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O54857
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PTEN_RAT
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Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (EC 3.1.3.16) (EC 3.1.3.48) (EC 3.1.3.67) (Phosphatase and tensin homolog)
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MTAIIKEIVSRNKRRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHYKIYNLCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSYLLKNHLDYRPVALLFHKMMFETIPMFSGGTCNPQFVVCQLKVKIYSSNSGPTRREDKLMYFEFPQPLPVCGDIKVEFFHKQNKMLKKDKMFHFWVNTFFIPGPEETSEKVENGSLCDQEIDSICSIERADNDKEYLVLTLTKNDLDKANKDKANRYFSPNFKVKLYFTKTVEEPSNPEASSSTSVTPDVSDNEPDHYRYSDTTDSDPENEPFDEDQHSQITKV
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Acts as a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins. Also acts as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring from phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-diphosphate, phosphatidylinositol 3-phosphate and inositol 1,3,4,5-tetrakisphosphate with order of substrate preference in vitro PtdIns(3,4,5)P3 > PtdIns(3,4)P2 > PtdIns3P > Ins(1,3,4,5)P4. Tumor suppressor, the lipid phosphatase activity is critical for its tumor suppressor function. Antagonizes the PI3K-AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thereby modulating cell cycle progression and cell survival. The unphosphorylated form cooperates with MAGI2 to suppress AKT1 activation. In motile cells, suppresses the formation of lateral pseudopods and thereby promotes cell polarization and directed movement (By similarity). Dephosphorylates tyrosine-phosphorylated focal adhesion kinase and inhibits cell migration and integrin-mediated cell spreading and focal adhesion formation. Required for growth factor-induced epithelial cell migration growth factor stimulation induces PTEN phosphorylation which changes its binding preference from the p85 regulatory subunit of the PI3K kinase complex to DLC1 and results in translocation of the PTEN-DLC1 complex to the posterior of migrating cells to promote RHOA activation (By similarity). Meanwhile, TNS3 switches binding preference from DLC1 to p85 and the TNS3-p85 complex translocates to the leading edge of migrating cells to activate RAC1 activation (By similarity). Plays a role as a key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation (By similarity). Involved in the regulation of synaptic function in excitatory hippocampal synapses. Recruited to the postsynaptic membrane upon NMDA receptor activation, is required for the modulation of synaptic activity during plasticity. Enhancement of lipid phosphatase activity is able to drive depression of AMPA receptor-mediated synaptic responses, activity required for NMDA receptor-dependent long-term depression (LTD) (Ref.7). May be a negative regulator of insulin signaling and glucose metabolism in adipose tissue. The nuclear monoubiquitinated form possesses greater apoptotic potential, whereas the cytoplasmic nonubiquitinated form induces less tumor suppressive ability (By similarity).
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O54861
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SORT_RAT
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Sortilin (Glycoprotein 110) (Gp110) (Neurotensin receptor 3) (NTR3)
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MERPRGAADGLLRWPLGLLLLLQLLPPAAVGQDRLDAPPPPAPPLLRWAGPVGVSWGLRAAAPGGPVPRAGRWRRGAPAEDQDCGRLPDFIAKLTNNTHQHVFDDLSGSVSLSWVGDSTGVILVLTTFQVPLVIVSFGQSKLYRSEDYGKNFKDITNLINNTFIRTEFGMAIGPENSGKVILTAEVSGGSRGGRVFRSSDFAKNFVQTDLPFHPLTQMMYSPQNSDYLLALSTENGLWVSKNFGEKWEEIHKAVCLAKWGPNNIIFFTTHVNGSCKADLGALELWRTSDLGKTFKTIGVKIYSFGLGGRFLFASVMADKDTTRRIHVSTDQGDTWSMAQLPSVGQEQFYSILAANDDMVFMHVDEPGDTGFGTIFTSDDRGIVYSKSLDRHLYTTTGGETDFTNVTSLRGVYITSTLSEDNSIQSMITFDQGGRWEHLQKPENSKCDATAKNKNECSLHIHASYSISQKLNVPMAPLSEPNAVGIVIAHGSVGDAISVMVPDVYISDDGGYSWAKMLEGPHYYTILDSGGIIVAIEHSNRPINVIKFSTDEGQCWQSYVFSQEPVYFTGLASEPGARSMNISIWGFTESFLTRQWVSYTIDFKDILERNCEENDYTTWLAHSTDPGDYKDGCILGYKEQFLRLRKSSVCQNGRDYVVAKQPSICPCSLEDFLCDFGYFRPENASECVEQPELKGHELEFCLYGKEEHLTTNGYRKIPGDRCQGGMNPAREVKDLKKKCTSNFLNPKKQNSKSSSVPIILAIVGLMLVTVVAGVLIVKKYVCGGRFLVHRYSVLQQHAEADGVEALDTASHAKSGYHDDSDEDLLE
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Functions as a sorting receptor in the Golgi compartment and as a clearance receptor on the cell surface. Required for protein transport from the Golgi apparatus to the lysosomes by a pathway that is independent of the mannose-6-phosphate receptor (M6PR). Lysosomal proteins bind specifically to the receptor in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelysosomal compartment where the low pH mediates the dissociation of the complex. The receptor is then recycled back to the Golgi for another round of trafficking through its binding to the retromer. Also required for protein transport from the Golgi apparatus to the endosomes. Promotes neuronal apoptosis by mediating endocytosis of the proapoptotic precursor forms of BDNF (proBDNF) and NGFB (proNGFB). Also acts as a receptor for neurotensin. May promote mineralization of the extracellular matrix during osteogenic differentiation by scavenging extracellular LPL. Probably required in adipocytes for the formation of specialized storage vesicles containing the glucose transporter SLC2A4/GLUT4 (GLUT4 storage vesicles, or GSVs). These vesicles provide a stable pool of SLC2A4 and confer increased responsiveness to insulin (By similarity). May also mediate transport from the endoplasmic reticulum to the Golgi.
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O54862
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MBTP2_CRIGR
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Membrane-bound transcription factor site-2 protease (EC 3.4.24.85) (Endopeptidase S2P) (Sterol regulatory element-binding proteins intramembrane protease) (SREBPs intramembrane protease)
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MIPVSLVVVVVGGWTAVYLADLVLKSSVYFKHSYEDWLEKNGLSISPFHIRWQTSVFNRAFYSWGRRKARMLYQWFNFGMVFGVIAMFSSFFLLGKTLMQTLAQMMADSPSSSSSSSSSSSSSSSSSIHNEQVLQVVVPGINLPVNQLTYFFAAVLISGVVHEIGHGIAAIREQVRFNGFGIFLFIIYPGAFVDLFTTHLQLISPVQQLRIFCAGIWHNFVLALLGILALVLLPVILLPFYYTGVGVLITEVAEDSPAIGPRGLFVGDLVTHLQDCPVTNVQDWNECLDTIAYEPQIGYCISASTLQQLSFPVRAYKRLDGSTECCNNHSLTDVCFSYRNNFNKRLHTCLPARKAVEATQVCRTNKDCKTSSSSSFCIVPSLETHTRLIKVKHPPQIDMLYVGHPLHLHYTVSITSFIPRFNFLSIDLPVIVETFVKYLISLSGALAIVNAVPCFALDGQWILNSFLDATLTSVIGDNDVKDLIGFFILLGGSVLLAANVTLGLWMVTAR
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Zinc metalloprotease that mediates intramembrane proteolysis of proteins such as ATF6, ATF6B, SREBF1/SREBP1 and SREBF2/SREBP2. Catalyzes the second step in the proteolytic activation of the sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2: cleaves SREBPs within the first transmembrane segment, thereby releasing the N-terminal segment with a portion of the transmembrane segment attached. Mature N-terminal SREBP fragments shuttle to the nucleus and activate gene transcription. Also mediates the second step in the proteolytic activation of the cyclic AMP-dependent transcription factor ATF-6 (ATF6 and ATF6B). Involved in intramembrane proteolysis during bone formation. In astrocytes and osteoblasts, upon DNA damage and ER stress, mediates the second step of the regulated intramembrane proteolytic activation of the transcription factor CREB3L1, leading to the inhibition of cell-cycle progression.
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O54863
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TSSK2_MOUSE
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Testis-specific serine/threonine-protein kinase 2 (TSK-2) (TSK2) (TSSK-2) (Testis-specific kinase 2) (EC 2.7.11.1) (Serine/threonine-protein kinase 22B)
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MDDAAVLRKKGYIVGINLGKGSYAKVKSAYSERLKFNVAVKIIDRKKTPTDFVERFLPREMDILATVNHRSIIKTYEIFETSDGRIYIVMELGVQGDLLEFIKCRGALHEDVARKMFRQLSSAVKYCHDLDVVHRDLKCENLLLDKDFNIKLSDFGFSKRCLRDGSGRIVLSKTFCGSAAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSDIKKMLRIQKEHRVDFPRSKNLTGECKDLIYRILQPDVNRRLHIDEILSHSWLQPPKPKAMSSASFKREGEGKYRADCKLDTRPGSRPEHRPDHKLATKPQQRMLVTPENEDRMEDRLAETSRAKDHHISGAEVEKAST
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Testis-specific serine/threonine-protein kinase required during spermatid development. Phosphorylates 'Ser-281' of TSKS and SPAG16. Involved in the late stages of spermatogenesis, during the reconstruction of the cytoplasm. During spermatogenesis, required for the transformation of a ring-shaped structure around the base of the flagellum originating from the chromatoid body.
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O54864
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SUV91_MOUSE
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Histone-lysine N-methyltransferase SUV39H1 (EC 2.1.1.355) (Histone H3-K9 methyltransferase 1) (H3-K9-HMTase 1) (Position-effect variegation 3-9 homolog) (Suppressor of variegation 3-9 homolog 1) (Su(var)3-9 homolog 1)
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MAENLKGCSVCCKSSWNQLQDLCRLAKLSCPALGVSKKNLYDFEVEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNLKCIRVLKQFHKDLERELVRRHRRSKPPRHLDPNLANYLVQKAKQRRALQRWEQELNAKRSHLGRITVENEVDLDGPPRSFVYINEYRVGEGITLNQVAVGCECQDCLLAPTGGCCPGASLHKFAYNDQGQVRLKAGQPIYECNSRCCCGYDCPNRVVQKGIRYDLCIFRTNDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDVYTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIWAGEELTFDYNMQVDPVDMESTRMDSNFGLAGLPGSPKKRVRIECKCGTTACRKYLF
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Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as repression of MYOD1-stimulated differentiation, regulation of the control switch for exiting the cell cycle and entering differentiation, repression by the PML-RARA fusion protein, BMP-induced repression, repression of switch recombination to IgA and regulation of telomere length. Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. Recruited by the PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation.
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O54865
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GCYB1_MOUSE
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Guanylate cyclase soluble subunit beta-1 (GCS-beta-1) (EC 4.6.1.2) (Guanylate cyclase soluble subunit beta-3) (GCS-beta-3) (Soluble guanylate cyclase small subunit)
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MYGFVNHALELLVIRNYGPEVWEDIKKEAQLDEEGQFLVRIIYDDSKTYDLVAAASKVLNLNAGEILQMFGKMFFVFCQESGYDTILRVLGSNVREFLQNLDALHDHLATIYPGMRAPSFRCTDAEKGKGLILHYYSEREGLQDIVIGIIKTVAQQIHGTEIDMKVIQQRNEECDHTQFLIEEKESKEEDFYEDLDRFEENGTQESRISPYTFCKAFPFHIIFDRNLVVTQCGNAIYRVLPQLQPGNCSLLSVFSLVRPHIDISFHGILSHINTVFVLRSKEGLLDVEKLECEDELTGAEISCLRLKGQMIYLPEADSILFLCSPSVMNLDDLTRRGLYLSDIPLHDATRDLVLLGEQFREEYKLTQELEILTDRLQLTLRALEDEKKKTDTLLYSVLPPSVANELRHKRPVPAKRYDNVTILFSGIVGFNAFCSKHASGEGAMKIVNLLNDLYTRFDTLTDSRKNPFVYKVETVGDKYMTVSGLPEPCIHHARSICHLALDMMEIAGQVQVDGESVQITIGIHTGEVVTGVIGQRMPRYCLFGNTVNLTSRTETTGEKGKINVSEYTYRCLMSPENSDPLFHLEHRGPVSMKGKKEPMQVWFLSRKNTGTEETNEEDEN
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Mediates responses to nitric oxide (NO) by catalyzing the biosynthesis of the signaling molecule cGMP.
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O54874
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MRCKA_RAT
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Serine/threonine-protein kinase MRCK alpha (EC 2.7.11.1) (CDC42-binding protein kinase alpha) (Myotonic dystrophy kinase-related CDC42-binding kinase alpha) (MRCK alpha) (Myotonic dystrophy protein kinase-like alpha)
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MSGEVRLRQLEQFILDGPAQTNGQCFSVETLLDILICLYDECNNSPLRREKNILEYLEWAKPFTSKVKQMRLHREDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETACFREERDVLVNGDSKWITTLHYAFQDDNNLYLVMDYYVGGDLLTLLSKFEDRLPEEMARFYLAEMVIAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSCLKLMEDGTVQSSVAVGTPDYISPEILQAMEDGKGRYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKERFQFPTQVTDVSENAKDLIRRLICSREHRLGQNGIEDFKKHPFFSGIDWDNIRNCEAPYIPEVSSPTDTSNFDVDDDCLKNSETMPPPTHTAFSGHHLPFVGFTYTSSCVLSDRSCLRVTAGPTSLDLDVNVQRTLDNNLATEAYERRIKRLEQEKLELTRKLQESTQTVQALQYSTVDGPLTASKDLEIKSLKEEIEKLRKQVAEVNHLEQQLEEANSVRRELDDAFRQIKAFEKQIKTLQQEREELNKELVQASERLKNQSKELKDAHCQRKLAMQEFMEINERLTELHTQKQKLARHVRDKEEEVDLVMQKAESLRQELRRAERAKKELEVHTEALIAEASKDRKLREQSRHYSKQLENELEGLKQKQISYSPGICSIEHQQEITKLKTDLEKKSIFYEEEISKREGIHASEIKNLKKELHDSEGQQLALNKEIMVLKDKLEKTRRESQSEREEFENEFKQQYEREKVLLTEENKKLTSELDKLTSLYESLSLRNQHLEEEVKDLADKKESVAHWEAQITEIIQWVSDEKDARGYLQALASKMTEELEALRNSSLGTRATDMPWKMRRFAKLDMSARLELQSALDAEIRAKQAIQEELNKVKASNIITECKLKDSEKKNLELLSEIEQLIKDTEELRSEKGVEHRDSQHSFLAFLNTPTDALDQFERSPSCTPAGKGRRIADSAPLPVHTPTLRKKGCPASAGFPPKRKTHQFFVKSFTAPTKCHQCTSLMVGLIRQGCSCEVCGFSCHITCVNKAPTTCPVPPEQTKGPLGIDPQKGVGTAYEGHVRIPKPAGVKKGWQRALAVVCDFKLFLYDIAEGKASQPSSVISQVIDMRDEEFSVSSVLASDVIHASRKDIPCIFRVTASQLSAPSDKCSILMLADSETERSKWVGVLSELHKVLKKNKFRDRSVYVPKEAYDSTLPLIKTTQAAAIIDHERVALGNEEGLFVVHVTKDEIIRVGDNKKIHQIELIPSDQLVAVISGRNRHVRLFPMSALDGRETDFYKLAETKGCQTIAAGKVRHGALSCLCVAMKRQVLCYELFQSKTRHRKFKEIQVPCNVQWMAIFSEHLCVGFQSGFLRYPLNGEGSPCNMLHSNDHTLAFITHQPMDAICAVEISNKEYLLCFSSIGIYTDCQGRRSRQQELMWPANPSSCCYNAPYLSIYSENAVDIFDVNSMEWIQTLPLKKVRPLNTEGSLNLLGLETIRLIYFKNKMAEGDELVVPETSDNSRKQMVRNINNKRRYSFRVPEEERMQQRREMLRDPEMRNKLISNPTNFNHIAHMGPGDGIQILKDLPMNPRPQESRTVFSGSVSIPSITKSRPEPGRSMSASSGLSARSSAQNGSALKREFSGGSYNTKRQPMPSPSEGSLSSGGVDQGSDAPVRDYDGEDSDSPRHSTASNSSNLSSPPSPVSPRKTKSLSLESTDRGSWDP
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Serine/threonine-protein kinase which is an important downstream effector of CDC42 and plays a role in the regulation of cytoskeleton reorganization and cell migration. Regulates actin cytoskeletal reorganization via phosphorylation of PPP1R12A and MYL9/MLC2. In concert with MYO18A and LURAP1, is involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration. Phosphorylates: PPP1R12C, LIMK1 and LIMK2. May play a role in TFRC-mediated iron uptake. In concert with FAM89B/LRAP25 mediates the targeting of LIMK1 to the lamellipodium resulting in its activation and subsequent phosphorylation of CFL1 which is important for lamellipodial F-actin regulation (By similarity). Triggers the formation of an extrusion apical actin ring required for epithelial extrusion of apoptotic cells (By similarity).
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O54879
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HMGB3_MOUSE
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High mobility group protein B3 (High mobility group protein 2a) (HMG-2a) (High mobility group protein 4) (HMG-4)
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MAKGDPKKPKGKMSAYAFFVQTCREEHKKKNPEVPVNFAEFSKKCSERWKTMSSKEKSKFDEMAKADKVRYDREMKDYGPAKGGKKKKDPNAPKRPPSGFFLFCSEFRPKIKSTNPGISIGDVAKKLGEMWNNLSDNEKQPYVTKAAKLKEKYEKDVADYKSKGKFDGAKGPAKVARKKVEEEEEEEEEEEEEEEEEEDE
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Multifunctional protein with various roles in different cellular compartments. May act in a redox sensitive manner. Associates with chromatin and binds DNA with a preference for non-canonical DNA structures such as single-stranded DNA. Can bend DNA and enhance DNA flexibility by looping thus providing a mechanism to promote activities on various gene promoters (By similarity). Proposed to be involved in the innate immune response to nucleic acids by acting as a cytoplasmic promiscuous immunogenic DNA/RNA sensor. Negatively regulates B-cell and myeloid cell differentiation. In hematopoietic stem cells may regulate the balance between self-renewal and differentiation. Involved in negative regulation of canonical Wnt signaling.
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O54880
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RPH3L_RAT
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Rab effector Noc2 (No C2 domains protein) (Rabphilin-3A-like protein)
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MADTIFSSGNDQWVCPNDRQLALRAKLQTGWSVHTYQTEKQRRTQCLSPGEVEVILQVIQRAERLDILEQQRIGRLVERLETMQKNVMGNGVSQCLLCGEMLGFLGSSSVFCKDCRKKVCTKCGIEASPGQKRPLWLCKICSEQREVWKRSGAWFYKGLPKYILPLKTPGRADDPHFRPLPVEPTEPQPQSAEVSRVYTWARGRVVSSDSDSDSDLSSSSLEDRPMPSGIKGTKYDKPRGDSGGSMESPRMGPARPPSHLSGSQSSLGSETGAGATDPQGGTLPRPEPRVSGKRHTWATTHY
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Rab GTPase effector involved in the late steps of regulated exocytosis, both in endocrine and exocrine cells. Regulates the exocytosis of dense-core vesicles in neuroendocrine cells through interaction with RAB27A. Acts as a potential RAB3B effector protein in epithelial cells.
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O54885
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TYOBP_MOUSE
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TYRO protein tyrosine kinase-binding protein (DNAX-activation protein 12) (Killer-activating receptor-associated protein) (KAR-associated protein)
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MGALEPSWCLLFLPVLLTVGGLSPVQAQSDTFPRCDCSSVSPGVLAGIVLGDLVLTLLIALAVYSLGRLVSRGQGTAEGTRKQHIAETESPYQELQGQRPEVYSDLNTQRQYYR
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Adapter protein which non-covalently associates with activating receptors found on the surface of a variety of immune cells to mediate signaling and cell activation following ligand binding by the receptors. TYROBP is tyrosine-phosphorylated in the ITAM domain following ligand binding by the associated receptors which leads to activation of additional tyrosine kinases and subsequent cell activation. Also has an inhibitory role in some cells. Non-covalently associates with activating receptors of the CD300 family to mediate cell activation (By similarity). Also mediates cell activation through association with activating receptors of the CD200R family. Required for neutrophil activation mediated by integrin. Required for the activation of myeloid cells mediated by the CLEC5A/MDL1 receptor (By similarity). Associates with natural killer (NK) cell receptors such as the KLRD1/KLRC2 heterodimer to mediate NK cell activation (By similarity). Also associates non-covalently with the NK cell receptors KLRA4/LY49D and KLRA8/LY49H which leads to NK cell activation. Associates with TREM1 to mediate activation of neutrophils and monocytes (By similarity). Associates with TREM2 on monocyte-derived dendritic cells to mediate up-regulation of chemokine receptor CCR7 and dendritic cell maturation and survival (By similarity). Association with TREM2 mediates cytokine-induced formation of multinucleated giant cells which are formed by the fusion of macrophages. Stabilizes the TREM2 C-terminal fragment (TREM2-CTF) which is produced by TREM2 ectodomain shedding (By similarity). In microglia, required with TREM2 for phagocytosis of apoptotic neurons. Required with ITGAM/CD11B in microglia to control production of microglial superoxide ions which promote the neuronal apoptosis that occurs during brain development. Promotes pro-inflammatory responses in microglia following nerve injury which accelerates degeneration of injured neurons. Positively regulates the expression of the IRAK3/IRAK-M kinase and IL10 production by liver dendritic cells and inhibits their T cell allostimulatory ability. Negatively regulates B cell proliferation. Required for CSF1-mediated osteoclast cytoskeletal organization. Positively regulates multinucleation during osteoclast development.
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O54889
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RPA1_RAT
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DNA-directed RNA polymerase I subunit RPA1 (RNA polymerase I subunit A1) (EC 2.7.7.6) (DNA-directed RNA polymerase I largest subunit) (DNA-directed RNA polymerase I subunit A) (RNA polymerase I 194 kDa subunit) (A194) (RPA194)
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MLASKHTPWRRLQGISFGMYSAEELKKLSVKSITNPRYVDSLGNPSADGLYDLALGPADSKEVCSTCVQDFNNCSGHLGHIDLPLTVYNPLLFDKLYLLLRGSCLNCHMLTCPRAAIHLLVCQLKVLDVGALQAVYELERILSRFLEETSDPSAFEIQEELEEYTSKILQNNLLGSQGAHVKNVCESRSKLVAHFWKTHMAAKRCPHCKTGRSVVRKEHNSKLTITYPAMVHKKSGQKDAELPEGAPAAPGIDEAQMGKRGYLTPSSAQEHLFAIWKNEGFFLNYLFSGLDDIGPESSFNPSMFFLDFIVVPPSRYRPINRLGDQMFTNGQTVNLQAVMKDAVLIRKLLAVMAQEQKLPCEMTEITIDKENDSSGAIDRSFLSLLPGQSLTDKLYNIWIRLQSHVNIVFDSDMDKLMLEKYPGIRQILEKKEGLFRKHMMGKRVDYAARSVICPDMYINTNEIGIPMVFATKLTYPQPVTPWNVQELRQAVINGPNVHPGASMVINEDGSRTALSAVDATQREAVAKQLLTPSTGIPKPQGAKVVCRHVKNGDILLLNRQPTLHRPSIQAHRAHILPEEKVLRLHYANCKAYNADFDGDEMNAHFPQSELGRAEAYVLACTDQQYLVPKDGQPLAGLIQDHMVSGANMTIRGCFFTREQYMELVYRGLTDKVGRVKLFPPAILKPFPLWTGKQVVSTLLINIIPEDYTPLNLTGKAKIGSKAWVKEKPRPVPDFDPDSMCESQVIIREGELLCGVLDKAHYGSSAYGLVHCCYEIYGGETSGRVLTCLARLFTAYLQLYRGFTLGVEDILVKPNADVMRQRIIEESTQCGPRAVRAALNLPEAASCDEIQGKWQDAIWRKDQRDFNMIDMKFKEEVNHYSNEINKACMPFGLHRQFPENNLQMMVQSGAKGSTVNTMQISCLLGQIELEGRRPPLMASGKSLPCFEPYEFTPRAGGFVTGRFLTGIRPPEFFFHCMAGREGLVDTAVKTSRSGYLQRCIIKHLEGLVIQYDLTVRDSDGSVVQFLYGEDGLDIPKTQFLQPKQFPFLASNYEVIMKSKHLHEVLSRADPQKVLRHFRAIKKWHHRHSSALLRKGAFLSFSQKIQAAVKALNLEGKTQNGRSPETQQMLQMWHELDEQSRRKYQKRAAPCPDPSLSVWRPDIHFASVSETFEKKIDDYSQEWAAQAEKSHNRSELSLDRLRTLLQLKWQRSLCDPGEAVGLLAAQSIGEPSTQMTLNTFHFAGRGEMNVTLGIPRLREILMVASANIKTPMMSVPVFNTKKALRRVKSLKKQLTRVCLGEVLQKVDIQESFCMGEKQNKFRVYELRFQFLPHAYYQQEKCLRPEDILHFMETRFFKLLMEAIKKKNSKASAFRSVNTRRATQKDLDDTEDSGRNRREEERDEEEEGNIVDAEAEEGDADASDTKRKEKQEEEVDYESEEEGEEEEEEDVQEEENIKGEGAHQTHEPDEEEGSGLEEESSQNPPCRHSRPQGAEAMERRIQAVRESHSFIEDYQYDTEESLWCQVTVKLPLMKINFDMSSLVVSLAHNAIVYTTKGITRCLLNETINSKNEKEFVLNTEGINLPELFKYSEVLDLRRLYSNDIHAVANTYGIEAALRVIEKEIKDVFAVYGIAVDPRHLSLVADYMCFEGVYKPLNRFGIQSSSSPLQQMTFETSFQFLKQATMMGSHDELKSPSACLVVGKVVKGGTGLFELKQPLR
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DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Forms the polymerase active center together with the second largest subunit. A single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol I. A bridging helix emanates from RPA1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol I by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition (By similarity).
