entry
stringlengths 6
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stringlengths 5
11
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stringlengths 3
2.44k
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stringlengths 2
35.2k
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stringlengths 7
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O88554
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PARP2_MOUSE
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Poly [ADP-ribose] polymerase 2 (PARP-2) (mPARP-2) (EC 2.4.2.30) (ADP-ribosyltransferase diphtheria toxin-like 2) (ARTD2) (DNA ADP-ribosyltransferase PARP2) (EC 2.4.2.-) (NAD(+) ADP-ribosyltransferase 2) (ADPRT-2) (Poly[ADP-ribose] synthase 2) (pADPRT-2) (Protein poly-ADP-ribosyltransferase PARP2) (EC 2.4.2.-)
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MAPRRQRSGSGRRVLNEAKKVDNGNKATEDDSPPGKKMRTCQRKGPMAGGKDADRTKDNRDSVKTLLLKGKAPVDPECAAKLGKAHVYCEGDDVYDVMLNQTNLQFNNNKYYLIQLLEDDAQRNFSVWMRWGRVGKTGQHSLVTCSGDLNKAKEIFQKKFLDKTKNNWEDRENFEKVPGKYDMLQMDYAASTQDESKTKEEETLKPESQLDLRVQELLKLICNVQTMEEMMIEMKYDTKRAPLGKLTVAQIKAGYQSLKKIEDCIRAGQHGRALVEACNEFYTRIPHDFGLSIPPVIRTEKELSDKVKLLEALGDIEIALKLVKSERQGLEHPLDQHYRNLHCALRPLDHESNEFKVISQYLQSTHAPTHKDYTMTLLDVFEVEKEGEKEAFREDLPNRMLLWHGSRLSNWVGILSHGLRVAPPEAPITGYMFGKGIYFADMSSKSANYCFASRLKNTGLLLLSEVALGQCNELLEANPKAQGLLRGKHSTKGMGKMAPSPAHFITLNGSTVPLGPASDTGILNPEGYTLNYNEFIVYSPNQVRMRYLLKIQFNFLQLW
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Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair. Mediates glutamate, aspartate or serine ADP-ribosylation of proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of target residues and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units. Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (By similarity). Mediates glutamate and aspartate ADP-ribosylation of target proteins in absence of HPF1 (By similarity). Following interaction with HPF1, catalyzes serine ADP-ribosylation of target proteins HPF1 conferring serine specificity by completing the PARP2 active site (By similarity). PARP2 initiates the repair of double-strand DNA breaks: recognizes and binds DNA breaks within chromatin and recruits HPF1, licensing serine ADP-ribosylation of target proteins, such as histones, thereby promoting decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks (By similarity). HPF1 initiates serine ADP-ribosylation but restricts the polymerase activity of PARP2 in order to limit the length of poly-ADP-ribose chains (By similarity). Specifically mediates formation of branched poly-ADP-ribosylation (By similarity). Branched poly-ADP-ribose chains are specifically recognized by some factors, such as APLF (By similarity). In addition to proteins, also able to ADP-ribosylate DNA: preferentially acts on 5'-terminal phosphates at DNA strand breaks termini in nicked duplex (By similarity).
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O88559
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MEN1_MOUSE
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Menin
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MGLKAAQKTLFPLRSIDDVVRLFAAELGREEPDLVLLSLVLGFVEHFLAVNRVIPTNVPELTFQPSPAPDPPGGLTYFPVADLSIIAALYARFTAQIRGAVDLSLYPREGGVSSRELVKKVSDVIWNSLSRSYFKDRAHIQSLFSFITGTKLDSSGVAFAVVGACQALGLRDVHLALSEDHAWVVFGPNGEQTAEVTWHGKGNEDRRGQTVNAGVAERSWLYLKGSYMRCDRKMEVAFMVCAINPSIDLHTDSLELLQLQQKLLWLLYDLGHLERYPMALGNLADLEELEPTPGRPDPLTLYHKGIASAKTYYQDEHIYPYMYLAGYHCRNRNVREALQAWADTATVIQDYNYCREDEEIYKEFFEVANDVIPNLLKEAASLLETGEERTGEQAQGTQGQGSALQDPECFAHLLRFYDGICKWEEGSPTPVLHVGWATFLVQSLGRFEGQVRQKVHIVSREAEAAEAEEPWGDEAREGRRRGPRRESKPEEPPPPKKPALDKGPGSGQSAGSGPPRKTSGTVPGTTRGGQEVGNAAQAPAPAASPPPEGPVLTFQSEKMKGMKELLVATKINSSAIKLQLTAQSQVQMKKQKVSTPSDYTLSFLKRQRKGL
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Essential component of a MLL/SET1 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3 (H3K4). Functions as a transcriptional regulator. Binds to the TERT promoter and represses telomerase expression. Plays a role in TGFB1-mediated inhibition of cell-proliferation, possibly regulating SMAD3 transcriptional activity. Represses JUND-mediated transcriptional activation on AP1 sites, as well as that mediated by NFKB subunit RELA. Positively regulates HOXC8 and HOXC6 gene expression (By similarity). May be involved in normal hematopoiesis through the activation of HOXA9 expression. May be involved in DNA repair.
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O88561
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S27A3_MOUSE
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Long-chain fatty acid transport protein 3 (FATP-3) (Fatty acid transport protein 3) (Arachidonate--CoA ligase) (EC 6.2.1.15) (Long-chain-fatty-acid--CoA ligase) (EC 6.2.1.3) (Solute carrier family 27 member 3) (Very long-chain acyl-CoA synthetase homolog 3) (VLCS-3) (EC 6.2.1.-)
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MAALLLLLPLLLLLPLLLKLDVWPQLRWLPADLAFTVRALRCKRALRARALAAAAADPESSESGCSLAWRLAYLAREQPTHTFLIHGAQRFSYAEAERESNRIARAFLRARGWTGGRRGSGRGSTEEGARVAPPAGDAAARGTTAPPLAPGATVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVLATEFLESLEPDLPALRAMGLHLWATGPETNVAGISNLLSEAADQVDEPVPGYLSAPQNIMDTCLYIFTSGTTGLPKAARISHLKVLQCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFNYTGRQGAVGRASWLYKHIFPFSLIRYDVMTGEPIRNAQGHCMTTSPGEPGLLVAPVSQQSPFLGYAGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHEGRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQESLATTETFKQQKVRMANEGFDPSVLSDPLYVLDQDIGAYLPLTPARYSALLSGDLRI
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Mainly functions as an acyl-CoA ligase catalyzing the ATP-dependent formation of fatty acyl-CoA using LCFA and very-long-chain fatty acids (VLCFA) as substrates. Can mediate the levels of long-chain fatty acids (LCFA) in the cell by facilitating their transport across membranes.
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O88563
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MRP3_RAT
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ATP-binding cassette sub-family C member 3 (EC 7.6.2.-) (EC 7.6.2.2) (EC 7.6.2.3) (Canalicular multispecific organic anion transporter 2) (MRP-like protein 2) (MLP-2) (Multidrug resistance-associated protein 3)
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MDRLCGSGELGSKFWDSNLTVYTNTPDLTPCFQNSLLAWVPCIYLWAALPCYLFYLRHHRLGYIVLSCLSRLKTALGVLLWCISWVDLFYSFHGLVHGSSPAPVFFITPLLVGITMLLATLLIQYERLRGVRSSGVLIIFWLLCVICAIIPFRSKILLALAEGKILDPFRFTTFYIYFALVLCAFILSCFQEKPPLFSPENLDTNPCPEASAGFFSRLSFWWFTKLAILGYRRPLEDSDLWSLSEEDCSHKVVQRLLEAWQKQQTQASGPQTAALEPKIAGEDEVLLKARPKTKKPSFLRALVRTFTSSLLMGACFKLIQDLSPSSTHSCSASSSGLFRPHGPYWWGFLLAGLMFVSSTMQTLILHQHYHCIFVMALRIRTAIIGVIYRKALTITNSVKREYTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQILGPSALAGVAVIVLLIPLNGAVSMKMKTYQVQQMKFKDSRIKLMSEILNGIKVLKLYAWEPTFLEQVEGIRQGELQLLRKGAYLQAISTFIWVCTPFMVTLITLGVYVCVDKNNVLDAEKAFVSLSLFNILKIPLNLLPQLISGMTQTSVSLKRIQDFLNQDELDPQCVERKTISPGRAITIHNGTFSWSKDLPPTLHSINIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGSVAYVPQQAWIQNCTLQENVLFGQPMNPKRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGPEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQITEMGHYSELLQHDGSFANFLRNYAPDENQEANEGVLQHANEEVLLLEDTLSTHTDLTDTEPAIYEVRKQFMREMSSLSSEGEGQNRPVLKRYTSSLEKEVPATQTKETGALIKEEIAETGNVKLSVYWDYAKSVGLCTTLFICLLYAGQNAVAIGANVWLSAWTNDVEEHGQQNNTSVRLGVYATLGILQGLLVMLSAFTMVVGAIQAARLLHTALLHNQIRAPQSFFDTTPSGRILNRFSKDIYVIHEVLAPTILMLFNSFYTSISTIVVIVASTPLFCVVVLPLAVFYGFVQRFYVATSRQLKRLESVSRSPIFSHFSETVTGTSVIRAYGRVQDFKVLSDAKVDSNQKTTYPYIASNRWLGVHVEFVGNCVVLFSALFAVIGRNSLNPGLVGLSVSYALQVTLSLNWMIRTLSDLESNIIAVERVKEYSKTETEAPWVLESNRAPEGWPRSGVVEFRNYSVRYRPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSDEDIWRTLELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIFYGMAKDAGLA
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ATP-dependent transporter of the ATP-binding cassette (ABC) family that binds and hydrolyzes ATP to enable active transport of various substrates including many drugs, toxicants and endogenous compound across cell membranes. Transports glucuronide conjugates such as bilirubin diglucuronide, estradiol-17-beta-o-glucuronide and GSH conjugates such as leukotriene C4 (LTC4) (By similarity). Transports also various bile salts (taurocholate, glycocholate, taurochenodeoxycholate-3-sulfate, taurolithocholate- 3-sulfate). Does not contribute substantially to bile salt physiology but provides an alternative route for the export of bile acids and glucuronides from cholestatic hepatocytes (By similarity). May contribute to regulate the transport of organic compounds in testes across the blood-testis-barrier (By similarity).
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O88566
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AXIN2_MOUSE
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Axin-2 (Axin-like protein) (Axil) (Axis inhibition protein 2) (Conductin)
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MSSAVLVTLLPDPSSSFREDAPRPPVPGEEGETPPCQPSVGKVQSTKPMPVSSNARRNEDGLGEPEGRASPDSPLTRWTKSLHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDTKTLRVAKAIYKRYIENNSVVSKQLKPATKTYIRDGIKKQQIGSVMFDQAQTEIQAVMEENAYQVFLTSDIYLEYVRSGGENTAYMSNGGLGSLKVLCGYLPTLNEEEEWTCADLKCKLSPTVVGLSSKTLRATASVRSTETAENGFRSFKRSDPVNPYHVGSGYVFAPATSANDSELSSDALTDDSMSMTDSSVDGVPPYRMGSKKQLQREMHRSVKANGQVSLPHFPRTHRLPKEMTPVEPAAFAAELISRLEKLKLELESRHSLEERLQQIREDEEKEGSEQALSSRDGAPVQHPLALLPSGSYEEDPQTILDDHLSRVLKTPGCQSPGVGRYSPRSRSPDHHHQHHHHQQCHTLLPTGGKLPPVAACPLLGGKSFLTKQTTKHVHHHYIHHHAVPKTKEEIEAEATQRVRCLCPGGTDYYCYSKCKSHPKAPEPLPGEQFCGSRGGTLPKRNAKGTEPGLALSARDGGMSSAAGAPQLPGEEGDRSQDVWQWMLESERQSKSKPHSAQSIRKSYPLESACAAPGERVSRHHLLGASGHSRSVARAHPFTQDPAMPPLTPPNTLAQLEEACRRLAEVSKPQKQRCCVASQQRDRNHSAAGQAGASPFANPSLAPEDHKEPKKLASVHALQASELVVTYFFCGEEIPYRRMLKAQSLTLGHFKEQLSKKGNYRYYFKKASDEFACGAVFEEIWDDETVLPMYEGRILGKVERID
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Inhibitor of the Wnt signaling pathway. Down-regulates beta-catenin. Probably facilitate the phosphorylation of beta-catenin and APC by GSK3B.
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O88569
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ROA2_MOUSE
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Heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1)
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MEKTLETVPLERKKREKEQFRKLFIGGLSFETTEESLRNYYEQWGKLTDCVVMRDPASKRSRGFGFVTFSSMAEVDAAMAARPHSIDGRVVEPKRAVAREESGKPGAHVTVKKLFVGGIKEDTEEHHLRDYFEEYGKIDTIEIITDRQSGKKRGFGFVTFDDHDPVDKIVLQKYHTINGHNAEVRKALSRQEMQEVQSSRSGRGGNFGFGDSRGGGGNFGPGPGSNFRGGSDGYGSGRGFGDGYNGYGGGPGGGNFGGSPGYGGGRGGYGGGGPGYGNQGGGYGGGYDNYGGGNYGSGSYNDFGNYNQQPSNYGPMKSGNFGGSRNMGGPYGGGNYGPGGSGGSGGYGGRSRY
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Heterogeneous nuclear ribonucleoprotein (hnRNP) that associates with nascent pre-mRNAs, packaging them into hnRNP particles. The hnRNP particle arrangement on nascent hnRNA is non-random and sequence-dependent and serves to condense and stabilize the transcripts and minimize tangling and knotting. Packaging plays a role in various processes such as transcription, pre-mRNA processing, RNA nuclear export, subcellular location, mRNA translation and stability of mature mRNAs. Forms hnRNP particles with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus. Involved in transport of specific mRNAs to the cytoplasm in oligodendrocytes and neurons: acts by specifically recognizing and binding the A2RE (21 nucleotide hnRNP A2 response element) or the A2RE11 (derivative 11 nucleotide oligonucleotide) sequence motifs present on some mRNAs, and promotes their transport to the cytoplasm (By similarity). Specifically binds single-stranded telomeric DNA sequences, protecting telomeric DNA repeat against endonuclease digestion (By similarity). Also binds other RNA molecules, such as primary miRNA (pri-miRNAs): acts as a nuclear 'reader' of the N6-methyladenosine (m6A) mark by specifically recognizing and binding a subset of nuclear m6A-containing pri-miRNAs. Binding to m6A-containing pri-miRNAs promotes pri-miRNA processing by enhancing binding of DGCR8 to pri-miRNA transcripts. Involved in miRNA sorting into exosomes following sumoylation, possibly by binding (m6A)-containing pre-miRNAs. Acts as a regulator of efficiency of mRNA splicing, possibly by binding to m6A-containing pre-mRNAs (By similarity). Plays a role in the splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (By similarity). Also plays a role in the activation of the innate immune response. Mechanistically, senses the presence of viral DNA in the nucleus, homodimerizes and is demethylated by JMJD6. In turn, translocates to the cytoplasm where it activates the TBK1-IRF3 pathway, leading to interferon alpha/beta production.
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O88572
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LRP6_MOUSE
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Low-density lipoprotein receptor-related protein 6 (LRP-6)
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MGAVLRSLLACSFCVLLRAAPLLLYANRRDLRLVDATNGKENATIVVGGLEDAAAVDFVFGHGLIYWSDVSEEAIKRTEFNKSESVQNVVVSGLLSPDGLACDWLGEKLYWTDSETNRIEVSNLDGSLRKVLFWQELDQPRAIALDPSSGFMYWTDWGEVPKIERAGMDGSSRFVIINTEIYWPNGLTLDYQERKLYWADAKLNFIHKSNLDGTNRQAVVKGSLPHPFALTLFEDTLYWTDWNTHSILACNKYTGEGLREIHSNIFSPMDIHAFSQQRQPNATNPCGIDNGGCSHLCLMSPVKPFYQCACPTGVKLMENGKTCKDGATELLLLARRTDLRRISLDTPDFTDIVLQLEDIRHAIAIDYDPVEGYIYWTDDEVRAIRRSFIDGSGSQFVVTAQIAHPDGIAVDWVARNLYWTDTGTDRIEVTRLNGTMRKILISEDLEEPRAIVLDPMVGYMYWTDWGEIPKIERAALDGSDRVVLVNTSLGWPNGLALDYDEGTIYWGDAKTDKIEVMNTDGTGRRVLVEDKIPHIFGFTLLGDYVYWTDWQRRSIERVHKRSAEREVIIDQLPDLMGLKATSVHRVIGSNPCAEDNGGCSHLCLYRPQGLRCACPIGFELIGDMKTCIVPEAFLLFSRRADIRRISLETNNNNVAIPLTGVKEASALDFDVTDNRIYWTDISLKTISRAFMNGSALEHVVEFGLDYPEGMAVDWLGKNLYWADTGTNRIEVSKLDGQHRQVLVWKDLDSPRALALDPAEGFMYWTEWGGKPKIDRAAMDGSERTTLVPNVGRANGLTIDYAKRRLYWTDLDTNLIESSDMLGLNREVIADDLPHPFGLTQYQDYIYWTDWSRRSIERANKTSGQNRTIIQGHLDYVMDILVFHSSRQAGWNECASSNGHCSHLCLAVPVGGFVCGCPAHYSLNADNRTCSAPSTFLLFSQKSAINRMVIDEQQSPDIILPIHSLRNVRAIDYDPLDKQLYWIDSRQNSIRKAHEDGGQGFNVVANSVANQNLEIQPYDLSIDIYSRYIYWTCEATNVIDVTRLDGRSVGVVLKGEQDRPRAIVVNPEKGYMYFTNLQERSPKIERAALDGTEREVLFFSGLSKPIALALDSKLGKLFWADSDLRRIESSDLSGANRIVLEDSNILQPVGLTVFENWLYWIDKQQQMIEKIDMTGREGRTKVQARIAQLSDIHAVKELNLQEYRQHPCAQDNGGCSHICLVKGDGTTRCSCPMHLVLLQDELSCGEPPTCSPQQFTCFTGDIDCIPVAWRCDGFTECEDHSDELNCPVCSESQFQCASGQCIDGALRCNGDANCQDKSDEKNCEVLCLIDQFRCANGQCVGKHKKCDHSVDCSDRSDELDCYPTEEPAPQATNTVGSVIGVIVTIFVSGTIYFICQRMLCPRMKGDGETMTNDYVVHSPASVPLGYVPHPSSLSGSLPGMSRGKSMISSLSIMGGSSGPPYDRAHVTGASSSSSSSTKGTYFPAILNPPPSPATERSHYTMEFGYSSNSPSTHRSYSYRPYSYRHFAPPTTPCSTDVCDSDYAPSRRMTSVATAKGYTSDVNYDSEPVPPPPTPRSQYLSAEENYESCPPSPYTERSYSHHLYPPPPSPCTDSS
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Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor-ligand complexes into ribosome-sized signalosomes. Cell-surface coreceptor of Wnt/beta-catenin signaling, which plays a pivotal role in bone formation. The Wnt-induced Fzd/LRP6 coreceptor complex recruits DVL1 polymers to the plasma membrane which, in turn, recruits the AXIN1/GSK3B-complex to the cell surface promoting the formation of signalosomes and inhibiting AXIN1/GSK3-mediated phosphorylation and destruction of beta-catenin. Required for posterior patterning of the epiblast during gastrulation (By similarity). {ECO:0000250, ECO:0000269|PubMed:15142971}.
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O88574
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SAP30_MOUSE
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Histone deacetylase complex subunit SAP30 (30 kDa Sin3-associated polypeptide) (Sin3 corepressor complex subunit SAP30) (Sin3-associated polypeptide p30)
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MNGFTPEEMSRGGDAAAAVAAVVAAAAAAASAGNGNAAGGGAEVPGAGAVSASGPPGAAGPGPGQLCCLREDGERCGRAAGNASFSKRIQKSISQKKVKIELDKSARHLYICDYHKNLIQSVRNRRKRKGSDDDGGDSPVQDIDTPEVDLYQLQVNTLRRYKRHFKLPTRPGLNKAQLVEIVGCHFKSIPVNEKDTLTCFIYSVRNDKNKSDLKADSGVH
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Involved in the functional recruitment of the Sin3-histone deacetylase complex (HDAC) to a specific subset of N-CoR corepressor complexes. Capable of transcription repression by N-CoR. Active in deacetylating core histone octamers (when in a complex) but inactive in deacetylating nucleosomal histones.
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O88575
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S620B_MOUSE
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Sodium- and chloride-dependent transporter XTRP3B (IMINO-K) (Solute carrier family 6 member 20B)
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MESPSAHAVSLPEDEELQPWGGAGGPGQHPGRPRSTECAHPGVVEKVRPKWDNPLQFLLVCISYAVGLGNVWRFPYLCQMYGGGNFLVPYIIMLIVEGMPLLYLELAVGQRMRQGSIGAWRTISPYLSGVGIASLVVSFLASVYFNVINTWALWYLFHSFQDPLPWSVCPLNSNHTGYDEECEKASSTQYFWYRKTLNISPSIQENGGVQWEPALCLTLAWLMVYLCILRGTESTGKVVYFTTSLPYFVLIIYLVRGLTLHGATNGLAYMFTPKIEQLANPKAWINAATQIFFSLGLGCGGLIAFASYNEPSNDCQKHALIVSVINSTTAIFSSIVTFSIYGFKATFNYENCLNKVILLLTNSFDLEDGFLTVSNLEEVKNYLASTYPNKYSEVFPHIRNCSLESELDTAVQGTGLAFIVYTEAIKNMEVSQLWSVLYFFMLLTLGMGSMVGTGTAILTPLTDSKIISSYLPKEAISGLVCLLNCAIGMVFTMEAGNYWFDLFNDYTATLSLLLIVLVETIAVCYVYGLKRFESDLRAMTGRTLSWYWKVMWAFVSPLLIVGLFIFYLSDYILTGTLQYQAWDATQGHVVTKDYPTYALAVIGLLVASSTMCIPLVALGTFVTRHFKIREQFSAA
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Does not show transporter activity with a range of tested amino acids including proline, glutamine, glutamic acid, leucine, alanine, histidine, glycine and arginine.
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O88576
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S6A18_MOUSE
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Sodium-dependent neutral amino acid transporter B(0)AT3 (Sodium- and chloride-dependent transporter XTRP2) (Solute carrier family 6 member 18) (System B(0) neutral amino acid transporter AT3)
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MAQASGMDPLVDIEDERPKWDNKLQYLLSCIGFAVGLGNIWRFPYLCQTHGGGAFLIPYFIALVFEGIPLFYIELAIGQRLRRGSIGVWKTISPYLGGVGLGCFSVSFLVSLYYNTVLLWVLWFFLNSFQHPLPWSTCPLDLNRTGFVQECQSSGTVSYFWYRQTLNITSDISNTGTIQWKLFLCLVACWSTVYLCVIRGIESTGKVIYFTALFPYLVLTIFLIRGLTLPGATEGLIYLFTPNMKTLQNPRVWLDAATQIFFSLSLAFGGHIAFASYNPPRNNCEKDAVIIALVNSMTSLYASIAIFSVMGFKASNDYGRCLDRNILSLINEFDLPELSISRDEYPSVLMYLNATQTARVAQLPLKTCHLEDFLDKSASGPGLAFIVFTEAVLHMPGASVWSVLFFGMLFTLGLSSMFGNMEGVITPLLDMGILPKGIPKEVMTGVICFACFLSAICFTLQSGGYWLEIFDSFAASLNLIIFAFMEVVGVIHIYGMKRFCDDIEWMTGRRPGLYWQVTWRVVSPMLLFGIFLSYIVLLIQTPPSYKAWNPQYEHFPSREEKFYPGWVQVTCVLLSFLPSLWVPGVALAQLLSQYKQRWKATHLESGLKLQESRGC
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Symporter that transports one amino acid molecule together with two sodium and one chloride ions in kidneys and plays a role in the neutral amino acids reabsorption. Preferentially transports neutral amino acids such as L-glycine and L-alanine but also other neutral amino acids. Required CLTRN for cell surface expression and for its amino acid transporter activity. The transport mechanism is pH-independent.
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O88582
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SOCS2_RAT
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Suppressor of cytokine signaling 2 (SOCS-2) (Cytokine-inducible SH2 protein 2)
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MTLRCLEPSGNGADRTRSQWGTAGSPEDQSPEAARLAKALRELSQTGWYWGSMTVNEAKEKLKEAPEGTFLIRDSSHSDYLLTISVKTSAGPTNLRIEYQDGKFRLDSIICVKSKLKQFDSVVHLIDYYVQMCKDKRTGPEAPRNGTVHLYLTKPLYTSAPTLQHFCRLSINKCTGTIRGLPLPTRLKDYLEEYKFQV
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SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. SOCS2 appears to be a negative regulator in the growth hormone/IGF1 signaling pathway. Probable substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity).
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O88583
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SOCS3_RAT
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Suppressor of cytokine signaling 3 (SOCS-3) (Cytokine-inducible SH2 protein 3)
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MVTHSKFPAAGMSRPLDTSLRLKTFSSKSEYQLVVNAVRKLQESGFYWSAVTGGEANLLLSAEPAGTFLIRDSSDQRHFFTLSVETQSGTKNLRIQCEGGSFSLQSDPRSTQPVPRFDCVLKLVHHYMPPPGAPSFSLPPTEPSFEVQEQPPAQALPGGTPKRAYYIYSGGEKIPLVLSRPLSSNVATLQHLCRKTVNGHLDSYEKVTQLPGPIREFLDQYDAPL
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SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. SOCS3 is involved in negative regulation of cytokines that signal through the JAK/STAT pathway. Inhibits cytokine signal transduction by binding to tyrosine kinase receptors including IL6ST/gp130, LIF, erythropoietin, insulin, IL12, GCSF and leptin receptors. Binding to JAK2 inhibits its kinase activity and regulates IL6 signaling. Suppresses fetal liver erythropoiesis. Regulates onset and maintenance of allergic responses mediated by T-helper type 2 cells (By similarity). Probable substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity).
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O88587
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COMT_MOUSE
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Catechol O-methyltransferase (EC 2.1.1.6)
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MLLAAVSLGLLLLAFLLLLRHLGWGLVAIGWFEFVQQPVHNLLMGGTKEQRILRHVQQHAKPGDPQSVLEAIDTYCSEKEWAMNVGDAKGQIMDAVIREYRPSLVLELGAYCGYSAVRMARLLPPGARLLTMEINPDYAAITQQMLDFAGLQDKVSILIGASQDLIPQLKKKYDVDTLDMVFLDHWKDRYLPDTLLLEECGLLRKGTVLLADNVIVPGTPDFLAYVRGSSSFECTHYSSYLEYMKVVDGLEKAVYQGPGSSPVKS
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Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol.
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O88593
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PGRP1_MOUSE
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Peptidoglycan recognition protein 1 (Cytokine tag7) (Peptidoglycan recognition protein short) (PGRP-S)
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MLFACALLALLGLATSCSFIVPRSEWRALPSECSSRLGHPVRYVVISHTAGSFCNSPDSCEQQARNVQHYHKNELGWCDVAYNFLIGEDGHVYEGRGWNIKGDHTGPIWNPMSIGITFMGNFMDRVPAKRALRAALNLLECGVSRGFLRSNYEVKGHRDVQSTLSPGDQLYQVIQSWEHYRE
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Innate immunity protein that plays several important functions in antimicrobial and antitumor defense systems. Acts as a pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria and thus provides bactericidal activity. Forms an equimolar complex with heat shock protein HSPA1A and induces programmed cell death through apoptosis and necroptosis in tumor cell lines by activating the TNFR1 receptor on the target cell membrane. In addition, acts in complex with the Ca(2+)-binding protein S100A4 as a chemoattractant able to induce lymphocyte movement. Mechanistically, this complex acts as a ligand of the chemotactic receptors CCR5 and CXCR3 which are present on the cells of the immune system. Promotes also the activation of lymphocytes that become able to kill virus-infected cells as well as tumor cells by modulating the spectrum of their target-cell specificity. Induction of cytotoxicity on monocyte surface requires interaction with TREM1 receptor (By similarity).
