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O08756
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HCD2_MOUSE
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3-hydroxyacyl-CoA dehydrogenase type-2 (EC 1.1.1.35) (17-beta-estradiol 17-dehydrogenase) (EC 1.1.1.62) (2-methyl-3-hydroxybutyryl-CoA dehydrogenase) (MHBD) (3-alpha-(17-beta)-hydroxysteroid dehydrogenase (NAD(+))) (EC 1.1.1.239) (3-hydroxy-2-methylbutyryl-CoA dehydrogenase) (EC 1.1.1.178) (3-hydroxyacyl-CoA dehydrogenase type II) (3alpha(or 20beta)-hydroxysteroid dehydrogenase) (EC 1.1.1.53) (7-alpha-hydroxysteroid dehydrogenase) (EC 1.1.1.159) (Endoplasmic reticulum-associated amyloid beta-peptide-binding protein) (Mitochondrial ribonuclease P protein 2) (Mitochondrial RNase P protein 2) (Short chain dehydrogenase/reductase family 5C member 1) (Short-chain type dehydrogenase/reductase XH98G2) (Type II HADH)
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MAAAVRSVKGLVAVVTGGASGPWLATAKRLVGQGATAVLLDVPDSEGESQAKKLGESCIFAPANVTSEKEIQAALTLAKEKFGRIDVAVNCAGIAVAIKTYHQKKNKIHTLEDFQRVINVNLIGTFNVIRLVAGEMGQNEPDQGGQRGVIINTASVAAFEGQVGQAAYSASKGGIDGMTLPIARDLAPTGIRVVTIAPGLFATPLLTTLPEKVRNFLASQVPFPSRLGDPAEYAHLVQTIIENPFLNGEVIRLDGAIRMQP
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Mitochondrial dehydrogenase involved in pathways of fatty acid, branched-chain amino acid and steroid metabolism (By similarity). Acts as (S)-3-hydroxyacyl-CoA dehydrogenase in mitochondrial fatty acid beta-oxidation, a major degradation pathway of fatty acids. Catalyzes the third step in the beta-oxidation cycle, namely the reversible conversion of (S)-3-hydroxyacyl-CoA to 3-ketoacyl-CoA. Preferentially accepts straight medium- and short-chain acyl-CoA substrates with highest efficiency for (3S)-hydroxybutanoyl-CoA (By similarity). Acts as 3-hydroxy-2-methylbutyryl-CoA dehydrogenase in branched-chain amino acid catabolic pathway. Catalyzes the oxidation of 3-hydroxy-2-methylbutanoyl-CoA into 2-methyl-3-oxobutanoyl-CoA, a step in isoleucine degradation pathway (By similarity). Has hydroxysteroid dehydrogenase activity toward steroid hormones and bile acids. Catalyzes the oxidation of 3alpha-, 17beta-, 20beta- and 21-hydroxysteroids and 7alpha- and 7beta-hydroxy bile acids. Oxidizes allopregnanolone/brexanolone at the 3alpha-hydroxyl group, which is known to be critical for the activation of gamma-aminobutyric acid receptors (GABAARs) chloride channel. Has phospholipase C-like activity toward cardiolipin and its oxidized species (By similarity). Likely oxidizes the 2'-hydroxyl in the head group of cardiolipin to form a ketone intermediate that undergoes nucleophilic attack by water and fragments into diacylglycerol, dihydroxyacetone and orthophosphate. Has higher affinity for cardiolipin with oxidized fatty acids and may degrade these species during the oxidative stress response to protect cells from apoptosis (By similarity). By interacting with intracellular amyloid-beta, it may contribute to the neuronal dysfunction associated with Alzheimer disease (AD) (By similarity). Essential for structural and functional integrity of mitochondria. In addition to mitochondrial dehydrogenase activity, moonlights as a component of mitochondrial ribonuclease P, a complex that cleaves tRNA molecules in their 5'-ends. Together with TRMT10C/MRPP1, forms a subcomplex of the mitochondrial ribonuclease P, named MRPP1-MRPP2 subcomplex, which displays functions that are independent of the ribonuclease P activity. The MRPP1-MRPP2 subcomplex catalyzes the formation of N(1)-methylguanine and N(1)-methyladenine at position 9 (m1G9 and m1A9, respectively) in tRNAs HSD17B10/MRPP2 acting as a non-catalytic subunit. The MRPP1-MRPP2 subcomplex also acts as a tRNA maturation platform: following 5'-end cleavage by the mitochondrial ribonuclease P complex, the MRPP1-MRPP2 subcomplex enhances the efficiency of 3'-processing catalyzed by ELAC2, retains the tRNA product after ELAC2 processing and presents the nascent tRNA to the mitochondrial CCA tRNA nucleotidyltransferase TRNT1 enzyme. Associates with mitochondrial DNA complexes at the nucleoids to initiate RNA processing and ribosome assembly.
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O08759
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UBE3A_MOUSE
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Ubiquitin-protein ligase E3A (EC 2.3.2.26) (HECT-type ubiquitin transferase E3A) (Oncogenic protein-associated protein E6-AP)
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MATACKRSPGESQSEDIEASRMKRAAAKHLIERYYHQLTEGCGNEACTNEFCASCPTFLRMDNNAAAIKALELYKINAKLCDPHPSKKGASSAYLENSKGASNNSEIKMNKKEGKDFKDVIYLTEEKVYEIYEFCRESEDYSPLIRVIGRIFSSAEALVLSFRKVKQHTKEELKSLQEKDEDKDEDEKEKAACSAAAMEEDSEASSSRMGDSSQGDNNVQKLGPDDVTVDIDAIRRVYSSLLANEKLETAFLNALVYLSPNVECDLTYHNVYTRDPNYLNLFIIVMENSNLHSPEYLEMALPLFCKAMCKLPLEAQGKLIRLWSKYSADQIRRMMETFQQLITYKVISNEFNSRNLVNDDDAIVAASKCLKMVYYANVVGGDVDTNHNEEDDEEPIPESSELTLQELLGDERRNKKGPRVDPLETELGVKTLDCRKPLISFEEFINEPLNDVLEMDKDYTFFKVETENKFSFMTCPFILNAVTKNLGLYYDNRIRMYSERRITVLYSLVQGQQLNPYLRLKVRRDHIIDDALVRLEMIAMENPADLKKQLYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDEATKLFWFNPSSFETEGQFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFRDLGDSHPVLYQSLKDLLEYEGSVEDDMMITFQISQTDLFGNPMMYDLKENGDKIPITNENRKEFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKYLFRPEEIELLICGSRNLDFQALEETTEYDGGYTRESVVIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGGLGKLKMIIAKNGPDTERLPTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKGFGML
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E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and transfers it to its substrates. Several substrates have been identified including the BMAL1, ARC, LAMTOR1, RAD23A and RAD23B, MCM7 (which is involved in DNA replication), annexin A1, the PML tumor suppressor, and the cell cycle regulator CDKN1B. Additionally, may function as a cellular quality control ubiquitin ligase by helping the degradation of the cytoplasmic misfolded proteins. Finally, UBE3A also promotes its own degradation in vivo (By similarity). Plays an important role in the regulation of the circadian clock: involved in the ubiquitination of the core clock component BMAL1, leading to its proteasomal degradation. Acts as a regulator of synaptic development by mediating ubiquitination and degradation of ARC. Required for synaptic remodeling in neurons by mediating ubiquitination and degradation of LAMTOR1, thereby limiting mTORC1 signaling and activity-dependent synaptic remodeling. Synergizes with WBP2 in enhancing PGR activity (By similarity).
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O08760
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OGG1_MOUSE
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N-glycosylase/DNA lyase [Includes: 8-oxoguanine DNA glycosylase (EC 3.2.2.-); DNA-(apurinic or apyrimidinic site) lyase (AP lyase) (EC 4.2.99.18)]
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MLFRSWLPSSMRHRTLSSSPALWASIPCPRSELRLDLVLASGQSFRWKEQSPAHWSGVLADQVWTLTQTEDQLYCTVYRGDDSQVSRPTLEELETLHKYFQLDVSLAQLYSHWASVDSHFQRVAQKFQGVRLLRQDPTECLFSFICSSNNNIARITGMVERLCQAFGPRLIQLDDVTYHGFPNLHALAGPEAETHLRKLGLGYRARYVRASAKAILEEQGGPAWLQQLRVAPYEEAHKALCTLPGVGAKVADCICLMALDKPQAVPVDVHVWQIAHRDYGWHPKTSQAKGPSPLANKELGNFFRNLWGPYAGWAQAVLFSADLRQPSLSREPPAKRKKGSKRPEG
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DNA repair enzyme that incises DNA at 8-oxoG residues. Excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine (FAPY) from damaged DNA. Has a beta-lyase activity that nicks DNA 3' to the lesion.
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O08762
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NETR_MOUSE
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Neurotrypsin (EC 3.4.21.-) (Brain-specific serine protease 3) (BSSP-3) (Motopsin) (Serine protease 12)
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MALARCVLAVILGALSVVARADPVSRSPLHRPHPSPPRSQHAHYLPSSRRPPRTPRFPLPLRIPAAQRPQVLSTGHTPPTIPRRCGAGESWGNATNLGVPCLHWDEVPPFLERSPPASWAELRGQPHNFCRSPDGSGRPWCFYRNAQGKVDWGYCDCGQGPALPVIRLVGGNSGHEGRVELYHAGQWGTICDDQWDNADADVICRQLGLSGIAKAWHQAHFGEGSGPILLDEVRCTGNELSIEQCPKSSWGEHNCGHKEDAGVSCVPLTDGVIRLAGGKSTHEGRLEVYYKGQWGTVCDDGWTEMNTYVACRLLGFKYGKQSSVNHFDGSNRPIWLDDVSCSGKEVSFIQCSRRQWGRHDCSHREDVGLTCYPDSDGHRLSPGFPIRLVDGENKKEGRVEVFVNGQWGTICDDGWTDKHAAVICRQLGYKGPARARTMAYFGEGKGPIHMDNVKCTGNEKALADCVKQDIGRHNCRHSEDAGVICDYLEKKASSSGNKEMLSSGCGLRLLHRRQKRIIGGNNSLRGAWPWQASLRLRSAHGDGRLLCGATLLSSCWVLTAAHCFKRYGNNSRSYAVRVGDYHTLVPEEFEQEIGVQQIVIHRNYRPDRSDYDIALVRLQGPGEQCARLSTHVLPACLPLWRERPQKTASNCHITGWGDTGRAYSRTLQQAAVPLLPKRFCKERYKGLFTGRMLCAGNLQEDNRVDSCQGDSGGPLMCEKPDESWVVYGVTSWGYGCGVKDTPGVYTRVPAFVPWIKSVTSL
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Plays a role in neuronal plasticity and the proteolytic action may subserve structural reorganizations associated with learning and memory operations.
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O08773
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RGS14_RAT
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Regulator of G-protein signaling 14 (RGS14)
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MPGKPKHLGVPNGRMVLAVSDGELTSTSGSQAQGEGRGSSLSIHSLPSGPSSPFSTDEQPVASWAQSFERLLQDPRGLAYFTEFLKKEFSAENVTFWQACERFQQIPASDTKQLAQEAHNIYHEFLSSQALSPVNIDRQAWLSEEVLAQPRPDMFRAQQLQIFNLMKFDSYARFVKSPLYQECLLAEAEGRPLREPGSSHLGSPDTARKKPKLKPGKSLPLGVEELGQLPLAEGRPLRKSFRREMPGGAVNSALRRESQGSLNSSASLDLGFLAFVSSKSESHRKSLGSGEGESESRPGKYCCVYLPDGTASLALARPGLTIRDMLAGICEKRGLSLPDIKVYLVGKEQKALVLDQDCTVLADQEVRLENRITFQLELVGLERVVRISAKPTKRLQEALQPILAKHGLSLDQVVLHRPGEKQLVDLENLVSSVASQTLVLDTLPDAKTREASSIPPCRSQGCLPRTQTKDSHLPPLSSSLSVEDASGSTGKRQTCDIEGLVELLNRVQSSGAHDQRGLLRKEDLVLPEFLQLPSQRPGSQEAPP
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Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. Besides, modulates signal transduction via G protein alpha subunits by functioning as a GDP-dissociation inhibitor (GDI). Has GDI activity on G(i) alpha subunits GNAI1 and GNAI3, but not on GNAI2 and G(o)-alpha subunit GNAO1. Has GAP activity on GNAI0, GNAI2 and GNAI3. May act as a scaffold integrating G protein and Ras/Raf MAPkinase signaling pathways. Inhibits platelet-derived growth factor (PDGF)-stimulated ERK1/ERK2 phosphorylation a process depending on its interaction with HRAS and that is reversed by G(i) alpha subunit GNAI1. Acts as a positive modulator of microtubule polymerisation and spindle organization through a G(i)-alpha-dependent mechanism. Plays a role in cell division required for completion of the first mitotic division of the embryo. Involved in visual memory processing capacity when overexpressed in the V2 secondary visual cortex area. Involved in hippocampal-based learning and memory acts as a suppressor of synaptic plasticity in CA2 neurons. Required for the nerve growth factor (NGF)-mediated neurite outgrowth. Involved in stress resistance.
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O08774
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RGS12_RAT
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Regulator of G-protein signaling 12 (RGS12)
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MYRAGEPGKRQSGPAPPRVRSVEVARGRAGYGFTLSGQAPCVLSCVMRGSPADFVGLRAGDQILAINEINVKKASHEDVVKLIGKCSGVLRMVISEGSSHVEPSSSDEEGGLCEGKGWLRPKLDSKALGINRAERVVEEVQSGGIFNMIFESPSLCASGSEPLKLKQRSLSESAALRLDVGQDSLCTPHPSMLSKEEISKVINDDSVFTVGLDNHDDFGLDASILNVAMVVGYLGSIELPSTSSNLEHDSLQAIRGCMRRLRAEQKIHSLVTMKVMHDCVQLVTDRAGVVAEYPAEKLAFSAVCPDDRRFFGLVTMQTNDDGCLAQEDEGALRTSCHVFMVDPDLFHHKIHQGIARRFGFACTADPDTSGCLEFPASSLPVLQFISVLYRDMGELIEGVRARAFLDGDADAHQNNSTSSNSDSGIGNFNQEEKSNRVLVVDLGGGSSRHGQGSSPGWESVSGRGSQPWSAPWNGTFCHDSEAGSPLETSPNTDRFWDLTKHSGPVFHMEVPPATLRSSIPPSKRGATGSSCGFNQRWLPVHVLQEWQCGHASDQESYTDSTDGWSSVNCGTLPPPMSKIPADRYRVEGSFAQAPLSTQKRDWSRKAFGMQNLFGPHRNVRKTKEDKKSSKLGRGVALAQTSQRTSARRSFGRSRRFSLTRSLDDLESATVSDGELTGADLKDCISNNSLSSNASLPSVQSCRRLRERRVASWAVSFERLLQDPVGVRYFSDFLRKEFSEENILFWQACECFSHVPAHDKKELSYRAREIFSKFLCSKATTPVNIDSQAQLADDILNAPHPDMFKEQQLQIFNLMKFDSYTRFLKSQLYQECVLAEVEGRTLPDSQQVPSSPASKHSISSDHSNVSTPKKLSGKSKSGRSLNEDVGEEDSEKKRKGAFFSWSRSRSTGRSQKKKDHGDHAHDALHANGGLCRRESQGSVSSAGSLDLSEACRTSALERDKAAKHCCVHLPDGTSCVVAVKSGFSIKEILSGLCERHGINGAAVDLFLVGGDKPLVLHQDSSILATRDLRLGKRTLFRLDLVPINRSVGLKAKPTKPVTEVLRPVVAKYGLDLGSLLVRLSGEKEPLDLGAPISSLDGQRVILEERDPSRGKVSTEKQKGAPVKQSSAVNSSPRNHSAMGEERTLGKSNSIKIRGENGKSARDPRLSKREESIAKIGKKKYQKINLDEAEEFFELISKAQSNRADDQRGLLRKEDLVLPEFLRLPPGSSELALSSPPPVKGFSKRAVTSHGQEGAVQTEESYSDSPATSPASAQSPCSAYSPGSAHSPGSAHSPGSAHSTPGPPGTAQPGEKPTKPSCISTVQEGTTQAWRRLSPELEAGGIQTVEEEQVADLTLMGEGDISSPNSTLLPPPPLPQDTPGPTRPGTSRF
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Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form.
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O08775
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VGFR2_RAT
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Vascular endothelial growth factor receptor 2 (VEGFR-2) (EC 2.7.10.1) (Fetal liver kinase 1) (FLK-1) (Protein-tyrosine kinase receptor flk-1) (CD antigen CD309)
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MESRALLAVALWFCVETRAASVGLPGDSLHPPKLSTQKDILTILANTTLQITCRGQRDLDWLWPNTPRDSEERVLVTECGDSIFCKTLTVPRVVGNDTGAYKCFYRDTDVSSIVYVYVQDHRSPFIASVSDEHGIVYITENKNKTVVIPCRGSISNLNVSLCARYPEKRFVPDGNRISWDSEKGFTIPSYMISYAGMVFCEAKINDETYQSIMYIVLVVGYRIYDVVLSPPHEIELSAGEKLVLNCTARTELNVGLDFSWQFPSSKHQHKKIVNRDVKSLPGTVAKMFLSTLTIDSVTKSDQGEYTCTAYSGLMTKKNKTFVRVHTKPFIAFGSGMKSLVEATVGSQVRIPVKYLSYPAPDIKWYRNGRPIESNYTMIVGDELTIMEVSERDAGNYTVILTNPISMEKQSHMVSLVVNVPPQIGEKALISPMDSYQYGTMQTLTCTVYANPPLHHIQWYWQLEEACSYRPSQTNPYTCKEWRHVKDFQGGNKIEVTKNQYALIEGKNKTVSTLVIQAAYVSALYKCEAINKAGRGERVISFHVIRGPEITVQPATQPTERESMSLLCTADRNTFENLTWYKLGSQATSVHMGESLTPVCKNLDALWKLNGTVFSNSTNDILIVAFQNASLQDQGNYVCSAQDKKTKKRHCLVKQLVILERMAPMITGNLENQTTTIGETIEVVCPTSGNPTPLITWFKDNETLVEDSGIVLKDGNRNLTIRRVRKEDGGLYTCQACNVLGCARAETLFIIEGVQEKTNLEVIILVGTAVIAMFFWLLLVILVRTVKRANEGELKTGYLSIVMDPDELPLDERCERLPYDASKWEFPRDRLKLGKPLGRGAFGQVIEADAFGIDKTATCKTVAVKMLKEGATHSEHRALMSELKILIHIGHHLNVVNLLGACTKPGGPLMVIVEFCKFGNLSTYLRGKRNEFVPYKSKGARFRSGKDYVGELSVDLKRRLDSITSSQSSASSGFVEEKSLSDVEEEEASEELYKDFLTLEHLICYSFQVAKGMEFLASRKCIHRDLAARNILLSEKNVVKICDFGLARDIYKDPDYVRKGDPRLPLKWMAPETIFDRIYTIQSGVWSFGVLLWEIFSLGASPYPGVKIDEKFCRRLKEGTRMRAPDYTTPEMYQTMLDCWHEDPNQRPAFSELVEHLGNLLQANAQQDGKDYIVLPMSETLSMEEDSGLSLPTSPVSCMEEEEVCDPKFHYDNTAGISHYLQNSKRKSRPVSVKTFEDIPLEEPEVKVIPDDSQTDSGMVLASEELKTLEDRNKLSPSFGGMMPSKSRESVASEGSNQTSGYQSGYHSDDTDTTVYSSDEAGLLKLVDVAGHVDSGTTLRSSPV
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Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFC and VEGFD. Plays an essential role in the regulation of angiogenesis, vascular development, vascular permeability, and embryonic hematopoiesis. Promotes proliferation, survival, migration and differentiation of endothelial cells. Promotes reorganization of the actin cytoskeleton. Isoforms lacking a transmembrane domain may function as decoy receptors for VEGFA, VEGFC and/or VEGFD. Modulates FLT1 and FLT4 signaling by forming heterodimers. Binding of vascular growth factors to isoform 1 leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol-1,4,5-trisphosphate and the activation of protein kinase C. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, reorganization of the actin cytoskeleton and activation of PTK2/FAK1. Required for VEGFA-mediated induction of NOS2 and NOS3, leading to the production of the signaling molecule nitric oxide (NO) by endothelial cells. Phosphorylates PLCG1. Promotes phosphorylation of FYN, NCK1, NOS3, PIK3R1, PTK2/FAK1 and SRC (By similarity).
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O08784
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TCOF_MOUSE
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Treacle protein (Treacher Collins syndrome protein homolog)
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MAEARKRRELLPLIYHHLLQAGYVRAAREVKEQSGQKSFLTQPVTLLDIYTHWQQTSELGQKQKAEDDETLQAKKSRVSDPVSSSESSDQEKEEEAATERAKATPRPTPVNSATAALPSKVKEKGKTKTANKTVNSVSHPGSGKTVVHLLSGKSPKKSAEPLANTVLASETEEEGNAQALGPTAKSGTVSAGQGSSSSEDSSISSDETDVEVKSPAKPAQAKASAAPAKDPPARTAPGPTKLGNVAPTPAKPARAAAAAAAAAVAAAAAAAAEESESSEEDSDSEDEAPAGLPSQVKASGKGPHVRADSVSAKGISGKGPILATPGKTGPAATQAKAERPEKDSETSSEDDSDSEDEMPVTVNTPQARTSGKSPRARGTSAPAKESSQKGAPAVTPGKARPVAAQAGKPEAKSSEESESDSGETPAAATLTTSPAKVKPLGKSSQVRPVSTVTPGSSGKGANLPCPGKVGSAALRVQMVKKEDVSESSSAELDSDGPGSPAKAKASLALPQKVRPVATQVKTDRGKGHSGSSEESSDSEEEAAPAASAAQAKPALEKQMKASSRKGTPASATGASTSSHCKAGAVTSSASLSSPALAKGTQRSDVDSSSESESEGAAPSTPRVQGKSGGKGLQGKAALGQGVAPVHTQKTGPSVKAMAQEDSESLEEDSSSEEEDETPAQATPLGRLPQAKANPPPTKTPPASASGKAVAAPTKGKPPVPNSTVSARGQRSVPAAGKAGAPATQAQKGPVAGTGEDSESSSKEESDSEEETPAQIKPVGKTSQVRAASAPAKESPKKGAHPGTPGKTGSSATQAQPGKTEDSDSSSEESDSDTEMPSAQAIKSPPVSVNRNSSPAVPAPTPEGVQAVNTTKKASGTTAQSSSSESEDGDEDLIPATQPSTYALRTSVTTPAALSRAASQPSKSEQSSRMPKGKKAKAAASAQTSSAVETLPMMPPQSAPIQPKATNKLGKSKLPEKQQLAPGYPKAPRSSEDSSDTSSEDEEDAKRPQMPKSAHRLDPDPSQKETVVEETPTESSEDEMVAPSQSLLSGYMTPGLTVANSQASKATPRPDSNSLASSAPATKDNPDGKQKSKSQHAADTALPKTGRKEASSGSTPQKPKKLKKSTSSSPAPTQTLPNSITQRLLEQAWPLSEAQVQASVVKVLTELLEQERLKATEAIKESGKKSQKRKLSGDLEAGAPKNKKKKEQPVPRASAVSPEKAPMTSKAKSKLDKGSAGGKGKGSPGPQGAKEKPDGELLGIKLESGEQSDPKSKSKKKKSLKKKKDKEKKEKKKGKKSLAKDSASPIQKKKKKKKKSAEPAV
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Nucleolar protein that acts as a regulator of RNA polymerase I by connecting RNA polymerase I with enzymes responsible for ribosomal processing and modification. Required for neural crest specification: following monoubiquitination by the BCR(KBTBD8) complex, associates with NOLC1 and acts as a platform to connect RNA polymerase I with enzymes responsible for ribosomal processing and modification, leading to remodel the translational program of differentiating cells in favor of neural crest specification.
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O08785
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CLOCK_MOUSE
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Circadian locomoter output cycles protein kaput (mCLOCK) (EC 2.3.1.48)
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MVFTVSCSKMSSIVDRDDSSIFDGLVEEDDKDKAKRVSRNKSEKKRRDQFNVLIKELGSMLPGNARKMDKSTVLQKSIDFLRKHKETTAQSDASEIRQDWKPTFLSNEEFTQLMLEALDGFFLAIMTDGSIIYVSESVTSLLEHLPSDLVDQSIFNFIPEGEHSEVYKILSTHLLESDSLTPEYLKSKNQLEFCCHMLRGTIDPKEPSTYEYVRFIGNFKSLTSVSTSTHNGFEGTIQRTHRPSYEDRVCFVATVRLATPQFIKEMCTVEEPNEEFTSRHSLEWKFLFLDHRAPPIIGYLPFEVLGTSGYDYYHVDDLENLAKCHEHLMQYGKGKSCYYRFLTKGQQWIWLQTHYYITYHQWNSRPEFIVCTHTVVSYAEVRAERRRELGIEESLPETAADKSQDSGSDNRINTVSLKEALERFDHSPTPSASSRSSRKSSHTAVSDPSSTPTKIPTDTSTPPRQHLPAHEKMTQRRSSFSSQSINSQSVGPSLTQPAMSQAANLPIPQGMSQFQFSAQLGAMQHLKDQLEQRTRMIEANIHRQQEELRKIQEQLQMVHGQGLQMFLQQSNPGLNFGSVQLSSGNSNIQQLTPVNMQGQVVPANQVQSGHISTGQHMIQQQTLQSTSTQQSQQSVMSGHSQQTSLPSQTPSTLTAPLYNTMVISQPAAGSMVQIPSSMPQNSTQSATVTTFTQDRQIRFSQGQQLVTKLVTAPVACGAVMVPSTMLMGQVVTAYPTFATQQQQAQTLSVTQQQQQQQQQPPQQQQQQQQSSQEQQLPSVQQPAQAQLGQPPQQFLQTSRLLHGNPSTQLILSAAFPLQQSTFPPSHHQQHQPQQQQQLPRHRTDSLTDPSKVQPQ
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Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-BMAL1|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. Regulates the circadian expression of ICAM1, VCAM1, CCL2, THPO and MPL and also acts as an enhancer of the transactivation potential of NF-kappaB. Plays an important role in the homeostatic regulation of sleep. The CLOCK-BMAL1 heterodimer regulates the circadian expression of SERPINE1/PAI1, VWF, B3, CCRN4L/NOC, NAMPT, DBP, MYOD1, PPARGC1A, PPARGC1B, SIRT1, GYS2, F7, NGFR, GNRHR, BHLHE40/DEC1, ATF4, MTA1, KLF10 and also genes implicated in glucose and lipid metabolism. Promotes rhythmic chromatin opening, regulating the DNA accessibility of other transcription factors. May play a role in spermatogenesis contributes to the chromatoid body assembly and physiology. The CLOCK-BMAL2 heterodimer activates the transcription of SERPINE1/PAI1 and BHLHE40/DEC1. The preferred binding motif for the CLOCK-BMAL1 heterodimer is 5'-CACGTGA-3', which contains a flanking adenine nucleotide at the 3-prime end of the canonical 6-nucleotide E-box sequence (By similarity). CLOCK specifically binds to the half-site 5'-CAC-3', while BMAL1 binds to the half-site 5'-GTGA-3' (By similarity). The CLOCK-BMAL1 heterodimer also recognizes the non-canonical E-box motifs 5'-AACGTGA-3' and 5'-CATGTGA-3'. CLOCK has an intrinsic acetyltransferase activity, which enables circadian chromatin remodeling by acetylating histones and nonhistone proteins, including its own partner BMAL1. Represses glucocorticoid receptor NR3C1/GR-induced transcriptional activity by reducing the association of NR3C1/GR to glucocorticoid response elements (GREs) via the acetylation of multiple lysine residues located in its hinge region. The acetyltransferase activity of CLOCK is as important as its transcription activity in circadian control. Acetylates metabolic enzymes IMPDH2 and NDUFA9 in a circadian manner (By similarity). Facilitated by BMAL1, rhythmically interacts and acetylates argininosuccinate synthase 1 (ASS1) leading to enzymatic inhibition of ASS1 as well as the circadian oscillation of arginine biosynthesis and subsequent ureagenesis. Drives the circadian rhythm of blood pressure through transcriptional activation of ATP1B1.