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O54890
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ITB3_MOUSE
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Integrin beta-3 (Platelet membrane glycoprotein IIIa) (GPIIIa) (CD antigen CD61)
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MRAQWPGQLWAALLALGALAGVVVGESNICTTRGVNSCQQCLAVSPVCAWCSDETLSQGSPRCNLKENLLKDNCAPESIEFPVSEAQILEARPLSSKGSGSSAQITQVSPQRIALRLRPDDSKIFSLQVRQVEDYPVDIYYLMDLSFSMKDDLSSIQTLGTKLASQMRKLTSNLRIGFGAFVDKPVSPYMYISPPQAIKNPCYNMKNACLPMFGYKHVLTLTDQVSRFNEEVKKQSVSRNRDAPEGGFDAIMQATVCDEKIGWRNDASHLLVFTTDAKTHIALDGRLAGIVLPNDGHCHIGTDNHYSASTTMDYPSLGLMTEKLSQKNINLIFAVTENVVSLYQNYSELIPGTTVGVLSDDSSNVLQLIVDAYGKIRSKVELEVRDLPEELSLSFNATCLNNEVIPGLKSCVGLKIGDTVSFSIEAKVRGCPQEKEQSFTIKPVGFKDSLTVQVTFDCDCACQAFAQPSSPRCNNGNGTFECGVCRCDQGWLGSMCECSEEDYRPSQQEECSPKEGQPICSQRGECLCGQCVCHSSDFGKITGKYCECDDFSCVRYKGEMCSGHGQCNCGDCVCDSDWTGYYCNCTTRTDTCMSTNGLLCSGRGNCECGSCVCVQPGSYGDTCEKCPTCPDACSFKKECVECKKFNRGTLHEENTCSRYCRDDIEQVKELTDTGKNAVNCTYKNEDDCVVRFQYYEDTSGRAVLYVVEEPECPKGPDILVVLLSVMGAILLIGLATLLIWKLLITIHDRKEFAKFEEERARAKWDTANNPLYKEATSTFTNITYRGT
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Integrin alpha-V/beta-3 (ITGAV:ITGB3) is a receptor for cytotactin, fibronectin, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin, vitronectin and von Willebrand factor. Integrin alpha-IIB/beta-3 (ITGA2B:ITGB3) is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. Integrins alpha-IIB/beta-3 and alpha-V/beta-3 recognize the sequence R-G-D in a wide array of ligands. Integrin alpha-IIB/beta-3 recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIB/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial surfaces. Fibrinogen binding enhances SELP expression in activated platelets. ITGAV:ITGB3 binds to fractalkine (CX3CL1) and acts as its coreceptor in CX3CR1-dependent fractalkine signaling. ITGAV:ITGB3 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling. ITGAV:ITGB3 binds to FGF1 and this binding is essential for FGF1 signaling. ITGAV:ITGB3 binds to FGF2 and this binding is essential for FGF2 signaling (By similarity). ITGAV:ITGB3 binds to IGF1 and this binding is essential for IGF1 signaling (By similarity). ITGAV:ITGB3 binds to IGF2 and this binding is essential for IGF2 signaling (By similarity). ITGAV:ITGB3 binds to IL1B and this binding is essential for IL1B signaling (By similarity). ITGAV:ITGB3 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1 (By similarity). ITGAV:ITGB3 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1 (By similarity). ITGAV:ITGB3 binds to the Lilrb4a/Gp49b receptor and enhances the Lilrb4a-mediated inhibition of mast cell activation. ITGAV:ITGB3 also suppresses marginal zone B cell antibody production through its interaction with Lilrb4a. In brain, plays a role in synaptic transmission and plasticity. Involved in the regulation of the serotonin neurotransmission, is required to localize to specific compartments within the synapse the serotonin receptor SLC6A4 and for an appropriate reuptake of serotonin. Controls excitatory synaptic strength by regulating GRIA2-containing AMPAR endocytosis, which affects AMPAR abundance and composition. ITGAV:ITGB3 act as a receptor for CD40LG (By similarity).
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O54898
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CAC1G_RAT
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Voltage-dependent T-type calcium channel subunit alpha-1G (Voltage-gated calcium channel subunit alpha Cav3.1)
|
MDEEEDGAGAEESGQPRSFTQLNDLSGAGGRQGPGSTEKDPGSADSEAEGLPYPALAPVVFFYLSQDSRPRSWCLRTVCNPWFERVSMLVILLNCVTLGMFRPCEDIACDSQRCRILQAFDDFIFAFFAVEMVVKMVALGIFGKKCYLGDTWNRLDFFIVIAGMLEYSLDLQNVSFSAVRTVRVLRPLRAINRVPSMRILVTLLLDTLPMLGNVLLLCFFVFFIFGIVGVQLWAGLLRNRCFLPENFSLPLSVDLEPYYQTENEDESPFICSQPRENGMRSCRSVPTLRGEGGGGPPCSLDYETYNSSSNTTCVNWNQYYTNCSAGEHNPFKGAINFDNIGYAWIAIFQVITLEGWVDIMYFVMDAHSFYNFIYFILLIIVGSFFMINLCLVVIATQFSETKQRESQLMREQRVRFLSNASTLASFSEPGSCYEELLKYLVYILRKAARRLAQVSRAIGVRAGLLSSPVARSGQEPQPSGSCTRSHRRLSVHHLVHHHHHHHHHYHLGNGTLRVPRASPEIQDRDANGSRRLMLPPPSTPTPSGGPPRGAESVHSFYHADCHLEPVRCQAPPPRCPSEASGRTVGSGKVYPTVHTSPPPEILKDKALVEVAPSPGPPTLTSFNIPPGPFSSMHKLLETQSTGACHSSCKISSPCSKADSGACGPDSCPYCARTGAGEPESADHVMPDSDSEAVYEFTQDAQHSDLRDPHSRRRQRSLGPDAEPSSVLAFWRLICDTFRKIVDSKYFGRGIMIAILVNTLSMGIEYHEQPEELTNALEISNIVFTSLFALEMLLKLLVYGPFGYIKNPYNIFDGVIVVISVWEIVGQQGGGLSVLRTFRLMRVLKLVRFLPALQRQLVVLMKTMDNVATFCMLLMLFIFIFSILGMHLFGCKFASERDGDTLPDRKNFDSLLWAIVTVFQILTQEDWNKVLYNGMASTSSWAALYFIALMTFGNYVLFNLLVAILVEGFQAEGDATKSESEPDFFSPSVDGDGDRKKRLALVALGEHAELRKSLLPPLIIHTAATPMSHPKSSSTGVGEALGSGSRRTSSSGSAEPGAAHHEMKCPPSARSSPHSPWSAASSWTSRRSSRNSLGRAPSLKRRSPSGERRSLLSGEGQESQDEEESSEEDRASPAGSDHRHRGSLEREAKSSFDLPDTLQVPGLHRTASGRSSASEHQDCNGKSASGRLARTLRTDDPQLDGDDDNDEGNLSKGERIQAWVRSRLPACCRERDSWSAYIFPPQSRFRLLCHRIITHKMFDHVVLVIIFLNCITIAMERPKIDPHSAERIFLTLSNYIFTAVFLAEMTVKVVALGWCFGEQAYLRSSWNVLDGLLVLISVIDILVSMVSDSGTKILGMLRVLRLLRTLRPLRVISRAQGLKLVVETLMSSLKPIGNIVVICCAFFIIFGILGVQLFKGKFFVCQGEDTRNITNKSDCAEASYRWVRHKYNFDNLGQALMSLFVLASKDGWVDIMYDGLDAVGVDQQPIMNHNPWMLLYFISFLLIVAFFVLNMFVGVVVENFHKCRQHQEEEEARRREEKRLRRLEKKRRSKEKQMAEAQCKPYYSDYSRFRLLVHHLCTSHYLDLFITGVIGLNVVTMAMEHYQQPQILDEALKICNYIFTVIFVFESVFKLVAFGFRRFFQDRWNQLDLAIVLLSIMGITLEEIEVNLSLPINPTIIRIMRVLRIARVLKLLKMAVGMRALLHTVMQALPQVGNLGLLFMLLFFIFAALGVELFGDLECDETHPCEGLGRHATFRNFGMAFLTLFRVSTGDNWNGIMKDTLRDCDQESTCYNTVISPIYFVSFVLTAQFVLVNVVIAVLMKHLEESNKEAKEEAELEAELELEMKTLSPQPHSPLGSPFLWPGVEGVNSTDSPKPGAPHTTAHIGAASGFSLEHPTMVPHPEEVPVPLGPDLLTVRKSGVSRTHSLPNDSYMCRNGSTAERSLGHRGWGLPKAQSGSILSVHSQPADTSCILQLPKDVHYLLQPHGAPTWGAIPKLPPPGRSPLAQRPLRRQAAIRTDSLDVQGLGSREDLLSEVSGPSCPLTRSSSFWGGSSIQVQQRSGIQSKVSKHIRLPAPCPGLEPSWAKDPPETRSSLELDTELSWISGDLLPSSQEEPLFPRDLKKCYSVETQSCRRRPGFWLDEQRRHSIAVSCLDSGSQPRLCPSPSSLGGQPLGGPGSRPKKKLSPPSISIDPPESQGSRPPCSPGVCLRRRAPASDSKDPSVSSPLDSTAASPSPKKDTLSLSGLSSDPTDMDP
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Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1G gives rise to T-type calcium currents. T-type calcium channels belong to the 'low-voltage activated (LVA)' group and are strongly blocked by nickel and mibefradil. A particularity of this type of channels is an opening at quite negative potentials and a voltage-dependent inactivation. T-type channels serve pacemaking functions in both central neurons and cardiac nodal cells and support calcium signaling in secretory cells and vascular smooth muscle. They may also be involved in the modulation of firing patterns of neurons which is important for information processing as well as in cell growth processes.
|
O54901
|
OX2G_MOUSE
|
OX-2 membrane glycoprotein (MRC OX-2 antigen) (CD antigen CD200)
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MGSLVFRRPFCHLSTYSLIWGMAAVALSTAQVEVVTQDERKALHTTASLRCSLKTSQEPLIVTWQKKKAVSPENMVTYSKTHGVVIQPAYKDRINVTELGLWNSSITFWNTTLEDEGCYMCLFNTFGSQKVSGTACLTLYVQPIVHLHYNYFEDHLNITCSATARPAPAISWKGTGTGIENSTESHFHSNGTTSVTSILRVKDPKTQVGKEVICQVLYLGNVIDYKQSLDKGFWFSVPLLLSIVSLVILLVLISILLYWKRHRNQERGESSQGMQRMK
|
Costimulates T-cell proliferation. May regulate myeloid cell activity in a variety of tissues (By similarity).
|
O54902
|
NRAM2_RAT
|
Natural resistance-associated macrophage protein 2 (NRAMP 2) (Divalent cation transporter 1) (Divalent metal transporter 1) (DMT-1) (Solute carrier family 11 member 2)
|
MVLDPEEKIPDDGASGDHGDSASLGAINPAYSNSSLPHSTGDSEEPFTTYFDEKIPIPEEEYSCFSFRKLWAFTGPGFLMSIAYLDPGNIESDLQSGAVAGFKLLWVLLLATIVGLLLQRLAARLGVVTGLHLAEVCHRQYPKVPRIILWLMVELAIIGSDMQEVIGSAIAINLLSAGRVPLYGGVLITIADTFVFLFLDKYGLRKLEAFFGFLITIMALTFGYEYVTVKPSQSQVLRGMFVPSCSGCHTPQVEQAVGIVGAVIMPHNMYLHSALVKSRQVNRANKQEVREANKYFFIESCIALFVSFIINVFVVSVFAEAFFEKTNEQVVEVCRNSSSPHADLFPNDNSTLAVDIYKGGVVLGCYFGPAALYIWAVGILAAGQSSTMTGTYSGQFVMEGFLNLKWSRFARVILTRSIAIIPTLLVAVFQDVEHLTGMNDFLNVLQSLQLPFALIPILTFTSLRPVMSEFSNGIGWRIAGGILVLLVCSINMYFVVVYVQELGHVALYVVAAVVSVAYLGFVFYLGWQCLIALGLSFLDCGRSYHLGLTARPEIYLLNTVDAVSLVSR
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Proton-coupled metal ion symporter operating with a proton to metal ion stoichiometry of 1:1. Selectively transports various divalent metal cations, in decreasing affinity: Cd(2+) > Fe(2+) > Co(2+), Mn(2+) >> Zn(2+), Ni(2+), VO(2+) (By similarity). Essential for maintenance of iron homeostasis by modulating intestinal absorption of dietary Fe(2+) and TF-associated endosomal Fe(2+) transport in erythroid precursors and other cells (By similarity). Enables Fe(2+) and Mn(2+) ion entry into mitochondria, and is thus expected to promote mitochondrial heme synthesis, iron-sulfur cluster biogenesis and antioxidant defense. Can mediate uncoupled fluxes of either protons or metal ions.
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O54904
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B3GT1_MOUSE
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Beta-1,3-galactosyltransferase 1 (Beta-1,3-GalTase 1) (Beta3Gal-T1) (Beta3GalT1) (EC 2.4.1.86) (UDP-Gal:betaGlcNAc beta 1,3-galactosyltransferase-I) (UDP-galactose:beta-N-acetyl-glucosamine-beta-1,3-galactosyltransferase 1)
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MASKVSCLYVLTVVCWASALWYLSITRPTSSYTGSKPFSHLTVARKNFTFGNIRTRPINPHSFEFLINEPNKCEKNIPFLVILISTTHKEFDARQAIRETWGDENNFKGIKIATLFLLGKNADPVLNQMVEQESQIFHDIIVEDFIDSYHNLTLKTLMGMRWVATFCSKAKYVMKTDSDIFVNMDNLIYKLLKPSTKPRRRYFTGYVINGGPIRDVRSKWYMPRDLYPDSNYPPFCSGTGYIFSADVAELIYKTSLHTRLLHLEDVYVGLCLRKLGIHPFQNSGFNHWKMAYSLCRYRRVITVHQISPEEMHRIWNDMSSKKHLRC
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Beta-1,3-galactosyltransferase that transfers galactose from UDP-alpha-D-galactose to substrates with a terminal beta-N-acetylglucosamine (beta-GlcNAc) residue. Involved in the biosynthesis of the carbohydrate moieties of glycolipids and glycoproteins.
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O54905
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B3GT2_MOUSE
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Beta-1,3-galactosyltransferase 2 (Beta-1,3-GalTase 2) (Beta3Gal-T2) (Beta3GalT2) (EC 2.4.1.86) (UDP-Gal:betaGlcNAc beta 1,3-galactosyltransferase-II)
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MLQWRRRHCCFAKMTWSPKRSLLRTPLTGVLSLVFLFAMFLFFNHHDWLPGRPGFKENPVTYTFRGFRSTKSETNHSSLRTIWKEVAPQTLRPHTASNSSNTELSPQGVTGLQNTLSANGSIYNEKGTGHPNSYHFKYIINEPEKCQEKSPFLILLIAAEPGQIEARRAIRQTWGNETLAPGIQIIRVFLLGISIKLNGYLQHAIQEESRQYHDIIQQEYLDTYYNLTIKTLMGMNWVATYCPHTPYVMKTDSDMFVNTEYLIHKLLKPDLPPRHNYFTGYLMRGYAPNRNKDSKWYMPPDLYPSERYPVFCSGTGYVFSGDLAEKIFKVSLGIRRLHLEDVYVGICLAKLRVDPVPPPNEFVFNHWRVSYSSCKYSHLITSHQFQPSELIKYWNHLQQNKHNACANAAKEKAGRYRHRKLH
|
Beta-1,3-galactosyltransferase that transfers galactose from UDP-galactose to substrates with a terminal beta-N-acetylglucosamine (beta-GlcNAc) residue. Can also utilize substrates with a terminal galactose residue, albeit with lower efficiency. Involved in the biosynthesis of the carbohydrate moieties of glycolipids and glycoproteins.
|
O54907
|
TNF12_MOUSE
|
Tumor necrosis factor ligand superfamily member 12 (TNF-related weak inducer of apoptosis) (TWEAK) [Cleaved into: Tumor necrosis factor ligand superfamily member 12, membrane form; Tumor necrosis factor ligand superfamily member 12, secreted form]
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MAARRSQRRRGRRGEPGTALLAPLVLSLGLALACLGLLLVVVSLGSWATLSAQEPSQEELTAEDRREPPELNPQTEESQDVVPFLEQLVRPRRSAPKGRKARPRRAIAAHYEVHPRPGQDGAQAGVDGTVSGWEETKINSSSPLRYDRQIGEFTVIRAGLYYLYCQVHFDEGKAVYLKLDLLVNGVLALRCLEEFSATAASSPGPQLRLCQVSGLLPLRPGSSLRIRTLPWAHLKAAPFLTYFGLFQVH
|
Binds to FN14 and possibly also to TNRFSF12/APO3. Weak inducer of apoptosis in some cell types. Mediates NF-kappa-B activation. Promotes angiogenesis and the proliferation of endothelial cells. Also involved in induction of inflammatory cytokines. Promotes IL8 secretion (By similarity).
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O54908
|
DKK1_MOUSE
|
Dickkopf-related protein 1 (Dickkopf-1) (Dkk-1) (mDkk-1)
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MMVVCAAAAVRFLAVFTMMALCSLPLLGASATLNSVLINSNAIKNLPPPLGGAGGQPGSAVSVAPGVLYEGGNKYQTLDNYQPYPCAEDEECGSDEYCSSPSRGAAGVGGVQICLACRKRRKRCMRHAMCCPGNYCKNGICMPSDHSHFPRGEIEESIIENLGNDHNAAAGDGYPRRTTLTSKIYHTKGQEGSVCLRSSDCAAGLCCARHFWSKICKPVLKEGQVCTKHKRKGSHGLEIFQRCYCGEGLACRIQKDHHQASNSSRLHTCQRH
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Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. Inhibits the pro-apoptotic function of KREMEN1 in a Wnt-independent manner, and has anti-apoptotic activity. Plays a role in limb development attenuates Wnt signaling in the developing limb to allow normal limb patterning.
|
O54909
|
RDH16_MOUSE
|
Retinol dehydrogenase 16 (EC 1.1.1.105) (EC 1.1.1.209) (EC 1.1.1.315) (EC 1.1.1.53) (Cis-retinol androgen dehydrogenase 1)
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MWLYLVALVGLWTLLRFFRVRQVVSHLQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGNRGLWGLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRVSLFGGGYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSARLCSNTQMLWDQTSSEIREIYGEKYLASYLKRLNKLDKRCNKDLSGVTDCMEHALTACHPRTRYSAGWDAKLFYLPLSYLPTFLVDALLYWTSLKPEKAL
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Oxidoreductase with a preference for NAD. Oxidizes all-trans-retinol, 9-cis-retinol, 11-cis-retinol and 13-cis-retinol to the corresponding aldehydes. Has higher activity towards CRBP-bound retinol than with free retinol. Oxidizes 3-alpha-hydroxysteroids. Oxidizes androstanediol and androsterone to dihydrotestosterone and androstanedione. Can also catalyze the reverse reaction.
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O54912
|
KCNK3_RAT
|
Potassium channel subfamily K member 3 (Acid-sensitive potassium channel protein TASK-1) (TWIK-related acid-sensitive K(+) channel 1) (Two pore potassium channel KT3.1) (Two pore K(+) channel KT3.1)
|
MKRQNVRTLALIVCTFTYLLVGAAVFDALESEPEMIERQRLELRQLELRARYNLSEGGYEELERVVLRLKPHKAGVQWRFAGSFYFAITVITTIGYGHAAPSTDGGKVFCMFYALLGIPLTLVMFQSLGERINTFVRYLLHRAKRGLGMRHAEVSMANMVLIGFVSCISTLCIGAAAFSYYERWTFFQAYYYCFITLTTIGFGDYVALQKDQALQTQPQYVAFSFVYILTGLTVIGAFLNLVVLRFMTMNAEDEKRDAEHRALLTHNGQAGGLGGLSCLSGSLGDGVRPRDPVTCAAAAGGMGVGVGVGGSGFRNVYAEMLHFQSMCSCLWYKSREKLQYSIPMIIPRDLSTSDTCVEHSHSSPGGGGRYSDTPSHPCLCSGTQRSAISSVSTGLHSLATFRGLMKRRSSV
|
pH-dependent, voltage-insensitive, background potassium channel protein. Rectification direction results from potassium ion concentration on either side of the membrane. Acts as an outward rectifier when external potassium concentration is low. When external potassium concentration is high, current is inward.
|
O54915
|
NR1I2_MOUSE
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Nuclear receptor subfamily 1 group I member 2 (Orphan nuclear receptor PXR) (Pregnane X receptor)
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MRPEESWSRVGLVQCEEADSALEEPINVEEEDGGLQICRVCGDKANGYHFNVMTCEGCKGFFRRAMKRNVRLRCPFRKGTCEITRKTRRQCQACRLRKCLESGMKKEMIMSDAAVEQRRALIKRKKREKIEAPPPGGQGLTEEQQALIQELMDAQMQTFDTTFSHFKDFRLPAVFHSGCELPEFLQASLLEDPATWSQIMKDRVPMKISLQLRGEDGSIWNYQPPSKSDGKEIIPLLPHLADVSTYMFKGVINFAKVISYFRDLPIEDQISLLKGATFEMCILRFNTMFDTETGTWECGRLAYCFEDPNGGFQKLLLDPLMKFHCMLKKLQLHKEEYVLMQAISLFSPDRPGVVQRSVVDQLQERFALTLKAYIECSRPYPAHRFLFLKIMAVLTELRSINAQQTQQLLRIQDSHPFATPLMQELFSSTDG
|
Nuclear receptor that binds and is activated by a variety of endogenous and xenobiotic compounds. Transcription factor that activates the transcription of multiple genes involved in the metabolism and secretion of potentially harmful xenobiotics, endogenous compounds and drugs. Response to specific ligands is species-specific, due to differences in the ligand-binding domain. Binds to a response element in the promoters of the CYP3A4 and ABCB1/MDR1 genes (By similarity). Activated by naturally occurring steroids such as pregnenolone and progesterone, the cholesterol metabolite 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol, synthetic glucocorticoids and antiglucocorticoids and 16-alpha-carbonitrile (PCN). {ECO:0000250, ECO:0000269|PubMed:12569201, ECO:0000269|PubMed:19297428}.
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O54916
|
REPS1_MOUSE
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RalBP1-associated Eps domain-containing protein 1 (RalBP1-interacting protein 1)
|
MEGLTLSDAEQKYYSDLFSYCDIESTKKVVVNGRVLELFRAAQLPNDVVLQIMELCGATRLGYFGRSQFYIALKLVAVAQSGFPLRVESINTVKDLPLPRFVASKNEQESRLAASYSSDSENQGSYSGVIPPPPGRGQVKKGPGSHDAVQPRPSAEQQEPVSPVVSPQQSPPTSPHTWRKHSRHPSGGNSERPLTGPGPFWSPFGDAQAGSSAGDAVWSGQSPPPPQDNWVSFADTPPTSALLTMHPASVQDQTTVRTVASAATANEIRRQSSSYEDPWKITDEQRQYYVNQFKTIQPDLNGFIPGSAAKEFFTKSKLPILELSHIWELSDFDKDGALTLDEFCAAFHLVVARKNGYDLPEKLPESLMPKLIDLEDSADVGEQPGEVGYSGSPAEAPPSKSPSMPSLNQTWPELNQSSEQWETFSERSSSSQTLTQFDSNIAPADPDTAIVHPVPIRMTPSKIHMQEMELKRTSSDHTNPTSPLLVKPSDLSEENKINSSVKFPSGNTVDGYSSSDSFPSDPEQIGSSVTRQRSHSGTSPDNTAPPPPPPRPQPSHSRSSSLDMNRTFAVTTGQQQAGVVAHPPAVPPRPQPSQAPGPSVHRPVDADGLITHTSTSPQQIPEQPNFADFSQFEVFAASNVSEEQDSEAEKHPEVLPAEKASDPSSSLRAAQADSKAEEKTATNVPANVSKGTTPLAPPPKPVRRRLKSEDELRPDVDEHTQKTGVLAAVLTSQPSIPRSVGKDKKAIQASIRRNKETNTVLARLNSELQQQLKDVLEERISLEVQLEQLRPFSHL
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May coordinate the cellular actions of activated EGF receptors and Ral-GTPases.