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O88597
|
BECN1_MOUSE
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Beclin-1 (Coiled-coil myosin-like BCL2-interacting protein) [Cleaved into: Beclin-1-C 35 kDa; Beclin-1-C 37 kDa]
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MEGSKASSSTMQVSFVCQRCSQPLKLDTSFKILDRVTIQELTAPLLTTAQAKPGETQEEEANSGEEPFIETRQDGVSRRFIPPARMMSTESANSFTLIGEASDGGTMENLSRRLKVTGDLFDIMSGQTDVDHPLCEECTDTLLDQLDTQLNVTENECQNYKRCLEILEQMNEDDSEQLQRELKELALEEERLIQELEDVEKNRKVVAENLEKVQAEAERLDQEEAQYQREYSEFKRQQLELDDELKSVENQVRYAQIQLDKLKKTNVFNATFHIWHSGQFGTINNFRLGRLPSVPVEWNEINAAWGQTVLLLHALANKMGLKFQRYRLVPYGNHSYLESLTDKSKELPLYCSGGLRFFWDNKFDHAMVAFLDCVQQFKEEVEKGETRFCLPYRMDVEKGKIEDTGGSGGSYSIKTQFNSEEQWTKALKFMLTNLKWGLAWVSSQFYNK
|
Plays a central role in autophagy. Acts as core subunit of different PI3K complex forms that mediate formation of phosphatidylinositol 3-phosphate and are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis. Involved in regulation of degradative endocytic trafficking and required for the abcission step in cytokinesis, probably in the context of PI3KC3-C2 (By similarity). Essential for the formation of PI3KC3-C2 but not PI3KC3-C1 PI3K complex forms. Involved in endocytosis including endosome formation in neuronal cells. May play a role in antiviral host defense (By similarity).
|
O88602
|
CCG2_MOUSE
|
Voltage-dependent calcium channel gamma-2 subunit (Neuronal voltage-gated calcium channel gamma-2 subunit) (Stargazin) (Transmembrane AMPAR regulatory protein gamma-2) (TARP gamma-2)
|
MGLFDRGVQMLLTTVGAFAAFSLMTIAVGTDYWLYSRGVCKTKSVSENETSKKNEEVMTHSGLWRTCCLEGNFKGLCKQIDHFPEDADYEADTAEYFLRAVRASSIFPILSVILLFMGGLCIAASEFYKTRHNIILSAGIFFVSAGLSNIIGIIVYISANAGDPSKSDSKKNSYSYGWSFYFGALSFIIAEMVGVLAVHMFIDRHKQLRATARATDYLQASAITRIPSYRYRYQRRSRSSSRSTEPSHSRDASPVGVKGFNTLPSTEISMYTLSRDPLKAATTPTATYNSDRDNSFLQVHNCIQKDSKDSLHANTANRRTTPV
|
Regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by slowing their rates of activation, deactivation and desensitization. Does not show subunit-specific AMPA receptor regulation and regulates all AMPAR subunits. Thought to stabilize the calcium channel in an inactivated (closed) state (By similarity).
|
O88609
|
LMX1B_MOUSE
|
LIM homeobox transcription factor 1-beta (LIM/homeobox protein 1.2) (LMX-1.2) (LIM/homeobox protein LMX1B)
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MDIATGPESLERCFPRGQTDCAKMLDGIKMEEHALRPGPATLGVLLGSDCPHPAVCEGCQRPISDRFLMRVNESSWHEECLQCAACQQALTTSCYFRDRKLYCKQDYQQLFAAKCSGCMEKIAPTEFVMRALECVYHLGCFCCCVCERQLRKGDEFVLKEGQLLCKGDYEKEKDLLSSVSPDESDSVKSEDEDGDMKPAKGQGSQSKGSGDDGKDPRRPKRPRTILTTQQRRAFKASFEVSSKPCRKVRETLAAETGLSVRVVQVWFQNQRAKMKKLARRHQQQQEQQNSQRLGQEVLSSRMEGMMASYTPLAPPQQQIVAMEQSPYGSSDPFQQGLTPPQMPGNDSIFHDIDSDTSLTSLSDCFLGSSDVGSLQARVGNPIDRLYSMQSSYFAS
|
Transcription factor involved in the regulation of podocyte-expressed genes. Essential for the specification of dorsal limb fate at both the zeugopodal and autopodal levels.
|
O88618
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FTCD_RAT
|
Formimidoyltransferase-cyclodeaminase (58 kDa microtubule-binding protein) (Formiminotransferase-cyclodeaminase) (FTCD) [Includes: Glutamate formimidoyltransferase (EC 2.1.2.5) (Glutamate formiminotransferase) (Glutamate formyltransferase); Formimidoyltetrahydrofolate cyclodeaminase (EC 4.3.1.4) (Formiminotetrahydrofolate cyclodeaminase)]
|
MSQLVECVPNFSEGNNQEVIDAISQAISQTPGCVLLDVDAGPSTNRTVYTFVGQPECVVEGALSAARTASQLIDMRKHKGEHPRMGALDVCPFIPVRGVSMDECVLCAKAFGQRLAEELNVPVYLYGEAAQMPSRQTLPAIRAGEYEALPEKLKQAEWVPDFGPSSFVPSWGATVTGARKFLIAFNINLLSTKEQAHRIALNLREQGRGKDQPGRLKKVQGIGWYLEEKNLAQVSTNLLDFEVTALHTVYEEARREAQELNLPVVGSQLVGLVPLKALLDAAAFYCDKEKLFVLEEEHRIRLVVNRLGLDSLAPFDPKERIIEYLVPDSGPEQSLLDASLRAFVREVGARSAAPGGGSVAAAVAALGAALASMVGQMTYGRRQFDHLDSTMRRLIPPFHAASAQLTSLVDADARAFAACLGAIKLPKNTPEERDRRTCALQEGLRQAVAVPLKLAETVSQLWPALQELAQCGNLSCLSDLQVAAKALETGVFGAYFNVLINLKDMTDDVFKEKTRHRISSLLQEAKTQAALVLGSLEARKE
|
Folate-dependent enzyme, that displays both transferase and deaminase activity. Serves to channel one-carbon units from formiminoglutamate to the folate pool.
|
O88621
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FOXH1_MOUSE
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Forkhead box protein H1 (Forkhead activin signal transducer 1) (Fast-1) (Forkhead activin signal transducer 2) (Fast-2)
|
MASGWDLASTYTPTTPSPQLALAPAQGYLPCMGPRDNSQLRPPEAESLSKTPKRRKKRYLRHDKPPYTYLAMIALVIQAAPFRRLKLAQIIRQVQAVFPFFRDDYEGWKDSIRHNLSSNRCFHKVPKDPAKPQAKGNFWAVDVSLIPAEALRLQNTALCRRWQNRGTHRAFAKDLSPYVLHGQPYQPPSPPPPPREGFSIKSLLGDPGKESTWPQHPGLPGQSTAAQAGTLSKGEEGMGTGPSSSSETPLWPLCSLPGPTIIEGESSQGEVIRPSPVTPDQGSWPLHLLEDSADSRGVPRRGSRASLWGQLPTSYLPIYTPNVVMPLATLPTTSCPQCPSSASPAYWSVGTESQGSQDLLCDLDSLFQGVPPNKSIYDVWVSHPRDLAAPAPGWLLSWYSM
|
Transcriptional activator. Recognizes and binds to the DNA sequence 5'-TGT[GT][GT]ATT-3'. Required for induction of the goosecoid (GSC) promoter by TGF-beta or activin signaling. Forms a transcriptionally active complex containing FOXH1/SMAD2/SMAD4 on a site on the GSC promoter called TARE (TGF-beta/activin response element).
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O88622
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PARG_MOUSE
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Poly(ADP-ribose) glycohydrolase (EC 3.2.1.143)
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MSAGPGWEPCTKRPRWGAAGTSAPTASDSRSFPGRQRRVLDPKDAPVQFRVPPSSPACVSGRAGPHRGNATSFVFKQKTITTWMDTKGPKTAESESKENNNTRIDSMMSSVQKDNFYPHKVEKLENVPQLNLDKSPTEKSSQYLNQQQTASVCKWQNEGKHAEQLLASEPPAGTPLPKQLSNANIGQSPHTDDHSDTDHEEDRDNQQFLTPIKLANTKPTVGDGQARSNCKCSGSRQSVKDCTGCQQEEVDVLPESPLSDVGAEDIGTGPKNDNKLTGQESSLGDSPPFEKESEPESPMDVDNSKNSCQDSEADEETSPVFDEQDDRSSQTANKLSSCQAREADGDLRKRYLTKGSEVRLHFQFEGENNAGTSDLNAKPSGNSSSLNVECRSSKQHGKRDSKITDHFMRISKSEDRRKEQCEVRHQRTERKIPKYIPPNLPPEKKWLGTPIEEMRKMPRCGIHLPSLRPSASHTVTVRVDLLRAGEVPKPFPTHYKDLWDNKHVKMPCSEQNLYPVEDENGERTAGSRWELIQTALLNKFTRPQNLKDAILKYNVAYSKKWDFTALVDFWDKVLEEAEAQHLYQSILPDMVKIALCLPNICTQPIPLLKQKMNHSVTMSQEQIASLLANAFFCTFPRRNAKMKSEYSSYPDINFNRLFEGRSSRKPEKLKTLFCYFRRVTEKKPTGLVTFTRQSLEDFPEWERCEKPLTRLHVTYEGTIEGNGRGMLQVDFANRFVGGGVTGAGLVQEEIRFLINPELIVSRLFTEVLDHNECLIITGTEQYSEYTGYAETYRWARSHEDGSEKDDWQRRCTEIVAIDALHFRRYLDQFVPEKVRRELNKAYCGFLRPGVPSENLSAVATGNWGCGAFGGDARLKALIQILAAAAAERDVVYFTFGDSELMRDIYSMHTFLTERKLDVGKVYKLLLRYYNEECRNCSTPGPDIKLYPFIYHAVESSAETTDMPGQKAGT
|
Poly(ADP-ribose) glycohydrolase that degrades poly(ADP-ribose) by hydrolyzing the ribose-ribose bonds present in poly(ADP-ribose). PARG acts both as an endo- and exoglycosidase, releasing poly(ADP-ribose) of different length as well as ADP-ribose monomers. It is however unable to cleave the ester bond between the terminal ADP-ribose and ADP-ribosylated residues, leaving proteins that are mono-ADP-ribosylated. Poly(ADP-ribose) is synthesized after DNA damage is only present transiently and is rapidly degraded by PARG. Required to prevent detrimental accumulation of poly(ADP-ribose) upon prolonged replicative stress, while it is not required for recovery from transient replicative stress. Responsible for the prevalence of mono-ADP-ribosylated proteins in cells, thanks to its ability to degrade poly(ADP-ribose) without cleaving the terminal protein-ribose bond. Required for retinoid acid-dependent gene transactivation, probably by removing poly(ADP-ribose) from histone demethylase KDM4D, allowing chromatin derepression at RAR-dependent gene promoters. Involved in the synthesis of ATP in the nucleus, together with PARP1, NMNAT1 and NUDT5. Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming.
|
O88623
|
UBP2_MOUSE
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Ubiquitin carboxyl-terminal hydrolase 2 (EC 3.4.19.12) (41 kDa ubiquitin-specific protease) (Deubiquitinating enzyme 2) (Ubiquitin thioesterase 2) (Ubiquitin-specific-processing protease 2)
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MSQLSSTLKRYTESSRYTDAPYAKPGYGTYTPSSYGANLAASFLEKEKLGFKPVSPTSFLPRPRTYGPSSILDCDRGRPLLRSDIIGSSKRSESQTRGNERPSGSGLNGGSGFSYGVSSNSLSYLPMNARDQGVTLSQKKSNSQSDLARDFSSLRTSDGYRTSDGYRTSEGFRIDPGNLGRSPMLARTRKELCALQGLYQAASRSEYLTDYLENYGRKGSAPQVLTQAPPPSRVPEVLSPTYRPSGRYTLWEKSKGQASGPSRSSSPGRDTMNSKSAQGLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLGHTSSAHTALMEEFAKLIQTIWTSSPNDVVSPSEFKTQIQRYAPRFMGYNQQDAQEFLRFLLDGLHNEVNRVAARPKASPETLDHLPDEEKGRQMWRKYLEREDSRIGDLFVGQLKSSLTCTDCGYCSTVFDPFWDLSLPIAKRGYPEVTLMDCMRLFTKEDILDGDEKPTCCRCRARKRCIKKFSVQRFPKILVLHLKRFSESRIRTSKLTTFVNFPLRDLDLREFASENTNHAVYNLYAVSNHSGTTMGGHYTAYCRSPVTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYELASPPSRM
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Hydrolase that deubiquitinates polyubiquitinated target proteins such as MDM2, MDM4 and CCND1 (By similarity). Isoform 1 and isoform 2 possess both ubiquitin-specific peptidase and isopeptidase activities (By similarity). Deubiquitinates MDM2 without reversing MDM2-mediated p53/TP53 ubiquitination and thus indirectly promotes p53/TP53 degradation and limits p53 activity (By similarity). Has no deubiquitinase activity against p53/TP53 (By similarity). Prevents MDM2-mediated degradation of MDM4 (By similarity). Plays a role in the G1/S cell-cycle progression in normal and cancer cells (By similarity). Plays a role in the regulation of myogenic differentiation of embryonic muscle cells (By similarity). Regulates the circadian clock by modulating its intrinsic circadian rhythm and its capacity to respond to external cues. Associates with clock proteins and deubiquitinates core clock component PER1 but does not affect its overall stability. Regulates the nucleocytoplasmic shuttling and nuclear retention of PER1 and its repressive role on the clock transcription factors CLOCK and BMAL1. [Isoform 2]: Circadian clock output effector that regulates Ca(2+) absorption in the small intestine. Probably functions by regulating protein levels of the membrane scaffold protein NHERF4 in a rhythmic manner, and is therefore likely to control Ca(2+) membrane permeability mediated by the Ca(2+) channel TRPV6 in the intestine.
|
O88627
|
S28A2_MOUSE
|
Sodium/nucleoside cotransporter 2 (Concentrative nucleoside transporter 2) (CNT 2) (Na(+)/nucleoside cotransporter 2) (Sodium-coupled nucleoside transporter 2) (Sodium/purine nucleoside cotransporter) (SPNT) (Solute carrier family 28 member 2)
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MEKSKGRKSVSQATVENCMENPGLELMEGGNLEQRYTQEEVTQGHSLEDGLGHSSLWSRRIFQPFTKARSFFERHAGLFRKILLGLLCLAYAAYFLAACILNFQRALALFVITCLVIFILACHFLKKFFPKEQLRCLKPLENTHLNLWAKRVFVGLSVVGLILWLALDTAQRPEQLISFAGICMFILILFACSKHHSAVCWRTVFWGLGLQFIFGILVIRTEPGFNAFQWLGDQIQIFLAYTVEGSSFVFGDTLVQNVFAFQSLPIIIFFGCVMSILYYLGLVQWVIQKVAWFLQITMGTTAAETLAVAGNIFVGMTEAPLLIRPYLADMTISEIHAVMTGGFATIAGTVLGAFISFGIDASSLISASVMAAPCALALSKLVYPEVEESKFKSKEGLKLPRGEERNILEAASNGATDAISLVANVAANLIAFLAVLAFINATLSWLGEMVDIHGLSFQVICSYVLRPMVFMMGVQWADCPLVAEIVGVKFFINEFVAYQQLSQYKNKRLSGVEEWINGEKQWISVKAEIITTFSLCGFANLSSIGITLGGLTSMIPQRKSDLCKIVVRALFTGACVSFISACMAGILYVPRGAETDCVSFLNTNFTNRTYETYVCCRELFQSTSLNGTNMPSFSGPWQDNVSSLRNLASCCDLYTSTVCA
|
Sodium-dependent and purine-selective transporter. Exhibits the transport characteristics of the nucleoside transport system cif or N1 subtype (N1/cif) (selective for purine nucleosides and uridine). Plays a critical role in specific uptake and salvage of purine nucleosides in kidney and other tissues. May contribute to regulate the transport of organic compounds in testes across the blood-testis-barrier (By similarity).
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O88630
|
GOSR1_MOUSE
|
Golgi SNAP receptor complex member 1 (28 kDa Golgi SNARE protein) (28 kDa cis-Golgi SNARE p28) (GOS-28)
|
MAAGTSNYWEDLRKQARQLENELDLKLVSFSKLCTSYSHSGSRDGGRDRYSSDTTPLLNGSSQDRMFETMAIEIEQLLARLTGVNDKMAEYTHSAGVPSLNAALMHTLQRHRDILQDYTHEFHKTKANFTAIRERENLMGSVRKDIESYKSGSGVNNRRTELFLKEHDHLRNSDRLIEETISIAMATKENMTSQRGMLKSIHSKMNTLANRFPAVNSLIQRINLRKRRDSLILGGVIGICTILLLLYAFH
|
Involved in transport from the ER to the Golgi apparatus as well as in intra-Golgi transport. It belongs to a super-family of proteins called t-SNAREs or soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor. May play a protective role against hydrogen peroxide induced cytotoxicity under glutathione depleted conditions in neuronal cells by regulating the intracellular ROS levels via inhibition of p38 MAPK (MAPK11, MAPK12, MAPK13 and MAPK14). Participates in docking and fusion stage of ER to cis-Golgi transport. Plays an important physiological role in VLDL-transport vesicle-Golgi fusion and thus in VLDL delivery to the hepatic cis-Golgi (By similarity).
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O88634
|
PAR4_MOUSE
|
Proteinase-activated receptor 4 (PAR-4) (Coagulation factor II receptor-like 3) (Thrombin receptor-like 3)
|
MCWPLLYPLVLGLSISLAEGIQTPSIYDDVESTRGSHEGPLGPTVELKEPKSSDKPNPRGYPGKFCANDSDTLELPASSQALLLGWVPTRLVPALYGLVVAVGLPANGLALWVLATRVPRLPSTILLMNLAVADLLLALVLPPRLAYHLRGQRWPFGEAACRVATAALYGHMYGSVLLLAAVSLDRYLALVHPLRARALRGQRLTTGLCLVAWLSAATLALPLTLHRQTFRLAGSDRMLCHDALPLTEQTSHWRPAFICLAVLGCFVPLLAMGLCYGATLRALAANGQRYSHALRLTALVLFSAVASFTPSNVLLVLHYSNPSPEAWGNLYGAYVPSLALSTLNSCVDPFIYYYVSHEFREKVRAMLCRQPEASSSSQASREAGSRGTAICSSTLL
|
Receptor for activated thrombin or trypsin coupled to G proteins that stimulate phosphoinositide hydrolysis. May play a role in platelets activation.
|
O88643
|
PAK1_MOUSE
|
Serine/threonine-protein kinase PAK 1 (EC 2.7.11.1) (Alpha-PAK) (CDC42/RAC effector kinase PAK-A) (p21-activated kinase 1) (PAK-1) (p65-PAK)
|
MSNNGVDIQDKPPAPPMRNTSTMIGAGSKDTGTLNHGSKPLPPNPEEKKKKDRFYRSILPGDKTNKKREKERPEISLPSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKSEQKKNPQAVLDVLEFYNSKKTSNSKKYMSFTDKSAEDYNSSNTLNVKTVSETPAVPPVSEDDEDDDDDATPPPVIAPRPEHTKSVYTRSVIEPLPVTPTRDVATSPISPTENNTTPPDALTRNTEKQKKKPKMSDEEILEKLRSIVSVGDPKKKYTPFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDFLQCCLEMDVEKRGSAKELLQHQFLKIAKPLSSLTPLMHAAKEATKNNH
|
Protein kinase involved in intracellular signaling pathways downstream of integrins and receptor-type kinases that plays an important role in cytoskeleton dynamics, in cell adhesion, migration, proliferation, apoptosis, mitosis, and in vesicle-mediated transport processes. Can directly phosphorylate BAD and protects cells against apoptosis. Activated by interaction with CDC42 and RAC1 (By similarity). Functions as GTPase effector that links the Rho-related GTPases CDC42 and RAC1 to the JNK MAP kinase pathway (By similarity). Phosphorylates and activates MAP2K1, and thereby mediates activation of downstream MAP kinases (By similarity). Involved in the reorganization of the actin cytoskeleton, actin stress fibers and of focal adhesion complexes (By similarity). Phosphorylates the tubulin chaperone TBCB and thereby plays a role in the regulation of microtubule biogenesis and organization of the tubulin cytoskeleton. Plays a role in the regulation of insulin secretion in response to elevated glucose levels. Part of a ternary complex that contains PAK1, DVL1 and MUSK that is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ). Activity is inhibited in cells undergoing apoptosis, potentially due to binding of CDC2L1 and CDC2L2 (By similarity). Phosphorylates MYL9/MLC2 (By similarity). Phosphorylates RAF1 at 'Ser-338' and 'Ser-339' resulting in: activation of RAF1, stimulation of RAF1 translocation to mitochondria, phosphorylation of BAD by RAF1, and RAF1 binding to BCL2 (By similarity). Phosphorylates SNAI1 at 'Ser-246' promoting its transcriptional repressor activity by increasing its accumulation in the nucleus (By similarity). In podocytes, promotes NR3C2 nuclear localization (By similarity). Required for atypical chemokine receptor ACKR2-induced phosphorylation of LIMK1 and cofilin (CFL1) and for the up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. In synapses, seems to mediate the regulation of F-actin cluster formation performed by SHANK3, maybe through CFL1 phosphorylation and inactivation (By similarity). Plays a role in RUFY3-mediated facilitating gastric cancer cells migration and invasion (By similarity). In response to DNA damage, phosphorylates MORC2 which activates its ATPase activity and facilitates chromatin remodeling (By similarity). In neurons, plays a crucial role in regulating GABA(A) receptor synaptic stability and hence GABAergic inhibitory synaptic transmission through its role in F-actin stabilization (By similarity). In hippocampal neurons, necessary for the formation of dendritic spines and excitatory synapses this function is dependent on kinase activity and may be exerted by the regulation of actomyosin contractility through the phosphorylation of myosin II regulatory light chain (MLC). Along with GIT1, positively regulates microtubule nucleation during interphase (By similarity). Phosphorylates FXR1, promoting its localization to stress granules and activity (By similarity).
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O88653
|
LTOR3_MOUSE
|
Ragulator complex protein LAMTOR3 (Late endosomal/lysosomal adaptor and MAPK and MTOR activator 3) (MEK-binding partner 1) (Mp1) (Mitogen-activated protein kinase kinase 1-interacting protein 1) (Mitogen-activated protein kinase scaffold protein 1)
|
MADDLKRFLYKKLPSVEGLHAIVVSDRDGVPVIKVANDSAPEHALRPGFLSTFALATDQGSKLGLSKNKSIICYYNTYQVVQFNRLPLVVSFIASSSANTGLIVSLEKELAPLFEELIKVVEVS
|
As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator plays a dual role for the small GTPases Rag (RagA/RRAGA, RagB/RRAGB, RagC/RRAGC and/or RagD/RRAGD): it (1) acts as a guanine nucleotide exchange factor (GEF), activating the small GTPases Rag and (2) mediates recruitment of Rag GTPases to the lysosome membrane (By similarity). Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated (By similarity). Adapter protein that enhances the efficiency of the MAP kinase cascade facilitating the activation of MAPK2.
|
O88658
|
KIF1B_RAT
|
Kinesin-like protein KIF1B
|
MSGASVKVAVRVRPFNSRETSKESKCIIQMQGNSTSIINPKNPKEAPKSFSFDYSYWSHTSPEDPCFASQSRVYNDIGKEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGKQEESQAGIIPQLCEELFEKINDNCNEDMSYSVEVSYMEIYCERVRDLLNPKNKGNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQKKQDPETNLSTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNCTSKSKKKKKTDFIPYRDSVLTWLLRENLGGNSRTAMVAALSPADINYDETLSTLRYADRAKQIKCNAVINEDPNAKLVRELKEEVTRLKDLLRAQGLGDIIDIDPLMDDYSGSGGKYLKDFQNNKHRYLLASENQRPGNFSTASMGSLTSSPSSCSLNSQAGLTSVTSIQERIMSTPGGEEAIERLKESEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGVFSPKKTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFRSERNNTGEVIVTLEPCERSETYVNGKRVAHPVQLRSGNRIIMGKNHVFRFNHPEQARAEREKTPSAETPSEPVDWTFAQRELLEKQGIDMKQEMEKRLQEMEILYKREKEEADLLLEQQRLDYESKLQALQKQVETRSLAAETTEEEEEEEEVPWTQHEFELAQWAFRKWKSHQFTSLRDLLWGNAVYLKEANAISVELKKKVQFQFVLLTDTLYSPVPPELLPTEMGKTHEDRPFPRTVVAVEVQDLKNGATHYWSLDKLKQRLDLMREMYDRAGEVGSNAQDDSETTMTGSDPFYDRFHWFKLVGSSPIFHGCVNERLADRTPSPTFSTADSDITELADEQQDAMEDFDDEAFVDDTGSDAGTEEGSELFSDGHDPFYDRSPWFILVGRAFVYLSNLLYPVPLIHRVAIVSEKGEVRGFLRVAVQAIAADEEAPDYGSGIRQSGTAKISFDNEYFNQSDFPSAAMTRSGLSLEELRIVEGQGQSSEVISPPEEVNRMNDLDLKSGTLLDGKMVMEGFSEEIGNHLKLGSAFTFRVTVLQASGILPEYADIFCQFNFLHRHDEAFSTEPLKNNGRGSPLGFYHVQNIAVEVTESFVDYIKTKPIVFEVFGHYQQHPLHLQGQELNSPPQPSRRFFPPPMPLSRPVPATKLNTMNKTSLGQSMSKYDLLVWFEISELEPTGEYIPAVVDHTAGLPCQGTFLLHQGIQRRITVTIIHEKGSELHWKDVRELVVGRIRNKPEVDEAAVDAILSLNIISAKSLKSSHSSSRTFYRFEAVWDSSLHNSLLLNRVTPYGEKIYMTLSAYLELDHCIQPAVITKDVCMVFYSRDAKISPPRSLRNLFGSGYSKSPDSNRVTGIYELSLCKMADTGSPGMQRRRRKVLDTSVAYVRGEENLAGWRPRGDSLILEHQWELEKLELLHEVEKTRHFLLLRERLGDSIPKSMSDSLSPSLSSGTLSTSTSISSQISTTTFESAITPSESSGYDSADIESLVDREKELATKCLQLLTHTFNREFSQVHGSISDCKLSDISPIGRDPSVSSFSSSTLTPSSTCPSLVDSRSSSMDQKTPEANSRASSPCQEFEQFQIIPTVETPYLARAGKNEFLNLVPDIEEVRAGSVVSKKGYLHFKEPLSSNWAKHFVVVRRPYVFIYNSDKDPVERGIINLSTAQVEYSEDQQAMLKTPNTFAVCTKHRGVLLQALNDKDMNDWLYAFNPLLAGTIRSKLSRRCPSQPKY
|
Motor for anterograde transport of mitochondria. Has a microtubule plus end-directed motility (By similarity). [Isoform 1]: Mediates the transport of synaptic vesicles in neuronal cells.
|
O88662
|
EMP2_MOUSE
|
Epithelial membrane protein 2 (EMP-2) (Protein XMP)
|
MLVILAFIIVFHIVSTALLFISTIDNAWWVGDSFSADLWRVCTNSTNCTEINELTGPEAFEGYSVMQAVQATMILSTILSCISFLIFLLQLFRLKQGERFVLTSIIQLMSCLCVMIGASIYTDRRQDLHQQNRKLYYLLQEGSYGYSFILAWVAFAFTFISGLMYMILRKRK
|
Functions as a key regulator of cell membrane composition by regulating protein surface expression. Also, plays a role in regulation of processes including cell migration, cell proliferation, cell contraction and cell adhesion. Regulates transepithelial migration of neutrophils into the alveolar lumen, potentially via mediation of cell surface expression of adhesion markers and lipid raft formation. Negatively regulates caveolae formation by reducing CAV1 expression and CAV1 amount by increasing lysosomal degradation. Facilitates surface trafficking and the formation of lipid rafts bearing GPI-anchor proteins. Regulates surface expression of MHC1 and ICAM1 proteins increasing susceptibility to T-cell mediated cytotoxicity. Regulates the plasma membrane expression of the integrin heterodimers ITGA6-ITGB1, ITGA5-ITGB3 and ITGA5-ITGB1 resulting in modulation of cell-matrix adhesion. Also regulates many processes through PTK2. Regulates blood vessel endothelial cell migration and angiogenesis by regulating VEGF protein expression through PTK2 activation (By similarity). Regulates cell migration and cell contraction through PTK2 and SRC activation (By similarity). Regulates focal adhesion density, F-actin conformation and cell adhesion capacity through interaction with PTK2 (By similarity). Positively regulates cell proliferation (By similarity). Plays a role during cell death and cell blebbing (By similarity). Promotes angiogenesis and vasculogenesis through induction of VEGFA via a HIF1A-dependent pathway (By similarity). Also plays a role in embryo implantation by regulating surface trafficking of integrin heterodimer ITGA5-ITGB3. Plays a role in placental angiogenesis and uterine natural killer cell regulation at the maternal-fetal placental interface, however not required in the maternal tissues for a viable pregnancy. Involved in the early stages of embryogenic development and cardiogenesis, potentially via regulation of epithelial-mesenchymal transition timing. May play a role in glomerular filtration (By similarity).
