entry
stringlengths 6
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| entry_name
stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
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A2AVJ5
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PRR5L_MOUSE
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Proline-rich protein 5-like (Protein observed with Rictor-2) (Protor-2)
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MTRGLAPLLPIEFHKMGSFRRPRPRFMSSPVLSELPRFQAARQALQLSSNSAWNSVQTAVINVFKGGGLQSNELYALNESIRRLLKSELGSFITDYFQNQLLAKGLSFVEEKIKLCEGDNRIEVLAEVWDHFFTETLPTLQAIFYPVQGQELTIRQISLLGFRDLVLLKVKLGDVLLLAQSKLPSSVIQMLLILQSVHEPTGPSEGYLQLEELVKQVVSPFLSISGDRSCSGPTYSLARRHSRVRPKVTVLNYASLMTTVGRPLNEMVLTPLTEQEGEAYLEKCGSVRRHTVANAHSDIQLLAMATMMHSGLGEEAGGEDKHLLLPPSFPPPHRQCSSEPSILDSPDELELEDVASGSQEDSELNCASLS
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Associates with the mTORC2 complex that regulates cellular processes including survival and organization of the cytoskeleton (By similarity). Regulates the activity of the mTORC2 complex in a substrate-specific manner preventing for instance the specific phosphorylation of PKCs and thereby controlling cell migration. Plays a role in the stimulation of ZFP36-mediated mRNA decay of several ZFP36-associated mRNAs, such as TNF-alpha and GM-CSF, in response to stress. Required for ZFP36 localization to cytoplasmic stress granule (SG) and P-body (PB) in response to stress.
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A2AVZ9
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S43A3_MOUSE
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Equilibrative nucleobase transporter 1 (Embryonic epithelia gene 1 protein) (Solute carrier family 43 member 3)
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MASKGLPLYLATLLTGLLECIGFAGVLFGWTSLLFVFKAENYFSEPCEQDCLLQSNVTGPSDLKAQDEKFSLIFTLASFMNNFMTFPTGYIFDRFKTTVARLIAIFFYTCATIIIAFTSANTAMLLFLAMPMLAVGGILFLITNLQIGNLFGKHRSTIITLYNGAFDSSSAVFLVIKLLYEQGISLRSSFIFMSVCSVWHIARTFLLMPKGHIPYPLPPNYSYGLCSRFGASKKENKAAEHETKELRSKECLPPKEENSGPEQQQQQEQQQQQQQQQEQHEQHSFRRCALSRRFILHVVWLSIIQLWHYLFIGTLNSLLTKLSGGDKVEVSAYTNAFAITQFFGVLCAPWNGLLMDRLKQKYQKAAKRTGSSSEAVALCSMVPSLALTSLLSLGFALCASIPVMQLQYATFILQVVSRSFLYGCNAAFLTLAFPSEHFGKLFGLVMALSAIVSLLQFPLFKVSPESNAVYVSMGLAIFLTLVHPFLVYRECRAEKTKSSVDA
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Sodium-independent purine-selective nucleobase transporter which mediates the equilibrative transport of extracellular purine nucleobases such as adenine, guanine and hypoxanthine (By similarity). May regulate fatty acid (FA) transport in adipocytes, acting as a positive regulator of FA efflux and as a negative regulator of FA uptake.