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O54917
|
E2F6_MOUSE
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Transcription factor E2F6 (E2F-6) (E2F-binding site-modulating activity protein) (EMA)
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MSQQRTARRQPSLLVDPAQETVRRRCRDPINVENLLPSKIRINLEENVQYVSMRKALKVKRPRFDVSLVYLTRKFMDLVRSAPGGILDLNKVATKLGVRKRRVYDITNVLDGIELVEKKSKNHIRWIGSDLNNFGAAPQQKKLQAELSDLSAMEDALDELIKDCAQQLLELTDDKENERLAYVTYQDIHGIQAFHEQIVIAVKAPEETRLDVPAPREDSITVHIRSTKGPIDVYLCEVEQNHSNGKTNDGIGASPSKSSHPQCPEKEDEPPQ
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Inhibitor of E2F-dependent transcription. Binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3'. Has a preference for the 5'-TTTCCCGC-3' E2F recognition site. E2F6 lacks the transcriptional activation and pocket protein binding domains. Appears to regulate a subset of E2F-dependent genes whose products are required for entry into the cell cycle but not for normal cell cycle progression (By similarity). Represses expression of some meiosis-specific genes, including SLC25A31/ANT4. May silence expression via the recruitment of a chromatin remodeling complex containing histone H3-K9 methyltransferase activity. Overexpression delays the exit of cells from the S-phase (By similarity).
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O54918
|
B2L11_MOUSE
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Bcl-2-like protein 11 (Bcl2-L-11) (Bcl2-interacting mediator of cell death)
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MAKQPSDVSSECDREGGQLQPAERPPQLRPGAPTSLQTEPQGNPDGEGDRCPHGSPQGPLAPPASPGPFATRSPLFIFVRRSSLLSRSSSGYFSFDTDRSPAPMSCDKSTQTPSPPCQAFNHYLSAMASIRQSQEEPEDLRPEIRIAQELRRIGDEFNETYTRRVFANDYREAEDHPQMVILQLLRFIFRLVWRRH
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Induces apoptosis and anoikis. The isoforms vary in cytotoxicity with isoform BimS being the most potent and isoform BimEL being the least potent.
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O54924
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EXOC8_RAT
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Exocyst complex component 8 (Exocyst complex 84 kDa subunit)
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MSDSGASRLRRQLESGGFEARLYVKQLSQQSDGDRDLQEHRQRVQALAEETAQNLKRNVYQNYRQFIETAREISYLESEMYQLSHLLTEQKSSLESIPLALLPAAAAGASTGEDTAGAGPRERGAAQAGFLPGPAGVPREGPGTGEEGKQRTLTTLLEKVEGCRDLLETPGQYLVYNGDLVEYEADHMAQLQRVHGFLMNDCLLVATWLPQRRGMYRYNALYPLDRLAVVNVKDNPPMKDMFKLLMFPESRIFQAENAKIKREWLEVLEETKRALSDKRRREQEEAAALRAPPPVTSKGSNPFEDEAEEELATPEAEEEKVDLSMEWIQELPEDLDVCIAQRDFEGAVDLLDKLNHYLEDKPSPPSVKELRAKVDERVRQLTEVLVFELSPDRSLRGGPKATRRAVSQLIRLGQCTKACELFLRNRAAAVHTAIRQLRIEGATLLYIHKLCHVFFTSLLETAREFETDFAGTDSGCYSAFVVWARSAMGMFVDAFSKQVFDSKESLSTAAECVKVAKEHCQQLGEIGLDLTFIIHALLVKDIQGALLSYKEIIIEATKHRNSEEMWRRMNLMTPEALGKLKEEMRSCGVSNFEQYTGDDCWVNLSYTVVAFTKQTMGFLEEALKLYFPELHMVLLESLVEVILVAVQHVDYSLRCEQDPEKKTFIRQNASFLYDTVLPVVERRFEEGVGKPAKQLQDLRNASRLLRVNPESTTSVV
|
Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
|
O54926
|
SIVA_MOUSE
|
Apoptosis regulatory protein Siva (CD27-binding protein) (CD27BP)
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MPKRSCPFADAAPLQLKVHVGLKELSHGVFAERYSREVFERTKQLLFQGARAYRDHISSEDCSVNHLQESLKSGVVGAPQPARGQMLIGPDGRLTRCQAQASEGGLPRTAPIACSSCMRSVDGKAVCSQCERALCGQCVYTCWGCGALACVLCGLADYADDGEKTLCTSCAMFEA
|
Induces CD27-mediated apoptosis. Inhibits BCL2L1 isoform Bcl-x(L) anti-apoptotic activity. Inhibits activation of NF-kappa-B and promotes T-cell receptor-mediated apoptosis (By similarity). {ECO:0000250, ECO:0000269|PubMed:9177220}.
|
O54928
|
SOCS5_MOUSE
|
Suppressor of cytokine signaling 5 (SOCS-5) (Cytokine-inducible SH2-containing protein 5)
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MDKVGKMWNNLKYRCQNLFSHEGGSRNENVEMNPNRCPSVKEKSISLGEAAPQQESSPLRENVALQLGLSPSKTFSRRNQNCAAEIPQVVEISIEKDSDSGATPGTRLARRDSYSRHAPWGGKKKHSCSTKTQSSLDTEKKFGRTRSGLQRRERRYGVSSMQDMDSVSSRAVGSRSLRQRLQDTVGLCFPMRTYSKQSKPLFSNKRKIHLSELMLEKCPFPAGSDLAQKWHLIKQHTAPVSPHSTFFDTFDPSLVSTEDEEDRLRERRRLSIEEGVDPPPNAQIHTFEATAQVNPLYKLGPKLAPGMTEISGDGSAIPQTNCDSEEDSTTLCLQSRRQKQRQVSGDSHAHVSRQGAWKVHTQIDYIHCLVPDLLQITGNPCYWGVMDRYEAEALLEGKPEGTFLLRDSAQEDYLFSVSFRRYNRSLHARIEQWNHNFSFDAHDPCVFHSSTVTGLLEHYKDPSSCMFFEPLLTISLNRTFPFSLQYICRAVICRCTTYDGIDGLPLPSMLQDFLKEYHYKQKVRVRWLEREPVKAK
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SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. May be a substrate-recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Inhibits for instance EGF signaling by mediating the degradation of the EGF receptor/EGFR. Involved in the regulation of T-helper cell differentiation by inhibiting of the IL4 signaling pathway which promotes differentiation into the Th2 phenotype. Can also partially inhibit IL6 and LIF signaling.
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O54937
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PDK4_RAT
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[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 4, mitochondrial (EC 2.7.11.2) (Pyruvate dehydrogenase kinase isoform 4)
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MKAARFVMRSASSLGNAGLVPREVELFSRYSPSPLSMKQLLDFGSENACERTSFSFLRQELPVRLANILKEIDILPEHLVNTPSVQLVKSWYIQSLMDLVEFHEKSPEDQKVLSDFVDTLVKVRNRHHNVVPTMAQGILEYKDNCTVDPVTNQNLQYFLDRFYMNRISTRMLMNQHILIFSDSKTGNPSHIGSIDPNCDVVAVVEDAFECAKMLCDQYYLTSPELKLTQVNGKFPGQPIHIVYVPSHLHHMLFELFKNAMRATVEHQENRPFLTPVEATVVLGKEDLTIKISDRGGGVPLRITDRLFSYTYSTAPTPVMDNSRNAPLAGFGYGLPISRLYAKYFQGDLNLYSMSGYGTDAIIYLKALSSESIEKLPVFNKSAFKHYQMSSEADDWCIPSKEPKNLSKEKLAV
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Kinase that plays a key role in regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Inhibition of pyruvate dehydrogenase decreases glucose utilization and increases fat metabolism in response to prolonged fasting and starvation. Plays an important role in maintaining normal blood glucose levels under starvation, and is involved in the insulin signaling cascade. Via its regulation of pyruvate dehydrogenase activity, plays an important role in maintaining normal blood pH and in preventing the accumulation of ketone bodies under starvation. In the fed state, mediates cellular responses to glucose levels and to a high-fat diet. Regulates both fatty acid oxidation and de novo fatty acid biosynthesis. Plays a role in the generation of reactive oxygen species. Protects detached epithelial cells against anoikis. Plays a role in cell proliferation via its role in regulating carbohydrate and fatty acid metabolism.
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O54939
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DHB3_RAT
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17-beta-hydroxysteroid dehydrogenase type 3 (17-beta-HSD 3) (Estradiol 17-beta-dehydrogenase 2) (EC 1.1.1.62) (Testicular 17-beta-hydroxysteroid dehydrogenase) (Testosterone 17-beta-dehydrogenase 3) (EC 1.1.1.64)
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MEQFLLSVGLLVCLVCLVKCVRFSRYLFLSFCKALPGSFLRSMGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQVISEEIERTTGSRVKVVQADFTREDIYDHIEEQLKGLEIGVLVNNVGMLPNLLPSHFLSTSGESQSVIHCNITSVVKMTQLVLKHMESRRRGLILNISSGVGVRPWPLYSLYSASKAFVCTFSKALNVEYRDKGIIIQVLTPYSVSTPMTKYLNTSRVTKTADEFVKESLKYVTIGAETCGCLAHEILAIILNLIPSRIFYSSTTQRFLLKQFSDYLKSNISNR
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Catalyzes the conversion of 17-oxosteroids to 17beta-hydroxysteroids. Favors the reduction of androstenedione to testosterone. Testosterone is the key androgen driving male development and function (By similarity). Uses NADPH while the two other EDH17B enzymes use NADH. Androgens such as epiandrosterone, dehydroepiandrosterone, androsterone and androstanedione are accepted as substrates and reduced at C-17. Can reduce 11-ketoandrostenedione as well as 11beta-hydroxyandrostenedione at C-17 to the respective testosterone forms (By similarity). Plays a role in the rate-limiting-step for the maximum level of testosterone production by the testis but does not affect basal testosterone production (By similarity).
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O54940
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BNIP2_MOUSE
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BCL2/adenovirus E1B 19 kDa protein-interacting protein 2
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MEGVELKEEWQDEDFPIPLPEDDSIEADTLDGTDPDRQPGSLEVNGNKVRKKLMAPDISLTLDPGEDSLWSDDLDEAGEVDLEGLDTPSENSDEFEWEDDLPKPKTTEVIRKGSITEYTATEEKGDGRRWRMFRIGEQDHRVDMKAIEPYKKVISHGGYYGDGLNAIVVFAVCFMPESGQPNYRYLMDNLFKYVIGTLELLVAENYMIIYLNGATTRRKMPSLGWLRRCYQQIDRRLRKNLKSLIIVHPSWFIRTLLAVTRPFISSKFSQKIRYVFNLAELAELVPMEYVGIPECIKQYEEEKFKKRQKRVDQELNGKQEPPKSEQ
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Implicated in the suppression of cell death. Interacts with the BCL-2 and adenovirus E1B 19 kDa proteins (By similarity).
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O54941
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SMCE1_MOUSE
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SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1 (BRG1-associated factor 57) (BAF57)
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MSKRPSYAPPPTPAPATQMPSTPGFVGYNPYSHLAYNNYRLGGNPGTNSRVTASSGITIPKPPKPPDKPLMPYMRYSRKVWDQVKASNPDLKLWEIGKIIGGMWRDLTDEEKQEYLNEYEAEKIEYNESMKAYHNSPAYLAYINAKSRAEAALEEESRQRQSRMEKGEPYMSIQPAEDPDDYDDGFSMKHTATARFQRNHRLISEILSESVVPDVRSVVTTARMQVLKRQVQSLMVHQRKLEAELLQIEERHQEKKRKFLESTDSFNNELKRLCGLKVEVDMEKIAAEIAQAEEQARKRQEEREKEAAEQAERSQSSMAPEEEQVANKAEEKKDEESIPMETEETHLEDTAESQQNGEEGTSTPEDKESGQEGVDSMEVEGTSDSNTGSESNSATVEEPPTDPVPEDEKKE
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Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth. Also specifically interacts with the CoREST corepressor resulting in repression of neuronal specific gene promoters in non-neuronal cells (By similarity). Required for the coactivation of estrogen responsive promoters by SWI/SNF complexes and the SRC/p160 family of histone acetyltransferases (HATs)(PubMed:12145209).
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O54942
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CLD5_MOUSE
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Claudin-5 (Brain endothelial cell clone 1 protein) (Lung-specific membrane protein)
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MGSAALEILGLVLCLVGWVGLILACGLPMWQVTAFLDHNIVTAQTTWKGLWMSCVVQSTGHMQCKVYESVLALSAEVQAARALTVGAVLLALVALFVTLTGAQCTTCVAPGPVKARVALTGGALYAVCGLLALVPLCWFANIVVREFYDPTVPVSQKYELGAALYIGWAASALLMCGGGLVCCGAWVCTGRPEFSFPVKYSAPRRPTANGDYDKKNYV
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Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
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O54943
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PER2_MOUSE
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Period circadian protein homolog 2 (mPER2) (Circadian clock protein PERIOD 2)
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MNGYVDFSPSPTSPTKEPGAPQPTQAVLQEDVDMSSGSSGNENCSTGRDSQGSDCDDNGKELRMLVESSNTHPSPDDAFRLMMTEAEHNPSTSGCSSEQSAKADAHKELIRTLKELKVHLPADKKAKGKASTLATLKYALRSVKQVKANEEYYQLLMSSESQPCSVDVPSYSMEQVEGITSEYIVKNADMFAVAVSLVSGKILYISNQVASIFHCKKDAFSDAKFVEFLAPHDVSVFHSYTTPYKLPPWSVCSGLDSFTQECMEEKSFFCRVSVGKHHENEIRYQPFRMTPYLVKVQEQQGAESQLCCLLLAERVHSGYEAPRIPPEKRIFTTTHTPNCLFQAVDERAVPLLGYLPQDLIETPVLVQLHPSDRPLMLAIHKKILQAGGQPFDYSPIRFRTRNGEYITLDTSWSSFINPWSRKISFIIGRHKVRVGPLNEDVFAAPPCPEEKTPHPSVQELTEQIHRLLMQPVPHSGSSGYGSLGSNGSHEHLMSQTSSSDSNGQEESHRRRSGIFKTSGKIQTKSHVSHESGGQKEASVAEMQSSPPAQVKAVTTIERDSSGASLPKASFPEELAYKNQPPCSYQQISCLDSVIRYLESCSEAATLKRKCEFPANIPSRKATVSPGLHSGEAARPSKVTSHTEVSAHLSSLTLPGKAESVVSLTSQCSYSSTIVHVGDKKPQPELETVEDMASGPESLDGAAGGLSQEKGPLQKLGLTKEVLAAHTQKEEQGFLQRFREVSRLSALQAHCQNYLQERSRAQASDRGLRNTSGLESSWKKTGKNRKLKSKRVKTRDSSESTGSGGPVSHRPPLMGLNATAWSPSDTSQSSCPSAPFPTAVPAYPLPVFQAPGIVSTPGTVVAPPAATHTGFTMPVVPMGTQPEFAVQPLPFAAPLAPVMAFMLPSYPFPPATPNLPQAFLPSQPHFPAHPTLASEITPASQAEFPSRTSTLRQPCACPVTPPAGTVALGRASPPLFQSRGSSPLQLNLLQLEEAPEGSTGAAGTLGTTGTAASGLDCTSGTSRDRQPKAPPTCNEPSDTQNSDAISTSSDLLNLLLGEDLCSATGSALSRSGASATSDSLGSSSLGFGTSQSGAGSSDTSHTSKYFGSIDSSENNHKAKMIPDTEESEQFIKYVLQDPIWLLMANTDDSIMMTYQLPSRDLQAVLKEDQEKLKLLQRSQPRFTEGQRRELREVHPWVHTGGLPTAIDVTGCVYCESEEKGNICLPYEEDSPSPGLCDTSEAKEEEGEQLTGPRIEAQT
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Transcriptional repressor 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 syndrome 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. PER1 and PER2 proteins transport CRY1 and CRY2 into the nucleus with appropriate circadian timing, but also contribute directly to repression of clock-controlled target genes through interaction with several classes of RNA-binding proteins, helicases and others transcriptional repressors. PER appears to regulate circadian control of transcription by at least three different modes. First, interacts directly with the CLOCK-BMAL1 at the tail end of the nascent transcript peak to recruit complexes containing the SIN3-HDAC that remodel chromatin to repress transcription. Second, brings H3K9 methyltransferases such as SUV39H1 and SUV39H2 to the E-box elements of the circadian target genes, like PER2 itself or PER1. The recruitment of each repressive modifier to the DNA seems to be very precisely temporally orchestrated by the large PER complex, the deacetylases acting before than the methyltransferases. Additionally, large PER complexes are also recruited to the target genes 3' termination site through interactions with RNA-binding proteins and helicases that may play a role in transcription termination to regulate transcription independently of CLOCK-BMAL1 interactions. Recruitment of large PER complexes to the elongating polymerase at PER and CRY termination sites inhibited SETX action, impeding RNA polymerase II release and thereby repressing transcriptional reinitiation. May propagate clock information to metabolic pathways via the interaction with nuclear receptors. Coactivator of PPARA and corepressor of NR1D1, binds rhythmically at the promoter of nuclear receptors target genes like BMAL1 or G6PC1. Directly and specifically represses PPARG proadipogenic activity by blocking PPARG recruitment to target promoters and thereby transcriptional activation. Required for fatty acid and lipid metabolism, is involved as well in the regulation of circulating insulin levels. Plays an important role in the maintenance of cardiovascular functions through the regulation of NO and vasodilatatory prostaglandins production in aortas. Controls circadian glutamate uptake in synaptic vesicles through the regulation of VGLUT1 expression. May also be involved in the regulation of inflammatory processes. Represses the CLOCK-BMAL1 induced transcription of BHLHE40/DEC1 and ATF4. Negatively regulates the formation of the TIMELESS-CRY1 complex by competing with TIMELESS for binding to CRY1.
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O54946
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DNJB6_MOUSE
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DnaJ homolog subfamily B member 6 (Heat shock protein J2) (HSJ-2) (MRJ) (mDj4)
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MVDYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGGIHFDSPFEFGFTFRNPDDVFREFFGGRDPFSFDFFEDPFDDFFGNRRGPRGNRSRGAGSFFSTFSGFPSFGSGFPAFDTGFTPFGSLGHGGLTSFSSTSFGGSGMGNFKSISTSTKIVNGKKITTKRIVENGQERVEVEEDGQLKSLTINGVADENALAEECQRRGQPTPALAPGPAPAPVRVPSQARPLAPTPAPTPAPTPAPAPAQTPAPSVSTRPQKPPRPAPTAKLGSKSNWEDDEQDRQRVPGNWDAPMTSAGLKEGGKRKKQKQKEDLKKKKSTKGNH
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Has a stimulatory effect on the ATPase activity of HSP70 in a dose-dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins. Also reduces cellular toxicity and caspase-3 activity (By similarity).
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O54947
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HAVR1_RAT
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Hepatitis A virus cellular receptor 1 homolog (HAVcr-1) (Kidney injury molecule 1) (KIM-1) (T cell immunoglobulin and mucin domain-containing protein 1) (TIMD-1) (CD antigen CD365)
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MVQLQVFISGLLLLLPGSVDSYEVVKGVVGHPVTIPCTYSTRGGITTTCWGRGQCPYSSCQNILIWTNGYQVTYRSSGRYNIKGRISEGDVSLTIENSVDSDSGLYCCRVEIPGWFNDQKMTFSLEVKPEIPTSPPTRPTTTRPTTTRPTTISTRSTHVPTSTRVSTSTPTPEQTQTHKPEITTFYAHETTAEVTETPSYTPADWNGTVTSSEEAWNNHTVRIPLRKPQRNPTKGFYVGMSVAALLLLLLASTVVVTRYIIIRKKMGSLSFVAFHVSKSRALQNAAIVHPRAEDNIYIIEDRSRGAE
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Phosphatidylserine receptor that plays an important functional role in regulatory B-cells homeostasis including generation, expansion and suppressor functions (By similarity). As P-selectin/SELPLG ligand, plays a specialized role in activated but not naive T-cell trafficking during inflammatory responses. Controls thereby T-cell accumulation in the inflamed central nervous system (CNS) and the induction of autoimmune disease (By similarity). Regulates also expression of various anti-inflammatory cytokines and co-inhibitory ligands including IL10. Acts as regulator of T-cell proliferation (By similarity). May play a role in kidney injury and repair (By similarity).
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O54949
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NLK_MOUSE
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Serine/threonine-protein kinase NLK (EC 2.7.11.24) (Nemo-like kinase)
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MSLCGTRANAKMMAAYNGGTSAAAAGHHHHHHHHLPHLPPPHLHHHHHPQHHLHPGSAAAVHPVQQHTSSAAAAAAAAAAAAAMLNPGQQQPYFPSPAPGQAPGPAAAAPAQVQAAAAATVKAHHHQHSHHPQQQLDIEPDRPIGYGAFGVVWSVTDPRDGKRVALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNVLSALDILQPPHIDYFEEIYVVTELMQSDLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEELDESRHMTQEVVTQYYRAPEILMGSRHYSNAIDIWSVGCIFAELLGRRILFQAQSPIQQLDLITDLLGTPSLEAMRTACEGAKAHILRGPHKQPSLPVLYTLSSQATHEAVHLLCRMLVFDPSKRISAKDALAHPYLDEGRLRYHTCMCKCCFSTSTGRVYTSDFEPVTNPKFDDTFEKNLSSVRQVKEIIHQFILEQQKGNRVPLCINPQSAAFKSFISSTVAQPSEMPPSPLVWE
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Serine/threonine-protein kinase that regulates a number of transcription factors with key roles in cell fate determination. Positive effector of the non-canonical Wnt signaling pathway, acting downstream of WNT5A, MAP3K7/TAK1 and HIPK2. Negative regulator of the canonical Wnt/beta-catenin signaling pathway. Binds to and phosphorylates TCF7L2/TCF4 and LEF1, promoting the dissociation of the TCF7L2/LEF1/beta-catenin complex from DNA, as well as the ubiquitination and subsequent proteolysis of LEF1. Together these effects inhibit the transcriptional activation of canonical Wnt/beta-catenin target genes. Negative regulator of the Notch signaling pathway. Binds to and phosphorylates NOTCH1, thereby preventing the formation of a transcriptionally active ternary complex of NOTCH1, RBPJ/RBPSUH and MAML1. Negative regulator of the MYB family of transcription factors. Phosphorylation of MYB leads to its subsequent proteolysis while phosphorylation of MYBL1 and MYBL2 inhibits their interaction with the coactivator CREBBP. Other transcription factors may also be inhibited by direct phosphorylation of CREBBP itself. Acts downstream of IL6 and MAP3K7/TAK1 to phosphorylate STAT3, which is in turn required for activation of NLK by MAP3K7/TAK1. Upon IL1B stimulus, cooperates with ATF5 to activate the transactivation activity of C/EBP subfamily members (By similarity). Phosphorylates ATF5 but also stabilizes ATF5 protein levels in a kinase-independent manner (By similarity). Acts as an inhibitor of the mTORC1 complex in response to osmotic stress by mediating phosphorylation of RPTOR, thereby preventing recruitment of the mTORC1 complex to lysosomes (By similarity).
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O54950
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AAKG1_MOUSE
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5'-AMP-activated protein kinase subunit gamma-1 (AMPK gamma1) (AMPK subunit gamma-1) (AMPKg)
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MESVAAESSPALENEHFQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLQELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDEHDVVKGIVSLSDILQALVLTGGEKKP
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AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton probably by indirectly activating myosin. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive (By similarity).
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O54951
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SEM6B_MOUSE
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Semaphorin-6B (Semaphorin VIB) (Sema VIB) (Semaphorin-N) (Sema N)
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MWTPRVPPPRPALSFFLLLLLGVTYGLFPEEPPPLSVAPRDYLSHYPVFVGSGPGRLTAAEGAEDLNIQRVLRVNRTLFIGDRDNLYQVELEPSTSTELRYQRKLTWRSNPSDIDVCRMKGKQEGECRNFVKVLLLRDESTLFVCGSNAFNPICANYSMDTLQLLGDSISGMARCPYDPKHANVALFSDGMLFTATVTDFLAIDAVIYRSLGDRPTLRTVKHDSKWFKEPYFVHAVEWGSHVYFFFREIAMEFNYLEKVVVSRVARVCKNDVGGSPRVLEKQWTSFLKARLNCSVPGDSHFYFNVLQAVTGVVSLGGRPVILAVFSTPSNSIPGSAVCAFDMNQVAAVFEGRFREQKSPESIWTPVPEDQVPRPRPGCCAAPGMQYNASSALPDEILNFVKTHPLMDEAVPSLGHSPWIVRTLMRHQLTRVAVDVGAGPWGNQTIVFLGSEAGTVLKFLVKPNASVSGTTGPSIFLEEFETYRPDRCGRPSSAGEWGQRLLSLELDAASGGLLAAFPRCVVRVPVARCQLYSGCMKNCIGSQDPYCGWAPDGSCIFLRPGTSATFEQDVSGASTSGLGDCTGLLRASLSDDRAGLVSVNLLVTSSVAAFVVGAVVSGFSVGWFVGLRERRELARRKDKEAILAHGGSEAVLSVSRLGERRGTGPGGRGGAGGGPGGPPEALLAPLMQNGWTKAALLHGGPHDLDTGLLPTPEQTPLPQKRLPTPHPHAHALGSRAWDHSHALLSASASTSLLLLAPARASEQPQVPAEPGPESRLCAPRSCRASHPGDFPLTPHASPDRRRVVSAPTGPLDPSVGDGLPGPWSPPATSSLRRPGPHGPPTAALRRTHTFNSGEARPGGHRPRRHPPADSTHLLPCGTGERTAPPVP
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Functions as a cell surface repellent for mossy fibers of developping neurons in the hippocampus where it plays a role in axon guidance. May function through the PLXNA4 receptor expressed by mossy cell axons.