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O08786
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CCKAR_MOUSE
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Cholecystokinin receptor type A (CCK-A receptor) (CCK-AR) (Cholecystokinin-1 receptor) (CCK1-R)
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MDVVDSLLMNGSNITPPCELGLENETLFCLDQPQPSKEWQSAVQILLYSFIFLLSVLGNTLVITVLIRNKRMRTVTNIFLLSLAVSDLMLCLFCMPFNLIPNLLKDFIFGSAVCKTTTYFMGTSVSVSTFNLVAISLERYGAICRPLQSRVWQTKSHALKVIAATWCLSFTIMTPYPIYSNLVPFTKNNNQTANMCRFLLPSDAMQQSWQTFLLLILFLIPGVVMVVAYGLISLELYQGIKFDASQKKSAKEKRLSSGGGGGGGSSSSRYEDSDGCYLQKSRPPRKLELQQLSTSSSGGRINRIRSSGSAANLIAKKRVIRMLIVIVVLFFLCWMPIFSANAWRAYDTVSAEKHLSGTPISFILLLSYTSSCVNPIIYCFMNKRFRLGFMATFPCCPNPGPTGVRGEVGEEEDGRTIRASLSRYSYSHMSTSAPPH
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Receptor for cholecystokinin. Mediates pancreatic growth and enzyme secretion, smooth muscle contraction of the gall bladder and stomach. Has a 1000-fold higher affinity for CCK rather than for gastrin. It modulates feeding and dopamine-induced behavior in the central and peripheral nervous system. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system (By similarity).
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O08788
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DCTN1_MOUSE
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Dynactin subunit 1 (150 kDa dynein-associated polypeptide) (DAP-150) (DP-150) (p150-glued)
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MAQSRRHMSSRTPSGSRMSTEASARPLRVGSRVEVIGKGHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRQSQIQVFEDGADTTSPETPDSSASKVLKREGADAAAKTSKLRGLKPKKAPTARKTTTRRPKPTRPASTGVAGPSSSLGPSGSASAGELSSSEPSTPAQTPLAAPIIPTPALTSPGAAPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQMEVAQANRHMSLLTAFMPDSFLRPGGDHDCVLVLLLMPRLICKAELIRKQAQEKFDLSENCSERPGLRGAAGEQLSFAAGLVYSLSLLQATLHRYEHALSQCSVDVYKKVGSLYPEMSAHERSLDFLIELLHKDQLDETVNVEPLTKAIKYYQHLYSIHLAEQPEDSTMQLADHIKFTQSALDCMGVEVGRLRAFLQGGQEATDIALLLRDLETSCSDTRQFCKKIRRRMPGTDAPGIPAALAFGSQVSDTLLDCRKHLTWVVAVLQEVAAAAAQLIAPLAENEGLPVAALEELAFKASEQIYGSPSSSPYECLRQSCTILISTMNKLATAMQEGEYDAERPPSKPPPVELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADERIEKVQTRLDETQTLLRKKEKDFEETMDALQADIDQLEAEKAELKQRLNSQSKRTIEGLRGPPPSGIATLVSGIAGEEPQRGGAPGQAPGALPGPGLVKDSPLLLQQISAMRLHISQLQHENSILRGAQMKASLAALPPLHVAKLSLPPHEGPGGNLVAGALYRKTSQLLEKLNQLSTHTHVVDITRSSPAAKSPSAQLMEQVAQLKSLSDTIEKLKDEVLKETVTQRPGATVPTDFATFPSSAFLRAKEEQQDDTVYMGKVTFSCAAGLGQRHRLVLTQEQLHQLHSRLIS
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Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity). Plays a key role in dynein-mediated retrograde transport of vesicles and organelles along microtubules by recruiting and tethering dynein to microtubules. Binds to both dynein and microtubules providing a link between specific cargos, microtubules and dynein. Essential for targeting dynein to microtubule plus ends, recruiting dynein to membranous cargos and enhancing dynein processivity (the ability to move along a microtubule for a long distance without falling off the track). Can also act as a brake to slow the dynein motor during motility along the microtubule. Can regulate microtubule stability by promoting microtubule formation, nucleation and polymerization and by inhibiting microtubule catastrophe in neurons. Inhibits microtubule catastrophe by binding both to microtubules and to tubulin, leading to enhanced microtubule stability along the axon. Plays a role in metaphase spindle orientation. Plays a role in centriole cohesion and subdistal appendage organization and function. Its recruitment to the centriole in a KIF3A-dependent manner is essential for the maintenance of centriole cohesion and the formation of subdistal appendage. Also required for microtubule anchoring at the mother centriole. Plays a role in primary cilia formation (By similarity).
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O08789
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MNT_MOUSE
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Max-binding protein MNT (Myc antagonist MNT) (Protein ROX)
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MSIETLLEAARFLEWQAQQQQRAREEQERLRLEREREREQEQKRASNLARLAHALPVEEPRIEAPPLPLSPPAPPPAPPPPLATPAPLTVIPIPVVTNSPQSLPPPPPLPPAAQPLPLAPRQPALVSTPGLSIKEPVTLPTRPQVPTPAPLLPDAKTTVAPTGSPKPLQPLPAPILTIAPHPGVQPQLAPQQPPPPTLGTLKLAPAEEAKSSEQKKRPGGIGTREVHNKLEKNRRAHLKECFETLKRNIPNVDDKKTSNLSVLRTALRYIQSLKRKEKEYEHEMERLAREKIATQQRLAELKHELSQWMDVLEIDRVLRQTGQPEDDQASTSTASEGEDNVDEEMEGDRAGLGPPKLNHRPQPELLKSALPTPSTAPAPLPTHPHPHPHPVALSPAHLPVQQQQPPQQKTPLPAPPPPPATPTQTLVPAPAHLVATAGGGSTVIAHTATTHASVIQTVNHVLQGPGGKHIAHIAPSAPSPAVQLAPATPPIGHITVHPATLNHVAHLGSQLPLYPQPVAVSQPVAVSHIAHTLSHQQVNGTAGLGPPATVMAKPAVGAQVVHHPQLVGQTVLNPVTMVTMPSFPVSTLKLA
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Binds DNA as a heterodimer with MAX and represses transcription. Binds to the canonical E box sequence 5'-CACGTG-3' and, with higher affinity, to 5'-CACGCG-3'.
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O08790
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FPRS1_MOUSE
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Formyl peptide receptor-related sequence 1 (FMLP-related receptor I) (FMLP-R-I) (Formyl peptide receptor related sequence 1) (Formyl peptide receptor-like 1) (Lipoxin A4 receptor) (LXA4 receptor) (N-formyl peptide receptor 2) (N-formyl peptide receptor 3)
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METNYSIPLNGSDVVIYDSTISRVLWILSMVVVSITFFLGVLGNGLVIWVAGFRMPHTVTTIWYLNLALADFSFTATLPFLLVEMAMKEKWPFGWFLCKLVHIAVDVNLFGSVFLIAVIALDRCICVLHPVWAQNHRTVSLARNVVVGSWIFALILTLPLFLFLTTVRDARGDVHCRLSFVSWGNSVEERLNTAITFVTTRGIIRFIVSFSLPMSFVAICYGLITTKIHKKAFVNSSRPFRVLTGVVASFFICWFPFQLVALLGTVWLKEMQFSGSYKIIGRLVNPTSSLAFFNSCLNPILYVFMGQDFQERLIHSLSSRLQRALSEDSGHISDTRTNLASLPEDIEIKAI
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Low affinity receptor for N-formyl-methionyl peptides. Receptor for lipoxin A4. May have an olfactory function associated with the identification of pathogens or of pathogenic states.
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O08791
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COE3_MOUSE
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Transcription factor COE3 (Early B-cell factor 3) (EBF-3) (Olf-1/EBF-like 2) (O/E-2) (OE-2)
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MFGIQENIPRGGTTMKEEPLGSGMNPVRSWMHTAGVVDANTAAQSGVGLARAHFEKQPPSNLRKSNFFHFVLALYDRQGQPVEIERTAFVDFVEKEKEPNNEKTNNGIHYKLQLLYSNGVRTEQDLYVRLIDSMTKQAIVYEGQDKNPEMCRVLLTHEIMCSRCCDKKSCGNRNETPSDPVIIDRFFLKFFLKCNQNCLKNAGNPRDMRRFQVVVSTTVNVDGHVLAVSDNMFVHNNSKHGRRARRLDPSEGTAPSYLENATPCIKAISPSEGWTTGGATVIIIGDNFFDGLQVVFGTMLVWSELITPHAIRVQTPPRHIPGVVEVTLSYKSKQFCKGAPGRFVYTALNEPTIDYGFQRLQKVIPRHPGDPERLPKEVLLKRAADLVEALYGMPHNNQEIILKRAADIAEALYSVPRNHNQIPTLGNTPAHTGMMGVNSFSSQLAVNVSETSQANDQVGYSRNTSSVSPRGYVPSSTPQQSNYNTVSTSMNGYGSGAMANLGVPGSPGFLNGSSANSPYGIVPSSPTMAASSVTLPSNCSSTHGIFSFSPANVISAVKQKSAFAPVVRPQASPPPSCTSANGNGLQAMSGLVVPPM
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Transcriptional activator. Recognizes variations of the palindromic sequence 5'-ATTCCCNNGGGAATT-3' (By similarity).
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O08792
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COE2_MOUSE
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Transcription factor COE2 (Early B-cell factor 2) (EBF-2) (Metencephalon-mesencephalon-olfactory transcription factor 1) (MET-mesencephalon-olfactory TF1) (MET-mesencephalon-olfactory transcription factor 1) (Olf-1/EBF-like 3) (O/E-3) (OE-3)
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MFGIQDTLGRGPALKDKSLGAEMDSVRSWVRNVGVVDANVAAQSGVALSRAHFEKQPPSNLRKSNFFHFVLALYDRQGQPVEIERTAFVDFVENDKEQGNEKTNNGTHYKLQLLYSNGVRTEQDLYVRLIDSVTKQPIAYEGQNKNPEMCRVLLTHEVMCSRCCEKKSCGNRNETPSDPVIIDRFFLKFFLKCNQNCLKTAGNPRDMRRFQVVLSTTVNVDGHVLAVSDNMFVHNNSKHGRRARRLDPSEATPCIKAISPSEGWTTGGAMVIIIGDNFFDGLQVVFGTMLVWSELITPHAIRVQTPPRHIPGVVEVTLSYKSKQFCKGAPGRFIYTALNEPTIDYGFQRLQKVIPRHPGDPERLAKEMLLKRAADLVEALYGTPHNNQDIILKRAADIAEALYSVPRNPSQIPALSSSPAHSGMMGINSYGSQLGVSISESTQGNNQGYIRNTSSISPRGYSSSSTPQQSNYSTSSNSMNGYSNVPMANLGVPGSPGFLNGSPTGSPYGIMSSSPTVGSSSTSSILPFSSSVFPAVKQKSAFAPVIRPQGSPSPACSSGNGNGFRAMTGLVVPPM
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Transcription factor that, in osteoblasts, activates the decoy receptor for RANKL, TNFRSF11B, which in turn regulates osteoclast differentiation. Acts in synergy with the Wnt-responsive LEF1/CTNNB1 pathway. Recognizes variations of the palindromic sequence 5'-ATTCCCNNGGGAATT-3'.
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O08795
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GLU2B_MOUSE
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Glucosidase 2 subunit beta (80K-H protein) (Glucosidase II subunit beta) (Protein kinase C substrate 60.1 kDa protein heavy chain) (PKCSH)
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MLLLLLLLLPLCWAVEVKRPRGVSLSNHHFYEESKPFTCLDGTATIPFDQVNDDYCDCKDGSDEPGTAACPNGSFHCTNTGYKPLYILSSRVNDGVCDCCDGTDEYNSGTVCENTCREKGRKEKESLQQLAEVTREGFRLKKILIEEWKTAREEKQSKLLELQAGKKSLEDQVETLRAAKEEAERPEKEAKDQHRKLWEEQQAAAKARREQERAASAFQELDDNMDGMVSLAELQTHPELDTDGDGALSEEEAQALLSGDTQTDTTSFYDRVWAAIRDKYRSEVPPTDIPVPEETEPKEEKPPVLPPTEEEEEEEEEPEEEEEEEEEEEEAPPPLQPPQPPSPTEDEKMPPYDEETQAIIDAAQEARSKFEEVERSLKEMEESIRSLEQEISFDFGPSGEFAYLYSQCYELTTNEYVYRLCPFKLVSQKPKHGGSPTSLGTWGSWAGPDHDKFSAMKYEQGTGCWQGPNRSTTVRLLCGKETVVTSTTEPSRCEYLMELMTPAACPEPPPEAPSDGDHDEL
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Regulatory subunit of glucosidase II that cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins. Required for efficient PKD1/Polycystin-1 biogenesis and trafficking to the plasma membrane of the primary cilia.
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O08796
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EF2K_MOUSE
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Eukaryotic elongation factor 2 kinase (eEF-2 kinase) (eEF-2K) (EC 2.7.11.20) (Calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase)
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MADEDLIFCLEGVDGGRCSRAGHNADSDTDSDDDEGYFICPITDDHMSNQNVSSKVQSYYSNLTKTECGSTGSPASSFHFKEAWKHAIEKAKHMPDPWAEFHLEDIATEHATRHRYNAVTGEWLKDEVLIKMASQPFGRGAMRECFRTKKLSNFLHAQQWKGASNYVAKRYIEPVDRSVYFEDVQLQMEAKLWGEDYNRHKPPKQVDIMQMCIIELKDRPGQPLFHLEHYIEGKYIKYNSNSGFVRDDNIRLTPQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQIHTEKGTDFGDGNLGVRGMALFFYSHACNRICQSMGLTPFDLSPREQDAVNQSTRLLQSAKTILRGTEEKCGSPRIRTLSSSRPPLLLRLSENSGDENMSDVTFDSLPSSPSSATPHSQKLDHLHWPVFGDLDNMGPRDHDRMDNHRDSENSGDSGYPSEKRSDLDDPEPREHGHSNGNRRHESDEDSLGSSGRVCVETWNLLNPSRLHLPRPSAVALEVQRLNALDLGRKIGKSVLGKVHLAMVRYHEGGRFCEKDEEWDRESAIFHLEHAADLGELEAIVGLGLMYSQLPHHILADVSLKETEENKTKGFDYLLKAAEAGDRHSMILVARAFDTGLNLSPDRCQDWSEALHWYNTALETTDCDEGGEYDGIQDEPQYALLAREAEMLLTGGFGLDKNPQRSGDLYTQAAEAAMEAMKGRLANQYYEKAEEAWAQMEE
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Threonine kinase that regulates protein synthesis by controlling the rate of peptide chain elongation. Upon activation by a variety of upstream kinases including AMPK or TRPM7, phosphorylates the elongation factor EEF2 at a single site, renders it unable to bind ribosomes and thus inactive. In turn, the rate of protein synthesis is reduced.
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O08807
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PRDX4_MOUSE
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Peroxiredoxin-4 (EC 1.11.1.24) (Antioxidant enzyme AOE372) (Peroxiredoxin IV) (Prx-IV) (Thioredoxin peroxidase AO372) (Thioredoxin-dependent peroxide reductase A0372) (Thioredoxin-dependent peroxiredoxin 4)
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MEARSKLLDGTTASRRWTRKLVLLLPPLLLFLLRTESLQGLESDERFRTRENECHFYAGGQVYPGEASRVSVADHSLHLSKAKISKPAPYWEGTAVINGEFKELKLTDYRGKYLVFFFYPLDFTFVCPTEIIAFGDRIEEFKSINTEVVACSVDSQFTHLAWINTPRRQGGLGPIRIPLLSDLNHQISKDYGVYLEDSGHTLRGLFIIDDKGVLRQITLNDLPVGRSVDETLRLVQAFQYTDKHGEVCPAGWKPGSETIIPDPAGKLKYFDKLN
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Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation (By similarity).
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O08808
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DIAP1_MOUSE
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Protein diaphanous homolog 1 (Diaphanous-related formin-1) (DRF1) (p140mDIA) (mDIA1)
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MEPSGGGLGPGRGTRDKKKGRSPDELPATGGDGGKHKKFLERFTSMRIKKEKEKPNSAHRNSSASYGDDPTAQSLQDISDEQVLVLFEQMLVDMNLNEEKQQPLREKDIVIKREMVSQYLHTSKAGMNQKESSRSAMMYIQELRSGLRDMHLLSCLESLRVSLNNNPVSWVQTFGAEGLASLLDILKRLHDEKEETSGNYDSRNQHEIIRCLKAFMNNKFGIKTMLETEEGILLLVRAMDPAVPNMMIDAAKLLSALCILPQPEDMNERVLEAMTERAEMDEVERFQPLLDGLKSGTSIALKVGCLQLINALITPAEELDFRVHIRSELMRLGLHQVLQELREIENEDMKVQLCVFDEQGDEDFFDLKGRLDDIRMEMDDFGEVFQIILNTVKDSKAEPHFLSILQHLLLVRNDYEARPQYYKLIEECVSQIVLHKNGTDPDFKCRHLQIDIERLVDQMIDKTKVEKSEAKATELEKKLDSELTARHELQVEMKKMENDFEQKLQDLQGEKDALDSEKQQITAQKQDLEAEVSKLTGEVAKLSKELEDAKNEMASLSAVVVAPSVSSSAAVPPAPPLPGDSGTVIPPPPPPPPLPGGVVPPSPPLPPGTCIPPPPPLPGGACIPPPPQLPGSAAIPPPPPLPGVASIPPPPPLPGATAIPPPPPLPGATAIPPPPPLPGGTGIPPPPPPLPGSVGVPPPPPLPGGPGLPPPPPPFPGAPGIPPPPPGMGVPPPPPFGFGVPAAPVLPFGLTPKKVYKPEVQLRRPNWSKFVAEDLSQDCFWTKVKEDRFENNELFAKLTLAFSAQTKTSKAKKDQEGGEEKKSVQKKKVKELKVLDSKTAQNLSIFLGSFRMPYQEIKNVILEVNEAVLTESMIQNLIKQMPEPEQLKMLSELKEEYDDLAESEQFGVVMGTVPRLRPRLNAILFKLQFSEQVENIKPEIVSVTAACEELRKSENFSSLLELTLLVGNYMNAGSRNAGAFGFNISFLCKLRDTKSADQKMTLLHFLAELCENDHPEVLKFPDELAHVEKASRVSAENLQKSLDQMKKQIADVERDVQNFPAATDEKDKFVEKMTSFVKDAQEQYNKLRMMHSNMETLYKELGDYFVFDPKKLSVEEFFMDLHNFRNMFLQAVKENQKRRETEEKMRRAKLAKEKAEKERLEKQQKREQLIDMNAEGDETGVMDSLLEALQSGAAFRRKRGPRQVNRKAGCAVTSLLASELTKDDAMAPGPVKVPKKSEGVPTILEEAKELVGRAS
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Actin nucleation and elongation factor required for the assembly of F-actin structures, such as actin cables and stress fibers. Binds to the barbed end of the actin filament and slows down actin polymerization and depolymerization. Required for cytokinesis, and transcriptional activation of the serum response factor. DFR proteins couple Rho and Src tyrosine kinase during signaling and the regulation of actin dynamics. Functions as a scaffold protein for MAPRE1 and APC to stabilize microtubules and promote cell migration. Has neurite outgrowth promoting activity. Acts in a Rho-dependent manner to recruit PFY1 to the membrane. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex (By similarity). It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity (By similarity). In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization (By similarity). Required in the control of cell shape (By similarity). Also acts as an actin nucleation and elongation factor in the nucleus by promoting nuclear actin polymerization inside the nucleus to drive serum-dependent SRF-MRTFA activity.
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O08810
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U5S1_MOUSE
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116 kDa U5 small nuclear ribonucleoprotein component (Elongation factor Tu GTP-binding domain-containing protein 2) (U5 snRNP-specific protein, 116 kDa) (U5-116 kDa)
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MDTDLYDEFGNYIGPELDSDEDDDELGRETKDLDEDEDEDEDDVGEHEDDHPGMEVVLHEDKKYYPTAEEVYGPEVETIVQEEDTQPLTEPIIKPVKTKKFTLMEQTLPVTVYEMDFLADLMDNSELIRNVTLCGHLHHGKTCFVDCLIEQTHPEIRKRYDQDLCYTDILFTEQERGVGIKSTPVTVVLPDTKGKSYLFNIMDTPGHVNFSDEVTAGLRISDGVVLFIDAAEGVMLNTERLIKHAVQERLAVTVCINKIDRLILELKLPPTDAYYKLRHIVDEVNGLISMYSTDENLILSPLLGNVCFSSSQYSICFTLGSFAKIYADTFGDINYQEFAKRLWGDIYFNPKTRKFTKKAPSSSSQRSFVEFILEPLYKILAQVVGDVDTSLPRTLDELGIHLTKEELKLNIRPLLRLVCKKFFGEFTGFVDMCVQHIPSPKVGAKPKIEHTYTGGVDSDLGEAMSDCDPDGPLMCHTTKMYSTDDGVQFHAFGRVLSGTIHAGQPVKVLGENYTLEDEEDSQICTVGRLWISVARYHIEVNRVPAGNWVLIEGVDQPIVKTATITEPRGNEEAQIFRPLKFNTTSVIKIAVEPVNPSELPKMLDGLRKVNKSYPSLTTKVEESGEHVILGTGELYLDCVMHDLRKMYSEIDIKVADPVVTFCETVVETSSLKCFAETPNKKNKITMIAEPLEKGLAEDIENEVVQITWNRKKLGEFFQTKYDWDLLAARSIWAFGPDATGPNILVDDTLPSEVDKALLGSVKDSIVQGFQWGTREGPLCDELIRNVKFKILDAVVAQEPLHRGGGQIIPTARRVVYSAFLMATPRLMEPYYFVEVQAPADCVSAVYTVLARRRGHVTQDAPIPGSPLYTIKAFIPAIDSFGFETDLRTHTQGQAFSLSVFHHWQIVPGDPLDKSIVIRPLEPQPAPHLAREFMIKTRRRKGLSEDVSISKFFDDPMLLELAKQDVVLNYPM
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Required for pre-mRNA splicing as component of the spliceosome, including pre-catalytic, catalytic and post-catalytic spliceosomal complexes (By similarity). Component of the U5 snRNP and the U4/U6-U5 tri-snRNP complex, a building block of the spliceosome (By similarity). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (By similarity).
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O08811
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ERCC2_MOUSE
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General transcription and DNA repair factor IIH helicase subunit XPD (TFIIH subunit XPD) (EC 3.6.4.12) (CXPD) (DNA excision repair protein ERCC-2) (DNA repair protein complementing XP-D cells) (Xeroderma pigmentosum group D-complementing protein)
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MKLNVDGLLVYFPYDYIYPEQFSYMLELKRTLDAKGHGVLEMPSGTGKTVSLLALIVAYQRAYPLEVTKLIYCSRTVPEIEKVIEELRKLLSFYEQQEGEKLPFLGLALSSRKNLCIHPEVTPLRFGKDVDGKCHSLTASYVRAQYQQDASLPHCRFYEEFDIHGRQMPLPAGIYNLDDLKALGQRQGWCPYFLARYSILHANVVVYSYHYLLDPKIADLVSKELARKAVVVFDEAHNIDNVCIDSMSVNLTRRTLDRCQSNLDTLQKTVLRIKETDEQRLRDEYRRLVEGLREASVARETDAHLANPVLPDEVLQEAVPGSIRTAEHFLGFLRRLLEYVKWRLRVQHVVQESPPAFLSGLAQRVCIQRKPLRFCAERLRSLLHTLEIADLADFSPLTLLANFATLVSTYAKGFTIIIEPFDDRTPTIANPVLHFSCMDASLAIKPVFERFQSVIITSGTLSPLDIYPKILDFHPVTMATFTMTLARVCLCPMIIGRGNDQVAISSKFETREDIAVIRNYGNLLLEMSAVVPDGIVAFFTSYQYMESTVASWYEQGILENIQRNKLLFIETQDGAETSVALEKYQEACENGRGAILLSVARGKVSEGIDFVHHYGRAVIMFGVPYVYTQSRILKARLEYLRDQFQIRENDFLTFDAMRHAAQCVGRAIRGKTDYGLMVFADKRFARADKRGKLPRWIQEHLTDSNLNLTVDEGVQVAKYFLRQMAQPFHREDQLGLSLLSLEQLQSEETLQRIEQIAQQL
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ATP-dependent 5'-3' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATP-dependent helicase activity of XPD/ERCC2 is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription. XPD/ERCC2 acts by forming a bridge between CAK and the core-TFIIH complex. Involved in the regulation of vitamin-D receptor activity. As part of the mitotic spindle-associated MMXD complex it plays a role in chromosome segregation. Might have a role in aging process and could play a causative role in the generation of skin cancers.
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O08812
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CTR3_RAT
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Cationic amino acid transporter 3 (CAT-3) (CAT3) (Cationic amino acid transporter y+) (Solute carrier family 7 member 3)
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MLWQALRRFGQKLVRRRLLELGMGETRLARCLSTLDLVALGVGSTLGAGVYVLAGEVAKEKAGPSIVICFLVAALSSVLAGLCYAEFGARVPGSGSAYLYSYVTVGELWAFTTGWNLILSYVIGTASVARAWSSAFDNLIGNHISQTLKGTILLNMPHVLAEYPDFFALALVLLLTGLLVLGANESGLVTKVFTGMNLLVLGFVIISGFIKGELRNWKLTKEDYCLTMSESNGTCSLDSMGSGGFMPFGLEGILRGAATCFYAFVGFDCIATTGEEAQNPQRSIPMGIVISLSICFLAYFGVSSALTLMMPYYKLQPESPLPEAFTYVGWEPARYLVAIGSLCALSTSLLGSMFPMPRVIYAMAEDGLLFRVLARVHNGTHTPIVATVVSGVIAAFMAFLFELTDLVDLMSIGTLLAYSLVSICVLILRYQPDQEMKNGEEEVELQEERTLEAEKLTVQALFCQVDSIPTLLSGRIVYVCSSLLAVLLTVLCLVLTWWTTPLHSGDPVWVTVVVLILGLILGISGVIWRQPQNRTPLHFKVPVVPLLPLVSIFVNVYLMMQMTADTWARFGVWMLIGFAIYFGYGIQHSVEEVKNHQTLPKTRPQTIDLDLTTSCVHSI
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Uniporter that mediates the uptake of cationic L-amino acids such as L-arginine, L-lysine and L-ornithine. The transport is sodium ions- and pH-independent, moderately trans-stimulated and is mediated by passive diffusion.
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O08815
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SLK_RAT
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STE20-like serine/threonine-protein kinase (STE20-like kinase) (EC 2.7.11.1) (STE20-related serine/threonine-protein kinase) (STE20-related kinase)
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MSFFNFRKIFKLGSEKKKKQYEHVKRDLNPEEFWEIIGELGDGAFGKVYKAQNKETNVLAAAKVIDTKSEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEFCAGGAVDAVMLELERPLTESQIQVVCKQTLEALNYLHDNKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRTIQRRDSFIGTPYWMAPEVVMCETSKDRPYDYKADVWSLGITLIEMAEIEPPHHELNPMRVLLKIAKSEPPTLAQPSRWSSNFKDFLKKCLEKNVDARWTTSQLLQHPFVTVDSNKPVRELIAEAKAEVTEEVEDGKEEDDDDETESALPIPANKRASSDLSIASSEEDKLSQNACILESVSERTEHNTSGDKFSNKVLSEKPTPEGPEKTVDVDGPANDVNLETVAEPNDQAVGFHENGREKKRPQLESQPDTEDQQTVDVNLVGEGNDSNIVILETNTDCLKPEEDRNEENQEIIENKLTQSEEIKDIHIQTMDLVSQETGEKEADFQAIDNEVGFTKEETQEKLGKDDKTHKVVISDITSEVGTDEPPGDTQKSAEQSQDAEGGAGEEAPEPAQTLTEKATEGPEAHGAEEEPRSGERVEDKQLEQQSAVCEGEGQVTSTSESTRATTEEPETDEVDQVSESNSIEELERLGVTGAEEQALGSKGEAATELDLEREENAQELPVKAEPQAPAASQASEPPPVLIPSINIHSENTENKGEMGALPKPETILPPEPENGKGNDTDSGTGSTVENSSSDLNLSISSFLSKTKDSGSVSLQETRRQKKTLKKTRKFIVDGVEVSVTTSKIVTDSDSKTEELRFLRRQELRELRLLQKEEQKAQQQLNGKLQQQREQIFRRFEQEMLSKKRQYDQEIENLEKQQKQTIERLEQEHTNRLRDEAKRIKGEQEKELSKFQNMLRNRKKEEQEFVQKQQQELDGALKKIIQQQKAELANIERECLNNKQQLLRAREAAIWELEERHLQEKHQLLKQQLKDQYFIQRHQLLKRHEKETEQMQRYNQRLIEELKNRQTQERARLPKIQRSEAKTRMAMFKKSLRINSTATPDQDREKIKQFAAQEEKRQKNERMAQHQKHESQMRDLQLQCEANVRELHQLQNEKCHLLVEHETQKLKELDEEHSQELKEWREKLRPRKKTLEEEFARKLQEQEVFFKMTGESECLNPSAQSRGCLQTSHPSSTRAPAWAG
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Mediates apoptosis and actin stress fiber dissolution.
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O08816
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WASL_RAT
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Actin nucleation-promoting factor WASL (Neural Wiskott-Aldrich syndrome protein) (N-WASP)
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MSSGQQPPRRVTNVGSLLLTPQENESLFSFLGKKCVTMSSAVVQLYAADRNCMWSKKCSGVACLVKDNPQRSYFLRIFDIKDGKLLWEQELYNNFVYNSPRGYFHTFAGDTCQVALNFANEEEAKKFRKAVTDLLGRRQRKSEKRRDAPNGPNLPMATVDIKNPEITTNRFYSSQVNNISHTKEKKKGKAKKKRLTKADIGTPSNFQHIGHVGWDPNTGFDLNNLDPELKNLFDMCGISEAQLKDRETSKVIYDFIEKTGGVEAVKNELRRQAPPPPPPSRGGPPPPPPPPHSSGPPPPPARGRGAPPPPPSRAPTAAPPPPPPSRPGVVVPPPPPNRMYPPPPPALPSSAPSGPPPPPPLSMAGSTAPPPPPPPPPPPGPPPPPGLPSDGDHQVPASSGNKAALLDQIREGAQLKKVEQNSRPVSCSGRDALLDQIRQGIQLKSVSDGQESTPPTPAPTSGIVGALMEVMQKRSKAIHSSDEDEDDDDEEDFQDDDEWED
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Regulates actin polymerization by stimulating the actin-nucleating activity of the Arp2/3 complex. Involved in various processes, such as mitosis and cytokinesis, via its role in the regulation of actin polymerization. Together with CDC42, involved in the extension and maintenance of the formation of thin, actin-rich surface projections called filopodia. In addition to its role in the cytoplasm, also plays a role in the nucleus by regulating gene transcription, probably by promoting nuclear actin polymerization (By similarity). Binds to HSF1/HSTF1 and forms a complex on heat shock promoter elements (HSE) that negatively regulates HSP90 expression. Plays a role in dendrite spine morphogenesis (By similarity).
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O08832
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GALT4_MOUSE
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Polypeptide N-acetylgalactosaminyltransferase 4 (EC 2.4.1.41) (Polypeptide GalNAc transferase 4) (GalNAc-T4) (pp-GaNTase 4) (Protein-UDP acetylgalactosaminyltransferase 4) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4)
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MAVRWTWAGKSCLLLALLTLAYILVEFSVSTLYASPGAGGARELGPRRLPDLDTREEDLSQPLYIKPPADSHALGEWGRASKLQLNEGELKQQEELIERYAINIYLSDRISLHRHIEDKRMYECKAKKFHYRSLPTTSVIIAFYNEAWSTLLRTIHSVLETSPAVLLKEIILVDDLSDRIYLKAQLETYISNLERVRLIRTNKREGLVRARLIGATFATGDVLTFLDCHCECNTGWLEPLLERISRDETAIVCPVIDTIDWNTFEFYMQTGEPMIGGFDWRLTFQWHSVPKHERDRRTSRIDPIRSPTMAGGLFAVSKKYFQYLGTYDTGMEVWGGENLELSFRVWQCGGKLEIHPCSHVGHVFPKRAPYARPNFLQNTARAAEVWMDEYKEHFYNRNPPARKEAYGDLSERKLLRERLKCKSFDWYLKNVFSNLHVPEDRPGWHGAIRSMGISSECLDYNAPDNNPTGANLSLFGCHGQGGNQFFEYTSNKEIRFNSVTELCAEVPQQKDYVGMQNCPKDGLPVPVNIIWHFKEDGTIFHPHTRLCLSAYRTAEGRPSVHMKTCDALDKNQLWRFEK
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Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a highest activity toward EA2 peptide substrate and a much lower activity with EPO-T, Muc2, Muc1a, Muc1b.
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O08835
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SYT11_RAT
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Synaptotagmin-11 (Synaptotagmin XI) (SytXI)
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MAEITNIRPSFDVSPVAAGLIGASVLVVCVSVTVFVWTCCHQQAEKKHKTPPYKFIHMLKGISIYPETLSNKKKIIKVRRDKDGSHRESGRGNLLVNAESGLLSHDRDPRGPSPASCIDQLPIKRDYGEELRSPMTSLTPGESKPTSPSSPEEDVMLGSLTFSVDYNFPKKALVVTIQEAHGLPVMDGQTQGSDPYIKMTILPDKRHRVKTRVLRKTLDPVFDETFTFYGIPYSQLQDLVLHFLVLSFDRFSRDDVIGEVMVPLAGVDPSTGKVQLTRDIIKRNIQKCISRGELQVSLSYQPVAQRMTVVVLKARHLPKMDITGLSGNPYVKVNVYYGRKRIAKKKTHVKKCTLNPIFNESFIYDIPTDLLPDISIEFLVIDFDRTTKNEVVGRLILGAHSVTTSGAEHWREVCESPRKPVAKWHSLSEY
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Synaptotagmin family member involved in vesicular and membrane trafficking which does not bind Ca(2+). Inhibits clathrin-mediated and bulk endocytosis in neurons, functions to ensure precision in vesicle retrieval. Plays an important role in dopamine transmission by regulating endocytosis and the vesicle-recycling process. Essential component of a neuronal vesicular trafficking pathway that differs from the synaptic vesicle trafficking pathway but is crucial for development and synaptic plasticity. In macrophages and microglia, inhibits the conventional cytokine secretion, of at least IL6 and TNF, and phagocytosis. In astrocytes, regulates lysosome exocytosis, mechanism required for the repair of injured astrocyte cell membrane (By similarity). Required for the ATP13A2-mediated regulation of the autophagy-lysosome pathway (By similarity).
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O08836
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IGBP1_RAT
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Immunoglobulin-binding protein 1 (Alpha4 phosphoprotein) (CD79a-binding protein 1) (Protein phosphatase 2/4/6 regulatory subunit)
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MAASEEELLLPRLPELFETSKKLLEELEVATEPTGSRTIQDKVSKGLELLEKAAGMLSQLDLFSRNEDLEEIASIDLKYLMVPALQGALTMKQVNPSKRLDHLQRAREHFIHFLTQCHCYHVAEFQLPQTKNNSAENNTARSSMAYPNLVAMASQRQAKIERYKQKKEVEHRLSALKSAVESGQADDERVREYYLLHLRRWIGISLEEIESIDQEIKILKDKDSPREESACQSSLPEKPPMKPFILTRNKAQAKVFGTGYPSLATMTVSDWYEQHQKYGALPDRGIAKPPSADFQRAAQQQEDQEQKDEENEEKALHRMREWDDWKDTHPRGYGNRQNMG
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Associated to surface IgM-receptor may be involved in signal transduction. Involved in regulation of the catalytic activity of the phosphatases PP2A, PP4 and PP6 by protecting their partially folded catalytic subunits from degradative polyubiquitination until they associate with regulatory subunits (By similarity).
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O08837
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CDC5L_RAT
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Cell division cycle 5-like protein (Cdc5-like protein) (Pombe Cdc5-related protein)
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MPRIMIKGGVWRNTEDEILKAAVMKYGKNQWSRIASLLHRKSAKQCKARWYEWLDPSIKKTEWSREEEEKLLHLAKLMPTQWRTIAPIIGRTAAQCLEHYEFLLDKTAQRDNEEETTDDPRKLKPGEIDPNPETKPARPDPIDMDEDELEMLSEARARLANTQGKKAKRKAREKQLEEARRLAALQKRRELRAAGIEIQKKRKKKRGVDYNAEIPFEKKPALGFYDTSEENYQALDADFRKLRQQDLDGELRSEKEGRDRKKDKQHLKRKKESDLPSAILQTSGVSEFTKKRSKLVLPAPQISDAELQEVVKVGQASEVARQTAEESGITNSASSTLLSEYNVTNNSIALRTPRTPASQDRILQEAQNLMALTNVDTPLKGGLNTPLHESDFSGVTPQRQVVQTPNTVLSTPFRTPSNGAEGLTPRSGTTPKPVTNATPGRTPLRDKLNINPEDGMADYSDPSYVKQMERESREHLRLGLLGLPAPKNDFEIVLPENAEKELEEREMDDTYIEDAADVDARKQAIRDAERVKEMKRMHKAVQKDLPRPSEVNETILRPLNVEPPLTDLQKSEELIKKEMITMLHYDLLHHPYEPSGNKKGKNVGFATNNSEHITYLEHSPYEKFSKEDLKKAQDVLVQEMEVVKQGMSHGELSSEAYNQVWEECYSQVLYLPAQSRYTRANLASKKDRIESLEKRLEINRGHMTTEAKRAAKMEKKMKILLGGYQSRAMGLLKQLNDLWDQIEQAHLELRTFEELKKHEDSAIPRRLECLKEDVQRQQEREKELQQRYADLLMEKETLQAKF
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DNA-binding protein involved in cell cycle control. May act as a transcription activator. Plays a role in pre-mRNA splicing as core component of precatalytic, catalytic and postcatalytic spliceosomal complexes. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. The PRP19-CDC5L complex may also play a role in the response to DNA damage (DDR). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs.
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O08838
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AMPH_RAT
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Amphiphysin
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MADIKTGIFAKNVQKRLNRAQEKVLQKLGKADETKDEQFEEYVQNFKRQEAEGTRLQRELRGYLAAIKGMQEASMKLTESLHEVYEPDWYGREDVKMVGEKCDVLWEDFHQKLVDGSLLTLDTYLGQFPDIKNRIAKRSRKLVDYDSARHHLEALQSSKRKDESRISKAEEEFQKAQKVFEEFNVDLQEELPSLWSRRVGFYVNTFKNVSSLEAKFHKEIAVLCHKLYEVMTKLGDQHADKAFSIQGAPSDSGPLRIAKTPSPPEEASPLPSPTASPNHTLAPASPAPVRPRSPSQTRKGPPVPPLPKVTPTKELQQENIINFFEDNFVPEINVTTPSQNEVLEVKKEETLLDLDFDPFKPDVTPAGSAAATHSPMSQTLPWDLWTTSTDLVQPASGGSFNDFTQPQDTSLFTMQTDQNMAETEQALPTEPQAEEPPTTAAAPTAGLDLGLEMEEPKEEAAIPPGTDAGETVGTEGSTGEEAEAEKAALPAGEGESPEGAKIDVESTELASSESPQAAELEAGAPQEKVIPSVVIEPASNHEGEEHQETTTGTETREATEDVAPQGPAGEKQELATEPTPLDSQAATPAPAGAVDASLSAGDAAQELPPGFLYKVETLHDFEAANSDELTLQRGDVVLVVPSDSEADQDAGWLVGVKESDWLQYRDLATYKGLFPENFTRHLE
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May participate in mechanisms of regulated exocytosis in synapses and certain endocrine cell types. May control the properties of the membrane associated cytoskeleton (By similarity).
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O08839
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BIN1_RAT
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Myc box-dependent-interacting protein 1 (Amphiphysin II) (Amphiphysin-like protein) (Bridging integrator 1)
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MAEMGSKGVTAGKIASNVQKKLTRAQEKVLQKLGKADETKDEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAMHEASKKLSECLQEVYEPEWPGRDEANKIAENNDLLWMDYHQKLVDQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESLQTAKKKDEAKIAKPVSLLEKAAPQWCQGKLQAHLVAQTNLLRNQAEEELIKAQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKEMSKLNQNLNDVLVSLEKQHGSNTFTVKAQPSDSAPEKGNKSPSPPPDGSPAATPEIRVNHEPEPASGASPGATIPKSPSQLRKGPPVPPPPKHTPSKEMKQEQILSLFDDAFVPEISVTTPSQFEAPGPFSEQASLLDLDFEPLPPVASPVKAPTPSGQSIPWDLWEPTESQAGVLPSGEPSSAEGSFAVAWPSQTAEPGPAQPAEASEVVGGTQEPGETAASEATSSSLPAVVVETFSATVNGAVEGSTTTGRLDLPPGFMFKVQAQHDYTATDTDELQLKAGDVVLVIPFQNPEEQDEGWLMGVKESDWNQHKELEKCRGVFPENFTERVQ
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Is a key player in the control of plasma membrane curvature, and membrane shaping and remodeling. Required in muscle cells for the formation of T-tubules, tubular invaginations of the plasma membrane that function in depolarization-contraction coupling. Required in muscle cells for the formation of T-tubules, tubular invaginations of the plasma membrane that function in depolarization-contraction coupling (By similarity). Is a negative regulator of endocytosis. Is also involved in the regulation of intracellular vesicles sorting, modulation of BACE1 trafficking and the control of amyloid-beta production (By similarity). In neuronal circuits, endocytosis regulation may influence the internalization of PHF-tau aggregates. May be involved in the regulation of MYC activity and the control cell proliferation (By similarity).
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O08841
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QSOX1_CAVPO
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Sulfhydryl oxidase 1 (EC 1.8.3.2) (FAD-dependent sulfhydryl oxidase-3) (SOx-3) (Glandular epithelial cells protein 3) (Quiescin Q6)
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MTGCGRRSGWLPPLRLLLLPLLLGGPGVGAAQLAALYSASDPLTLLQADTVRSTVLNSPSAWAVEFFASWCGHCIAFAPTWKALAKDIKDWRPALNLAALNCADETNNAVCRDFNIAGFPSVRFFKAFSKNSTGTTLPVAGANVQMLRERLIDALESHHDTWPSACPPLEPVKPKEIDTFFARNNQEYLVLIFEQENSYLGREVTLDLSQHHDLVVRRVLSTEANVVRKFGVADFPSCYLLFRNGSVSRVPVLVESRRFYTAYLQRLSEVTREGTPTPAVPTISDQIAPTVWKFADRSKIYMADLESALHYILRVEVGRFSVLEGQRLMALKKFVTVLTKYFPGQPLVRNFLQSTNEWLKRQHKKKMPYSFFKTAMDSRNEEAVITKEVNWVGCQGSESHFRGFPCSLWILFHFLTVQASQKNAESSQKPANGQEVLQAIRNYVRFFFGCRDCANHFEQMAAGSMHRVKSPNDAVLWLWTSHNRVNARLAGAPSEDPQFPKVQWPPPELCSACHNELSGEPVWDVDATLRFLKTHFSPSNIVLNFPPAEPASRSSVHSWGATPHLELDALGLVTRNSALALERAEISESPGSNAMPNIPAERPELFEALSHSR
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Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide. Plays a role in disulfide bond formation in a variety of extracellular proteins. In fibroblasts, required for normal incorporation of laminin into the extracellular matrix, and thereby for normal cell-cell adhesion and cell migration.
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O08842
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GFRA2_MOUSE
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GDNF family receptor alpha-2 (GDNF receptor alpha-2) (GDNFR-alpha-2) (GFR-alpha-2) (GDNF receptor beta) (GDNFR-beta) (Neurturin receptor alpha) (NRTNR-alpha) (NTNR-alpha) (TGF-beta-related neurotrophic factor receptor 2)
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MILANAFCLFFFLDETLRSLASPSSPQGSELHGWRPQVDCVRANELCAAESNCSSRYRTLRQCLAGRDRNTMLANKECQAALEVLQESPLYDCRCKRGMKKELQCLQIYWSIHLGLTEGEEFYEASPYEPVTSRLSDIFRLASIFSGTGADPVVSAKSNHCLDAAKACNLNDNCKKLRSSYISICNREISPTERCNRRKCHKALRQFFDRVPSEYTYRMLFCSCQDQACAERRRQTILPSCSYEDKEKPNCLDLRSLCRTDHLCRSRLADFHANCRASYRTITSCPADNYQACLGSYAGMIGFDMTPNYVDSNPTGIVVSPWCNCRGSGNMEEECEKFLKDFTENPCLRNAIQAFGNGTDVNMSPKGPTFSATQAPRVEKTPSLPDDLSDSTSLGTSVITTCTSIQEQGLKANNSKELSMCFTELTTNISPGSKKVIKLYSGSCRARLSTALTALPLLMVTLAQ
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Receptor for neurturin. Mediates the NRTN-induced autophosphorylation and activation of the RET receptor. Also able to mediate GDNF signaling through the RET tyrosine kinase receptor.
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O08848
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RO60_MOUSE
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RNA-binding protein Ro60 (60 kDa SS-A/Ro ribonucleoprotein) (60 kDa Ro protein) (60 kDa ribonucleoprotein Ro) (RoRNP) (TROVE domain family member 2)
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MEGSANQLQPLSETQVVNSEGGCVWQVTDMNRLRRFLCFGSEGGTYYIKEQKLGLENAEALIRLIEDGRGCEVIQEIKSFSQEGRTAKQEPLLFALAVCSQCADINTKQAAFKAVPEVCRIPTHLFTFIQFKKDLKESMKCGMWGRALRKAVADWYNEKGGMAVALVVTKYKQRNGWSHKDLLRLSHLKPSSEGLAIVTKYITKGWKEVHEEYKEKALSVEAEKLLKYLEAVEKVKRTKDDLEVIHLIEEHQLVREHLLTNHLKSKEVWKALLQEMPLTALLRNLGKMTANSVLEPGNSEVSLICEKLSNEKLLKKARIHPFHVLIALETYRAGHGLRGKLKWIPDKDILQALDAAFYTTFKTVEPTGKRFLLAVDVSASMNQRALGSVLNASTVAAAMCMVVTRTEKESSVVAFACDMVPFPVTTDMTLQQVLTAMNKVPAGNTDCSLPMIWAQKTDTAADVFVVFTDNETFAGQVHPAVALREYRKKMDIPAKLIVCGMTSNGFTIADPDDRGMLDMCGFDTAALDVIRNFTLDVI
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RNA-binding protein that binds to misfolded non-coding RNAs, pre-5S rRNA, and several small cytoplasmic RNA molecules known as Y RNAs (By similarity). May play roles in cilia formation and/or maintenance.
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O08849
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RGS2_MOUSE
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Regulator of G-protein signaling 2 (RGS2)
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MQSAMFLAVQHDCVPMDKSAGNGPKVEEKREKMKRTLLKDWKTRLSYFLQNSSAPGKPKTGKKSKQQTFIKPSPEEAQLWAEAFDELLASKYGLAAFRAFLKSEFCEENIEFWLACEDFKKTKSPQKLSSKARKIYTDFIEKEAPKEINIDFQTKSLIAQNIQEATSGCFTTAQKRVYSLMENNSYPRFLESEFYQDLCKKPQITTEPHAT
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Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form (By similarity). It is involved in the negative regulation of the angiotensin-activated signaling pathway (By similarity). Plays a role in the regulation of blood pressure in response to signaling via G protein-coupled receptors and GNAQ. Plays a role in regulating the constriction and relaxation of vascular smooth muscle. Binds EIF2B5 and blocks its activity, thereby inhibiting the translation of mRNA into protein (By similarity).
