422, ECO:0000269|PubMed:23172145, ECO:0000269|PubMed:24139800, ECO:0000269|PubMed:8939971}." T37PT46P 148.07 "T,2;T,0;" 28 100 uniprot_mouse_length brain_ETD 714.3101807 715.944702 715.944143 25 17864.58427 0.780994499 AGR2_MOUSE Anterior gradient protein 2 homolog; Short=AG-2; Short=mAG-2;AltName: Full=Protein Gob-4;AltName: Full=Secreted cement gland protein XAG-2 homolog;Flags: Precursor O88312 KDTTVKSGAKKDPKDSRPKLPQTLSRGWGDQLIWTQTYEEALYRSKTSNRPLMVIHHLDECPHSQALKKVFAEHKEIQKLAEQFVLLNLVYETTDKHLSPDGQYVPRIVFVDPSLTVRADITGRYSNRLYAYEPSDTALLYDNMKKALKLLKTEL 155 "FUNCTION: Required for MUC2 post-transcriptional synthesis and secretion. May play a role in the production of mucus by intestinal cells. Proto-oncogene that may play a role in cell migration, cell differentiation and cell growth (By similarity). {ECO:0000250}." null 774.15 null null 100 uniprot_mouse_length brain_ETD 647.5200195 644.254211 644.25181 37 23787.28999 3.727464547 ALRF2_MOUSE Aly/REF export factor 2;AltName: Full=Alyref;AltName: Full=RNA and export factor-binding protein 2 Q9JJW6 MADKMDMSLDDIIKLNRNQRRVNRGGGPRRNRPAIARGGRNRPAPYSRPKPLPDKWQHDLFDSGCGGGEGVETGAKLLVSNLDFGVSDADIQELFAEFGTLKKAAVDYDRSGRSLGTADVHFERRADALKAMKQYKGVPLDGRPMDIQLVASQIDPQRRPAQSGNRGGMTRSRGSGGFGGRGSQGRGRGTGRNSKQQQLSAEELDAQLDAYNARMDTS 218 "FUNCTION: Export adapter involved in spliced and unspliced mRNA nuclear export. Binds mRNA which is transferred to the NXF1-NXT1 heterodimer for export (TAP/NFX1 pathway); enhances NXF1-NXT1 RNA- binding activity. {ECO:0000269|PubMed:10786854, ECO:0000269|PubMed:11158589, ECO:0000269|PubMed:18364396}." R24dMeR32dMeR37Me 1234.92 "R,3;R,0;R,0;" 149 100 uniprot_mouse_length brain_ETD 544.1689453 541.782715 541.785492 53 28647.59999 -5.125933217 AQP1_MOUSE Aquaporin-1; Short=AQP-1;AltName: Full=Aquaporin-CHIP;AltName: Full=Delayed early response protein 2; Short=DER2;AltName: Full=Water channel protein for red blood cells and kidney proximal tubule Q02013 ASEIKKKLFWRAVVAEFLAMTLFVFISIGSALGFNYPLERNQTLVQDNVKVSLAFGLSIATLAQSVGHISGAHLNPAVTLGLLLSCQISILRAVMYIIAQCVGAIVATAILSGITSSLVDNSLGRNDLAHGVNSGQGLGIEIIGTLQLVLCVLATTDRRRRDLGGSAPLAIGLSVALGHLLAIDYTGCGINPARSFGSAVLTRNFSNHWIFWVGPFIGGALAVLIYDFILAPRSSDFTDRMKVWTSGQVEEYDLDADDINSRVEMKPK 268 "FUNCTION: Forms a water-specific channel that provides the plasma membranes of red cells and kidney proximal tubules with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient. {ECO:0000269|PubMed:12133842}." null 741.09 null null 100 uniprot_mouse_length brain_ETD 907.5322266 909.580994 909.581439 21 19070.18894 -0.489618232 ARL11_MOUSE ADP-ribosylation factor-like protein 11 Q6P3A9 GSVNSRGHKAEAQVVMMGLDSAGKTTILYKLKGNQLVDTLPTVGFNVEPLEAPGHVSLTLWDIGGQTQLRATWKDYLEGIDLLVYVLDSTDEARLPEAVAELKEVLEDPNMAGVPFLVLANKQEAPGALPLLEIRNRLGLEGFQKHCWELRACSALTGQGLQEALQSLLHLLKSR 175 FUNCTION: May play a role in apoptosis. May act as a tumor suppressor (By similarity). {ECO:0000250}. null 458.1 null null 100 uniprot_mouse_length brain__ETD_2 1003.970093 1002.531006 1002.521717 15 15015.81165 9.26549442 ATPD_MOUSE "ATP synthase subunit delta, mitochondrial;AltName: Full=F-ATPase delta subunit;Flags: Precursor" Q9D3D9 AEAAAAPAPAAGPGQMSFTFASPTQVFFDSANVKQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHTEDGTTTKYFVSSGSVTVNADSSVQLLAEEAVTLDMLDLGAARANLEKAQSELSGAADEAARAEIQIRIEANEALVKALE 146 "FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP turnover in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits." null 304.82 null null 100 uniprot_mouse_length brain_ETD 770.4797363 766.900452 766.89824 26 19902.331 2.883903028 B2LA1_MOUSE Bcl-2-related protein A1;AltName: Full=A1-A;AltName: Full=Hemopoietic-specific early response protein;AltName: Full=Protein BFL-1 Q07440 MAESELMHIHSLAEHYLQYVLQVPAFESAPSQACRVLQRVAFSVQKEVEKNLKSYLDDFHVESIDTARIIFNQVMEKEFEDGIINWGRIVTIFAFGGVLLKKLPQEQIALDVCAYKQVSSFVAEFIMNNTGEWIRQNGGWEDGFIKKFEPKSGWLTFLQMTGQIWEMLFLLK 172 FUNCTION: Retards apoptosis induced by IL-3 deprivation. May function in the response of hemopoietic cells to external signals and in maintaining endothelial survival during infection. Can inhibit apoptosis induced by serum starvation in the mammary epithelial cell line HC11 (PubMed:11888890). {ECO:0000269|PubMed:11888890}. null 1024.48 null null 100 uniprot_mouse_length brain_ETD 650.3545532 649.07959 649.082784 34 22023.78903 -4.921030612 BASP1_MOUSE Brain acid soluble protein 1;AltName: Full=22 kDa neuronal tissue-enriched acidic protein;AltName: Full=Neuronal axonal membrane protein NAP-22 Q91XV3 GGKLSKKKKGYNVNDEKAKDKDKKAEGAGTEEEGTPKESEPQAAADATEVKESTEEKPKDAADGEAKAEEKEADKAAAAKEEAPKAEPEKSEGAAEEQPEPAPAPEQEAAAPGPAAGGEAPKAGEASAESTGAADGAAPEEGEAKKTEAPAAAGPEAKSDAAPAASDSKPSSAEPAPSSKETPAASEAPSSAAKAPAPAAPAAAEPQAEAPAAAASSEQSVAVKE 225 "SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. Cell projection, growth cone. Note=Associated with the membranes of growth cones that form the tips of elongating axons." T30P 413.1 "T,0;" 96 100 uniprot_mouse_length brain_ETD 658.1273804 654.559265 654.568542 22 14371.49615 -14.17248567 BOLA1_MOUSE BolA-like protein 1 Q9D8S9 MLSARSAQCMVSMATRSCVSRGSAGSAAAGPVEAAIRAKLEQALSPEVLELRNESGGHAVPAGSETHFRVAVVSSRFEGMSPLQRHRLVHEALSEELAGPVHALAIQAKTPAQWRENPQLDISPPCLGGSKKTRGTS 137 SUBCELLULAR LOCATION: Secreted. Note=Could be secreted via a non- classical export pathway. {ECO:0000250}. null 165.82 null null 100 uniprot_mouse_length brain_ETD 650.3545532 645.481262 645.482222 37 23832.81164 -1.486939432 C1QBP_MOUSE "Complement component 1 Q subcomponent-binding protein, mitochondrial;AltName: Full=GC1q-R protein;AltName: Full=Glycoprotein gC1qBP; Short=C1qBP;Flags: Precursor" O35658 LHTEGDKAFVEFLTDEIKEEKKIQKHKSLPKMSGDWELEVNGTEAKLLRKVAGEKITVTFNINNSIPPTFDGEEEPSQGQKAEEQEPERTSTPNFVVEVTKTDGKKTLVLDCHYPEDEIGHEDEAESDIFSIKEVSFQATGDSEWRDTNYTLNTDSLDWALYDHLMDFLADRGVDNTFADELVELSTALEHQEYITFLEDLKSFVKNQ 208 "FUNCTION: Is believed to be a multifunctional and multicompartmental protein involved in inflammation and infection processes, ribosome biogenesis, regulation of apoptosis, transcriptional regulation and pre-mRNA splicing. At the cell surface is thought to act as an endothelial receptor for plasma proteins of the complement and kallikrein-kinin cascades. Putative receptor for C1q; specifically binds to the globular ""heads"" of C1q thus inhibiting C1; may perform the receptor function through a complex with C1qR/CD93. In complex with cytokeratin-1/KRT1 is a high affinity receptor for kininogen-1/HMWK. Can also bind other plasma proteins, such as coagulation factor XII leading to its