|
O88664
|
TAOK1_RAT
|
Serine/threonine-protein kinase TAO1 (EC 2.7.11.1) (Thousand and one amino acid protein 1)
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MPSTNRAGSLKDPEIAELFFKEDPEKLFTDLREIGHGSFGAVYFARDVRTNEVVAIKKMSYSGKQSTEKWQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEYCLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHTMIHRDIKAGNILLTEPGQVKLADFGSASMASPANSFVGTPYWMAPEVILAMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPTLQSNEWSDYFRNFVDSCLQKIPQDRPTSEELLKHMFVLRERPETVLIDLIQRTKDAVRELDNLQYRKMKKLLFQEAHNGPAVEAQEEEEEQDHGGGRTGTVNSVGSNQSIPSMSISASSQSSSVNSLPDASDDKSELDMMEGDHTVMSNSSVIHLKPEEENYQEEGDPRTRASAPQSPPQVSRHKSHYRNREHFATIRTASLVTRQMQEHEQDSELREQMSGYKRMRRQHQKQLMTLENKLKAEMDEHRLRLDKDLETQRNNFAAEMEKLIKKHQASMEKEAKVMANEEKKFQQHIQAQQKKELNSFLESQKREYKLRKEQLKEELNENQSTPKKEKQEWLSKQKENIQHFQAEEEANLLRRQRQYLELECRRFKRRMLLGRHNLEQDLVREELNKRQTQKDLEHAMLLRQHESMQELEFRHLNTIQKMRCELIRLQHQTELTNQLEYNKRRERELRRKHVMEVRQQPKSLKSKELQIKKQFQDTCKIQTRQYKALRNHLLETTPKSEHKAVLKRLKEEQTRKLAILAEQYDHSINEMLSTQALRLDEAQEAECQVLKMQLQQELELLNAYQSKIKMQAEAQHDRELRELEQRVSLRRALLEQKIEEEMLALQNERTERIRSLLERQAREIEAFDSESMRLGFSNMVLSNLSPEAFSHSYPGASSWSHNPTGGSGPHWGHPMGGTPQAWGHPMQGGPQPWGHPSGPMQGVPRGSSIGVRNSPQALRRTASGGRTEQGMSRSTSVTSQISNGSHMSYT
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Serine/threonine-protein kinase involved in various processes such as p38/MAPK14 stress-activated MAPK cascade, DNA damage response and regulation of cytoskeleton stability. Phosphorylates MAP2K3, MAP2K6 and MARK2. Acts as an activator of the p38/MAPK14 stress-activated MAPK cascade by mediating phosphorylation and subsequent activation of the upstream MAP2K3 and MAP2K6 kinases. Involved in G-protein coupled receptor signaling to p38/MAPK14. In response to DNA damage, involved in the G2/M transition DNA damage checkpoint by activating the p38/MAPK14 stress-activated MAPK cascade, probably by mediating phosphorylation of MAP2K3 and MAP2K6. Acts as a regulator of cytoskeleton stability by phosphorylating 'Thr-208' of MARK2, leading to activate MARK2 kinase activity and subsequent phosphorylation and detachment of MAPT/TAU from microtubules. Also acts as a regulator of apoptosis: regulates apoptotic morphological changes, including cell contraction, membrane blebbing and apoptotic bodies formation via activation of the MAPK8/JNK cascade. During fetal development, it plays an essential role in the regulation of neuronal differentiation and migration to the cortical plate (By similarity).
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O88665
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BRD7_MOUSE
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Bromodomain-containing protein 7 (75 kDa bromodomain protein)
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MGKKHKKHKSDRHFYEEYVEKPLKLVLKVGGSEVTELSTGSSGHDSSLFEDRSDHDKHKDRKRKKRKKGEKQAPGEEKGRKRRRVKEDKKKRDRDRAENEVDRDLQCHVPIRLDLPPEKPLTSSLAKQEEVEQTPLQEALNQLMRQLQRKDPSAFFSFPVTDFIAPGYSMIIKHPMDFSTMKEKIKNNDYQSIEELKDNFKLMCTNAMIYNKPETIYYKAAKKLLHSGMKILSQERIQSLKQSIDFMSDLQKTRKQKERTDACQSGEDSGCWQREREDSGDAETQAFRSPAKDNKRKDKDVLEDKWRSSNSEREHEQIERVVQESGGKLTRRLANSQCEFERRKPDGTTTLGLLHPVDPIVGEPGYCPVRLGMTTGRLQSGVNTLQGFKEDKRNRVTPVLYLNYGPYSSYAPHYDSTFANISKDDSDLIYSTYGEDSDLPNNFSISEFLATCQDYPYVMADSLLDVLTKGGHSRSLQDLDMSSPEDEGQTRALDTAKEAEITQIEPTGRLESSSQDRLTALQAVTTFGAPAEVFDSEEAEVFQRKLDETTRLLRELQEAQNERLSTRPPPNMICLLGPSYREMYLAEQVTNNLKELTQQVTPGDVVSIHGVRKAMGISVPSPIVGNSFVDLTGECEEPKETSTAECGPDAS
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Acts both as coactivator and as corepressor. May play a role in chromatin remodeling. Transcriptional corepressor that down-regulates the expression of target genes. Binds to target promoters, leading to increased histone H3 acetylation at 'Lys-9' (H3K9ac). Binds to the ESR1 promoter. Recruits BRCA1 and POU2F1 to the ESR1 promoter. Coactivator for TP53-mediated activation of transcription of a set of target genes. Required for TP53-mediated cell-cycle arrest in response to oncogene activation. Promotes acetylation of TP53 at 'Lys-382', and thereby promotes efficient recruitment of TP53 to target promoters. Inhibits cell cycle progression from G1 to S phase (By similarity). Activator of the Wnt signaling pathway in a DVL1-dependent manner by negatively regulating the GSK3B phosphotransferase activity. Induces dephosphorylation of GSK3B at 'Tyr-216'. Down-regulates TRIM24-mediated activation of transcriptional activation by AR. {ECO:0000250, ECO:0000269|PubMed:12941796, ECO:0000269|PubMed:18809673, ECO:0000269|PubMed:19909775}.
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O88667
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RAD_MOUSE
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GTP-binding protein RAD
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MTLNGGSGASGSRGAGGRERDRRRGSTPWGPAPPLHRRSMPVDERDLQAALAPGSLATTAAGTRTQGQRLDWPEGSSDSLSSGGSGSEEGVYKVLLLGAPGVGKSALARIFGGIEDGPEAEAAGHTYDRSITVDGEEASLLVYDIWEEDGGCWLPGHCMAMGDAYVIVYSITDKGSFEKASELRVQLRRARQTDDVPIILVGNKSDLVRSREVSVDEGRACAVVFDCKFIETSAALHHNVQALFEGVVRQIRLRRDSKEDNARRQAGTRRRESLGKKAKRFLGRIVARNSRKMAFRAKSKSCHDLSVL
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May regulate basal voltage-dependent L-type Ca(2+) currents and be required for beta-adrenergic augmentation of Ca(2+) influx in cardiomyocytes, thereby regulating increases in heart rate and contractile force. May play an important role in cardiac antiarrhythmia via the strong suppression of voltage-dependent L-type Ca(2+) currents. Regulates voltage-gated L-type calcium channel subunit alpha-1C trafficking to the cell membrane. Inhibits cardiac hypertrophy through the calmodulin-dependent kinase II (CaMKII) pathway. Inhibits phosphorylation and activation of CAMK2D (By similarity).
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O88668
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CREG1_MOUSE
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Protein CREG1 (Cellular repressor of E1A-stimulated genes 1)
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MAARAPELARSLLAALLAPALVALLVSPASGRGGRDHGDWDVDRRLPPLPPREDGPRVARFVTHVSDWGSLATISTIKEVRGWPFADIISISDGPPGEGTGEPYMYLSPLQQAVSDLQENPEATLTMSLAQTVYCRNHGFDPQSPLCVHIMMSGTVTKVNKTEEDYARDSLFVRHPEMKHWPSSHNWFFAKLKISRIWVLDYFGGPKVVTPEEYFNVTLQ
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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).
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O88671
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DLL3_RAT
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Delta-like protein 3 (Drosophila Delta homolog 3) (Delta3)
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MVSLQVSSLPQTLILAFLLPQALPAGVFELQIHSFGPGPGPGTPRSPCNARGPCRLFFRVCLKPGVSQEAAESLCALGAALSTSGPVYTEQPGVPAAALSLPDGLVRVPFLDAWPGTFSLIIETWREQLGERAAGPAWNLLARVAGRRRLAAGAPWARDVQRTGAWELHFSYRARCEPPAVGAACARLCRSRSAPSRCGPGLRPCTPFPDECEAPRESLTVCRAGCSPEHGYCEEPDECHCLEGWTGPLCTVPVSTSSCLNSRVSGPAGTGCLLPGPGPCDGNPCANGGSCSETPGSFECACPRGFYGPRCEVSGVTCADGPCFNGGLCVGGEDPDSAYVCHCPPAFQGSNCERRVDRCSLQPCQNGGLCLDLGHALRCRCRAGFAGPRCEHDLDDCAGRACANGGTCVEGGGARRCSCALGFGGRDCRERADPCASRPCAHGGRCYAHFSGLVCACAPGYMGVRCEFAVRPDGADAVPAAPRGLRQADSQRFLLPPALGLLAAAALAGAALLLIHVRRRGPGRDTGTRLLSGTREPSVHTLPDALNNLRLQDGAGDGPTSSADWNHPEDGDSRSIYVIPAPSIYAREA
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Inhibits primary neurogenesis. May be required to divert neurons along a specific differentiation pathway. Plays a role in the formation of somite boundaries during segmentation of the paraxial mesoderm (By similarity).
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O88673
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DGKA_MOUSE
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Diacylglycerol kinase alpha (DAG kinase alpha) (EC 2.7.1.107) (80 kDa diacylglycerol kinase) (Diglyceride kinase alpha) (DGK-alpha)
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MAKEKGLISPEDFAQLQKYIEYSTKRVSDVLKVFDDGEMNRFCQGDAIGYLGFEQFMKMYLEMEEVPHHLCWALFWSFHTSQVAAEKTKSKANVICLSDVYCYFTLLEGGRPEDKLEFTFKLYDMDRNGILDSTEVEKIILQMMRVAEYLDWDVSELRPILQEMMREMDQDGSGSVSLDEWVRAGATTVPLLVLLGMDVTMKDDGNHIWRPKRFTRLVYCNLCEQSISLGKQGLSCNFCKYIVHDHCAMKAQPCEVSTYAKSRKDIGVQSHLWVRGGCHSGRCDRCQKKIRTYHSLTGLHCVWCHLEIHDDCLQAVGPECDCGLLRDHILPPCSIYPSVLVSGQECKHKTTDDTSLCTPEAFRIEPVSNTHPLLVFINLKSGGKQGQSVLWKFQYILNPRQVFDLKDGPEPGLRFFKDVPQFRILVCGGDGTVGWVLETIDKANFATVPPVAVLPLGTGNDLARCLRWGRGYEGENLRKILKDIELSKVVYLDRWFLEVIPQQNGEKSDPVPSQIINNYFSIGVDASIAHRFHLMREKYPEKFNSRMKNKLWYFEFATSESIFSTCKKLEESVTVEICGKLLDLSDLSLEGIAVLNIPSTHGGSNLWGDTKRPHGDTCEINQALGSAAKIITDPDILKTCVPDMSDKRLEVVGIEGAIEMGQIYTRLKSAGHRLAKCSEITFQTTKTLPMQIDGEPWMQAPCTIKITHKNQMPMLMGPPSNSYNFFGFWS
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Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids. Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes. Also plays an important role in the biosynthesis of complex lipids. Can also phosphorylate 1-alkyl-2-acylglycerol in vitro as efficiently as diacylglycerol provided it contains an arachidonoyl group. Also involved in the production of alkyl-lysophosphatidic acid, another bioactive lipid, through the phosphorylation of 1-alkyl-2-acetyl glycerol.
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O88676
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MMP23_MOUSE
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Matrix metalloproteinase-23 (MMP-23) (EC 3.4.24.-) (Cysteine array matrix metalloproteinase) (CA-MMP) (CAMP metalloproteinase) [Cleaved into: Matrix metalloproteinase-23, soluble form]
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MGCRACLRPEASGAVQGRWLGAALSGLCLLSALALLEWLGAPTETAWRAAQGNVDAPNVGSSTAQVPRLLTMSVTRRRRYTLTPARLRWDHFNLTYRVLSFPRNLLSPEETRRGLAAAFRMWSDVSPFSFREVAPERPSDLKIGFYPVNHTDCLVSAVHHCFDGPTGELAHAFFPPHGGIHFDDSEYWVLGPTRYSWKKGVWLTNLVHVAAHEIGHALGLMHSQQDQALMHLNATLRGWKALSQDELWGLHRLYGCLDRIFVCASWARKGFCDVRQRLMKRLCPRSCDFCYEFPFPTVATTTSPTRTKTRLVREGRNMTFHCGQKILHKKGKVYWYKDQEPLEFSYPGYLALGEAQLSIIANAVNEGTYTCVVRRHQRVLSTYSWRVRVRN
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Protease. May regulate the surface expression of some potassium channels by retaining them in the endoplasmic reticulum (By similarity).
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O88689
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PCDA4_MOUSE
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Protocadherin alpha-4 (PCDH-alpha-4)
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MEFSWGSGQESQRLLLSFLLLAIWEAGNSQIHYSIPEEAKHGTFVGRIAQDLGLELTELVPRLFRVASKDRGDLLEVNLQNGILFVNSRIDREELCGRSAECSIHLEVIVDRPLQVFHVEVEVRDINDNPPRFPTTQKNLFIAESRPLDTWFPLEGASDADIGINAVLTYRLSPNDYFSLEKPSNDERVKGLGLVLRKSLDREETPEIILVLTVTDGGKPELTGSVQLLITVLDANDNAPVFDRSLYTVKLPENVPNGTLVVKVNASDLDEGVNGDIMYSFSTDISPNVKYKFHIDPVSGEIIVKGYIDFEECKSYEILIEGIDKGQLPLSGHCKVIVQVEDINDNVPELEFKSLSLPIRENSPVGTVIALISVSDRDTGVNGQVTCSLTSHVPFKLVSTFKNYYSLVLDSALDRETTADYKVVVTARDGGSPSLWATASVSVEVADVNDNAPVFAQPEYTVFVKENNPPGAHIFTVSAMDADAQENALVSYSLVERRVGERLLSSYVSVHAESGKVFALQPLDHEELELLRFQVSARDAGVPALGSNVTLQVFVLDENDNAPTLLEPEAGVSGGIVSRLVSRSVGAGHVVAKVRAVDADSGYNAWLSYELQSSEGNSRSLFRVGLYTGEISTTRILDEADSPRQRLLVLVKDHGDPAMIVTATVLVSLVENGPVPKAPSRVSTSVTHSEASLVDVNVYLIIAICAVSSLLVLTLLLYTALRCSTVPSESVCGPPKPVMVCSSAVGSWSYSQQRRQRVCSGEYPPKTDLMAFSPSLSDSRDREDQLQSAEDSSGKPRQPNPDWRYSASLRAGMHSSVHLEEAGILRAGPGGPDQQWPTVSSATPEPEAGEVSPPVGAGVNSNSWTFKYGPGNPKQSGPGELPDKFIIPGSPAIISIRQEPANNQIDKSDFITFGKKEETKKKKKKKKGNKTQEKKEKGNSTTDNSDQ
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Calcium-dependent cell-adhesion protein involved in cells self-recognition and non-self discrimination (Probable). Thereby, it is involved in the establishment and maintenance of specific neuronal connections in the brain.
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O88693
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CEGT_MOUSE
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Ceramide glucosyltransferase (EC 2.4.1.80) (GLCT-1) (Glucosylceramide synthase) (GCS) (Glycosylceramide synthase) (UDP-glucose ceramide glucosyltransferase) (UDP-glucose:N-acylsphingosine D-glucosyltransferase)
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MALLDLAQEGMALFGFVLFVVLWLMHFMSIIYTRLHLNKKATDKQPYSKLPGVSLLKPLKGVDPNLINNLETFFELDYPKYEVLLCVQDHDDPAIDVCKKLLGKYPNVDARLFIGGKKVGINPKINNLMPAYEVAKYDLIWICDSGIRVIPDTLTDMVNQMTEKVGLVHGLPYVADRQGFAATLEQVYFGTSHPRSYISANVTGFKCVTGMSCLMRKDVLDQAGGLIAFAQYIAEDYFMAKAIADRGWRFSMSTQVAMQNSGSYSISQFQSRMIRWTKLRINMLPATIICEPISECFVASLIIGWAAHHVFRWDIMVFFMCHCLAWFIFDYIQLRGVQGGTLCFSKLDYAVAWFIRESMTIYIFLSALWDPTISWRTGRYRLRCGGTAEEILDV
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Participates in the initial step of the glucosylceramide-based glycosphingolipid/GSL synthetic pathway at the cytosolic surface of the Golgi. Catalyzes the transfer of glucose from UDP-glucose to ceramide to produce glucosylceramide/GlcCer (such as beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine). Glucosylceramide is the core component of glycosphingolipids/GSLs, amphipathic molecules consisting of a ceramide lipid moiety embedded in the outer leaflet of the membrane, linked to one of hundreds of different externally oriented oligosaccharide structures. Glycosphingolipids are essential components of membrane microdomains that mediate membrane trafficking and signal transduction. They are implicated in many fundamental cellular processes, including growth, differentiation, migration, morphogenesis, cell-to-cell and cell-to-matrix interactions. They are required for instance in the proper development and functioning of the nervous system. As an example of their role in signal transduction, they regulate the leptin receptor/LEPR in the leptin-mediated signaling pathway. They also play an important role in the establishment of the skin barrier regulating keratinocyte differentiation and the proper assembly of the cornified envelope. The biosynthesis of GSLs is also required for the proper intestinal endocytic uptake of nutritional lipids. Catalyzes the synthesis of xylosylceramide/XylCer (such as beta-D-xylosyl-(1<->1')-N-acylsphing-4-enine) using UDP-Xyl as xylose donor.
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O88696
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CLPP_MOUSE
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ATP-dependent Clp protease proteolytic subunit, mitochondrial (EC 3.4.21.92) (Endopeptidase Clp)
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MWPRVLLGEARVAVDGCRALLSRLAVHFSPPWTAVSCSPLRRSLHGTATRAFPLIPIVVEQTGRGERAYDIYSRLLRERIVCVMGPIDDSVASLVIAQLLFLQSESNKKPIHMYINSPGGVVTAGLAIYDTMQYILNPICTWCVGQAASMGSLLLAAGSPGMRHSLPNSRIMIHQPSGGARGQATDIAIQAEEIMKLKKQLYNIYAKHTKQSLQVIESAMERDRYMSPMEAQEFGILDKVLVHPPQDGEDEPELVQKETATAPTDPPAPTST
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Protease component of the Clp complex that cleaves peptides and various proteins in an ATP-dependent process. Has low peptidase activity in the absence of CLPX. The Clp complex can degrade CSN1S1, CSN2 and CSN3, as well as synthetic peptides (in vitro) and may be responsible for a fairly general and central housekeeping function rather than for the degradation of specific substrates. Cleaves PINK1 in the mitochondrion.
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O88697
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STK16_MOUSE
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Serine/threonine-protein kinase 16 (EC 2.7.11.1) (Embryo-derived protein kinase) (Edpk) (Myristoylated and palmitoylated serine/threonine-protein kinase) (MPSK) (Protein kinase Krct) (Protein kinase PKL12) (TGF-beta-stimulated factor 1) (TSF-1) (Tyrosine-protein kinase STK16) (EC 2.7.10.2)
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MGHALCVCSRGTVIIDNKRYLFVQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDQEEAQREAEMHRLFQHPNILRLMAYSLKERGAKHEAWLLLPFFKKGTLWNEIERLKDQGSFLTEDQILPLLLGISRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIQVEGSRQALALQDWAAQRCTISYRAPELFSVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDMVFQKGDSVALAVQNELSIPQSPRHSSALRQLLSSMMTVDPQQRPHIPVLLSQLEALQPPAPGQHTTQI
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Membrane-associated protein kinase that phosphorylates on serine and threonine residues. In vitro substrates include DRG1, ENO1 and EIF4EBP1. Also autophosphorylates (By similarity). May be involved in secretory vesicle trafficking or intracellular signaling. May have a role in regulating stromal-epithelial interactions that occur during ductal morphogenesis in the mammary gland. May be involved in TGF-beta signaling. Able to autophosphorylate on Tyr residue it is however unclear whether it has tyrosine-protein kinase toward other proteins. {ECO:0000250, ECO:0000269|PubMed:9878782}.
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O88700
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BLM_MOUSE
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RecQ-like DNA helicase BLM (EC 3.6.4.12) (Bloom syndrome protein homolog) (mBLM) (RecQ helicase homolog)
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MAAVPLNNLQEQLQRHSARKLNNQPSLSKPKSLGFTFKKKTSEGDVSVTSVSVVKTPALSDKDVNVSEAFSFTESPLHKPKQQAKIEGFFKHFPGRQQSKGTCSEPSLPATVQTAQDTLCTTPKTPTAKKLPVAVFKKLEFSSSADSLSDWADMDDFDMSASDAFASLAKNPATRVSTAQKMKKTKRNFFKPPPRKANAVKTDLTPPSPECLQVDLTKESEEEEEEEEEAEGADCLSRDVICIDNDSASEELTEKDTQESQSLKAHLGAERGDSEKKSHEDEAVFHSVQNTEYFEHNDNDYDIDFVPPSPEEIISTASSSLKCSSMLKDLDDSDKEKGILSTSEELLSKPEEMTTHKSDAGTSKDCDAQQIRIQQQLIHVMEHICKLVDTVPTDELEALNCGTELLQQRNIRRKLLAEAGFNGNDVRLLGSLWRHRPDSLDNTVQGDSCPVGHPNKELNSPYLLSHSPSTEECLPTTTPGKTGFSATPKNLFERPLLNSHLQKSFVSSNWAETPRMENRNESTDFPGSVLTSTTVKAQSKQAASGWNVERHGQASYDIDNFNIDDFDDDDDDDDWENIMHNFPASKSSTATYPPIKEGGPVKSLSERISSAKAKFLPVVSTAQNTNLSESIQNCSDKLAQNLSSKNPKHEHFQSLNFPHTKEMMKIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTIVISPLRSLIVDQVQKLTSFDIPATYLTGDKTDSEAANIYLQLSKKDPIIKLLYVTPEKVCASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRQDYKRMNMLRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFNRHNLKYYVLPKKPKKVAFDCLEWIRKHHPYDSGIIYCLSRRECDTMADTLQREGLAALAYHAGLSDSARDEVQHKWINQDNCQVICATIAFGMGIDKPDVRFVIHASLPKSMEGYYQESGRAGRDGEISHCVLFYTYHDVTRLKRLIMMEKDGNYHTKETHVNNLYSMVHYCENITECRRIQLLAYFGEKGFNPDFCKKYPDVSCDNCCKTKDYKTKDVTDDVKNIIRFVQEHSSSPGTRNIGPAGRFTLNMLVDIFLGSKSAKVKSGIFGKGTTYSRHNAERLFKKLILDKILDEDLYINANDQPIAYVMLGTKAHSVLSGHLKVDFMETENSSSIKKQKALVAKVSQREEVVKKCLGELTEVCKLLGKVFGVHYFNIFNTATLKKLAESLSSDPEVLLQIDGVTEDKLEKYGAEVIPVLQKYSEWTVPAEDGSPGARGAPEDTEEEEEEAPVSSHYFANQTRNERKRKKMSATHKPKRRRTSYGGFRAKGGSTTCRKTTSKSKFYGVTGSRSASCASQATSSASRKLGIMAPPKPVNRTFLRPSYAFS
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ATP-dependent DNA helicase that unwinds single- and double-stranded DNA in a 3'-5' direction. Participates in DNA replication and repair (By similarity). Involved in 5'-end resection of DNA during double-strand break (DSB) repair: unwinds DNA and recruits DNA2 which mediates the cleavage of 5'-ssDNA. Negatively regulates sister chromatid exchange (SCE). Stimulates DNA 4-way junction branch migration and DNA Holliday junction dissolution. Binds single-stranded DNA (ssDNA), forked duplex DNA and DNA Holliday junction (By similarity). Recruited by the KHDC3-OOEP scaffold to DNA replication forks where it is retained by TRIM25 ubiquitination, it thereby promotes the restart of stalled replication forks.
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O88703
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HCN2_MOUSE
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Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 (Brain cyclic nucleotide-gated channel 2) (BCNG-2) (Hyperpolarization-activated cation channel 1) (HAC-1)
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MDARGGGGRPGDSPGTTPAPGPPPPPPPPAPPQPQPPPAPPPNPTTPSHPESADEPGPRARLCSRDSACTPGAAKGGANGECGRGEPQCSPEGPARGPKVSFSCRGAASGPSAAEEAGSEEAGPAGEPRGSQASFLQRQFGALLQPGVNKFSLRMFGSQKAVEREQERVKSAGAWIIHPYSDFRFYWDFTMLLFMVGNLIIIPVGITFFKDETTAPWIVFNVVSDTFFLMDLVLNFRTGIVIEDNTEIILDPEKIKKKYLRTWFVVDFVSSIPVDYIFLIVEKGIDSEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVMRICNLISMMLLLCHWDGCLQFLVPMLQDFPSDCWVSINNMVNHSWSELYSFALFKAMSHMLCIGYGRQAPESMTDIWLTMLSMIVGATCYAMFIGHATALIQSLDSSRRQYQEKYKQVEQYMSFHKLPADFRQKIHDYYEHRYQGKMFDEDSILGELNGPLREEIVNFNCRKLVASMPLFANADPNFVTAMLTKLKFEVFQPGDYIIREGTIGKKMYFIQHGVVSVLTKGNKEMKLSDGSYFGEICLLTRGRRTASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAFETVAIDRLDRIGKKNSILLHKVQHDLSSGVFNNQENAIIQEIVKYDREMVQQAELGQRVGLFPPPPPPQVTSAIATLQQAVAMSFCPQVARPLVGPLALGSPRLVRRAPPGPLPPAASPGPPAASPPAAPSSPRAPRTSPYGVPGSPATRVGPALPARRLSRASRPLSASQPSLPHGVPAPSPAASARPASSSTPRLGPAPTARTAAPSPDRRDSASPGAASGLDPLDSARSRLSSNL
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Hyperpolarization-activated ion channel exhibiting weak selectivity for potassium over sodium ions. Contributes to the native pacemaker currents in heart (If) and in neurons (Ih). Can also transport ammonium in the distal nephron. Produces a large instantaneous current.