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O08852
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PKD1_MOUSE
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Polycystin-1 (Autosomal dominant polycystic kidney disease 1 protein homolog)
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MPLGAPALLALALGLGLWLGALAGDPGRGCGPCPLPCFCGPAPDAACRVNCSGRWLQTLGPSLRIPADATALDLSHNLLQTLDIGLLVNLSALVELDLSNNRISTLEEGVFANLFNLSEINLSGNPFECNCGLAWLPRWAKEHQVHVVQSEATTCRGPIPLAGQPLLSIPLLDNACGEEYVACLPDNSSGAVAAVPFYFAHEGPLETEACSAFCFSAGEGLAALSEQNQCLCGAGQASNSSAACSSWCSSISLSLNSACGGPTLLQHTFPASPGATLVGPHGPLASGQPADFHITSSLPISSTRWNFGDGSPEVDMASPAATHFYVLPGSYHMTVVLALGAGSALLETEVQVEATPTVLELVCPSFVHSNESLELGIRHRGGSALEVTYSILALDKEPAQVVHPLCPLDTEIFPGNGHCYRLVAEKAPWLQAQEQCRTWAGAALAMVDSPAIQHFLVSKVTRSLDVWIGFSSVEGTEGLDPRGEAFSLESCQNWLPGEPHPATAEHCVRLGPAGQCNTDLCSAPHSYVCELRPGGPVWDTENFVMGMSGGGLSGPLHPLAQQETVQGPLRPVEVMVFPGLSPSREAFLTAAEFSTQKLEEPAQMRLQVYRPSGGAAAVPEGSSEPDNRTEPAPKCVPEELWCPGANVCIPFDASCNSHVCINGSVSRLGLSRASYTLWKEFFFSVPAGPPTQYLVTLHSQDVPMLPGDLIGLQHDAGPGTLLQCPLASSCPGQALYLSTNASDWMTNLPVHLEEAWAGPVCSLQLLLVTERLTPLLGLGPNPGLQHPGHYEVRATVGNSVSRQNLSCSFSVVSPIAGLRVIHPIPLDGHIYVPTNGSVLVLQVDSGANATATAQWFGGNISAPFEDACPPEVDFLKQDCTEEANGTLFSVLMLPRLKEGDHTVEIVAQNGASQANLSLRVTAEEPICGLRAVPSPEARVLQGILVRYSPMVEAGSDVAFRWTIDDKQSLTFHNTVFNVIYQSAAIFKLSLTASNHVSNITVNYNVTVERMNKMHGLWVSAVPTVLPPNATLALTGGVLVDSAVEVAFLWNFGDGEQVLRQFKPPYDESFQVPDPTVAQVLVEHNTTHIYTTPGEYNLTVLVSNTYENLTQQVTVSVRTVLPNVAIGMSSNVLVAGQPITFSPYPLPSTDGVLYTWDFGDGSPVLIQSQPVLNHTYSMTGAYRITLEVNNTVSSVTAHADIRVFQELHGLTVYLSPSVEQGAPMVVSASVESGDNITWTFDMGDGTVFTGPEATVQHVYLRAQNFTVTVEAANPAGHLSQSLHVQVFVLEVLHIEPSTCIPTQPSAQLMAHVTGDPVHYLFDWTFGDGSSNVTVHGHPSVTHNFTRSGIFPLALVLSSHVNKAHYFTSICVEPEIRNITLQPERQFVKLGDEARLVAYSWPPFPYRYTWDFGTEDTTHTQTGGSEVKFIYREPGSYLVIVTVSNNISSTNDSAFVEVQEPVLVTGIRINGSHVLELQQPYLLSAMGSGSPATYLWELGDGSQSEGPEVTHIYSSTGDFTVRVSGWNEVSRSEAQLNITVKQRVRGLTINASRTVVPLNGSVSFSTLLEVGSDVHYSWVLCDRCTPIPGGPTISYTFRSVGTFNIIVTAENEVGSAQDSIFIYVLQFIEGLQVAGGDNGCCFPTNYTLQLQAAVRDGTNISYSWTAQQEGSLITLFGSGKCFSLTSLKASTYYVHLRATNMLGSAAANRTIDFVEPVESLILSASPNPAAVNMSLTLCAELAGGSGVVYTWYLEEGLSWKTSMPSTTHTFAAPGLHLVRVTAENQLGSVNATVEVAIQVPVGGLSIRTSEPDSIFVAAGSTLPFWGQLAEGTNVTWCWTLPGGSKDSQYIAVRFSTAGSFSLQLNASNAVSWVSAMYNLTVEEPIVNLMLWASSKVVAPGQPVHFEILLAAGSALTFRLQVGGSVPEVLPSPHFSHSFFRVGDHLVNVQAENHVSHAQAQVRILVLEAVVGLQVPNCCEPGMATGTEKNFTARVQRGSRVAYAWYFSLQKVQGDSLVILSGRDVTYTPVAAGLLEIHVRAFNELGGVNLTLMVEVQDIIQYVTLQSGRCFTNRSARFEAATSPSPRRVTYHWDFGDGTPVQKTEEFWADHYYLRPGDYHVEVNATNLVSFFVAQATVTVQVLACREPEVEVALPLQVLMRRSQRNYLEAHVDLRNCVSYQTEYRWEIYRTASCQRPGRMAQMVLPGVDVSRPQLVVPRLALPVGHYCFVFVVSFGDTPLARSIQANVTVAAERLVPIIEGGSYRVWSDTQDLVLDGSKSYDPNLEDGDQTPLNFHWACVASTQSETGGCVLNFGPRGSSVVTIPLERLEAGVEYTFNLIVWKAGRKEEATNQTVLIRSGRVPIVSLECVSCKAQAVYEVSRSSYVYLEGHCHNCSRGYKQGCWAARTFSNKTLVLNETTTSTGSTGMNLVVRPGALRDGEGYIFTLTVLGHSGEEEGCASIRLSPNRPPLGGSCRLFPLDSVRGLTTKVHFECTGWRDAEDGGAPLVYALLLKRCRQSYCENFCIYKGSLSTYGAVLPPGFQPLFVVSLAVVVQDQLGAAVVALNRSLTIVLPEPSGNPADLVPWLHSLTASVLPGLLKQADPQHVIEYSLALITVLNEYEQAPDVSEPNVEQQLRAQMRKNITETLISLRVNTVDDIQQITAALAQCMVSSRELMCRSCLKKMLQKLEGMMRILQAETTEGTLTPTTIADSILNITGDLIHLASLDMQGPQPLELGVEPPSLMVASKAYNLSSALMRILMRSRVLNEEPLTLAGEEIVALGKRSDPLSLLCYGKALGPSCHFSIPEAFSGALSNLSDVVQLIFLVDSNPFPFGYISNYTVSTKVASMAFQTQTGTQIPIEQLAAERAITVKVPNNSDQAAQSSHNPVGSTIVQPQTSVSAVVTADNSNPQAGLHLRITYTVLNERYLSAEPEPYLAVYLHSVSQPNEYNCSASRRISLEVLEGADHRLYTFFIAPGTGTLDRSYYLNLTSHFHWSALEVSVGLYTSLCQYFSEEMMMWRTEGIVPLEETSPSQAVCLTRHLTAFGASLFVPPSHVQFIFPEPSASINYIVLLTCVICLVTYVVMAMILRKLDQLDVSRVRVIPFCGKGGRFKYEILVKTGWSRGSGTTAHVGIMLYGEDNRSGHRHLDGDRAFHRNSLDIFQIATPHSLGSVWKIRVWHDNKGLSPAWFLQHIIVRDLQSARSTFFLVNDWLSVETEANGGLVEKEVLAANEAALWQFQRLLVAELQRGFFDKHIWLSIWDRPPRSRFTRVQRVTCCVLLLCLFLAANAVWYGVVRDTTYSMGPVSSLISPGVDTVAIGLVSSVVVYPVYLAVLFLFRMSRSKVSGDQNPTPTGQQALDVDSYLDPSVLDSSLLTLSGLTEAFAGQVKNDLFLEDAKSLVCWPSSEGTLSWPDLLSDPSVVSSTLQRLTQGRPGCMLGSEEDGASLVSPSLPAKYLSASDEDLIHQVLADGANNLVPTQDTLLETDLLTSLSSVPGEKTETLILQTVGEERPASMGLSWEQSPVTRLSRTGLVEGFQKRLLPAWCAPLAHGLSLLLVAVAVAVSGWIGASFPPSVSVMWLLSSSSSFLASFLGWEPLKVLLEALYFSLVAKRLHPDEDDTLVESPAVTPVSERVPRVRPPHGFALFLAKEEARKVKRLHDMLKRLLVYMLFLLVTLLANYGDASCHGHAYRLQSAIKQELDSQAFLAITRSDEFWPWMSHVFLPYVHGNQSSPELGPPRLRQVRLQEAFCPDPSSSEHMCSAAGSLSTSDYGIGWQSVVQNGSETWAYSAPDLLGAWYWGYCAVYDSGGYIQELGLSLEESRARLGFLQLHNWLDSRSRAVFVELTRYSPAVGLHAAVTLRLEFPVAGHALAAFSVRPFALRRLSTGLSLPLLTSVCLLLFALYFSMAEVQTWRKDGCACTARPDTWARCLLVILTAATGLVRLAQLGIADRQWTHFVQDHPRHFTSFDQVAQLGSVARGLAASLLFLLLVKAAQQLRFVRQWSVFGKTLCRALPELMGATLGLVLLGVAYAQMAILLISSGADTLYNMARAFLVLCPGARVPTLCPSESWYLSPLLCVGLWALRVWGALRLGAILLRWRYHALRGELYRPAWEPQDYEMVELFLRRLRLWMGFSKVKEFRHKVRFEGMDPLPSRSSRGSKSSPVVLPPSSGSEASHPSTSSSQPDGPSASLSRSTLKLEPEPSRLHAVFESLLVQFDRLNQATEDVYQLEQQLQSLQGHGHNGPPSSPSPGCFPGSQPALPSRLSRASQGLDQTVGPNRVSLWPNNKVHPSST
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Component of a heteromeric calcium-permeable ion channel formed by PKD1 and PKD2 that is activated by interaction between PKD1 and a Wnt family member, such as WNT3A and WNT9B. Both PKD1 and PKD2 are required for channel activity (By similarity). Involved in renal tubulogenesis. Involved in fluid-flow mechanosensation by the primary cilium in renal epithelium. Acts as a regulator of cilium length, together with PKD2. The dynamic control of cilium length is essential in the regulation of mechanotransductive signaling. The cilium length response creates a negative feedback loop whereby fluid shear-mediated deflection of the primary cilium, which decreases intracellular cAMP, leads to cilium shortening and thus decreases flow-induced signaling. May be an ion-channel regulator. Involved in adhesive protein-protein and protein-carbohydrate.
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O08856
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ELL_MOUSE
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RNA polymerase II elongation factor ELL (Eleven-nineteen lysine-rich leukemia protein)
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MAALKEARSYGLSCGRVSDGSRVSVFHVKLTDSALKAFESYRAHQDSVSLRPSIRFEGSQGHISIPQPDCPEEVRAFSFYLSNIGRDSPQGSFDCIQQYVSSYGDVHLDCLGSIQDKVTVCATDDSYQKARQSMAQAEEETRSRSAIVIKAGGRYMGKKVQFRKPAPGAADAVPSRKRATPINLASAIRKSSGSGASSVVQRPFRDRVLHLLALRPYRKAELLLRLQKDGLTQADKDTLDSLLQQVASVNPKDGTCTLQDCMYKSLQKDWPGYSEGDRQLLKRMLMRKLCQPQNATTDSSPPREHGRSASPSQKRPTDFIDPLASKKPRISHFTQRAQPTLNGKLGAPNGHETLLPAPGPTPSDTLSSSHLPPRLEPPRTHDPLADVSNDLGHSTQDYKHQEATPAPAPHLGLPLLTDFPQAEQPTSSSHTHSRPKKKSKKHKDKERPPEERPPAPQPDAPTAPALPPDAPGLNGACDNEPTSSSETPDYLLKYPAISSSEQRQSYKNDFNAEYSEYRSLHARIEQITRRFTQLDAQLRQLSQGSDEYETTRGQILQEYRKIKKTNTNYSCEKRRCEYLHRKLAHIKRLIAEYDQRQLQAWP
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Elongation factor component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. Specifically required for stimulating the elongation step of RNA polymerase II- and III-dependent snRNA gene transcription. ELL also plays an early role before its assembly into in the SEC complex by stabilizing RNA polymerase II recruitment/initiation and entry into the pause site. Required to stabilize the pre-initiation complex and early elongation. Specifically required for stimulating the elongation step of RNA polymerase II- and III-dependent snRNA gene transcription (By similarity). Elongation factor component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III. {ECO:0000250, ECO:0000269|PubMed:22195968}.
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O08858
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SSR5_MOUSE
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Somatostatin receptor type 5 (SS-5-R) (SS5-R) (SS5R)
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MEPLSLTSTPSWNASAASSSSHNWSLVDPVSPMGARAVLVPVLYLLVCTVGLGGNTLVIYVVLRYAKMKTVTNVYILNLAVADVLFMLGLPFLATQNAVSYWPFGSFLCRLVMTLDGINQFTSIFCLMVMSVDRYLAVVHPLRSARWRRPRVAKLASAAVWVFSLLMSLPLLVFADVQEGWGTCNLSWPEPVGLWGAAFITYTSVLGFFGPLLVICLCYLLIVVKVKAAGMRVGSSRRRRSERKVTRMVVVVVLVFVGCWLPFFIVNIVNLAFTLPEEPTSAGLYFFVVVLSYANSCANPLLYGFLSDNFRQSFRKALCLRRGYGVEDADAIEPRPDKSGRPQTTLPTRSCEANGLMQTSRL
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Receptor for somatostatin-28. The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase. Increases cell growth inhibition activity of SSTR2 following heterodimerization.
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O08859
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TSG6_MOUSE
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Tumor necrosis factor-inducible gene 6 protein (TNF-stimulated gene 6 protein) (TSG-6) (Tumor necrosis factor alpha-induced protein 6) (TNF alpha-induced protein 6)
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MVVLLCLCVLLWEEAHGWGFKNGIFHNSIWLEQAAGVYHREARAGRYKLTYAEAKAVCEFEGGRLATYKQLEAARKIGFHVCAAGWMAKGRVGYPIVKPGPNCGFGKTGIIDYGIRLNRSERWDAYCYNPHAKECGGVFTDPKRIFKSPGFPNEYDDNQVCYWHIRLKYGQRIHLSFLDFDLEHDPGCLADYVEIYDSYDDVHGFVGRYCGDELPEDIISTGNVMTLKFLSDASVTAGGFQIKYVTVDPASKSSQAKNTSTTGNKKFLPGRFSHL
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Major regulator of extracellular matrix organization during tissue remodeling (By similarity). Catalyzes the transfer of a heavy chain (HC) from inter-alpha-inhibitor (I-alpha-I) complex to hyaluronan. Cleaves the ester bond between the C-terminus of the HC and GalNAc residue of the chondroitin sulfate chain in I-alpha-I complex followed by transesterification of the HC to hyaluronan. In the process, potentiates the antiprotease function of I-alpha-I complex through release of free bikunin (By similarity). Acts as a catalyst in the formation of hyaluronan-HC oligomers and hyaluronan-rich matrix surrounding the cumulus cell-oocyte complex, a necessary step for oocyte fertilization. Assembles hyaluronan in pericellular matrices that serve as platforms for receptor clustering and signaling. Enables binding of hyaluronan deposited on the surface of macrophages to LYVE1 on lymphatic endothelium and facilitates macrophage extravasation. Alters hyaluronan binding to functionally latent CD44 on vascular endothelium, switching CD44 into an active state that supports leukocyte rolling (By similarity). Modulates the interaction of chemokines with extracellular matrix components and proteoglycans on endothelial cell surface, likely preventing chemokine gradient formation. In a negative feedback mechanism, may limit excessive neutrophil recruitment at inflammatory sites by antagonizing the association of CXCL8 with glycosaminoglycans on vascular endothelium (By similarity). Has a role in osteogenesis and bone remodeling. Inhibits BMP2-dependent differentiation of mesenchymal stem cell to osteoblasts. Protects against bone erosion during inflammation by inhibiting TNFSF11/RANKL-dependent osteoclast activation (By similarity).
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O08863
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BIRC3_MOUSE
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Baculoviral IAP repeat-containing protein 3 (EC 2.3.2.27) (Cellular inhibitor of apoptosis 2) (C-IAP2) (Inhibitor of apoptosis protein 1) (mIAP1) (RING-type E3 ubiquitin transferase BIRC3)
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MVQDSAFLAKLMKSADTFELKYDFSCELYRLSTYSAFPRGVPVSERSLARAGFYYTGANDKVKCFCCGLMLDNWKQGDSPMEKHRKLYPSCNFVQTLNPANSLEASPRPSLPSTAMSTMPLSFASSENTGYFSGSYSSFPSDPVNFRANQDCPALSTSPYHFAMNTEKARLLTYETWPLSFLSPAKLAKAGFYYIGPGDRVACFACDGKLSNWERKDDAMSEHQRHFPSCPFLKDLGQSASRYTVSNLSMQTHAARIRTFSNWPSSALVHSQELASAGFYYTGHSDDVKCFCCDGGLRCWESGDDPWVEHAKWFPRCEYLLRIKGQEFVSQVQAGYPHLLEQLLSTSDSPEDENADAAIVHFGPGESSEDVVMMSTPVVKAALEMGFSRSLVRQTVQWQILATGENYRTVSDLVIGLLDAEDEMREEQMEQAAEEEESDDLALIRKNKMVLFQHLTCVTPMLYCLLSARAITEQECNAVKQKPHTLQASTLIDTVLAKGNTAATSFRNSLREIDPALYRDIFVQQDIRSLPTDDIAALPMEEQLRKLQEERMCKVCMDREVSIVFIPCGHLVVCKDCAPSLRKCPICRGTIKGTVRTFLS
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Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, mitogenic kinase signaling and cell proliferation, as well as cell invasion and metastasis. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and regulates both canonical and non-canonical NF-kappa-B signaling by acting in opposite directions: acts as a positive regulator of the canonical pathway and suppresses constitutive activation of non-canonical NF-kappa-B signaling. The target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, RIPK2, RIPK3, RIPK4, CASP3, CASP7, CASP8, IKBKE, TRAF1, and BCL10. Acts as an important regulator of innate immune signaling via regulation of Toll-like receptors (TLRs), Nodlike receptors (NLRs) and RIG-I like receptors (RLRs), collectively referred to as pattern recognition receptors (PRRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8.
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O08873
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MADD_RAT
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MAP kinase-activating death domain protein (Rab3 GDP/GTP exchange factor) (RabGEF) (Rab3 GDP/GTP exchange protein) (RabGEP)
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MVQKKFCPRLLDYLVIVGARHPSSDSVAQTPELLRRYPLEDHPEFPLPPDVVFFCQPEGCLSVRQRRMSLRDDTSFVFTLTDKDTGVTRYGICVNFYRSFQKRMPKEKAEGGAGPRGKEGAHAPCASEEAATESSESGSTLQPPSADSTPDVNQSPRGKRRAKAGNRSRNSTLTSLCVLSHYPFFSTFRECLYTLKRLVDCCSERLLGKKPGIPRGVQRDTMWRIFTGSLLVEEKSSALLHDLREIEAWIYRLLRSPVPVSGQKRVDIEVLPQEVQQALTFALPDPSRFTLVDFPLHLPLELLGVDACLQVLTCILLEHKVVLQSRDYNALSMSVMAFVAMIYPLEYMFPVIPLLPTCMASAEQLLLAPTPYIIGVPASFFLYKLDFKMPDDVWLVDLDSNRVIAPTNAEVLPILPEPESLELKKHLKQALASMSLNTQPILNLEKFHEGQETPLLLGRFSNDLQSTPSTEFNPLIYGNDVDSVDVATRVAMVRFFNSANVLQGFQMHTRTLRLFPRPVVAFQAGSFLASRPRQTPFAEKLARTQAVEYFGEWILNPSNYAFQRIHNNTFDPALIGDKPKWYAHQLQPIHYRVYDSNSQLAEALSVPPERDSESDPTDDSGSDSMDYDDSSSSYSSLGDFVSEMMKCDINGDTPNVDPLTHAALGDASEVEIDELQPQKEGEEPGPDSENSQENLPLRSSSSTTASSSPSTIVHGAHSEPADSTEVGDKAATGISKPLPPVPPSICKSTVDRRQTETGEGSVCQRTYDHPYFEPQYGSPAEEDDDEQGESYTPRFSQHASGSRAQKLLRPNSLKLASDSDAESDSRASSPNSTVSNNSTEGFGGIMSFASSLYRNHSTSFSLSNLTLPTKGAREKTTPFPSLKGNRRALVDQKSSVIKHSPTVKREPPSPQGRSSNSSENQQFLKEVVHSVLDGQGVGWLNMKKVRRLLESEQLRVFVLSKLSRAVQSEDDARQDVIQDVEISRKVYKGMLDLLKCTVLSLEQSYAHAGLGGMASIFGLLEIAQTHYYSKEPDKRKRSPTENVNTPVGKDPGLAGRGDPKAMAQLRVPQLGPRAPSATGRGPKELDTRSLKEENFVASVGPEVIKPVFDLGETEEKKSQISADSGVSLASASQRTDQDSVIGVSPAVMIRSSSQDSEVSNSSGETLGADSDLSSNAGDGPGGEGSAHLASSRATLSDSEIETNSATSTIFGKAHSLKPKEKPASSPVRSSEDVSQRVYLYEGLLGRDKGSMWDQLEDAAMETFSISKERSTLWDQMQFWEDAFLDAVMLEREGMGMDQGPQEMIDRYLSLGEHDRKRLEDDEDRLLATLLHNLISYMLLMKVNKNDIRKKVRRLMGKSHVGLVYSQQINEVLDQLTNLNGRDLSIRSSGSRHMKKQTFVVHAGTDTNGDIFFMEVCDDCVVLRSNIGTVYERWWYEKLINMTYCPKTKVLCLWRRNGSETQLNKFYTKKCRELYYCVKDSMERAAARQQSIKPGPELGGEFPVQDMKTGEGGLLQVTLEGINLKFMHNQVFIELNHIKKCNTVRGVFVLEEFVPEIKEVVSHKYKTPMAHEICYSVLCLFSYVAAVRSSEEDLRTPPRPVSS
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Guanyl-nucleotide exchange factor that regulates small GTPases of the Rab family. Converts GDP-bound inactive form of RAB27A and RAB27B to the GTP-bound active forms (By similarity). Converts GDP-bound inactive form of RAB3A, RAB3C and RAB3D to the GTP-bound active forms, GTPases involved in synaptic vesicle exocytosis and vesicle secretion. Plays a role in synaptic vesicle formation and in vesicle trafficking at the neuromuscular junction (By similarity). Involved in up-regulating a post-docking step of synaptic exocytosis in central synapses (By similarity). Probably by binding to the motor proteins KIF1B and KIF1A, mediates motor-dependent transport of GTP-RAB3A-positive vesicles to the presynaptic nerve terminals (By similarity). Plays a role in TNFA-mediated activation of the MAPK pathway, including ERK1/2 (By similarity). May link TNFRSF1A with MAP kinase activation (By similarity). May be involved in the regulation of TNFA-induced apoptosis (By similarity).
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O08874
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PKN2_RAT
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Serine/threonine-protein kinase N2 (EC 2.7.11.13) (Cardiolipin-activated protein kinase Pak2) (PKN gamma) (Protease-activated kinase 2) (PAK-2) (Protein kinase C-like 2) (Protein-kinase C-related kinase 2) (p140 kinase)
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MASNPDRGEILLTELQVDSRPLPFSENVSAVQKLDFSDTIVQQKLDDVKDRIKREIRKELKIKEGAENLRKVTTDKKNLAYVDNILKKSNKKLEELHHKLQELNAHIVVSDPEDYTDCPRTPDTPNSDSRSSTSNNRRLMALQKQLDIELKVKQGAENMIQMYSNGPSKDRKLHGTAQQLLQDNKTKIEVIRMHILQAVLTNELAFDNAKPVISPLELRNGRIIEHHFRIEFAVAEGAKNVMKLLGSGKVTDRKALSEAQARFNESSQKLDLLKYSLEQRLNELPKNHPKSSVVIEELSLVASPTLSPRQSMLSTQNQYSTLSKPAALTGTLEVRLWGAKISWENVPGRSKATSVALPGWSPSENRSSFMSRTSKSKSGSSRNLLKTDDLSNDVCAVLKLDNTVVGQTIWKPISNQSWDQKFTLELDRSRELEISVYWRDWRSLCAVKFLRLEDFLDNQRHGMALYLEPQGTLFAEVTFFNPVIERRPKLQRQKKIFSKQQGKTFLRAPQMNINIATWGRLVRRAIPTVNHSGTFSPQTPVPATVPVVDARTPELAPPASDSTVTKLDFDLEPEAPPAPPRASSLGEIDDSSELRVLDIPGQGSETVFDIENDRNNMRPKSKSEYELNIPDSSRSCWSVGELEDKRSQQRFQFNLQDFRCCAVLGRGHFGKVLLAEYKHTNEMFAIKALKKGDIVARDEVDSLMCEKRIFETVNSVRHPFLVNLFACFQTKEHVCFVMEYAAGGDLMMHIHTDVFSEPRAVFYAACVVLGLQYLHEHKIVYRDLKLDNLLLDTEASVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTETSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAISIMRRLLRRNPERRLGAGEKDAEDVKKHPFFRLTDWSALLDKKVKPPFVPTIRGREDVSNFDDEFTSEAPILTPPREPRILLEEEQEMFRDFDYVADWC
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PKC-related serine/threonine-protein kinase and Rho/Rac effector protein that participates in specific signal transduction responses in the cell. Plays a role in the regulation of cell cycle progression, actin cytoskeleton assembly, cell migration, cell adhesion, tumor cell invasion and transcription activation signaling processes. Phosphorylates CTTN in hyaluronan-induced astrocytes and hence decreases CTTN ability to associate with filamentous actin. Phosphorylates HDAC5, therefore lead to impair HDAC5 import. Direct RhoA target required for the regulation of the maturation of primordial junctions into apical junction formation in bronchial epithelial cells. Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2-dependent manner. Stimulates FYN kinase activity that is required for establishment of skin cell-cell adhesion during keratinocytes differentiation. Regulates epithelial bladder cells speed and direction of movement during cell migration and tumor cell invasion. Inhibits Akt pro-survival-induced kinase activity. Mediates Rho protein-induced transcriptional activation via the c-fos serum response factor (SRF). Involved in the negative regulation of ciliogenesis.
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O08875
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DCLK1_RAT
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Serine/threonine-protein kinase DCLK1 (EC 2.7.11.1) (Calcium/calmodulin-dependent protein kinase type I-like CPG16) (Doublecortin-like and CAM kinase-like 1) (Doublecortin-like kinase 1)
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MLELIEVNGTPGSQLSTPRSGKSPSPSPTSPGSLRKQRISQHGGSSTSLSSTKVCSSMDENDGPGEEESDEGFQIPATITERYKVGRTIGDGNFAVVKECIERSTAREYALKIIKKSKCRGKEHMIQNEVSILRRVKHPNIVLLIEEMDVPTELYLVMELVKGGDLFDAITSTSKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQDGSKSLKLGDFGLATIVDGPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQEVLFDQILMGQVDFPSPYWDNVSDSAKELINMMLLVNVDQRFSAVQVLEHPWVNDDGLPENEHQLSVAGKIKKHFNTGPKPSSTAAGVSVIATTALDKERQVFRRRRNQDVRGRYKAQPAPPELNSESEDYSPSSSETVRSPNSPF
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Probable kinase that may be involved in a calcium-signaling pathway controlling neuronal migration in the developing brain. May also participate in functions of the mature nervous system (By similarity).
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O08876
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KLF10_RAT
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Krueppel-like factor 10 (Transforming growth factor-beta-inducible early growth response protein 1) (TGFB-inducible early growth response protein 1) (TIEG-1) (Zinc finger transcription factor homolog CPG20)
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MLNFGASLQQASEGKMELISEKSKEGAHPWDKAEQSDFEAVEALMSMSCDWKSHFKKYLENRPVTPVSDTSEEDSLLPGTPDLQTVPAFCLTPPYSPSDFEPSQGSNLTAPAPPTGHFRSLSDAAKPPSIAPFKEEEKSPLAAPPLPKAQATSVIRHTADAQLCNHQSCPVKAASILNYQDNSFRRRTHINVEATRKNIPCAAVSPNRPKPEPSTAANGAEKAGTAPYDFAVPSSETVICRSSQPAPTSPVQKSVLMSSPTVSTGGVPPLPVICQMVPLPANNSLVTTVVPSSPPSQPPAVCSPVLFMGTQVPKGTVMFVVPQPVVQSPKPPVVSPNGTRLSPIAPAPGFSPSAARVTPQIDSSRVRSHICSHPGCGKTYFKSSHLKAHVRTHTGEKPFSCSWKGCERRFARSDELSRHRRTHTGEKKFACPMCDRRFMRSDHLTKHARRHLSAKKLPNWQMEVSKLNDIALPPATASAQ
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Transcriptional repressor which binds to the consensus sequence 5'-GGTGTG-3'. Regulates the circadian expression of genes involved in lipogenesis, gluconeogenesis, and glycolysis in the liver. Represses the expression of PCK2, a rate-limiting step enzyme of gluconeogenesis. May play a role in the cell cycle regulation (By similarity). Plays a role in the regulation of the circadian clock binds to the GC box sequence in the promoter of the core clock component ARTNL/BMAL1 and represses its transcriptional activity.