autoactivation. May function to bind initially fluid kininogen-1 to the cell membrane. The secreted form may enhance both extrinsic and intrinsic coagulation pathways. It is postulated that the cell surface form requires docking with transmembrane proteins for downstream signaling which might be specific for a cell-type or response. By acting as C1q receptor is involved in chemotaxis of immature dendritic cells and neutrophils and is proposed to signal through CD209/DC-SIGN on immature dendritic cells, through integrin alpha-4/beta-1 during trophoblast invasion of the decidua, and through integrin beta-1 during endothelial cell adhesion and spreading. Signaling involved in inhibition of innate immune response is implicating the PI3K-AKT/PKB pathway. In mitochondrial translation may be involved in formation of functional 55S mitoribosomes; the function seems to involve its RNA-binding activity. May be involved in the nucleolar ribosome maturation process; the function may involve the exchange of FBL for RRP1 in the association with pre-ribosome particles. Involved in regulation of RNA splicing by inhibiting the RNA-binding capacity of SRSF1 and its phosphorylation. Is required for the nuclear translocation of splicing factor U2AF1L4. Involved in regulation of CDKN2A- and HRK-mediated apoptosis. Stabilizes mitochondrial CDKN2A isoform smARF. May be involved in regulation of FOXC1 transcriptional activity and NFY/CCAAT-binding factor complex-mediated transcription. In infection processes acts as an attachment site for microbial proteins. May play a role in antibacterial defense. Involved in regulation of antiviral response by inhibiting DDX58- and IFIH1-mediated signaling pathways probably involving its association with MAVS after viral infection. {ECO:0000269|PubMed:17486078, ECO:0000269|PubMed:18166172, ECO:0000269|PubMed:18460468, ECO:0000269|PubMed:22904065}." Y114P 397.72 "Y,2;" 78 100 uniprot_mouse_length brain_ETD 755.0137329 757.11969 757.117938 22 16626.57775 2.313961033 CALM4_MOUSE Calmodulin-4;AltName: Full=Calcium-binding protein Dd112 Q9JM83 SHGFTKEEVAEFQAAFNRFDKNKDGHISVEELGDVMKQLGKNLPEKDLKALISKLDTDGDGKISFEEFLTAIEKYKKGHRAGELRAVFNVLDQNGDGYITVDELKESLSKLGESLSQEELEDMIRVADVDQDGKVKYEEFVRLHVEN 147 FUNCTION: Implicated in the early stage of ectopic ossification. null 213.33 null null 100 uniprot_mouse_length brain_ETD 656.1594238 659.416626 659.416873 29 19084.06742 -0.374608912 CBLN4_MOUSE Cerebellin-4;AltName: Full=Cerebellin-like glycoprotein 1;Flags: Precursor Q8BME9 QNDTEPIVLEGKCLVVCDSNPATDSKGSSSSPLGISVRAANSKVAFSAVRSTNHEPSEMSNKTRIIYFDQILVNVGNFFTLESVFVAPRKGIYSFSFHVIKVYQSQTIQVNLMLNGKPVISAFAGDKDVTREAATNGVLLYLDKEDKVYLKLEKGNLLGGWQYSTFSGFLVFPL 174 FUNCTION: May be involved in synaptic functions in the CNS. May play a role in CBLN3 export from the endoplasmic reticulum and secretion. null 289.51 null null 100 uniprot_mouse_length brain_ETD 860.5370483 864.675781 864.669011 9 7769.018 7.829874685 CCL1_MOUSE C-C motif chemokine 1;AltName: Full=P500;AltName: Full=SIS-epsilon;AltName: Full=Small-inducible cytokine A1;AltName: Full=T-cell activation protein 3; Short=TCA-3; Short=TCA3;Flags: Precursor P10146 KSMLTVSNSCCLNTLKKELPLKFIQCYRKMGSSCPDPPAVVFRLNKGRESCASTNKTWVQNHLKKVNPC 69 FUNCTION: Cytokine that is chemotactic for neutrophils. null 121.96 null null 100 uniprot_mouse_length brain_ETD 712.6324463 712.878357 712.883511 11 7826.71498 -7.229885846 CCL4_MOUSE C-C motif chemokine 4;AltName: Full=Immune activation protein 2; Short=ACT-2; Short=ACT2;AltName: Full=Macrophage inflammatory protein 1-beta; Short=MIP-1-beta;AltName: Full=Protein H400;AltName: Full=SIS-gamma;AltName: Full=Small-inducible cytokine A4;Flags: Precursor P14097 APMGSDPPTSCCFSYTSRQLHRSFVMDYYETSSLCSKPAVVFLTKRGRQICANPSEPWVTEYMSDLELN 69 FUNCTION: Monokine with inflammatory and chemokinetic properties. null 140.24 null null 100 uniprot_mouse_length brain_ETD 618.2376709 619.348999 619.347905 32 19776.11067 1.766411784 CETN2_MOUSE Centrin-2;AltName: Full=Caltractin isoform 1 Q9R1K9 ASNFKKTTMASSAQRKRMSPKPELTEDQKQEIREAFDLFDADGTGTIDIKELKVAMRALGFEPKKEEIKKMISEIDKEGTGKMNFSDFLTVMTQKMSEKDTKEEILKAFKLFDDDETGKISFKNLKRVAKELGENLTDEELQEMIDEADRDGDGEVNEQEFLRIMKKTSLY 171 FUNCTION: Plays a fundamental role in microtubule organizing center structure and function. Required for centriole duplication and correct spindle formation. Has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CCP110 (By similarity). {ECO:0000250}. A1AcS19P 6791.03 "A,267;S,3;" 248 100 uniprot_mouse_length brain_ETD 780.4105225 782.700806 782.70008 24 18750.78205 0.927129153 CGBP1_MOUSE CGG triplet repeat-binding protein 1; Short=CGG-binding protein 1;AltName: Full=20 kDa CGG-binding protein;AltName: Full=p20-CGGBP DNA-binding protein Q8BHG9 MERFVVTAPPARNRSKTALYVTPLDRVTEFGGELHEDGGKLFCTSCNVVLNHVRKSAISDHLKSKTHTKRKAEFEEQNVRKKQRPLTASLQCNSPAQTEKASVIQDFVKMCLEANIPLEKADHPAVRAFLSRHVKNGGSIPKSDQLRRAYLPDGYENENQLLSSQDC 167 FUNCTION: Binds to nonmethylated 5'-d(CGG)(n)-3' trinucleotide repeats in the FMR1 promoter. May play a role in regulating FMR1 promoter (By similarity). {ECO:0000250}. null 1129.34 null null 100 uniprot_mouse_length brain_ETD 892.5549316 892.787537 892.79079 18 16044.21868 -3.644055184 CHSP1_MOUSE Calcium-regulated heat stable protein 1;AltName: Full=Calcium-regulated heat-stable protein of 24 kDa; Short=CRHSP-24 Q9CR86 SSEPPPPPLQPPTHQTSVGLLDTPRTRDRSPSPLRGNVVPSPLPTRRTRTFSATVRASQGPVYKGVCKCFCRSKGHGFITPADGGPDIFLHISDVEGEYVPVEGDEVTYKMCSIPPKNEKLQAVEVVITHLAPGTKHETWSGHVISN 147 FUNCTION: Binds mRNA and regulates the stability of target mRNA. {ECO:0000269|PubMed:21078874}. S1AcS30P 377.24 "S,34;S,0;" 56 100 uniprot_mouse_length brain_ETD 682.9458618 682.386414 682.382044 27 18387.29513 6.403413245 CITE4_MOUSE Cbp/p300-interacting transactivator 4;AltName: Full=MSG1-related protein 2; Short=MRG-2 Q9WUL8 MADHLMLAEGYCLLQVPPHTHGPHAPRTLQPYAGPGMDSGLRPRGAPLGPPPPPGTLAYGSFGSPVSFQPFPVSQSPGAGSTHLQSAATPSPGRIPAPPAAAGGPSPLQPAPGAAASLPPPPPPPALGCMDTELIDEEALTSLELELGLHRVRELPELFLGQSEFDCFSDLGSAPAAGSVSC 182 "FUNCTION: Acts as transcriptional coactivator for TFAP2/AP-2. Enhances estrogen-dependent transactivation mediated by estrogen receptors. May function as an inhibitor of transactivation by HIF1A by disrupting HIF1A interaction with CREBBP. May be involved in regulation of gene expression during development and differentiation of blood cells, endothelial cells and mammary epithelial cells. {ECO:0000269|PubMed:11581164, ECO:0000269|PubMed:12504852}." null 1664.97 null null 100 uniprot_mouse_length brain_ETD 