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O88704
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HCN1_MOUSE
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Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1 (Brain cyclic nucleotide-gated channel 1) (BCNG-1) (Hyperpolarization-activated cation channel 2) (HAC-2)
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MEGGGKPNSASNSRDDGNSVFPSKAPATGPVAADKRLGTPPGGGAAGKEHGNSVCFKVDGGGGEEPAGSFEDAEGPRRQYGFMQRQFTSMLQPGVNKFSLRMFGSQKAVEKEQERVKTAGFWIIHPYSDFRFYWDLIMLIMMVGNLVIIPVGITFFTEQTTTPWIIFNVASDTVFLLDLIMNFRTGTVNEDSSEIILDPKVIKMNYLKSWFVVDFISSIPVDYIFLIVEKGMDSEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVVRIFNLIGMMLLLCHWDGCLQFLVPLLQDFPPDCWVSLNEMVNDSWGKQYSYALFKAMSHMLCIGYGAQAPVSMSDLWITMLSMIVGATCYAMFVGHATALIQSLDSSRRQYQEKYKQVEQYMSFHKLPADMRQKIHDYYEHRYQGKIFDEENILSELNDPLREEIVNFNCRKLVATMPLFANADPNFVTAMLSKLRFEVFQPGDYIIREGAVGKKMYFIQHGVAGVITKSSKEMKLTDGSYFGEICLLTKGRRTASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAFETVAIDRLDRIGKKNSILLQKFQKDLNTGVFNNQENEILKQIVKHDREMVQAIPPINYPQMTALNCTSSTTTPTSRMRTQSPPVYTATSLSHSNLHSPSPSTQTPQPSAILSPCSYTTAVCSPPIQSPLATRTFHYASPTASQLSLMQQPQQQLPQSQVQQTQTQTQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQPQTPGSSTPKNEVHKSTQALHNTNLTKEVRPLSASQPSLPHEVSTLISRPHPTVGESLASIPQPVAAVHSTGLQAGSRSTVPQRVTLFRQMSSGAIPPNRGVPPAPPPPAAVQRESPSVLNTDPDAEKPRFASNL
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Hyperpolarization-activated ion channel exhibiting weak selectivity for potassium over sodium ions. Contributes to the native pacemaker currents in heart (If) and in neurons (Ih). May mediate responses to sour stimuli.
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O88705
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HCN3_MOUSE
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Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 3 (Hyperpolarization-activated cation channel 3) (HAC-3)
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MEEEARPAAGAGEAATPARETPPAAPAQARAASGGVPESAPEPKRRQLGTLLQPTVNKFSLRVFGSHKAVEIEQERVKSAGAWIIHPYSDFRFYWDLIMLLLMVGNLIVLPVGITFFKEENSPPWIVFNVLSDTFFLLDLVLNFRTGIVVEEGAEILLAPRAIRTRYLRTWFLVDLISSIPVDYIFLVVELEPRLDAEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVVRIFNLIGMMLLLCHWDGCLQFLVPMLQDFPSDCWVSMNRMVNHSWGRQYSHALFKAMSHMLCIGYGQQAPVGMPDVWLTMLSMIVGATCYAMFIGHATALIQSLDSSRRQYQEKYKQVEQYMSFHKLPADTRQRIHEYYEHRYQGKMFDEESILGELSEPLREEIINFTCRGLVAHMPLFAHADPSFVTAVLTKLRFEVFQPGDLVVREGSVGRKMYFIQHGLLSVLARGARDTRLTDGSYFGEICLLTRGRRTASVRADTYCRLYSLSVDHFNAVLEEFPMMRRAFETVAMDRLRRIGKKNSILQRKRSEPSPGSSGGVMEQHLVQHDRDMARGVRGLAPGTGARLSGKPVLWEPLVHAPLQAAAVTSNVAIALTHQRGPLPLSPDSPATLLARSARRSAGSPASPLVPVRAGPLLARGPWASTSRLPAPPARTLHASLSRTGRSQVSLLGPPPGGGARRLGPRGRPLSASQPSLPQRATGDGSPRRKGSGSERLPPSGLLAKPPGTVQPPRSSVPEPVTPRGPQISANM
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Hyperpolarization-activated potassium channel. May also facilitate the permeation of sodium ions.
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O88708
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ORC4_MOUSE
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Origin recognition complex subunit 4
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MSSRKTKSNAHAECLSQVQRILRERFCHHSPHSNLFGVQVQYKHLIELLKRTAIYGESNSVLIVGPRGSGKTTLLNHALKELMEIEVSENVIQVHLNGLLQTNEKIALKEITRQLNLDNVVEDKVFGSFAENLSFLLEALQKGDRTSSCPVIFILDEFDIFAHQKNQTLLYNLFDISQSAQTPVAVIGLTCRLDILELLEKRVKSRFSHRQIHLMNSFDFPQYLKIFKEQLSLPAEFPDKAFAERWNENVHCLSEDSTVLEVLQKHFSVNKNLQSLHMLLMLALNRVTVSHPFMTSADLMEAQHMCSLDSKANIVHGLSVLEICLIIAMKHLNDIYEEEPFNFQMVYNEFQKFIQRKAHSVYNFEKPVVMKAFEHLQQLELIKPVERTSVNSQREYQLVKLLLDNTQIMNALQKYSNCPTDVRQWATSSLSWL
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Binds histone H3 and H4 trimethylation marks H3K9me3, H3K27me3 and H4K20me3 (By similarity). Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication.
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O88712
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CTBP1_MOUSE
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C-terminal-binding protein 1 (CtBP1) (EC 1.1.1.-)
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MGSSHLLNKGLPLGVRPPIMNGPMHPRPLVALLDGRDCTVEMPILKDVATVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRTTWLHQALREGTRVQSVEQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGIERALGLQRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPDSLKNCVNKDHLTAATHWASMDPAVVHPELNGAAYSRYPPGVVSVAPTGIPAAVEGIVPSAMSLSHGLPPVAHPPHAPSPGQTVKPEADRDHTSDQL
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Corepressor targeting diverse transcription regulators such as GLIS2 or BCL6. Has dehydrogenase activity. Involved in controlling the equilibrium between tubular and stacked structures in the Golgi complex. Functions in brown adipose tissue (BAT) differentiation.
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O88713
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KLRG1_MOUSE
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Killer cell lectin-like receptor subfamily G member 1 (Mast cell function-associated antigen 2F1)
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MADSSIYSTLELPEAPQVQDESRWKLKAVLHRPHLSRFAMVALGLLTVILMSLLMYQRILCCGSKDSTCSHCPSCPILWTRNGSHCYYFSMEKKDWNSSLKFCADKGSHLLTFPDNQGVKLFGEYLGQDFYWIGLRNIDGWRWEGGPALSLRILTNSLIQRCGAIHRNGLQASSCEVALQWICKKVLY
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Plays an inhibitory role on natural killer (NK) cells and T-cell functions upon binding to their non-MHC ligands. May mediate missing self recognition by binding to a highly conserved site on classical cadherins, enabling it to monitor expression of E-cadherin/CDH1, N-cadherin/CDH2 and R-cadherin/CDH4 on target cells.
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O88721
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V2R_MOUSE
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Vasopressin V2 receptor (V2R) (AVPR V2) (Antidiuretic hormone receptor) (Renal-type arginine vasopressin receptor)
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MILVSTTSAVPGALSSPSSPSNSSQEELLDDRDPLLVRAELALLSTIFVAVALSNGLVLGALIRRGRRGRWAPMHVFISHLCLADLAVALFQVLPQLAWDATDRFHGPDALCRAVKYLQMVGMYASSYMILAMTLDRHRAICRPMLAYRHGGGARWNRPVLVAWAFSLLLSLPQLFIFAQRDVGNGSGVFDCWARFAEPWGLRAYVTWIALMVFVAPALGIAACQVLIFREIHASLVPGPSERAGRRRRGHRTGSPSEGAHVSAAMAKTVRMTLVIVIVYVLCWAPFFLVQLWAAWDPEAPLERPPFVLLMLLASLNSCTNPWIYASFSSSVSSELRSLLCCAQRHTTHSLGPQDESCATASSSLMKDTPS
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Receptor for arginine vasopressin. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Involved in renal water reabsorption (By similarity).
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O88728
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IFM5_MOUSE
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Interferon-induced transmembrane protein 5 (Bone-restricted interferon-induced transmembrane protein-like protein) (Bril) (Dispanin subfamily A member 1) (DSPA1) (Fragilis family member 4)
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MDTSYPREDPRAPSSRKADAAAHTALSMGTPGPTPRDHMLWSVFSTMYLNLCCLGFLALVHSVKARDQKMAGNLEAARQYGSKAKCYNILAAMWTLVPPLLLLGLVVTGALHLSKLAKDSAAFFSTKFDEEDYN
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Required for normal bone mineralization.
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O88735
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MAP7_MOUSE
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Ensconsin (Epithelial microtubule-associated protein of 115 kDa) (E-MAP-115) (Microtubule-associated protein 7) (MAP-7)
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MAEQGAGGDGHRGGDGATHSDPASDGYKVQEKRTAPSRPTSTVSGQTSNHSGNKPDPPPVLRVDDRQRLARERREEREKQLAARETVWLEREERARQHYERHLEARKKKLEDQRLKEERRRAAVEEKRRQRLEEDKERHEAVVRRTMERSQKPRQKSNRWSWGSPLHGSSSIHSGDPDRRSVSTMNLSKHVDPVISKRLSSSSATLLNSPDRARRLQLSPWESSVVSRLLTPTHSFLARSKSTAALSGDTASCSPIIMPFKAAHSRNPVDRPKLFVTPPEGSARRRTIHGLASHKREREREHVPFHVSPGARRTLSPSNLKARSPAPARLWLPSKSMPHLPGTPRPASSLPPGSVRAASAQAPSSSPGNIRPFKREVKVEPEKKDPLPAVKSRVPLVKVEEVTVEEGTPVKPPEPAAPASAPIATPAPAPATDPAPVPAPSSTVTVGVVPKTSAGTTDPEEATRLLAEKRRLAREQREKEERERKEKEELERQKIEELARRVAEERSRREEEARRLEEEQAREKEELALRLAEEERERWEREEVERVQKQKEEEARAREEAERARQEREKHFQKEEQERLERKKRLEEIMRRTRRTETADKKTTEQRNGDIAKGVLTGEPEVPALPCMASSGNGESAESPHGVALQQSEVTTESSPDLEKQPNENGMSIQNENFEEVINLPVGSKASRLDVTNENPEIPLKPILAFNDEGTLGPLPQVDGVQTQQTAEVI
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Microtubule-stabilizing protein that may play an important role during reorganization of microtubules during polarization and differentiation of epithelial cells. Associates with microtubules in a dynamic manner. May play a role in the formation of intercellular contacts. Colocalization with TRPV4 results in the redistribution of TRPV4 toward the membrane and may link cytoskeletal microfilaments.
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O88736
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DHB7_MOUSE
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3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7 (17-beta-hydroxysteroid dehydrogenase 7) (17-beta-HSD 7) (3-keto-steroid reductase) (EC 1.1.1.270) (Dihydrotestosterone oxidoreductase) (EC 1.1.1.210) (Estradiol 17-beta-dehydrogenase 7) (EC 1.1.1.62)
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MRKVVLITGASSGIGLALCGRLLAEDDDLHLCLACRNLSKARAVRDTLLASHPSAEVSIVQMDVSSLQSVVRGAEEVKQKFQRLDYLYLNAGILPNPQFNLKAFFCGIFSRNVIHMFTTAEGILTQNDSVTADGLQEVFETNLFGHFILIRELEPLLCHADNPSQLIWTSSRNAKKANFSLEDIQHSKGPEPYSSSKYATDLLNVALNRNFNQKGLYSSVMCPGVVMTNMTYGILPPFIWTLLLPIMWLLRFFVNALTVTPYNGAEALVWLFHQKPESLNPLTKYASATSGFGTNYVTGQKMDIDEDTAEKFYEVLLELEKRVRTTVQKSDHPS
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Bifunctional enzyme involved in steroid-hormone metabolism and cholesterol biosynthesis. Catalyzes the NADP(H)-dependent reduction of estrogens and androgens and regulates the biological potency of these steroids. Converts estrone (E1)to a more potent estrogen, 17beta-estradiol (E2). Converts moderately dihydrotestosterone (DHT) to their inactive forms 5a-androstane-3beta,17b-diol and 5alpha-androstane-3alpha,17beta-diol. Does not metabolize progesterone. Additionally, participates in the post-squalene cholesterol biosynthesis, as a 3-ketosteroid reductase.
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O88737
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BSN_MOUSE
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Protein bassoon
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MGNEASLEGGAGEGPLPPGGSGLGPGPGAGKPPSALAGGGQLPVAGAARAAGPPTPGLGPVPGPGPGPGPGSVPRRLDPKEPLGSQRTTSPTPKQASATAPGRESPRETRAQGPSGQEAESPRRTLQVDSRTQRSGRSPSVSPDRGSTPTSPYSVPQIAPLPSSTLCPICKTSDLTSTPSQPNFNTCTQCHNKVCNQCGFNPNPHLTQVKEWLCLNCQMQRALGMDMTTAPRSKSQQQLHSPALSPAHSPAKQPLGKPEQERSPRGPGATQSGPRQAEAARATSVPGPTQATAPPEVGRVSPQPPLSTKPSTAEPRPPAGEAQGKSATTVPSGLGAGEQTQEGLTGKLFGLGASLLTQASTLMSVQPEADTQGQPSPSKGQPKIVFSDASKEAGPRPPGSGPGPGPTPGAKTEPGARMGPGSGPGALAKTGGTASPKHGRAEHQAASKAAAKPKTMPKERASACPLCQAELNMGSRGPANYNTCTACKLQVCNLCGFNPTPHLVEKTEWLCLNCQTKRLLEGSLGEPAPLPLPTPQQPPAGVPHRAAGAAPLKQKGPQGLGQPSGSLPAKASPQATKASPQATKASPQATKASPQTTKASPQAKPLRATEPSKTSSSAQEKKTVTSAKAEPVPKPPPETTVPPGTPKAKSGVKRTDPATPVVKPVPEAPKGGEAEEPVPKPYSQDLSRSPQSLSDTGYSSDGVSSSQSEITGVVQQEVEQLDSAGVTGPRPPSPSELHKVGSSLRPSLEAQAVAPSAEWSKPPRSSSSAVEDQKRRPHSLSITPEAFDSDEELGDILEEDDSLAWGRQREQQDTAESSDDFGSQLRHDYVEDSSEGGLSPLPPQPPARADMTDEEFMRRQILEMSAEEDNLEEDDTAVSGRGLAKHSAQKASARPRPESSQEPKRRLPHNATTGYEELLSEAGPAEPTDSSGALQGGLRRFKTIELNSTGSYGHELDLGQGPDPNLDREPELEMESLTGSPEDRSRGEHSSTLPASTPSYTSGTSPTSLSSLEEDSDSSPSRRQRLEEAKQQRKARHRSHGPLLPTIEDSSEEEELREEEELLREQEKMREVEQQRIRSTARKTRRDKEELRAQRRRERSKTPPSNLSPIEDASPTEELRQAAEMEELHRSSCSEYSPSPSLDSEAETLDGGPTRLYKSGSEYNLPAFMSLYSPTETPSGSSTTPSSGRPLKSAEEAYEDMMRKAEMLQRQQGQVAGARGPHGGPSQPTGPRSQGSFEYQDTQDHDYGGRASQPVAESTPAGLGAAVYEEILQTSQSIARMRQASSRDLGFTEDKKKEKQFLNAESAYMDPMKQNGGPLTPGTSPTQLAAPVSFSTSTSSDSSGGRVIPDVRVTQHFAKEPQDPLKLHSSPVSSTLTSKEVGMTFSQGPGSPATTASPTRGYMTPTSPAGSERSPSTSSTIHSYGQPPTTANYGSQTEELPHAPSGPPGSGRAPREKPLSGGDSEVGAPQPSRGYSYFTGSSPPLSPSTPSESPTFSPGKLGPRATAEFSTQTPSLTLSSDIPRSPGPPSPMVAQGTQTPHRPSTPRLVWQQSSQEAPIMVITLASDASSQTRMVHASASTSPLCSPTDSQPTSHSYSQTTPPSASQMPSEPAGPPGFPRAPSAGTDGPLALYGWGALPAENISLCRISSVPGTSRVEPGPRPPGTAVVDLRTAVKPTPIILTDQGMDLTSLAVEARKYGLALDPVSGRQSTAVQPLVINLNAQEQTHTFLATATTVSITMASSVLMAQQKQPVVYGDPFQSRLDFGQGSGSPVCLAQVKQVEQAVQTAPYRGGPRGRPREAKFARYNLPNQVTPLARRDILITQMGTAQGVGLKPGPVPEPGAEPHRATPAELRSHAPPGTRKPHTVVVQMGEGTAGTVTTLLPEEPAGALDLTGMRPESQLACCDMVYKFPFGSSCTGTFHPAPSAPDKSVTDTALPGQSSGPFYSPRDPEPPEPLTFRTQGVVGPGPHEEQRPYPQGLPGRLYSSMSDTNLAEAGLNYHAQRLGQLFQGPGRDSAVDLSSLKHSYSLGFADGRYLGQGLQYGSFTDLRHPTDLLSHPLPLRRYSSVSNIYSDHRYGPRGDAVGFQEASLAQYSATTAREISRMCAALNSMDQYGGRHGSGSGGPDLVQYQPQHGPGLSAPQGLAPLRSGLLGNPTYPEGQPSPGNLAQYGPAASQATAVRQLLPSTATVRAADGMIYSTINTPIAATLPITTQPASVLRPMVRGGMYRPYVSGGVTAVPLTSLTRVPMIAPRVPLGPAGLYRYPAPRFPIASSVPPAEGPVYLGKPAAAKASGAGGPPRPELPAGVAREEPFSTTAPAVIKEAPVAPAPGPAPAPPPGQKPAGEAVAGSGSGVLSRPASEKEEASQEDRQRKQQEQLLQLERERVELEKLRQLRLQEELERERVELQRHREEEQLLVQRELQELQTIKQHVLQQQQEERQAQFALQREQLAQQRLQLEQIQQLQQQLQLQLEEQKQRQKAPFPATCEAPSRGPPPAATELAQNGQYWPPLTHAAFIAVAGTEGPGQPREPVLHRGLPSSASDMSLQTEEQWEAGRSGIKKRHSMPRLRDACEPESGPDPSTVRRIADSSVQTDDEEGEGRYLVTRRRRTRRSADCSVQTDDEDNADWEQPVRRRRSRLSRHSDSGSDSKHDATASSSTTAAATARAMSSVGIQTISDCSVQTEPEQLPRVSPAIHITAATDPKVEIVRYISAPEKTGRGESLACQTEPDGQAQGVAGPQLIGPTAISPYLPGIQIVTPGALGRFEKKKPDPLEIGYQAHLPPESLSQLVSRQPPKSPQVLYSPVSPLSPHRLLDTSFASSERLNKAHVSPQKQFIADSTLRQQTLPRPMKTLQRSLSDPKPLSPTAEESAKERFSLYQHQGGLGSQVSALPPNGLVRKVKRTLPSPPPEEAHLPLAGQVPSQLYAASLLQRGLAGPTTVPATKASLLRELDRDLRLVEHESTKLRKKQAELDEEEKEIDAKLKYLELGITQRKESLAKDRGGRDYPPLRGLGEHRDYLSDSELNQLRLQGCTTPAGQYVDYPASAAVPATPSGPTAFQQPRFPPAAPQYTAGSSGPTQNGFPAHQAPTYTGPSTYPAPTYPPGTGYPAEPGLPSQPAFHPTGHYAAPTPMPTTQSAPFPVQADSRAAHQKPRQTSLADLEQKVPTNYEVIGSPAVTMSSAPPETGYSGPAVSGSYEQGKAPEHPRGSDRSSVSQSPAPTYPSDSHYTSLEQNVPRNYVMIDDISELTKDSTPTASESQRLEPLGPGGVSGRPGKDPGEPAVLEGPTLPCCYGRGEEESEEDSYDPRGKSGHHRSMESNGRPSTHYYGDSDYRHGARADKYGPGPMGPKHPSKSLAPAAISSKRSKHRKQGMEQKISKFSPIEEAKDVESDLASYPPPTVSSSLTSRGRKFQDEITYGLKKNVYEQQRYYGVSSRDAAEEDERMYGSSSRSRMASAYSGEKLSSHDYSSRGKGYERERDTAERLQKAGSKPSSLSMAHGRARPPMRSQASEEESPVSPLGRPRPAGGALPPGDTCPQFCSSHSMPDVQEHVKDGPRAHAYKREEGYMLDDSHCVVSDSEAYHLGQEETDWFDKPRDARSDRFRHHGGHTVSSSQKRGPARHSYHDYDEPPEEGLWPHDEGGPGRHTSAKEHRHHSDHGRHSGRHAGEEPGRRAAKPHARDMGRHEARPHPQASPAPAMQKKGQPGYPSSADYSQSSRAPSAYHHASESKKGSRQAHTGPSALQPKADTQAQPQMQGRQAAPGPQQSQPPSSRQTPSGTASRQPQTQQQQQQQQQQQGLGQQAPQQAPSQARLQPQSQPTTRGTAPAASQPAGKPQPGPTTAPGPQPAGPPRAEQASSSKPPAAKAPQQGRAPQAQTTPGPGPAGAKPGARPGGTPGAPASQPGAEGESVFSKILPGGAAEQAGKLTEAVSAFGKKFSSFW
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Scaffold protein of the presynaptic cytomatrix at the active zone (CAZ) which is the place in the synapse where neurotransmitter is released. After synthesis, participates in the formation of Golgi-derived membranous organelles termed Piccolo-Bassoon transport vesicles (PTVs) that are transported along axons to sites of nascent synaptic contacts (By similarity). At the presynaptic active zone, regulates the spatial organization of synaptic vesicle cluster, the protein complexes that execute membrane fusion and compensatory endocytosis (By similarity). Functions also in processes other than assembly such as the regulation of specific presynaptic protein ubiquitination by interacting with SIAH1 or the regulation of presynaptic autophagy by associating with ATG5 (By similarity). Mediates also synapse to nucleus communication leading to reconfiguration of gene expression by associating with the transcriptional corepressor CTBP1 and by subsequently reducing the size of its pool available for nuclear import (By similarity).
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O88738
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BIRC6_MOUSE
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Baculoviral IAP repeat-containing protein 6 (EC 2.3.2.27) (BIR repeat-containing ubiquitin-conjugating enzyme) (BRUCE) (RING-type E3 ubiquitin transferase BIRC6) (Ubiquitin-conjugating BIR domain enzyme apollon) (APOLLON)
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MVTGCGAAPPGTVTERLPSVIVLSAGRKMAAAAAEASGPSCSSAAAAAGAGAAGVSEWLVLRDGCMRCDADGLHSLSYHPALNAILAVTSRGTIKVIDGTSGATLQASALSAKPGGQVKCQYISAVDKVIFVDDYAVGCRKDLNGILLLDTALQTPVSKQDDVVQLELPVTEAQQLLSACIEKIDVSSTEGYDLFITQLKDGLKNTSHETAANHKVAKWATVTFHLPHHVLKSIASAIVNELKKINQNVAALPVASSVMDRLSYLLPSARPELGVGPGRSVDRALMYSEANRRETFTSWPHVGYRWAQPDPMAQAGFYHQPASSGDDRAMCFTCSVCLVCWEPTDEPWSEHERHSPNCPFVKGEHTQNVPLSVTLATSPAQLPSADGADRIACFGSGSCPQFLAAATKRGKICIWDVSKLMKVHLKFEINAYDPAIVQQLILSGDPSSGVDSRRPTLAWLEDSSSCSDIPKLEGDSDDLLEDSDSEEHSRSDSVTGHTSQKEAMEVSLDITALSILQQPEKLQWEIVANVLEDTVKDLEELGANPSLTNSKSEKTKEKHQEQHNIPFPCLLAGGLLTYKSPATSPISSNSHRSLDGLSRTQGESISEQGSTDNESCTNSELNSPLVRRTLPVLLLYSIKESDEKAGKIFSQMNNIMSKSLHDDGFTVPQIIEMELDNQEQLLLQDPPVTYIQQFADAAASLTSPDSEKWNSVFPKPGALVQCLRLPKFAEEETLCIDSITPCADGIHLLVGLRTCSVESLSAINQVEALNNLNKLNSALCNRRKGDLESNLAVVNGANISVIQHESPADVPEHLLIRPEQRNVVSGGYLVLYKMNYTTRIVTLEEEPVKIQHIKDPQDTITSLILLPPDILDNREDDCEEPAEEMQLASKNGIEREKKSDISTLGHLVVTTQGGYVKVLDLSNFEILAKVEPPKKEGTEEQDTFVSVIYCSGTDRLCACTKGGELHFLQIGGTCDDIDEADILVDGSLSKGIEPALEGSRPLSNPSSPGISGVELLVDQPFTLEILTSLVELTRFETLTPRFSATVPPCWVEVQQEQQQRRHPQHLHQQHHGDAAQHTRTWKLQTDSNSWDEHVFELVLPKACMVGHVDFKFVLNSNITSVPQIQVTLLKNKAPGLGKANALNIEVEHNGNPSLVDLNEEMHHMDVEESQCLRLCPFLEDHKEDILCGPVWLASGLDLSGHAGMLTLTSPKLVKGMAGGKYRSFLIHVKAVSDRGAADEMCSSGLRPVVRLPSLKQQGHKGYSLASLLAKVAAGKEKSSNVKNENAGGTRKSENLRGCDLLQEVSVTIRRFKKTSICKERVQRCAMLQFSEFHEKLLNTLCRRSDDGQVTEHAQSLVLDALCWLAGVHSNGSGSSKEGNECLLSKTRKCLSDIVRVCFFEAGRSIAHKCARFLALCISNGKCEPCQPGFGSVLLKALLDNMCFLPAAATGGSVYWYFVLLNYVKDEDLAGCSTACAALLTAVSRQLQDRLTPLEALLQTRYGLYSSPFDPVLFDLEMSGSSWKTVYSSSTAVQSDEIDLSDVLSGNGRVSSCTAAEGSFTSLTGLLEVEPLHFTCVSTSDGTRIERDDASTFTVSSFGVPPAVGGLSSGTVGEASTALSSAAQVALQSLSHAMASAEQQLQVLQEKQQQLLKLQQQKAKLEAKLHQTTAAAAAAASAAAAAAAGPVHNAVPSNPVAAPGFFIHPSDVIPPTPKTTPLFMTPPLTPPNEAVSVVINAELAQLFPGSVIDPPAVNLAAQNKNSSKSRMNPLGSGLALAISHASHFLQPPPHQSIIIERMHSGARRFVTLDFGRPILLTDVLIPTCGDLASLSIDIWTLGEEVDGRRLVVATDISTHSLILHDLIPPPVCRFMKITVIGRYGSTNARAKIPLGFYYGHSYILPWESELKLMHDPLRGEGESASQPEIDQHLAMMVALQEDIQCRYNLACHRLEALLQSIDLPPLNSANNAQYFLRKPDKAVEEDSRVFSAYQDCIQLQLQLNLAHNAVQRLKVAIGASRKLLNETSGPEDLIQTSSTEQLRTIVRYLLDTLLSLLHSSNGHSVPAVLQSTFHAQACEELFKHLCISGTPKIRLHTGLLLVQLCGGERWWGQFLSNVLQELYNSEQLLIFPQDRVFMLLSCIGQRSLSNSGVLESLLNLLDNLLSPLQPELSMHRRTEGVLDIPMISWVVMLVSRLLDYVATVEDEAAAAKKPLNGKDRERFLTGNQWSFINNNLHTQNLNRSSKGGSSLDRLYSRKIRKQLVHHKQQLNLLKAKQKALVEQMEKEKIQSNKGSSYKLLVEQAKLKQATSKHFKDLIRLRRTAEWSRSNLDTEVTTTKESPEIEPLPFTLAHDRCISVVQKLVLFLLSMDFTCHADLLLFVCKVLARIANATRPTIHLCEIVNEPQLERLLLLLVGTDFNRGDISWGGAWAQYSLTCMLQDILAGELLAPVAAEAMEECTVSEDVGATAGDSDDSLQQSPAQLLETIDEPLTHEIAGTPPLSSLEKDKEIDLELLQDLMEVDIDPLDIDLEKDPLAAKVFKPISSTWYDYWGADYGTYNYNPYIGGLGMPVAKPPSNTEKNGSQTVSVSVSQALDARLEVGLEQQAELMLKMMSTLEADSILQALTNTSPTFSQSPTGTDDSLLGNLQPANQNSQLMIQLSSVPMLNVCFNKLFSMLQVHHVQLESLLQLWLTLSLNSSSSGNKENGADIFLYNANRIPVISLNQASIASFLTVLAWYPNTLLRTWCLVLHSLTLMTNMQLNSGSSSSIGIQETTAHLLVSDPNLIHVLVKFLSGTSPHGTNQHSPQVGPTATQAMQEFLTRLQVHLSSTCPQIFSELLLKLIHILSTERGAFQTGQGPLDAQVKLLEFTLEQNFEVVSVSTISAVIESVTFLVHHYITCSDKVMSRSGSDSSAGARACFGGLFANLIRPGDAKAVCGEMTRDQLMFDLLKLVNILVQLPLSSNREYSARVSVTTNTTDSVSDEEKVSGGKDVNGSSASTPGSPACVADLVLANQQIMSQILSALGLCNSSAMAMIIGASGLHLTKHENFHGGLDAISVGDGLFTILTTLSKKASTVHMMLQPILTYMACGYMGRQGSLATCQLSEPLLWFILRVLDTSDALKAFHDMGGVQLICNNMVTSTRAIVNTARSMVSTIMKFLDSGPNKAVDSTLKTRILASEPDNAEGIHNFAPLGTITSSSPTAQPAEVLLQATPPHRRARSAAWSYIFLPEEAWCDLTIHLPSAVLLKEIHIQPHLASLATCPSSVSVEVSADGVNMLPLSTPVVTSGLTYIKIQLVKAEVASAVCLRLHRPRDASTLGLSQIKLLGLTAFGTTSSATVNNPFLPSEDQVSKTSIGWLRLLHHCLTHISDLEGMMASAAAPTANLLQTCAALLMSPYCGMHSPNIEVVLVKIGLQSTRIGLKLIDILLRNCAASGSDPTDLNSPLLFGRLNGLSSDSTIDILYQLGTTQDPGTKDRIQALLKWVSDSAKMAALKRSGRMNYMCPSSSAVEYGLLMPSPSHLHCVAAILWHSYELLVEYDLPALLDRELFELLFNWSMSLPCNVVLKKAVDSLLCSMCHIHPNYFSLLMGWMGIIPPPVQCHHRLSMTDDSKKQDLSSSLTDDSKNAQAPLSLTESHLATLASSSQSPEAIKQLLDSGLPSLLVRSLASFCFSHISYSESIAQSVDNSQDKLRRHHVPQHCNKMPITADLVAPILRFLTEVGNSHIMKDWLGGSEVNPLWTALLFLLCHSGSTAGGHNLGAQQSSTRSASHSSATTTVLTTQQRTAIENATVAFFLQCISCHPNNQKLMAQVLCELFQTAPQRGSLPTSGNISGFVRRLFLQLMLEDEKVTMFLQSPCPLYKGRINATSHVIQHPMFGAGHKFRTLHLPVSTTLSDVLDRVSDTPSITAKLISEQKDDKEKKNHEEKEKVKAENGFQDNYSVVVASGLKSQSKRAMASTPPRPPSRRGRTIPDKIGSASSSADAASKIITVPVFHLFHRLLAGQPLPAEMTLAQLLTLLYDRKLPQGYRSIDLTVKLGSKVITDPSLSKTDSFKRLHPEKDHGDLVGSCPEDEALTPSDECMDGVLDESLLETCPIQSPLQVFAGMGGLALIAERLPMLYPEVIQQVSAPVIASTTQEKPKDSDQFEWVTIEQSGELVYEAPETIAAEPPPVKSAVQATSPIPAHSLAAFGLFLRLPGYAEVLLKERKHAQCLLRLVLGVTDDGEGSHILQSPSANVLPTLPFHVLRSLFSATPLTTDDGVLLRRMALEIGALHLILVCLSALSHHAPRVPNSSLSQTEPQVSNSHNPTSAEEQQLYWAKGTGFGTGSTASGWDVEQALTKQRLEEEHVTCLLQVLASYINPMSGAVNGEAQASPESRAQNSSALPSVLLELLSQSCLIPAMSSYLRNDSVLDMARHVPLYRALLELLRAIASCTSMVPLLLPLSTENGEEEEDEQSECQTSVGTLLAKMKTCVDTYTNRLRSKRENVKAGVKPDAPDQEPEGLALLVPDIQRTAEIVHAATANLRQANQEKKLGEYSKKVVMKPKPLSVLKSLEEKYVAVMKKLQFDTFEMVSEDDDGKLGFKVNYHYMSQVKNANDANSAARARRLAQEAVTLSTSLPLSSSSSVFVRCDEERLDIMKVLITGPADTPYANGCFEFDVYFPQDYPSSPPLVNLETTGGHSVRFNPNLYNDGKVCLSILNTWHGRPEEKWNPQTSSFLQVLVSVQSLILVAEPYFNEPGYERSRGTPSGTQSSREYDGNIRQATVKWAMLEQIRNPSPCFKEVIHKHFYLKRIELMAQCEEWIADIQQYSSDKRVGRTMSHHAAALKRHTAQLREELLKLPCPEGLDPDIEDASPVCRATAGAEDTLTHDHVNPSSSKDLPSDFQL
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Anti-apoptotic protein which can regulate cell death by controlling caspases and by acting as an E3 ubiquitin-protein ligase. Has an unusual ubiquitin conjugation system in that it could combine in a single polypeptide, ubiquitin conjugating (E2) with ubiquitin ligase (E3) activity, forming a chimeric E2/E3 ubiquitin ligase. Its targets include CASP9 and DIABLO/SMAC. Acts as an inhibitor of CASP3, CASP7 and CASP9. Important regulator for the final stages of cytokinesis. Crucial for normal vesicle targeting to the site of abscission, but also for the integrity of the midbody and the midbody ring, and its striking ubiquitin modification. Required for normal placenta development.