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A2AWL7
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MGAP_MOUSE
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MAX gene-associated protein
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MEEKQQIILANQDGGTVTGGAPTFFVILKQPGNGKTDQGILVTNRDARALLSRESSPGKSKEKICLPADCTVGKITVTLDNNSMWNEFHNRSTEMILTKQGRRMFPYCRYWITGLDSNLKYILVMDISPVDSHRYKWNGRWWEPSGKAEPHILGRVFIHPESPSTGHYWMHQPVSFYKLKLTNNTLDQEGHIILHSMHRYLPRLHLVPAEKATEVIQLNGPGVHTFTFPQTEFFAVTAYQNIQITQLKIDYNPFAKGFRDDGLSSKPQREGKQRNSSDQEGNSVSSSPAHRVRLTEGEGSEIHSGDFDPVLRGHEASSLSLEKAPHNVKQDFLGFMNTDSTHEVPQLKHEISESRIVNSFEDDSQISSPSNPNGNFNVVIKEEPLDDYDYELGECPEGITVKQEETDEETDVYSNSDDDPILEKQLKRHNKVDNLEADHPSYKWLPNSPGVAKAKMFKLDAGKMPVVYLEPCAVTKSTVKISELPDNMLSTSRKDKSMLAELEYLPAYIENSDGTDFCLSKDSENSLRKHSPDLRIVQKYTLLKEPNWKYPDILDNSSTERIHDSSKGSTAESFSGKEDLGKKRTTMLKMAIPSKTVTASHSASPNTPGKRGRPRKLRLSKAGRPPKNTGKSLTAAKNIPVGPGSTFPDVKPDLEDVDGVLFVSFESKEALDIHAVDGTTEEPSSLQTTTTNDSGCRTRISQLEKELIEDLKSLRHKQVIHPALQEVGLKLNSVDPTVSIDLKYLGVQLPLAPATSFPLWNVTGTNPASPDAGFPFVSRTGKTNDFTKIKGWRGKFQNASASRNEGGNSEASLKNRSAFCSDKLDEYLENEGKLMETNIGFSSNAPTSPVVYQLPTKSTSYVRTLDSVLKKQSTISPSTSHSVKPQSVTTASRKTKAQNKQTTLSGRTKSSYKSILPYPVSPKQKNSHVSQGDKITKNSLSSTSDNQVTNLVVPSVDENAFPKQISLRQAQQQHLQQQGTRPPGLSKSQVKLMDLEDCALWEGKPRTYITEERADVSLTTLLTAQASLKTKPIHTIIRKRAPPCNNDFCRLGCVCSSLALEKRQPAHCRRPDCMFGCTCLKRKVVLVKGGSKTKHFHKKAANRDPLFYDTLGEEGREGGGVREDEEQLKEKKKRKKLEYTVCEAEPEQPVRHYPLWVKVEGEVDPEPVYIPTPSVIEPIKPLVLPQPDLSSTTKGKLTPGIKPARTYTPKPNPVIREEDKDPVYLYFESMMTCARVRVYERKKEEQRQLSPPLSPSSSFQQQSSCYSSPENRVTKELDSEQTLKQLICDLEDDSDKSQEKSWKSSCNEGESSSTSYVHQRSPGGPTKLIEIISDCNWEEDRNKILSILSQHINSNMPQSLKVGSFIIELASQRKCRGEKTPPVYSSRVKISMPSSQDQDDMAEKSGSETPDGPLSPGKMDDISPVQTDALDSVRERLHGGKGLPFYAGLSPSGKLVAYKRKPSSTTSGLIQVASNAKVAASRKPRTLLPSTSNSKMASSGPATNRSGKNLKAFVPAKRPIAARPSPGGVFTQFVMSKVGALQQKIPGVRTPQPLTGPQKFSIRPSPVMVVTPVVSSEQVQVCSTVAAAVTTSPQVFLENVTAVPSLTANSDMGAKEATYSSSASTAGVVEISETNNTTLVTSTQSTATVNLTKTTGITTSPVASVSFAKPLVASPTITLPVASTASTSIVMVTTAASSSVVTTPTSSLSSVPIILSGINGSPPVSQRPENAPQIPVTTPQISSNNVKRTGPRLLHPNGQIVQLLPLHQIRGSNAQPSLQPVVFRNPGSMVGIRLPAPCKSSETPSSSASSSAFSVMSPVIQAVGSSPTVNVISQAPSLLSSGSSFVSQAGTLTLRISPPETQNLASKTGSESKITPSTGGQPVGTASLIPLQSGSFALLQLPGQKPIPSSVLQHVASLQIKKESQSTDQKDETNSIKREEETKKALPSKDKALDSEANIMKQNSGIIASENTSNNSLDDGGDLLDEETLREDARPYEYSYSTGSHTDEDKDGDEDSGNKNQNSPKEKQTVPEVRAGSKNIDIMALQSIRSIRPQKCVKVKVEPQEGSDNPENPDDFLVLSKDSKFELSGNQVKEQQSNSQAEAKKDCEDSLGKDSLRERWRKHLKGPLTQKYIGISQNFNKEANVQFFTEMKPCQENSEQDISELLGKSGTIESGGVLKTEDGSWSGISSSAAFSIIPRRATKGRRGSRHFQGHLLLPREQMKPKQQTKDGRSSAADFTVLDLEDEDEEDEKTDDSLDEIVDVVSGYQSEEVDVEKNNYVDYLEDDEQVDVETIEELSEEINFPYKKTTATHTQSFKQQCHSHISADEKASEKSRKVSLISSKLKDDCWGDKPHKETEAFAYYRRTHTANERRRRGEMRDLFEKLKITLGLLHSSKVSKSLILNRAFSEIQGLTDQADKLIGQKNLLSRKRSILIRKVSSLSGKTEEVVLKKLEYIYAKQQALEAQKRKKKLGSDEFCVSPRIGTQLEGSSASSVDLGQMLMNNRRGKPLILSRKRDQATENASPSDTPHSSANLVMTPQGQLLTLKGPLFSGPVVAVSPALLEGGLKPQVASSTMSQSENDDLFMMPRIVNVTSLAAEEDLGGMSGNKYRHEVPDGKPLDHLRDIAGSEASSLKDTERISSRGNHRDSRKALGPTQVLLANKDSGFPHVADVSTMQAAQEFIPKNMSGDVRGHRYKWKECELRGERLKSKESQFHKLKMKDLKDSSIEMELRKVASAIEEAALHPSELLTNMEDEDDTDETLTSLLNEIAFLNQQLNDDSGLAELSGSMDTEFSGDAQRAFISKLAPGNRSAFQVGHLGAGVKELPDVQEESESISPLLLHLEDDDFSENEKQLGDTASEPDVLKIVIDPEIKDSLVSHRKSSDGGQSTSGLPAEPESVSSPPILHMKTGPENSNTDTLWRPMPKLAPLGLKVANPPSDADGQSLKVMPALAPIAAKVGSIGHKMNLAGIDQEGRGSKVMPTLAPVVPKLGNSGAPSSSSGK
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Functions as a dual-specificity transcription factor, regulating the expression of both MAX-network and T-box family target genes. Functions as a repressor or an activator. Binds to 5'-AATTTCACACCTAGGTGTGAAATT-3' core sequence and seems to regulate MYC-MAX target genes. Suppresses transcriptional activation by MYC and inhibits MYC-dependent cell transformation. Function activated by heterodimerization with MAX. This heterodimerization serves the dual function of both generating an E-box-binding heterodimer and simultaneously blocking interaction of a corepressor.