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O54952
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BRCA1_RAT
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Breast cancer type 1 susceptibility protein homolog (EC 2.3.2.27) (RING-type E3 ubiquitin transferase BRCA1)
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MDLSAVRIQEVQNVLHAMQKILECPICLELIKEPVSTQCDHIFCKFCMLKLLNQKKGPSQCPLCKNEITKRSLQGSARFSQLVEELLKIIDAFELDTGMQCANGFSFSKKKNSSSELLNEDASIIQSVGYRNRVKKLQQIESGSATLKDSLSVQLSNLGIVRSMKKNRQTQPQNKSVYIALESDSSEERVNAPDGCSVRDQELFQIAPGGAGDEGKLNSAKKAACDFSEGIRNIEHHQCSDKDLNPTENHATERHPEKCPRISVANVHVEPCGTDARASSLQRGTRSLLFTEDRLDAEKAEFCDRSKQSGAAVSQQSRWADSKETCNGRPVPRTEGKADPNVDSLCGRKQWNHPKSLCPENSGATTDVPWITLNSSIQKVNEWFSRTGEMLTSDNASDRRPASNAEAAVVLEVSNEVDGCFSSSKKIDLVAPDPDNAVMCTSGRDFSKPVENIINDKIFGKTYQRKGSRPHLNHVTEIIGTFTTEPQIIQEQPFTNKLKRKRSTCLHPEDFIKKADLTVVQRISENLNQGTDQMEPNDQAMSITSNGQENRATGNDLQRGRNAHPIESLRKEPAFTAKAKSISNSISDLEVELNVHSSKAPKKNRLRRKSTRCVLPLEPISRNPSPPTCAELQIESCGSSEETKKNNSNQTPAGHIREPQLIEDTEPAADAKKNEPNEHIRKRSASDAFPEEKLMNKAGLLTSCSSPRKPQGPVNPSPERKGIEQLEMCQMPDNNKELGDLVLGGEPSGKPTEPSEESTSVSLVPDTDYDTQNSVSILEANTVRYARTGSVQCMTQFVASENPKELVHGSNNAGSGSECFKHPLRHELNHNQETIEMEDSELDTQYLQNTFQVSKRQSFALFSKLRSPQKDCTLVGARSVPSREPSPKVTSRGEQKERQGQEESEISHVQAVTVTVGLPVPCQEGKPGAVTMCADVSRLCPSSHYRSCENGLNTTDKSGISQNSHFRQSVSPLRSSIKTDNRKTLTEGRFEKHTERGMGNETAVQSTIHTISLNNRGDACLEASSGSVIEVHSTGENVQGQLDRNRGPKVNTVSLLDSTQPGVSKQSAPVSDKYLEIKQESKAVSADFSPCLFSDHLEKPMRSDKTFQVCSETPDDLLDDVEIQENASFGEGGITEKSAIFNGSVLRRESSRSPSPVTHASKSRSLHRGSRKLEFSEESDSTEDEDLPCFQHLLSRVSSTPELTRCSSVVTQRVPEKAKGTQAPRKSSISDCNNEVILGEASQEYQFSEDAKCSGSMFSSQHSAALGSPANALSQDPDFNPPSKQRRHQAENEEAFLSDKELISDHEDMAACLEEASDQEEDSIIPDSVASGYESEANLSEDCSQSDILTTQQRATMKDNLIKLQQEMAQLEAVLEQHGSQPSGHPPCLPADPCALEDLPDPEQNRSGTAILTSKNINENPVSQNPKRACDDKSQPQPPDGLPSGDKESGMRRPSPFKSPLTSSRCSARGHSRSLQNRNSTSQEELLQPAXLEKSCEPHNLTGRSCLPRQDLEGTPYPESGIRLVSSRDPDSESPKVSALVCTAPASTSALKISQGQVAGSCRSPAAGGADTAVVEIVSKIKPEVTSPKERAERDISMVVSGLTPKEVMIVQKFAEKYRLALTDVITEETTHVIIKTDAEFVCERTLKYFLGIAGGKWIVSYSWVIKSIQERKLLSVHEFEVKGDVVTGSNHQGPRRSRESQEKLFEGLQIYCCEPFTNMPKDELERMLQLCGASVVKELPLLTRDTGAHPIVLVQPSAWTEDNDCPDIGQLCKGRLVMWDWVLDSISVYRCRDLDAYLVQNITCGRDGSEPQDSND
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E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. It is unclear whether it also mediates the formation of other types of polyubiquitin chains. The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Regulates centrosomal microtubule nucleation. Required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle. Required for FANCD2 targeting to sites of DNA damage. Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation. Contributes to homologous recombination repair (HRR) via its direct interaction with PALB2, fine-tunes recombinational repair partly through its modulatory role in the PALB2-dependent loading of BRCA2-RAD51 repair machinery at DNA breaks. Component of the BRCA1-RBBP8 complex which regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage via BRCA1-mediated ubiquitination of RBBP8. Acts as a transcriptional activator.
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O54957
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LAT_MOUSE
|
Linker for activation of T-cells family member 1 (36 kDa phosphotyrosine adapter protein) (pp36) (p36-38)
|
MEADALSPVGLGLLLLPFLVTLLAALCVRCRELPVSYDSTSTESLYPRSILIKPPQITVPRTPAVSYPLVTSFPPLRQPDLLPIPRSPQPLGGSHRMPSSQQNSDDANSVASYENQEPACKNVDADEDEDDYPNGYLVVLPDSSPAAVPVVSSAPVPSNPDLGDSAFSVESCEDYVNVPESEESAEASLDGSREYVNVSPEQQPVTRAELASVNSQEVEDEGEEEGVDGEEAPDYENLQELN
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Required for TCR (T-cell antigen receptor)- and pre-TCR-mediated signaling, both in mature T-cells and during their development. Involved in FCGR3 (low affinity immunoglobulin gamma Fc region receptor III)-mediated signaling in natural killer cells and FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Couples activation of these receptors and their associated kinases with distal intracellular events such as mobilization of intracellular calcium stores, PKC activation, MAPK activation or cytoskeletal reorganization through the recruitment of PLCG1, GRB2, GRAP2, and other signaling molecules.
|
O54960
|
CAPON_RAT
|
Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein (C-terminal PDZ ligand of neuronal nitric oxide synthase protein) (Nitric oxide synthase 1 adaptor protein)
|
MPSKTKYNLVDDGHDLRIPLHNEDAFQHGISFEAKYVGSLDVPRPNSRVEIVAAMRRIRYEFKAKNIKKKKVSIMVSVDGVKVILKKKKKKKEWTWDESKMLVMQDPIYRIFYVSHDSQDLKIFSYIARDGASNIFRCNVFKSKKKSQAMRIVRTVGQAFEVCHKLSLQHTQQNADGQEDGESERNSDGSGDPGRQLTGAERVSTATAEETDIDAVEVPLPGNDILEFSRGVTDLDAIGKDGGSHIDTTVSPHPQEPMLAASPRMLLPSSSSSKPPGLGTGTPLSTHHQMQLLQQLLQQQQQQTQVAVAQVHLLKDQLAAEAAARLEAQARVHQLLLQNKDMLQHISLLVKQVQELELKLSGQSTMGSQDSLLEITFRSGALPVLCESTTPKPEDLHSPLLGAGLADFAHPVGSPLGRRDCLVKLECFRFLPAEDNQPMAQGEPLLGGLELIKFRESGIASEYESNTDESEERDSWSQEELPRLLNVLQRQELGDSLDDEIAV
|
Adapter protein involved in neuronal nitric-oxide (NO) synthesis regulation via its association with nNOS/NOS1. The complex formed with NOS1 and synapsins is necessary for specific NO and synapsin functions at a presynaptic level. Mediates an indirect interaction between NOS1 and RASD1 leading to enhance the ability of NOS1 to activate RASD1. Competes with DLG4 for interaction with NOS1, possibly affecting NOS1 activity by regulating the interaction between NOS1 and DLG4. In kidney podocytes, plays a role in podosomes and filopodia formation through CDC42 activation.
|
O54962
|
BAF_MOUSE
|
Barrier-to-autointegration factor (LAP2-binding protein 1) [Cleaved into: Barrier-to-autointegration factor, N-terminally processed]
|
MTTSQKHRDFVAEPMGEKPVGSLAGIGDVLSKRLEERGFDKAYVVLGQFLVLKKDEDLFREWLKDTCGANAKQSRDCFGCLREWCDAFL
|
Non-specific DNA-binding protein that plays key roles in mitotic nuclear reassembly, chromatin organization, DNA damage response, gene expression and intrinsic immunity against foreign DNA (By similarity). Contains two non-specific double-stranded DNA (dsDNA)-binding sites which promote DNA cross-bridging (By similarity). Plays a key role in nuclear membrane reformation at the end of mitosis by driving formation of a single nucleus in a spindle-independent manner (By similarity). Transiently cross-bridges anaphase chromosomes via its ability to bridge distant DNA sites, leading to the formation of a dense chromatin network at the chromosome ensemble surface that limits membranes to the surface (By similarity). Also acts as a negative regulator of innate immune activation by restricting CGAS activity toward self-DNA upon acute loss of nuclear membrane integrity. Outcompetes CGAS for DNA-binding, thereby preventing CGAS activation and subsequent damaging autoinflammatory responses (By similarity). Also involved in DNA damage response: interacts with PARP1 in response to oxidative stress, thereby inhibiting the ADP-ribosyltransferase activity of PARP1 (By similarity). Involved in the recognition of exogenous dsDNA in the cytosol: associates with exogenous dsDNA immediately after its appearance in the cytosol at endosome breakdown and is required to avoid autophagy (By similarity).
|
O54963
|
REST_RAT
|
RE1-silencing transcription factor (Neural-restrictive silencer factor)
|
MATQVMGQSSGGGSLFNNSGNMGMALPNDMYDLHDLSKAELAAPQLIMLANVALTGEVNGSCCDYLVGEERQMAELMPVGDNHFSDSEGEGLEESAELKGDPSGLDNMELRSLELSVVEPQPVFEASAAPEVYSSNKDPAPEAPVAEDKCKNLKAKPFRCKPCQYEAESEEQFVHHIRVHSAKKFFVEESAEKQAKARESGASPSEEGEFSKGPIRCDRCGYNTNRYDHYTAHLKHHLRAGDNERVYKCIICTYTTVSEYHWRKHLRNHFPRKVYTCSKCNYFSTEKNNYVQHVRTHTGERPYKCELCPYSSSQKTHLTRHMRTHSGEKPFKCDQCNYVASNQHEVTRHARQVHNGPKPLNCPHCDYKTADRSNFKKHVELHVNPRQFNCPVCDYAASKKCNLQYHFKSKHPTCPSKTMDVSKVKLKKTKRREADLHRDAAAAATEQTDTEQAKTKGVDASARRSERPVKGVGKDVPKEKKPCSNASVVQVTTRTRKSAVETKAAEGKHTDGQTGNNAEKSSKAKKSKRKMDAEAHPSVEPVTEGPVTKKKKTESKPKTSGEVPKGSRVEDRKADKQQSASIKKGGKKTALKTKTAKKGSKLAPKWVGHTEPSSEMAQGGESPVPALTQAVVTPSGSTQTELSSPMDIAQTEPAQMDVSQTGPPQVQRPLPVEPAQLEPSPPQEPPQVEPPACVEPPPPVEPPCPMEPAEMEPSPPMEPSQVEPPPHLEPPLPMELPQVELPPVEDCQKELPPVEHAQTKVAQTGPTQVGAVQEEPLFCLRATSSQANQKVISPKDRAKEKLSVLSEMARQEQVLIEVGLVPVRDSQLLKASKSAPDLPAPPSPLPKGHLRREETPKDQEMFSDGEGNKVSPLEKGGTEEAGESRAELAAPMESTSALSSEQSSNAPDGETLHSECQADSTAVCEMEVDTEQKTDRVPLKDSAVEPVSPLNPRVDPEAAAPAVVASPPITLAESQEIDEDEGIHSHDGSDLSDNMSEGSDDSGLHGARPAPQEATSKSGKEGLAVKVTEGEFVCIFCDRSFRKEKDYSKHLNRHLVNVYFLEEAAEEQE
|
Transcriptional repressor which binds neuron-restrictive silencer element (NRSE) and represses neuronal gene transcription in non-neuronal cells (By similarity). Restricts the expression of neuronal genes by associating with two distinct corepressors, SIN3A and RCOR1, which in turn recruit histone deacetylase to the promoters of REST-regulated genes (By similarity). Mediates repression by recruiting the BHC complex at RE1/NRSE sites which acts by deacetylating and demethylating specific sites on histones, thereby acting as a chromatin modifier. Transcriptional repression by REST-CDYL via the recruitment of histone methyltransferase EHMT2 may be important in transformation suppression (By similarity). Represses the expression of SRRM4 in non-neural cells to prevent the activation of neural-specific splicing events and to prevent production of REST isoform 6 (By similarity). Repressor activity may be inhibited by forming heterodimers with isoform 6, thereby preventing binding to NRSE or binding to corepressors and leading to derepression of target genes (By similarity). Also maintains repression of neuronal genes in neural stem cells, and allows transcription and differentiation into neurons by dissociation from RE1/NRSE sites of target genes (By similarity). Thereby is involved in maintaining the quiescent state of adult hippocampal neural stem cells and preventing premature differentiation into mature neurons (By similarity). Plays a role in the developmental switch in synaptic NMDA receptor composition during postnatal development, by repressing GRIN2B expression and thereby altering NMDA receptor properties from containing primarily GRIN2B to primarily GRIN2A subunits. Acts as a regulator of osteoblast differentiation (By similarity). Key repressor of gene expression in hypoxia represses genes in hypoxia by direct binding to an RE1/NRSE site on their promoter regions (By similarity). May also function in stress resistance in the brain during aging possibly by regulating expression of genes involved in cell death and in the stress response (By similarity). Repressor of gene expression in the hippocampus after ischemia by directly binding to RE1/NRSE sites and recruiting SIN3A and RCOR1 to promoters of target genes, thereby promoting changes in chromatin modifications and ischemia-induced cell death. After ischemia, might play a role in repression of miR-132 expression in hippocampal neurons, thereby leading to neuronal cell death. [Isoform 6]: Binds to the 3' region of the neuron-restrictive silencer element (NRSE), with lower affinity than full-length REST isoform 1 (By similarity). Exhibits weaker repressor activity compared to isoform 1 (By similarity). May negatively regulate the repressor activity of isoform 1 by binding to isoform 1, thereby preventing its binding to NRSE and leading to derepression of target genes (By similarity). However, in another study, does not appear to be implicated in repressor activity of a NRSE motif-containing reporter construct nor in inhibitory activity on the isoform 1 transcriptional repressor activity (By similarity). Post-transcriptional inactivation of REST by SRRM4-dependent alternative splicing into isoform 6 is required in mechanosensory hair cells in the inner ear for derepression of neuronal genes and hearing (By similarity).
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O54965
|
RNF13_MOUSE
|
E3 ubiquitin-protein ligase RNF13 (EC 2.3.2.27) (RING finger protein 13)
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MLLSIGMLMLSATQVYTILTVQLFAFLNLLPVEADILAYNFENASQTFEDLPARFGYRLPAEGLKGFLINSKPENACEPIVPPPLKDNSSGTFIVLIRRLDCNFDIKVLNAQRAGYKAAIVHNVDSDDLISMGSNDIDTLKKIDIPSVFIGESSANSLKDEFTYEKGGHIILVPELSLPLEYYLIPFLIIVGICLILIVIFMITKFVQDRHRNRRNRLRKDQLKKLPVHKFKKGDEYDVCAICLEEYEDGDKLRILPCSHAYHCKCVDPWLTKTKKTCPVCKQKVVPSQGDSDSDTDSSQEENQVSEHTPLLPPSASARTQSFGSLSESHSHHNMTESSDYEDDDNEETDSSDADNEITDHSVVVQLQPNGEQDYNIANTV
|
E3 ubiquitin-protein ligase that regulates cell proliferation. Involved in apoptosis regulation (By similarity). Mediates ER stress-induced activation of JNK signaling pathway and apoptosis by promoting ERN1 activation and splicing of XBP1 mRNA (By similarity). Also involved in protein trafficking and localization (By similarity).
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O54967
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ACK1_MOUSE
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Activated CDC42 kinase 1 (ACK-1) (EC 2.7.10.2) (EC 2.7.11.1) (Non-receptor protein tyrosine kinase Ack) (Tyrosine kinase non-receptor protein 2)
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MQPEEGTGWLLELLSEVQLQQYFLRLRDDLNITRLSHFEYVKNEDLEKIGMGRPGQRRLWEAVKRRKAMCKRKSWMSKVFSGKRLEAEFPSQHSQSTFRKPSPTPGSLPGEGTLQSLTCLIGEKDLRLLEKLGDGSFGVVRRGEWDAPAGKTVSVAVKCLKPDVLSQPEAMDDFIREVNAMHSLDHRNLIRLYGVVLTLPMKMVTELAPLGSLLDRLRKHQGHFLLGTLSRYAVQVAEGMAYLESKRFIHRDLAARNLLLATRDLVKIGDFGLMRALPQNDDHYVMQEHRKVPFAWCAPESLKTRTFSHASDTWMFGVTLWEMFTYGQEPWIGLNGSQILHKIDKEGERLPRPEDCPQDIYNVMVQCWAHKPEDRPTFVALRDFLLEAQPTDMRALQDFEEPDKLHIQMNDVITVIEGRAENYWWRGQNTRTLCVGPFPRNVVTSVAGLSAQDISQPLQNSFIHTGHGDSDPRHCWGFPDRIDELYLGNPMDPPDLLSVELSTSRPTQHLGRVKREPPPRPPQPAIFTQKTTYDPVSEDPDPLSSDFKRLGLRKPALPRGLWLAKPSARVPGTKADRSSGGEVTLIDFGEEPVVPTPRPCAPSLAQLAMDACSLLDKTPPQSPTRALPRPLHPTPVVDWDARPLPPPPAYDDVAQDEDDFEVCSINSTLVGAGLPAGPSQGETNYAFVPEQAQMPPALEDNLFLPPQGGGKPPSSVQTAEIFQALQQECMRQLQVPTGQLTPSPTPGGDDKPQVPPRVPIPPRPTRPRVELSPAPSGEEETSRWPGPASPPRVPPREPLSPQGSRTPSPLVPPGSSPLPHRLSSSPGKTMPTTQSFASDPKYATPQVIQAPGPRAGPCILPIVRDGRKVSSTHYYLLPERPPYLERYQRFLREAQSPEEPAALPVPPLLPPPSTPAPAAPTATVRPMPQAAPDPKANFSTNNSNPGARPPSLRAAARLPQRGCPGDGQEAARPADKVQMLQAMVHGVTTEECQAALQSHSWSVQRAAQYLKVEQLFGLGLRPRVECHKVLEMFDWNLEQAGCHLLGSCGPAHHKR
|
Non-receptor tyrosine-protein and serine/threonine-protein kinase that is implicated in cell spreading and migration, cell survival, cell growth and proliferation. Transduces extracellular signals to cytosolic and nuclear effectors. Phosphorylates AKT1, AR, MCF2, WASL and WWOX. Implicated in trafficking and clathrin-mediated endocytosis through binding to epidermal growth factor receptor (EGFR) and clathrin. Binds to both poly- and mono-ubiquitin and regulates ligand-induced degradation of EGFR, thereby contributing to the accumulation of EGFR at the limiting membrane of early endosomes. Downstream effector of CDC42 which mediates CDC42-dependent cell migration via phosphorylation of BCAR1. May be involved both in adult synaptic function and plasticity and in brain development. Activates AKT1 by phosphorylating it on 'Tyr-176'. Phosphorylates AR on 'Tyr-267' and 'Tyr-363' thereby promoting its recruitment to androgen-responsive enhancers (AREs). Phosphorylates WWOX on 'Tyr-287'. Phosphorylates MCF2, thereby enhancing its activity as a guanine nucleotide exchange factor (GEF) toward Rho family proteins. Contributes to the control of AXL receptor levels. Confers metastatic properties on cancer cells and promotes tumor growth by negatively regulating tumor suppressor such as WWOX and positively regulating pro-survival factors such as AKT1 and AR.
|
O54968
|
NF2L2_RAT
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Nuclear factor erythroid 2-related factor 2 (NF-E2-related factor 2) (NFE2-related factor 2) (Nuclear factor, erythroid derived 2, like 2)
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MMDLELPPPGLQSQQDMDLIDILWRQDIDLGVSREVFDFSQRQKDYELEKQKKLEKERQEQLQKEQEKAFFAQLQLDEETGEFLPIQPAQHIQTDTSGSVSYSQVAHIPKQDALYFEDCMQLLAETFPFVDDHEVSSPTFQSLALDIPSHVESSVFTTPDQAQSLDSSLETAMTDLSSIQQDMEQVWQELFSIPELQCLNTENKQQAETTTVPSPEATLTEMDSNYHFYSSIPSLEKEVDSCSPHFLHGFEDSFSSILSTDDASQLNSLDSNPTLNTDFGDEFYSAFLAEPSGGGSMPSSAAISQSLSELLGGPIEGCDLSLCKAFNQKHTEGTVEFNDSDSGISLNTSPSRASPEHSVESSIYGDPPPGFSDSEMEELDSAPGSVKQNGPKAQPTHSSGDTVQPLSPAQGHSAAVHESQCENTTKKEVPVSPGHQKVPFTKDKHSSRLEAHLTRDELRAKALHIPFPVEKIINLPVDDFNEMMSKEQFNEAQLALIRDIRRRGKNKVAAQNCRKRKLENIVELEQDLGHLKDEREKLLREKGENDRNLHLLKRKLSTLYLEVFSMLRDEDGKPYSPSEYSLQQTRDGNVFLVPKSKKPDTKKN
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Transcription factor that plays a key role in the response to oxidative stress: binds to antioxidant response (ARE) elements present in the promoter region of many cytoprotective genes, such as phase 2 detoxifying enzymes, and promotes their expression, thereby neutralizing reactive electrophiles. In normal conditions, ubiquitinated and degraded in the cytoplasm by the BCR(KEAP1) complex. In response to oxidative stress, electrophile metabolites inhibit activity of the BCR(KEAP1) complex, promoting nuclear accumulation of NFE2L2/NRF2, heterodimerization with one of the small Maf proteins and binding to ARE elements of cytoprotective target genes. The NFE2L2/NRF2 pathway is also activated in response to selective autophagy: autophagy promotes interaction between KEAP1 and SQSTM1/p62 and subsequent inactivation of the BCR(KEAP1) complex, leading to NFE2L2/NRF2 nuclear accumulation and expression of cytoprotective genes (By similarity). May also be involved in the transcriptional activation of genes of the beta-globin cluster by mediating enhancer activity of hypersensitive site 2 of the beta-globin locus control region (By similarity). Also plays an important role in the regulation of the innate immune response. It is a critical regulator of the innate immune response and survival during sepsis by maintaining redox homeostasis and restraint of the dysregulation of pro-inflammatory signaling pathways like MyD88-dependent and -independent and TNF-alpha signaling. Suppresses macrophage inflammatory response by blocking pro-inflammatory cytokine transcription and the induction of IL6. Binds to the proximity of pro-inflammatory genes in macrophages and inhibits RNA Pol II recruitment. The inhibition is independent of the Nrf2-binding motif and reactive oxygen species level (By similarity). Represses antiviral cytosolic DNA sensing by suppressing the expression of the adapter protein STING1 and decreasing responsiveness to STING1 agonists while increasing susceptibility to infection with DNA viruses (By similarity).
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O54972
|
MTG16_MOUSE
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Protein CBFA2T3 (Eight twenty one protein 2) (MTG8-related protein 2) (Protein ETO-2)
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MSQASTTTLESGALLSGPRGLQYGSPAHRKEKAAAMPDSPAEVKTQPRSTPPSMPPPPPTSSQGATRPPSFTPHTHGEDGPATSLPHGRFHGCLKWSMVCLLMNGSSHSPTAIHGAPSTPNGFSNGPATSSTASLSTQHLPPACGARQLSKLKRFLTTLQQFGSDISPEIGERVRTLVLGLVNSTLTIEEFHAKLQEATNFPLRPFVIPFLKANLPLLQRELLHCARLAKQTPAQYLAQHEQLLLDASATSPVDSSELLLEVNENGKRRTPDRTKENGSDRDPLHPDHLSKRSCTLSPAQRCSPSNGLPHPTPPPPPHYRLEDMAMAHHFRDSYRHPDPRELRERHRPLAIPGSRQEEVIDHRLTEREWAEEWKHLNSLLNCIMDMVEKTRRSLTVLRRCQEADREELNHWIRCYSDSEEGKKGPTPISARSLNSCSGPEGSQLDVHRDFTPRTLSGYMPEEIWRKAEEAVNEVKRQAMSELQKAVSDAERKAHELITTERAKMERALAEAKRQASEDALTVINQQEDSSESCWNCGRKASETCSGCNAARYCGSFCQHKDWEKHHHVCGQSLQGPAAAVADPLPGQPDATASPSEAGSAGPSRPCSPGPPGPLDAAVPR
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Transcriptional corepressor which facilitates transcriptional repression via its association with DNA-binding transcription factors and recruitment of other corepressors and histone-modifying enzymes. Can repress the expression of MMP7 in a ZBTB33-dependent manner. Reduces the protein levels and stability of the transcriptinal regulator HIF1A interacts with EGLN1 and promotes the HIF1A prolyl hydroxylation-dependent ubiquitination and proteasomal degradation pathway. Contributes to inhibition of glycolysis and stimulation of mitochondrial respiration by down-regulating the expression of glycolytic genes including PFKFB3, PFKFB4, PDK1, PFKP, LDHA and HK1 which are direct targets of HIF1A (By similarity). Regulates the proliferation and the differentiation of erythroid progenitors by repressing the expression of TAL1 target genes. Plays a role in granulocyte differentiation.