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O88741
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GDAP1_MOUSE
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Ganglioside-induced differentiation-associated protein 1 (GDAP1)
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MARRQDEARAGVPLRVEGPPDKEVHLILYHWTHSFSSQKVRLVIAEKALKCEEHDVSLPLSEHNEPWFMRLNSAGEVPVLVHGENIICEATQIIDYLEQTFLDERTPRLMPDEGSMYYPRVQHYRELLDSLPMDAYTHGCILHPELTVDSMIPAYATTRIRSQIGNTESELKKLAEENPDLQEAYIAKQKRLKSKLLDHDNVKYLKKILDELEKVLDQVETELQRRNEETPEEGNQPWLCGESFTLADVSLAVTLHRLKFLGFARRNWGHGKRPNLETYYERVLKRKTFNKVLGHVNNILISAVLPTAFRVAKKRAPKVLGSTLVVGLLVGMGYFAFMLFRRRLGSMILALRPRPNYF
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Regulates the mitochondrial network by promoting mitochondrial fission. {ECO:0000250, ECO:0000269|PubMed:16172208}.
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O88746
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TOM1_MOUSE
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Target of Myb1 membrane trafficking protein (Target of Myb protein 1)
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MDFLLGNPFSSPVGQRIEKATDGSLQSEDWALNMEICDIINETEEGPKDAFRAVKKRIMGNKNFHEVMLALTVLETCVKNCGHRFHVLVANQDFVENVLVRTILPKNNPPTIVHDKVLNLIQSWADAFRSSPDLTGVVAVYEDLRRKGLEFPMTDLDMLSPIHTPQRTVFNSETPSRQNSVSSNTSQRGDLSQHATPLPTPAVLPGDSPITPTPEQIGKLRSELEMVSGNVRVMSEMLTELVPTQVEPADLELLQELNRTCRAMQQRILELIPRISNEQLTEELLMINDNLNNVFLRHERFERFRTGQTAKASSEAELATDLIDMGPDPAATNNLSSQLAGMNLGSRSVRAGLQSLETSGHLEDDFDMFALTRGSSLADQRKGVKYEAPQTTDGLAGALDARQQSTGAIPATQARIMEDIEQWLSTDVGNSAEEPSGVTSEEFDKFLEERAKAADRLPNLASPSAEGPPRPSPGTAPRRKTQEKDDDMLFAL
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Adapter protein that plays a role in the intracellular membrane trafficking of ubiquitinated proteins, thereby participating in autophagy, ubiquitination-dependent signaling and receptor recycling pathways (By similarity). Acts as a MYO6/Myosin VI adapter protein that targets MYO6 to endocytic structures (By similarity). Together with MYO6, required for autophagosomal delivery of endocytic cargo, the maturation of autophagosomes and their fusion with lysosomes (By similarity). MYO6 links TOM1 with autophagy receptors, such as TAX1BP1 CALCOCO2/NDP52 and OPTN (By similarity). Binds to polyubiquitinated proteins via its GAT domain (By similarity). In a complex with TOLLIP, recruits ubiquitin-conjugated proteins onto early endosomes (By similarity). The Tom1-Tollip complex may regulate endosomal trafficking by linking polyubiquitinated proteins to clathrin (By similarity). Mediates clathrin recruitment to early endosomes by ZFYVE16 (By similarity). Modulates binding of TOLLIP to phosphatidylinositol 3-phosphate (PtdIns(3)P) via binding competition the association with TOLLIP may favor the release of TOLLIP from endosomal membranes, allowing TOLLIP to commit to cargo trafficking (By similarity). Acts as a phosphatidylinositol 5-phosphate (PtdIns(5)P) effector by binding to PtdIns(5)P, thereby regulating endosomal maturation. PtdIns(5)P-dependent recruitment to signaling endosomes may block endosomal maturation. Also inhibits Toll-like receptor (TLR) signaling and participates in immune receptor recycling (By similarity).
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O88751
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CABP1_RAT
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Calcium-binding protein 1 (CaBP1) (Caldendrin)
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MSSHIAKSESKTSLLKAAAASGGSRAPRHSSARDPGLRGRRLPGPCPDSPATCGDPSSRRPLCRPVPRDEGARGSRRGLPQAHCRPRETLPPARGRDGEERGLAPALSLRGSLRSRGRGDPAPAGTPEADPFLHQLRPMLSSAFGQDRSLRPEEIEELREAFREFDKDKDGYINCRDLGNCMRTMGYMPTEMELIELSQQINMNLGGHVDFDDFVELMGPKLLAETADMIGVKELRDAFREFDTNGDGEISTSELREAMRKLLGHQVGHRDIEEIIRDVDLNGDGRVDFEEFVRMMSR
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Modulates calcium-dependent activity of inositol 1,4,5-triphosphate receptors (ITPRs). Inhibits agonist-induced intracellular calcium signaling (By similarity). Enhances inactivation and does not support calcium-dependent facilitation of voltage-dependent P/Q-type calcium channels. Causes calcium-dependent facilitation and inhibits inactivation of L-type calcium channels by binding to the same sites as calmodulin in the C-terminal domain of CACNA1C, but has an opposite effect on channel function. Suppresses the calcium-dependent inactivation of CACNA1D. Inhibits TRPC5 channels. Prevents NMDA receptor-induced cellular degeneration. Required for the normal transfer of light signals through the retina (By similarity).
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O88763
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PK3C3_RAT
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Phosphatidylinositol 3-kinase catalytic subunit type 3 (PI3-kinase type 3) (PI3K type 3) (PtdIns-3-kinase type 3) (EC 2.7.1.137) (Phosphoinositide-3-kinase class 3)
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MGEAEKFHYIYSCDLDINVQLKIGSLEGKREQKSYKAVLEDPMLKFSGLYQETCSDLYVTCQVFAEGKPLALPVRTSYKPFSTRWNWNEWLKLPVKYPDLPRNAQVALTIWDVYGPGRAVPVGGTTVSLFGKYGMFRQGMHDLKVWPNVEADGSEPTRTPGRTSSTLSEDQMSRLAKLTKAHRQGHMVKVDWLDRLTFREIEMINESEKRSSNFMYLMVEFRCVKCDDKEYGIVYYEKDGDESSPILTSFELVKVPDPQMSMENLVESKHHKLARSLRSGPSDHDLKPNATTRDQLNIIVSYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDVEDSLELLSSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDIKNGLEPTKKDSQASVSESLSSSGVSSADIDSSQIITNPLPPVASPPPASKSKEVSDGENLEQDLCTFLISRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMYLNVMRRFSQALLKGDKSVRVMRSLLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALLGDNEKMNLSDVELIPLPLEPQVKIRGIIPETATLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFMQFIQSVPVAEVLDTEGSIQNFFRKYAPSETGPNGISAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGRDPKPLPPPMKLNKEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEPDKTVKKVQDKFRLDLSDEEAVHYMQSLIDESVHALFAAVVEQIHKFAQYWRK
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Catalytic subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis. As part of PI3KC3-C1, promotes endoplasmic reticulum membrane curvature formation prior to vesicle budding. Involved in regulation of degradative endocytic trafficking and required for the abcission step in cytokinesis, probably in the context of PI3KC3-C2 (By similarity). Involved in the transport of lysosomal enzyme precursors to lysosomes. Required for transport from early to late endosomes.
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O88764
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DAPK3_RAT
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Death-associated protein kinase 3 (DAP kinase 3) (EC 2.7.11.1) (DAP-like kinase) (Dlk) (MYPT1 kinase) (ZIP-kinase)
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MSTFRQEDVEDHYEMGEELGSGQFAIVRKCQQKGTGMEYAAKFIKKRRLPSSRRGVSREEIEREVSILREIRHPNIITLHDVFENKTDVVLILELVSGGELFDFLAEKESLTEDEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKHAASPRIKLIDFGIAHRIEAGSEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSSTSELAKDFIRRLLVKDPKRRMTIAQSLEHSWIKVRRREDGARKPERRRLRAARLREYSLKSHSSMPRNTSYASFERFSRVLEDVAAAEQGLRELQRGRRQCRERVCALRVAAEQREARCRDGSAGLGRDLRRLRTELGRTEALRTRAQEEARAALLGAGGLKRRLCRLENRYDALAAQVAAEVQFVRDLVRALEQERLQAECGVR
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Serine/threonine kinase which is involved in the regulation of apoptosis, autophagy, transcription, translation and actin cytoskeleton reorganization. Regulates both type I (caspase-dependent) apoptotic and type II (caspase-independent) autophagic cell deaths signal, depending on the cellular setting. Involved in formation of promyelocytic leukemia protein nuclear body (PML-NB). Involved in apoptosis involving PAWR which mediates cytoplasmic relocation in vitro phosphorylates PAWR. Phosphorylates MYL12B in non-muscle cells leading to reorganization of actin cytoskeleton such as in regulation of cell polarity and cell migration. Positively regulates canonical Wnt/beta-catenin signaling through interaction with NLK and TCF7L2 disrupts the NLK-TCF7L2 complex thereby influencing the phosphorylation of TCF7L2 by NLK. Phosphorylates RPL13A on 'Ser-77' upon interferon-gamma activation which is causing RPL13A release from the ribosome, RPL13A association with the GAIT complex and its subsequent involvement in transcript-selective translation inhibition (By similarity). Phosphorylates STAT3 and enhances its transcriptional activity (By similarity). Enhances transcription from AR-responsive promoters in a hormone- and kinase-dependent manner. Phosphorylates histone H3 on 'Thr-11' at centromeres during mitosis.
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O88766
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MMP8_RAT
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Neutrophil collagenase (EC 3.4.24.34) (Matrix metalloproteinase-8) (MMP-8)
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MLHLKTLPFLFFFHTQLATALPVPPEHLEEKNMKTAENYLRKFYHLPSNQFRSARNATMIAEKLKEMQRFFGLPETGKPDAATIEIMEKPRCGVPDSGDFLLTPGSPKWTHTNLTYRIINHTPQMSKAEVKTEIEKAFKIWSVPSTLTFTETLEGEADINIAFVSRDHGDNSPFDGPNGILAHAFQPGRGIGGDAHFDSEETWTQDSKNYNLFLVAAHEFGHSLGLSHSTDPGALMYPNYAYREPSTYSLPQDDINGIQTIYGPSDNPVQPTGPSTPTACDPHLRFDAATTLRGEIYFFKDKYFWRRHPQLRTVDLNFISLFWPFLPNGLQAAYEDFDRDLVFLFKGRQYWALSAYDLQQGYPRDISNYGFPRSVQAIDAAVSYNGKTYFFVNNQCWRYDNQRRSMDPGYPTSIASVFPGINCRIDAVFQQDSFFLFFSGPQYFAFNLVSRRVTRVARSNLWLNCP
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Can degrade fibrillar type I, II, and III collagens.
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O88767
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PARK7_RAT
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Parkinson disease protein 7 homolog (Contraception-associated protein 1) (Protein CAP1) (Fertility protein SP22) (Maillard deglycase) (Parkinsonism-associated deglycase) (Protein DJ-1) (DJ-1) (Protein/nucleic acid deglycase DJ-1) (EC 3.1.2.-, EC 3.5.1.-, EC 3.5.1.124)
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MASKRALVILAKGAEEMETVIPVDIMRRAGIKVTVAGLAGKDPVQCSRDVVICPDTSLEEAKTQGPYDVVVLPGGNLGAQNLSESALVKEILKEQENRKGLIAAICAGPTALLAHEVGFGCKVTSHPLAKDKMMNGSHYSYSESRVEKDGLILTSRGPGTSFEFALAIVEALSGKDMANQVKAPLVLKD
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Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of advanced glycation endproducts (AGE) that cause irreversible damage. Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Also displays an apparent glyoxalase activity that in fact reflects its deglycase activity. Plays an important role in cell protection against oxidative stress and cell death acting as oxidative stress sensor and redox-sensitive chaperone and protease functions probably related to its primary function. It is involved in neuroprotective mechanisms like the stabilization of NFE2L2 and PINK1 proteins, male fertility as a positive regulator of androgen signaling pathway as well as cell growth and transformation through, for instance, the modulation of NF-kappa-B signaling pathway. Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death. Required for correct mitochondrial morphology and function as well as for autophagy of dysfunctional mitochondria. Plays a role in regulating expression or stability of the mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra pars compacta and attenuates the oxidative stress induced by calcium entry into the neurons via L-type channels during pacemaking. Regulates astrocyte inflammatory responses, may modulate lipid rafts-dependent endocytosis in astrocytes and neuronal cells (By similarity). In pancreatic islets, involved in the maintenance of mitochondrial reactive oxygen species (ROS) levels and glucose homeostasis in an age- and diet dependent manner. Protects pancreatic beta cells from cell death induced by inflammatory and cytotoxic setting (By similarity). Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress. Metal-binding protein able to bind copper as well as toxic mercury ions, enhances the cell protection mechanism against induced metal toxicity (By similarity). In macrophages, interacts with the NADPH oxidase subunit NCF1 to direct NADPH oxidase-dependent ROS production, and protects against sepsis (By similarity).
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O88775
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EMB_RAT
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Embigin
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MRSHTGLRALVAPGCSLLLLYLLAATRPDRAVGDPADSAFTSLPVREEMMAKYANLSLETYNISLTEQTRVSEQNITLERPSHLELECTFTATEDVMSMNVTWKKDDALLETTDGFNTTKMGDTLYSQYRFTVFNSKQMGKYSCFLGEELRGTFNIRVPKVHGKNKPLITYVGDSTVLKCECQNCLPLNWTWYMSNGTAQVPIDVHVNDKFDINGSYANETKLKVKHLLEEDGGSYWCRAAFPLGESEEHIKLVVLSFMVPLKPFLAIIAEVILLVAIILLCEVYTQKKKNDPDDGKEFEQIEQLKSDDSNGIENNVPRYRKTDSGDQ
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Plays a role in the outgrowth of motoneurons and in the formation of neuromuscular junctions. Following muscle denervation, promotes nerve terminal sprouting and the formation of additional acetylcholine receptor clusters at synaptic sites without affecting terminal Schwann cell number or morphology. Delays the retraction of terminal sprouts following re-innervation of denervated endplates (By similarity). Plays a role in targeting the monocarboxylate transporters SLC16A1 and SLC16A7 to the cell membrane. {ECO:0000250, ECO:0000269|PubMed:19473976, ECO:0000269|PubMed:20695846}.
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O88777
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PSN2_RAT
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Presenilin-2 (PS-2) (EC 3.4.23.-) [Cleaved into: Presenilin-2 NTF subunit; Presenilin-2 CTF subunit]
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MLTFMASDSEEEVCDERTSLMSAESPTSRSCQDSRPGPEDGENTAQWRSQENEDDCEEDPDHYACSGVPGRPSGLEEELTLKYGAKHVIMLFVPVTLCMIVVVATIKSVRFYTEKNGQLIYTPFTEDTPSVGQRLLNSVLNTLIMISVIVVMTIFLVVLYKYRCYKFIHGWLIMSSLMLLFLFTYIYLGEVFKTYNVAMDYPTLFLAVWNFGAVGMVCIHWKGPLVLQQAYLIVISALMALVFIKYLPEWSAWVILGAISVYDLVAVLCPKGPLRMLVETAQERNEPIFPALIYSSAMVWTVGMAKLDPSSQGALQLPYDPEMEEDSYDSFGEPSYPEAFEAPQPGYPGEEPEEEEERGVKLGLGDFIFYSVLVGKAAATGNGDWSTTLACFIAILIGLCLTLLLLAVFKKALPALPISITFGLIFYFSTDNLVRPFMDTLASHQLYI
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Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). Requires the other members of the gamma-secretase complex to have a protease activity. May play a role in intracellular signaling and gene expression or in linking chromatin to the nuclear membrane. May function in the cytoplasmic partitioning of proteins. The holoprotein functions as a calcium-leak channel that allows the passive movement of calcium from endoplasmic reticulum to cytosol and is involved in calcium homeostasis (By similarity). Is a regulator of mitochondrion-endoplasmic reticulum membrane tethering and modulates calcium ions shuttling between ER and mitochondria.
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O88778
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BSN_RAT
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Protein bassoon
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MGNEASLEGGAGEGPLPPGGSGLGPGPGAGKPPSALAGGGQLPVAGAARAAGPPTPGLGLVPGPGPGPGPGSVSRRLDPKEPLGSQRATSPTPKQASATAPGRESPRETRAQGLSGQEAEGPRRTLQVDSRTQRSGRSPSVSPDRGSTPTSPYSVPQIAPLPSSTLCPICKTSDLTSTSSQPNFNTCTQCHNKVCNQCGFNPNPHLTQVKEWLCLNCQMQRALGMDMTTAPRSKSQQQLHSPALSPAHSPAKQPLGKPEQERSRSPGATQSGPRQAEAARATSVPGPTQATAPPEVGRVSPQPPLSTKPSTAEPRPPAGEAQGKSATTVPSGLGAAEQTQGGLTGKLFGLGASLLTQASTLMSVQPEADTQGQPSPSKGPPKIVFSDASKEAGPRPPGSGPGPGPTPGAKTEPGPRTGPGSGPGALAKTGGTPSPKHGRADHQAASKAAAKPKTMPKERAACPLCQAELNVGSRGPANYNTCTACKLRVCTLCGFNPTPHLVEKTEWLCLNCQTKRLLEGSLGEPAPLPLPTPQEPPAGVPQRAAGASPLKQKGPQGPGQPSGSLPPKASPQAAKASPQAAKASPQAKPLRASEPSKTSSSAPEKKTGIPVKAEPVPKPPPETAVPPGTPKAKSGVKRTDPATPVVKPVPEAPKSGEAEEPVPKPYSQDLSRSPQSLSDTGYSSDGVSSSQSEITGVVQQEVEQLDSAGVTGPRPPSPSELHKVGSSMRPSLEAQAVAPSGEWSKPPSGSAVEDQKRRPHSLSIMPEAFDSDEELGDILEEDDSLAMGRQREQQDTAESSDDFGSQLRHDYVEDSSEGGLSPLPPQPPARADMTDEEFMRRQILEMSAEEDNLEEDDTAVSGRGLAKHGAQKASARPRPESSQESVALPKRRLPHNATTGYEELLSEEGPAEPTDGALQGGLRRFKTIGLNSTGRLWSTSLDLGQGSDPNLDREPELEMESLTGSPEDRSRGEHSSTLPASTPSYTSGTSPTSLSSLEEDSDSSPSRRQRLEEAKQQRKARHRSHGPLLPTIEDSSEEEELREEEELLREQEKMREVEQQRIRSTARKTRRDKEELRAQRRRERSKTPPSNLSPIEDASPTEELRQAAEMEELHRSSCSEYSPSPSLDSEAETLDGGPTRLYKSGSEYNLPAFMSLCSPTETPSGSSTTPSSGRPLKSAEEAYEDMMRKAELLQRQQGQAAGARGPHGGPSQPTGPRSQGSFEYQDTLDHDYGGRASQPAADGTPAGLGATVYEEILQTSQSIARMRQASSRDLAFTEDKKKEKQFLNAESAYMDPMKQNGGPLTPGTSPTQLAAPVSFPTSTSSDSSGGRVIPDVRVTQHFAKEPQEPLKLHSSPASPSLASKEVGMTFSQGPGTPATTAMAPCPASLPRGYMTPAGPERSPSTSSTIHSYGQPPTTANYGSQTEELPHAPSGPAGSGRASREKPLSGGDGEVGPPQPSRGYSYFTGSSPPLSPSTPSESPTFSPSKLGPRATAEFSTQTPSLTPSSDIPRSVGTPSPMVAQGTQTPHRPSTPRLVWQQSSQEAPVMVITLASDASSQTRMVHASASTSPLCSPTDSQPASHSYSQTTPPSASQMPSEPAGPPGFPRAPSAGVDGPLALYGWGALPAENISLCRISSVPGTSRVEPGPRPPGTAVVDLRTAVKPTPIILTDQGMDLTSLAVEARKYGLALDPVPGRQSTAVQPLVINLNAQEQTHTFLATATTVSITMASSVLMAQQKQPVVYGDPFQSRLDFGQGSGSPVCLAQVKQVEQAVQTAPYRGGPRGRPREAKFARYNLPNQVTPLARRDILITQMGTAQSVSLKPGPVPEPGAEPHRATPAELRAHALPGTRKPHTVVVQMGEGAAGTVTTLLPEEPAGALDLTGMRPESRLACCDMAYKFPFGSSCTGTFHPAPSAPDKSVTDAALPGQSSGPFYSPRDPEPPEPLTFRAQGVVGPGPHEEQRPYPQGLPGRLYSSMSDTNLAEAGLNYHAQRIGQLFQGPGRDSAVDLSSLKHSYSLGFADGRYLGQGLQYGSFTDLRHPTDLLSHPLPMRPYSSVSNIYSDHRYGPRGDAVGFQEASLAQYSATTAREISRMCAALNSMDQYGGRHGGGSGGPDLVPYQPQHGPGLNAPQGLASLRSGLLGNPTYPEGQPSPGNLAQYGPAASQGTAVRQLLPSTATVRAADGMIYSTINTPIAATLPITTQPASVLRPMVRGGMYRPYGSGGVTAVPLTSLTRVPMIAPRVPLGPAGLYRYPAPSRFPIASTIPPAEGPVYLGKPAAAKASGAGGPPRPELPAGGAREEPLSTTAPPAVIKEAPVAQAPAPPPGQKPAGDAAAGSGSGVLGRPVMEKEEASQEDRQRKQQEQLLQLERERVELEKLRQLRLQEELERERVELQRHREEEQLLVQRELQELQTIKHHVLQQQQEERQAQFALQREQLAQQRLQLEQIQQLQQQLQQQLEEQKQRQKAPFPATCEAPSRGPPPAATELAQNGQYWPPLTHTAFIAVAGTEGPGQAREPVLHRGLPSSASDMSLQTEEQWEAGRSGIKKRHSMPRLRDACEPESGPDPSTVRRIADSSVQTDDEEGEGRYLLTRRRRTRRSADCSVQTDDEDNAEWEQPVRRRRSRLSRHSDSGSDSKHEASASSSAAAAAARAMSSVGIQTISDCSVQTEPEQLPRVSPAIHITAATDPKVEIVRYISAPEKTGRGESLACQTEPDGQAQGVAGPQLIGPTAISPYLPGIQIVTPGALGRFEKKKPDPLEIGYQAHLPPESLSQLVSRQPPKSPQVLYSPVSPLSPHRLLDTSFASSERLNKAHVSPQKQFIADSTLRQQTLPRPMKTLQRSLSDPKPLSPTAEESAKERFSLYQHQGGLGSQVSALPPNGLVRKVKRTLPSPPPEEAHLPLAGQVPSQLYAASLLQRGLAGPTTVPATKASLLRELDRDLRLVEHESTKLRKKQAELDEEEKEIDAKLKYLELGITQRKESLAKDRVGRDYPPLRGLGEHRDYLSDSELNQLRLQGCTTPAGQYVDYPASAAVPATPSGPTAFQQPRFPPAATQYTAGSSGPTQNGFLAHQAPTYTGPSTYPAPTYPPGTSYPAEPGLPSQPAFHPTGHYAAPTPMPTTQSAPFPVQADSHAAHQKPRQTSLADLEQKVPTNYEVISSPAVTVSSTPSETGYSGPAVSSSYEHGKAPEHPRGGDRSSVSQSPAPTYPSDSHYTSLEQNVPRNYVMIDDISELTKDSTPTASDSQRPEPLGPGGVSGRPGKDPGEPAVLEGPTLPCCYGRGEEESEEDSYDPRGKSGHHRSMESNGRPASTHYYSDSDYRHGARADKYGPGPMGPKHPSKNLAPAAISSKRSKHRKQGMEQKISKFSPIEEAKDVESDLASYPPPTVSSSLTSRSRKFQDEITYGLKKNVYEQQRYYGVSSRDTAEEDDRMYGGSSRSRVASAYSGEKLSSHDFSSRSKGYERERETAQRLQKAGPKPSSLSMAHGRARPPMRSQASEEESPVSPLGRPRPAGGALPPGDTCPQFCSSHSMPDVQEHVKDGPRAHAYKREEGYILDDSHCVVSDSEAYHLGQEETDWFDKPRDARSDRFRHHGGHTVSSSQKRGPARHSYHDYDEPPEEGLWPHDEGGPGRHTSAKEHRHHGDHGRHSGRHAGEEPGRRAARPHARDMGRHETRPHPQASPAPAMQKKGQPGYPSSADYSQPSRAPSAYHHASDSKKGSRQAHSGPTVLQPKPEAQAQPQMQGRQAVPGPQQSQPPSSRQTPSGTASRQPQTQQQQQQQQQQQQQQQQQQQQQQQQGLGQQAPQQAPSQARLQQQSQPTTRSTAPAASHPAGKPQPGPTTAPGPQPAGLPRAEQAGSSKPAAKAPQQGRAPQAQSAPGPAGAKTGARPGGTPGAPAGQPAAEGESVFSKILPGGAAEQAGKLTEAVSAFGKKFSSFW
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Scaffold protein of the presynaptic cytomatrix at the active zone (CAZ) which is the place in the synapse where neurotransmitter is released. After synthesis, participates in the formation of Golgi-derived membranous organelles termed Piccolo-Bassoon transport vesicles (PTVs) that are transported along axons to sites of nascent synaptic contacts. At the presynaptic active zone, regulates the spatial organization of synaptic vesicle cluster, the protein complexes that execute membrane fusion and compensatory endocytosis. Functions also in processes other than assembly such as the regulation of specific presynaptic protein ubiquitination by interacting with SIAH1 or the regulation of presynaptic autophagy by associating with ATG5. Mediates also synapse to nucleus communication leading to reconfiguration of gene expression by associating with the transcriptional corepressor CTBP1 and by subsequently reducing the size of its pool available for nuclear import.