808.8605957 809.263855 809.275904 25 20195.87545 -14.88864239 CL045_MOUSE Uncharacterized protein C12orf45 homolog Q9CX66 MEFQGERGTGPGVSSSSVACSQVTVSRELLTAGSEGSGGIWDQLLISSKPHPRKTSTLQTVRMQRSPLLDQVQAFLPQMAQANEKLRREMAAAPAGHFNIENIDETSGNIIQMDVALFEMSRSDSKEEDSPEESSRDSSGDSSESEEDVCVPSEVTIENIKLPNAEGGKGKIEILDSPASKKKKQ 185 "-------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License--------------------------------------------------" S34PS66PS177P 474.88 "S,9;S,0;S,22;" 83 100 uniprot_mouse_length brain_ETD 745.3196411 749.329407 749.330158 25 18698.23442 -1.002577717 CNPY2_MOUSE Protein canopy homolog 2;AltName: Full=MIR-interacting saposin-like protein;AltName: Full=Putative secreted protein ZSIG9;AltName: Full=Transmembrane protein 4;Flags: Precursor Q9QXT0 RRSQDLHCGACRALVDELEWEIARVDPKKTIQMGSFRINPDGSQSVVEVPYARSEAHLTELLEEVCDRMKEYGEQIDPSTHRKNYVRVVSRNGESSELDLQGIRIDSDISGTLKFACESIVEEYEDELIEFFSREADNVKDKLCSKRTDLCDHALHRSHDEL 162 FUNCTION: Positive regulator of neurite outgrowth by stabilizing myosin regulatory light chain (MRLC). It prevents MIR-mediated MRLC ubiquitination and its subsequent proteasomal degradation (By similarity). {ECO:0000250}. S95P 1011.07 "S,105;" 105 100 uniprot_mouse_length brain_ETD 627.8300781 623.26825 623.260009 30 18657.77961 13.22162757 COF1_MOUSE "Cofilin-1;AltName: Full=Cofilin, non-muscle isoform" P18760 ASGVAVSDGVIKVFNDMKVRKSSTPEEVKKRKKAVLFCLSEDKKNIILEEGKEILVGDVGQTVDDPYTTFVKMLPDKDCRYALYDATYETKESKKEDLVFIFWAPENAPLKSKMIYASSKDAIKKKLTGIKHELQANCYEEVKDRCTLAEKLGGSAVISLEGKPL 165 "FUNCTION: Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity. Regulates actin cytoskeleton dynamics. Important for normal progress through mitosis and normal cytokinesis. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required for the up-regulation of atypical chemokine receptor ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation (By similarity). {ECO:0000250}." S2PS7PT24P 431.26 "S,0;S,0;T,0;" 73 100 uniprot_mouse_length brain_ETD 692.3396606 688.480835 688.484871 23 15804.13569 -5.862204433 COTL1_MOUSE Coactosin-like protein Q9CQI6 ATKIDKEACRAAYNLVRDDGSAVIWVTFRYDGATIVPGDQGADYQHFIQQCTDDVRLFAFVRFTTGDAMSKRSKFALITWIGEDVSGLQRAKTGTDKTLVKEVVQNFAKEFVISDRKELEEDFIRSELKKAGGANYDAQSE 141 "FUNCTION: Binds to F-actin in a calcium-independent manner. Has no direct effect on actin depolymerization. Acts as a chaperone for ALOX5 (5LO), influencing both its stability and activity in leukotrienes synthesis (By similarity). {ECO:0000250}." null 507.34 null null 100 uniprot_mouse_length brain_ETD 650.3545532 649.909363 649.901853 41 26591.9499 11.55527244 CR025_MOUSE Uncharacterized protein C18orf25 homolog Q8BH50 MKMEEAVGKVEELIESAAPPKASEQETAKEEDGSVELESQVQKDGVADSTVLSSMPCLLMELRRDSSESQLASTESDKPTTGRVYESDSSNHCMLSPSSSGHLADSDTLSSVEENEPSQAETTVEGDTSGVSGATVGRKSRRSRSESETSTMAAKKNRQSSDKQNGRVTKVKGHRSQKHKERIRLLRQKREAAARKKYNLLQDSSTSDSDLTCDSSTSSSDDDDEVSGSSKTITAEIPGRGCFLN 245 "ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q8BH50-1; Sequence=Displayed; Name=2; IsoId=Q8BH50-2; Sequence=VSP_014754, VSP_014755; Note=No experimental confirmation available.;-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" S66PS143P 616.13 "S,24;S,0;" 116 100 uniprot_mouse_length brain_ETD 547.2451782 543.374939 543.382733 36 19515.75628 -14.34354587 CS2LA_MOUSE Alpha-S2-casein-like A;AltName: Full=Casein alpha S2-like A;AltName: Full=Gamma-casein;AltName: Full=PP22;Flags: Precursor Q02862 KHEIKDKSSSEESSASIYPGKSKLDNSVFFQTTKDSASSSSSEESSEEVSEKIVQSEEQKVNLNQQKKFKQFSQESSFSQCCTPLHQQQQSSVNQWPQPNAIHNTPTQESISTSVEEILKKIIDMIKYIQYQQVTIPQLPQALHPQIPVSYWYPSKDYTFPNAHYTRFY 169 FUNCTION: Important role in the capacity of milk to transport calcium phosphate. S8P 340.26 "S,0;" 65 100 uniprot_mouse_length brain_ETD 708.522522 709.510071 709.50157 22 15579.01979 11.98136994 CT085_MOUSE Uncharacterized protein C20orf85 homolog Q9DA42 MAQKPLSTTAAERMNLVAQDEIWKYRLRAESEARQNWPAKWGYLTTSMKELLEGEEEPQTPKPKPELPSHFYVRPVSPMDKHIKILPSPPVPKTTQGFIGWRSGKPALYCLEKYSEVCSCKGAYARELCWPEQGVH 136 "-------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License--------------------------------------------------" null 786.96 null null 100 uniprot_mouse_length brain_ETD 822.0629272 822.560364 822.560458 8 6569.48116 -0.114557499 CX7A2_MOUSE "Cytochrome c oxidase subunit 7A2, mitochondrial;AltName: Full=Cytochrome c oxidase subunit VIIa-liver/heart; Short=Cytochrome c oxidase subunit VIIa-L;Flags: Precursor" P48771 FENKVPEKQKLFQEDNGMPVHLKGGASDALLYRATMALTLGGTAYAIYLLAMAAFPKKQN 60 "FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport." null 1824.19 null null 100 uniprot_mouse_length brain_ETD 578.4246216 582.148621 582.143122 26 15101.70439 9.44545295 CYB5_MOUSE Cytochrome b5 P56395 AGQSDKDVKYYTLEEIQKHKDSKSTWVILHHKVYDLTKFLEEHPGGEEVLREQAGGDATENFEDVGHSTDARELSKTYIIGELHPDDRSKIAKPSDTLITTVESNSSWWTNWVIPAISALAVALMYRLYMAED 133 "FUNCTION: Cytochrome b5 is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases. It is also involved in several steps of the sterol biosynthesis pathway, particularly in the C-5 double bond introduction during the C-5 desaturation." null 360.02 null null 100 uniprot_mouse_length brain_ETD 734.6553345 738.65332 738.650179 15 11059.74461 4.252774303 DAP1_MOUSE Death-associated protein 1; Short=DAP-1 Q91XC8 SSPPEGKLETKAGHPPAVKAGGMRIVQKHPHTGDGKEERDKDDQEWESTSPPKPTVFISGVIARGDKDFPPAAAQVAHQKPHASMDKHVSPRTQHIQQPRK 101 FUNCTION: Negative regulator of autophagy. Involved in mediating interferon-gamma-induced cell death (By similarity). {ECO:0000250}. S1Ac 982.52 "S,4;" 88 100 uniprot_mouse_length brain_ETD 616.9859619 618.415405 618.419361 28 17278.72397 -6.396511513 DAZP2_MOUSE DAZ-associated protein 2;AltName: Full=Deleted in azoospermia-associated protein 2;AltName: Full=Proline-rich protein expressed in brain Q9DCP9 MNSKGQYPTQPTYPVQPPGNPVYPQTLHLPQAPPYTDAPPAYSELYRPSFVHPGAATVPTMSAAFPGASLYLPMAQSVAVGPLGSTIPMAYYPVGPIYPPGSAVLVEGGYDAGARFGAGATAGNIPPPPPGCPPNAAQLAVMQGANVLVTQRKGNFFMGGSDGGYTIW 168 "SUBUNIT: Interacts with DAZ and DAZL (By similarity). Interacts with IL17RB (By similarity). May interact with FAM168B (By similarity). Interacts with SOX6. {ECO:0000250, ECO:0000269|PubMed:14530442}." null 165.45 null null 100 uniprot_mouse_length brain_ETD 618.2376709 617.295044 617.301439 12 7392.61612 -10.35969509 DFB18_MOUSE "Beta-defensin 18; Short=BD-18; Short=mBD-18;AltName: Full=Defensin, beta 18;Flags: Precursor" Q30KP5 APQMKTREVAERTHKCSLVRGTCKSECNSWEYKYNYCHTEPCCVVREYKRMEKLLSTPKYTT 62 FUNCTION: Has antibacterial activity. {ECO:0000250}. null 516.51 null null 100 uniprot_mouse_length brain_ETD 660.9111938 659.12854 659.126045 29 19075.63472 3.785374712 DNPH1_MOUSE 2'-deoxynucleoside 5'-phosphate N-hydrolase 1 {ECO:0000255|HAMAP-Rule:MF_03036}; EC=3.2.2.