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O54975
|
XPP1_RAT
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Xaa-Pro aminopeptidase 1 (EC 3.4.11.9) (Aminoacylproline aminopeptidase) (Cytosolic aminopeptidase P) (Soluble aminopeptidase P) (sAmp) (X-Pro aminopeptidase 1) (X-prolyl aminopeptidase 1, soluble)
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MAPKVTSELLRQLRQAMRNSECVAEPIQAYIIPSGDAHQSEYIAPCDCRRAFVSGFDGSAGTAIITEEHAAMWTDGRYFLQAAKQMDNNWTLMKMGLKDTPTQEDWLVSVLPEGSRVGVDPLIIPTDYWKKMAKVLRSAGHHLVPVKENLVDKIWTDRPERPCKPLLTLGLDYTGISWKEKVADLRLKMAERSIVWFVVTALDEIAWLFNLRGSDVEHNPVFFSYAIIGLERIMLFIDGDRIDAPGVKQHLLLDLGLEAEYKIQVLPYKSILSELKTLCADLSPREKVWVSDKASYAVSEAIPKDHRCCMPYTPICIAKAVKNSAESAGMRRAHIKDAVALCELFNWLEQEVPKGGVTEISAADKAEEFRRQQADFVDLSFPTISSTGPNGAIIHYAPIPETNRTLSLDEVYLIDSGAQYKDGTTDVTRTMHFGTPTAYEKECFTYVLKGHIAVSAAVFPTGTKGHLLDSFARSALWDSGLDYLHGTGHGVGSFLNVHEGPCGISYKTFSDEPLEAGMIVTDEPGYYEDGAFGIRIENVVLVVPAKTKYNFNNRGSLTFEPLTLVPIQTKMIDVDALTDKECDWLNSYHQTCRDVIGKELQTQGRQEALEWLLRETEPISRQH
|
Metalloaminopeptidase that catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro. Contributes to the degradation of bradykinin (By similarity).
|
O54980
|
SNG2_RAT
|
Synaptogyrin-2 (Cellugyrin)
|
MESGAYGAANAGGSFDLRRYVSQPQVVTRLVSMVLALIVFSCIFGEGYINLHSSDQLHCVFNRNEDACRYGSAIGVLAFLASAFFLVVDAFFSQISNATDRKYLVIGDLLFSALWTFLWFVGFCFLTNQWAATKPDDVLVGADSARAAITFSFFSIFSWGVLASLAYQRYKAGVDAFIQNYVDPTPDPTTAYASYPSASVENYQQPPFTQNVETTEGYQPPPVY
|
May play a role in regulated exocytosis. In neuronal cells, modulates the localization of synaptophysin/SYP into synaptic-like microvesicles and may therefore play a role in the formation and/or the maturation of this vesicles. May also play a role in GLUT4 storage and transport to the plasma membrane.
|
O54982
|
KCNU1_MOUSE
|
Potassium channel subfamily U member 1 (Calcium-activated potassium channel subunit alpha-3) (Calcium-activated potassium channel, subfamily M subunit alpha-3) (Pore-forming subunit of the sperm-specific alkalization activated K(+) current) (KSper) (Slowpoke homolog 3) (mSlo3) (pH-sensitive maxi potassium channel)
|
MSQTLLDSLNQKELTETSCTIEIQAAFILSSLATFFGGLIILFLFRIALKSSRSWKYVKGPRGLLELFSSRRIEANPLRKLYFHGVFRQRIEMLLSAQTVVGQVLVILVFVLSIGSLVIYFINSMDPVRRCSSYEDKIVHGDLSFNAFFSFYFGLRFWAAEDKIKFWLEMNSIVDIFTIPPTFISYYLKSNWLGLRFLRALRLLELPKILQILQVIKTSNSVKLSKLLSIVISTWFTAAGFLHLVENSGDPWLNGRNSQTMSYFESIYLVTATMSTVGFGDVVAKTSLGRIFIVFFTLGSLILFANYIPEMVELFSTRKKYTKPYEAVKGKKFIVVCGNITVDSVTAFLRNFLHWKSGEINIEIVFLGETLPCLELETLLKCHTSCTNFVCGTALKFEDLKRVAVENSEACLILANHFCSDLHDEDNSNIMRVLSIKNYYPQTRVIIQILQSQNKVFLSKIPNWDWSAGDNILCFAELKLGFIAQGCLVPGLCTFLTTLFIEQNQKVFPKHPWQKHFLNGLKNKILTQRLSNDFVGMTFPQVSRLCFVKLNLMLIAIQHKPFFHSCCTLILNPSSQVRLNKDTLGFFIADSSKAVKRAFFYCSNCHSDVCNPELIGKCNCKIKSRQQLIAPTIMVMKSSLTDFTTSSHIHASMSTEIHTCFSREQPSLITITTNRPTTNDTVDDTDMLDSSGMFHWCRAMPLDKVVLKRSEKAKHEFQNHIVVCVFGDAQCTLVGLRNFVMPLRASNYTRQELKDIVFIGSLEYFQREWRFLRNFPKIHIMPGSALYMGDLIAVNVEQCSMCVILATPYKALSSQILVDTEAIMATLNIQSLRITSPTPGSSKSEVKPSSAFDSKERKQRYKQIPILTELKNPSNIHFIEQMGGLDGMLKGTSLHLSTSFSTGAVFSDTFLDSLLATSFYNYHVVELLQMLVTGGISSEMEHYLVKEKPYKTTDDYEAIKSGRTRCKLGLLSLDQTVLSGINPRKTFGQLFCGSLDNFGILCVGLYRMIDEEEPSQEHKRFVITRPSNECHLLPSDLVFCAIPFNTTCGKSDSSPSIQAQNNSTNATTPLAQGSNFFDSHHADESHDLYPVDDTGERWSQHHHSRVYPLDTLDASDIVQEK
|
Testis-specific potassium channel activated by both intracellular pH and membrane voltage that mediates export of K(+). Represents the primary spermatozoan K(+) current. In contrast to KCNMA1/SLO1, it is not activated by Ca(2+) or Mg(2+). Critical for fertility. May play an important role in sperm osmoregulation required for the acquisition of normal morphology and motility when faced with osmotic challenges, such as those experienced after mixing with seminal fluid and entry into the vagina.
|
O54983
|
CRYM_MOUSE
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Ketimine reductase mu-crystallin (EC 1.5.1.25) (NADP-regulated thyroid-hormone-binding protein)
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MKRAPAFLSAEEVQDHLRSSSLLIPPLEAALANFSKGPDGGVMQPVRTVVPVAKHRGFLGVMPAYSAAEDALTTKLVTFYEGHSNTAVPSHQASVLLFDPSNGSLLAVMDGNVITAKRTAAVSAIATKLLKPPGSDVLCILGAGVQAYSHYEIFTEQFSFKEVRMWNRTRENAEKFASTVQGDVRVCSSVQEAVTGADVIITVTMATEPILFGEWVKPGAHINAVGASRPDWRELDDELMRQAVLYVDSREAALKESGDVLLSGADIFAELGEVISGAKPAHCEKTTVFKSLGMAVEDLVAAKLVYDSWSSGK
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Specifically catalyzes the reduction of imine bonds in brain substrates that may include cystathionine ketimine (CysK) and lanthionine ketimine (LK). Binds thyroid hormone which is a strong reversible inhibitor. Presumably involved in the regulation of the free intracellular concentration of triiodothyronine and access to its nuclear receptors (By similarity).
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O54988
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SLK_MOUSE
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STE20-like serine/threonine-protein kinase (STE20-like kinase) (mSLK) (EC 2.7.11.1) (Etk4) (STE20-related kinase SMAK) (STE20-related serine/threonine-protein kinase) (STE20-related kinase) (Serine/threonine-protein kinase 2)
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MSFFNFRKIFKLGSEKKKKQYEHVKRDLNPEEFWEIIGELGDGAFGKVYKAQNKETNVLAAAKVIDTKSEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEFCAGGAVDAVMLELERPLTESQIQVVCKQTLEALNYLHDNKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRTIQRRDSFIGTPYWMAPEVVMCETSKDRPYDYKADVWSLGITLIEMAEIEPPHHELNPMRVLLKIAKSEPPTLAQPSKWSSNFKDFLRKCLEKNVDARWTTSQLLQHPFVTVDSNKPVRELIAEAKAEVTEEVEDGKEEDEEEEAENALPIPANKRASSDLSIASSEEDKLSQNACILESVSERTEQSTSEDKFSNKILNEKPTTDGPEKAVDEHASDVNLETGAELNDQTVGIHENGREKKRPKLENLPDTQDQQTVDVNSVSEENENNRVTLETNTDCLKPEEDRNKENQETLESKLIQSEEINDTHIQTMDLVSQETGEKEADFQAVDNEVGLTKEETQEKLGKDGTAQKVITSDRSSEVGTDEALDDTQKAAELSKAAQSGEGDEALAPTQTLAEKPTEGPEAGGAEEEPPGGERVEDKQPEQQPAVCEAEGQLTSTSETTRATLEQPETDEVEQVSESNSIEELERLVVTGAEARALGSEGEAAATEVDLERKENAQKVPVKAESQAPAASQPSEPHPVLIPSININSETTENKEEMGALPKPETILPPEPEHEKGNDTDSGTGSTVENSSGDLNLSISSFLSKAKDSGSVSLQETRRQKKTLKKTRKFIVDGVEVSVTTSKIVTDSDSKTEELRFLRRQELRELRLLQKEEQRAQQQLNGKLQQQREQIFRRFEQEMLSKKRQYDQEIENLEKQQKQTIERLEQEHTNRLRDEAKRIKGEQEKELSKFQNVLKNRKKEVMNEVEKAPRELRRELTKRRKEELAQSQHAQEQEFVQKQQQELDGSLKKIIQQQKAELANIERECLNNKQQLMRAREAAIWELEERHLQEKHQLLKQQLKDQYFMQRHQLLKRHEKETEQMQRYNQRLIEELKNRQTQERARLPKIQRSEAKTRMAMFKKSLRINSTATPDQDREKIKQFAAQEEKRQKNERMAQHQKHESQMRDLQLQCEANVRELHQLQNEKCHLLVEHETQKLKELDEEHSQELKEWREKLRPRKKTLEEEFARKLQEQEVFFKMTGESECLNPSAQSRISKFYPIPTLHSTGS
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Mediates apoptosis and actin stress fiber dissolution.
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O54990
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PROM1_MOUSE
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Prominin-1 (Antigen AC133 homolog) (Prominin-like protein 1) (CD antigen CD133)
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MALVFSALLLLGLCGKISSEGQPAFHNTPGAMNYELPTTKYETQDTFNAGIVGPLYKMVHIFLSVVQPNDFPLDLIKKLIQNKKFDISVDSKEPEIIVLALKIALYEIGVLICAILGLLFIILMPLVGCFFCMCRCCNKCGGEMHQRQKQNAPCRRKCLGLSLLVICLLMSLGIIYGFVANQQTRTRIKGTQKLAKSNFRDFQTLLTETPKQIDYVVEQYTNTKNKAFSDLDGIGSVLGGRIKDQLKPKVTPVLEEIKAMATAIKQTKDALQNMSSSLKSLQDAATQLNTNLSSVRNSIENSLSSSDCTSDPASKICDSIRPSLSSLGSSLNSSQLPSVDRELNTVTEVDKTDLESLVKRGYTTIDEIPNTIQNQTVDVIKDVKNTLDSISSNIKDMSQSIPIEDMLLQVSHYLNNSNRYLNQELPKLEEYDSYWWLGGLIVCFLLTLIVTFFFLGLLCGVFGYDKHATPTRRGCVSNTGGIFLMAGVGFGFLFCWILMILVVLTFVVGANVEKLLCEPYENKKLLQVLDTPYLLKEQWQFYLSGMLFNNPDINMTFEQVYRDCKRGRGIYAAFQLENVVNVSDHFNIDQISENINTELENLNVNIDSIELLDNTGRKSLEDFAHSGIDTIDYSTYLKETEKSPTEVNLLTFASTLEAKANQLPEGKPKQAFLLDVQNIRAIHQHLLPPVQQSLNTLRQSVWTLQQTSNKLPEKVKKILASLDSVQHFLTNNVSLIVIGETKKFGKTILGYFEHYLHWVFYAITEKMTSCKPMATAMDSAVNGILCGYVADPLNLFWFGIGKATVLLLPAVIIAIKLAKYYRRMDSEDVYDDVETVPMKNLEIGSNGYHKDHLYGVHNPVMTSPSRY
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May play a role in cell differentiation, proliferation and apoptosis. Binds cholesterol in cholesterol-containing plasma membrane microdomains and may play a role in the organization of the apical plasma membrane in epithelial cells. During early retinal development acts as a key regulator of disk morphogenesis. Involved in regulation of MAPK and Akt signaling pathways. In neuroblastoma cells suppresses cell differentiation such as neurite outgrowth in a RET-dependent manner.
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O54991
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CNTP1_MOUSE
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Contactin-associated protein 1 (Caspr) (Caspr1) (MHDNIV) (NCP1) (Neurexin IV) (Neurexin-4) (Paranodin)
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MMSLRLFSILLATVVSGAWGWGYYGCNEELVGPLYARSLGASSYYGLFTTARFARLHGISGWSPRIGDPNPWLQIDLMKKHRIRAVATQGAFNSWDWVTRYMLLYGDRVDSWTPFYQKGHNATFFGNVNDSAVVRHDLHYHFTARYIRIVPLAWNPRGKIGLRLGIYGCPYTSSILYFDGDDAISYRFQRGASQSLWDVFAFSFKTEEKDGLLLHTEGSQGDYVTLELQGAHLLLHMSLGSSPIQPRPGHTTVSLGGVLNDLSWHYVRVDRYGRDANFTLDGYAHHFVLNGDFERLNLENEIFIGGLVGAARKNLAYRHNFRGCIENVIYNRINIAEMAVMRHSRITFEGNVAFRCLDPVPHPINFGGPHNFVQVPGFPRRGRLAVSFRFRTWDLTGLLLFSHLGDGLGHVELMLSEGQVNVSIAQTGRKKLQFAAGYRLNDGFWHEVNFVAQENHAVISIDDVEGAEVRVSYPLLIRTGTSYFFGGCPKPASRWGCHSNQTAFHGCMELLKVDGQLVNLTLVEFRKLGYFAEVLFDTCGITDRCSPNMCEHDGRCYQSWDDFICYCELTGYKGVTCHEPLYKESCEAYRLSGKYSGNYTIDPDGSGPLKPFVVYCDIRENRAWTVVRHDRLWTTRVTGSSMDRPFLGAIQYWNASWEEVSALANASQHCEQWIEFSCYNSRLLNTAGGYPYSFWIGRNEEQHFYWGGSQPGIQRCACGLDQSCVDPALHCNCDADQPQWRTDKGLLTFVDHLPVTQVVVGDTNRSNSEAQFFLRPLRCYGDRNSWNTISFHTGAALRFPPIRANHSLDVSFYFRTSAPSGVFLENMGGPFCRWRRPYVRVELNTSRDVVFAFDIGNGDENLTVHSDDFEFNDDEWHLVRAEINVKQARLRVDHRPWVLRPMPLQTYIWLVYDQPLYVGSAELKRRPFVGCLRAMRLNGVTLNLEGRANASEGTFPNCTGHCTHPRFPCFHGGRCVERYSYYTCDCDLTAFDGPYCNHDIGGFFETGTWMRYNLQSALRSAAREFSHMLSRPVPGYEPGYVPGYDTPGYVPGYHGPGYRLPEYPRPGRPVPGYRGPVYNVTGEEVSFSFSTNSAPAVLLYVSSFVRDYMAVLIKEDGTLQLRYQLGTSPYVYQLTTRPVTDGQPHSVNITRVYRNLFIQVDYFPLTEQKFSLLVDSQLDSPKALYLGRVMETGVIDPEIQRYNTPGFSGCLSGVRFNNVAPLKTHFRTPRPMTAELAEAMRVQGELSESNCGAMPRLVSEVPPELDPWYLPPDFPYYHDDGWIAILLGFLVAFLLLGLVGMLVLFYLQNHRYKGSYHTNEPKATHDSHPGGKAPLPPSGPAQAPAPTPAPTQLPTPAPAPAPAPASGPGPRDQNLPQILEESRSE
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Required, with CNTNAP2, for radial and longitudinal organization of myelinated axons. Plays a role in the formation of functional distinct domains critical for saltatory conduction of nerve impulses in myelinated nerve fibers. Demarcates the paranodal region of the axo-glial junction. In association with contactin involved in the signaling between axons and myelinating glial cells.
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O54992
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MAPK5_MOUSE
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MAP kinase-activated protein kinase 5 (MAPK-activated protein kinase 5) (MAPKAP kinase 5) (MAPKAPK-5) (EC 2.7.11.1)
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MSEDSDMEKAIKETSILEEYSINWTQKLGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLHMMCATHPNIVQIIEVFANSVQFPHESSPRARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQIALALQHCHLLNIAHRDLKPENLLFKDNSLDAPVKLCDFGFAKVDQGDLMTPQFTPYYVAPQVLEAQRRHQKEKSGIIPTSPTPYTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDMRKKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNSTEALDNVLPSAQLMMDKAVVAGIQQAHAEQLANMRIQDLKVSLKPLHSVNNPILRKRKLLGTKPKDGIYIHDHENGTEDSNVALEKLRDVIAQCILPQAGKGENEDEKLNEVMQEAWKYNRECKLLRDALQSFSWNGRGFTDKVDRLKLAEVVKQVIEEQTLPHEPQ
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Tumor suppressor serine/threonine-protein kinase involved in mTORC1 signaling and post-transcriptional regulation. Phosphorylates FOXO3, ERK3/MAPK6, ERK4/MAPK4, HSP27/HSPB1, p53/TP53 and RHEB. Acts as a tumor suppressor by mediating Ras-induced senescence and phosphorylating p53/TP53. Involved in post-transcriptional regulation of MYC by mediating phosphorylation of FOXO3: phosphorylation of FOXO3 leads to promote nuclear localization of FOXO3, enabling expression of miR-34b and miR-34c, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent MYC translation. Acts as a negative regulator of mTORC1 signaling by mediating phosphorylation and inhibition of RHEB. Part of the atypical MAPK signaling via its interaction with ERK3/MAPK6 or ERK4/MAPK4: the precise role of the complex formed with ERK3/MAPK6 or ERK4/MAPK4 is still unclear, but the complex follows a complex set of phosphorylation events: upon interaction with atypical MAPK (ERK3/MAPK6 or ERK4/MAPK4), ERK3/MAPK6 (or ERK4/MAPK4) is phosphorylated and then mediates phosphorylation and activation of MAPKAPK5, which in turn phosphorylates ERK3/MAPK6 (or ERK4/MAPK4). Mediates phosphorylation of HSP27/HSPB1 in response to PKA/PRKACA stimulation, inducing F-actin rearrangement.
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O54998
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FKBP7_MOUSE
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Peptidyl-prolyl cis-trans isomerase FKBP7 (PPIase FKBP7) (EC 5.2.1.8) (23 kDa FK506-binding protein) (23 kDa FKBP) (FKBP-23) (FK506-binding protein 7) (FKBP-7) (Rotamase)
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MNLLFRLAVFLSLWCCSDAQGQTKEESTEEVKIEVLHRPENCSKTSRKGDLLNAHYDGYLAKDGSKFYCSRTQDEGHPKWFVLGVGHVIKGLDIAMMDMCPGEKRKVIIPPSFAYGKEGYAEGKIPPNATLMFEIELYAVTKGPRSIETFKQIDTDNDRQLSKAEIELYLQKDFEKDANPRDKSYQKAVLEDIFKKNDHNGDGFISPKEYNVHQHDEL
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PPIases accelerate the folding of proteins during protein synthesis.
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O55000
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PP1RA_RAT
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Serine/threonine-protein phosphatase 1 regulatory subunit 10 (MHC class I region proline-rich protein CAT53) (Phosphatase 1 nuclear targeting subunit) (Protein PNUTS)
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MGSGPIDPKELLKGLDSFLTRDGEVKSVDGIAKIFSLMKEARKMVSRCTYLNIILQTRAPEVLVKFIDVGGYKLLNSWLTYSKTTNNIPLLQQILLTLQHLPLTVDHLKQNNTAKLVKQLSKSSEDEELRKLASVLVSDWMAVIRSQSSTQPAEKDKKKRKEEGKSRTTLPERPLTEVKAETRAEEAPEKKKEKPKSLRTTAPSHAKFRSTGLELDTPSLVPVKKNSSTVVVSDKYNLKPIPLKRQSATAAPGDAAPPAEKKYKPLNTTPNTTKEIKVKIIPPQPMEGLGFLDALNSAPVPGIKIKKKKKVLSPTAAKPSPFEGKTSTEPSTAKPSSPEPAAPAEPMDTDRPGTPVPAVEVPELMDAASSEPGALDAKPVESPGDPNQLTRKGRKRKTVTWPEEGKLREYFYFELDETERVNVNKIKDFGEAAKREILSDRHAFETARRLSHDNMEEKVPWVCPRPLVLPSPLVIPGSNSQERYIQAEREKGILQELFLNKESPHEPDPEPYEPIPPKLIPLDEECAMDETPYVETLEPGGSGGSPDGAGGSKLPPVLANLMGSMGAGKSPQGPGGGGINVQEILTSIMGSPNNHPSEELLKQPDYSDKLKQMLVPHGLLGPGPVANGFPPGGPGGPKGMQHFPPGPGGPMPGPHGGPGGPVGPRLLGPPPPSRGGDPFWDGPGDPMRGGPMRGGPGPGPGPYHRGRGGRGGNEPPPPPPFRGARGGRSGGGPPNGRGGPGGGGMVGGGGHRPHEGPGGSMGSGHRSHEGPGGSMGSGHRSHEGPGHGGPHGHRPHDVPSHRGHDHRGPPPHEHRGHDGHGGGGHRGHDGGHSHGGDMSNRPVCRHFMMKGNCRYENNCAFYHPGVNGPPLP
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Scaffold protein which mediates the formation of the PTW/PP1 phosphatase complex by providing a binding platform to each component of the complex. The PTW/PP1 phosphatase complex plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Mediates interaction of WDR82 and PPP1CA. Inhibitor of PPP1CA and PPP1CC phosphatase activities. Has inhibitory activity on PPP1CA only when phosphorylated. Binds to mRNA, single-stranded DNA (ssDNA), poly(A) and poly(G) homopolymers.
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O55003
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BNIP3_MOUSE
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BCL2/adenovirus E1B 19 kDa protein-interacting protein 3
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MSQSGEENLQGSWVELHFSNGNGSSVPASVSIYNGDMEKILLDAQHESGRSSSKSSHCDSPPRSQTPQDTNRAEIDSHSFGEKNSTLSEEDYIERRREVESILKKNSDWIWDWSSRPENIPPKEFLFKHPKRTATLSMRNTSVMKKGGIFSADFLKVFLPSLLLSHLLAIGLGIYIGRRLTTSTSTF
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Apoptosis-inducing protein that can overcome BCL2 suppression. May play a role in repartitioning calcium between the two major intracellular calcium stores in association with BCL2 (By similarity). Involved in mitochondrial quality control via its interaction with SPATA18/MIEAP: in response to mitochondrial damage, participates in mitochondrial protein catabolic process (also named MALM) leading to the degradation of damaged proteins inside mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane may play a critical role in the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix (By similarity). The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix (By similarity). Plays an important role in the calprotectin (S100A8/A9)-induced cell death pathway (By similarity).