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A2AWP0
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BIRC7_MOUSE
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Baculoviral IAP repeat-containing protein 7 (EC 2.3.2.27) (Livin) (RING-type E3 ubiquitin transferase BIRC7) [Cleaved into: Baculoviral IAP repeat-containing protein 7 30 kDa subunit (Truncated livin) (p30-Livin) (tLivin)]
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MFSPADLFRAAVFSMGPESRARDSVRGPELSHREDGSGRTQEQDKPHCPCNHVLGQDCLDGQILGQLRPLSEEEESSGAAFLGEPAFPEMDSEDLRLASFYDWPSTAGIQPEPLAAAGFFHTGQQDKVRCFFCYGGLQSWERGDDPWTEHARWFPRCQFLLRSKGRDFVERIQTYTPLLGSWDQREEPEDAVSATPSAPAHGSPELLRSRRETQPEDVSEPGAKDVQEQLRQLQEERRCKVCLDRAVSIVFVPCGHFVCTECAPNLQLCPICRVPICSCVRTFLS
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Apoptotic regulator capable of exerting proapoptotic and anti-apoptotic activities and plays crucial roles in apoptosis, cell proliferation, and cell cycle control. Its anti-apoptotic activity is mediated through the inhibition of CASP3, CASP7 and CASP9, as well as by its E3 ubiquitin-protein ligase activity. As it is a weak caspase inhibitor, its anti-apoptotic activity is thought to be due to its ability to ubiquitinate DIABLO/SMAC targeting it for degradation thereby promoting cell survival. May contribute to caspase inhibition, by blocking the ability of DIABLO/SMAC to disrupt XIAP/BIRC4-caspase interactions. Protects against apoptosis induced by TNF or by chemical agents such as adriamycin, etoposide or staurosporine. Suppression of apoptosis is mediated by activation of MAPK8/JNK1, and possibly also of MAPK9/JNK2. This activation depends on TAB1 and MAP3K7/TAK1. In vitro, inhibits CASP3 and proteolytic activation of pro-CASP9.
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A2AWT3
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AT7L3_MOUSE
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Ataxin-7-like protein 3 (SAGA-associated factor 11 homolog)
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MKMEEMSLSGLDNSKLEAIAQEIYADLVEDSCLGFCFEVHRAVKCGYFFLDDTDPDSMKDFEIVDQPGLDIFGQVFNQWKSKECVCPNCSRSIAASRFAPHLEKCLGMGRNSSRIANRRIANSNNMNKSESDQEDNDDINDNDWSYGSEKKAKKRKSDKNPNSPRRSKSLKHKNGELSNSDPFKYSNSTGISYETLGPEELRSLLTTQCGVISEHTKKMCTRSLRCPQHTDEQRRTVRIYFLGPSAVLPEVESSLDNDGFDMTDSQALISRLQWDGSSDLSPSDSGSSKTSENQGWGLGTNSSESRKTKKKKSHLSLVGTASGLGSNKKKKPKPPAPPTPSIYDDIN
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Component of the transcription regulatory histone acetylation (HAT) complex SAGA, a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates both histones H2A and H2B. The SAGA complex is recruited to specific gene promoters by activators such as MYC, where it is required for transcription. Required for nuclear receptor-mediated transactivation. Within the complex, it is required to recruit USP22 and ENY2 into the SAGA complex. Regulates H2B monoubiquitination (H2Bub1) levels. Affects subcellular distribution of ENY2, USP22 and ATXN7L3B. {ECO:0000255|HAMAP-Rule:MF_03047}.