- {ECO:0000255|HAMAP-Rule:MF_03036};AltName: Full=c-Myc-responsive protein Rcl {ECO:0000255|HAMAP-Rule:MF_03036} Q80VJ3 AASGELVPCSVYFCGSIRGGREDQALYSRIVSRLRRYGKVLTEHVADAELEPRGEEAAGGDQFIHERDLAWLRQADVVVAEVTQPSLGVGYELGRAVALGKPILCLFRPQSGRVLSAMIRGAADGSRFQVWDYAEEEVETMLHRYFEAYLPQGTASSSNPSACLNPTVLEKI 172 FUNCTION: Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5- phosphate and a purine or pyrimidine base. Deoxyribonucleoside 5'- monophosphates containing purine bases are preferred to those containing pyrimidine bases. {ECO:0000255|HAMAP-Rule:MF_03036}. S16PS86PS116P 1472.91 "S,34;S,0;S,0;" 157 100 uniprot_mouse_length brain_ETD 679.3267822 678.137878 678.132293 18 12182.37037 8.236472479 DPOE4_MOUSE DNA polymerase epsilon subunit 4; EC=2.7.7.7;AltName: Full=DNA polymerase II subunit 4;AltName: Full=DNA polymerase epsilon subunit p12 Q9CQ36 AAAAAAGSGTPREEEAPGGEAAASQAQAPTSAPGGVRLSRLPLARVKALVKADPDVTLAGQEAIFILARAAELFVETIAKDAYCCAQQGKRKTLQRRDLDNAIEAVDEFAFLEGTLD 117 FUNCTION: May play a role in allowing polymerase epsilon to carry out its replication and/or repair function. T10P 248.44 "T,1;" 56 100 uniprot_mouse_length brain_ETD 544.1689453 540.322327 540.328098 35 18866.46265 -10.68117661 EFNA2_MOUSE Ephrin-A2;AltName: Full=CEK7-ligand; Short=CEK7-L;AltName: Full=ELF-1;AltName: Full=EPH-related receptor tyrosine kinase ligand 6; Short=LERK-6;Flags: Precursor P52801 RNEDPARANADRYAVYWNRSNPRFQVSAVGDGGGYTVEVSINDYLDIYCPHYGAPLPPAERMERYILYMVNGEGHASCDHRQRGFKRWECNRPAAPGGPLKFSEKFQLFTPFSLGFEFRPGHEYYYISATPPNLVDRPCLRLKVYVRPTNETLYEAPEPIFTSN 164 "FUNCTION: Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. With the EPHA2 receptor may play a role in bone remodeling through regulation of osteoclastogenesis and osteoblastogenesis. {ECO:0000269|PubMed:19299512, ECO:0000269|PubMed:9053851}." null 308.17 null null 100 uniprot_mouse_length brain_ETD 543.0609741 545.869019 545.870522 54 29408.97685 -2.754215976 EI3JA_MOUSE Eukaryotic translation initiation factor 3 subunit J-A {ECO:0000255|HAMAP-Rule:MF_03009}; Short=eIF3j-A {ECO:0000255|HAMAP-Rule:MF_03009};AltName: Full=Eukaryotic translation initiation factor 3 subunit 1-A {ECO:0000255|HAMAP-Rule:MF_03009};AltName: Full=eIF-3-alpha-A {ECO:0000255|HAMAP-Rule:MF_03009};AltName: Full=eIF3 p35 {ECO:0000255|HAMAP-Rule:MF_03009} Q3UGC7 MAAAAAAAAAAGDSDSWDADTFSMEDPVRKVAGGGTAGGDRWEGEDEDEDVKDNWDDDDDENKEEAEVKPEVKISEKKKIAEKIKEKERQQKKRQEEIKKRLEEPEESKVLTPEEQLADKLRLKKLQEESDLELAKETFGVNNTVYGIDAMNPSSRDDFTEFGKLLKDKITQYEKSLYYASFLEALVRDVCISLEIDDLKKITNSLTVLCSEKQKQEKQSKAKKKKKGVVPGGGLKATMKDDLADYGGYEGGYVQDYEDFM 261 "FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. This subunit binds directly within the mRNA entry channel of the 40S ribosome to the aminoacyl (A) site. It may regulate the interaction between the 43S PIC and mRNA. {ECO:0000250|UniProtKB:O75822, ECO:0000255|HAMAP-Rule:MF_03009}." S14P 187.8 "S,0;" 46 100 uniprot_mouse_length brain_ETD 658.0564575 656.983643 656.98776 30 19669.6119 -6.267121133 EIF1A_MOUSE Probable RNA-binding protein EIF1AD;AltName: Full=Eukaryotic translation initiation factor 1A domain-containing protein Q3THJ3 MSQASKRKHVVQEVLGEHMVPSDHQQIVKVLRTPGNNLHEVETAQGQRFLVSMPSKYRKNIWIKRGDFLIVDPIEEGEKVKAEISFVLCKNHVRSLQKEGHWPEAFSEVAEKQNNMNRESQPELPAEPQLSGEGSSSEDDSDLFVNTNHRQYHESEEESEEDEEEEEEAA 170 FUNCTION: Plays a role into cellular response to oxidative stress. Decreases cell proliferation (By similarity). {ECO:0000250}. T33PS155P 189.2 "T,14;S,0;" 47 100 uniprot_mouse_length brain_ETD 542.0762939 543.272705 543.269368 23 12466.18596 6.142584732 ELOC_MOUSE Transcription elongation factor B polypeptide 1;AltName: Full=Elongin 15 kDa subunit;AltName: Full=Elongin-C; Short=EloC;AltName: Full=RNA polymerase II transcription factor SIII subunit C;AltName: Full=SIII p15;AltName: Full=Stromal membrane-associated protein SMAP1B homolog P83940 MDGEEKTYGGCEGPDAMYVKLISSDGHEFIVKREHALTSGTIKAMLSGPGQFAENETNEVNFREIPSHVLSKVCMYFTYKVRYTNSSTEIPEFPIAPEIALELLMAANFLDC 112 "FUNCTION: SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex)." null 217.52 null null 100 uniprot_mouse_length brain_ETD 907.6459351 909.244446 909.256282 17 15432.34061 -13.01745113 F107B_MOUSE Protein FAM107B Q3TGF2 AEPDYIEDDNPELIRPQKLINPVKSSRNHQDLHRELLMNQKRGLAPQNKPELQKVMEKRRRDQVIKQKEEEAQKKKSDLEIELLKRQQKLEQLELEKQKLQEEQENAPEFVKVKGNLRRTGQEVAQAQES 130 SIMILARITY: Belongs to the FAM107 family. {ECO:0000305}. null 172.39 null null 100 uniprot_mouse_length brain_ETD 649.0559082 651.721985 651.727018 27 17560.61037 -7.722768245 F180A_MOUSE Protein FAM180A;Flags: Precursor Q8BR21 TASCRWSRAALFPAAHRPKRSLSLPLNPVLQTSLEEVELLYELLLAEIEISPDLEISIKDEELASLRKALSFHSICNNIIPKRIPDIRRLSANLANHPGILKKEDFERITLTLAYTAYRTALSEGHQKDIWAQSLISLFQALRHDLMRSSSPAVSS 156 SUBCELLULAR LOCATION: Secreted {ECO:0000305}. null 1918.79 null null 100 uniprot_mouse_length brain_ETD 776.7281494 777.737122 777.733311 22 17079.1144 4.899599872 FIS1_MOUSE Mitochondrial fission 1 protein;AltName: Full=FIS1 homolog;AltName: Full=Tetratricopeptide repeat protein 11; Short=TPR repeat protein 11 Q9CQ92 MEAVLNELVSVEDLKNFERKFQSEQAAGSVSKSTQFEYAWCLVRSKYNEDIRRGIVLLEELLPKGSKEEQRDYVFYLAVGNYRLKEYEKALKYVRGLLQTEPQNNQAKELERLIDKAMKKDGLVGMAIVGGMALGVAGLAGLIGLAVSKSKS 152 "FUNCTION: Involved in the fragmentation of the mitochondrial network and its perinuclear clustering. Plays a minor role in the recruitment and association of the fission mediator dynamin- related protein 1 (DNM1L) to the mitochondrial surface and mitochondrial fission. May be not essential for the assembly of functional fission complexes and the subsequent membrane scission event. Can induce cytochrome c release from the mitochondrion to the cytosol, ultimately leading to apoptosis. Also mediates peroxisomal fission. {ECO:0000269|PubMed:23283981}." S10P 1211.22 "S,84;" 112 100 uniprot_mouse_length brain_ETD 614.2875977 612.4151 612.415827 30 18332.45619 -1.186942453 FLOWR_MOUSE Calcium channel flower homolog;AltName: Full=Calcium channel flower domain-containing protein 1 Q8BG21 MSGSGAAGAAAGPAPPAQEEGMTWWYRWLCRLAGVLGAVSCAISGLFNCVTIHPLNIAAGVWMIMNAFILLLCEAPFCCQFVEFANTVAEKVDRLRSWQKAVFYCGMAIVPIVMSLTLTTLLGNAIAFATGVLYGLSALGKKGDAISYARIQQQRQQADEEKLAETFEGEL 171 SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. null 327.58 null null 100 uniprot_mouse_length brain_ETD 642.4686279 638.082214 638.076396 26 16554.96737 9.118587531 FUND2_MOUSE FUN14 domain-containing protein 2;AltName: Full=Hepatitis C virus core-binding protein 6 Q9D6K8 MAANSQGNFDGKFEALDLAELTKKQPWWRKLFGQESGPSAEKYSVATQLVIGGVTGWCTGFVFQKVGKLAATAVGGGFFLLQLANHTGYIKVDWQRVEKDMKKAKEQLKIRKNKQIPTEVKSKAEEVVSFVKKNVLVTGGFFGGFLLGMAS 151 "SIMILARITY: Belongs to the FUN14 family. {ECO:0000305}.