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O55005
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ROBO1_RAT
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Roundabout homolog 1
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MKWKHLPLLVMISLLTLSKKHLLLAQLIPDPEDLERGNDNGTPAPTSDNDDNSLGYTGSRLRQEDFPPRIVEHPSDLIVSKGEPATLNCKAEGRPTPTIEWYKGGERVETDKDDPRSHRMLLPSGSLFFLRIVHGRKSRPDEGVYICVARNYLGEAVSHNASLEVAILRDDFRQNPSDVMVAVGEPAVMECQPPRGHPEPTISWKKDGSPLDDKDERITIRGGKLMITYTRKSDAGKYVCVGTNMVGERESKVADVTVLERPSFVKRPSNLAVTVDDSAEFKCEARGDPVPTFGWRKDDGELPKSRYEIRDDHTLKIRKVTAGDMGSYTCVAENMVGKAEASATLTVQEPPHFVVKPRDQVVALGRTVTFQCEATGNPQPAIFWRREGSQNLLFSYQPPQSSSRFSVSQTGDLTVTNVQRSDVGYYICQTLNVAGSIITKAYLEVTDVIADRPPPVIRQGPVNQTVAVDGTLTLSCVATGSPVPTILWRKDGVLVSTQDSRIKQLESGVLQIRYAKLGDTGRYTCTASTPSGEATWSAYIEVQEFGVPVQPPRPTDPNLIPSAPSKPEVTDVSKNTVTLLWQPNLNSGATPTSYIIEAFSHASGSSWQTVAENVKTETFAIKGLKPNAIYLFLVRAANAYGISDPSQISDPVKTQDVPPTTQGVDHKQVQRELGNVVLHLHNPTILSSSSVEVHWTVDQQSQYIQGYKILYRPSGASHGESEWLVFEVRTPTKNSVVIPDLRKGVNYEIKARPFFNEFQGADSEIKFAKTLEERPSAPPRSVTVSKNDGNGTAILVTWQPPPEDTQNGMVQEYKVWCLGNETRYHINKTVDGSTFSVVIPFLVPGIRYSVEVAASTGAGPGVKSEPQFIQLDSHGNPVSPEDQVSLAQQISDVVKQPAFIAGIGAACWIILMVFSIWLYRHRKKRNGLSSTYAGIRKVPSFTFTPTVTYQRGGEAVSSGGRPGLLNISEPATQPWLADTWPNTGNSHNDCSINCCTASNGNSDSNLTTYSRPADCIANYNNQLDNKQTNLMLPESTVYGDVDLSNKINEMKTFNSPNLKDGRFVNPSGQPTPYATTQLIQANLINNMNNGGGDSSEKHWKPPGQQKQEVAPIQYNIMEQNKLNKDYRANDTILPTIPYNHSYDQNTGGSYNSSDRGSSTSGSQGHKKGARTPKAPKQGGMNWADLLPPPPAHPPPHSNSEEYSMSVDESYDQEMPCPVPPARMYLQQDELEEEEAERGPTPPVRGAASSPAAVSYSHQSTATLTPSPQEELQPMLQDCPEDLGHMPHPPDRRRQPVSPPPPPRPISPPHTYGYISGPLVSDMDTDAPEEEEDEADMEVAKMQTRRLLLRGLEQTPASSVGDLESSVTGSMINGWGSASEEDNISSGRSSVSSSDGSFFTDADFAQAVAAAAEYAGLKVARRQMQDAAGRRHFHASQCPRPTSPVSTDSNMSAAVIQKARPTKKQKHQPGHLRREAYTDDLPPPPVPPPAIKSPSVQSKAQLEARPIMGPKLASIEARADRSSDRKGGSYKGREALDGRQVTDLRTSPGDPREAQEQPNEGKARGTKTAKRDLPPAKTHLIPEDILPYCRPTFPTSNNPRDPSSSSSMSSRGSGSRQREQANVGRRNMAEMQVLGGFERGDENNEELEETES
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Receptor for SLIT1 and SLIT2 that mediates cellular responses to molecular guidance cues in cellular migration, including axonal navigation at the ventral midline of the neural tube and projection of axons to different regions during neuronal development. Interaction with the intracellular domain of FLRT3 mediates axon attraction towards cells expressing NTN1 (By similarity). In axon growth cones, the silencing of the attractive effect of NTN1 by SLIT2 may require the formation of a ROBO1-DCC complex (By similarity). Plays a role in the regulation of cell migration via its interaction with MYO9B inhibits MYO9B-mediated stimulation of RHOA GTPase activity, and thereby leads to increased levels of active, GTP-bound RHOA (By similarity). May be required for lung development (By similarity).
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O55012
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PICAL_RAT
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Phosphatidylinositol-binding clathrin assembly protein (Clathrin assembly lymphoid myeloid leukemia protein) (rCALM)
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MSGQSLTDRITAAQHSVTGSAVSKTVCKATTHEIMGPKKKHLDYLIQCTNEMNVNIPQLADSLFERTTNSSWVVVFKSLITTHHLMVYGNERFIQYLASRNTLFNLSNFLDKSGLQGYDMSTFIRRYSRYLNEKAVSYRQVAFDFTKVKRGADGVMRTMNTEKLLKTVPIIQNQMDALLDFNVNSNELTNGVINAAFMLLFKDAIRLFAAYNEGIINLLEKYFDMKKNQCKEGLDIYKKFLTRMTRISEFLKVAEQVGIDRGDIPDLSQAPSSLLDALEQHLASLEGKKIKDSTAASRATTLSNAVSSLASTGLSLTKVDEREKQAALEEEQARLKALKEQRLKELAKKPHTSLTTAASPVSTSAGGIMTAPAIDIFSTPSSSNSTSKLPNDLLDLQQPTFHPSVHAMSAAPQVASTWGDAVDDAIPSLNPFLTKSSGDVHLPISSDVSTFTTRTPTHEMFVGFSPSPVTQPHPSAGLNVDFESVFGNKSTNVAVDSGGGLLKPTVASQNQSLPVAKLPPNKLVSDDLDSSLANLVGNLGIGNGTTKNDVSCSQPGEKKLTGGSNWQPKVAPTTAWSAATMAPPVMAYPATTPTGMIGYGIPPQMGSVPVMTQPTLIYSQPVMRPPNPFGPVPGAQIQFM
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Cytoplasmic adapter protein that plays a critical role in clathrin-mediated endocytosis which is important in processes such as internalization of cell receptors, synaptic transmission or removal of apoptotic cells. Recruits AP-2 and attaches clathrin triskelions to the cytoplasmic side of plasma membrane leading to clathrin-coated vesicles (CCVs) assembly. Furthermore, regulates clathrin-coated vesicle size and maturation by directly sensing and driving membrane curvature. In addition to binding to clathrin, mediates the endocytosis of small R-SNARES (Soluble NSF Attachment Protein REceptors) between plasma membranes and endosomes including VAMP2, VAMP3, VAMP4, VAMP7 or VAMP8. In turn, PICALM-dependent SNARE endocytosis is required for the formation and maturation of autophagic precursors. Modulates thereby autophagy and the turnover of autophagy substrates such as MAPT/TAU or amyloid precursor protein cleaved C-terminal fragment (APP-CTF).
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O55013
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TPPC3_MOUSE
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Trafficking protein particle complex subunit 3 (BET3 homolog)
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MSRQANRGTESKKMSSELFTLTYGALVTQLCKDYENDEDVNKQLDRMGYNIGVRLIEDFLARSNVGRCHDFRETADVIAKVAFKMYLGITPSITNWSPAGDEFSLILENNPLVDFVELPDNHSALIYSNLLCGVLRGALEMVQMAVEAKFVQDTLKGDGVTEIRMRFIRRIEDNLPAGEE
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May play a role in vesicular transport from endoplasmic reticulum to Golgi.
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O55017
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CAC1B_MOUSE
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Voltage-dependent N-type calcium channel subunit alpha-1B (Brain calcium channel III) (BIII) (Calcium channel, L type, alpha-1 polypeptide isoform 5) (Voltage-gated calcium channel subunit alpha Cav2.2)
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MVRFGDELGGRYGGTGGGERARGGGAGGAGGPGQGGLPPGQRVLYKQSIAQRARTMALYNPIPVKQNCFTVNRSLFVFSEDNVVRKYAKRITEWPPFEYMILATIIANCIVLALEQHLPDGDKTPMSERLDDTEPYFIGIFCFEAGIKIIALGFVFHKGSYLRNGWNVMDFVVVLTGILATAGTDFDLRTLRAVRVLRPLKLVSGIPSLQVVLKSIMKAMVPLLQIGLLLFFAILMFAIIGLEFYMGKFHKACFPNSTDTEPVGDFPCGKDPPARQCDGDTECREYWPGPNFGITNFDNILFAILTVFQCITMEGWTDILYNTNDAAGNTWNWLYFIPLIIIGSFFMLNLVLGVLSGEFAKERERVENRRAFLKLRRQQQIERELNGYLEWIFKAEEVMLAEEDKNAEEKSPLDVLKRAATKKSRNDLIHAEEGEDRFVDLCAVGSPFARASLKSGKTESSSYFRRKEKMFRFFIRRMVKAQSFYWVVLCVVALNTLCVAMVHYNQPQRLTTALYFAEFVFLGLFLTEMSLKMYGLGPRSYFRSSFNCFDFGVIVGSIFEVVWAAIKPGTSFGISVLRALRLLRIFKVTKYWNSLRNLVVSLLNSMKSIISLLFLLFLFIVVFALLGMQLFGGQFNFQDETPTTNFDTFPAAILTVFQILTGEDWNAVMYHGIESQGGVSKGMFSSFYFIVLTLFGNYTLLNVFLAIAVDNLANAQELTKDEEEMEEAANQKLALQKAKEVAEVSPMSAANISIAARQQNSAKARSVWEQRASQLRLQNLRASCEALYSEMDPEERLRYASTRHVRPDMKTHMDRPLVVEPGRDGLRGPVGSKSKPEGTEATESADLPRRHHRHRDRDKTSATAPAGGEQDRTESTETGAREERARPRRSHSKETPGADTQVRCERSRRHHRRGSPEEATEREPRRHRAHRHAQDSSKEGTAPVLVPKGERRARHRGPRTGPREAENNEEPTRRHRARHKVPPTLQPPEREAAEKESNAVEGDKETRNHQPKEPHCDLEAIAVTGVGPLHMLPSTCLQKVDEQPEDADNQRNVTRMGSQPSDPSTTVHVPVTLTGPPGETPVVPSGNMNLEGQAEGKKEAEADDVLRRGPRPIVPYSSMFCLSPTNLLRRFCHYIVTMRYFEMVILVVIALSSIALAAEDPVRTDSFRNNALKYMDYIFTGVFTFEMVIKMIDLGLLLHPGAYFRDLWNILDFIVVSGALVAFAFSSFMGGSKGKDINTIKSLRVLRVLRPLKTIKRLPKLKAVFDCVVNSLKNVLNILIVYMLFMFIFAVIAVQLFKGKFFYCTDESKELERDCRGQYLDYEKEEVEAQPRQWKKYDFHYDNVLWALLTLFTVSTGEGWPMVLKHSVDATYEEQGPSPGFRMELSIFYVVYFVVFPFFFVNIFVALIIITFQEQGDKVMSECSLEKNERACIDFAISAKPLTRYMPQNKQSFQYKTWTFVVSPPFEYFIMAMIALNTVVLMMKFYDAPYEYELMLKCLNIVFTSMFSMECILKIIAFGVLNYFRDAWNVFDFVTVLGSITDILVTEIANNFINLSFLRLFRAARLIKLLRQGYTIRILLWTFVQSFKALPYVCLLIAMLFFIYAIIGMQVFGNIALDDDTSINRHNNFRTFLQALMLLFRSATGEAWHEIMLSCLGNRACDPHANASECGSDFAYFYFVSFIFLCSFLMLNLFVAVIMDNFEYLTRDSSILGPHHLDEFIRVWAEYDPAACGRISYNDMFEMLKHMSPPLGLGKKCPARVAYKRLVRMNMPISNEDMTVHFTSTLMALIRTALEIKLAPAGTKQHQCDAELRKEISSVWANLPQKTLDLLVPPHKPDEMTVGKVYAALMIFDFYKQNKTTRDQTHQAPGGLSQMGPVSLFHPLKATLEQTQPAVLRGARVFLRQKSATSLSNGGAIQTQESGIKESLSWGTQRTQDALYEARAPLERGHSAEIPVGQSGTLAVDVQMQNMTLRGPDGEPQPGLESQGRAASMPRLAAETQPAPNASPMKRSISTLAPRPHGTQLCSTVLDRPPPSQASHHHHHRCHRRRDKKQRSLEKGPSLSVDPEGAPSTAAGPGLPHGEGSTACRRDRKQERGRSQERRQPSSSSSEKQRFYSCDRFGSREPPQLMPSLSSHPTSPTAALEPAPHPQGSGSVNGSPLMSTSGASTPGRGGRRQLPQTPLTPRPSITYKTANSSPVHFAEGQSGLPAFSPGRLSRGLSEHNALLQKEPLSQPLAPGSRIGSDPYLGQRLDSEASAHTLPEDTLTFEEAVATNSGRSSRTSYVSSLTSQSHPLRRVPNGYHCTLGLSTGVRARHSYHHPDQDHWC
|
Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. This alpha-1B subunit gives rise to N-type calcium currents. N-type calcium channels belong to the 'high-voltage activated' (HVA) group. They are involved in pain signaling. Calcium channels containing alpha-1B subunit may play a role in directed migration of immature neurons. Mediates Ca(2+) release probability at hippocampal neuronal soma and synaptic terminals (By similarity).
|
O55022
|
PGRC1_MOUSE
|
Membrane-associated progesterone receptor component 1 (mPR)
|
MAAEDVVATGADPSELEGGGLLHEIFTSPLNLLLLGLCIFLLYKIVRGDQPGASGDNDDDEPPPLPRLKRRDFTPAELRRFDGVQDPRILMAINGKVFDVTKGRKFYGPEGPYGVFAGRDASRGLATFCLDKEALKDEYDDLSDLTPAQQETLSDWDSQFTFKYHHVGKLLKEGEEPTVYSDDEEPKDETARKNE
|
Component of a progesterone-binding protein complex. Binds progesterone. Has many reported cellular functions (heme homeostasis, interaction with CYPs). Required for the maintenance of uterine histoarchitecture and normal female reproductive lifespan. Intracellular heme chaperone. Regulates heme synthesis via interactions with FECH and acts as a heme donor for at least some hemoproteins.
|
O55023
|
IMPA1_MOUSE
|
Inositol monophosphatase 1 (IMP 1) (IMPase 1) (EC 3.1.3.25) (D-galactose 1-phosphate phosphatase) (EC 3.1.3.94) (Inositol-1(or 4)-monophosphatase 1) (Lithium-sensitive myo-inositol monophosphatase A1)
|
MADPWQECMDYAVILARQAGEMIREALKNEMDVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPCHSFIGEESVAAGEKTVFTESPTWFIDPIDGTTNFVHRFPFVAVSIGFLVNKEMEFGIVYSCVEDKMYTGRKGKGAFCNGQKLQVSQQEDITKSLLVTELGSSRKPETLRIVLSNMEKLCSIPIHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVTEAGGVLMDVTGGPFDLMSRRIIAANSITLAKRIAKEIEIIPLQRDDES
|
Responsible for the provision of inositol required for synthesis of phosphatidylinositol and polyphosphoinositides and has been implicated as the pharmacological target for lithium action in brain. Has broad substrate specificity and can use myo-inositol monophosphates, myo-inositol 1,3-diphosphate, myo-inositol 1,4-diphosphate, scyllo-inositol-phosphate, D-galactose 1-phosphate, glucose-1-phosphate, glucose-6-phosphate, fructose-1-phosphate, beta-glycerophosphate, and 2'-AMP as substrates.
|
O55026
|
ENTP2_MOUSE
|
Ectonucleoside triphosphate diphosphohydrolase 2 (NTPDase 2) (EC 3.6.1.-) (CD39 antigen-like 1) (Ecto-ATP diphosphohydrolase 2) (Ecto-ATPDase 2) (Ecto-ATPase 2)
|
MAGKLVSLVPPLLLAAVGLAGLLLLCVPTQDVREPPALKYGIVLDAGSSHTSMFVYKWPADKENDTGIVGQHSSCDVRGGGISSYANDPSRAGQSLVECLEQALRDVPKDRYASTPLYLGATAGMRLLNLTSPEATAKVLEAVTQTLTRYPFDFRGARILSGQDEGVFGWVTANYLLENFIKYGWVGRWIRPRKGTLGAMDLGGASTQITFETTSPSEDPDNEVHLRLYGQHYRVYTHSFLCYGRDQVLQRLLASALQIHRFHPCWPKGYSTQVLLREVYQSPCTMGQRPQTFNSSATVSLSGTSNAALCRDLVSGLFNISSCPFSQCSFNGVFQPPVAGNFIAFSAFYYTVDFLKTVMGLPVGTLKQLEDATETTCNQTWAELQARVPGQQTRLPDYCAVAMFIHQLLSRGYRFDERSFRGVVFEKKAADTAVGWALGYMLNLTNLIPADLPGLRKGTHFSSWVALLLLFTVLILAALVLLLRQVRSAKSPGAL
|
In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Hydrolyzes ADP only to a marginal extent (By similarity).
|
O55028
|
BCKD_MOUSE
|
[3-methyl-2-oxobutanoate dehydrogenase [lipoamide]] kinase, mitochondrial (EC 2.7.11.4) (Branched-chain alpha-ketoacid dehydrogenase kinase) (BCKD-kinase) (BCKDHKIN)
|
MILTSVLGSGPRSWSSLWPLLGSSLSLRARSTSATDTHHVELARERSKTVTSFYNQSAIDVAAEKPSVRLTPTMMLYSGRSQDGSHLLKSGRYLQQELPVRIAHRIKGFRSLPFIIGCNPTILHVHELYIRAFQKLTDFPPIKDQADEAQYCQLVRQLLDDHKDVVTLLAEGLRESRKHIQDEKLVRYFLDKTLTSRLGIRMLATHHLALHEDKPDFVGIICTRLSPKKIIEKWVDFARRLCEHKYGNAPRVRINGHVAARFPFIPMPLDYILPELLKNAMRATMESHLDTPYNVPDVVITIANNDIDLIIRISDRGGGIAHKDLDRVMDYHFTTAEASTQDPRINPLFGHLDMHSGGQSGPMHGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRLRHIDGREESFRI
|
Catalyzes the phosphorylation and inactivation of the branched-chain alpha-ketoacid dehydrogenase complex, the key regulatory enzyme of the valine, leucine and isoleucine catabolic pathways. Key enzyme that regulate the activity state of the BCKD complex.
|
O55029
|
COPB2_MOUSE
|
Coatomer subunit beta' (Beta'-coat protein) (Beta'-COP) (p102)
|
MPLRLDIKRKLTARSDRVKSVDLHPTEPWMLASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNTLERVHMFEAHSDYIRCIAVHPTQPFILTSSDDMLIKLWDWDKKWSCSQVFEGHTHYVMQIVINPKDNNQFASASLDRTIKVWQLGSSSPNFTLEGHEKGVNCIDYYSGGDKPYLISGADDRLVKIWDYQNKTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIWHSSTYRLESTLNYGMERVWCVASLRGSNNVALGYDEGSIIVKLGREEPAMSMDANGKIIWAKHSEVQQANLKAMGDTEIKDGERLPLAVKDMGSCEIYPQTIQHNPNGRFVVVCGDGEYIIYTAMALRNKSFGSAQEFAWAHDSSEYAIRESNSIVKIFKNFKEKKSFKPDFGAESIYGGFLLGVRSVNGLAFYDWENTELIRRIEIQPKHIFWSDSGELVCIATEESFFILKYLSEKVLAAQETHEGVTEDGIEDAFEVLGEIQEIVKTGLWVGDCFIYTSSVNRLNYYVGGEIVTIAHLDRTMYLLGYIPKDNRLYLGDKELNIVSYSLLVSVLEYQTAVMRRDFSMADKVLPTIPKEQRTRVAHFLEKQGFKQQALTVSTDPEHRFELALQLGELKIAYQLAVEAESEQKWKQLAELAISKCQFSLAQECLHHAQDYGGLLLLATASGNASMVNKLAEGAERDGKNNVAFMSYFLQGKLDACLELLIRTGRLPEAAFLARTYLPSQVSRVVKLWRENLSKVNQKAAESLADPTEYENLFPGLKEAFVVEEWVKETHADLWPAKQYPLVTPNEERNVMEEAKGFQPSRPTAQQEPDGKPASSPVIMASQTTHKEEKSLLELEVDLDNLELEDIDTTDINLDEDILDD
|
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). This coatomer complex protein, essential for Golgi budding and vesicular trafficking, is a selective binding protein (RACK) for protein kinase C, epsilon type. It binds to Golgi membranes in a GTP-dependent manner.
|
O55033
|
NCK2_MOUSE
|
Cytoplasmic protein NCK2 (Growth factor receptor-bound protein 4) (NCK adaptor protein 2) (Nck-2) (SH2/SH3 adaptor protein NCK-beta)
|
MTEEVIVIAKWDYTAQQDQELDIRKNERLWLLDDSKTWWRVRNAANRTGYVPSNYVERKNSLKKGSLVKNLKDTLGLGKTRRKPSARDASPTPSTDAEYPANGSGADRIYDLNIPAFVKFAYVAEREDELSLVKGSRVTVMEKCSDGWWRGSFNGQIGWFPSNYVLEEADEAAAEAPSFLSLRRGTALSNGQGARVLHVVQTLYPFSSVTEEELSFEKGETMEVIEKPENDPEWWKCKNARGQVGLVPKNYVVVLSDGPALHPAHTPQISYTGPSASGRFAGREWYYGNVTRHQAECALNERGVEGDFLIRDSESSPSDFSVSLKASGRNKHFKVQLVDSVYCIGQRRFHSMDELVEHYKKAPIFTSEHGEKLYLVRALQ
|
Adapter protein which associates with tyrosine-phosphorylated growth factor receptors or their cellular substrates. Maintains low levels of EIF2S1 phosphorylation by promoting its dephosphorylation by PP1. Plays a role in ELK1-dependent transcriptional activation in response to activated Ras signaling (By similarity).
|
O55034
|
SPAG4_RAT
|
Sperm-associated antigen 4 protein (Outer dense fiber-associated protein SPAG4) (SUN domain-containing protein 4)
|
MRRNPRPGSAASSHNHTPNFYSENSNSSHSATSGDSNGRRSAGPELGEPDGRMARGSSCGEPALSSGVPGGDTWAGSSRPKLAPRSHNGQTACGAATVRGGASEPSGSPAVLEEQLNLLPILDLRQEMPPPPVSKSFLSLFFQVLSVFLSLVADGLVCVYREICSIRFLFTAVSLLSIFLAALWWGLLYLIPPLENEPKEMLTLSQYHHRVHSQGQQLQQLQAELSKLHKEVTSVRAAHSERVAKLVFQRLNEDFVRKPDYALSSVGASIDLEKTSSDYEDRNTAYFWNRLSFWNYARPPSVILEPDVFPGNCWAFEGEQGQVVIRLPGHVQLSDITLQHPPPTVAHTGGASSAPRDFAVFGLQADDDETEVFLGKFIFEVQKSEIQTFHLQNDPPSAFPKVKIQILSNWGHPRFTCLYRVRAHGVRISESAEDNAMGVTGGPH
|
Involved in spermatogenesis. Required for sperm head formation but not required to establish and maintain general polarity of the sperm head. Required for anchoring and organization of the manchette. Required for targeting of SUN3 and probably SYNE1 through a probable SUN1:SYNE3 LINC complex to the nuclear envelope and involved in accurate posterior sperm head localization of the complex. May anchor SUN3 the nuclear envelope. Involved in maintenance of the nuclear envelope integrity (By similarity). May assist the organization and assembly of outer dense fibers (ODFs), a specific structure of the sperm tail.
|
O55035
|
PPIG_RAT
|
Peptidyl-prolyl cis-trans isomerase G (PPIase G) (Peptidyl-prolyl isomerase G) (EC 5.2.1.8) (Cyclophilin G) (Matrin cyclophilin) (Matrin-cyp) (Rotamase G)
|
MGIKVQRPRCFFDIAINNQPAGRVVFELFSDVCPKTCENFRCLCTGEKGTGKSTQKPLHYKSCLFHRVVKDFMVQGGDFSEGNGRGGESIYGGFFEDESFAVKHNKEFLLSMANRGKDTNGSQFFITTKPTPHLDGHHVVFGQVISGQEVVREIENQKTDAASKPFAEVRILSCGELVPKSKVKKEEKKRHKSSSSSSSSDSDSSSDSQSSSDSSDSESASEEKSRKRKKKHRKNSRKHKKEKKKRKKSKKSPSSESEADNVDAQPQSTVRPEEIPPIPENRFLMRKSPPKADDKERKNRERERERECNPPNSQPASYQRRFLVTRFGRKIKGRGPRRYRTPSRSRSRDRFRRSETPPHWRQEMQRAQRMRVSSGERWIKGDKSELNEIKENQRSPVRVKEKKITDHRHMSESPNRKIEKEKKVKDHKSESKERDIRRNSEKDDKYNKNKVKKRGKSKSRSKSKERSKSKERDSKHSRHEDKRVRSRSKERDHETTKEKEKQLDSKGKDQERSRSKENSKQVESKSNEHDHSKSKEKDRRAQSRSRERDLTKSKHSYNSRTRERSRSRDRSRRVRSRSHDRDRSRSKEYHRYREQEYRRRGRSRSRDRRTPGRSRSKDRRRRRRDSRSSEREESQSRNKEKYRSQDSKSSHRKENSEGEKRMYSKSRDHSSSNNNREKKADIDQSPVSKTKQSSQDNEVKSSTLKNQEDEKTRSPVEKENQKSKGQENDHVHDKNKKCDHESSPGTDEDKSG
|
PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. May be implicated in the folding, transport, and assembly of proteins. May play an important role in the regulation of pre-mRNA splicing.
|
O55038
|
CXL13_MOUSE
|
C-X-C motif chemokine 13 (B lymphocyte chemoattractant) (CXC chemokine BLC) (Small-inducible cytokine B13)
|
MRLSTATLLLLLASCLSPGHGILEAHYTNLKCRCSGVISTVVGLNIIDRIQVTPPGNGCPKTEVVIWTKMKKVICVNPRAKWLQRLLRHVQSKSLSSTPQAPVSKRRAA
|
Strongly chemotactic for B-lymphocytes, weakly for spleen monocytes and macrophages but no chemotactic activity for granulocytes. Binds to BLR1/CXCR5. May play a role in directing the migration of B-lymphocytes to follicles in secondary lymphoid organs.
|
O55042
|
SYUA_MOUSE
|
Alpha-synuclein (Non-A beta component of AD amyloid) (Non-A4 component of amyloid precursor) (NACP)
|
MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQMGKGEEGYPQEGILEDMPVDPGSEAYEMPSEEGYQDYEPEA
|
Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release (By similarity). Participates as a monomer in synaptic vesicle exocytosis by enhancing vesicle priming, fusion and dilation of exocytotic fusion pores (By similarity). Mechanistically, acts by increasing local Ca(2+) release from microdomains which is essential for the enhancement of ATP-induced exocytosis (By similarity). Acts also as a molecular chaperone in its multimeric membrane-bound state, assisting in the folding of synaptic fusion components called SNAREs (Soluble NSF Attachment Protein REceptors) at presynaptic plasma membrane in conjunction with cysteine string protein-alpha/DNAJC5. This chaperone activity is important to sustain normal SNARE-complex assembly during aging (By similarity). Also plays a role in the regulation of the dopamine neurotransmission by associating with the dopamine transporter (DAT1) and thereby modulating its activity (By similarity).