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O08878
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GPER1_RAT
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G-protein coupled estrogen receptor 1 (Chemoattractant receptor-like 2) (G protein-coupled estrogen receptor 1) (G-protein coupled receptor 30) (G-protein coupled receptor 41) (Membrane estrogen receptor) (mER)
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MAATTPAQDVGVEIYLGPVWPAPSNSTPLALNLSLALREDAPGNLTGDLSEHQQYVIALFLSCLYTIFLFPIGFVGNILILVVNISFREKMTIPDLYFINLAAADLILVADSLIEVFNLDEQYYDIAVLCTFMSLFLQINMYSSVFFLTWMSFDRYLALAKAMRCGLFRTKHHARLSCGLIWMASVSATLVPFTAVHLRHTEEACFCFADVREVQWLEVTLGFIVPFAIIGLCYSLIVRALIRAHRHRGLRPRRQKALRMIFAVVLVFFICWLPENVFISVHLLQWAQPGDTPCKQSFRHAYPLTGHIVNLAAFSNSCLSPLIYSFLGETFRDKLRLYVAQKTSLPALNRFCHATLKAVIPDSTEQSDVKFSSAV
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G-protein coupled estrogen receptor that binds to 17-beta-estradiol (E2) with high affinity, leading to rapid and transient activation of numerous intracellular signaling pathways. Stimulates cAMP production, calcium mobilization and tyrosine kinase Src inducing the release of heparin-bound epidermal growth factor (HB-EGF) and subsequent transactivation of the epidermal growth factor receptor (EGFR), activating downstream signaling pathways such as PI3K/Akt and ERK/MAPK. Mediates pleiotropic functions among others in the cardiovascular, endocrine, reproductive, immune and central nervous systems. Has a role in cardioprotection by reducing cardiac hypertrophy and perivascular fibrosis in a RAMP3-dependent manner. Regulates arterial blood pressure by stimulating vasodilation and reducing vascular smooth muscle and microvascular endothelial cell proliferation. Plays a role in blood glucose homeostasis contributing to the insulin secretion response by pancreatic beta cells. Triggers mitochondrial apoptosis during pachytene spermatocyte differentiation. Stimulates uterine epithelial cell proliferation. Enhances uterine contractility in response to oxytocin. Contributes to thymic atrophy by inducing apoptosis. Attenuates TNF-mediated endothelial expression of leukocyte adhesion molecules. Promotes neuritogenesis in developing hippocampal neurons. Plays a role in acute neuroprotection against NMDA-induced excitotoxic neuronal death. Increases firing activity and intracellular calcium oscillations in luteinizing hormone-releasing hormone (LHRH) neurons. Inhibits early osteoblast proliferation at growth plate during skeletal development. Inhibits mature adipocyte differentiation and lipid accumulation. Involved in the recruitment of beta-arrestin 2 ARRB2 at the plasma membrane in epithelial cells. Functions also as a receptor for aldosterone mediating rapid regulation of vascular contractibility through the PI3K/ERK signaling pathway. Involved in cancer progression regulation. Stimulates cancer-associated fibroblast (CAF) proliferation by a rapid genomic response through the EGFR/ERK transduction pathway. Associated with EGFR, may act as a transcription factor activating growth regulatory genes (c-fos, cyclin D1). Promotes integrin alpha-5/beta-1 and fibronectin (FN) matrix assembly in breast cancer cells.
|
O08888
|
PTSS2_CRIGR
|
Phosphatidylserine synthase 2 (PSS-2) (PtdSer synthase 2) (EC 2.7.8.29) (Serine-exchange enzyme II)
|
MRRAERRVAGGSGSGSPLLEGRRSTESEVYDDGTNTFFWRAHTLTVLFILTCSLGYVTLLEETPQDTAYNTKRGIVASILVFLCFGVTQAKDGPFSRPHPAYWRFWLCVSVVYELFLIFILFQTVQDGRQFLKYVDPRLGVPLPERDYGGNCLIYDADNKTDPFHNIWDKLDGFVPAHFIGWYLKTLMIRDWWMCMIISVMFEFLEYSLEHQLPNFSECWWDHWIMDVLICNGLGIYCGMKTLEWLSLKTYKWQGLWNIPTYKGKMKRIAFQFTPYSWVRFEWKPASSLHRWLAVCGIILVFLLAELNTFYLKFVLWMPPEHYLVLLRLVFFVNVGGVAMREIYDFMDELKPHRKLGQQAWLVAAITVTELLIVVKYDPHTLTLSLPFYISQCWTLGSILVLTWTVWRFFLRDITMRYKETRRQKQQSHQGRAINNGDGHPGPDDDLLGTGTAEEEGSTNDSVPAEKEGASAAS
|
Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine. Catalyzes the conversion of phosphatatidylethanolamine and does not act on phosphatidylcholine. Shows a substrate specificity for phosphatatidylethanolamine and does not act on phosphatidylcholine (By similarity). Can utilize both phosphatidylethanolamine (PE) plasmalogen and diacyl PE as substrate and the latter is six times better utilized, indicating the importance of an ester linkage at the sn-1 position (By similarity). Although it shows no sn-1 fatty acyl preference, exhibits significant preference towards docosahexaenoic acid (22:6n-3) compared with 18:1 or 20:4 at the sn-2 position (By similarity).
|
O08892
|
5HT1B_CAVPO
|
5-hydroxytryptamine receptor 1B (5-HT-1B) (5-HT1B) (Serotonin receptor 1B)
|
MGNPEASCTPPAVLGSQTGLPHANVSAPPNNCSAPSHIYQDSIALPWKVLLVVLLALITLATTLSNAFVIATVYRTRKLHTPANYLIASLAFTDLLVSILVMPISTMYTVTGRWTLGQALCDFWLSSDITCCTASIMHLCVIALDRYWAITDAVGYSAKRTPRRAAGMIALVWVFSICISLPPFFWRQAKAEEEVLDCLVNTDHVLYTVYSTGGAFYLPTLLLIALYGRIYVEARSRILKQTPNKTGKRLTRAQLITDSPGSTSSVTSINSRAPEVPCDSGSPVYVNQVKVRVSDALLEKKKLMAARERKATKTLGVILGAFIVCWLPFFIISLVMPICKDACWFHMAIFDFFTWLGYLNSLINPIIYTMSNEDFKQAFHKLIRFKCTT
|
G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. 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. Signaling inhibits adenylate cyclase activity. Arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Regulates the release of 5-hydroxytryptamine, dopamine and acetylcholine in the brain, and thereby affects neural activity, nociceptive processing, pain perception, mood and behavior. Besides, plays a role in vasoconstriction of cerebral arteries (By similarity). {ECO:0000250, ECO:0000269|PubMed:9225276}.
|
O08900
|
IKZF3_MOUSE
|
Zinc finger protein Aiolos (Ikaros family zinc finger protein 3)
|
MEDIQPTVELKSTEEQPLPTESPDALNDYSLPKPHEIENVDSREAPANEDEDAGEDSMKVKDEYSDRDENIMKPEPMGDAEESEMPYSYAREYSDYESIKLERHVPYDNSRPTGGKMNCDVCGLSCISFNVLMVHKRSHTGERPFQCNQCGASFTQKGNLLRHIKLHTGEKPFKCHLCNYACQRRDALTGHLRTHSVEKPYKCEFCGRSYKQRSSLEEHKERCRAFLQNPDLGDAASVEARHIKAEMGSERALVLDRLASNVAKRKSSMPQKFIGEKRHCFDANYNPGYMYEKENEMMQTRMMDQAINNAISYLGAEALRPLVQTPPAPTSEMVPVISSVYPIALTRADMPNGAPQEMEKKRILLPEKILPSERGLSPNNSAQDSTDTDSNHEDRQHLYQQSHVVLPQARNGMPLLKEVPRSFELLKPPPICLRDSIKVINKEGEVMDVFRCDHCHVLFLDYVMFTIHMGCHGFRDPFECNMCGYRSHDRYEFSSHIARGEHRAMLK
|
Transcription factor that plays an important role in the regulation of lymphocyte differentiation. Binds to GGGAA. Plays an essential role in regulation of B-cell differentiation, proliferation and maturation to an effector state. Involved in regulating BCL2 expression and controlling apoptosis in T-cells in an IL2-dependent manner.
|
O08901
|
BUB1_MOUSE
|
Mitotic checkpoint serine/threonine-protein kinase BUB1 (mBUB1) (EC 2.7.11.1) (BUB1A)
|
MDNLENVFRMFEAHMQSYTGNDPLGEWESFIKWVEENFPDNKEYLMTLLEHLMKEFLHKKNYHNDSRFINYCLKFAEYNSDRHQFFEFLYNQGIGTKSSYIYMSWAGHLEAQGELQHASAIFQTGIHNEAEPKELLQQQYRLFQARLTGIHLPAQATTSEPLHSAQILNQVMMTNSSPEKNSACVPKSQGSECSGVASSTCDEKSNMEQRVIMISKSECSVSSSVAPKPEAQQVMYCKEKLIRGDSEFSFEELRAQKYNQRKKHEQWVSEDRNYMKRKEANAFEEQLLKQKMDELHKKLHQVVELSHKDLPASENRPDVSLVCVGQNTCSQQELRGPSLSSISHQTSESSGEKPQEEPSVPLMVNAVNSTLLFPAANLPALPVPVSGQSLTDSRCVNQSVHEFMPQCGPETKEVCETNKVASINDFHTTPNTSLGMVQGTPCKVQPSPTVHTKEALGFIMDMFQAPTLPDISDDKDEWPSLDQNEDAFEAQFQKNAVSSGDWGVKKIMTLSSAFPIFEDGNKENYGLPQPKNKPLGARTFGERSLSKYSSRSNEMPHTDEFMDDSTVCGIRCNKTLAPSPKSIGDFTSAAQLSSTPFHKFPADLVQIPEDKENVVATQYTHMALDSCKENIVDLSKGRKLGPIQEKISASLPCPSQPATGGLFTQEAVFGLEAFKCTGIDHATVEDLSDANAGLQVECVQTLGNVNAPSFTVENPWDDELILKLLSGLSKPVTSYSNTFEWQSKLPAIKTKTEYQLGSLLVYVNHLLGEGAFAQVFEAIHGDVRNAKSEQKCILKVQRPANSWEFYIGMQLMERLKPEVHHMFIKFYSAHLFKNGSILVGELYSYGTLLNVINLYKNTSEKVMPQALVLTFAIRMLYMVEQVHSCEIIHGDIKPDNFILGHRFLEQADEDLATGLALIDLGQSIDMKLFPKGTVFTGKCETSGFQCPEMLSNKPWNYQIDYFGVAATIYCMLFGSYMKVKNEGGVWKPEGLFRRLPHLDMWEEFFHIMLNIPDCHNLPSLDFLRQNMKKLLEQQYSNKIKTLRNRLIVMLSEYKRSRK
|
Serine/threonine-protein kinase that performs 2 crucial functions during mitosis: it is essential for spindle-assembly checkpoint signaling and for correct chromosome alignment. Has a key role in the assembly of checkpoint proteins at the kinetochore, being required for the subsequent localization of CENPF, BUB1B, CENPE and MAD2L1. Required for the kinetochore localization of PLK1. Required for centromeric enrichment of AUKRB in prometaphase. Plays an important role in defining SGO1 localization and thereby affects sister chromatid cohesion. Promotes the centromeric localization of TOP2A (By similarity). Acts as a substrate for anaphase-promoting complex or cyclosome (APC/C) in complex with its activator CDH1 (APC/C-Cdh1). Necessary for ensuring proper chromosome segregation and binding to BUB3 is essential for this function. Can regulate chromosome segregation in a kinetochore-independent manner. Can phosphorylate BUB3. The BUB1-BUB3 complex plays a role in the inhibition of APC/C when spindle-assembly checkpoint is activated and inhibits the ubiquitin ligase activity of APC/C by phosphorylating its activator CDC20. This complex can also phosphorylate MAD1L1. Kinase activity is essential for inhibition of APC/CCDC20 and for chromosome alignment but does not play a major role in the spindle-assembly checkpoint activity. Mediates cell death in response to chromosome missegregation and acts to suppress spontaneous tumorigenesis. Essential during early and later stages of embryonic development. Necessary for postimplantation embryogenesis and proliferation of primary embryonic fibroblasts and plays an important role in spermatogenesis and fertility.
|
O08908
|
P85B_MOUSE
|
Phosphatidylinositol 3-kinase regulatory subunit beta (PI3-kinase regulatory subunit beta) (PI3K regulatory subunit beta) (PtdIns-3-kinase regulatory subunit beta) (Phosphatidylinositol 3-kinase 85 kDa regulatory subunit beta) (PI3-kinase subunit p85-beta) (PtdIns-3-kinase regulatory subunit p85-beta)
|
MAGAEGFQYRAVYPFRRERPEDLELLPGDLLVVSRVALQALGVADGGERCPHNVGWMPGFNERTRQRGDFPGTYVEFLGPVALARPGPRPRGPRPLPARPLDGSSESGHILPDLAEQFSPPDPAPPILVKLVEAIEQAELDSECYSKPELPATRTDWSLSDLEQWDRTALYDAVKGFLLALPAAVVTPEAAAEAYRALREVAGPVGLVLEPPTLPLHQALTLRFLLQHLGRVARRAPSPDTAVHALASAFGPLLLRIPPSGGEGDGSEPVPDFPVLLLERLVQEHVEEQDAAPPALPPKPSKAKPAPTALANGGSPPSLQDAEWYWGDISREEVNERLRDTPDGTFLVRDASSKIQGEYTLTLRKGGNNKLIKVFHRDGHYGFSEPLTFCSVVELISHYRHESLAQYNAKLDTRLLYPVSKYQQDQVVKEDSIEAVGAQLKVYHQQYQDKSREYDQLYEEYTRTSQELQMKRTAIEAFNETIKIFEEQGQTQEKCSKEYLERFRREGNEKEMQRILLNSERLKSRIAEIHESRTKLEQDLRAQASDNREIDKRMNSLKPDLMQLRKIRDQYLVWLTQKGARQRKINEWLGIKNETEDQYSLMEDEDALPHHEERTWYVGKINRTQAEEMLSGKRDGTFLIRESSQRGCYACSVVVDGDTKHCVIYRTATGFGFAEPYNLYGSLKELVLHYQHASLVQHNDALTVTLAHPVRAPGPGPPSAAR
|
Regulatory subunit of phosphoinositide-3-kinase (PI3K), a kinase that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Binds to activated (phosphorylated) protein-tyrosine kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Indirectly regulates autophagy (By similarity). Promotes nuclear translocation of XBP1 isoform 2 in a ER stress- and/or insulin-dependent manner during metabolic overloading in the liver and hence plays a role in glucose tolerance improvement.
|
O08911
|
MK12_MOUSE
|
Mitogen-activated protein kinase 12 (MAP kinase 12) (MAPK 12) (EC 2.7.11.24) (Extracellular signal-regulated kinase 6) (ERK-6) (Mitogen-activated protein kinase p38 gamma) (MAP kinase p38 gamma) (Stress-activated protein kinase 3)
|
MSSPPPARKGFYRQEVTKTAWEVRAVYQDLQPVGSGAYGAVCSAVDSRTGNKVAIKKLYRPFQSELFAKRAYRELRLLKHMRHENVIGLLDVFTPDESLDDFTDFYLVMPFMGTDLGKLMKHETLSEDRIQFLVYQMLKGLKYIHAAGVIHRDLKPGNLAVNEDCELKILDFGLARQADSEMTGYVVTRWYRAPEVILNWMRYTQTVDIWSVGCIMAEMITGKILFKGNDHLDQLKEIMKITGTPPPEFVQKLQSAEAKNYMEGLPELEKKDFASVLTNASPQAVNLLERMLVLDAEQRVTAAEALTHPYFESLRDTEDEPKAQKYDDSFDDVDRTLEEWKRVTYKEVLSFKPPRQLGARVPKETAL
|
Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK12 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as pro-inflammatory cytokines or physical stress leading to direct activation of transcription factors such as ELK1 and ATF2. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. Some of the targets are downstream kinases such as MAPKAPK2, which are activated through phosphorylation and further phosphorylate additional targets. Plays a role in myoblast differentiation and also in the down-regulation of cyclin D1 in response to hypoxia in adrenal cells suggesting MAPK12 may inhibit cell proliferation while promoting differentiation. Phosphorylates DLG1. Following osmotic shock, MAPK12 in the cell nucleus increases its association with nuclear DLG1, thereby causing dissociation of DLG1-SFPQ complexes. This function is independent of its catalytic activity and could affect mRNA processing and/or gene transcription to aid cell adaptation to osmolarity changes in the environment. Regulates UV-induced checkpoint signaling and repair of UV-induced DNA damage and G2 arrest after gamma-radiation exposure. MAPK12 is involved in the regulation of SLC2A1 expression and basal glucose uptake in L6 myotubes and negatively regulates SLC2A4 expression and contraction-mediated glucose uptake in adult skeletal muscle. C-Jun (JUN) phosphorylation is stimulated by MAPK14 and inhibited by MAPK12, leading to a distinct AP-1 regulation. MAPK12 is required for the normal kinetochore localization of PLK1, prevents chromosomal instability and supports mitotic cell viability. MAPK12-signaling is also positively regulating the expansion of transient amplifying myogenic precursor cells during muscle growth and regeneration.
|
O08912
|
GALT1_MOUSE
|
Polypeptide N-acetylgalactosaminyltransferase 1 (EC 2.4.1.41) (Polypeptide GalNAc transferase 1) (GalNAc-T1) (pp-GaNTase 1) (Protein-UDP acetylgalactosaminyltransferase 1) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1) [Cleaved into: Polypeptide N-acetylgalactosaminyltransferase 1 soluble form]
|
MRKFAYCKVVLATSLVWVLLDMFLLLYFSECNKCEEKQERGLPAGDVLELVQKPHEGPGEMGKPVVIPKEDQEKMKEMFKINQFNLMASEMIALNRSLPDVRLEGCKTKVYPDNLPTTSVVIVFHNEAWSTLLRTVHSVINRSPRHMIEEIVLVDDASERDFLKRPLESYVKKLKVPVHVIRMEQRSGLIRARLKGAAVSRGQVITFLDAHCECTAGWLEPLLARIKHDRRTVVCPIIDVISDDTFEYMAGSDMTYGGFNWKLNFRWYPVPQREMDRRKGDRTLPVRTPTMAGGLFSIDRDYFQEIGTYDAGMDIWGGENLEISFRIWQCGGTLEIVTCSHVGHVFRKATPYTFPGGTGQIINKNNRRLAEVWMDEFKNFFYIISPGVTKVDYGDISSRLGLRRKLQCKPFSWYLENIYPDSQIPRHYFSLGEIRNVETNQCLDNMARKENEKVGIFNCHGMGGNQVFSYTANKEIRTDDLCLDVSKLNGPVTMLKCHHLKGNQLWEYDPVKLTLQHVNSNQCLDKATEEDSQVPSIRDCTGSRSQQWLLRNVTLPEIF
|
Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad spectrum of substrates such as apomucin-, MUC5AC-, MUC1- and MUC2-derived peptides (By similarity).
|
O08914
|
FAAH1_MOUSE
|
Fatty-acid amide hydrolase 1 (EC 3.5.1.99) (Anandamide amidohydrolase 1) (Fatty acid ester hydrolase) (EC 3.1.1.-) (Oleamide hydrolase 1)
|
MVLSEVWTALSGLSGVCLACSLLSAAVVLRWTRSQTARGAVTRARQKQRAGLETMDKAVQRFRLQNPDLDSEALLALPLLQLVQKLQSGELSPEAVLFTYLGKAWEVNKGTNCVTSYLTDCETQLSQAPRQGLLYGVPVSLKECFSYKGHASTLGLSLNEGVTSESDCVVVQVLKLQGAVPFVHTNVPQSMLSYDCSNPLFGQTMNPWKPSKSPGGSSGGEGALIGSGGSPLGLGTDIGGSIRFPSAFCGICGLKPTGNRLSKSGLKSCVYGQTAVQLSVGPMARDVDSLALCMKALLCEDLFRLDSTIPPLPFREEIYRSSRPLRVGYYETDNYTMPTPAMRRAVMETKQSLEAAGHTLVPFLPNNIPYALEVLSAGGLFSDGGCSFLQNFKGDFVDPCLGDLVLVLKLPRWFKKLLSFLLKPLFPRLAAFLNSMCPRSAEKLWELQHEIEMYRQSVIAQWKAMNLDVVLTPMLGPALDLNTPGRATGAISYTVLYNCLDFPAGVVPVTTVTAEDDAQMEHYKGYFGDMWDNILKKGMKKGIGLPVAVQCVALPWQEELCLRFMREVERLMTPEKRPS
|
Catalyzes the hydrolysis of endogenous amidated lipids like the endocannabinoid anandamide (N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine), as well as other fatty amides such as the taurine-conjugated fatty acids (a structural class of central nervous system (CNS) metabolites), to their corresponding fatty acids, thereby regulating the signaling functions of these molecules. FAAH cooperates with PM20D1 in the hydrolysis of amino acid-conjugated fatty acids such as N-fatty acyl glycine and N-fatty acyl-L-serine, thereby acting as a physiological regulator of specific subsets of intracellular, but not of extracellular, N-fatty acyl amino acids. It can also catalyze the hydrolysis of the endocannabinoid 2-arachidonoylglycerol (2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol) (By similarity).
|
O08915
|
AIP_MOUSE
|
AH receptor-interacting protein (AIP) (Aryl-hydrocarbon receptor-interacting protein)
|
MADLIARLREDGIQKRVIQEGRGELPDFQDGTKATFHFRTLHSDNEGSVIDDSRTRGKPMELIVGKKFKLPVWETIVCTMREGEIAQFLCDIKHVVLYPLVAKSLRNIAEGKDPLEGQRHCCGIAQMHEHSSLGHADLDALQQNPQPLIFHIEMLKVESPGTYQQDPWAMTDEEKAKAVPVIHQEGNRLYREGQVKEAAAKYYDAIACLKNLQMKEQPGSPDWIQLDLQITPLLLNYCQCKLVAQEYYEVLDHCSSILNKYDDNVKAYFKRGKAHAAVWNAQEAQADFAKVLELDPALAPVVSRELRALETRIRQKDEEDKARFRGIFSH
|
May play a positive role in AHR-mediated (aromatic hydrocarbon receptor) signaling, possibly by influencing its receptivity for ligand and/or its nuclear targeting.
|
O08917
|
FLOT1_MOUSE
|
Flotillin-1
|
MFFTCGPNEAMVVSGFCRSPPVMVAGGRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIQGQNKEMLAAACQMFLGKTEAEIAHIALETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQCLSEIEMAKAQRDYELKKATYDIEVNTRRAQADLAYQLQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYRLERLAEAEKAQLIMQAEAEAESVRMRGEAEAFAIGARARAEAEQMAKKAEAFQMYQEAAQLDMLLEKLPQVAEEISGPLTSANKITLVSSGSGTMGAAKVTGEVLDILSRLPESVERLTGVSISQVNHNKPLRTA
|
May act as a scaffolding protein within caveolar membranes, functionally participating in formation of caveolae or caveolae-like vesicles.
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O08919
|
NUMBL_MOUSE
|
Numb-like protein
|
MSRSAAASGGPRRPDQHLSPAPCGASGPPETFRTESDGAGTMNKLRQSLRRRKPAYVPEASRPHQWQADEDAVRKGTCSFPVRYLGHVEVEESRGMHVCEDAVKKLKAMGRKSVKSVLWVSADGLRVVDDKTKDLLVDQTIEKVSFCAPDRNLDKAFSYICRDGTTRRWICHCFLALKDSGERLSHAVGCAFAACLERKQRREKECGVTAAFDASRTSFAREGSFRLSGGGRPAEREAGDKKKAEAAAAPAVAPGPAQPGHVSPTPATTSPGEKGEAGTPVAAGTTAAAIPRRHAPLEQLVRQGSFRGFPALSQKNSPFKRQLSLRLNELPSTLQRRTDFQVKGTVPEMEPPGTGDSDGINALCTQISSSFASAGAPASGPPPATTGTSAWGEPSVPAAAAFQPGHKRTPSEAERWLEEVSQVAKAQQQQQQQQQQQQQQQATSVPPMPTMAPTLQPFSAPVGPFDTAAAQVAVFLPPTHMQPPFVPAYPGLGYPPMPRVPVVGITPSQMVANAFCSAAQLQPQPATLLGKAGAFPPPAAPSAPGGQARPRPNGAPWPPEPAPAPAPELDPFEAQWAALEGKPAVEKPSNPFSGDLQKTFEIEL
|
Plays a role in the process of neurogenesis. Required throughout embryonic neurogenesis to maintain neural progenitor cells, also called radial glial cells (RGCs), by allowing their daughter cells to choose progenitor over neuronal cell fate. Not required for the proliferation of neural progenitor cells before the onset of embryonic neurogenesis. Also required postnatally in the subventricular zone (SVZ) neurogenesis by regulating SVZ neuroblasts survival and ependymal wall integrity. Negative regulator of NF-kappa-B signaling pathway. The inhibition of NF-kappa-B activation is mediated at least in part, by preventing MAP3K7IP2 to interact with polyubiquitin chains of TRAF6 and RIPK1 and by stimulating the 'Lys-48'-linked polyubiquitination and degradation of TRAF6 in cortical neurons.