-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" null 565.13 null null 100 uniprot_mouse_length brain_ETD 659.1465454 654.795959 654.792757 35 22870.71965 4.890818693 GDIR2_MOUSE Rho GDP-dissociation inhibitor 2; Short=Rho GDI 2;AltName: Full=D4;AltName: Full=Rho-GDI beta Q61599 TEKDAQPQLEEADDDLDSKLNYKPPPQKSLKELQEMDKDDESLTKYKKTLLGDVPVVADPTVPNVTVTRLSLVCDSAPGPITMDLTGDLEALKKDTFVLKEGIEYRVKINFKVNKDIVSGLKYVQHTYRTGMRVDKATFMVGSYGPRPEEYEFLTPVEEAPKGMLARGTYHNKSFFTDDDKQDHLTWEWNLAIKKDWTE 199 "FUNCTION: Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them." T1AcK19AcY22P 2504.38 "T,2;K,0;Y,73;" 188 100 uniprot_mouse_length brain_ETD 650.3545532 647.537109 647.538842 29 18739.60632 -2.675708217 GEMI6_MOUSE Gem-associated protein 6; Short=Gemin-6 Q9CX53 MSEWMKKSPLEWEDYVYKEVRVIACEKEYKGWLLTTDPVSANIVLVNFLEDGRLSVTGIMGHSVQTVETISEGDHRVREKLMHVFASGDCKGYSPEDLEEKRTSLKKWLEKNHIPVTEQGDAQRTLCVAGVLTIDPPYAPENCSSSNEIILSRIQDLIQGHLSASQ 166 "FUNCTION: The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus (By similarity). {ECO:0000250}." null 223.02 null null 100 uniprot_mouse_length brain_ETD 578.4246216 575.617676 575.622577 37 21250.00981 -8.514639533 H12_MOUSE Histone H1.2;AltName: Full=H1 VAR.1;AltName: Full=H1c P15864 SEAAPAAPAAAPPAEKAPAKKKAAKKPAGVRRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGILVQTKGTGASGSFKLNKKAASGEAKPQAKKAGAAKAKKPAGAAKKPKKATGAATPKKAAKKTPKKAKKPAAAAVTKKVAKSPKKAKVTKPKKVKSASKAVKPKAAKPKVAKAKKVAAKKK 211 "FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250}." S1AcK16AcK25Ac 798.58 "S,2;K,0;K,0;" 141 100 uniprot_mouse_length brain_ETD 578.4246216 578.702515 578.700071 37 21363.87712 4.222651007 H12_MOUSE Histone H1.2;AltName: Full=H1 VAR.1;AltName: Full=H1c P15864 SEAAPAAPAAAPPAEKAPAKKKAAKKPAGVRRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGILVQTKGTGASGSFKLNKKAASGEAKPQAKKAGAAKAKKPAGAAKKPKKATGAATPKKAAKKTPKKAKKPAAAAVTKKVAKSPKKAKVTKPKKVKSASKAVKPKAAKPKVAKAKKVAAKKK 211 "FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250}." S1PS35PS103P 820.32 "S,3;S,0;S,0;" 142 100 uniprot_mouse_length brain_ETD 646.1099854 641.286499 641.279308 22 14079.13063 11.21355913 H2A1F_MOUSE Histone H2A type 1-F Q8CGP5 SGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKPKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1AcQ104Me 232.64 "S,0;Q,41;" 50 100 uniprot_mouse_length brain_ETD 672.4310913 673.774841 673.76893 21 14121.13337 8.773495379 H2A1F_MOUSE Histone H2A type 1-F Q8CGP5 SGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKPKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1AcK5AcQ104Me 396.87 "S,0;K,0;Q,52;" 76 100 uniprot_mouse_length brain_ETD 616.9859619 612.736572 612.741798 23 14063.04726 -8.528444431 H2A3_MOUSE Histone H2A type 3 Q8BFU2 SGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK 129 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S1P 113.99 "S,19;" 30 100 uniprot_mouse_length brain_ETD 570.305603 566.321289 566.318488 25 14125.9488 4.946090512 H2B1A_MOUSE "Histone H2B type 1-A;AltName: Full=Histone H2B, testis;AltName: Full=Testis-specific histone H2B" P70696 PEVAVKGATISKKGFKKAVTKTQKKEGRKRKRCRKESYSIYIYKVLKQVHPDTGISSKAMSIMNSFVTDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 126 "FUNCTION: Variant histone specifically required to direct the transformation of dissociating nucleosomes to protamine in male germ cells. Entirely replaces classical histone H2B prior nucleosome to protamine transition and probably acts as a nucleosome dissociating factor that creates a more dynamic chromatin, facilitating the large-scale exchange of histones. Also expressed maternally and is present in the female pronucleus, suggesting a similar role in protamine replacement by nucleosomes at fertilization. Also found in fat cells, its function and the presence of post-translational modifications specific to such cells are still unclear. Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. {ECO:0000269|PubMed:23884607}." K47MeR87Me 1130.75 "K,23;R,0;" 101 100 uniprot_mouse_length brain_ETD 788.9112549 793.709473 793.716668 18 14261.88661 -9.065380683 H2B1A_MOUSE "Histone H2B type 1-A;AltName: Full=Histone H2B, testis;AltName: Full=Testis-specific histone H2B" P70696 PEVAVKGATISKKGFKKAVTKTQKKEGRKRKRCRKESYSIYIYKVLKQVHPDTGISSKAMSIMNSFVTDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 126 "FUNCTION: Variant histone specifically required to direct the transformation of dissociating nucleosomes to protamine in male germ cells. Entirely replaces classical histone H2B prior nucleosome to protamine transition and probably acts as a nucleosome dissociating factor that creates a more dynamic chromatin, facilitating the large-scale exchange of histones. Also expressed maternally and is present in the female pronucleus, suggesting a similar role in protamine replacement by nucleosomes at fertilization. Also found in fat cells, its function and the presence of post-translational modifications specific to such cells are still unclear. Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. {ECO:0000269|PubMed:23884607}." P1AcS37PK86tMe 210.5 "P,0;S,20;K,35;" 43 100 uniprot_mouse_length brain_ETD 992.4509888 990.920349 990.910097 14 13851.72767 10.34616675 H2B1C_MOUSE Histone H2B type 1-C/E/G Q6ZWY9 PEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." K46MeK57dMeK85tMe 196.22 "K,6;K,5;K,30;" 38 100 uniprot_mouse_length brain_ETD 603.3554077 608.15564 608.159174 23 13957.64737 -5.811556766 H2B1F_MOUSE Histone H2B type 1-F/J/L;AltName: Full=H2B 291A P10853 PEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." S14PS36P 171.56 "S,1;S,0;" 40 100 uniprot_mouse_length brain_ETD 992.4509888 990.920349 990.910097 14 13851.72767 10.34616675 H2B1K_MOUSE Histone H2B type 1-K Q8CGP1 PEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK 125 "FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling." K46MeK57dMeR79dMe 263.72 "K,8;K,6;R,7;" 43 100 uniprot_mouse_length brain_ETD 582.3046265 582.304626 582.306339 29 16848.8656 -2.940952282 AP4A_MOUSE "Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]; EC=3.6.1.17;AltName: Full=Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase; Short=Ap4A hydrolase; Short=Ap4Aase; Short=Diadenosine tetraphosphatase;AltName: Full=Nucleoside diphosphate-linked moiety X motif 2; Short=Nudix motif 2" P56380 ALRACGLIIFRRHLIPKMDNSTIEFLLLQASDGIHHWTPPKGHVDPGENDLETALRETREETGIEASQLTIIEGFRRELNYVARQKPKTVIYWLAEVKDYNVEIRLSQEHQAYRWLGLEEACQLAQFKEMKATLQEGHQFLCSTPA 146 FUNCTION: Asymmetrically hydrolyzes Ap4A to yield AMP and ATP. Plays a major role in maintaining homeostasis (By similarity). {ECO:0000250}. null 153.04 null null 100 uniprot_mouse_length brain_ETD 658.0213013 653.875671 653.882109 26 16965.9164 -9.845220098 CA100_MOUSE Uncharacterized protein C1orf100 homolog Q9DAA7 MSTIRLREFVERRPSIPPRLYITHQGRDIKGYYPGQLARLHFDYSGRKAPRPLIDLTIPLKSTTPYQPQLDQQTLIRSICSRRLSRPTDLWHNETSYQRDYSLPFYESGWDRKLGTISLHPRPVNSVPEVYCCGGERSSYARSTF 145 "-------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License--------------------------------------------------" null 152.4 null null 100 uniprot_mouse_length brain_ETD 658.0213013 656.558289 656.55687 27 17691.01673 2.160626571 CASK_MOUSE Kappa-casein;Flags: Precursor P06796 EIQNPDSNCRGEKNDIVYDEQRVLYTPVRSVLNFNQYEPNYYHYRPSLPATASPYMYYPLVVRLLLLRSPAPISKWQSMPNFPQSAGVPYAIPNPSFLAMPTNENQDNTAIPTIDPITPIVSTPVPTMESIVNTVANPEASTVSINTPETTTVPVSSTAA 160 "FUNCTION: Kappa-casein stabilizes micelle formation, preventing casein precipitation in milk." null 275.5 null null 100 uniprot_mouse_length brain_ETD 544.1690674 539.286255 539.291617 27 14526.86037 -9.942889929 CBY1_MOUSE "Protein chibby homolog 1;AltName: Full=Cytosolic leucine-rich protein;AltName: Full=PIGEA-14;AltName: Full=PKD2 interactor, Golgi and endoplasmic reticulum-associated 1" Q9D1C2 MPLFGSIFSPKKTPPRKSASLSNLHSLDRSTRELELGLDYGTPTMNLAGQSLKFENGQWVADSVISGGVDRRETQRLRKRNQQLEEENNLLRLKVDILLDMLSETTAESHLKDKELDELKVTNRRRK 127 "FUNCTION: Inhibits the Wnt/Wingless pathway by binding to beta- catenin and inhibiting beta-catenin-mediated transcriptional activation through competition with TCF/LEF transcription factors. Has also been shown to play a role in regulating the intracellular trafficking of polycystin-2/PKD2 and possibly of other intracellular proteins (By similarity). Promotes adipocyte and cardiomyocyte differentiation. {ECO:0000250, ECO:0000269|PubMed:17261658, ECO:0000269|PubMed:17403895}." null 287.4 null null 100 uniprot_mouse_length brain_ETD 623.6751099 623.20874 623.200354 15 9329.0006 13.45672274 CCL12_MOUSE C-C motif chemokine 12;AltName: Full=MCP-1-related chemokine;AltName: Full=Monocyte chemoattractant protein 5;AltName: Full=Monocyte chemotactic protein 5; Short=MCP-5;AltName: Full=Small-inducible cytokine A12;Flags: Precursor Q62401 GPDAVSTPVTCCYNVVKQKIHVRKLKSYRRITSSQCPREAVIFRTILDKEICADPKEKWVKNSINHLDKTSQTFILEPSCLG 82 "FUNCTION: Chemotactic factor that attracts eosinophils, monocytes, and lymphocytes but not neutrophils. Potent monocyte active chemokine that signals through CCR2. Involved in allergic inflammation and the host response to pathogens and may play a pivotal role during early stages of allergic lung inflammation." null 1829.93 null null 100 uniprot_mouse_length brain_ETD 542.5922241 543.806152 543.798177 35 18987.91534 14.66599942 CD3E_MOUSE T-cell surface glycoprotein CD3 epsilon chain;AltName: Full=T-cell surface antigen T3/Leu-4 epsilon chain;AltName: CD_antigen=CD3e;Flags: Precursor P22646 DDAENIEYKVSISGTSVELTCPLDSDENLKWEKNGQELPQKHDKHLVLQDFSEVEDSGYYVCYTPASNKNTYLYLKARVCEYCVEVDLTAVAIIIIVDICITLGLLMVIYYWSKNRKAKAKPVTRGTGAGSRPRGQNKERPPPVPNPDYEPIRKGQRDLYSGLNQRAV 168 FUNCTION: The CD3 complex mediates signal transduction. null 151.44 null null 100 uniprot_mouse_length brain_ETD 814.2467651 814.337524 814.338988 12 9756.06239 -1.797268655 CDC26_MOUSE Anaphase-promoting complex subunit CDC26;AltName: Full=Cell division cycle protein 26 homolog Q99JP4 MLRRKPTRLELKLDDIEEFESIRKDLEARKKQKEDVEGVGTSDGEGAAGLSSDPKSREQMINDRIGYKPQLKSNNRTSQFGNFEF 85 "FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. May recruit the E2 ubiquitin-conjugating enzymes to the complex (By similarity). {ECO:0000250}." null 190.68 null null 100 uniprot_mouse_length brain_ETD 632.6774902 635.872498 635.874114 14 8884.23216 -2.542077702 CG034_MOUSE Uncharacterized protein C7orf34 homolog;Flags: Precursor Q9D9P8 LIVSASLDGDKSQKDKVSSEDQGEEEYEEHFEASSEGEQWQEIDMVQQEDTISQAITLQDHLLDLAFCFNLASIMFFL 78 "SUBCELLULAR LOCATION: Secreted {ECO:0000305}.-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" null 1188.07 null null 100 uniprot_mouse_length brain_ETD 632.6774902 636.201416 636.201699 15 9524.02001 -0.444802922 CKS1_MOUSE Cyclin-dependent kinases regulatory subunit 1; Short=CKS-1;AltName: Full=Sid 1334 P61025 SHKQIYYSDKYDDEEFEYRHVMLPKDIAKLVPKTHLMSESEWRNLGVQQSQGWVHYMIHEPEPHILLFRRPLPKKPKK 78 FUNCTION: Binds to the catalytic subunit of the cyclin dependent kinases and is essential for their biological function. {ECO:0000250}. null 1945.16 null null 100 uniprot_mouse_length brain_ETD 542.5922241 539.593872 539.595453 37 19917.00874 -2.929842494 CO057_MOUSE Uncharacterized protein C15orf57 homolog;AltName: Full=Protein CCDC32 Q8BS39 MKMFESLDSSATKSGRDLWAEICSCLPSPAQEDVSDNAFSDSFMDSHPAGESHTAAADSAVQPAGKPWAPLHDSEVYLASLEKKLRRIKGLNEEVTSKDMLRTLAQAKKECWDRFLQEKLASEFFVDGLDSDERTLEHFKRWLQPDKVAISTEEVQFLIPPESQAEKPEAGDKPAAAEQ 179 ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q8BS39-1; Sequence=Displayed; Name=2; IsoId=Q8BS39-2; Sequence=VSP_027488; null 162.59 null null 100 uniprot_mouse_length brain_ETD 677.2935791 673.622437 673.612811 31 20839.97368 14.2894008 COMD8_MOUSE COMM domain-containing protein 8 Q9CZG3 MEPEEGTPLWRLQKLPPEQGAGLLHKIIDGFCGRAYPAHQDYHSVWNSAEWKHVLEDVTTFFKAVVGKNFSEEETLQQLNQLNSCHQEAVLKCLKSRRNEIKQALLGEIVDISCAQLQDFDWQLKLALSSDKIATLQMPLLNLHLDVKEDDKVKPYTVEMSKEELQSLISSLEAANKVVLQLK 183 FUNCTION: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes. May down-regulate activation of NF-kappa-B. {ECO:0000250|UniProtKB:Q9NX08}. null 3083.32 null null 100 uniprot_mouse_length brain_ETD 673.6005249 677.328918 677.335048 15 10140.02043 -9.049499191 DAR12_MOUSE Alpha-defensin-related sequence 12;AltName: Full=CRS4C5;AltName: Full=Cryptdin-related protein 4C-5;AltName: Full=Defensin-related cryptdin-related sequence 12;Flags: Precursor P50716 MKKLVLLSAFVLLAFQVQADSIQNTDEEIKTEEQPGEENQAVSISFGDPEGYALQDAAIRRARRCPPCPSCLSCPWCPRCLRCPMCKCNPK 91 "FUNCTION: Apparent precursor of a secreted, cationic, proline- and cysteine-rich peptide that contains Cys-Pro-Xaa repeats. Unlike cryptdin, the proposed mature peptide region lacks the structural motif characteristic of defensins. It may have microbicidal activities (By similarity). {ECO:0000250}." null 123.16 null null 100 uniprot_mouse_length