|
O55043
|
ARHG7_RAT
|
Rho guanine nucleotide exchange factor 7 (Beta-Pix) (PAK-interacting exchange factor beta)
|
MTDNANSQLVVRAKFNFQQTNEDELSFSKGDVIHVTRVEEGGWWEGTHNGRTGWFPSNYVREIKPSEKPVSPKSGTLKSPPKGFDTTAINKSYYNVVLQNILETEHEYSKELQSVLSTYLWPLQTSEKLSSANTSYLMGNLEEISSFQQVLVQSLEECTKSPEAQQRVGGCFLSLMPQMRTLYLAYCANHPSAVSVLTEHSEDLGEFMETKGASSPGILVLTTGLSKPFMRLDKYPTLLKELERHMEDYHPDRQDIQKSMTAFKNLSAQCQEVRKRKELELQILTEPIRSWEGDDIKTLGSVTYMSQVTIQCAGSEEKNERYLLLFPNLLLMLSASPRMSGFIYQGKLPTTGMTITKLEDSENHRNAFEISGSMIERILVSCNNQQDLHEWVEHLQRQTKVTSVSNPTIKPHSVPSHTLPSHPLTPSSKHADSKPVALTPAYHTLPHPSHHGTPHTTISWGPLEPPKTPKPWSLSCLRPAPPLRPSAALCYKEDLSRSPKTMKKLLPKRKPERKPSDEEFAVRKSTAALEEDAQILKVIEAYCTSAKTRQTLNSSSRKESAPQVLLPEEEKIIVEETKSNGQTVIEEKSLVDTVYALKDEVQELRQDNKKMKKSLEEEQRARKDLEKLVRKVLKNMNDPAWDETNL
|
Acts as a RAC1 guanine nucleotide exchange factor (GEF) and can induce membrane ruffling. Functions in cell migration, attachment and cell spreading. Promotes targeting of RAC1 to focal adhesions. May function as a positive regulator of apoptosis. Downstream of NMDA receptors and CaMKK-CaMK1 signaling cascade, promotes the formation of spines and synapses in hippocampal neurons (By similarity).
|
O55044
|
G6PD_CRIGR
|
Glucose-6-phosphate 1-dehydrogenase (G6PD) (EC 1.1.1.49)
|
MAEQVALSRTQVCGILREELYQGDAFHQADTHIFIIMGASGDLAKKKIYPTIWWLFRDGLLPEDTFIVGYARSRLTVDDIRKQSEPFFKATPEERPKLEEFFARNSYVAGQYDDPASYKHLNSHMNALHQGMQANRLFYLALPPTVYEAVTKNIQETCMSQTGWNRIIVEKPFGRDLQSSNQLSNHISSLFREDQIYRIDHYLGKEMVQNLMVLRFANRIFGPIWNRDNIACVILTFKEPFGTEGRGGYFDEFGIIRDVMQNHLLQMLCLVAMEKPASTDSDDVRDEKVKVLKCISEVETSNVVLGQYVGNPNGEGEATNGYLDDPTVPRGSTTATFAAAVLYVENERWDGVPFILRCGKALNERKAEVRLQFRDVAGDIFHQQCKRNELVIRVQPNEAVYTKMMTKKPGMFFNPEESELDLTYGNRYKNVKLPDAYERLILDVFCGSQMHFVRSDELREAWRIFTPLLHKIDQEKPQPIPYVYGSRGPTEADELMKRVGFQYEGTYKWVNPHKL
|
Cytosolic glucose-6-phosphate dehydrogenase that catalyzes the first and rate-limiting step of the oxidative branch within the pentose phosphate pathway/shunt, an alternative route to glycolysis for the dissimilation of carbohydrates and a major source of reducing power and metabolic intermediates for fatty acid and nucleic acid biosynthetic processes.
|
O55047
|
TLK2_MOUSE
|
Serine/threonine-protein kinase tousled-like 2 (EC 2.7.11.1) (PKU-alpha) (Tousled-like kinase 2)
|
MMEELHSLDPRRQELLEARFTGVGVSKGPLNSESSNQSLCSVGSLSDKEVETPEKKQNDQRNRKRKAEPYDTSQGKGTPRGHKISDYFERRAEQPLYGLDGSAAKEASEEQSALPTLMSVMLAKPRLDTEQLAPRGAGLCFTFVSAQQNSPSSTGSGNTEHSCSSQKQISIQHRQTQSDLTIEKISALENSKNSDLEKKEGRIDDLLRANCDLRRQIDEQQKMLEKYKERLNRCVTMSKKLLIEKSKQEKMACRDKSMQDRLRLGHFTTVRHGASFTEQWTDGYAFQNLIKQQERINSQREEIERQRKMLAKRKPPAMGQAPPATNEQKQRKSKTNGAENETLTLAEYHEQEEIFKLRLGHLKKEEAEIQAELERLERVRNLHIRELKRIHNEDNSQFKDHPTLNDRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDSFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKPPIIHYDLKPGNILLVNGTACGEIKITDFGLSKIMDDDSYNSVDGMELTSQGAGTYWYLPPECFVVGKEPPKISNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDILQENTILKATEVQFPPKPVVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYLLPHIRKSVSTSSPAGAAIASTSGASNNSSSN
|
Serine/threonine-protein kinase involved in the process of chromatin assembly and probably also DNA replication, transcription, repair, and chromosome segregation (By similarity). Phosphorylates the chromatin assembly factors ASF1A and ASF1B (By similarity). Phosphorylation of ASF1A prevents its proteasome-mediated degradation, thereby enhancing chromatin assembly (By similarity). Negative regulator of amino acid starvation-induced autophagy (By similarity).
|
O55055
|
TRDMT_MOUSE
|
tRNA (cytosine(38)-C(5))-methyltransferase (EC 2.1.1.204) (DNA (cytosine-5)-methyltransferase-like protein 2) (Dnmt2) (DNA methyltransferase homolog MmuIIP) (DNA MTase homolog MmuIIP) (M.MmuIIP) (Met-2)
|
MEPLRVLELYSGIGGMHHALRESHIPAHVVAAIDVNTVANEVYKHNFPHTHLLSKTIEGISLEDFDKLSFNMILMSPPCQPFTRIGLQGDMTDPRTTSFLYILDILPRLQKLPKYILLENVKGFEVSSTRGLLIQTIEACGFQYQEFLLSPSSLGIPNSRLRYFLIAKLQSEPFPFQAPGQILMEFPKIVTVEPQKYAVVEESQPRVQRTGPRICAESSSTQSSGKDTILFKLETVEERDRKHQQDSDLSVQMLKDFLEDGDTDEYLLPPKLLLRYALLLDIVKPTSRRSMCFTKGYGSYIEGTGSVLQAAEDAQIENIYKSLPDLPPEEKIAKLSMLKLRYFTPKEIANLQGFPPEFGFPEKTTVKQRYRLLGNSLNVHVVAKLLTVLCEGFGNASESCHKMPLILDSNSKILS
|
Specifically methylates cytosine 38 in the anticodon loop of tRNA(Asp).
|
O55058
|
FBLN4_CRIGR
|
EGF-containing fibulin-like extracellular matrix protein 2 (Fibulin-4) (FIBL-4) (Protein H411)
|
MLPFASCLPGSLLLWALLLLLLGAASPQDSEEPDSYTECTDGYEWDADSQHCRDVNECLTIPEACKGEMKCINHYGGYLCLPRSAAVINDLHGEGPPPPVPPAQHPNPCPPGYEPDEQESCVDVDECAQALHDCRPSQDCHNLPGSYQCTCPDGYRKVGPECVDIDECRYRYCQHRCVNLPGSFRCQCEPGFQLGPNNRSCVDVNECDMGAPCEQRCFNSYGTFLCRCNQGYELHRDGFSCSDIDECSYSSYLCQYRCVNEPGRFSCHCPQGYQLLATRLCQDIDECETGAHQCSEAQTCVNFHGGYRCVDTNRCVEPYVQVSDNRCFCPVSNPLCREQPSSIVHRYMSITSERSVPADVFQIQATSVYPGAYNAFQIRAGNTQGDFYIRQINNVSAMLVLARPVTGPREYVLDLEMVTMNSLMSYRASSVLRLTVFVGAYTF
|
Plays a crucial role in elastic fiber formation in tissue, and in the formation of ultrastructural connections between elastic laminae and smooth muscle cells in the aorta, therefore participates in terminal differentiation and maturation of smooth muscle cell (SMC) and in the mechanical properties and wall integrity maintenance of the aorta. In addition, is involved in the control of collagen fibril assembly in tissue throught proteolytic activation of LOX leading to cross- linking of collagen and elastin. Also promotes ELN coacervation and participates in the deposition of ELN coacervates on to microfibrils but also regulates ELN cross- linking through LOX interaction. Moreover adheres to the cells through heparin binding in a calcium-dependent manner and regulates vascularlar smooth muscle cells proliferation through angiotensin signaling.
|
O55060
|
TPMT_MOUSE
|
Thiopurine S-methyltransferase (EC 2.1.1.67) (Thiopurine methyltransferase)
|
MSLDMKEHPDAEVQKNQVLTLEDWKEKWVTRHISFHQEQGHQLLKKHLDTFLKGQSGLRVFFPLCGKAIEMKWFADRGHTVVGVEISEIGIREFFAEQNLSYTEEPLAEIAGAKVFKSSSGSISLYCCSIFDLPRANIGKFDRIWDRGALVAINPGDHDRYADIILSLLRKEFQYLVAVLSYDPTKHAGPPFYVPSAELKRLFGTKCSMQCLEEVDALEERHKAWGLDYLFEKLYLLTEK
|
Catalyzes the S-methylation of thiopurine drugs such as 6-mercaptopurine (also called mercaptopurine, 6-MP or its brand name Purinethol) using S-adenosyl-L-methionine as the methyl donor. TPMT activity modulates the cytotoxic effects of thiopurine prodrugs. A natural substrate for this enzyme has yet to be identified.
|
O55070
|
DNSL3_MOUSE
|
Deoxyribonuclease gamma (DNase gamma) (EC 3.1.21.-) (DNase I homolog protein DHP2) (Deoxyribonuclease I-like 3) (DNase I-like 3) (Liver and spleen DNase) (LS-DNase) (LSD)
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MSLHPASPRLASLLLFILALHDTLALRLCSFNVRSFGASKKENHEAMDIIVKIIKRCDLILLMEIKDSSNNICPMLMEKLNGNSRRSTTYNYVISSRLGRNTYKEQYAFVYKEKLVSVKTKYHYHDYQDGDTDVFSREPFVVWFHSPFTAVKDFVIVPLHTTPETSVKEIDELVDVYTDVRSQWKTENFIFMGDFNAGCSYVPKKAWQNIRLRTDPKFVWLIGDQEDTTVKKSTSCAYDRIVLCGQEIVNSVVPRSSGVFDFQKAYDLSEEEALDVSDHFPVEFKLQSSRAFTNNRKSVSLKKRKKGNRS
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Has DNA hydrolytic activity. Is capable of both single- and double-stranded DNA cleavage, producing DNA fragments with 3'-OH ends (By similarity). Can cleave chromatin to nucleosomal units and cleaves nucleosomal and liposome-coated DNA. Acts in internucleosomal DNA fragmentation (INDF) during apoptosis and necrosis. The role in apoptosis includes myogenic and neuronal differentiation, and BCR-mediated clonal deletion of self-reactive B cells. Is active on chromatin in apoptotic cell-derived membrane-coated microparticles and thus suppresses anti-DNA autoimmunity. Together with DNASE1, plays a key role in degrading neutrophil extracellular traps (NETs). NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation. Degradation of intravascular NETs by DNASE1 and DNASE1L3 is required to prevent formation of clots that obstruct blood vessels and cause organ damage following inflammation.
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O55071
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CP2BJ_MOUSE
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Cytochrome P450 2B19 (EC 1.14.14.1) (CYPIIB19)
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MEFSVLLLLALTTGFLIFLVSQSQPKTHGHFPPGPRPLPFLGNLLQMDRRGLLSSFIQLQEKYGDVFTVHLGPRPVVMLCGTDTIREALVNQAEAFSGRGTVAVLDPIVQGYGVIFSSGERWKTLRRFSLATMRDFGMGKRSVEERIKEEAQCLVEELKKYKGAPLNPTFYFQCIVANIICSIVFGERFDYKDHQFLHLLNLIYQTFSLMSSLSSQVFELFSAILKYFPGAHRQISKNLQEILDYIGHSVEKHRATLDPSAPRDFIDTYLLRMEKEKSNHHTEFHHQNLVISVLSLFFAGTETTSTTLRYSFLIMLKYPHVAEKVQKEIDQVIGSHRLPTLDDRTKMPYTDAVIHEIQRFTDLAPIGLPHKVTKDTLFRGYLIPKNTEVYPILSSALHDPRYFEQPDSFNPEHFLDANGALKTNEAFMPFSTGKRICLGEGIARNELFLFFTTILQNFSLASPVAPENIDLIPNNSGATKTPPQYQIHFLSR
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Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.
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O55074
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AKA7A_MOUSE
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A-kinase anchor protein 7 isoform alpha (AKAP-7 isoform alpha) (A-kinase anchor protein 18) (AKAP-18) (A-kinase anchor protein 9 kDa) (AKAP 9) (Protein kinase A-anchoring protein 7 isoform alpha) (PRKA7 isoform alpha)
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MGQLCCFPFARDEGKICEKDRREPEDAELVRLSKRLVENAVLKAVQQYLEETQNKKQPGEGNSTKAEEGDRNGDGSDNNRK
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Targets the cAMP-dependent protein kinase (PKA) to the plasma membrane, and permits functional coupling to the L-type calcium channel. The membrane-associated form reduces epithelial sodium channel (ENaC) activity, whereas the free cytoplasmic form may negatively regulate ENaC channel feedback inhibition by intracellular sodium (By similarity). {ECO:0000250, ECO:0000269|PubMed:9620705}.
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O55076
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CDK2_CRIGR
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Cyclin-dependent kinase 2 (EC 2.7.11.22) (Cell division protein kinase 2)
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MENFQKVEKIGEGTYGVVYKAKNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASAVTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINAEGSIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSFPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL
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Serine/threonine-protein kinase involved in the control of the cell cycle essential for meiosis, but dispensable for mitosis. Phosphorylates CTNNB1, USP37, p53/TP53, NPM1, CDK7, RB1, BRCA2, MYC, NPAT, EZH2. Triggers duplication of centrosomes and DNA. Acts at the G1-S transition to promote the E2F transcriptional program and the initiation of DNA synthesis, and modulates G2 progression controls the timing of entry into mitosis/meiosis by controlling the subsequent activation of cyclin B/CDK1 by phosphorylation, and coordinates the activation of cyclin B/CDK1 at the centrosome and in the nucleus. Crucial role in orchestrating a fine balance between cellular proliferation, cell death, and DNA repair in human embryonic stem cells (hESCs). Activity of CDK2 is maximal during S phase and G2 activated by interaction with cyclin E during the early stages of DNA synthesis to permit G1-S transition, and subsequently activated by cyclin A2 (cyclin A1 in germ cells) during the late stages of DNA replication to drive the transition from S phase to mitosis, the G2 phase. EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing. Phosphorylates CABLES1 (By similarity). Cyclin E/CDK2 prevents oxidative stress-mediated Ras-induced senescence by phosphorylating MYC. Involved in G1-S phase DNA damage checkpoint that prevents cells with damaged DNA from initiating mitosis regulates homologous recombination-dependent repair by phosphorylating BRCA2, this phosphorylation is low in S phase when recombination is active, but increases as cells progress towards mitosis. In response to DNA damage, double-strand break repair by homologous recombination a reduction of CDK2-mediated BRCA2 phosphorylation. Phosphorylation of RB1 disturbs its interaction with E2F1. NPM1 phosphorylation by cyclin E/CDK2 promotes its dissociates from unduplicated centrosomes, thus initiating centrosome duplication. Cyclin E/CDK2-mediated phosphorylation of NPAT at G1-S transition and until prophase stimulates the NPAT-mediated activation of histone gene transcription during S phase. Required for vitamin D-mediated growth inhibition by being itself inactivated. Involved in the nitric oxide- (NO) mediated signaling in a nitrosylation/activation-dependent manner. USP37 is activated by phosphorylation and thus triggers G1-S transition. CTNNB1 phosphorylation regulates insulin internalization. Phosphorylates FOXP3 and negatively regulates its transcriptional activity and protein stability (By similarity). Phosphorylates CDK2AP2 (By similarity). Phosphorylates ERCC6 which is essential for its chromatin remodeling activity at DNA double-strand breaks (By similarity).
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O55082
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PTN20_MOUSE
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Tyrosine-protein phosphatase non-receptor type 20 (EC 3.1.3.48) (Testis-specific tyrosine phosphatase)
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MSSPRKVRGKTGRDNDEEEGNSGNLNLRNSLPSSSQKMTPTKPIFGNKMNSENVKPSHHLSFSDKYELVYPEPLESDTDETVWDVSDRSLRNRWNSMDSETAGPSKTVSPVLSGSSRLSKDTETSVSEKELTQLAQIRPLIFNSSARSAMRDCLNTLQKKEELDIIREFLELEQMTLPDDFNSGNTLQNRDKNRYRDILPYDSTRVPLGKNKDYINASYIRIVNHEEEYFYIATQGPLPETIEDFWQMVLENNCNVIAMITREIECGVIKCYSYWPISLKEPLEFEHFSVFLETFHVTQYFTVRVFQIVKKSTGKSQCVKHLQFTKWPDHGTPASADFFIKYVRYVRKSHITGPLLVHCSAGVGRTGVFICVDVVFSAIEKNYSFDIMNIVTQMRKQRCGMIQTKEQYQFCYEIVLEVLQNLLALY
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Tyrosine-protein phosphatase targeted to sites of actin polymerization in response of varied extracellular stimuli. Has tyrosine phosphatase activity towards various tyrosyl phosphorylated substrates.
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O55087
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MEF2B_MOUSE
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Myocyte-specific enhancer factor 2B
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MGRKKIQISRILDQRNRQVTFTKRKFGLMKKAYELSVLCDCDIALIIFNSAQRLFQYASSDMDRVLLKYTEYSEPHESRTNADILQTLKRRGVGLDGPELDMEEGPEGPGEKLLRTLGGDRGSASPRPRIYPVAPAMSVSELSYRVPPATPGCDPGGLGEVPSVHSRPAYFRPPGLGHPIFSPSHLASKTPPPLYLATDGRRPDLPPGLVGARGGLGTSRSLYSGLQSPGAPGPALGSFAFLPSGSTDCSPGDAAQGPLQPSPWPPTRDAVDPARPVARSLCKEGPPSRGASPPTPPVSIKSERLSPVTGTSGDFPRSFPYPLLLARPLAEPLRPSASLHRLTPDSWPR
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Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific genes. Activates transcription via this element. May be involved in muscle-specific and/or growth factor-related transcription.
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O55091
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IMPCT_MOUSE
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Protein IMPACT (Imprinted and ancient gene protein)
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MAEEEVGNSQRQSEEIEAMAAIYGEEWCVIDENAKIFCIRVTDFMDDPKWTLCLQVMLPSEYPGTAPPSYQLNAPWLKGQERADLSNSLEEIYVHNMGESILYQWVEKIRDALIQKSQITEPDPDVKKKTEEVEVESEEDPILEHPPENPVKTLDLKISEETQPETEELPPVAHGVPITDRRSTFQAHVAPVVCPEQVKLVLAKLYENKKIASATHNIYAYRIFCEDKQTFLQDCEDDGETAAGGRLLHLMEILNVKNVMVVVSRWYGGILLGPDRFKHINNCARNILVEKNFTNTPDESTKNLGKKKVKKDKKKNDH
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Translational regulator that ensures constant high levels of translation upon a variety of stress conditions, such as amino acid starvation, UV-C irradiation, proteasome inhibitor treatment and glucose deprivation. Plays a role as a negative regulator of the EIF2AK4/GCN2 kinase activity impairs GCN1-mediated EIF2AK4/GCN2 activation, and hence EIF2AK4/GCN2-mediated eIF-2-alpha phosphorylation and subsequent down-regulation of protein synthesis. May be required to regulate translation in specific neuronal cells under amino acid starvation conditions by preventing GCN2 activation and therefore ATF4 synthesis. Through its inhibitory action on EIF2AK4/GCN2, plays a role in differentiation of neuronal cells by stimulating neurite outgrowth.
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O55092
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SLK_CAVPO
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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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MSFFNFRKIFKLGSEKKKKQYEHVKRDLNPEEFWETIGELGDGAFGKVYKAQNKETNVLAAAKVIDTKSEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEFCAGGAVDAVMLELERPLTESQIQVVCKQTLEALNYLHDNKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRTIQRRDSFIGTPYWMAPEVVMCETSKDRPYDYKADVWSLGITLIEMAEIEPPHHELNPMRVLLKIAKSEPPTLAQPSRWSSNFKDFLKKCLEKNVDARWTTSQLLQHPFVTIDSNKPIRELIAEAKAEVTEEVEDGKEEDDDEEIENSLPIPTNKRASSDLSIASSEEDKLSQNACILESVSEKTEHNASGDKFSTKVLNEKPCPGEPENAVELVGGAVAVLPDRATELPESGREEKRPKLDRLPDTEDQEMADINSVSEGEEDHAVTSETNIEHNLKPEKERDQEKQPVLENKLVKSEDTTIQTVDLVSQETGEKEVDIHILDSEVVHAVEDTHEKLRKDDTTQKDVISDTSSVGERDEEIGAVPKTAESSAEGAQGDGGKETDEGAQILISKATEGPKASGTEEAPPVTEITETNDTDQKLVENTHEKQLPISSETTLDTSEGLGASEGREVTESGSTEEVEVEGAVSETDEEDVQSETRGAPMAVTQMDTEKNETPHEAPAQVEVQVPVPPQPSEPPPAPIPSININSEAAENKGEMGASLNTETILLPESESQKENDTDSGTGSTADNSSIDLNLSISSFLSKTKDNGSISLQETRRQKKTLKKTRKFIVDGVEVSVTTSKIVTDSDSKTEELRFLRRQELRELRFLQKEEQRAQQQLNGKLQQQREQIFRRFEQEMMSKKRQYDQEIENLEKQQKQTIERLEQEHTNRLRDEAKRIKGEQEKELSKFQNILKNRKKEVLNEVEKAPKDLRKELMKRRKEELAQSQHVQEQDFVQKQQQELDGSLKKIIQQQKAELANIERECLNNKQQLMRAREAAIWELEERHLQEKHQLLKQQLKDQYFMQRHQLLKRHEKETEQMQRYNQRLIEELKNRQTQERARLPKIQRSEAKTRMAMFKKSLRINSTATPDQDRDKIKQFSAQEEKRQKNERMAQHQKHENQMRDLQLQCEANVRELHQLQNEKCHLLVEHETQKLKELDEEHSQELKEWREKLRPRKKTLEEEFARKLQEQEVFFKMTGESECLNPSTQSRISKFYPIPSLHSTGS
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Mediates apoptosis and actin stress fiber dissolution.
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O55096
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DPP3_RAT
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Dipeptidyl peptidase 3 (EC 3.4.14.4) (Dipeptidyl aminopeptidase III) (Dipeptidyl arylamidase III) (Dipeptidyl peptidase III) (DPP III) (Enkephalinase B)
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MADTQYILPNDIGVSSLDCREAFRLLSPTERLYAHHLSRAAWYGGLAVLLQTSPEAPYIYALLSRLFRAQDPDQLRQHALAEGLTEEEYQAFLVYAAGVYSNMGNYKSFGDTKFVPNLPKEKLERVILGSKAAQQHPEEVRSLWQTCGELMFSLEPRLRHLGLGKEGVTTYFSGDCAMEDAKLAQDFLDSQNLSAYNTRLFKVVGQEGKYHYEVRLASVLNTEPALDSELTSKLKSYEFQGNHFQVTRGDYAPILQKVVEHLEKAKAYAANSHQEQMLAQYVESFTQGSIEAHKRGSRFWIQDKGPIVESYIGFIESYRDPFGSRGEFEGFVAMVNKDMSAKFERLVASAEQLLKELPWPPAFEKDKFLTPDFTSLDVLTFAGSGIPAGINIPNYDDLRQTEGFKNVSLGNVLAVAYATKREKLTFMEEEDKDLYIRWKGPSFDVQVGLHELLGHGSGKLFVQDEKGAFNFDQETVINPETGEQIQSWYRSGETWDSKFSTIASSYEECRAESVGLYLCLNPQVLQIFGFEGTDAEDVIYVNWLNMVRAGLLALEFYTPETANWRQAHMQARFVILRVLLEAGEGLVTVTPTTGSDGRPDARVHLDRSKIRSVGKPALERFLRRLQVLKSTGDVVAGRALYEGYAAVTDAPPECFLTLRDTVLLRKESRKLIVQPNTRLEGSEVQLVEYEASAAGLIRSFCERFPEDGPELEEVLTQLATADAQFWRDQVQEAPSGQA
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Cleaves and degrades bioactive peptides, including angiotensin, Leu-enkephalin and Met-enkephalin (By similarity). Also cleaves Arg-Arg-beta-naphthylamide.