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O88780
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KLK8_RAT
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Kallikrein-8 (EC 3.4.21.118) (Brain serine protease 1) (Neuropsin) (NP) (Serine protease 19)
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MGRPPPCAIQTWILLFLLMGAWAGLTRAQGSKILEGQECKPHSQPWQTALFQGERLVCGGVLVGDRWVLTAAHCKKDKYSVRLGDHSLQKRDEPEQEIQVARSIQHPCFNSSNPEDHSHDIMLIRLQNSANLGDKVKPIELANLCPKVGQKCIISGWGTVTSPQENFPNTLNCAEVKIYSQNKCERAYPGKITEGMVCAGSSNGADTCQGDSGGPLVCNGVLQGITTWGSDPCGKPEKPGVYTKICRYTNWIKKTMGKRD
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Serine protease which is capable of degrading a number of proteins such as casein, fibrinogen, kininogen, fibronectin and collagen type IV. Also cleaves L1CAM in response to increased neural activity. Induces neurite outgrowth and fasciculation of cultured hippocampal neurons. Plays a role in the formation and maturation of orphan and small synaptic boutons in the Schaffer-collateral pathway, regulates Schaffer-collateral long-term potentiation in the hippocampus and is required for memory acquisition and synaptic plasticity. Involved in skin desquamation and keratinocyte proliferation. Plays a role in the secondary phase of pathogenesis following spinal cord injury (By similarity).
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O88783
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FA5_MOUSE
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Coagulation factor V (Activated protein C cofactor) [Cleaved into: Coagulation factor V heavy chain; Coagulation factor V light chain]
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MLLVCPCFFLLVVLGTRWAGWGSHQAEAAQLRQFYVAAQGILWNYHPEPTDPSLNSIPSFKKIVYREYEQYFKKEKPRSSNSGLLGPTLYAEVGDVIKVHFRNKADKPLSIHPQGIKYSKFSEGASYADHTFPAERKDDAVAPGEEYTYEWIVSEDSGPTPDDPPCLTHIYYSYENLTQDFNSGLIGPLLICKKGTLTEDGTQKMFDKQHVLLFAVFDESKSRSQSPSLMYTINGFVNKTMPDITVCAHDHVSWHLIGMSSGPELFSIHFNGQVLEQNQHKVSTVTLVSATSTTANMTMSPEGRWIVSSLIPKHYQAGMQAYIDIKNCPKKTRSPKTLTREQRRYMKRWEYFIAAEEVIWNYAPVIPANMDKIYRSQHLDNFSNQIGKHYKKVIYRQYEEETFTKRTDNPSIKQSGILGPVIRAQVRDTLKIVFKNMASRPYSIYPHGVTFSPYEDGINSSSTSGSHTTIRPVQPGETFTYKWNILEFDEPTENDAQCLTRPYYSDVDVTRDIASGLIGLLLICKSRSLDQRGVQRVADIEQQAVFAVFDENKSWYIEDNINKFCENPDEVKRDDPKFYESNIMSTINGYVPESISTLGFCFDDTVQWHFCSVGTHDDILTIHFTGHSFIYGRRHEDTLTLFPMRGESVTVTMDNVGTWMLTTMNSNPKRRNLRLRFRDVKCNRDYDNEDSYEIYEPPAPTSMTTRRIHDSLENEFGIDNEDDDYQYLLASSLGIRSFKNSSLNPEENEFNLTALALENSSEFISPSTDRVVDSNSSRILSKIINNNLKDFQRTLPGSGATVAGTLLRNLIGLDENFVLNSSTEHRSSSYHENDMENPQSNITMVYLLPLGPKGSGNREQDKPKTIKTGRPHMMKHRFSWMKAPAGKTGRHSNPKNSYSGMKSEEDIPSELIPLKQKITSKFLNRRWRVASEKGSYEIIAANGEDTDVDKLTNSPQNQNITVPRGESTSHTNTTRKPSDLPTFSGVGHKSPHVRQEEENSGFQKRQLFIRTRKKKKNKKLALHSPLSPRGFDPLRGHNHSPFPDRRLLNHSLLLHKSNETALSPDLNQTSPSMSTDRSLPDYNQYSKNDTEQMSSSLDLYQSVPAEEHSPTFPAQDPDQTHSTTDPSYRSSPPELSQGLDYDLSHDFYPDDIGLTSFFPDQSQKSSFSSDDDQAIPSSDLSLFTISPELDQTIIYPDLDQLLLSPEDNQKTSSPDLGQVPLSPDDNQKTSSPDLGQVSLSPDDNQKTSSPDLGQVPLSLDDNQKTTSPDLGQVPLSPDDNQMITSPDLGQVPLSSDNQKTSSPDLGQVPLFPEDNQNYFLDLSQVPLSSDQNQETSSTDLLTLSPDFGQTVLSPDLDQLPLPSDNSQVTVSPDLSLLTLSPDFNEIILAPDLGQVTLSPDLIQTNPALNHGHKASSADPDQASYPPDSGQASSLPELNRTLPHPDLTHIPPPSPSPTLNNTSLSRKFNPLVVVGLSRVDGDDVEIVPSEEPERIDEDYAEDDFVTYNDPYRTDTRTDVNSSRNPDTIAAWYLRGHGGHKKFYYIAAEEITWNYAEFAQSEMDHEDTGHTPKDTTYKKVVFRKYLDSTFTSRDPRAEYEEHLGILGPVIRAEVDDVIQVRFKNLASRPYSLHAHGLSYEKSSEGKTYEDESPEWFQEDDAVQPNSSYTYVWHATKRSGPENPGSACRAWAYYSAVNVERDIHSGLIGPLLICRKGTLHMERNLPMDMREFVLLFMVFDEKKSWYYEKSKGSRRIESPEEKNAHKFYAINGMIYNLPGLRMYEQEWVRLHLLNMGGSRDIHVVHFHGQTLLDNRTKQHQLGVWPLLPGSFKTLEMKASKPGWWLLDTEVGENQVAGMQTPFLIIDKECKMPMGLSTGVISDSQIKASEYLTYWEPRLARLNNAGSYNAWSIEKTALDFPIKPWIQVDMQKEVVVTGIQTQGAKHYLKSCFTTEFQVAYSSDQTNWQIFRGKSGKSVMYFTGNSDGSTIKENRLDPPIVARYIRIHPTKSYNRPTLRLELQGCEVNGCSTPLGLEDGRIQDKQITASSFKKSWWGDYWEPSLARLNAQGRVNAWQAKANNNKQWLQVDLLKIKKVTAIVTQGCKSLSSEMYVKSYSIQYSDQGVAWKPYRQKSSMVDKIFEGNSNTKGHMKNFFNPPIISRFIRIIPKTWNQSIALRLELFGCDIY
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Central regulator of hemostasis. It serves as a critical cofactor for the prothrombinase activity of factor Xa that results in the activation of prothrombin to thrombin.
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O88786
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I13R2_MOUSE
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Interleukin-13 receptor subunit alpha-2 (IL-13 receptor subunit alpha-2) (IL-13R subunit alpha-2) (IL-13R-alpha-2) (IL-13RA2) (CD antigen CD213a2)
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MAFVHIRCLCFILLCTITGYSLEIKVNPPQDFEILDPGLLGYLYLQWKPPVVIEKFKGCTLEYELKYRNVDSDSWKTIITRNLIYKDGFDLNKGIEGKIRTHLSEHCTNGSEVQSPWIEASYGISDEGSLETKIQDMKCIYYNWQYLVCSWKPGKTVYSDTNYTMFFWYEGLDHALQCADYLQHDEKNVGCKLSNLDSSDYKDFFICVNGSSKLEPIRSSYTVFQLQNIVKPLPPEFLHISVENSIDIRMKWSTPGGPIPPRCYTYEIVIREDDISWESATDKNDMKLKRRANESEDLCFFVRCKVNIYCADDGIWSEWSEEECWEGYTGPDSKIIFIVPVCLFFIFLLLLLCLIVEKEEPEPTLSLHVDLNKEVCAYEDTLC
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Binds as a monomer with high affinity to interleukin-13 (IL13).
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O88792
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JAM1_MOUSE
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Junctional adhesion molecule A (JAM-A) (Junctional adhesion molecule 1) (JAM-1) (CD antigen CD321)
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MGTEGKAGRKLLFLFTSMILGSLVQGKGSVYTAQSDVQVPENESIKLTCTYSGFSSPRVEWKFVQGSTTALVCYNSQITAPYADRVTFSSSGITFSSVTRKDNGEYTCMVSEEGGQNYGEVSIHLTVLVPPSKPTISVPSSVTIGNRAVLTCSEHDGSPPSEYSWFKDGISMLTADAKKTRAFMNSSFTIDPKSGDLIFDPVTAFDSGEYYCQAQNGYGTAMRSEAAHMDAVELNVGGIVAAVLVTLILLGLLIFGVWFAYSRGYFERTKKGTAPGKKVIYSQPSTRSEGEFKQTSSFLV
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Seems to play a role in epithelial tight junction formation. Appears early in primordial forms of cell junctions and recruits PARD3. The association of the PARD6-PARD3 complex may prevent the interaction of PARD3 with JAM1, thereby preventing tight junction assembly. Plays a role in regulating monocyte transmigration involved in integrity of epithelial barrier. Ligand for integrin alpha-L/beta-2 involved in memory T-cell and neutrophil transmigration (By similarity). Involved in platelet activation (By similarity).
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O88797
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DAB2_RAT
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Disabled homolog 2 (Adaptor molecule disabled-2) (C9) (Differentially expressed in ovarian carcinoma 2) (DOC-2) (Mitogen-responsive phosphoprotein)
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MSNEVETSTTNGQPDQQAAPKAPSKKEKKKGSEKTDEYLLARFKGDGVKYKAKLIGIDDVPDARGDKMSQDSMMKLKGMAAAGRSQGQHKQRIWVNISLSGIKIIDEKTGVIEHEHPVNKISFIARDVTDNRAFGYVCGGEGQHQFFAIKTGQQAEPLVVDLKDLFQVIYNVKKKEEEKKKVEEANKAEENGSEALMTLDDQANKLKLGVDQMDLFGDMSTPPDLNNPTESRDILLVDLNSEIDTNQNSLRENPFLTNGVTSCSLPRPKPQASFLPESAFSANLNFFPTPNPDPFRDDPFAQPDQSAPSSFHSLTSADQKKANPGSLSTPQSKGPLNGDTDYFGQQFDQISNRTGKQEAQGGPWPYPSSQTQQAVRTQNGVSEKEQNGFHIKSSPNPFVGSPPKGLSVPNGVKQDLESSVQSSAHDSIAIIPPPQSTKPGRGRRTAKSSANDLLASDIFASEPPGQMSPTGQPAVPQANFMDLFKTSAPAPMGSGPLVGLGTVPVTPPQAGPWTPVVFTPSTTVVPGAIISGQPSGFGQPLVFGTTPAVQVWNQPSSFATAASPPPPAVWCPTTSVAPNTWSSTSPLGNPFQSSNIFPPSTISTQSFPQPMMSSVLVTPPQPPPRNGPLKDTLSDAFTGLDPLGDKEVKEVKEMFKDFQLRQPPLVPSRKGETPSSGTSSAFSSYFNNKVGIPQEHVDHDDFDANQLLNKINEPPKPAPRQGVLSGTKSADNSLENPFSKGFSSTNPSVVSQPASSDAHRSPFGNPFA
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Adapter protein that functions as clathrin-associated sorting protein (CLASP) required for clathrin-mediated endocytosis of selected cargo proteins. Can bind and assemble clathrin, and binds simultaneously to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and cargos containing non-phosphorylated NPXY internalization motifs, such as the LDL receptor, to recruit them to clathrin-coated pits. Can function in clathrin-mediated endocytosis independently of the AP-2 complex. Involved in endocytosis of integrin beta-1 this function seems to redundant with the AP-2 complex and seems to require DAB2 binding to endocytosis accessory EH domain-containing proteins such as EPS15, EPS15L1 and ITSN1. Involved in endocytosis of cystic fibrosis transmembrane conductance regulator/CFTR. Involved in endocytosis of megalin/LRP2 lipoprotein receptor during embryonal development. Required for recycling of the TGF-beta receptor. Involved in CFTR trafficking to the late endosome. Involved in several receptor-mediated signaling pathways. Involved in TGF-beta receptor signaling and facilitates phosphorylation of the signal transducer SMAD2. Mediates TFG-beta-stimulated JNK activation. May inhibit the canoniocal Wnt/beta-catenin signaling pathway by stabilizing the beta-catenin destruction complex through a competing association with axin preventing its dephosphorylation through protein phosphatase 1 (PP1). Sequesters LRP6 towards clathrin-mediated endocytosis, leading to inhibition of Wnt/beta-catenin signaling. May activate non-canonical Wnt signaling. In cell surface growth factor/Ras signaling pathways proposed to inhibit ERK activation by interrupting the binding of GRB2 to SOS1 and to inhibit SRC by preventing its activating phosphorylation at 'Tyr-419'. Proposed to be involved in modulation of androgen receptor (AR) signaling mediated by SRC activation seems to compete with AR for interaction with SRC. Plays a role in the CSF-1 signal transduction pathway. Plays a role in cellular differentiation. Involved in cell positioning and formation of visceral endoderm (VE) during embryogenesis and proposed to be required in the VE to respond to Nodal signaling coming from the epiblast. Required for the epithelial to mesenchymal transition, a process necessary for proper embryonic development. May be involved in myeloid cell differentiation and can induce macrophage adhesion and spreading. May act as a tumor suppressor.
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O88799
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ZAN_MOUSE
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Zonadhesin
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MALPVWTLMLLVGAAWGQEQVPAWRPNSPDLGPMVHTSREDSILSKCDFEDNSRPFCDWSQMSADDGDWIRTTGPSLTGTSGPPGGYPNGEGYYLHMDPKTFPQGGVARLRSPDIWEQGPLCVHFAFHMFGLSWGAQLRLLLLRGRKHLRPYVLWKHVNTQSPSWMPTTVTVPADHDIPSWLMFEGMRGNTAYLDISLDGLSIQRGTCNQVCMSQMCTFDTLNDLCGWSWVPTATGAKWTQKKGPTGKQGVGPAEDFSNPGNGYYMLLDSTNARPGQKAVLLSPLSHSRGCMTLSFHYIMHGQGHEEGLFVYATFLGNIRKYTLFSGHPGPDWQAVSVNYTGQGQIQFMVVGMFGNIPEPAIAVDAISIAPCGESFPQCDFEDRVHPFCDWNQVYGDMGHWSWGSKSVPTLIAGSPREFPYGGEHYIFFDSVKLSQEGQSARLVSPPFCAPGGICVEFAYHMYGLGKGTTLKLLLGSPAGSSPIPLWNRVGSQSSGWMNSSVTIPKGYQQPMQLFIEATRGTSTAFVVALNFILISHGPCRVLLQTEIPSSPLLPPTGPSESTVPTLPMEQPTSPTKATTVTIEIPTTPTEEATIPTETTTVPTEVINVSPKETSIPPEVTIPTEVITVSPEEIISPTEVTPVPTDVTAAYVEATNASPEETSVPPEVTILTEVTTVSPEETTVPTEVPIVLIEATAFPTGETTLYTEVPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTVPTEVPIVLIEATASPTGEITLYTEVPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTTLYTEVPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTEITTVSPEETVFPIEGTTLPTEVLTVPIEVTTFPTGETTVPTEVPTVSTEMTGVHTEVTTVFPEETSIPTEVATVLPASIPPEETTTPTEVTTTPPEETTIPAEVTTVPPASIPPEETASLTEVTTTPPEETTTPTEVTTVPPEKTTIPTEVTTVPPASIFPEETTVPPEETTIASEETTVSTQETTLLTEQSAVTQTSIACRPPCPSPPLMPIGPLLSKPPGVSMFSLAPTTGVSTTESCPPNAHIELCACPASCESPKPSCQPPCIPGCVCNPGFLFSNNQCINESSCNCPYNNKHYKPGEEWFTPNCTERCRCLPGSLMECQISQCGTHTVCQLKSDQYQCEPYGKATCLVYGDLHFVTFDERHIGFTGTCTYILTQTCSNSTDHFFRITANTEERGVEGVSCLDKVVISLPETTVTMISGRHTLIGDQEVTLPAILSDDTYVGLSGRFVELRTTFGLRVRWDGDQQLFVTVSSTFSGKLCGFCGNYDGDSSNDNLKSDGMMTHDEEELRLSWQVEEDEDKDWVSSRCQKKKNPPSCDAALGSTMSGPKLCGQLVNPSGPFEACLLHLKASSFLDNCVTDMCSFQGLQQKLCARMSAMTATCQDAGYPVKPWREPQFCPLVCPKNSRYSLCAKPCPETCHPISTTQHCSDKCVEGCECDPGFILSGSECVPSSQCGCTSFQGRYFKLQEQWFNPDCKEICTCESHNHILCKPWKCKAQEACSYKNGVLGCHAQGAATCMVSGDPHYLTFDGALHHFMGTCTYVLTQPCWSKSQENNFVVSATNEIHDGNLEVSYVKAVHVQVFDLKISMFKGQKVVLNNQRVVLPVWPSQGRVTIRLSGIFVLLYTNFGLQVRYDGRHLVEVTVPSSYTGSLCGLCGNYNNNSMDDNLRADMKPAGNSLLLGAAWKILEASDPGCFLAGGKPSRCADSDMDDVWTKKCAILMNPLGPFSNCHEAVPPQASFSSCVYGQCETNGDNLTFCHSLQAYASLCAQAGQVTTWRNSTFCPMRCPPRSSYNPCANSCPATCLTLSTPRDCPTLPCVEGCECQSGHILSGTTCVPLRQCGCSDQDGSYHLLGESWYTEKTCTTLCTCSAHSNITCSPTACKANHVCLRQEGLLRCAAEMGECRISEDSQIVSFDDHSHPIQDTCTYILVKVCHPNTNMPFFMISAKTDINTNGKNKTFGVYQLYIDIFNFHITLQKDHLVLISLINDSIVTLPTTTHIPGVSVMTEDVYTIVTIKDEIQVKFESNNFLDVKIPASSNGKVCGVCGNFNGEEEDELMTPSGELAEDEQEFMNSWKDKSMDPNCQKIEGQNLQVEQQEIMNGKCRPIDFEKAQANCQTALQGPAWAHCSSRVPIKPFLLKCMNSFCEFRELFRALCDSLQSFEDACQNQGLKPPIWRNSSFCPLECPAHSHYTNCLPSCPPSCLDPDSRCEGSGHKVPATCREGCICQPDYVLLNDKCVLRSHCGCKDAQGVFIPAGKTWISEDCTQSCTCMKGSMRCWDFQCPPGTYCKNSNDGSSNCVKISLQCPAHSKFTDCLPPCHPSCSDPDGHCEGISTNAHSNCKEGCVCQPGYVLRNDKCVLRIECGCQHTQGGFIPAGKNWTSRGCSQSCDCMEGVIRCQNFQCPSGTYCQDIEDGTSNCANITLQCPAHSSFTNCLPPCQPSCSDPEGHCGGSTTKAPSACQEGCVCEPDYVVLNNKCVPRIECGCKDAQGVLIPADKIWINKGCTQTCACVTGTIHCRDFQCPSGTYCKDIKDDASNCTEIILQCPDHSLYTHCLPSCLLSCSDPDGLCRGTSPEAPSTCKEGCVCDPDYVLSNDKCVLRIECGCKDAQGVLIPAGKTWINRGCTQSCSCMGGAIQCQNFKCPSEAYCQDMEDGNSNCTSIPLQCPAHSHYTNCLPTCQPSCSDPDGHCEGSSTKAPSACKEGCVCEPDYVMLNNKCVPRIECGCKDTQGVLIPADKTWINRGCTQSCTCRGGAIQCQKYHCSSGTYCKDMEDDSSSCATITLQCPAHSHFTNCLPPCQPSCLDSEGHCEGSTTKAPSACQEGCVCEPDYVVLNNKCVPRIECGCKDAQGVLIPADKTWINRGCTQSCTCKGGAIQCQKFQCPSETYCKDIEDGNSNCTRISLQCPANSNFTSCLPSCQPSCSNTDVHCEGSSPNTLSSCREGCVCQSGYVLHNDKCILRNQCGCKDAQGALIPEGKTWITSGCTQSCNCTGGAIQCQNFQCPLKTYCKDLKDGSSNCTNIPLQCPAHSRYTNCLPSCPPLCLDPEGLCEGTSPKVPSTCREGCICQPGYLMHKNKCVLRIFCGCKNTQGAFISADKTWISRGCTQSCTCPAGAIHCRNFKCPSGTYCKNGDNGSSNCTEITLQCPTNSQFTDCLPSCVPSCSNRCEVTSPSVPSSCREGCLCNHGFVFSEDKCVPRTQCGCKDARGAIIPAGKTWTSKGCTQSCACVEGNIQCQNFQCPPETYCKDNSEGSSTCTKITLQCPAHTQYTSCLPSCLPSCLDPEGLCKDISPKVPSTCKEGCVCQSGYVLNSDKCVLRAECDCKDAQGALIPAGKTWTSPGCTQSCACMGGAVQCQSSQCPPGTYCKDNEDGNSNCAKITLQCPAHSLFTNCLPPCLPSCLDPDGLCKGASPKVPSTCKEGCICQSGYVLSNNKCLLRNRCGCKDAHGALIPEDKTWVSRGCTQSCVCTGGSIQCLSSQCPPGAYCKDNEDGSSNCARIPPQCPANSHYTDCFPPCPPSCSDPEGHCEASGPRVLSTCREGCLCNPGFVLDRDKCVPRVECGCKDAQGALIPSGKTWTSPGCTQSCACMGGVVQCQSSQCPPGTYCKDNEDGNSNCAKITLQCPTHSNYTDCLPFCLPSCLDPSALCGGTSPKGPSTCKEGCVCQPGYVLDKDKCILKIECGCRDTQGAVIPAGKTWLSTGCIQSCACVEGTIQCQNFQCPPGTYCNHNNNCAKIPLQCPAHSHFTSCLPSCPPSCANLDGSCEQTSPKVPSTCKEGCLCQPGYFLNNGKCVLQTHCDCKDAEGGLVPAGKTWTSKDCTQSCACTGGAVQCQNFQCPLGTYCKDSGDGSSNCTKIHKGAMGDGVLMAGGIRALQCPAHSHFTSCLPSCPPSCSNLDGSCVESNFKAPSVCKKGCICQPGYLLNNDKCVLRIQCGCKDTQGGLIPAGRTWISSDCTKSCSCMGGIIQCRDFQCPPGTYCKESNDSSRTCAKIPLQCPAHSHYTNCLPACSRSCTDLDGHCEGTSPKVPSPCKEGCLCQPGYVVHNHKCVLQIHCGCKDAQGGFVPAGKTWISRGCTQSCACVGGAVQCHNFTCPTGTQCQNSSCSKITVQCPAHSQYTTCLPSCLPSCFDPEGLCGGASPRAPSTCREGCVCEADYVLREDKCVLRTQCGCKDAQGDLIPANKTWLTRGCAQKCTCKGGNIHCWNFKCPLGTECKDSVDGGSNCTKIALQCPAHSHHTYCLPSCIPSCSNVNDRCESTSLQRPSTCIEGCLCHSGFVFSKDKCVPRTQCGCKDSQGTLIPAGKNWITTGCSQRCTCTGGLVQCHDFQCPSGAECQDIEDGNSNCVEITVQCPAHSHYSKCLPPCQPSCSDPDGHCEGTSPEAPSTCEEGCVCEPDYVLSNDKCVPSSECGCKDAHGVLIPESKTWVSRGCTKNCTCKGGTVQCHDFSCPTGSRCLDNNEGNSNCVTYALKCPAHSLYTNCLPSCLPSCSDPEGLCGGTSPEVPSTCKEGCICQSGYVLHKNKCMLRIHCDCKDFQGSLIKTGQTWISSGCSKICTCKGGFFQCQSYKCPSGTQCEESEDGSSNCVSSTMKCPANSLYTHCLPTCLPSCSNPDGRCEGTSHKAPSTCREGCVCQPGYLLNKDTCVHKNQCGCKDIRGNIIPAGNTWISSDCTQSCACTDGVIQCQNFVCPSGSHCQYNEDGSSDCAANKLERCTIFGDPYYLTFDGFTYHFLGRMNYYLIKTVDKLPRGIEPLIMEGRNKISPKGSSTLHEVTTIVYGYKIQLQEELVVLVNDEKVAVPYNPNEHLRVMLRAQRLLLVTDFEMVLDFDGKHSAVISLPTTYRGLTRGLCGNYDRDQSNELMLPSGVLTSNVHVFGNSWEVKAQHAFFRFPRALPEDEERDEEPDLLQSECSQEQTALISSTQACRVLVDPQGPFAACHQIIAPEPFEQRCMLDMCTGWKTKEEEELRCRVLSGYAIICQEAGANMTGWRDHTHCAMTCPANTVYQRCMTPCPASCAKFVTPKVCEGPCVEGCASLPGYIYSDTQSLPVTHCGCTADGIYYKLGDSFVTNDCSQHCTCASQGILLCEPYGCRAGESCMVANFTRGCFQDSPCLQNPCHNDGRCEEQGATFICHCDFGYGGEFCTEPQDITTRKKIEASSLVAILPGVLVMVLVPVLLPRVYVYMATRTTMGRRRMKRKEKKLLRQSRLRLEDADVPEPTFKATEF
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Binds in a species-specific manner to the zona pellucida of the egg. May be involved in gamete recognition and/or signaling.