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A2AX52
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CO6A4_MOUSE
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Collagen alpha-4(VI) chain
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MGTWKTFWLIISLAAGLGFVKSQRIVCREASVGDIVFLVHNSINPQHAHSVRNFLYILANSLQVGRDNIRVGLAQYSDTPTSEFLLSVYHRKGDVLKHIRGLQFKPGGNRMGQALQFILEHHFREGAGSRASQGVPQVAVVVSSGLTEDHIREPAEALRRAGILVYAIGVKDASQAELREISSSPKDNFTFFVPNFPGLPGLAQKLRPELCSTLGKAAQYTERESPACSEASPADIVFLVDSSTSIGLQNFQKVKHFLHSVVSGLDVRSDQVQVGLVQYSDNIYPAFPLKQSSLKSAVLDRIRNLPYSMGGTSTGSALEFIRANSLTEMSGSRAKDGVPQIVVLVTDGESSDEVQDVADQLKRDGVFVFVVGINIQDVQELQKIANEPFEEFLFTTENFSILQALSGTLLQALCSTVERQMKKSTKTYADVVFLIDTSQGTSQASFQWMQNFISRIIGILEVGQDKYQIGLAQYSDQGHTEFLFNTHKTRNEMVAHIHELLVFQGGSRKTGQGLRFLHRTFFQEAAGSRLLQGVPQYVVVITSGKSEDEVGEVAQILRKRGVDIVSVGLQDFDRAELEGIGPVVLVSDLQGEDRIRQLMLDVNMFIQGSPKPPRVMTDVAKDAVEECLVPVPADLVFLVEDFSSARQPNFQRVVHFLTTTVHSLNIHPDTTRVSLVFYSEKPRLEFSLDMYQSAAQVLRHLDRLTFRARRGRAKAGAALDFLRKEVFLPEKGSRPHRGVQQIAVVIIESPSLDNVSTPASYLRRAGVTIYAAGTQPASESKDLEKIVTYPPWKHAIRLESFLQLSVVGNKLKKKLCPEMLSGMPPLMSFIPESTRQSTQEGCESVEKADIYFLIDGSGSIKPNDFIEMKDFMKEVIKMFHIGPDRVRFGVVQYSDKIISQFFLTQYASMAGLSAAIDNIQQVGGGTTTGKALSKMVPVFQNTARIDVARYLIVITDGQSTDPVAEAAQGLRDIGVNIYAIGVRDANTTELEEIASKKMFFIYEFDSLKSIHQEVIRDICSSENCKSQKADIIFLIDGSESIAPKDFEKMKDFMERMVNQSNIGADEIQIGLLQFSSNPQEEFRLNRYSSKVDMCRAILSVQQMSDGTHTGKALNFTLPFFDSSRGGRPRVHQYLIVITDGVSQDNVAPPAKALRDRNIIIFAIGVGNVQRAQLLEITNDQDKVFQEENFESLQSLEKEILSEVCSSQGCNIDLSVGVDTSTSSERAQQELRRLLPELMQQLAFLSNISCEAPGQMEPRFRYVVPGSSDQPVFDSGFEKYSDETIQKFLVHQGSVNNRMDVDFLQSLGETAIHLSLAKVKVLLVFTDGLDEDLERLRRTSEFLRSRGLSGLLLIGLGGAHKLEELQELEFGRGFAYRQPLSSSLPSLPSVLLKQLDTIVERTCCNMYAKCYGDDGIRGEPGSRGEQGERGLDGLPGHPGEEGDHGQRGPRGLPGLRGEEGCPGVRGPKGARGFSGEKGNPGEEGVGGLDGEQGDRGAAGPSGEKGSSGSRGLTGLPGPAGPRGEPGLRGDPGDPGIDNLIQGPKGEKGRRGHQGSPGFHGPLGEAGSVGPRGSLGRHGLPGLKGVLGETGELGSRGEPGHPGPQGPRGRQGPPGFFGQKGDPGTQGNPGLPGPSGSKGPDGPRGLKGEVGPAGERGPRGQQGPRGQPGLFGPDGHGYPGRKGRKGEPGFPGYPGVQGEDGNPGRGGEKGAKGIRGKRGNSGFPGLAGTPGDQGPPGKMGTKGSKGLADRTPCEIVDFVRGNCPCSTGISRCPAFPTEVVFTLDMSNDVAPSDFERMRNILLSLLMKLEMCESNCPTGARVAIVSYNTRTDYLVRLSDHRGKAALLQAVRKIPLERSSGSRNLGATMRFVARHVFKRVRSGLLVRKVAVFFQAGRNYDTASVSTATLELHAADIATAVVTFTEEHNLPEAGLVDGPNEFHLFTWETEGQQDVERLASCTLCYDKCRPALGCQLRAPGPQKLDMDLVFLVDSSQGVSRDIYLGALRLVDSVLKDLEVAAQPGTSWHGARAALLTHTTPGFWPGVDQAPVLEYFHLTSHGHRTEMQRQIREAASGLLQGGPALGHALEWTLENVLLTAVLPRRSRVLYAIVASETSIWDREKLRTLSQEAKCKGIALFVLAVGPGVGAQELAELAKVASAPWEQHLLRLEGVSEAEVAYASRFTEAFLNLLNSGINQYPPPELVKECGGPNRGDTLLHFFTSAKRFSRSQSGTSAAFANDSEALKSQGIFLGERKSRVASVALQEALGSHGKDRADTEDIDQETPAKGRHLGPTHGPCPMGPEEGECLNYVLK
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Collagen VI acts as a cell-binding protein.