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O55098
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STK10_MOUSE
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Serine/threonine-protein kinase 10 (EC 2.7.11.1) (Lymphocyte-oriented kinase)
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MAFANFRRILRLSTFEKRKSREYEHVRRDLDPNDVWEIVGELGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEDYIVEIEILATCDHPYIVKLLGAYYYDGKLWIMIEFCPGGAVDAIMLELDRGLTEPQIQVVCRQMLEALNFLHGKRIIHRDLKAGNVLMTLEGDIRLADFGVSAKNLKTLQKRDSFIGTPYWMAPEVVLCETMKDAPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSDPPTLLTPSKWSVEFRDFLKIALDKNPETRPSAAQLLQHPFVSRVTSNKALRELVAEAKAEVMEEIEDGREDGEEEDAVDAVPPLVNHTQDSANVTQPSLDSNKLLQDSSTPLPPSQPQEPVSGSCSQPSGDGPLQTTSPADGLSKNDNDLKVPVPLRKSRPLSMDARIQMDEEKQIPDQDENPSPAASKSQKANQSRPNSSALETLGGEALTNGGLELPSSVTPSHSKRASDCSNLSTSESMDYGTSLSADLSLNKETGSLSLKGSKLHNKTLKRTRRFVVDGVEVSITTSKIISEDEKKDEEMRFLRRQELRELRLLQKEEHRNQTQLSSKHELQLEQMHKRFEQEINAKKKFYDVELENLERQQKQQVEKMEQDHSVRRKEEAKRIRLEQDRDYAKFQEQLKQMKKEVKSEVEKLPRQQRKESMKQKMEEHSQKKQRLDRDFVAKQKEDLELAMRKLTTENRREICDKERDCLSKKQELLRDREAALWEMEEHQLQERHQLVKQQLKDQYFLQRHDLLRKHEKEREQMQRYNQRMMEQLKVRQQQEKARLPKIQRSDGKTRMAMYKKSLHINGAGSASEQREKIKQFSQQEEKRQKAERLQQQQKHENQMRDMVAQCESNMSELQQLQNEKCHLLVEHETQKLKALDESHNQSLKEWRDKLRPRKKALEEDLNQKKREQEMFFKLSEEAEPRPTTPSKASNFFPYSSGDAS
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Serine/threonine-protein kinase involved in regulation of lymphocyte migration. Phosphorylates MSN, and possibly PLK1. Involved in regulation of lymphocyte migration by mediating phosphorylation of ERM proteins such as MSN. Acts as a negative regulator of MAP3K1/MEKK1. May also act as a cell cycle regulator by acting as a polo kinase kinase: mediates phosphorylation of PLK1 in vitro however such data require additional evidences in vivo.
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O55099
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AURKB_RAT
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Aurora kinase B (EC 2.7.11.1) (Aurora 1) (Aurora- and IPL1-like midbody-associated protein 1) (Aurora/IPL1-related kinase 2) (ARK-2) (Aurora-related kinase 2) (STK-1) (Serine/threonine-protein kinase 12) (Serine/threonine-protein kinase 5) (Serine/threonine-protein kinase aurora-B)
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MAQKENVYPWPYGSKTSQSGLNTLPQRVLRKEPAVTPAQALMNRSNSQSTAVPGQKLTENKGATALQGSQSRQPFTIDNFEIGRPLGKGKFGNVYLAREKKSRFIVALKILFKSQIEKEGVEHQLRREIEIQAHLKHPNILQLYNYFYDQQRIYLILEYAPRGELYKELQKSGTFDEQRTATIMEELSDALMYCHKKKVIHRDIKPENLLLGLQGELKIADFGWSVHAPSLRRKTMCGTLDYLPPEMIEGRMHNEMVDLWCIGVLCYELMVGNPPFESPSHSETYRRIVKVDLKFPSSMPLGAKDLISKLLKHNPSQRLPLEQVSAHPWVRANSRRVLPPSAL
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Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis (By similarity). The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly (By similarity). Involved in the bipolar attachment of spindle microtubules to kinetochores and is a key regulator for the onset of cytokinesis during mitosis. Required for central/midzone spindle assembly and cleavage furrow formation (By similarity). Key component of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage: phosphorylates CHMP4C, leading to retain abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis (By similarity). AURKB phosphorylates the CPC complex subunits BIRC5/survivin, CDCA8/borealin and INCENP (By similarity). Phosphorylation of INCENP leads to increased AURKB activity (By similarity). Other known AURKB substrates involved in centromeric functions and mitosis are CENPA, DES/desmin, GPAF, KIF2C, NSUN2, RACGAP1, SEPTIN1, VIM/vimentin, HASPIN, and histone H3 (By similarity). A positive feedback loop involving HASPIN and AURKB contributes to localization of CPC to centromeres (By similarity). Phosphorylation of VIM controls vimentin filament segregation in cytokinetic process, whereas histone H3 is phosphorylated at 'Ser-10' and 'Ser-28' during mitosis (H3S10ph and H3S28ph, respectively) (By similarity). AURKB is also required for kinetochore localization of BUB1 and SGO1 (By similarity). Phosphorylation of p53/TP53 negatively regulates its transcriptional activity (By similarity). Key regulator of active promoters in resting B- and T-lymphocytes: acts by mediating phosphorylation of H3S28ph at active promoters in resting B-cells, inhibiting RNF2/RING1B-mediated ubiquitination of histone H2A and enhancing binding and activity of the USP16 deubiquitinase at transcribed genes (By similarity). Acts as an inhibitor of CGAS during mitosis: catalyzes phosphorylation of the N-terminus of CGAS during the G2-M transition, blocking CGAS liquid phase separation and activation, and thereby preventing CGAS-induced autoimmunity (By similarity). Phosphorylates KRT5 during anaphase and telophase (By similarity).
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O55100
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SNG1_MOUSE
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Synaptogyrin-1
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MEGGAYGAGKAGGAFDPYTLVRQPHTILRVVSWVFSIVVFGSIVNEGYLNNPEEEEEFCIYNRNPNACSYGVTVGVLAFLTCLLYLALDVYFPQISSVKDRKKAVLSDIGVSAFWAFFWFVGFCFLANQWQVSKPKDNPLNEGTDAARAAIAFSFFSIFTWAGQAVLAFQRYQIGADSALFSQDYMDPSQDSSMPYAPYVEPSAGSDPAGMGGTYQHPANAFDAEPQGYQSQGY
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May play a role in regulated exocytosis. Modulates the localization of synaptophysin/SYP into synaptic-like microvesicles and may therefore play a role in synaptic-like microvesicle formation and/or maturation (By similarity). Involved in the regulation of short-term and long-term synaptic plasticity.
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O55102
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BL1S1_MOUSE
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Biogenesis of lysosome-related organelles complex 1 subunit 1 (BLOC-1 subunit 1) (GCN5-like protein 1)
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MLSRLLKEHQAKQNERKELQEKRRREAIAAATCLTEALVDHLNVGVAQAYMNQRKLDHEVKTLQVQAAQFAKQTGQWIGMVENFNQALKEIGDVENWARSIELDMRTIATALEYVYKGQLQSAPS
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Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. The BORC complex is most probably associated with the cytosolic face of lysosomes, may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor (By similarity).
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O55103
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PRAX_MOUSE
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Periaxin
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MEARSRSAEELRRAELVEIIVETEAQTGVSGFNVAGGGKEGIFVRELREDSPAAKSLSLQEGDQLLSARVFFENFKYEDALRLLQCAEPYKVSFCLKRTVPTGDLALRPGTVSGYEMKGPRAKVAKLNIQSLAPVKKKKMVTGALGTPADLAPVDVEFSFPKFSRLRRGLKAEAVKGPVPAAPARRRLQLPRLRVREVAEEAQVARMAAAAPPPRKAKAEAEAATGAGFTAPQIELVGPRLPSAEVGVPQVSVPKGTPSTEAASGFALHLPTLGLGAPAAPAVEPPATGIQVPQVELPTLPSLPTLPTLPCLDTQEGAAVVKVPTLDVAAPSMGVDLALPGAEVEAQGEVPEVALKMPRLSFPRFGIRGKEATEAKVVKGSPEAKAKGPRLRMPTFGLSLLEPRPSGPEAVAESKLKLPTLKMPSFGIGVAGPEVKAPTGPEVKLPKVPEVKLPKVPEAAIPDVQLPEVQLPKMSDMKLPKIPEMVVPDVRLPEVQLPKVPEMKVPEMKLPKWPEMAVPDVHLPDVQLPKVPEMKLPKVPEMAVPDVHLPDVQLPKVPEMKLPEMKLPKVPEMAVPDVRLPEVQLPKVSEVKLPKMPEMAVPDVHLPELQLPKMSEVKLPKMPEMAVPDVRLPEVQLPKVSEMKLPKMPEMTMPDIRLPEVQLPKVPDIKLPEMKLPEIKLPKVPDMAVPDVPLPELQLPKVSDIRLPEMQVSQVPEVQLPKMPEMKLSKVPEVQRKSAGAEQAKGTEFSFKLPKMTMPKLGKVGKPGEASIEVPDKLMTLPCLQPEVGTEASHVGVPSLSLPSVELDLPGALGLEGQVQEAVPGKVEKPEGPRVAVGVGEVGFRVPSVEIVTPQLPTVEVEKEQLEMVEMKVKPSSKFSLPKFGLSGPKAVKGEVEGPGRATKLKVSKFTISLPKARAGTEAEAKGAGEAGLLPALDLSIPQLSLDAQLPSGKVEVADSKPKSSRFALPKFGVKGRDSEADVLVAGEAELEGKGWGWDGKVKMPKLKMPSFGLSRGKEAETQDGRVSPGEKLEAIAGQLKIPAVELVTPGAQETEKVTSGVKPSGLQVSTTGQVVAEGQESVQRVSTLGISLPQVELASFGEAGPEIVAPSAEGTAGSRVQVPQVMLELPGTQVAGGDLLVGEGIFKMPTVTVPQLELDVGLGHEAQAGEAAKSEGGIKLKLPTLGTGSRGEGVEPQGPEAQRTFHLSLPDVELTSPVSSHAEYQVVEGDGDGGHKLKVRLPLFGLAKAKEGIEVGEKVKSPKLRLPRVGFSQSESVSGEGSPSPEEEEEGSGEGASSRRGRVRVRLPRVGLASPSKVSKGQEGDATSKSPVGEKSPKFRFPRVSLSPKARSGSRDREEGGFRVRLPSVGFSETAVPGSTRIEGTQAAAI
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Scaffolding protein that functions as part of a dystroglycan complex in Schwann cells, and as part of EZR and AHNAK-containing complexes in eye lens fiber cells. Required for the maintenance of the peripheral myelin sheath that is essential for normal transmission of nerve impulses and normal perception of sensory stimuli. Required for normal transport of MBP mRNA from the perinuclear to the paranodal regions. Required for normal remyelination after nerve injury. Required for normal elongation of Schwann cells and normal length of the internodes between the nodes of Ranvier. The demyelinated nodes of Ranvier permit saltatory transmission of nerve impulses shorter internodes cause slower transmission of nerve impulses. Required for the formation of appositions between the abaxonal surface of the myelin sheath and the Schwann cell plasma membrane the Schwann cell cytoplasm is restricted to regions between these appositions. Required for the formation of Cajal bands and of Schmidt-Lanterman incisures that correspond to short, cytoplasm-filled regions on myelinated nerves. Recruits DRP2 to the Schwann cell plasma membrane. Required for normal protein composition of the eye lens fiber cell plasma membrane and normal eye lens fiber cell morphology.
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O55106
|
STRN_MOUSE
|
Striatin
|
MDEQAGPGVFFSNNHPGAGGAKGLGPLAEAAAAGDGAAAAGAARAQYSLPGILHFLQHEWARFEVERAQWEVERAELQAQIAFLQGERKGQENLKKDLVRRIKMLEYALKQERAKYHKLKYGTELNQGDMKPPSYDSDEGNETEVQPQQNSQLMWKQGRQLLRQYLQEVGYTDTILDVKSKRVRALLGFSSDVTDREDDKNQDSVINGTEAEVKETAMIGKSELTDSASVLDNFKFLESAAADVSDEDEDEDTDGRAKSVIDTSTIVRKKALPDTSEDRDTKEALKEFDFLVTSEEGDNESRSAGDGTDWEKEDQCLTPEAWNVDQGVISKLKEQYKKERKGKKGVKRPNRSKLQDMLANLRDVDELPSLQPSVGSPSRPSSSRLPEQELSRADEVEALTFPPSSGKSFIMGADEALESELGLGELAGLTVANEADSLAYDIANNKDALRKTWNPKFTLRSHFDGIRALAFHPIEPVLITASEDHTLKMWNLQKTAPAKKSTSLDVEPIYTFRAHKGPVLCVVMSSNGEQCYSGGTDGRIQSWSTTNPNVDPYDAYDPSVLRGPLLGHTDAVWGLAYSAAHQRLLSCSADGTLRLWNTTEVAPALSVFNDNQELGIPASVDLVSSDPSHMVASFSKGYTSIFNMETQQRVLTLESNVDSTSSSSCQINRVISHPTLPISITAHEDRHIKFYDNNTGKLIHSMVAHLEAVTSLAVDPNGLYLMSGSHDCSIRLWNLESKTCIQEFTAHRKKFEESIHDVAFHPSKCYIASAGADALAKVFV
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Binds calmodulin in a calcium dependent manner. May function as scaffolding or signaling protein.
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O55111
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DSG2_MOUSE
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Desmoglein-2
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MARSPGDRCALLLLVQLLAVVCLDFGNGLHLEVFSPRNEGKPFPKHTHLVRQKRAWITAPVALREGEDLSRKNPIAKIHSDLAEEKGIKITYKYTGKGITEPPFGIFVFDRNTGELNITSILDREETPYFLLTGYALDSRGNNLEKPLELRIKVLDINDNEPVFTQEVFVGSIEELSAAHTLVMKITATDADDPETLNAKVSYRIVSQEPANSHMFYLNKDTGEIYTTSFTLDREEHSSYSLTVEARDGNGQITDKPVQQAQVQIRILDVNDNIPVVENKMYEGTVEENQVNVEVMRIKVTDADEVGSDNWLANFTFASGNEGGYFHIETDTQTNEGIVTLVKEVDYEEMKKLDLSIIVTNKAAFHKSILSKYKATPIPITVKVKNVVEGIHFKSSVVSFRASEAMDRSSLSRSIGNFQVFDEDTGQAAKVTYVKVQDTDNWVSVDSVTSEIKLVKIPDFESRYVQNGTYTAKVVAISKEHPQKTITGTIVITVEDVNDNCPVLVDSVRSVCEDEPYVNVTAEDLDGAQNSAPFSFSIIDQPPGTAQKWKITHQESTSVLLQQSERKRGRSEIPFLISDSQGFSCPERQVLQLTVCECLKGGGCVAAQYDNYVGLGPAAIALMILALLLLLLVPLLLLICHCGGGAKGFTPIPGTIEMLHPWNNEGAPPEDKVVPSLLVADHAESSAVRGGVGGAMLKEGMMKGSSSASVTKGQHELSEVDGRWEEHRSLLTAGATHHVRTAGTIAANEAVRTRATGSSRDMSGARGAVAVNEEFLRSYFTEKAASYNGEDDLHMAKDCLLVYSQEDTASLRGSVGCCSFIEGELDDLFLDDLGLKFKTLAEVCLGRKIDLDVDIEQRQKPVREASVSAASGSHYEQAVTSSESAYSSNTGFPAPKPLHEVHTEKVTQEIVTESSVSSRQSQKVVPPPDPVASGNIIVTETSYAKGSAVPPSTVLLAPRQPQSLIVTERVYAPTSTLVDQHYANEEKVLVTERVIQPNGGIPKPLEVTQHLKDAQYVMVRERESILAPSSGVQPTLAMPSVAAGGQNVTVTERILTPASTLQSSYQIPSETSITARNTVLSSVGSIGPLPNLDLEESDRPNSTITTSSTRVTKHSTMQHSYS
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Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion.
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O55112
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AFF2_MOUSE
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AF4/FMR2 family member 2 (Protein FMR-2) (FMR2P) (Protein Ox19)
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MDLFDFFRDWDLEQQCHYEQDRSALKKREWERRNQEVQQEEDLFSSGFDLFGEPYKVAEYTNKGDALANRVQNTLGSYDEMKDLLSNHSSQNHLVGIPKNSAPQTPISKSEASFYPEQKNRMIPSHQETTHSSTPMPPPSVVILNSTLIHSNRKSKSEWPRDSHNTSPAQASQTSSQPNKMQTSTQDPPQTRLEDFFVYPAEQPQIGTVEKSNPSSKEENNPNSGGEDTFKEIFQSNSPEESEFTVQAPGSPLVASSLLAPSSGLSVPTFPPGLYCKTSMGQQKPTAYVRPMDGQDQATDISPTLKPSIEFENSFGNLSFGSLLDGKPSAVSSKTKLPKFTILQTSEVSLTSDPSCVEEILRESQHLTPGFTLQKWSDPSSRASTKMLEDDLKLSSDEDDLEPVKTLTTQCTANELYQAVEKAKPKNNPVNPLLATPQSTPATQTNVGSGSSSESESSSESDSDTESSTTDSESNEAPRVATPEPEPPSTNKWQLDKWLNKVTSQNKSFICGQNETPTETISLPPPIIQPVEVQVKVKPNPSQAVAVPKERPLLSLIREKARPRPTQKTPETKALKHKLSTSVDTVSQRTIGKKQPKKVEKNTSFEEFTWPKPNITNSTPKEKGSVELPDPPRSRNKATAHKPVPRKEPRPHVPLATEKKKYRGPGKIVPKSREFIETDSSTSDSNTDQEETLQIKVLPPCITSKSKETSNASLTLSTLTNGNSNNLSTSNEETAFSPPPAMQTELLSPLRDHENPKNLWVKIDLDLLSRVPGQNSVPVTPAKTDYKETASKPKRQTAATAVEKPAPKGKRKHKPAETAEKIPEKKQRLEDNTTICLLPPCISPAPPHKPPSTRENSSRRANRKKEEKLFPPALSPLAEDPPRRRNVSGNNGHFGQDKNISMAGQITSSKPKRSEGKFCATFKGISINEGDAPKKAASATVTVANMALATATATATVPAIVTATVTATATTTATATTTTTTTTISSITPTITSGLMDSSHLEMTSWAALPLLSSSSANVRRPKLTFDDSVHNADFYMQEAKKLKHKADALFEKFGKAVNYADAALSFTECGNAMERDPLEAKSPYTMYSETVELLRYAMRLKNFASPLASDGDKKLAVLCYRCLSLLYLRMFKLKKDHAMKYSRSLMEYFKQNASKVTQIPSPWVGNGKNTPSPVSLNNVSPINSVGNCNNGPVTIPQRIHHMAASHVNITSNVLRGYEHWDMADKLTRDNKEFFGDLDTLMGPLTQHSSMTNLVRYVRQGLCWLRIDAHLL
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RNA-binding protein. Might be involved in alternative splicing regulation through an interaction with G-quartet RNA structure.
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O55123
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MMP10_MOUSE
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Stromelysin-2 (SL-2) (EC 3.4.24.22) (Matrix metalloproteinase-10) (MMP-10) (Transin-2)
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MEPLAILALLSLPICSAYPLHGAVTQGHPSMDLAQQYLEKYYNFKKNEKQIFKRKDSSPVVKKIQEMQKFLGLEMTGKLDSNTMELMHKPRCGVPDVGGFSTFPGSPKWRKSHITYRIVNYTPDLPRQSVDSAIEKALKVWEEVTPLTFSRISEGEADIMISFAVGEHGDFYPFDGPGQSLAHAYPPGPGFYGDVHFDDDEKWTLAPSGTNLFLVAAHELGHSLGLFHSDKKESLMYPVYRFSTSPANFHLSQDDIEGIQSLYGAGPSSDATVVPVLSVSPRPETPDKCDPALSFDSVSTLRGEVLFFKDRYFWRRSHWNPEPEFHLISAFWPTLPSDLDAAYEAHNTDSVLIFKGSQFWAVRGNEVQAGYPKGIHTLGFPPTVKKIDAAVFEKEKKKTYFFVGDKYWRFDETRHVMDKGFPRQITDDFPGIEPQVDAVLHEFGFFYFFRGSSQFEFDPNARTVTHILKSNSWLLC
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Can degrade fibronectin, gelatins of type I, III, IV, and V weakly collagens III, IV, and V. Activates procollagenase.
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O55127
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CP26A_MOUSE
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Cytochrome P450 26A1 (CYP26A1) (EC 1.14.13.-) (Cytochrome P450RAI) (Retinoic acid 4-hydroxylase) (Retinoic acid-metabolizing cytochrome)
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MGLPALLASALCTFVLPLLLFLAALKLWDLYCVSSRDRSCALPLPPGTMGFPFFGETLQMVLQRRKFLQMKRRKYGFIYKTHLFGRPTVRVMGADNVRRILLGEHRLVSVHWPASVRTILGAGCLSNLHDSSHKQRKKVIMQAFSREALQCYVLVIAEEVSSCLEQWLSCGERGLLVYPEVKRLMFRIAMRILLGCEPGPAGGGEDEQQLVEAFEEMTRNLFSLPIDVPFSGLYRGVKARNLIHARIEENIRAKIRRLQATEPDGGCKDALQLLIEHSWERGERLDMQALKQSSTELLFGGHETTASAATSLITYLGLYPHVLQKVREEIKSKGLLCKSNQDNKLDMETLEQLKYIGCVIKETLRLNPPVPGGFRVALKTFELNGYQIPKGWNVIYSICDTHDVADIFTNKEEFNPDRFIVPHPEDASRFSFIPFGGGLRSCVGKEFAKILLKIFTVELARHCDWQLLNGPPTMKTSPTVYPVDNLPARFTYFQGDI
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A cytochrome P450 monooxygenase involved in the metabolism of retinoates (RAs), the active metabolites of vitamin A, and critical signaling molecules in animals. RAs exist as at least four different isomers: all-trans-RA (atRA), 9-cis-RA, 13-cis-RA, and 9,13-dicis-RA, where atRA is considered to be the biologically active isomer, although 9-cis-RA and 13-cis-RA also have activity (By similarity). Catalyzes the hydroxylation of atRA primarily at C-4 and C-18, thereby contributing to the regulation of atRA homeostasis and signaling. Hydroxylation of atRA limits its biological activity and initiates a degradative process leading to its eventual elimination (By similarity). Involved in the convertion of atRA to all-trans-4-oxo-RA. Able to metabolize other RAs such as 9-cis, 13-cis and 9,13-di-cis RA. Can oxidize all-trans-13,14-dihydroretinoate (DRA) to metabolites which could include all-trans-4-oxo-DRA, all-trans-4-hydroxy-DRA, all-trans-5,8-epoxy-DRA, and all-trans-18-hydroxy-DRA (Probable). May play a role in the oxidative metabolism of xenobiotics such as tazarotenic acid (By similarity).
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O55128
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SAP18_MOUSE
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Histone deacetylase complex subunit SAP18 (18 kDa Sin3-associated polypeptide) (Sin3-associated polypeptide p18)
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MAVESRVTQEEIKKEPEKPIDREKTCPLLLRVFTTNNGRHHRMDEFSRGNVPSSELQIYTWMDATLKELTSLVKEVYPEARKKGTHFNFAIVFMDLKRPGYRVKEIGSTMSGRKGTDDSMTLQSQKFQIGDYLDIAITPPNRAPPSSGRMRPY
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Component of the SIN3-repressing complex. Enhances the ability of SIN3-HDAC1-mediated transcriptional repression. When tethered to the promoter, it can direct the formation of a repressive complex to core histone proteins. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP and PSAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets. The ASAP complex can inhibit mRNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes) specifically inhibits the formation of proapoptotic isoforms such as Bcl-X(S) the activity is different from the established EJC assembly and function (By similarity). {ECO:0000250, ECO:0000269|PubMed:22388736}.
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O55131
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SEPT7_MOUSE
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Septin-7 (CDC10 protein homolog)
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MSVSARSAAAEERSVNCGTMAQPKNLEGYVGFANLPNQVYRKSVKRGFEFTLMVVGESGLGKSTLINSLFLTDLYSPEYPGPSHRIKKTVQVEQSKVLIKEGGVQLLLTIVDTPGFGDAVDNSNCWQPVIDYIDSKFEDYLNAESRVNRRQMPDNRVQCCLYFIAPSGHGLKPLDIEFMKRLHEKVNIIPLIAKADTLTPEECQQFKKQIMKEIQEHKIKIYEFPETDDEEENKLVKKIKDRLPLAVVGSNTIIEVNGKRVRGRQYPWGVAEVENGEHCDFTILRNMLIRTHMQDLKDVTNNVHYENYRSRKLAAVTYNGVDNNKNKGQLTKSPLAQMEEERREHVAKMKKMEMEMEQVFEMKVKEKVQKLKDSEAELQRRHEQMKKNLEAQHKELEEKRRQFEEEKANWEAQQRILEQQNSSRTLEKNKKKGKIF
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Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Required for normal progress through mitosis. Involved in cytokinesis. Required for normal association of CENPE with the kinetochore. Plays a role in ciliogenesis and collective cell movements. Forms a filamentous structure with SEPTIN12, SEPTIN6, SEPTIN2 and probably SEPTIN4 at the sperm annulus which is required for the structural integrity and motility of the sperm tail during postmeiotic differentiation (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q16181}.
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