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O88801
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HOME2_RAT
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Homer protein homolog 2 (Homer-2) (Cupidin) (VASP/Ena-related gene up-regulated during seizure and LTP 2) (Vesl-2)
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MGEQPIFTTRAHVFQIDPSTKKNWVPASKQAVTVSYFYDVTRNSYRIISVDGAKVIINSTITPNMTFTKTSQKFGQWADSRANTVFGLGFSSEQQLTKFAEKFQEVREAARLARDKSQEKIETSSNHSQESGCETPSSTQASSVNGTDDEKASHASPADTHLKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEINREKEKNTQLKRRIEELESEVREKEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGELKSFLEVLDGKIDDLHDFRRGLSKLGTDN
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Postsynaptic density scaffolding protein. Binds and cross-links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2, SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with ER-associated ITPR1 receptors, it aids the coupling of surface receptors to intracellular calcium release. May also couple GRM1 to PI3 kinase through its interaction with AGAP2. Isoforms can be differently regulated and may play an important role in maintaining the plasticity at glutamatergic synapses. Required for normal hearing (By similarity). Negatively regulates T cell activation by inhibiting the calcineurin-NFAT pathway. Acts by competing with calcineurin/PPP3CA for NFAT protein binding, hence preventing NFAT activation by PPP3CA (By similarity).
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O88807
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PADI4_RAT
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Protein-arginine deiminase type-4 (EC 3.5.3.15) (PAD-R4) (Peptidylarginine deiminase IV) (Peptidylarginine deiminase type alpha) (Protein-arginine deiminase type IV)
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MAQGAVIHVAPEEPTHAVCVVGTATPLDIRGSAPRGSTSFSITASPEVVVDVIHGPPSKKSTTGASKWPLDPKLEVTLQMKAASSRIDDQKVRISYYGPKTSSTQALLYLTGVELSLSADVTRTGKAKPAPAGKDQSTWTWGPDGHGAILLVNCDKEDPKSSGMDFEDDKVLDNKDLQDMSPMTLSTKTPKDFFDKYQLVLQVPKAKMNKVRVFRATRGKLPSRYKVVLGPQQFSHRLELLGGQHSTDFYVEGLAFPDADFKGLIPLTISLLDKSNPELPEALVFQDTVMFRVAPWIMTPNTQPPQEVYVCRFSDNEDFLKSLATFTKKAKCKLTVCPEEENQDDQWMQDEMEIGYIQAPHKTLPVVFDSPRDRGLKDFPVKRVMGPNFGYVTRGLYRAEVTGLDAFGNLEVSPPVTVRGKEYPLGRILIGSSGYSSSESRDMHQILQDFLGAQQVQAPVRLFSDWLFVGHVDEFLSFVPARGKQGFRLLLSSPRACYQMFQELQTEGHGEASLFEGLKRKRQTISDILSSQKLRDQNAYVESCIDWNREVLKRELGLTEGDIIDIPQLFRIVGNSRGNPKAEAFFPNMVNMLVLGKHLGIPKPFGPIINGRCCLEEKVCSLLEPLGLHCTFINDFYSYHMYHGEVHCGTNVRRKPFAFKWWHMVP
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Catalyzes the citrullination/deimination of arginine residues of proteins such as histones, thereby playing a key role in histone code and regulation of stem cell maintenance. Citrullinates histone H1 at 'Arg-54' (to form H1R54ci), histone H3 at 'Arg-2', 'Arg-8', 'Arg-17' and/or 'Arg-26' (to form H3R2ci, H3R8ci, H3R17ci, H3R26ci, respectively) and histone H4 at 'Arg-3' (to form H4R3ci). Acts as a key regulator of stem cell maintenance by mediating citrullination of histone H1: citrullination of 'Arg-54' of histone H1 (H1R54ci) results in H1 displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance. Promotes profound chromatin decondensation during the innate immune response to infection in neutrophils by mediating formation of H1R54ci (By similarity). Required for the formation of neutrophil extracellular traps (NETs) NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation (By similarity). Citrullination of histone H3 prevents their methylation by CARM1 and HRMT1L2/PRMT1 and represses transcription. Citrullinates EP300/P300 at 'Arg-2142', which favors its interaction with NCOA2/GRIP1 (By similarity).
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O88809
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DCX_MOUSE
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Neuronal migration protein doublecortin (Doublin) (Lissencephalin-X) (Lis-X)
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MELDFGHFDERDKASRNMRGSRMNGLPSPTHSAHCSFYRTRTLQALSNEKKAKKVRFYRNGDRYFKGIVYAVSSDRFRSFDALLADLTRSLSDNINLPQGVRYIYTIDGSRKIGSMDELEEGESYVCSSDNFFKKVEYTKNVNPNWSVNVKTSANMKAPQSLASSNSAQARENKDFVRPKLVTIIRSGVKPRKAVRVLLNKKTAHSFEQVLTDITEAIKLETGVVKKLYTLDGKQVTCLHDFFGDDDVFIACGPEKFRYAQDDFSLDENECRVMKGNPSAAAGPKASPTPQKTSAKSPGPMRRSKSPADSGNDQDANGTSSSQLSTPKSKQSPISTPTSPGSLRKHKVDLYLPLSLDDSDSLGDSM
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Microtubule-associated protein required for initial steps of neuronal dispersion and cortex lamination during cerebral cortex development. May act by competing with the putative neuronal protein kinase DCLK1 in binding to a target protein. May in that way participate in a signaling pathway that is crucial for neuronal interaction before and during migration, possibly as part of a calcium ion-dependent signal transduction pathway. May participate along with PAFAH1B1/LIS-1 in a distinct overlapping signaling pathway that promotes neuronal migration.
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O88811
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STAM2_MOUSE
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Signal transducing adapter molecule 2 (STAM-2) (Hrs-binding protein)
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MPLFTANPFEQDVEKATNEYNTTEDWSLIMDICDRVGSTPSGAKDCLKAIMKRVNHKVPHVALQALTLLGACVANCGKIFHLEVCSRDFATEVRSVIKNKAHPKVCEKLKSLMVEWSEEFQKDPQFSLISATIKSMKEEGVTFPSAGSQTVAAAAKNGTSLNKNKEDEDIAKAIELSLQEQKQQYTETKALYPPAESQLNNKAARRVRALYDFEAVEDNELTFKHGELITVLDDSDANWWQGENHRGTGLFPSNFVTTDLSTEVETATVDKLNVIDDDVEEIKKSEPEPVYIDEGKMDRALQILQSIDPKESKPDSQDLLDLEDVCQQMGPMIDEKLEEIDRKHSELSELNVKVLEALDLYNKLVNEAPVYSVYSKLHPAHYPPAAAGVPVQTYPVQSHGGNYLGHGIHQVSVAQNYNLGPDPMGSLRSLPPNMNSVTAHTVQPPYLSTGQDTVSNPSYMNQSSRLQAAAGTAAYTQPVGMSTDVSSFQNTASGLPQLAGFPVAVPAPVAAQPQASYHQQPLL
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Involved in intracellular signal transduction mediated by cytokines and growth factors. Upon IL-2 and GM-CSL stimulation, it plays a role in signaling leading to DNA synthesis and MYC induction. May also play a role in T-cell development. Involved in down-regulation of receptor tyrosine kinase via multivesicular body (MVBs) when complexed with HGS (ESCRT-0 complex). The ESCRT-0 complex binds ubiquitin and acts as sorting machinery that recognizes ubiquitinated receptors and transfers them to further sequential lysosomal sorting/trafficking processes (By similarity). {ECO:0000250, ECO:0000269|PubMed:12972556}.
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O88813
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ACSL5_RAT
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Long-chain-fatty-acid--CoA ligase 5 (EC 6.2.1.3) (Arachidonate--CoA ligase) (EC 6.2.1.15) (Long-chain acyl-CoA synthetase 5) (LACS 5)
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MLFIFNFLFSPLPTPALICLLTFGTAIFLWLINRPQPVLPLIDLDNQSVGIEGGARRGAFQKNNDLILYYFSDAKTLYEVFQRGLAVSDNGPCLGYRKPNQPYKWISYKQVSDRAEYLGSCLLHKGYKPSQDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVICDTPQKATMLIENVEKDLTPGLKTVILMDPFDDDLMKRGEKCGIEMLSLHDAENLGKENFKKPMPPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFLEPIFQPTPEDVTISYLPLAHMFERLVQGVIFSCGGKIGFFQGDIRLLPDDMKALKPTVFPTVPRLLNRVYDKVQNEAKTPLKKFLLNLAIISKFNEVRNGIIRRNSLWDKLVFSKIQSSLGGKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTAGCSITSPGDWTAGHVGTPVSCNFVKLEDVADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIIDRKKNIFKLAQGEYIAPEKIENVYSRSRPILQVFVHGESLRSFLIGVVVPDPESLPSFAAKIGVKGSFEELCQNQCVKKAILEDLQKVGKEGGLKSFEQVKSIFVHPEPFSIENGLLTPTLKAKRVELAKFFQTQIKSLYESIEE
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Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoAs for both synthesis of cellular lipids, and degradation via beta-oxidation. ACSL5 may sensitize epithelial cells to apoptosis specifically triggered by the death ligand TRAIL at the villus tip of the crypt-villus axis of the small intestine (By similarity). May have a role in the survival of glioma cells (By similarity). May activate fatty acids from exogenous sources for the synthesis of triacylglycerol destined for intracellular storage. It was suggested that it may also stimulate fatty acid oxidation. Utilizes a wide range of saturated fatty acids with a preference for C16-C18 unsaturated fatty acids. {ECO:0000250, ECO:0000269|PubMed:16263710, ECO:0000269|PubMed:17761945, ECO:0000269|PubMed:28209804, ECO:0000269|PubMed:9722683}.
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O88816
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SNAT_MOUSE
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Serotonin N-acetyltransferase (Serotonin acetylase) (EC 2.3.1.87) (Aralkylamine N-acetyltransferase) (AA-NAT)
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MLNINSLKPEALHLPLGTSEFLGCQRRHTLPASEFRCLTPEDATSAFEIEREAFISVSGTCPLYLDEIRHFLTLCPELSLGWFEEGCLVAFIIGSLWDKERLTQESLTLHRPGGRTAHLHVLAVHRTFRQQGKGSVLLWRYLHHLGSQPAVRRAVLMCEDALVPFYEKFGFQAVGPCAITVGSLTFTELQCSLRCHAFLRRNSGC
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Controls the night/day rhythm of melatonin production in the pineal gland. Catalyzes the N-acetylation of serotonin into N-acetylserotonin, the penultimate step in the synthesis of melatonin.
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O88819
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FUT9_MOUSE
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4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9 (EC 2.4.1.152) (Fucosyltransferase 9) (Fucosyltransferase IX) (Fuc-TIX) (FucT-IX) (Galactoside 3-L-fucosyltransferase)
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MTSTSKGILRPFLIVCIILGCFMACLLIYIKPTNSWVFSPMESASSVLKMKNFFSTKTDYFNETTILVWVWPFGQTFDLTSCQAMFNIQGCHLTTDRSLYNKSHAVLIHHRDISWDLTNLPQQARPPFQKWIWMNLESPTHTPQKSGIEHLFNLTLTYRRDSDIQVPYGFLTVSTNPFVFEVPSKEKLVCWVVSNWNPEHARVKYYNELSKSIEIHTYGQAFGEYVNDKNLIPTISTCKFYLSFENSIHKDYITEKLYNAFLAGSVPVVLGPSRENYENYIPADSFIHVEDFNSPSELAKYLKEVDKNNKLYLSYFNWRKDFTVNLPRFWESHACLACDHVKRHQEYKSVGNLEKWFWN
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Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the N-acetyl glucosamine (GlcNAc) of a distal lactosamine unit of a glycoprotein or a glycolipid-linked polylactosamine chains through an alpha-1,3 glycosidic linkage and participates in particular to the Lewis x (Lex)/CD15 epitope biosynthesis in neurons which allows cell differentiation, cell adhesion, and initiation of neurite outgrowth. Also fucosylates di-, tri- and tetraantennary N-glycans linked to glycoproteins and the inner lactosamine unit of the alpha2,3-sialylated polylactosamine resulting in sLex (CD15s) epitope synthesis (By similarity). Furthermore, it is capable of synthesizing Lewis a (Lea), although to a lesser extent than Lex and Lewis y (Ley) and to confer SELE-dependent, but not SELL- and SELP-selectin-dependent, cell rolling and adhesion by enhancing Lex and sLex synthesis (By similarity). May also fucosylate the internal LacNAc unit of the polylactosamine chain to form VIM-2 antigen that serves as recognition epitope for SELE.
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O88824
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JTB_MOUSE
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Protein JTB
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MLAGAGRRGLPRAGHLCWLLCAFTLKLCEAEAPVREEKLSVSTSTSPCWLAEEFVVTEECTPCSNFQIKTTPECGSTGYVEKITCSSSKRNEFKSCRSALLEQHLFWKFEGVVVAVALVFACLVIVRQRQLDRKALEKVRKQIESI
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Required for normal cytokinesis during mitosis. Plays a role in the regulation of cell proliferation. May be a component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Increases AURKB activity (By similarity). Inhibits apoptosis induced by TGFB1. Overexpression induces swelling of mitochondria and reduces mitochondrial membrane potential. {ECO:0000250, ECO:0000269|PubMed:17369841}.
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O88829
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SIAT9_MOUSE
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Lactosylceramide alpha-2,3-sialyltransferase (EC 2.4.3.9) (CMP-NeuAc:lactosylceramide alpha-2,3-sialyltransferase) (Ganglioside GM3 synthase) (ST3Gal V) (ST3GalV) (Sialyltransferase 9)
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MHTEAVGGAARRPQKLRSQAAAPACRAMPSEFTSAKLRSDCSRTSLQWYTRTQHKMRRPSLLIKDICKCTLVAFGVWLLYILILNYTAEECDMKRMHYVDPDRIKRAQSYAQEVLQKECRPRYAKTAMALLFEDRYSINLEPFVQKVPTASEAELKYDPPFGFRKFSSKVQSLLDMLPEHDFPEHLRAKACKRCVVVGNGGILHGLELGHALNQFDVVIRLNSAPVEGYSEHVGNKTTIRMTYPEGAPLSDVEYYANDLFVTVLFKSVDFKWLQAMVKNESLPFWVRLFFWKQVAEKVPLQPKHFRILNPVIIKETAFDILQYSEPQSRFWGHDKNIPTIGVIAVVLATHLCDEVSLAGFGYDLSQPRTPLHYFDSQCMGAMHWQVMHNVTTETKFLLKLLKEGVVEDLSGGIH
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(Microbial infection) Gangliosides GD1b and GT1b (derived from GM3) may serve as receptors for some C.botulinum neurotoxins (minimally types BoNT/A, B, C). Transfers the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc to the non-reducing terminal galactose (Gal) of glycosphingolipids forming gangliosides (important molecules involved in the regulation of multiple cellular processes, including cell proliferation and differentiation, apoptosis, embryogenesis, development, and oncogenesis). Mainly involved in the biosynthesis of ganglioside GM3 but can also use different glycolipids as substrate acceptors such as D-galactosylceramide (GalCer), asialo-GM2 (GA2) and asialo-GM1 (GA1), although less preferentially than beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer (LacCer) (By similarity).
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O88831
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KKCC2_RAT
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Calcium/calmodulin-dependent protein kinase kinase 2 (CaM-KK 2) (CaM-kinase kinase 2) (CaMKK 2) (EC 2.7.11.17) (Calcium/calmodulin-dependent protein kinase kinase beta) (CaM-KK beta) (CaM-kinase kinase beta) (CaMKK beta)
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MSSCVSSQPTSDRAAPQDELGSGGVSRESQKPCEALRGLSSLSIHLGMESFIVVTECEPGRGVDLSLARDQPLEADGQELPLDASEPESRSLLSGGKMSLQERSQGGPASSSSLDMNGRCICPSLSYSPASSPQSSPRMPRRPTVESHHVSITGLQDCVQLNQYTLKDEIGKGSYGVVKLAYNENDNTYYAMKVLSKKKLIRQAGFPRRPPPRGTRPAPGGCIQPRGPIEQVYQEIAILKKLDHPNVVKLVEVLDDPNEDHLYMVFELVNQGPVMEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDIKPSNLLVGEDGHIKIADFGVSNEFKGSDALLSNTVGTPAFMAPESLSETRKIFSGKALDVWAMGVTLYCFVFGQCPFMDERIMCLHSKIKSQALEFPDQPDIAEDLKDLITRMLDKNPESRIVVPEIKLHPWVTRHGAEPLPSEDENCTLVEVTEEEVENSVKHIPSLATVILVKTMIRKRSFGNPFEGSRREERSLSAPGNLLTKKPTREWEPLSEPKEARQRRQPPGPRASPCGGGGSALVKGGPCVESCGAPAPGSPPRTPPQQPEEAMEPE
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Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Phosphorylates CAMK1 and CAMK4. Phosphorylates CAMK1D (By similarity). Seems to be involved in hippocampal activation of CREB1 (By similarity). Efficiently phosphorylates 5'-AMP-activated protein kinase (AMPK) trimer, including that consisting of PRKAA1, PRKAB1 and PRKAG1. This phosphorylation is stimulated in response to Ca(2+) signals. May play a role in neurite growth. Isoform 2 may promote neurite elongation, while isoform 1 may promoter neurite branching. {ECO:0000250, ECO:0000269|PubMed:21807092, ECO:0000269|PubMed:21957496, ECO:0000269|PubMed:8631893, ECO:0000269|PubMed:9822657}.
|
O88833
|
CP4AA_MOUSE
|
Cytochrome P450 4A10 (CYPIVA10) (Cytochrome P450-LA-omega 1) (Cytochrome P452) (Lauric acid omega-hydroxylase) (Long-chain fatty acid omega-monooxygenase) (EC 1.14.14.80)
|
MSVSALSPTRFADSLSGFLQVASVLGLLLLLVKAVQFYLHRQWLLKAFQQFPSPPFHWFFGHEKFKGDQELQEIVSCIENFPSAFPRWFWGSKAYLTVYDPDYMKVILGRSDPKANGAYRLLAPWIGYGLLLLNGQPWFQHRRMLTPAFHYDILKPYVKNMADSIRLMLDKWERLADQDSSIEIFQHISLMTLDTVMKCAFSHKGSVQVDGNYRTYLQAIGDLNNLFHSRVRNIFHQNDTIYKLSSNGRLAKQACQLAHDHTDGVIKLRKDQLQDEGELEKIKKKRRLDFLDILLFARMENGDSMSDKDLRAEVDTFMFEGHDTTASGVSWIFYALATHPDHQQRCREEVQSLLGDGSSITWDHLDQIPYTTMCIKEALRLYPPVPGIVRELSTSVTFPDGRSLPKGVQVTLSIYGLHHNPKVWPNPEVFDPSRFAPDSPRHSHSFLPFSGGARNCIGKQFAMSELKVIVALTLLRFELLPDPTRVPMPLARLVLKSKNGIYLHLKKLH
|
A cytochrome P450 monooxygenase involved in the metabolism of fatty acids. Catalyzes predominantly the oxidation of the terminal carbon (omega-oxidation) of long-chain fatty acids (By similarity). Acts as a major omega-hydroxylase for dodecanoic (lauric) acid in liver (By similarity). In kidney, may play an important role in omega-hydroxylation of (5Z,8Z,11Z,14Z)-eicosatetraenoic acid (arachidonate) to 20-hydroxyeicosatetraenoic acid (20-HETE), a signaling molecule acting both as vasoconstrictive and natriuretic with overall effect on arterial blood pressure (By similarity). Also participates in the formation of anti-inflammatory hydroxyepoxyeicosatrienoic acids (HEETs) in kidney by converting 8,9-epoxyeicosatrienoic acid (EET) to 20,8,9-HEET, an activator of PPARA. Displays substantially lower fatty acid omega-1 hydroxylase activity (By similarity). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR NADPH-ferrihemoprotein reductase).
|
O88838
|
SPSB2_MOUSE
|
SPRY domain-containing SOCS box protein 2 (SSB-2) (Gene-rich cluster protein C9)
|
MGQTALARGSSSTPTSQALYSDFSPPEGLEELLSAPPPDLVAQRHHGWNPKDCSENIDVKEGGLCFERRPVAQSTDGVRGKRGYSRGLHAWEISWPLEQRGTHAVVGVATALAPLQADHYAALLGSNSESWGWDIGRGKLYHQSKGLEAPQYPAGPQGEQLVVPERLLVVLDMEEGTLGYSIGGTYLGPAFRGLKGRTLYPSVSAVWGQCQVRIRYMGERRVEEPQSLLHLSRLCVRHALGDTRLGQISTLPLPPAMKRYLLYK
|
Substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Negatively regulates nitric oxide (NO) production and limits cellular toxicity in activated macrophages by mediating the ubiquitination and proteasomal degradation of NOS2. Acts as a bridge which links NOS2 with the ECS E3 ubiquitin ligase complex components ELOC and CUL5 (By similarity).
|
O88839
|
ADA15_MOUSE
|
Disintegrin and metalloproteinase domain-containing protein 15 (ADAM 15) (EC 3.4.24.-) (AD56) (Metalloprotease RGD disintegrin protein) (Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 15) (MDC-15) (Metargidin)
|
MRLALLWALGLLGAGSPRPSPPLPNIGGTEEEQQASPERTLSGSMESRVVQDSPPMSLADVLQTGLPEALRISLELDSESHVLELLQNRDLIPGRPTLVWYQPDGTRMVSEGYSLENCCYRGRVQGHPSSWVSLCACSGIRGLIVLSPERGYTLELGPGDLQRPVISRIQDHLLLGHTCAPSWHASVPTRAGPDLLLEQHHAHRLKRDVVTETKIVELVIVADNSEVRKYPDFQQLLNRTLEAALLLDTFFQPLNVRVALVGLEAWTQHNLIEMSSNPAVLLDNFLRWRRTDLLPRLPHDSAQLVTVTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDSPGHSCPCPGPAPAKSCIMEASTDFLPGLNFSNCSRQALEKALLEGMGSCLFERQPSLAPMSSLCGNMFVDPGEQCDCGFPDECTDPCCDHFTCQLRPGAQCASDGPCCQNCKLHPAGWLCRPPTDDCDLPEFCPGDSSQCPSDIRLGDGEPCASGEAVCMHGRCASYARQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRSPGGSYMPCAPRDVMCGQLQCQWGRSQPLLGSVQDRLSEVLEANGTQLNCSWVDLDLGNDVAQPLLALPGTACGPGLVCIGHRCQPVDLLGAQECRRKCHGHGVCDSSGHCRCEEGWAPPDCMTQLKATSSLTTGLLLSLLLLLVLVLLGASYWHRARLHQRLCQLKGSSCQYRAPQSCPPERPGPPQRAQQMTGTKQASVVSFPVPPSRPLPPNPVPKKLQAALADRSNPPTRPLPADPVVRRPKSQGPTKPPPPRKPLPANPQGQHPPGDLPGPGDGSLPLVVPSRPAPPPPAASSLYL
|
Active metalloproteinase with gelatinolytic and collagenolytic activity. Plays a role in the wound healing process. Mediates both heterotypic intraepithelial cell/T-cell interactions and homotypic T-cell aggregation. Inhibits beta-1 integrin-mediated cell adhesion and migration of airway smooth muscle cells. Suppresses cell motility on or towards fibronectin possibly by driving alpha-v/beta-1 integrin (ITAGV-ITGB1) cell surface expression via ERK1/2 inactivation. Cleaves E-cadherin in response to growth factor deprivation. Plays a role in glomerular cell migration (By similarity). Plays a role in pathological neovascularization. May play a role in cartilage remodeling. May be proteolytically processed, during sperm epididymal maturation and the acrosome reaction. May play a role in sperm-egg binding through its disintegrin domain. Interactions with egg membrane could be mediated via binding between the disintegrin-like domain to one or more integrin receptors on the egg. {ECO:0000250, ECO:0000269|PubMed:11882657, ECO:0000269|PubMed:12897135, ECO:0000269|PubMed:15818704, ECO:0000269|PubMed:18390692}.
|
O88843
|
CRADD_MOUSE
|
Death domain-containing protein CRADD (Caspase and RIP adapter with death domain) (RIP-associated protein with a death domain)
|
MEARDKQVLRSLRLELGAEVLVEGLVLQYLYQEGILTENHIQEIKAQTTGLRKTMLLLDILPSRGPKAFDTFLDSLQEFPWVREKLEKAREEVTAELPTGDWMAGIPSHILSSSPSDQQINQLAQRLGPEWEPVVLSLGLSQTDIYRCKANHPHNVHSQVVEAFVRWRQRFGKQATFLSLHKGLQAVEADPSLLQHMLE
|
Adapter protein that associates with PIDD1 and the caspase CASP2 to form the PIDDosome, a complex that activates CASP2 and triggers apoptosis. Also recruits CASP2 to the TNFR-1 signaling complex through its interaction with RIPK1 and TRADD and may play a role in the tumor necrosis factor-mediated signaling pathway.
|
O88844
|
IDHC_MOUSE
|
Isocitrate dehydrogenase [NADP] cytoplasmic (IDH) (IDH1) (EC 1.1.1.42) (Cytosolic NADP-isocitrate dehydrogenase) (IDPc) (NADP(+)-specific ICDH) (Oxalosuccinate decarboxylase)
|
MSRKIQGGSVVEMQGDEMTRIIWELIKEKLILPYVELDLHSYDLGIENRDATNDQVTKDAAEAIKKYNVGVKCATITPDEKRVEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVTGWVKPIIIGRHAYGDQYRATDFVVPGPGKVEITYTPKDGTQKVTYMVHDFEEGGGVAMGMYNQDKSIEDFAHSSFQMALSKGWPLYLSTKNTILKKYDGRFKDIFQEIYDKKYKSQFEAQKICYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVAQGYGSLGMMTSVLICPDGKTVEAEAAHGTVTRHYRMYQKGQETSTNPIASIFAWSRGLAHRAKLDNNTELSFFAKALEDVCIETIEAGFMTKDLAACIKGLPNVQRSDYLNTFEFMDKLGENLKAKLAQAKL
|
Catalyzes the NADP(+)-dependent oxidative decarboxylation of isocitrate (D-threo-isocitrate) to 2-ketoglutarate (2-oxoglutarate), which is required by other enzymes such as the phytanoyl-CoA dioxygenase. Plays a critical role in the generation of NADPH, an important cofactor in many biosynthesis pathways. May act as a corneal epithelial crystallin and may be involved in maintaining corneal epithelial transparency (By similarity).
|
O88845
|
AKA10_MOUSE
|
A-kinase anchor protein 10, mitochondrial (AKAP-10) (Dual specificity A kinase-anchoring protein 2) (D-AKAP-2) (Protein kinase A-anchoring protein 10) (PRKA10)
|
MRGAGPSPRHSPRALRPDPGPAMSFFRRKVKGKEQEKTLDVKSTKASVAVHSPQKSTKNHALLEAAGPSHVAINAISANMDSFSSSRTATLKKQPSHMEAAHFGDLGRSCLDYQTQETKSSLSKTLEQVLRDTVVLPYFLQFMELRRMEHLVKFWLEAESFHSTTWSRIRAHSLNTVKQSSLAEPVSPSKRHETPASSVTEALDRRLGDSSSAPLLVTQSEGTDLSSRTQNPQNHLLLSQEGHSARSLHREVARTGSHQIPTDSQDSSSRLAVGSRNSCSSPLRELSEKLMKSIEQDAVNTFTKYISPDAAKPIPITEAMRNDIIAKICGEDGQVDPNCFVLAQAVVFSAMEQEHFSEFLRSHHFCKYQIEVLTSGTVYLADILFCESALFYFSEYMEKEDAVNILQFWLAADNFQSQLAAKKGQYDGQEAQNDAMILYDKYFSLQATHPLGFDDVVRLEIESNICREGGPLPNCFTTPLRQAWTTMEKVFLPGFLSSNLYYKYLNDLIHSVRGDEFLGGNVSLAAHGSVCLPEESHSGGSDGSTAQSSVKKASIKILKNFDEAIIVDAASLDPESLYQRTYAGKMSFGRVSDLGQFIRESEPEPDVKKSKGFMFSQAMKKWVQGNTDEAQEELAWKIAKMIVSDVMQQAHHDQPLEKSTKL
|
Differentially targeted protein that binds to type I and II regulatory subunits of protein kinase A and anchors them to the mitochondria or the plasma membrane. Although the physiological relevance between PKA and AKAPS with mitochondria is not fully understood, one idea is that BAD, a proapoptotic member, is phosphorylated and inactivated by mitochondria-anchored PKA. It cannot be excluded too that it may facilitate PKA as well as G protein signal transduction, by acting as an adapter for assembling multiprotein complexes. With its RGS domain, it could lead to the interaction to G-alpha proteins, providing a link between the signaling machinery and the downstream kinase.