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O08934
|
UNC4_MOUSE
|
Homeobox protein unc-4 homolog (Homeobox protein Uncx4.1)
|
MMDGRLLEHPHAQFGGSLGGVVGFPYPLGHHHVYELAGHQLQSAAAAAAAASVPFSIDGLLSGSCAAAAASVVNPTPLLPAACGVAGESQPFKLADSGDPDKESPGCKRRRTRTNFTGWQLEELEKAFNESHYPDVFMREALALRLDLVESRVQVWFQNRRAKWRKKENTKKGPGRPAHNSHPTTCSGEPMDPEEIARKELEKMEKKKRKHEKKLLKSQSRHLHSPGGLSLHSAPSSDSDSGGGGLSPEPPEPPPPTAAAKGPGAHGSGIAGSAPVPPGEPPAPGTCDPAFYPSQRSGAGSQPRLGRPADKDTVPCGPGAAATAGLPKASPFSVESLLSDSPPRRKATPANAAATAGLDFTPGLPCAPRTLIGKGHFLLYPITQPLGFLVPQAALKGGAGPELVPKDAPPAPPAPPAPPAQASFGTFPGPGGAADPAFARRSPEVVASPGPPAPASFRDLTAAAAESGAGDCADVGTVCPAASPPPPLETSPGPGPRAPSPPGEPATCGAAEPGAATGPSPPEGEEVDMD
|
Transcription factor involved in somitogenesis and neurogenesis. Required for the maintenance and differentiation of particular elements of the axial skeleton. May act upstream of PAX9. Plays a role in controlling the development of connections of hypothalamic neurons to pituitary elements, allowing central neurons to reach the peripheral blood circulation and to deliver hormones for control of peripheral functions.
|
O08949
|
TF2AA_RAT
|
Transcription initiation factor IIA subunit 1 (General transcription factor IIA subunit 1) [Cleaved into: Transcription initiation factor IIA alpha chain (TFIIA p35 subunit); Transcription initiation factor IIA beta chain (TFIIA p19 subunit)]
|
MANSANTNTVPKLYRSVIEDVINDVRDIFLDDGVDEQVLMELKTLWENKLMQSRAVDGFHSEEQQLLLQVQQQHQPQQQQHHHHHHHQQAQPQQTVPQQAQTQQVLIPASQQATAPQVIVPDSKLIQHMNASSITSAAATAATLALPAGVTPVQQILTNSGQLLQVVRAANGAQYIFQPQQSVVLQQQVIPQMQPGGVQAPVIQQVLAPLPGGISPQTGVIIQPQQILFTGNKTQVIPTTVAAPTPAQAQIPAAGQQQPQAQPAQQQAPLVLQVDGTGDTSSEEDEDEEEDYDDDEEEDKEKDGAEDGQVEEEPLNSEDDVSDEEGQELFDTENVVVCQYDKIHRSKNKWKFHLKDGIMNLNGRDYIFSKAIGDAEW
|
TFIIA is a component of the transcription machinery of RNA polymerase II and plays an important role in transcriptional activation. TFIIA in a complex with TBP mediates transcriptional activity (By similarity).
|
O08954
|
SNAI2_RAT
|
Zinc finger protein SNAI2 (Neural crest transcription factor Slug) (Protein snail homolog 2)
|
MPRSFLVKKHFNASKKPNYSELDTHTVIISPYLCESYPMPVIPKPEILTSGAYSPITVWTSAVPFHSPLPSGLSPLTGYSSSLGRVSPLPSSDTSSKDHSGSESPISDEEERLQPKLSDPHAIEAEKFQCNLCNKTYSTFSGLAKHKQLHCDAQARKSFSCKYCDKEYVSLGALKMHIRTHTLPCVCKICGKAFSRPWLLQGHIRTHTGEKPFSCPHCNRAFADRSNLRAHLQTHSDVKKYQCKNCSKTFSRMSLLHKHEESGCCVAH
|
Transcriptional repressor that modulates both activator-dependent and basal transcription. Involved in the generation and migration of neural crest cells. Plays a role in mediating RAF1-induced transcriptional repression of the TJ protein, occludin (OCLN) and subsequent oncogenic transformation of epithelial cells. Represses BRCA2 expression by binding to its E2-box-containing silencer and recruiting CTBP1 and HDAC1 in breast cells. In epidermal keratinocytes, binds to the E-box in ITGA3 promoter and represses its transcription. Involved in the regulation of ITGB1 and ITGB4 expression and cell adhesion and proliferation in epidermal keratinocytes. Binds to E-box2 domain of BSG and activates its expression during TGFB1-induced epithelial-mesenchymal transition (EMT) in hepatocytes. Represses E-Cadherin/CDH1 transcription via E-box elements. Involved in osteoblast maturation. Binds to RUNX2 and SOC9 promoters and may act as a positive and negative transcription regulator, respectively, in osteoblasts. Binds to CXCL12 promoter via E-box regions in mesenchymal stem cells and osteoblasts. Plays an essential role in TWIST1-induced EMT and its ability to promote invasion and metastasis (By similarity). {ECO:0000250, ECO:0000269|PubMed:16924233}.
|
O08961
|
ZN423_RAT
|
Zinc finger protein 423 (Olf1/EBF-associated zinc finger protein) (rOAZ) (Smad- and Olf-interacting zinc finger protein)
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MSRRKQAKPRSVKVEEGEASDFSLAWDSSVAAAGGLEGESECDRKSSRALEDRNSVTSQEERNEDDEDVEDESIYTCDHCQQDFESLADLTDHRAHRCPGDGDDDPQLSWVASSPSSKDVASPTQMIGDGCDLGLGEEEGGTGLPYPCQFCDKSFIRLSYLKRHEQIHSDKLPFKCTFCSRLFKHKRSRDRHIKLHTGDKKYHCHECEAAFSRRDHLKIHLKTHSSSKPFKCSVCKRGFSSTSSLQSHMQAHKKNKEHLAKSEKEAKKDDFMCDYCEDTFSQTEELEKHVLTLHPQLSEKADLQCIHCPEVFVDESTLLAHIHQAHANQKHKCPMCPEQFSSVEGVYCHLDSHRQPDSSNHSVSPDPVLGSVASMSSATPDSTPDPVLGSVASMSSATPDSSASVERGSTPDSTLKPLRGQKKMRDDGQSWSKVVYSCPYCSKRDFTSLAVLEIHLKTIHADKPQQSHTCQICLDSMPTLYNLNEHVRKLHKSHAYPVMQFGNISAFHCNYCPEMFADINSLQEHIRVSHCGPNANPPDGNNAFFCNQCSMGFLTESSLTEHIQQAHCSVGSTKLESPVIQPTQSFMEVYSCPYCTNSPIFGSILKLTKHIKENHKNIPLAHSKKSKAEQSPVSSDVEVSSPKRQRLSGSANSISNGEYPCNQCDLKFSNFESFQTHLKLHLELLLRKQACPQCKEDFDSQESLLQHLTVHYMTTSTHYVCESCDKQFSSVDDLQKHLLDMHTFVLYHCTLCQEVFDSKVSIQVHLAVKHSNEKKMYRCTACNWDFRKEADLQVHVKHSHLGNPAKAHKCIFCGETFSTEVELQCHITTHSKKYNCRFCSKAFHAVLLLEKHLREKHCVFDPAAENGTANGVPPTSTKKAEPADLQGMLLKNPEAPNSHEASEDDVDASEPMYGCDICGAAYTMEVLLQNHRLRDHNIRPGEDDGSRKKAEFIKGSHKCNVCSRTFFSENGLREHLQTHRGPAKHYMCPICGERFPSLLTLTEHKVTHSKSLDTGTCRICKMPLQSEEEFIEHCQMHPDLRNSLTGFRCVVCMQTVTSTLELKIHGTFHMQKLAGSSAASSPNGQGLQKLYKCALCLKEFRSKQDLVRLDVNGLPYGLCAGCMARSANGQVGGLAPPEPADRPCAGLRCPECNVKFESAEDLESHMQVDHRDLTPETSGPRKGAQTSPVPRKKTYQCIKCQMTFENEREIQIHVANHMIEEGINHECKLCNQMFDSPAKLLCHLIEHSFEGMGGTFKCPVCFTVFVQANKLQQHIFAVHGQEDKIYDCSQCPQKFFFQTELQNHTMSQHAQ
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Transcription factor that can both act as an activator or a repressor depending on the context. Plays a central role in BMP signaling and olfactory neurogenesis. Associates with SMADs in response to BMP2 leading to activate transcription of BMP target genes. Acts as a transcriptional repressor via its interaction with EBF1, a transcription factor involved in terminal olfactory receptor neurons differentiation this interaction preventing EBF1 to bind DNA and activate olfactory-specific genes. Involved in olfactory neurogenesis by participating in a developmental switch that regulates the transition from differentiation to maturation in olfactory receptor neurons. Controls proliferation and differentiation of neural precursors in cerebellar vermis formation.
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O08962
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KCNH2_RAT
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Potassium voltage-gated channel subfamily H member 2 (Ether-a-go-go-related gene potassium channel 1) (ERG-1) (Eag-related protein 1) (Ether-a-go-go-related protein 1) (RERG) (r-ERG) (Voltage-gated potassium channel subunit Kv11.1)
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MPVRRGHVAPQNTFLDTIIRKFEGQSRKFIIANARVENCAVIYCNDGFCELCGYSRAEVMQRPCTCDFLHGPRTQRRAAAQIAQALLGAEERKVEIAFYRKDGSCFLCLVDVVPVKNEDGAVIMFILNFEVVMEKDMVGSPAHDTNHRGPSTSWLASGRAKTFRLKLPALLALTARESPMRTGSTGSPGAPGAVVVDVDLTPAAPSSESLALDEVSAMDNHVAGLGPAEERRALVGPASASPVASIPGPHPSPRAQSLNPDASGSSCSLARTRSRESCASVRRASSADDIEAMRAGALPLPPRHASTGAMHPLRSGLLNSTSDSDLVRYRTISKIPQITLNFVDLKGDPFLASPTSDREIIAPKIKERTHNVTEKVTQVLSLGADVLPEYKLQAPRIHRWTILHYSPFKAVWDWLILLLVIYTAVFTPYSAAFLLKETEDGSQAPDCGYACQPLAVVDLLVDIMFIVDILINFRTTYVNANEEVVSHPGRIAVHYFKGWFLIDMVAAIPFDLLIFGSGSEELIGLLKTARLLRLVRVARKLDRYSEYGAAVLFLLMCTFALIAHWLACIWYAIGNMEQPHMDSHIGWLHNLGDQIGKPYNSSGLGGPSIKDKYVTALYFTFSSLTSVGFGNVSPNTNSEKIFSICVMLIGSLMYASIFGNVSAIIQRLYSGTARYHTQMLRVREFIRFHQIPNPLRQRLEEYFQHAWSYTNGIDMNAVLKGFPECLQADICLHLNRSLLQHCKPFRGATKGCLRALAMKFKTTHAPPGDTLVHAGDLLTALYFISRGSIEILRGDVVVAILGKNDIFGEPLNLYARPGKSNGDVRALTYCDLHKIHRDDLLEVLDMYPEFSDHFWSSLEITFNLRDTNMIPGSPSSAELESGFNRQRKRKLSFRRRTDKDTEQPGEVSALGQGPARVGPGPSCRGQPGGPWGESPSSGPSSPESSEDEGPGRSSSPLRLVPFSSPRPPGDSPGGEPLTEDGEKSSDTCNPLSGAFSGVSNIFSFWGDSRGRQYQELPRCPAPAPSLLNIPLSSPGRRSRGDVESRLDALQRQLNRLETRLSADMATVLQLLQRQMTLVPPAYSAVTTPGPGPTSTSPLLPVGPVPTLTLDSLSQVSQFVAFEELPAGAPELPQDGPTRRLSLPGQLGALTSQPLHRHGSDPGS
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Pore-forming (alpha) subunit of voltage-gated inwardly rectifying potassium channel. Channel properties are modulated by cAMP and subunit assembly. Mediates the rapidly activating component of the delayed rectifying potassium current in heart (IKr) (By similarity).
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O08966
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S22A1_MOUSE
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Solute carrier family 22 member 1 (Organic cation transporter 1) (mOCT1)
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MPTVDDVLEHVGEFGWFQKQAFLLLCLISASLAPIYVGIVFLGFTPDHHCRSPGVAELSQRCGWSPAEELNYTVPGLGSAGEASFLSQCMKYEVDWNQSTLDCVDPLSSLAANRSHLPLSPCEHGWVYDTPGSSIVTEFNLVCGDAWKVDLFQSCVNLGFFLGSLVVGYIADRFGRKLCLLVTTLVTSLSGVLTAVAPDYTSMLLFRLLQGMVSKGSWVSGYTLITEFVGSGYRRTTAILYQVAFTVGLVGLAGVAYAIPDWRWLQLAVSLPTFLFLLYYWFVPESPRWLLSQKRTTQAVRIMEQIAQKNRKVPPADLKMMCLEEDASERRSPSFADLFRTPSLRKHTLILMYLWFSCAVLYQGLIMHVGATGANLYLDFFYSSLVEFPAAFIILVTIDRIGRIYPIAASNLVAGAACLLMIFIPHELHWLNVTLACLGRMGATIVLQMVCLVNAELYPTFIRNLGMMVCSALCDLGGIFTPFMVFRLMEVWQALPLILFGVLGLSAGAVTLLLPETKGVALPETIEEAENLGRRKSKAKENTIYLQVQTGKSPHT
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Electrogenic voltage-dependent transporter that mediates the transport of a variety of organic cations such as endogenous bioactive amines, cationic drugs and xenobiotics. Functions as a pH- and Na(+)-independent, bidirectional transporter (By similarity). Cation cellular uptake or release is driven by the electrochemical potential (i.e. membrane potential and concentration gradient) and substrate selectivity (By similarity). Hydrophobicity is a major requirement for recognition in polyvalent substrates and inhibitors. Primarily expressed in the basolateral membrane of hepatocytes and proximal tubules and involved in the uptake and disposition of cationic compounds from the blood by hepatic and renal clearance (By similarity). Most likely functions as an uptake carrier in enterocytes contributing to the intestinal elimination of organic cations from the systemic circulation. Transports endogenous monoamines such as N-1-methylnicotinamide (NMN), guanidine, neurotransmitters dopamine, serotonin, noradrenaline, adrenaline and histamine, and quaternary ammonium compound such as choline. Also transports natural polyamines such as spermidine, agmatine and putrescine at low affinity, but relatively high turnover. Involved in the hepatic and intestinal uptake of the vitamin B1/thiamine, hence regulating hepatic lipid and energy metabolism. Contributes to the influx and efflux of fatty acid carriers carnitines and acylcarnitines across the basolateral membrane of hepatocytes, from the liver to the systemic circulation and inversely and may be involved in regulating the systemic availability of hepatic acylcarnitines. Also capable of transporting non-amine endogenous compounds such as prostaglandin E2 (PGE2) and prostaglandin F2-alpha (PGF2-alpha) (By similarity). May contribute to the transport of cationic compounds in testes across the blood-testis-barrier (By similarity). Also mediates the uptake of xenobiotics tributylmethylammonium (TBuMA), quinidine, N-methyl-quinine (NMQ), N-methyl-quinidine (NMQD) N-(4,4-azo-n-pentyl)-quinuclidine (APQ), azidoprocainamide methoiodide (AMP), N-(4,4-azo-n-pentyl)-21-deoxyajmalinium (APDA) and 4-(4-(dimethylamino)styryl)-N-methylpyridinium (ASP).
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O08967
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CYH3_MOUSE
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Cytohesin-3 (ARF nucleotide-binding site opener 3) (Protein ARNO3) (General receptor of phosphoinositides 1) (Grp1) (PH, SEC7 and coiled-coil domain-containing protein 3) (CLM3) (SEC7 homolog C) (mSec7-3)
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MDEGGGGEGGSVPEDLSLEEREELLDIRRRKKELIDDIERLKYEIAEVMTEIDNLTSVEESKTTQRNKQIAMGRKKFNMDPKKGIQFLIENDLLQSSPEDVAQFLYKGEGLNKTVIGDYLGERDDFNIKVLQAFVELHEFADLNLVQALRQFLWSFRLPGEAQKIDRMMEAFASRYCLCNPGVFQSTDTCYVLSFAIIMLNTSLHNHNVRDKPTAERFITMNRGINEGGDLPEELLRNLYESIKNEPFKIPEDDGNDLTHTFFNPDREGWLLKLGGRVKTWKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSIREVEDPRKPNCFELYNPSHKGQVIKACKTEADGRVVEGNHVVYRISAPSPEEKEEWMKSIKASISRDPFYDMLATRKRRIANKK
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Promotes guanine-nucleotide exchange on ARF1. Promotes the activation of ARF factors through replacement of GDP with GTP. Plays a role in the epithelial polarization.
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O08969
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PHLA2_MOUSE
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Pleckstrin homology-like domain family A member 2 (Imprinted in placenta and liver protein) (Protein 50C15)
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MASKIVMSSKTVKTSDEILCEGELEKRSDSLFQVWKKKRCVLTADRLRLFSGKTSPAKELFFHSILKVDCVEHTSKYVYFTIVTNYYKEIDFRCTVESCWNAAITMALIDFQNRRALQDFPRYRYQRSESEMPSEPGEQSALGP
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Plays a role in regulating placenta growth. May act via its PH domain that competes with other PH domain-containing proteins, thereby preventing their binding to membrane lipids.
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O08983
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HPS1_MOUSE
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BLOC-3 complex member HPS1 (Hermansky-Pudlak syndrome 1 protein homolog)
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MKCVLVATEGAEVLFYWTDEEFAESLRLKLQQSEDEEEELPVLEDQLSTLLAPVIISSMTMLEKLSDTYTCFSTENDNHLYVLHLFGEYLFVAINGDHSESEGDLRRKLCVLKYLFEVHFGLVTVDGQLIRKELRPPDLEERARVWKHFQRLLGTYSYLRDREQSFAVEAVERLIHPQLCEQSIETLERHVVQAINASPERGGEEVLHAFLLVHCKLLAFYSGHGASTLRPADLLALILLVQDLQPSPGTTEEEEEEEDSDSPQRRPKSSQNIPVQQARSQSTSVPTRSSRETDTDSISLPEEYFTPAPSPGDQSSGSLVWLDGGTPPSDALQMAEDTPEGLASHSPELPSPRRIFLDANIKENYCPLVPHTMYCLPLWPGINMVLLTKSPSTPLALILYQLLDGFSLLEKKLKEGQEAGSALRSQPFVADLRQKMDKFIKNRVGQEIQNTWLEFKSKAFSRSEPGSSWELLQVCGKLKRQLCVIYRLSFLVTAPSRGGPHLPQHLQDRAQKLMKERLLDWKDFLLVKSRRNVTMVSYLEDFPGLVHFIYVDRTTGQMVAPSLSPNEKMSSELGKGPLAAFVKAKVWALVRLARRYLQKGCTTLLFQEGDFRCSYFLWFENDMGYKLQMIEVPVLSDDSVPIGVLGGDYYRKLLRYYSKSHPSEPVRCYELLTLHLSVIPTDLLVQQASQLARRLGEASRVTLP
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Component of the BLOC-3 complex, a complex that acts as a guanine exchange factor (GEF) for RAB32 and RAB38, promotes the exchange of GDP to GTP, converting them from an inactive GDP-bound form into an active GTP-bound form. The BLOC-3 complex plays an important role in the control of melanin production and melanosome biogenesis and promotes the membrane localization of RAB32 and RAB38.
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O08984
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LBR_RAT
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Delta(14)-sterol reductase LBR (Delta-14-SR) (EC 1.3.1.70) (3-beta-hydroxysterol Delta (14)-reductase) (C-14 sterol reductase) (C14SR) (Integral nuclear envelope inner membrane protein) (Lamin-B receptor) (NBP60) (Sterol C14-reductase)
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MPGRKFADGEVVRGRWPGSSLYYEVEILSHDSTSQLYTVKYKDGTELELKESDIKPLKSFKQRKSGSTSSSPSRRRSSRSRSRSRSRSPGRAPKGSRRSVSASYQADAKEKEMRREILQVKLTPLVLKPFANSVSVYNGEPEHMEKSATPPKNKQERVILSTEDSYIATQYSLRPRREEVKPKHRVRGTNLVTRGPVPLGTFQVTTPQRRDLEFGGVPGALLIMLGLPACVFLLLLQCAQKDPGLLQFPPPLPALRELWEARVCGVYLLWFFLQALFSLLPVGKVVEGTPLVDGRRLKYRLNGLYAFILTSAAVGTAVFWDIELYYLYTHFLQFALAAIVFSVVLSVYLYARSLKVPRDELSPASSGNAVYDFFIGRELNPRIGAFDLKFFCELRPGLIGWVVINLVMLLAEMKVQERSAPSLAMTLVNSFQLLYVVDALWFEEALLTTMDIIHDGFGFMLAFGDLVWVPFTYSLQAFYLVNHPQDLSWPLTSVIIALKLCGYVIFRCANSQKNAFRKNPTDPKLAHLKTIPTSTWKSLLVSGWWGFVRHPNYLGDLIMALAWSLPCGFNHILPYFYVIYFTALLIHREARDEHQCRRKYGLAWEKYCQRVPYRIFPYIY
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Catalyzes the reduction of the C14-unsaturated bond of lanosterol, as part of the metabolic pathway leading to cholesterol biosynthesis (By similarity). Plays a critical role in myeloid cell cholesterol biosynthesis which is essential to both myeloid cell growth and functional maturation (By similarity). Mediates the activation of NADPH oxidases, perhaps by maintaining critical levels of cholesterol required for membrane lipid raft formation during neutrophil differentiation (By similarity). Anchors the lamina and the heterochromatin to the inner nuclear membrane (By similarity).
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O08992
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SDCB1_MOUSE
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Syntenin-1 (Scaffold protein Pbp1) (Syndecan-binding protein 1)
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MSLYPSLEDLKVDKVIQAQTAYSANPASQAFVLVDASAALPPDGNLYPKLYPELSQYMGLSLNEAEICESMPMVSGAPAQGQLVARPSSVNYMVAPVTGNDAGIRRAEIKQGIREVILCKDQDGKIGLRLKSIDNGIFVQLVQANSPASLVGLRFGDQVLQINGENCAGWSSDKAHKVLKQAFGEKITMTIRDRPFERTVTMHKDSSGHVGFIFKSGKITSIVKDSSAARNGLLTDHHICEINGQNVIGLKDAQIADILSTAGTVVTITIMPTFIFEHIIKRMAPSIMKSLMDHTIPEV
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Multifunctional adapter protein involved in diverse array of functions including trafficking of transmembrane proteins, neuro and immunomodulation, exosome biogenesis, and tumorigenesis. Positively regulates TGFB1-mediated SMAD2/3 activation and TGFB1-induced epithelial-to-mesenchymal transition (EMT) and cell migration in various cell types. May increase TGFB1 signaling by enhancing cell-surface expression of TGFR1 by preventing the interaction between TGFR1 and CAV1 and subsequent CAV1-dependent internalization and degradation of TGFR1. In concert with SDC1/4 and PDCD6IP, regulates exosome biogenesis (By similarity). Regulates migration, growth, proliferation, and cell cycle progression in a variety of cancer types. In adherens junctions may function to couple syndecans to cytoskeletal proteins or signaling components. Seems to couple transcription factor SOX4 to the IL-5 receptor (IL5RA). May also play a role in vesicular trafficking. Seems to be required for the targeting of TGFA to the cell surface in the early secretory pathway (By similarity).
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O09000
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NCOA3_MOUSE
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Nuclear receptor coactivator 3 (NCoA-3) (EC 2.3.1.48) (Amplified in breast cancer-1 protein homolog) (AIB-1) (CBP-interacting protein) (p/CIP) (pCIP) (Receptor-associated coactivator 3) (RAC-3) (Steroid receptor coactivator protein 3) (SRC-3) (Thyroid hormone receptor activator molecule 1) (ACTR) (TRAM-1)
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MSGLGESSLDPLAAESRKRKLPCDAPGQGLVYSGEKWRREQESKYIEELAELISANLSDIDNFNVKPDKCAILKETVRQIRQIKEQGKTISSDDDVQKADVSSTGQGVIDKDSLGPLLLQALDGFLFVVNRDGNIVFVSENVTQYLQYKQEDLVNTSVYSILHEPRRKDFLNTYQNPQLMEFLGLMRTRDKKAPYILIVRMLMKTHDILEDVNASPETRQRYETMQCFALSQPRAMLEEGEDLQCCMICVARRVTAPFPSSPESFITRHDLSGKVVNIDTNSLRSSMRPGFEDIIRRCIQRFFSLNDGQSWSQKRHYQEAYVHGHAETPVYRFSLADGTIVSAQTKSKLFRNPVTNDRHGFISTHFLQREQNGYRPNPIPQDKGIRPPAAGCGVSMSPNQNVQMMGSRTYGVPDPSNTGQMGGARYGASSSVASLTPGQSLQSPSSYQNSSYGLSMSSPPHGSPGLGPNQQNIMISPRNRGSPKMASHQFSPAAGAHSPMGPSGNTGSHSFSSSSLSALQAISEGVGTSLLSTLSSPGPKLDNSPNMNISQPSKVSGQDSKSPLGLYCEQNPVESSVCQSNSRDPQVKKESKESSGEVSETPRGPLESKGHKKLLQLLTCSSDDRGHSSLTNSPLDPNCKDSSVSVTSPSGVSSSTSGTVSSTSNVHGSLLQEKHRILHKLLQNGNSPAEVAKITAEATGKDTSSTASCGEGTTRQEQLSPKKKENNALLRYLLDRDDPSDVLAKELQPQADSGDSKLSQCSCSTNPSSGQEKDPKIKTETNDEVSGDLDNLDAILGDLTSSDFYNNPTNGGHPGAKQQMFAGPSSLGLRSPQPVQSVRPPYNRAVSLDSPVSVGSGPPVKNVSAFPGLPKQPILAGNPRMMDSQENYGANMGPNRNVPVNPTSSPGDWGLANSRASRMEPLASSPLGRTGADYSATLPRPAMGGSVPTLPLRSNRLPGARPSLQQQQQQQQQQQQQQQQQQQQQQQMLQMRTGEIPMGMGVNPYSPAVQSNQPGSWPEGMLSMEQGPHGSQNRPLLRNSLDDLLGPPSNAEGQSDERALLDQLHTFLSNTDATGLEEIDRALGIPELVNQGQALESKQDVFQGQEAAVMMDQKAALYGQTYPAQGPPLQGGFNLQGQSPSFNSMMGQISQQGSFPLQGMHPRAGLVRPRTNTPKQLRMQLQQRLQGQQFLNQSRQALEMKMENPAGTAVMRPMMPQAFFNAQMAAQQKRELMSHHLQQQRMAMMMSQPQPQAFSPPPNVTASPSMDGVLAGSAMPQAPPQQFPYPANYGMGQPPEPAFGRGSSPPSAMMSSRMGPSQNAMVQHPQPTPMYQPSDMKGWPSGNLARNGSFPQQQFAPQGNPAAYNMVHMNSSGGHLGQMAMTPMPMSGMPMGPDQKYC
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Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Plays a central role in creating a multisubunit coactivator complex, probably via remodeling of chromatin. Involved in the coactivation of different nuclear receptors, such as for steroids (GR and ER), retinoids (RARs and RXRs), thyroid hormone (TRs), vitamin D3 (VDR) and prostanoids (PPARs). Displays histone acetyltransferase activity. Also involved in the coactivation of the NF-kappa-B pathway via its interaction with the NFKB1 subunit (By similarity). {ECO:0000250, ECO:0000269|PubMed:10823921}.
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O09005
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DEGS1_MOUSE
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Sphingolipid delta(4)-desaturase DES1 (EC 1.14.19.17) (Degenerative spermatocyte homolog 1) (Dihydroceramide desaturase-1) (Retinol isomerase) (EC 5.2.1.-)
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MGSRVSREEFEWVYTDQPHAARRKEILAKYPEIKSLMKPDHNLIWIVAMMLLVQLASFYLVKDLDWKWVIFWSYVFGSCLNHSMTLAIHEISHNFPFGHHKALWNRWFGMFANLSLGVPYSISFKRYHMDHHRYLGADKIDVDIPTDFEGWFFCTTFRKFVWVILQPLFYAFRPLFINPKPITYLEIINTVIQITFDIIIYYVFGVKSLVYMLAATLLGLGLHPISGHFIAEHYMFLKGHETYSYYGPLNLLTFNVGYHNEHHDFPNVPGKNLPMVRKIASEYYDDLPHYNSWIKVLYDFVTDDTISPYSRMKRPPKGNEILE
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Has sphingolipid-delta-4-desaturase activity. Converts D-erythro-sphinganine to D-erythro-sphingosine (E-sphing-4-enine). Catalyzes the equilibrium isomerization of retinols (By similarity).
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O09008
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MFNG_MOUSE
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Beta-1,3-N-acetylglucosaminyltransferase manic fringe (EC 2.4.1.222) (O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase)
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MHCRLFRGMAGALFTLLCVGLLSLRYHSSLSQRMIQGALRLNQRNPGPLELQLGDIFIAVKTTWAFHRSRLDLLLDTWVSRIRQQTFIFTDSPDERLQERLGPHLVVTNCSAEHSHPALSCKMAAEFDAFLVSGLRWFCHVDDDNYVNPKALLQLLKTFPQDRDVYVGKPSLNRPIHASELQSKNRTKLVRFWFATGGAGFCINRQLALKMVPWASGSHFVDTSALIRLPDDCTVGYIIECKLGGRLQPSPLFHSHLETLQLLGAAQLPEQVTLSYGVFEGKLNVIKLPGPFSHEEDPSRFRSLHCLLYPDTPWCPLLAAP
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Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in inhibition of NOTCH1 activation by JAG1 and enhancement of NOTCH1 activation by DLL1 via an increase in its binding to DLL1.