brain_ETD 685.5716553 688.187561 688.186246 30 20604.56349 1.910871024 DBLOH_MOUSE "Diablo homolog, mitochondrial;AltName: Full=Direct IAP-binding protein with low pI;AltName: Full=Second mitochondria-derived activator of caspase; Short=Smac;Flags: Precursor" Q9JIQ3 AVPIAQKSEPQSLSNEALMRRAVSLVTDSTSTFLSQTTYALIEAITEYTKAVYTLVSLYRQYTSLLGKMNSQEEDEVWQVIIGARVEMTSKQQEYLKLETTWMTAVGLSEMAAEAAYQTGADQASITARNHIQLVKSQVQEVRQLSQKAETKLAEAQTKELHQKAQEVSDEGADQEEEAYLRED 184 FUNCTION: Promotes apoptosis by activating caspases in the cytochrome c/Apaf-1/caspase-9 pathway. Acts by opposing the inhibitory activity of inhibitor of apoptosis proteins (IAP). Inhibits the activity of BIRC6/bruce by inhibiting its binding to caspases (By similarity). {ECO:0000250}. null 560.91 null null 100 uniprot_mouse_length brain_ETD 649.0442505 646.736206 646.737981 12 7744.85318 -2.744458134 DEFB1_MOUSE "Beta-defensin 1; Short=BD-1; Short=mBD-1;AltName: Full=Defensin, beta 1;Flags: Precursor" P56386 MKTHYFLLVMICFLFSQMEPGVGILTSLGRRTDQYKCLQHGGFCLRSSCPSNTKLQGTCKPDKPNCCKS 69 FUNCTION: Has bactericidal activity. {ECO:0000250}. null 181.83 null null 100 uniprot_mouse_length brain_ETD 658.0213013 654.519165 654.509959 16 10451.15372 14.06554467 DFA25_MOUSE Alpha-defensin 25;AltName: Full=Defensin-related cryptdin-25;Flags: Precursor Q5G864 MKTLVLLSALALLAFQVQADPIQNRDEESKIDEQPGKEDQAVSVSFGDPEGSSLQEECEDLICYCRTRGCKRRERLNGTCRKGHLMYMLWCC 92 FUNCTION: May have microbicidal activities. {ECO:0000250}. null 129.73 null null 100 uniprot_mouse_length brain_ETD 622.8914795 623.841797 623.841958 35 21788.44444 -0.258278556 EVI2A_MOUSE Protein EVI2A;AltName: Full=Ecotropic viral integration site 2A protein; Short=EVI-2A;Flags: Precursor P20934 SSSSGTRPNYTHLWASSVTASGSSNQNGSSRHPSDNNTNLVTPAVGHKVSATDKPASSPPVPLASTSTLKSSTPHAFRNSSPTAEIKSQGETFKKEVCEENTSNTAMLICLIVIAVLFLICTFLFLSTVVLANKVSSLKRSKQVGKRQPRSNGDFLASSGLWTAESDTWKRAKELTGSNLLLQSPGVLTAARERKHEEGTEKLN 204 "FUNCTION: May complex with itself or/and other proteins within the membrane, to function as part of a cell-surface receptor." null 636.37 null null 100 uniprot_mouse_length brain_ETD 709.6485596 706.625061 706.615272 21 14809.90637 13.85341578 F150B_MOUSE Protein FAM150B;Flags: Precursor Q80UG6 QSRGPADRQTLLRLLVELVQELKKFHIGDSKRLQLLGESDFALGRREATDYGADQEEQRVEIVPRDLRMKDKFLKHLTGPLYFSPKCSKHFHRLYHNTRDCTIPAYYKRCARLLTRLAVSPMCMER 126 SUBCELLULAR LOCATION: Secreted {ECO:0000305}. null 278.57 null null 100 uniprot_mouse_length brain_ETD 660.9133911 658.769043 658.772887 28 18407.62074 -5.835138825 FA96A_MOUSE MIP18 family protein FAM96A Q9DCL2 MERVSGLLSWTLSRVLWLSGFSEHGAAWQPRIMEEKALEVYDLIRTIRDPEKPNTLEELEVVTESCVEVQEINEDDYLVIIKFTPTVPHCSLATLIGLCLRVKLQRCLPFKHKLEIYISEGTHSTEEDINKQINDKERVAAAMENPNLREIVEQCVLEPD 160 FUNCTION: May play a role in chromosome segregation through establishment of sister chromatid cohesion. {ECO:0000250}. null 465.54 null null 100 uniprot_mouse_length brain_ETD 650.3548584 653.809326 653.80392 20 13050.06784 8.268796974 FKBP2_MOUSE Peptidyl-prolyl cis-trans isomerase FKBP2; Short=PPIase FKBP2; EC=5.2.1.8;AltName: Full=13 kDa FK506-binding protein; Short=13 kDa FKBP; Short=FKBP-13;AltName: Full=FK506-binding protein 2; Short=FKBP-2;AltName: Full=Immunophilin FKBP13;AltName: Full=Rotamase;Flags: Precursor P45878 AEGKRKLQIGVKKRVDHCPIKSRKGDVLHMHYTGKLEDGTEFDSSLPQNQPFVFSLGTGQVIKGWDQGLLGMCEGEKRKLVIPSELGYGERGAPPKIPGGATLVFEVELLKIERRSEL 118 FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. null 177.05 null null 100 uniprot_mouse_length brain_ETD 779.8978271 780.315552 780.307301 12 9346.68331 10.57372884 HEPC_MOUSE Hepcidin;Flags: Precursor Q9EQ21 MALSTRTQAACLLLLLLASLSSTTYLHQQMRQTTELQPLHGEESRADIAIPMQKRRKRDTNFPICIFCCKCCNNSQCGICCKT 83 "FUNCTION: Liver-produced hormone that constitutes the main circulating regulator of iron absorption and distribution across tissues. Acts by promoting endocytosis and degradation of ferroportin, leading to the retention of iron in iron-exporting cells and decreased flow of iron into plasma. Controls the major flows of iron into plasma: absorption of dietary iron in the intestine, recycling of iron by macrophages, which phagocytose old erythrocytes and other cells, and mobilization of stored iron from hepatocytes. {ECO:0000269|PubMed:11447267, ECO:0000269|PubMed:24880340}." null 491.5 null null 100 uniprot_mouse_length brain_ETD 623.6751099 620.408325 620.410531 15 9287.1521 -3.555395302 HMGN2_MOUSE Non-histone chromosomal protein HMG-17;AltName: Full=High mobility group nucleosome-binding domain-containing protein 2 P09602 PKRKAEGDAKGDKTKVKDEPQRRSARLSAKPAPPKPEPKPKKAPAKKGEKVPKGKKGKADAGKDANNPAENGDAKTDQAQKAEGAGDAK 89 FUNCTION: Binds to the inner side of the nucleosomal DNA thus altering the interaction between the DNA and the histone octamer. May be involved in the process which maintains transcribable genes in a unique chromatin conformation (By similarity). {ECO:0000250}. null 4039 null null 100 uniprot_mouse_length brain_ETD 683.3497925 685.909363 685.906362 27 18482.45279 4.374930945 HSPB9_MOUSE Heat shock protein beta-9; Short=HspB9 Q9DAM3 MQRVGSSFSTGQREPGENRVASRCPSVALAERNQVATLPVRLLRDEVQGNGCEQPSFQIKVDAQGFAPEDLVVRIDGQNLTVTGQRQHESNDPSRGRYRMEQSVHRQMQLPPTLDPAAMTCSLTPSGHLWLRGQNKCLPPPEAQTGQSQKPRRGGPKSSLQNESVKNP 168 SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Translocates to nuclear foci during heat shock. {ECO:0000250}. null 486.1 null null 100 uniprot_mouse_length brain_ETD 544.1690674 544.980591 544.979259 24 13048.48952 2.443799999 HVM15_MOUSE Ig heavy chain V region BCL1;Flags: Precursor P01759 QVQLQQSGPEVVRPGVSVKISCKGSGYTFTDYAMHWVKQSHAKSLEWIGVISTYNGNTSYNQKFKGKATMTVDKSSSTVHMELARLTSEDSANLYCARYYGNYFDYWGQGTTLTVSS 117 "SIMILARITY: Contains 1 Ig-like (immunoglobulin-like) domain. {ECO:0000305}.