|
O88846
|
RNF4_RAT
|
E3 ubiquitin-protein ligase RNF4 (EC 2.3.2.27) (RING finger protein 4) (Small nuclear ring finger protein) (Protein SNURF)
|
MSTRNPQRKRRGGAVNSRQTQKRTRETTSTPEISLEAEPIELVETVGDEIVDLTCESLEPVVVDLTHNDSVVIVEERRRPRRNGRRLRQDHADSCVVSSDDEELSKDKDVYVTTHTPRSTKDEGTTGLRPSGTVSCPICMDGYSEIVQNGRLIVSTECGHVFCSQCLRDSLKNANTCPTCRKKINHKRYHPIYI
|
E3 ubiquitin-protein ligase which binds polysumoylated chains covalently attached to proteins and mediates 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination of those substrates and their subsequent targeting to the proteasome for degradation. Regulates the degradation of several proteins including PML and the transcriptional activator PEA3. Involved in chromosome alignment and spindle assembly, it regulates the kinetochore CENPH-CENPI-CENPK complex by targeting polysumoylated CENPI to proteasomal degradation (By similarity). Regulates the cellular responses to hypoxia and heat shock through degradation of respectively EPAS1 and PARP1 (By similarity). Alternatively, it may also bind DNA/nucleosomes and have a more direct role in the regulation of transcription for instance enhancing basal transcription and steroid receptor-mediated transcriptional activation. Catalyzes ubiquitination of sumoylated PARP1 in response to PARP1 trapping to chromatin, leading to PARP1 removal from chromatin by VCP/p97 (By similarity).
|
O88848
|
ARL6_MOUSE
|
ADP-ribosylation factor-like protein 6
|
MGLLDRLSGLLGLKKKEVHVLCLGLDNSGKTTIINKLKPSNAQSQDIVPTIGFSIEKFKSSSLSFTVFDMSGQGRYRNLWEHYYKDGQAIIFVIDSSDKLRMVVAKEELDTLLNHPDIKHRRIPILFFANKMDLRDSVTSVKVSQLLCLESIKDKPWHICASDAIKGEGLQEGVDWLQDQIQAVKT
|
Involved in membrane protein trafficking at the base of the ciliary organelle (By similarity). Mediates recruitment onto plasma membrane of the BBSome complex which would constitute a coat complex required for sorting of specific membrane proteins to the primary cilia (By similarity). Together with BBS1, is necessary for correct trafficking of PKD1 to primary cilia. Together with the BBSome complex and LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation (By similarity). May regulate cilia assembly and disassembly and subsequent ciliary signaling events such as the Wnt signaling cascade (By similarity). Isoform 2 may be required for proper retinal function and organization.
|
O88850
|
HIPK3_RAT
|
Homeodomain-interacting protein kinase 3 (EC 2.7.11.1) (Androgen receptor-interacting nuclear protein kinase) (ANPK)
|
MASQVLVYPPYVYQTQSSAFCSVKKLKVEPSGCVFQERACPQIHVNGRHFGNPLPSTKGSAFQTKIPFSKPRGHSFSLQAGAIVVKDTAGATKVIAAQAQQAGVEAPRAVVWRNRLHFLGGPQRCGLKRKSEELDNHSGAMQIVDELSILPAMLQTNMGNPVTVVTATTGSKQNCTSGEGDYQLVQHEVLCSVKNTYEVLDFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILARLSTENADEYNFVRAYECFQHRNHTCLVFEMLEQNLYDFLKQNKFSPLPLKVIRPVLQQVATALKKLKSLGLIHADLKPENIMLVDPVRQPYRVKVIDFGSASHVSKTVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGALEYDQIRYISQTQGLPGEQLLNVGTKSTRFFCRETDMSHSGWRLKTLEEHEAETGMKSKEARKYIFNSLDDIVHVNTVMDLEGSDLLAEKADRREFVSLLKKMLLIDADLRITPIETLNHPFVSMKHLLDFPHSSHVKSCFHIMDICKSPSSCETNNHSKMSLLRPVASNGTAALAANFTKVGTLRSQALTTSAHSVVHHGIPLQAGTAQFGCGDAFHQTLIICPPAIQGIPAAHGKPTSYSIRVDNTVPLVTQAPAVQPLQIRPGVLSQTWSGRTQQMLIPAWQQVTPMAPAAATLTSEGMAGSQRLGDWGKMIPHSNHYNSVMPPPLLTNQITLSAPQPISVGIAHVVWPQPATTKKNKLCQNRSNSLQNTNVPHSAFISPKIISGKEVEEVSCVETQDNHTSEGEARTCHEASVRQDSSVSDKQRQTIIIADSPSPAVSVITISSDTDDEETSPRPSLRECKGSLDCEACQSTLNIDRMCSLSSPDSTLSTSSSGQSSPSPCKRPNSMSDDEQESGCETVDGSPTSDSSGHDSPFAESSFVEDTPQNPELGTCAGTEAKPALSTAVEPPVGTERGLNVDAHMANTDSTCQPLTKGQPAPGKLNQPSASAARQQKPTSAFQQQHLNLSQVQHFGTGHQEWNGNFGHRRQQAYIPTSVTSNPFTLSHGSPNHTAVHAHLAGSAHLGGQPTLLPYPPSTALSSAAPVAHLLASPCTSRPMLQHPTYNISHPSGIVHQVPVGINPRLLPSPTIHQTQYKPIFPPHSYIAASPAYTGFPLSPTKLSQYPYM
|
Seems to negatively regulate apoptosis by promoting FADD phosphorylation. Enhances androgen receptor-mediated transcription. May act as a transcriptional corepressor for NK homeodomain transcription factors.
|
O88854
|
GALR2_MOUSE
|
Galanin receptor type 2 (GAL2-R) (GALR-2)
|
MNGSDSQGAEDSSQEGGGGWQPEAVLVPLFFALIFLVGAVGNALVLAVLLRGGQAVSTTNLFILNLGVADLCFILCCVPFQATIYTLDDWVFGSLLCKAVHFLIFLTMHASSFTLAAVSLDRYLAIRYPLHSRELRTPRNALAAIGLIWGLALLFSGPYLSYYSQSQLANLTVCHPAWSAPRRRAMDLCTFVFSYLLPVLVLSLTYARTLHYLWRTVDPVAAGSGSQRAKRKVTRMIVIVAVLFCLCWMPHHALILCVWFGRFPLTRATYALRILSHLVSYANSCVNPIVYALVSKHFRKGFRKICAGLLRRAPRRASGRVCILAPGNHSGGMLEPESTDLTQVSEAAGPLVPAPALPNCTTLSRTLDPAC
|
Receptor for the hormone galanin, GALP and spexin-1. The activity of this receptor is mediated by G proteins that activate the phospholipase C/protein kinase C pathway (via G(q)) and that inhibit adenylyl cyclase (via G(i)).
|
O88856
|
TPST2_MOUSE
|
Protein-tyrosine sulfotransferase 2 (EC 2.8.2.20) (Tyrosylprotein sulfotransferase 2) (TPST-2)
|
MRLSVRKVLLAAGCALALVLAVQLGQQVLECRAVLGGTRNPRRMRPEQEELVMLGADHVEYRYGKAMPLIFVGGVPRSGTTLMRAMLDAHPEVRCGEETRIIPRVLAMRQAWTKSGREKLRLDEAGVTDEVLDAAMQAFILEVIAKHGEPARVLCNKDPFTLKSSVYLARLFPNSKFLLMVRDGRASVHSMITRKVTIAGFDLSSYRDCLTKWNKAIEVMYAQCMEVGRDKCLPVYYEQLVLHPRRSLKRILDFLGIAWSDTVLHHEDLIGKPGGVSLSKIERSTDQVIKPVNLEALSKWTGHIPRDVVRDMAQIAPMLARLGYDPYANPPNYGNPDPIVINNTHRVLKGDYKTPANLKGYFQVNQNSTSPHLGSS
|
Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides, using 3'-phosphoadenylyl sulfate (PAPS) as cosubstrate.
|
O88867
|
KMO_RAT
|
Kynurenine 3-monooxygenase (EC 1.14.13.9) (Kynurenine 3-hydroxylase)
|
MASSDTEGKRVVVIGGGLVGALNACFLAKRNFQVDVYEAREDIRVANFMRGRSINLALSYRGRQALKAVGLEDQIVSKGVPMKARMIHSLSGKKSAIPYGNKSQYILSISREKLNKDLLTAVESYPNAKVHFGHKLSKCCPEEGILTMLGPNKVPRDITCDLIVGCDGAYSTVRAHLMKKPRFDYSQQYIPHGYMELTIPPKNGEYAMEPNCLHIWPRNAFMMIALPNMDKSFTCTLFMSFEEFEKLPTHSDVLDFFQKNFPDAIPLMGEQALMRDFFLLPAQPMISVKCSPFHLKSRCVLMGDAAHAIVPFFGQGMNAGFEDCLVFDELMDKFNNDLSVCLPEFSRFRIPDDHAISDLSMYNYIEMRAHVNSRWFLFQRLLDKFLHALMPSTFIPLYTMVAFTRIRYHEAVLRWHWQKKVINRGLFVLGSLVAIGSAYILVHHLSPRPLELLRSAWTGTSGHWNRSADISPRVPWSH
|
Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid, a neurotoxic NMDA receptor antagonist and potential endogenous inhibitor of NMDA receptor signaling in axonal targeting, synaptogenesis and apoptosis during brain development. Quinolinic acid may also affect NMDA receptor signaling in pancreatic beta cells, osteoblasts, myocardial cells, and the gastrointestinal tract. {ECO:0000255|HAMAP-Rule:MF_03018, ECO:0000269|PubMed:26752518, ECO:0000269|PubMed:28398044}.
|
O88869
|
RASF9_RAT
|
Ras association domain-containing protein 9 (PAM COOH-terminal interactor protein 1) (P-CIP1) (Peptidylglycine alpha-amidating monooxygenase COOH-terminal interactor)
|
MAPFGRNLLKTRHKNRSPTKDMDPEEKEIVVWVCQEEKIVCGLTKRTTSIDVIQALLEEHEATFGEKRFLLGKASDYCIVEKWRGSERALPPLTRILKLWKAWGDEQPNMQFVLVKTDAFLPVPLWRTAETKLVQNNEKPWELSPANYMKTLPPDKQKRIVRKTFRKLAKIRQDTGSHDRDNMECLVHLIISQDHTIHQQVQRMKELDMEIEKCEAKIHLDRIGNDGADYVQEAYLMPRSSEEEQKLDFQSEDNQTLEDLNDGEGVSQLEEQLQYYRALIDKLSAEIEREVKGAGTDGSEDMEGAAACELENSDLESVKCDLEKSMKAGLKIHSHLSGIQREIKYSDSLLQMKAREYELLAKEFSSLHISSKDGCQGKENRGKEAEASSSNGEIPPLTQRVFNTYTNDTDSDTGISSNHSQDSETTLGDVLLLAT
|
May play a role in regulating vesicuar trafficking in cells.
|
O88871
|
GABR2_RAT
|
Gamma-aminobutyric acid type B receptor subunit 2 (GABA-B receptor 2) (GABA-B-R2) (GABA-BR2) (GABABR2) (Gb2) (G-protein coupled receptor 51)
|
MASPPSSGQPRPPPPPPPPARLLLPLLLSLLLWLAPGAWGWTRGAPRPPPSSPPLSIMGLMPLTKEVAKGSIGRGVLPAVELAIEQIRNESLLRPYFLDLRLYDTECDNAKGLKAFYDAIKYGPNHLMVFGGVCPSVTSIIAESLQGWNLVQLSFAATTPVLADKKKYPYFFRTVPSDNAVNPAILKLLKHFRWRRVGTLTQDVQRFSEVRNDLTGVLYGEDIEISDTESFSNDPCTSVKKLKGNDVRIILGQFDQNMAAKVFCCAFEESMFGSKYQWIIPGWYEPAWWEQVHVEANSSRCLRRSLLAAMEGYIGVDFEPLSSKQIKTISGKTPQQFEREYNSKRSGVGPSKFHGYAYDGIWVIAKTLQRAMETLHASSRHQRIQDFNYTDHTLGKIILNAMNETNFFGVTGQVVFRNGERMGTIKFTQFQDSREVKVGEYNAVADTLEIINDTIRFQGSEPPKDKTIILEQLRKISLPLYSILSALTILGMIMASAFLFFNIKNRNQKLIKMSSPYMNNLIILGGMLSYASIFLFGLDGSFVSEKTFETLCTVRTWILTVGYTTAFGAMFAKTWRVHAIFKNVKMKKKIIKDQKLLVIVGGMLLIDLCILICWQAVDPLRRTVERYSMEPDPAGRDISIRPLLEHCENTHMTIWLGIVYAYKGLLMLFGCFLAWETRNVSIPALNDSKYIGMSVYNVGIMCIIGAAVSFLTRDQPNVQFCIVALVIIFCSTITLCLVFVPKLITLRTNPDAATQNRRFQFTQNQKKEDSKTSTSVTSVNQASTSRLEGLQSENHRLRMKITELDKDLEEVTMQLQDTPEKTTYIKQNHYQELNDILSLGNFTESTDGGKAILKNHLDQNPQLQWNTTEPSRTCKDPIEDINSPEHIQRRLSLQLPILHHAYLPSIGGVDASCVSPCVSPTASPRHRHVPPSFRVMVSGL
|
Component of a heterodimeric G-protein coupled receptor for GABA, formed by GABBR1 and GABBR2. Within the heterodimeric GABA receptor, only GABBR1 seems to bind agonists, while GABBR2 mediates coupling to G proteins. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase (PubMed:9872315, PubMed:9872317, Ref.4, PubMed:10075644, PubMed:9872744, PubMed:10924501). Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis. Plays a critical role in the fine-tuning of inhibitory synaptic transmission. Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials. Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception (By similarity).
|
O88873
|
GMEB2_RAT
|
Glucocorticoid modulatory element-binding protein 2 (GMEB-2)
|
MATPDVSVHMEEVVVVTTPDTAVDGSGVEEVKTVLVTTNLAPHGGDLTEDNMETENAAAAACAFTASSQLKEAVLVKMAEEGENLEAEIVYPITCGDSRANLIWRKFVCPGINVKCVQYDEHVISPKEFVHLAGKSTLKDWKRAIRMNGIMLRKIMDSGELDFYQHDKVCSNTCRSTKIDLSGARVSLSSPTSTEYIPLTPAAADVNGSPATITIETCEDPGDWTTTIGDDTFAFWRGLKDAGLLDEVIQEFQQELEETMKGLQQRVQDPPLQLRDAVLLNNIVQNFGMLDLVKKVLASHKCQMDRSREQYARDLAALEQQCDEHRRRAKELKHKSQHLSNVLMTLTPVSLPSPMKRPRLARATSGPAAMASQVLTQSAQIALGPGMPMSQLTSVPLGKVVSTLPSTVLGKGSPQAAPASSPASPLLGGYTVLASSGSTFPSTVEIHPDTSSLTVLSTAAMQDGTTVLKVVSPLQLLTLPGLGPTLQNVAQASPAGSTIVTMPTAAATGPEEHTATIEVAAVAEDHEQK
|
Trans-acting factor that binds to glucocorticoid modulatory elements (GME) present in the TAT (tyrosine aminotransferase) promoter and increases sensitivity to low concentrations of glucocorticoids. Binds also to the transferrin receptor promoter (By similarity).
|
O88874
|
CCNK_MOUSE
|
Cyclin-K
|
MKENKENSSPSVTSANLDHTKPCWYWDKKDLAHTPSQLEGLDPATEARYRREGARFIFDVGTRLGLHYDTLATGIIYFHRFYMFHSFKQFPRYVTGACCLFLAGKVEETPKKCKDIIKTARSLLNDVQFGQFGDDPKEEVMVLERILLQTIKFDLQVEHPYQFLLKYAKQLKGDKNKIQKLVQMAWTFVNDSLCTTLSLQWEPEIIAVAVMYLAGRLCKFEIQEWTSKPMYRRWWEQFVQDVPVDVLEDICHQILDLYSQGKQQMPHHTPHQLQQPPSLQPTPQVPQGPQSQPSQGSEAAQPPQKDSQQSAQQQQQQAQQPKKPSPQPSPPRQAKRAVVVSPKEENKATEPPPPPKIPKLEATHPPLPPAHPPPDRKPPLAPALGEAEATGPVETSDLPKVQIPPPAHPAPVHQPPPLPHRPPPPPPSSYMTGMSTTSSYMSGEGYQSLQSMMKTEGPSYGALPPASFPPPTIPPPTPGYPPPPPTYNPNFPPPPPRLPPTHAVPPHPPPGLGLPPASYPPPAVPPGGQPPVPPPIPPPGMPPVGGLGRAAWMR
|
Regulatory subunit of cyclin-dependent kinases that mediates activation of target kinases. Plays a role in transcriptional regulation via its role in regulating the phosphorylation of the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A).
|
O88875
|
BY55_MOUSE
|
CD160 antigen (Natural killer cell receptor BY55) (CD antigen CD160) [Cleaved into: CD160 antigen, soluble form]
|
MQRILMAPGQSCCALAILLAIVNFQHGGCIHVTSSASQKGGRLDLTCTLWHKKDEAEGLILFWCKDNPWNCSPETNLEQLRVKRDPETDGITEKSSQLVFTIEQATPSDSGTYQCCARSQKPEIYIHGHFLSVLVTGNHTEIRQRQRSHPDFSHINGTLSSGFLQVKAWGMLVTSLVALQALYTL
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[CD160 antigen]: Receptor on immune cells capable to deliver stimulatory or inhibitory signals that regulate cell activation and differentiation. Exists as a GPI-anchored and as a transmembrane form, each likely initiating distinct signaling pathways via phosphoinositol 3-kinase in activated NK cells and via LCK and CD247/CD3 zeta chain in activated T cells (By similarity). Receptor for both classical and non-classical MHC class I molecules. Receptor or ligand for TNF superfamily member TNFRSF14, participating in bidirectional cell-cell contact signaling between antigen presenting cells and lymphocytes. Upon ligation of TNFRSF14, provides stimulatory signal to NK cells enhancing IFNG production and anti-tumor immune response. On activated CD4+ T cells, interacts with TNFRSF14 and down-regulates CD28 costimulatory signaling, restricting memory and alloantigen-specific immune response (By similarity). In the context of bacterial infection, acts as a ligand for TNFRSF14 on epithelial cells, triggering the production of antimicrobial proteins and pro-inflammatory cytokines. [CD160 antigen, soluble form]: The soluble GPI-cleaved form, usually released by activated lymphocytes, might play an immune regulatory role by limiting lymphocyte effector functions.
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O88876
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DHRS3_MOUSE
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Short-chain dehydrogenase/reductase 3 (EC 1.1.1.300) (Retinal short-chain dehydrogenase/reductase 1) (retSDR1)
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MVWKWLGALVVFPLQMIYLVTKAAVGMVLPPKLRDLSRESVLITGGGRGIGRHLAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDCPGVSATTVLPFHTSTEMFQGMRVRFPNLFPPLKPETVARRTVDAVQQNQALLLLPWTMNILIILKSILPQAALEEIHRFSGTYTCMNTFKGRT
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Catalyzes the reduction of all-trans-retinal to all-trans-retinol in the presence of NADPH.
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O88878
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ZFAN5_MOUSE
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AN1-type zinc finger protein 5 (Zinc finger A20 domain-containing protein 2) (Zinc finger protein 216)
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MAQETNQTPGPMLCSTGCGFYGNPRTNGMCSVCYKEHLQRQQNSGRMSPMGTASGSNSPTSDSASVQRADAGLNNCEGAAGSTSEKSRNVPVAALPVTQQMTEMSISREDKITTPKTEVSEPVVTQPSPSVSQPSSSQSEEKAPELPKPKKNRCFMCRKKVGLTGFDCRCGNLFCGLHRYSDKHNCPYDYKAEAAAKIRKENPVVVAEKIQRI
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Involved in protein degradation via the ubiquitin-proteasome system. May act by anchoring ubiquitinated proteins to the proteasome. Plays a role in ubiquitin-mediated protein degradation during muscle atrophy. Plays a role in the regulation of NF-kappa-B activation and apoptosis. Inhibits NF-kappa-B activation triggered by overexpression of RIPK1 and TRAF6 but not of RELA. Inhibits also tumor necrosis factor (TNF), IL-1 and TLR4-induced NF-kappa-B activation in a dose-dependent manner. Overexpression sensitizes cells to TNF-induced apoptosis. Is a potent inhibitory factor for osteoclast differentiation.
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O88879
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APAF_MOUSE
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Apoptotic protease-activating factor 1 (APAF-1)
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MDAKARNCLLQHREALEKDIKTSYIMDHMISNGVLSVIEEEKVKSQATQYQRAAALIKMILNKDNCAYISFYNALLHEGYKDLAALLQSGLPLVSSSSGKDTDGGITSFVRTVLCEGGVPQRPVIFVTRKKLVHAIQQKLWKLNGEPGWVTIYGMAGCGKSVLAAEAVRDHSLLEGCFSGGVHWVSIGKQDKSGLLMKLQNLCMRLDQEESFSQRLPLNIEEAKDRLRVLMLRKHPRSLLILDDVWDPWVLKAFDNQCQILLTTRDKSVTDSVMGPKHVVPVESGLGREKGLEILSLFVNMKKEDLPAEAHSIIKECKGSPLVVSLIGALLRDFPNRWAYYLRQLQNKQFKRIRKSSSYDYEALDEAMSISVEMLREDIKDYYTDLSILQKDVKVPTKVLCVLWDLETEEVEDILQEFVNKSLLFCNRNGKSFCYYLHDLQVDFLTEKNRSQLQDLHRKMVTQFQRYYQPHTLSPDQEDCMYWYNFLAYHMASANMHKELCALMFSLDWIKAKTELVGPAHLIHEFVAYRHILDEKDCAVCENFQEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYRQAKLQAKQEGDTGRLYLEWINKKTIKNLSRLVVRPHTDAVYHACFSQDGQRIASCGADKTLQVFKAETGEKLLDIKAHEDEVLCCAFSSDDSYIATCSADKKVKIWDSATGKLVHTYDEHSEQVNCCHFTNKSNHLLLATGSNDFFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDELLASCSADGTLRLWDVRSANERKSINVKRFFLSSEDPPEDVEVIVKCCSWSADGDKIIVAAKNKVLLFDIHTSGLLAEIHTGHHSTIQYCDFSPYDHLAVIALSQYCVELWNIDSRLKVADCRGHLSWVHGVMFSPDGSSFLTASDDQTIRVWETKKVCKNSAIVLKQEIDVVFQENETMVLAVDNIRGLQLIAGKTGQIDYLPEAQVSCCCLSPHLEYVAFGDEDGAIKIIELPNNRVFSSGVGHKKAVRHIQFTADGKTLISSSEDSVIQVWNWQTGDYVFLQAHQETVKDFRLLQDSRLLSWSFDGTVKVWNVITGRIERDFTCHQGTVLSCAISSDATKFSSTSADKTAKIWSFDLLSPLHELKGHNGCVRCSAFSLDGILLATGDDNGEIRIWNVSDGQLLHSCAPISVEEGTATHGGWVTDVCFSPDSKTLVSAGGYLKWWNVATGDSSQTFYTNGTNLKKIHVSPDFRTYVTVDNLGILYILQVLE
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Oligomeric Apaf-1 mediates the cytochrome c-dependent autocatalytic activation of pro-caspase-9 (Apaf-3), leading to the activation of caspase-3 and apoptosis. This activation requires ATP (By similarity).
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O88881
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BEGIN_RAT
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Brain-enriched guanylate kinase-associated protein
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MWTGGRRPGRLRRAASAADMEKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDKLYRMGQHYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQCSQTYGRVHKVSELPSDFQQRVSLHMEKHGCSLPSPLCHPSYADSVPTCVIAKVLEKPDPGSLSSRMSDASARDLAYRDGVENPGPRPPYKGDIYCSDTALYCPDERDHDRRPSVDTPVTDVGFLRAQNSTDSLAEEEEAEAAAFPEAYRREAFQGYAASLPTSSSYSSFSATSEEKEHAQASTLTASQQAIYLNSREELFSRKPPSATYGSSPRYAKAAATLGSPLEAQVAPGFARTVSPYPAEPYRYPASQQALMPPNLWSLRAKPSGNRLAAREDIRGQWRPLSVEDVGAYSYQAGAAGRAASPCNFSERFYGGGGGGGSPGKNAEGRASPLYASYKADSFSEGDDLSQGHLAEPCFLRAGGDLSLSPSRSADPLPGYATSDGDGDRLGVQLCGPGSSPEPEHGSRDSLEPSSMEASPEMHPPTRLSPQQAFPRTGGSGLSRKDSLTKAQLYGTLLN
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May sustain the structure of the postsynaptic density (PSD).
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O88884
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AKAP1_RAT
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A-kinase anchor protein 1, mitochondrial (A-kinase anchor protein 121 kDa) (AKAP 121) (Dual specificity A-kinase-anchoring protein 1) (D-AKAP-1) (Protein kinase A-anchoring protein 1) (PRKA1) (Spermatid A-kinase anchor protein 84) (S-AKAP84)
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MAIQFRSLFPLALPGMLALLGWWWFFSRKKDRLSSNGKQVGTLKVGPAIEDRLPTEEACPGVLSVTPSVTQPPGKEEQRSMDRPLSDPPALPRTRQVRRRSESSGNLPSIVDTRLQAGQCSDENSKVVLSLMGDEAKSIPLGRPLFPKDLSFPYEAVEGCKQESALGRTPGRGWLSQCAASGENARETGGAEGTGDAVLGESVLEEGLLPQECVSEVEKSEFPILAPGGGGGEKVRSGPPQVDELLKKEEYIVGKLPSSFVGPVHSELVKDEGALVPQVKGSQDRSLARELDKDKTLPEKDQIEQTAFQIISQVILEATEEIRATTVGKTVAQVHPTPGTQPQGQEESCVPASQETSLGQEIPDPASTRTGATASPSAGAPPPKTYVSCLSSPLSGPTKDQKPKNSAHHISLAPCPPPVTPQRQSLDGASNPRGDDTFVTCTSNNSQSVLSVTSLGLCSDPVSTSRLEDSCTETISSSGDKAVTPPLPDSTEPFSNGVLKEELSDLGTEDGWTMDTEADHSGGSDGNSMDSVDSCCGLTKPDSPQTVQAGSNPKKVDLIIWEIEVPKHLVGRLIGKQGRYVSFLKQTSGAKIYISTLPYTQNIQICHIEGSQHHVDKALNLIGKKFKELNLTNIYAPPLPSLALPSLPMTSWLMLPDGITVEVIVVNQVNAGHLFVQQHTHPTFHALRSLDQQMYLCYSQPGIPTLPTPVEITVICAAPGADGAWWRAQVVASYEETNEVEIRYVDYGGYKRVKVDVLRQIRSDFVTLPFQGAEVLLDSVVPLSDDDHFSPEADAAMSEMTGNTALLAQVTSYSATGLPLIQLWSVVGDEVVLINRSLVERGLAQWVDSCYASL
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Binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane (By similarity). Involved in mitochondrial-mediated antiviral innate immunity (By similarity). Promotes translocation of NDUFS1 into mitochondria to regulate mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) activity (By similarity).
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