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O09009
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RFNG_MOUSE
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Beta-1,3-N-acetylglucosaminyltransferase radical fringe (EC 2.4.1.222) (O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase)
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MSRARRVLCRACLALAAVLAVLLLLPLPLPLPLPRAPAPDPDRVPTRSLTLEGDRLQPDDVFIAVKTTRKNHGPRLRLLLRTWISRAPRQTFIFTDGDDPELQMLAGGRMINTNCSAVRTRQALCCKMSVEYDKFLESGRKWFCHVDDDNYVNPKSLLHLLSTFSSNQDIYLGRPSLDHPIEATERVQGGGTSNTVKFWFATGGAGFCLSRGLALKMSPWASLGSFMSTAERVRLPDDCTVGYIVEGLLGARLLHSPLFHSHLENLQRLPSGAILQQVTLSYGGPENPHNVVNVAGSFNIQQDPTRFQSVHCLLYPDTHWCPMKNRVEGAFQ
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Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in enhancement of NOTCH1 activation by DLL1 and JAG1. May be involved in limb formation and in neurogenesis (By similarity).
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O09010
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LFNG_MOUSE
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Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe (EC 2.4.1.222) (O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase)
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MLQRCGRRLLLALVGALLACLLVLTADPPPTPMPAERGRRALRSLAGSSGGAPASGSRAAVDPGVLTREVHSLSEYFSLLTRARRDADPPPGVASRQGDGHPRPPAEVLSPRDVFIAVKTTRKFHRARLDLLFETWISRHKEMTFIFTDGEDEALAKLTGNVVLTNCSSAHSRQALSCKMAVEYDRFIESGKKWFCHVDDDNYVNLRALLRLLASYPHTQDVYIGKPSLDRPIQATERISEHKVRPVHFWFATGGAGFCISRGLALKMGPWASGGHFMSTAERIRLPDDCTIGYIVEALLGVPLIRSGLFHSHLENLQQVPTTELHEQVTLSYGMFENKRNAVHIKGPFSVEADPSRFRSVHCHLYPDTPWCPRSAIF
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Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in inhibition of NOTCH1 activation by JAG1 and enhancement of NOTCH1 activation by DLL1 via an increase in its binding to DLL1. Decreases the binding of JAG1 to NOTCH2 but not that of DLL1 (By similarity). Essential mediator of somite segmentation and patterning. During somite boundary formation, it restricts Notch activity in the presomitic mesoderm to a boundary-forming territory in the posterior half of the prospective somite. In this region, Notch function activates a set of genes that are involved in boundary formation and in anterior-posterior somite identity. Ectopically expressed in the thymus, Lfgn inhibits Notch signaling which results in inhibition of T-cell commitment and promotes B-cell development in lymphoid progenitors. May play a role in boundary formation of the enamel knot.
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O09012
|
PEX5_MOUSE
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Peroxisomal targeting signal 1 receptor (PTS1 receptor) (PTS1R) (PTS1-BP) (PXR1P) (Peroxin-5) (Peroxisomal C-terminal targeting signal import receptor) (Peroxisome receptor 1)
|
MAMRELVEGECGGANPLMKLATHFTQDKALRQEGLRPGPWPPGASAAETVSKPLGVGTEDELVSEFLQDQNATLVSRAPQTFKMDDLLAEMQEIEQSNFRQAPQRAPGVADLALSENWAQEFLAAGDAVDVAQDYNETDWSQEFIAEVTDPLSVSPARWAEEYLEQSEEKLWLGDQEGSSTADRWYDEYHPEEDLQHTASDFVSKVDDPKLANSEFLKFVRQIGEGQVSLESAAGSGGAQAEQWAAEFIQQQGTSEAWVDQFTRPGNKIAALQVEFERAKSAIESDVDFWDKLQAELEEMAKRDAEAHPWLSDYDDLTSASYDKGYQFEEENPLRDHPQPFEEGLHRLEEGDLPNAVLLFEAAVQQDPKHMEAWQYLGTTQAENEQELLAISALRRCLELKPDNRTALMALAVSFTNESLQRQACETLRDWLRYSPAYAHLVAPGEEGATGAGPSKRILGSLLSDSLFLEVKDLFLAAVRLDPTSIDPDVQCGLGVLFNLSGEYDKAVDCFTAALSVRPNDYLMWNKLGATLANGNQSEEAVAAYRRALELQPGYIRSRYNLGISCINLGAHREAVEHFLEALNMQRKSRGPRGEGGAMSENIWSTLRLALSMLGQSDAYGAADARDLSALLAMFGLPQ
|
Receptor that mediates peroxisomal import of proteins containing a C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type). Binds to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, and translocates them into the peroxisome matrix by passing through the PEX13-PEX14 docking complex along with cargo proteins. PEX5 receptor is then retrotranslocated into the cytosol, leading to release of bound cargo in the peroxisome matrix, and reset for a subsequent peroxisome import cycle. [Isoform 1]: In addition to promoting peroxisomal translocation of proteins containing a PTS1 peroxisomal targeting signal, mediates peroxisomal import of proteins containing a C-terminal PTS2-type peroxisomal targeting signal via its interaction with PEX7. Interaction with PEX7 only takes place when PEX7 is associated with cargo proteins containing a PTS2 peroxisomal targeting signal. PEX7 along with PTS2-containing cargo proteins are then translocated through the PEX13-PEX14 docking complex together with PEX5.
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O09014
|
S15A4_RAT
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Solute carrier family 15 member 4 (Peptide/histidine transporter 1) (rPHT1)
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MEGERAPLLGSRRAAAAAGVFAGRRAACGAVLLAELLERAAFYGVTANLVLFLNGAPFNWEGAQASQALLLFMGLTYLGSPFGGWLADARLGRARAILLSLALYLLGMLAFPLLAAPRSRSFLCGDPHPELVRNCSAPFPNGTAVCPDAAARRCAPATFAGLVLVGLGVATVKANITPFGADQVKDRGPEATRRFFNWFYWSINLGAILSLGGIAYIQQNVSFLTGYLIPTVCVAIAFLVFLCGQSVFITKPPDGSAFTDMFRILTYSCCSQRGGQRRSGEGLGVFQQSSKHSLFDSCKMSRGGPFTEDKVEDVKALVKIVPVFLALIPYWTVYFQMQTTYVLQSLHLKIPEISSITTTHHTLPAAWLTMFDAVLILLLIPLKDKLVDPVLRRHGLLPSSLKRIAVGMFFVTCSAFAAGILESKRLDLVKEKTINQTIGGVVYHAADLPIWWQIPQYVLIGISEIFASIAGLEFAYSAAPKSMQSAIMGLFFFFSGIGSFVGSGLLALVSLKAIGWMSSHTDFGNINSCHLHYYFFLLAAIQGATLLLFLIVSVKYDRQRARTDGGTASTRT
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Proton-coupled amino-acid transporter that mediates the transmembrane transport of L-histidine and some di- and tripeptides from inside the lysosome to the cytosol, and plays a key role in innate immune response. Able to transport a variety of di- and tripeptides, including carnosine and some peptidoglycans (By similarity). Transporter activity is pH-dependent and maximized in the acidic lysosomal environment. Involved in the detection of microbial pathogens by toll-like receptors (TLRs) and NOD-like receptors (NLRs), probably by mediating transport of bacterial peptidoglycans across the endolysosomal membrane: catalyzes the transport of certain bacterial peptidoglycans, such as muramyl dipeptide (MDP), the NOD2 ligand, and L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate (tri-DAP), the NOD1 ligand. Required for TLR7, TLR8 and TLR9-mediated type I interferon (IFN-I) productions in plasmacytoid dendritic cells (pDCs). Independently of its transporter activity, also promotes the recruitment of innate immune adapter TASL to endolysosome downstream of TLR7, TLR8 and TLR9: TASL recruitment leads to the specific recruitment and activation of IRF5 (By similarity). Required for isotype class switch recombination to IgG2c isotype in response to TLR9 stimulation. Required for mast cell secretory-granule homeostasis by limiting mast cell functions and inflammatory responses (By similarity).
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O09017
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NR2F6_RAT
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Nuclear receptor subfamily 2 group F member 6 (COUPg) (Ovalbumin upstream promoter gamma nuclear receptor) (V-erbA-related protein 2) (EAR-2)
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MAMVTGGWGGPGGDTNGVDKAGGSYPRATEDDSASPPGATSDAEPGDEERPGLQVDCVVCGDKSSGKHYGVFTCEGCKSFFKRTIRRNLSYTCRSNRDCQIDQHHRNQCQYCRLKKCFRVGMRKEAVQPGPIPHALPGPAACSPPGAAGVEPFAGPPVSELIAQLLRAEPYPAAGRFGGGGAVLGIDNVCELAARLLFSTVEWARHAPFFPELPAADQVGLLRLSWSELFVLNAAQAPVPLHTAPLLAAAGLHAGPMAAERAVAFMDQVRAFQEQVDKLGRLQVDAAEYGCLKAIALFTPDACGLSDPAHVESLQEKAQVALTEYVRAQYPSQPQRFGRLLLRLPALRAVPASLISQLFFMRLVGKTPIETLIRDMLLSGSTFNWPYGSG
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Transcription factor predominantly involved in transcriptional repression. Binds to promoter/enhancer response elements that contain the imperfect 5'-AGGTCA-3' direct or inverted repeats with various spacings which are also recognized by other nuclear hormone receptors. Involved in modulation of hormonal responses. Represses transcriptional activity of the lutropin-choriogonadotropic hormone receptor/LHCGR gene, the renin/REN gene and the oxytocin-neurophysin/OXT gene. Represses the triiodothyronine-dependent and -independent transcriptional activity of the thyroid hormone receptor gene in a cell type-specific manner. The corepressing function towards thyroid hormone receptor beta/THRB involves at least in part the inhibition of THRB binding to triiodothyronine response elements (TREs) by NR2F6. Inhibits NFATC transcription factor DNA binding and subsequently its transcriptional activity. Acts as transcriptional repressor of IL-17 expression in Th-17 differentiated CD4(+) T cells and may be involved in induction and/or maintenance of peripheral immunological tolerance and autoimmunity. Involved in development of forebrain circadian clock is required early in the development of the locus coeruleus (LC) (By similarity). {ECO:0000250, ECO:0000269|PubMed:9343308}.
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O09018
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COT2_RAT
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COUP transcription factor 2 (COUP-TF2) (Apolipoprotein A-I regulatory protein 1) (ARP-1) (COUP transcription factor II) (COUP-TF II) (COUPb) (Nuclear receptor subfamily 2 group F member 2) (Ovalbumin upstream promoter beta nuclear receptor)
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MAMVVSTWRDPQDEVPGSQGSQASQAPPVPGPPPGAPHTPQTPGQGGPASTPAQTAAGSQGGPGGPGSDKQQQQQHIECVVCGDKSSGKHYGQFTCEGCKSFFKRSVRRNLSYTCRANRNCPIDQHHRNQCQYCRLKKCLKVGMRREAVQRGRMPPTQPTHGQFALTNGDPLNCHSYLSGYISLLLRAEPYPTSRFGSQCMQPNNIMGIENICELAARMLFSAVEWARNIPFFPDLQITDQVALLRLTWSELFVLNAAQCSMPLHVAPLLAAAGLHASPMSADRVVAFMDHIRIFQEQVEKLKALHVDSAEYSCLKAIVLFTSDACGLSDVAHVESLQEKSQCALEEYVRSQYPNQPTRFGKLLLRLPSLRTVSSSVIEQLFFVRLVGKTPIETLIRDMLLSGSSFNWPYMAIQ
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Ligand-activated transcription factor. Activated by high concentrations of 9-cis-retinoic acid and all-trans-retinoic acid, but not by dexamethasone, cortisol or progesterone (in vitro). Regulation of the apolipoprotein A-I gene transcription. Binds to DNA site A. May be required to establish ovary identity during early gonad development.
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O09027
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ACKR2_RAT
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Atypical chemokine receptor 2 (C-C chemokine receptor D6) (CCR10-related receptor) (Chemokine-binding protein 2) (Chemokine-binding protein D6)
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MPTIASPLPLATTGPENGSSIYDYDYLDDVTVLVCSKDEVLSFGRVFLPVVYSLIFVLGLAGNLLLLVVLLHSVPQRRRMIELYLLNLAVSNLLFVVTMPFWAISVAWHWVFGSFLCKVVSTLYSINFYCGIFFITCMSLDKYLEIVHAQPLHRPKTRFRNLLLIVMVWITALAVSVPEMVFVKVHQTLDGVWHCYADFGGHATIWKLYLRFQMNLLGFLFPLLAMIFFYSRIGCVLVRLRPPGQGRALRMAAALVVVFFLLWFPYNLTLFLHSLLDLHVFGNCKISHRLDYMLQVTESLAFSHCCFTPVLYAFSSHSFRQYLKAVLSVVLRRHQAPGTAHAPPCSHSESSRVTAQEDVVSMNDLGERQADISLNKGEIGNN
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Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines including CCL2, CCL3, CCL3L1, CCL4, CCL5, CCL7, CCL8, CCL11, CCL13, CCL17, CCL22, CCL23, CCL24, SCYA2/MCP-1, SCY3/MIP-1-alpha, SCYA5/RANTES and SCYA7/MCP-3. Upon active ligand stimulation, activates a beta-arrestin 1 (ARRB1)-dependent, G protein-independent signaling pathway that results in the phosphorylation of the actin-binding protein cofilin (CFL1) through a RAC1-PAK1-LIMK1 signaling pathway. Activation of this pathway results in up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. By scavenging chemokines in tissues, on the surfaces of lymphatic vessels, and in placenta, plays an essential role in the resolution (termination) of the inflammatory response and in the regulation of adaptive immune responses. Plays a major role in the immune silencing of macrophages during the resolution of inflammation. Acts as a regulator of inflammatory leukocyte interactions with lymphatic endothelial cells (LECs) and is required for immature/mature dendritic cells discrimination by LECs.
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O09032
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ELAV4_RAT
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ELAV-like protein 4 (Hu-antigen D) (HuD) (Paraneoplastic encephalomyelitis antigen HuD)
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MEWNGLKMIISTMEPQVSNGPTSNTSNGPSSNNRNCPSPMQTGAATDDSKTNLIVNYLPQNMTQEEFRSLFGSIGEIESCKLVRDKITGQSLGYGFVNYIDPKDAEKAINTLNGLRLQTKTIKVSYARPSSASIRDANLYVSGLPKTMTQKELEQLFSQYGRIITSRILVDQVTGVSRGVGFIRFDKRIEAEEAIKGLNGQKPSGATEPITVKFANNPSQKSSQALLSQLYQSPNRRYPGPLHHQAQRFRLDNLLNMAYGVKRLMSGPVPPSACPPRFSPITIDGMTSLVGMNIPGHTGTGWCIFVYNLSPDSDESVLWQLFGPFGAVNNVKVIRDFNTNKCKGFGFVTMTNYDEAAMAIASLNGYRLGDRVLQVSFKTNKAHKS
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RNA-binding protein that is involved in the post-transcriptional regulation of mRNAs. Plays a role in the regulation of mRNA stability, alternative splicing and translation. Binds to AU-rich element (ARE) sequences in the 3' untranslated region (UTR) of target mRNAs, including GAP43, VEGF, FOS, CDKN1A and ACHE mRNA. Many of the target mRNAs are coding for RNA-binding proteins, transcription factors and proteins involved in RNA processing and/or neuronal development and function (By similarity). By binding to the mRNA 3'UTR, decreases mRNA deadenylation and thereby contributes to the stabilization of mRNA molecules and their protection from decay (By similarity). Also binds to the polyadenylated (poly(A)) tail in the 3'UTR of mRNA, thereby increasing its affinity for mRNA binding (By similarity). Mainly plays a role in neuron-specific RNA processing by stabilization of mRNAs such as GAP43, ACHE and mRNAs of other neuronal proteins, thereby contributing to the differentiation of neural progenitor cells, nervous system development, learning and memory mechanisms. Involved in the negative regulation of the proliferative activity of neuronal stem cells and in the positive regulation of neuronal differentiation of neural progenitor cells (By similarity). Promotes neuronal differentiation of neural stem/progenitor cells in the adult subventricular zone of the hippocampus by binding to and stabilizing SATB1 mRNA (By similarity). Binds and stabilizes MSI1 mRNA in neural stem cells (By similarity). Exhibits increased binding to ACHE mRNA during neuronal differentiation, thereby stabilizing ACHE mRNA and enhancing its expression (By similarity). Protects CDKN1A mRNA from decay by binding to its 3'-UTR. May bind to APP and BACE1 mRNAS and the BACE1AS lncRNA and enhance their stabilization (By similarity). Plays a role in neurite outgrowth and in the establishment and maturation of dendritic arbors, thereby contributing to neocortical and hippocampal circuitry function (By similarity). Stabilizes GAP43 mRNA and protects it from decay during postembryonic development in the brain. By promoting the stabilization of GAP43 mRNA, plays a role in NGF-mediated neurite outgrowth. Binds to BDNF long 3'UTR mRNA, thereby leading to its stabilization and increased dendritic translation after activation of PKC. By increasing translation of BDNF after nerve injury, may contribute to nerve regeneration (By similarity). Acts as a stabilizing factor by binding to the 3'UTR of NOVA1 mRNA, thereby increasing its translation and enhancing its functional activity in neuron-specific splicing (By similarity). Stimulates translation of mRNA in a poly(A)- and cap-dependent manner, possibly by associating with the EIF4F cap-binding complex (By similarity). May also negatively regulate translation by binding to the 5'UTR of Ins2 mRNA, thereby repressing its translation (By similarity). Upon glucose stimulation, Ins2 mRNA is released form ELAVL4 and translational inhibition is abolished (By similarity). Also plays a role in the regulation of alternative splicing (By similarity). May regulate alternative splicing of CALCA pre-mRNA into Calcitonin and calcitonin gene-related peptide 1 (CGRP) by competing with splicing regulator TIAR for binding to U-rich sequences of CALCA pre-mRNA (By similarity).
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O09037
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REG3A_MOUSE
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Regenerating islet-derived protein 3-alpha (REG-3-alpha) (Islet of Langerhans regenerating protein 3) (Lithostathine 3) (Pancreatitis-associated protein 2) (Regenerating islet-derived protein III-alpha) (Reg III-alpha) [Cleaved into: Regenerating islet-derived protein 3-alpha 16.5 kDa form; Regenerating islet-derived protein 3-alpha 15 kDa form]
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MLPHLVLNSISWMLLSCLLFVFQVQGEDFQKEVPSPRTSCPMGYKAYRSHCYALVMTPKSWFQADLVCQKRPSGHLVSILSGGEASFVSSLVNGRVDNYQDIWIGLHDPTMGQQPNGGGWEWSNSDVLNYLNWDGDPSSTVNRGHCGSLTASSGFLKWGDYYCDGTLPFVCKFKQ
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Bactericidal C-type lectin. The lack of the EPN motif may explain its inability to bind peptidoglycan. Acts as a hormone in response to different stimuli like anti-inflammatory signals, such as IL17A, or gut microbiome. Secreted by different cell types to activate its receptor EXTL3 and induce cell specific signaling pathways. Induced by IL17A in keratinocytes, regulates keratinocyte proliferation and differentiation after skin injury via activation of EXTL3-PI3K-AKT signaling pathway (By similarity). In parallel, inhibits skin inflammation through the inhibition of inflammatory cytokines such as IL6 and TNF. In pancreas, is able to permealize beta-cells membrane and stimulate their proliferation.
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O09039
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SH2B3_MOUSE
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SH2B adapter protein 3 (Lymphocyte adapter protein) (Lymphocyte-specific adapter protein Lnk) (Signal transduction protein Lnk)
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MNEPTVQPSRTSSAPASPASPRGWSDFCEQHAAAAARELARQYWLFARAHPQPPRADLVSLQFAELFQRHFCREVRESLAGPPGHDYRATAPPRPALPKARSSEDLGPRPACALQHLRRGLRQLFRRRSAGELPGATSDTNDIDTTAASRPGPARKLLPWGLREPPTEALKEVVLRYSLADEAAMDSGARWQRGRLVLRSPGPGHSHFLQLFDPPKSSKPKLQEACSSIREVRPCTRLEMPDNLYTFVLKVQDQTDIIFEVGDEQQLNSWLAELRASTGLGLEHPDTELPLSLAAEPGPARSPRGSTDSLDQGASPGVLLDPACQKTDHFLSCYPWFHGPISRVRAAQLVQLQGPDAHGVFLVRQSESRRGEYVLTFNLQGRAKHLRLVLTERGQCRVQHLHFPSVVDMLRHFQRSPIPLECGAACDVRLSGYVVVLSQAPGSSNTVLFPFSLPHWDSELGHPHLSSVGCPPSHGAEALPGQVTPPEQIFHLVPSPEELANSLRQLELESVSSARDSDYDMDSSSRGHLRAIDNQYTPLSQLCREADV
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Links T-cell receptor activation signal to phospholipase C-gamma-1, GRB2 and phosphatidylinositol 3-kinase.
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O09043
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NAPSA_MOUSE
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Napsin-A (EC 3.4.23.-) (KDAP-1) (Kidney-derived aspartic protease-like protein) (KAP)
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MSPLLLLLLCLLLGNLEPEEAKLIRVPLQRIHLGHRILNPLNGWEQLAELSRTSTSGGNPSFVPLSKFMNTQYFGTIGLGTPPQNFTVVFDTGSSNLWVPSTRCHFFSLACWFHHRFNPKASSSFRPNGTKFAIQYGTGRLSGILSQDNLTIGGIHDAFVTFGEALWEPSLIFALAHFDGILGLGFPTLAVGGVQPPLDAMVEQGLLEKPVFSFYLNRDSEGSDGGELVLGGSDPAHYVPPLTFIPVTIPAYWQVHMESVKVGTGLSLCAQGCSAILDTGTSLITGPSEEIRALNKAIGGYPFLNGQYFIQCSKTPTLPPVSFHLGGVWFNLTGQDYVIKILQSDVGLCLLGFQALDIPKPAGPLWILGDVFLGPYVAVFDRGDKNVGPRVGLARAQSRSTDRAERRTTQAQFFKRRPG
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May be involved in processing of pneumocyte surfactant precursors.
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O09044
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SNP23_MOUSE
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Synaptosomal-associated protein 23 (SNAP-23) (Syndet) (Vesicle-membrane fusion protein SNAP-23)
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MDNLSPEEVQLRAHQVTDESLESTRRILGLAIESQDAGIKTITMLDEQGEQLNRIEEGMDQINKDMREAEKTLTELNKCCGLCICPCNRTKNFESGKNYKATWGDGGDNSPSNVVSKQPSRITNGQPQQTTGAASGGYIKRITNDAREDEMEENLTQVGSILGNLKNMALDMGNEIDAQNQQIQKITEKADTNKNRIDIANTRAKKLIDS
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Essential component of the high affinity receptor for the general membrane fusion machinery and an important regulator of transport vesicle docking and fusion.
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O09046
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OXLA_MOUSE
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L-amino-acid oxidase (LAAO) (LAO) (EC 1.4.3.2) (EC 1.4.3.25) (Interleukin-4-induced protein 1) (IL4-induced protein 1) (mIL4I1) (Protein Fig-1) (mFIG1)
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MAGLALRLVLAATLLGLAGSLDWKAASSLNPIEKCMEDHDYEQLLKVVTLGLNRTSKPQKVVVVGAGVAGLVAAKMLSDAGHKVTILEADNRIGGRIFTFRDEKTGWIGELGAMRMPSSHRILHKLCRTLGLNLTQFTQYDENTWTEVHNVKLRNYVVEKMPEKLGYNLNNRERGHSPEDIYQMALNKAFKDLKALGCKKAMNKFNKHTLLEYLLEEGNLSRPAVQLLGDVMSEEGFFYLSFAEALRAHACLSDRLRYSRIVGGWDLLPRALLSSLSGALLLNAPVVSITQGRNDVRVHIATSLHSEKTLTADVVLLTASGPALQRITFSPPLTRKRQEALRALHYVAASKVFLSFRRPFWHEEHIEGGHSNTDRPSRLIFYPARGEGSLLLASYTWSDAAAPFAGLSTDQTLRLVLQDVAALHGPVVFRLWDGRGVVKRWAEDPHSQGGFVVQPPLYGREAEDYDWSAPFGRIYFAGEHTALPHGWVETAVKSGLRAAVRINNNYGYGEVDPQMMEHAYAEANYLDQYPEGERPEEQQAREEVSPDEQEPSHKHLLVETSPEGQQHAFVEAIPELQGHVFVETVPQEKGHAHQNIYPSEHVQVHGEVIPEWHGHGGSGTPQMHRVGDHS
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Secreted L-amino-acid oxidase that acts as a key immunoregulator. Has preference for L-aromatic amino acids: converts phenylalanine (Phe), tyrosine (Tyr) and tryptophan (Trp) to phenylpyruvic acid (PP), hydroxyphenylpyruvic acid (HPP), and indole-3-pyruvic acid (I3P), respectively. Also has weak L-arginine oxidase activity (By similarity). Acts as a negative regulator of anti-tumor immunity by mediating Trp degradation via an indole pyruvate pathway that activates the transcription factor AHR. IL4I1-mediated Trp catabolism generates I3P, giving rise to indole metabolites (indole-3-acetic acid (IAA) and indole-3-aldehyde (I3A)) and kynurenic acid, which act as ligands for AHR, a ligand-activated transcription factor that plays important roles in immunity and cancer (By similarity). AHR activation by indoles following IL4I1-mediated Trp degradation enhances tumor progression by promoting cancer cell motility and suppressing adaptive immunity. Also has an immunoregulatory function in some immune cell, probably by mediating Trp degradation and promoting downstream AHR activation: inhibits T-cell activation and proliferation, promotes the differentiation of naive CD4(+) T-cells into FOXP3(+) regulatory T-cells (Treg) and regulates the development and function of B-cells. Also regulates M2 macrophage polarization by inhibiting T-cell activation. Also has antibacterial properties by inhibiting growth of Gram negative and Gram positive bacteria through the production of NH4(+) and H2O2 (By similarity).
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O09047
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C3AR_MOUSE
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C3a anaphylatoxin chemotactic receptor (C3AR) (C3a-R) (Complement component 3a receptor 1)
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MESFDADTNSTDLHSRPLFQPQDIASMVILGLTCLLGLLGNGLVLWVAGVKMKTTVNTVWFLHLTLADFLCCLSLPFSLAHLILQGHWPYGLFLCKLIPSIIILNMFASVFLLTAISLDRCLIVHKPIWCQNHRNVRTAFAICGCVWVVAFVMCVPVFVYRDLFIMDNRSICRYNFDSSRSYDYWDYVYKLSLPESNSTDNSTAQLTGHMNDRSAPSSVQARDYFWTVTTALQSQPFLTSPEDSFSLDSANQQPHYGGKPPNVLTAAVPSGFPVEDRKSNTLNADAFLSAHTELFPTASSGHLYPYDFQGDYVDQFTYDNHVPTPLMAITITRLVVGFLVPFFIMVICYSLIVFRMRKTNFTKSRNKTFRVAVAVVTVFFICWTPYHLVGVLLLITDPESSLGEAVMSWDHMSIALASANSCFNPFLYALLGKDFRKKARQSIKGILEAAFSEELTHSTNCTQDKASSKRNNMSTDV
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Receptor for the chemotactic and inflammatory peptide anaphylatoxin C3a. This receptor stimulates chemotaxis, granule enzyme release and superoxide anion production.