-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" null 215.43 null null 100 uniprot_mouse_length brain_ETD 589.0162354 593.432129 593.430095 23 13618.87892 3.427372941 HVM20_MOUSE Ig heavy chain V region M603 P01789 EVKLVESGGGLVQPGGSLRLSCATSGFTFSDFYMEWVRQPPGKRLEWIAASRNKGNKYTTEYSASVKGRFIVSRDTSQSILYLQMNALRAEDTAIYYCARNYYGSTWYFDVWGAGTTVTVSS 122 MISCELLANEOUS: This chain was isolated from a myeloma protein that binds phosphorylcholine. null 520.43 null null 100 uniprot_mouse_length brain_ETD 614.286499 610.96167 610.970249 21 12803.36489 -14.04172812 HVM32_MOUSE Ig heavy chain V-III region J606 P01801 EVKLEESGGGLVQPGGSMKLSCVASGFTFSNYWMNWVRQSPEKGLEWVAEIRLKSNNYATHYAESVKGRFTISRDDSKSSVYLQMNNLRAEDTGIYYCTTGFAYWGQGTLVTVSA 115 MISCELLANEOUS: This chain was isolated from a myeloma protein that binds inulin. null 137.25 null null 100 uniprot_mouse_length brain_ETD 659.8546143 663.293396 663.287473 20 13238.73618 8.929757209 HVM37_MOUSE Ig heavy chain V region X44 P01807 EVKLLESGGGLVQPGGSLKLSCAASGFDFSRYWMSWVRQAPGKGLEWIGEINPDSSTINYTPSLKDKFIISRDNAKNTLYLQMSKVRSEDTALYYCARLHYYGYAAYWGQGTLVTVSAE 119 MISCELLANEOUS: This chain was isolated from an IgA myeloma protein that binds galactan. null 128.66 null null 100 uniprot_mouse_length brain_ETD 642.4708862 641.651855 641.648407 21 13446.60241 5.37438995 HVM46_MOUSE Ig heavy chain V region MOPC 315;Flags: Precursor P01822 DVQLQESGPGLVKPSQSLSLTCSVTGYSITSGYFWNWIRQFPGNKLEWLGFIKYDGSNGYNPSLKNRVSITRDTSENQFFLKLNSVTTEDTATYYCAGDNDHLYYFDYWGQGTTLTVSS 119 "MISCELLANEOUS: This alpha chain was isolated from a myeloma protein that has anti-dinitrophenyl activity.-----------------------------------------------------------------------Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsDistributed under the Creative Commons Attribution-NoDerivs License-----------------------------------------------------------------------" null 185.45 null null 100 uniprot_mouse_length brain_ETD 830.6020508 832.484558 832.491338 13 10804.37992 -8.144102193 HVM54_MOUSE Ig heavy chain V region 5-84;Flags: Precursor P18525 EVKLVESGGGLVQPGGSLKLSCAASGFTFSSYTMSWVRQTPEKRLEWVAYISNGGGSTYYPDTVKGRFTISRDNAKNNLYLQMSSLKSEDTAMYYCAR 98 "INTERACTION: P01636:-; NbExp=1; IntAct=EBI-1035995, EBI-1036001;" null 153.39 null null 100 uniprot_mouse_length brain_ETD 589.0162354 588.138672 588.144487 25 14671.59995 -9.887238814 HYPK_MOUSE Huntingtin-interacting protein K;AltName: Full=Huntingtin yeast partner K Q9CR41 MRRRGEIEMATEGDVELELETETSGPERPPEKPRKHDSGAADLERVTDYAEEKEIQSSNLETAMSVIGDRRSREQKAKQEREKELAKVTIKKEDLELIMTEMEISRAAAERSLREHMGNVVEALIALTN 129 FUNCTION: Has a chaperone-like activity preventing polyglutamine (polyQ) aggregation of HTT. Protects against HTT polyQ-mediated apoptosis in neuronal cells. Required for optimal NAA10-NAA15 complex-mediated N-terminal acetylation (By similarity). {ECO:0000250}. null 457.35 null null 100 uniprot_mouse_length brain_ETD 767.18396 771.879578 771.872873 13 10016.34078 8.686192964 IAPP_MOUSE Islet amyloid polypeptide;AltName: Full=Amylin;AltName: Full=Diabetes-associated peptide; Short=DAP;Flags: Precursor P12968 MMCISKLPAVLLILSVALNHLRATPVRSGSNPQMDKRKCNTATCATQRLANFLVRSSNNLGPVLPPTNVGSNTYGKRNAAGDPNRESLDFLLV 93 "FUNCTION: Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism." null 222.33 null null 100 uniprot_mouse_length brain_ETD 544.1690674 544.207458 544.207018 27 14658.57542 0.809427441 IFM5_MOUSE Interferon-induced transmembrane protein 5;AltName: Full=Bone-restricted interferon-induced transmembrane protein-like protein; Short=Bril;AltName: Full=Dispanin subfamily A member 1; Short=DSPA1;AltName: Full=Fragilis family member 4 O88728 MDTSYPREDPRAPSSRKADAAAHTALSMGTPGPTPRDHMLWSVFSTMYLNLCCLGFLALVHSVKARDQKMAGNLEAARQYGSKAKCYNILAAMWTLVPPLLLLGLVVTGALHLSKLAKDSAAFFSTKFDEEDYN 134 "FUNCTION: Required for normal bone mineralization. {ECO:0000269|PubMed:18442316, ECO:0000269|PubMed:20838829, ECO:0000269|PubMed:24058703, ECO:0000269|PubMed:24715519}." null 327.86 null null 100 uniprot_mouse_length brain_ETD 660.9133911 658.455627 658.451547 29 19056.07456 6.197026076 IFNAD_MOUSE Interferon alpha-13; Short=IFN-alpha-13;Flags: Precursor Q80SU4 CDLPQTHNLRNKRALTLLEQMRRLSPLSCLKDRKDFGFPQEKVDAQQIKKAQAIPFVHELTQQILTLFTSNDSSAAWNATLLDSFCNDLHQQLNDLKACLMQQVGVQEFPLTQEDSLLAVRKYFHSITVYLREKKHSPCAWEVVRAEVQRTLSSSANLLARLSKEE 166 "FUNCTION: Exhibits antiviral activity against Theiler's virus, Mengo virus and vesicular stomatitis virus. Interferons alpha stimulate the production of two enzymes: a protein kinase and an oligoadenylate synthetase. {ECO:0000269|PubMed:12930842}." null 468.91 null null 100 uniprot_mouse_length brain_ETD 616.9188232 615.348633 615.348056 32 19648.11595 0.937376001 IL23A_MOUSE Interleukin-23 subunit alpha; Short=IL-23 subunit alpha; Short=IL-23-A;AltName: Full=Interleukin-23 subunit p19; Short=IL-23p19;Flags: Precursor Q9EQ14 VPRSSSPDWAQCQQLSRNLCMLAWNAHAPAGHMNLLREEEDEETKNNVPRIQCEDGCDPQGLKDNSQFCLQRIRQGLAFYKHLLDSDIFKGEPALLPDSPMEQLHTSLLGLSQLLQPEDHPRETQQMPSLSSSQQWQRPLLRSKILRSLQAFLAIAARVFAHGAATLTEPLVPTA 175 "FUNCTION: Associates with IL12B to form the IL-23 interleukin, a heterodimeric cytokine which functions in innate and adaptive immunity. IL-23 may constitute with IL-17 an acute response to infection in peripheral tissues. IL-23 binds to a heterodimeric receptor complex composed of IL12RB1 and IL23R, activates the Jak- Stat signaling cascade, stimulates memory rather than naive T- cells and promotes production of proinflammatory cytokines. IL-23 induces autoimmune inflammation and thus may be responsible for autoimmune inflammatory diseases and may be important for tumorigenesis. {ECO:0000269|PubMed:11114383, ECO:0000269|PubMed:11390512, ECO:0000269|PubMed:12610626, ECO:0000269|PubMed:12847224, ECO:0000269|PubMed:14662908, ECO:0000269|PubMed:14978083, ECO:0000269|PubMed:16157683, ECO:0000269|PubMed:16648837, ECO:0000269|PubMed:16670770, ECO:0000269|PubMed:16688182}." null 543.19 null null 100 uniprot_mouse_length brain_ETD 542.6261597 543.276489 543.2805 25 13550.00185 -7.382451952 IL4_MOUSE Interleukin-4; Short=IL-4;AltName: Full=B-cell IgG differentiation factor;AltName: Full=B-cell growth factor 1;AltName: Full=B-cell stimulatory factor 1; Short=BSF-1;AltName: Full=IGG1 induction factor;AltName: Full=Lymphocyte stimulatory factor 1;Flags: Precursor P07750 HIHGCDKNHLREIIGILNEVTGEGTPCTEMDVPNVLTATKNTTESELVCRASKVLRIFYLKHGKTPCLKKNSSVLMELQRLFRAFRCLDSSISCTMNESKSTSLKDFLESLKSIMQMDYS 120 FUNCTION: Participates in at least several B-cell activation processes as well as of other cell types. It is a costimulator of DNA-synthesis. It induces the expression of class II MHC molecules on resting B-cells. It enhances both secretion and cell surface expression of IgE and IgG1. It also regulates the expression of the low affinity Fc receptor for IgE (CD23) on both lymphocytes and monocytes. null 268.02 null null 100 uniprot_mouse_length brain_ETD 646.1060791 644.924194 644.918841 22 14158.20215 8.300790111 IL9_MOUSE Interleukin-9; Short=IL-9;AltName: Full=Cytokine P40;AltName: Full=T-cell growth factor P40;Flags: Precursor P15247 QRCSTTWGIRDTNYLIENLKDDPPSKCSCSGNVTSCLCLSVPTDDCTTPCYREGLLQLTNATQKSRLLPVFHRVKRIVEVLKNITCPSFSCEKPCNQTMAGNTLSFLKSLLGTFQKTEMQRQKSRP 126 FUNCTION: Supports IL-2 independent and IL-4 independent growth of helper T-cells. null 213.41 null null 100