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O09049
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REG3G_MOUSE
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Regenerating islet-derived protein 3-gamma (REG-3-gamma) (Pancreatitis-associated protein 3) (Regenerating islet-derived protein III-gamma) (Reg III-gamma) [Cleaved into: Regenerating islet-derived protein 3-gamma 16.5 kDa form; Regenerating islet-derived protein 3-gamma 15 kDa form]
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MLPRITITIMSWMLLSCLMLLSQVQGEVAKKDAPSSRSSCPKGSRAYGSYCYALFSVSKNWYDADMACQKRPSGHLVSVLSGAEASFLSSMIKSSGNSGQYVWIGLHDPTLGYEPNRGGWEWSNADVMNYINWETNPSSSSGNHCGTLSRASGFLKWRENYCNLELPYVCKFKA
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Bactericidal C-type lectin which acts exclusively against Gram-positive bacteria and mediates bacterial killing by binding to surface-exposed carbohydrate moieties of peptidoglycan. Restricts bacterial colonization of the intestinal epithelial surface and consequently limits activation of adaptive immune responses by the microbiota. Acts as a hormone in response to different stimuli like anti-inflammatory signals, such as IL17A, or gut microbiome. Is secreted by different cell types to activate its receptor EXTL3 and induce cell specific signaling pathways. Induced by IL17A in keratinocytes, regulates keratinocyte proliferation and differentiation after skin injury. In parallel, inhibits skin inflammation through the inhibition of inflammatory cytokines such as IL6 and TNF. Induced by IL22 in lung epithelial cells, inhibits cytokine production and regulates allergic airway inflammation. Induced in small intestine by inulin-enriched diet and Lactobacillus gasseri enriched microbiome, plays a role in the improvement of gut barrier function, the regulation of energy balance and glucose levels. Modulates microbiota composition in duodenal contents. Produced by nociceptor in response to endotoxins, prevents endotoxic death by targeting kynurenine pathway in microglia.
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O09051
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GUC2B_MOUSE
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Guanylate cyclase activator 2B [Cleaved into: Uroguanylin (UGN)]
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MSRSQLWAAVVLLLLLQSAQGVYIKYHGFQVQLESVKKLNELEEKEMSNPQPRRSGLLPAVCHNPALPLDLQPVCASQEAASTFKALRTIATDECELCINVACTGC
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Endogenous activator of intestinal guanylate cyclase. It stimulates this enzyme through the same receptor binding region as the heat-stable enterotoxins. May be a potent physiological regulator of intestinal fluid and electrolyte transport. May be an autocrine/paracrine regulator of intestinal salt and water transport (By similarity).
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O09053
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WRN_MOUSE
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Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN (Werner syndrome protein homolog) [Includes: 3'-5' exonuclease (EC 3.1.-.-); ATP-dependent helicase (EC 3.6.4.12)]
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METTSLQRKFPEWMSMQSQRCATEEKACVQKSVLEDNLPFLEFPGSIVYSYEASDCSFLSEDISMRLSDGDVVGFDMEWPPIYKPGKRSRVAVIQLCVSESKCYLFHISSMSVFPQGLKMLLENKSIKKAGVGIEGDQWKLLRDFDVKLESFVELTDVANEKLKCAETWSLNGLVKHVLGKQLLKDKSIRCSNWSNFPLTEDQKLYAATDAYAGLIIYQKLGNLGDTAQVFALNKAEENLPLEMKKQLNSISEEMRDLANRFPVTCRNLETLQRVPVILKSISENLCSLRKVICGPTNTETRLKPGSSFNLLSSEDSAAAGEKEKQIGKHSTFAKIKEEPWDPELDSLVKQEEVDVFRNQVKQEKGESENEIEDNLLREDMERTCVIPSISENELQDLEQQAKEEKYNDVSHQLSEHLSPNDDENDSSYIIESDEDLEMEMLKSLENLNSDVVEPTHSTWLEMGTNGRLPPEEEDGHGNEAIKEEQEEEDHLLPEPNAKQINCLKTYFGHSSFKPVQWKVIHSVLEERRDNVVVMATGYGKSLCFQYPPVYTGKIGIVISPLISLMEDQVLQLELSNVPACLLGSAQSKNILGDVKLGKYRVIYITPEFCSGNLDLLQQLDSSIGITLIAVDEAHCISEWGHDFRSSFRMLGSLKTALPLVPVIALSATASSSIREDIISCLNLKDPQITCTGFDRPNLYLEVGRKTGNILQDLKPFLVRKASSAWEFEGPTIIYCPSRKMTEQVTAELGKLNLACRTYHAGMKISERKDVHHRFLRDEIQCVVATVAFGMGINKADIRKVIHYGAPKEMESYYQEIGRAGRDGLQSSCHLLWAPADFNTSRNLLIEIHDEKFRLYKLKMMVKMEKYLHSSQCRRRIILSHFEDKCLQKASLDIMGTEKCCDNCRPRLNHCLTANNSEDASQDFGPQAFQLLSAVDILQEKFGIGIPILFLRGSNSQRLPDKYRGHRLFGAGKEQAESWWKTLSHHLIAEGFLVEVPKENKYIKTCSLTKKGRKWLGEASSQSPPSLLLQANEEMFPRKVLLPSSNPVSPETTQHSSNQNPAGLTTKQSNLERTHSYKVPEKVSSGTNIPKKSAVMPSPGTSSSPLEPAISAQELDARTGLYARLVEARQKHANKMDVPPAILATNKVLLDMAKMRPTTVENMKQIDGVSEGKAALLAPLLEVIKHFCQVTSVQTDLLSSAKPHKEQEKSQEMEKKDCSLPQSVAVTYTLFQEKKMPLHSIAENRLLPLTAAGMHLAQAVKAGYPLDMERAGLTPETWKIIMDVIRNPPINSDMYKVKLIRMLVPENLDTYLIHMAIEILQSGSDSRTQPPCDSSRKRRFPSSAESCESCKESKEAVTETKASSSESKRKLPEWFAKGNVPSADTGSSSSMAKTKKKGLFS
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Multifunctional enzyme that has both magnesium and ATP-dependent DNA-helicase activity and 3'->5' exonuclease activity towards double-stranded DNA with a 5'-overhang. Has no nuclease activity towards single-stranded DNA or blunt-ended double-stranded DNA. Binds preferentially to DNA substrates containing alternate secondary structures, such as replication forks and Holliday junctions. May play an important role in the dissociation of joint DNA molecules that can arise as products of homologous recombination, at stalled replication forks or during DNA repair. Alleviates stalling of DNA polymerases at the site of DNA lesions. Important for genomic integrity. Plays a role in the formation of DNA replication focal centers stably associates with foci elements generating binding sites for RP-A (By similarity). Plays a role in double-strand break repair after gamma-irradiation (By similarity). {ECO:0000250, ECO:0000269|PubMed:10757812, ECO:0000269|PubMed:17229737}.
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O09061
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PSB1_MOUSE
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Proteasome subunit beta type-1 (Macropain subunit C5) (Multicatalytic endopeptidase complex subunit C5) (Proteasome component C5) (Proteasome gamma chain)
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MLSTAAYRDVERELGMGPHGSAGPVQLRFSPYAFNGGTVLAIAGEDFSIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLTLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVPLRKD
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Non-catalytic component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex).
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O09100
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GATA2_MOUSE
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Endothelial transcription factor GATA-2 (GATA-binding protein 2)
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MEVAPEQPRWMAHPAVLNAQHPDSHHPGLAHNYMEPAQLLPPDEVDVFFNHLDSQGNPYYANPAHARARVSYSPAHARLTGGQMCRPHLLHSPGLPWLDGGKAALSAAAAHHHSPWTVSPFSKTPLHPSAAGAPGGPLSVYPGAAGGSGGGSGSSVASLTPTAAHSGSHLFGFPPTPPKEVSPDPSTTGAASPASSSAGGSVARGEDKDGVKYQVSLSESMKMEGGSPLRPGLATMGTQPATHHPIPTYPSYVPAAAHDYGSSLFHPGGFLGGPASSFTPKQRSKARSCSEGRECVNCGATATPLWRRDGTGHYLCNACGLYHKMNGQNRPLIKPKRRLSAARRAGTCCANCQTTTTTLWRRNANGDPVCNACGLYYKLHNVNRPLTMKKEGIQTRNRKMSSKSKKSKKGAECFEELSKCMQEKSPPFSAAALAGHMAPVGHLPPFSHSGHILPTPTPIHPSSSLSFGHPHPSSMVTAMG
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Transcriptional activator which regulates endothelin-1 gene expression in endothelial cells. Binds to the consensus sequence 5'-AGATAG-3'.
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O09102
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GCM2_MOUSE
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Chorion-specific transcription factor GCMb (mGCMb) (GCM motif protein 2) (Glial cells missing homolog 2)
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MPADSTQDEDAVLSYGMKLTWDINDPQMPQEPTHFDHFREWPDGYVRFIYSSQEKKAQRHLSGWAMRNTNNHNGHILKKSCLGVVVCARACALKDGSHLQLRPAICDKARLKQQKKACPNCHSPLELVPCRGHSGYPVTNFWRLDGNAIFFQAKGVHDHPRPESKSETEGRRSALKRQMASFYQPQKRRSEEPEARSTQDIRGHLNSTAALEPTELFDMTADTSFPIPGQPSPSFPNSDVHRVTCDLPTFQGDIILPFQKYPNPSIYFPGPPWGYELASSGVTGSSPYSTLYKDSSVVPDDPDWIPLNSLQYNVSSYGSYERTLDFTARYHSWKPTHGKPSLEEKVDCEQCQAVPTSPYYNLELPCRYLPVPAAGTQALQTVITTTVAYQAYQHPALKHSDSMQEVSSLASCTYASENLPMPIYPPALDPQEGVIQAASPSGRAPLKVPGDCQAPRPTLDFPQEADPSGTDGADVWDVCLSGVGSVMGYLDRTGQPFSFDNEDF
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Transcription factor that binds specific sequences on gene promoters and activate their transcription. Through the regulation of gene transcription, may play a role in parathyroid gland development.
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O09105
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NDF4_MOUSE
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Neurogenic differentiation factor 4 (NeuroD4) (Helix-loop-helix protein mATH-3) (mATH3) (Protein atonal homolog 3)
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MAKMYMKSKDMVELVNTQSWMDKGLSSQNEMKEQERRPGSYGMLGTLTEEHDSIEEDEEEEEDGDKPKRRGPKKKKMTKARLERFRARRVKANARERTRMHGLNDALDNLRRVMPCYSKTQKLSKIETLRLARNYIWALSEVLETGQTLEGKGFVEMLCKGLSQPTSNLVAGCLQLGPQSTLLEKHEEKSSICDSTISVHSFNYQSPGLPSPPYGHMETHSLHLKPQPFKSLGDSFGSHPPDCSTPPYEGPLTPPLSISGNFSLKQDGSPDLEKSYNFMPHYTSASLSSGHVHSTPFQTGTPRYDVPVDLSYDSYSHHSIGTQLNTIFSD
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Probably acts as a transcriptional activator. Mediates neuronal differentiation. Required for the regulation of amacrine cell fate specification in the retina.
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O09106
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HDAC1_MOUSE
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Histone deacetylase 1 (HD1) (EC 3.5.1.98) (Protein deacetylase HDAC1) (EC 3.5.1.-) (Protein decrotonylase HDAC1) (EC 3.5.1.-)
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MAQTQGTKRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEEDPDKRISICSSDKRIACEEEFSDSDEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA
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Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (By similarity). Also functions as deacetylase for non-histone targets, such as NR1D2, RELA, SP1, SP3 and TSHZ3 (By similarity). Deacetylates SP proteins, SP1 and SP3, and regulates their function (By similarity). Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-mediated transcription in resting neurons (By similarity). Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation (By similarity). Deacetylates TSHZ3 and regulates its transcriptional repressor activity (By similarity). Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B (By similarity). Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression activity (By similarity). Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator: CLOCK-BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex or CRY1 through histone deacetylation. In addition to protein deacetylase activity, also has protein-lysine deacylase activity: acts as a protein decrotonylase by mediating decrotonylation ((2E)-butenoyl) of histones.
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O09107
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INSL3_MOUSE
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Insulin-like 3 (Leydig insulin-like peptide) (Ley-I-L) (Relaxin-like factor) [Cleaved into: Insulin-like 3 B chain; Insulin-like 3 A chain]
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MRAPLLLMLLALGSALRSPQPPEARAKLCGHHLVRTLVRVCGGPRWSPEATQPVETRDRELLQWLEQRHLLHALVADVDPALDPQLPRQASQRQRRSAATNAVHRCCLTGCTQQDLLGLCPH
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Seems to play a role in testicular function. May be a trophic hormone with a role in testicular descent in fetal life. Is a ligand for LGR8 receptor (By similarity). {ECO:0000250, ECO:0000269|PubMed:10391220, ECO:0000269|PubMed:11342953}.
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O09110
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MP2K3_MOUSE
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Dual specificity mitogen-activated protein kinase kinase 3 (MAP kinase kinase 3) (MAPKK 3) (EC 2.7.12.2) (MAPK/ERK kinase 3) (MEK 3)
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MESPAASPPASLPQTKGKSKRKKDLRISCVSKPPVSNPTPPRNLDSRTFITIGDRNFEVEADDLVTISELGRGAYGVVEKVRHAQSGTIMAVKRIRATVNTQEQKRLLMDLDINMRTVDCFYTVTFYGALFREGDVWICMELMDTSLDKFYRKVLEKNMKIPEDILGEIAVSIVRALEHLHSKLSVIHRDVKPSNVLINKEGHVKMCDFGISGYLVDSVAKTMDAGCKPYMAPERINPELNQKGYNVKSDVWSLGITMIEMAILRFPYESWGTPFQQLKQVVEEPSPQLPADQFSPEFVDFTSQCLRKNPAERMSYLELMEHPFFTLHKTKKTDIAAFVKEILGEDS
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Dual specificity kinase. Is activated by cytokines and environmental stress in vivo. Catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in the MAP kinase p38. Part of a signaling cascade that begins with the activation of the adrenergic receptor ADRA1B and leads to the activation of MAPK14.
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O09112
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DUS8_MOUSE
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Dual specificity protein phosphatase 8 (EC 3.1.3.16) (EC 3.1.3.48) (Neuronal tyrosine threonine phosphatase 1)
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MAGDRLPRKVMDAKKLASLLRGGPGGPLVIDSRSFVEYNSCHVLSSVNICCSKLVKRRLQQGKVTIAELIQPATRSQVDATEPQDVVVYDQSTRDASVLAADSFLSILLSKLDGCFDSVAILTGGFATFSSCFPGLCEGKPATLPSMSLSQPCLPVPSVGLTRILPHLYLGSQKDVLNKDLMTQNGISYVLNASNSCPKPDFICESRFMRIPINDNYCEKLLPWLDKSIEFIDKAKLSSCQVIVHCLAGISRSATIAIAYIMKTMGMSSDDAYRFVKDRRPSISPNFNFLGQLLEYERSLKLLAALQTDGPHLGTPEPLMGPAAGIPLPRLPPSTSESAATGSEAATAAREGSPSAGGDAPIPSTAPATSALQQGLRGLHLSSDRLQDTNRLKRSFSLDIKSAYAPSRRPDFPGPPDPGEAPKLCKLDSPSGGTLGLPSPSPDSPDSVPECRPRPRRRRPPASSPARSPAHGLGLNFGDTARQTPRHGLSALSAPGLPGPGQPAGPGGWVPPLDSPGTPSPDGPWCFSPEGAQGPGAVFSAFGRVSAGAPGPGNSSSSGGGGGGGGGGGGGGGGGGSSSSNSSSSSSSSSSSSSSSSSSSDLRRRDVRTGWPEEPAADAQFKRRSCQMEFEEGMVEGRARGEELAALGKQTSFSGSVEVIEVS
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Has phosphatase activity with synthetic phosphatase substrates and negatively regulates mitogen-activated protein kinase activity, presumably by catalysing their dephosphorylation. Expected to display protein phosphatase activity toward phosphotyrosine, phosphoserine and phosphothreonine residues (Probable).
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O09113
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OTP_MOUSE
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Homeobox protein orthopedia
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MLSHADLLDARLGMKDAAELLGHREAVKCRLGVGGSDPGGHPGDLAPNSDPVEGATLLPGEDITTVGSTPASLAVSAKDPDKQPGPQGGPNPSQAGQQQGQQKQKRHRTRFTPAQLNELERSFAKTHYPDIFMREELALRIGLTESRVQVWFQNRRAKWKKRKKTTNVFRAPGTLLPTPGLPQFPSAAAAAAAAMGDSLCSFHANDTRWAAAAMPGVSQLPLPPALGRQQAMAQSLSQCSLAAGPPPNSMGLSNSLAGSNGAGLQSHLYQPAFPGMVPASLPGPSNVSGSPQLCSSPDSSDVWRGTSIASLRRKALEHTVSMSFT
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Involved in the specification of hypothalamic neuroendocrine cells. Specifically required for the specification of diencephalic dopaminergic neurons of the A11 group.
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O09114
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PTGDS_MOUSE
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Prostaglandin-H2 D-isomerase (EC 5.3.99.2) (Glutathione-independent PGD synthase) (Lipocalin-type prostaglandin-D synthase) (Prostaglandin-D2 synthase) (L-PGDS) (PGD2 synthase) (PGDS2)
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MAALRMLWMGLVLLGLLGFPQTPAQGHDTVQPNFQQDKFLGRWYSAGLASNSSWFREKKAVLYMCKTVVAPSTEGGLNLTSTFLRKNQCETKIMVLQPAGAPGHYTYSSPHSGSIHSVSVVEANYDEYALLFSRGTKGPGQDFRMATLYSRTQTLKDELKEKFTTFSKAQGLTEEDIVFLPQPDKCIQE
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Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. Binds small non-substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophobic molecules and as a secretory retinoid and thyroid hormone transporter. Possibly involved in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor and blood-testis barrier. It is likely to play important roles in both maturation and maintenance of the central nervous system and male reproductive system. Involved in PLA2G3-dependent maturation of mast cells. PLA2G3 is secreted by immature mast cells and acts on nearby fibroblasts upstream to PTDGS to synthesize PGD2, which in turn promotes mast cell maturation and degranulation via PTGDR.
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O09118
|
NET1_MOUSE
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Netrin-1
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MMRAVWEALAALAAVACLVGAVRGGPGLSMFAGQAAQPDPCSDENGHPRRCIPDFVNAAFGKDVRVSSTCGRPPARYCVVSERGEERLRSCHLCNSSDPKKAHPPAFLTDLNNPHNLTCWQSENYLQFPHNVTLTLSLGKKFEVTYVSLQFCSPRPESMAIYKSMDYGRTWVPFQFYSTQCRKMYNRPHRAPITKQNEQEAVCTDSHTDMRPLSGGLIAFSTLDGRPSAHDFDNSPVLQDWVTATDIRVAFSRLHTFGDENEDDSELARDSYYYAVSDLQVGGRCKCNGHAARCVRDRDDSLVCDCRHNTAGPECDRCKPFHYDRPWQRATAREANECVACNCNLHARRCRFNMELYKLSGRKSGGVCLNCRHNTAGRHCHYCKEGFYRDMGKPITHRKACKACDCHPVGAAGKTCNQTTGQCPCKDGVTGITCNRCAKGYQQSRSPIAPCIKIPVAPPTTAASSVEEPEDCDSYCKASKGKLKMNMKKYCRKDYAVQIHILKADKAGDWWKFTVNIISVYKQGTSRIRRGDQSLWIRSRDIACKCPKIKPLKKYLLLGNAEDSPDQSGIVADKSSLVIQWRDTWARRLRKFQQREKKGKCKKA
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Netrins control guidance of CNS commissural axons and peripheral motor axons. Its association with either DCC or some UNC5 receptors will lead to axon attraction or repulsion, respectively. Binding to UNC5C might cause dissociation of UNC5C from polymerized TUBB3 in microtubules and thereby lead to increased microtubule dynamics and axon repulsion. Involved in dorsal root ganglion axon projection towards the spinal cord. It also serves as a survival factor via its association with its receptors which prevent the initiation of apoptosis. Involved in colorectal tumorigenesis by regulating apoptosis (By similarity).
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O09126
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SEM4D_MOUSE
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Semaphorin-4D (M-Sema G) (Semaphorin-C-like 2) (Semaphorin-J) (Sema J) (CD antigen CD100)
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MRMCAPVRGLFLALVVVLRTAVAFAPVPRLTWEHGEVGLVQFHKPGIFNYSALLMSEDKDTLYVGAREAVFAVNALNISEKQHEVYWKVSEDKKSKCAEKGKSKQTECLNYIRVLQPLSSTSLYVCGTNAFQPTCDHLNLTSFKFLGKSEDGKGRCPFDPAHSYTSVMVGGELYSGTSYNFLGSEPIISRNSSHSPLRTEYAIPWLNEPSFVFADVIQKSPDGPEGEDDKVYFFFTEVSVEYEFVFKLMIPRVARVCKGDQGGLRTLQKKWTSFLKARLICSKPDSGLVFNILQDVFVLRAPGLKEPVFYAVFTPQLNNVGLSAVCAYTLATVEAVFSRGKYMQSATVEQSHTKWVRYNGPVPTPRPGACIDSEARAANYTSSLNLPDKTLQFVKDHPLMDDSVTPIDNRPKLIKKDVNYTQIVVDRTQALDGTFYDVMFISTDRGALHKAVILTKEVHVIEETQLFRDSEPVLTLLLSSKKGRKFVYAGSNSGVVQAPLAFCEKHGSCEDCVLARDPYCAWSPAIKACVTLHQEEASSRGWIQDMSGDTSSCLDKSKESFNQHFFKHGGTAELKCFQKSNLARVVWKFQNGELKAASPKYGFVGRKHLLIFNLSDGDSGVYQCLSEERVRNKTVSQLLAKHVLEVKMVPRTPPSPTSEDAQTEGSKITSKMPVASTQGSSPPTPALWATSPRAATLPPKSSSGTSCEPKMVINTVPQLHSEKTVYLKSSDNRLLMSLLLFIFVLFLCLFSYNCYKGYLPGQCLKFRSALLLGKKTPKSDFSDLEQSVKETLVEPGSFSQQNGDHPKPALDTGYETEQDTITSKVPTDREDSQRIDELSARDKPFDVKCELKFADSDADGD
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Cell surface receptor for PLXNB1 and PLXNB2 that plays an important role in cell-cell signaling (By similarity). Regulates GABAergic synapse development. Promotes the development of inhibitory synapses in a PLXNB1-dependent manner. Modulates the complexity and arborization of developing neurites in hippocampal neurons by activating PLXNB1 and interaction with PLXNB1 mediates activation of RHOA (By similarity). Promotes the migration of cerebellar granule cells. Plays a role in the immune system induces B-cells to aggregate and improves their viability (in vitro) (By similarity). Induces endothelial cell migration through the activation of PTK2B/PYK2, SRC, and the phosphatidylinositol 3-kinase-AKT pathway (By similarity).
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O09127
|
EPHA8_MOUSE
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Ephrin type-A receptor 8 (EC 2.7.10.1) (EPH- and ELK-related kinase) (Tyrosine-protein kinase receptor EEK)
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MAPARARLSPALWVVTAAAAATCVSAGRGEVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFRPIHTYQVCNVMSPNQNNWLRTNWVPRDGARRVYAEIKFTLRDCNSIPGVLGTCKETFNLHYLESDRDLGASTQESQFLKIDTIAADESFTGADLGVRRLKLNTEVRGVGPLSKRGFYLAFQDIGACLAILSLRIYYKKCPAMVRNLAAFSEAVTGADSSSLVEVRGQCVRHSEERDTPKMYCSAEGEWLVPIGKCVCSAGYEERRDACMACELGFYKSAPGDQLCARCPPHSHSATPAAQTCRCDLSYYRAALDPPSAACTRPPSAPVNLISSVNGTSVTLEWAPPLDPGGRSDITYNAVCRRCPWALSHCEACGSGTRFVPQQTSLAQASLLVANLLAHMNYSFWIEAVNGVSNLSPEPRSAAVVNITTNQAAPSQVVVIRQERAGQTSVSLLWQEPEQPNGIILEYEIKYYEKDKEMQSYSTLKAVTTRATVSGLKPGTRYVFQVRARTSAGCGRFSQAMEVETGKPRPRYDTRTIVWICLTLITGLVVLLLLLICKKRHCGYSKAFQDSDEEKMHYQNGQAPPPVFLPLNHPPGKFPETQFSAEPHTYEEPGRAGRSFTREIEASRIHIEKIIGSGESGEVCYGRLQVPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLDALVHSPESLRATATVSRCPPPAFARSCFDLRAGGSGNGDLTVGDWLDSIRMGRYRDHFAAGGYSSLGMVLRMNAQDVRALGITLMGHQKKILGSIQTMRAQLSSTQGPRRHL
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Receptor tyrosine kinase which binds promiscuously GPI-anchored ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. The GPI-anchored ephrin-A EFNA2, EFNA3, and EFNA5 are able to activate EPHA8 through phosphorylation. With EFNA5 may regulate integrin-mediated cell adhesion and migration on fibronectin substrate but also neurite outgrowth. During development of the nervous system also plays a role in axon guidance. Downstream effectors of the EPHA8 signaling pathway include FYN which promotes cell adhesion upon activation by EPHA8 and the MAP kinases in the stimulation of neurite outgrowth.
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O09130
|
NF2IP_MOUSE
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NFATC2-interacting protein (45 kDa NF-AT-interacting protein) (45 kDa NFAT-interacting protein) (Nuclear factor of activated T-cells, cytoplasmic 2-interacting protein)
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MAEPLRGRGPRSRGGRGARRARGARGRCPRARQSPARLIPDTVLVDLVSDSDEEVLEVADPVEVPVARLPAPAKPEQDSDSDSEGAAEGPAGAPRTLVRRRRRRLLDPGEAPVVPVYSGKVQSSLNLIPDNSSLLKLCPSEPEDEADLTNSGSSPSEDDALPSGSPWRKKLRKKCEKEEKKMEEFPDQDISPLPQPSSRNKSRKHTEALQKLREVNKRLQDLRSCLSPKQHQSPALQSTDDEVVLVEGPVLPQSSRLFTLKIRCRADLVRLPVRMSEPLQNVVDHMANHLGVSPNRILLLFGESELSPTATPSTLKLGVADIIDCVVLASSSEATETSQELRLRVQGKEKHQMLEISLSPDSPLKVLMSHYEEAMGLSGHKLSFFFDGTKLSGKELPADLGLESGDLIEVWG
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In T-helper 2 (Th2) cells, regulates the magnitude of NFAT-driven transcription of a specific subset of cytokine genes, including IL3, IL4, IL5 and IL13, but not IL2. Recruits PRMT1 to the IL4 promoter this leads to enhancement of histone H4 'Arg-3'-methylation and facilitates subsequent histone acetylation at the IL4 locus, thus promotes robust cytokine expression. Down-regulates formation of poly-SUMO chains by UBE2I/UBC9.
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