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A2BD05
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NEK6_PIG
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Serine/threonine-protein kinase Nek6 (EC 2.7.11.34) (Never in mitosis A-related kinase 6) (NimA-related protein kinase 6)
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MAGQPSHMPHGGSPNNLCHTPGPAHPPDPQRHPNALSFRCSLADFQIEKKIGRGQFSEVYKATCLLDRKTVALKKVQIFEMMDAKARQDCVKEIGLLKQLNHPNIIKYLDSFIEDNELNIVLELADAGDLSQMIKYFKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGIVKLGDLGLGRFFSSETTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLFSLCQKIEQCDYPPLPGEHYSEKLRELVSMCIYPDPNQRPDIGYVHQVARQMHVWTSST
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Protein kinase which plays an important role in mitotic cell cycle progression. Required for chromosome segregation at metaphase-anaphase transition, robust mitotic spindle formation and cytokinesis. Phosphorylates ATF4, CIR1, PTN, RAD26L, RBBP6, RPS7, RPS6KB1, TRIP4, STAT3 and histones H1 and H3. Phosphorylates KIF11 to promote mitotic spindle formation. Involved in G2/M phase cell cycle arrest induced by DNA damage. Inhibition of activity results in apoptosis. May contribute to tumorigenesis by suppressing p53/TP53-induced cancer cell senescence (By similarity). Phosphorylates EML4 at 'Ser-144', promoting its dissociation from microtubules during mitosis which is required for efficient chromosome congression (By similarity).
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A2BDX3
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MOCS3_MOUSE
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Adenylyltransferase and sulfurtransferase MOCS3 (Molybdenum cofactor synthesis protein 3) [Includes: Molybdopterin-synthase adenylyltransferase (EC 2.7.7.80) (Adenylyltransferase MOCS3) (Sulfur carrier protein MOCS2A adenylyltransferase); Molybdopterin-synthase sulfurtransferase (EC 2.8.1.11) (Sulfur carrier protein MOCS2A sulfurtransferase) (Sulfurtransferase MOCS3)]
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MAAPEDVAALQAEITRREEELASLKRRLAAALTAEPEPERPLRVPPPPLAPRAALSRDEILRYSRQLLLPELGVRGQLRLAAAAVLVVGCGGLGCPLAQYLAAAGVGRLGLVDHDVVETSNLARQVLHGEAQAGESKARSAAAALRRLNSAVECVAYPRALAEDWALDLVRGYDVVADCCDNVPTRYLVNDACVLAGRPLVSASALRFEGQMTVYHHDGGPCYRCVFPRPPPPETVTNCADGGVLGAVPGVLGCAQALEVLKIAAGLGSSYSGSMLLFDGLGGHFRRIRLRRRRPDCVVCGQQPTVTRLQDYEAFCGSSATDKCRALKLLCPEERISVTDYKRLLDSGAPHVLLDVRPQVEVDICRLPHSLHIPLSQLERRDADSLKLLGAALRKGKQESQEGVALPVYVICKLGNDSQKAVKVLQSLTAVPELDSLTVQDIVGGLMAWAAKIDGTFPQY
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Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and MOCS2A. Its N-terminus first activates URM1 and MOCS2A as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 and MOCS2A to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards URM1 and MOCS2A. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor NFS1 probably acting as a sulfur donor for thiocarboxylation reactions. {ECO:0000255|HAMAP-Rule:MF_03049}.
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A2BGM5
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FOXN4_DANRE
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Forkhead box protein N4
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MTVQSKLQGRGKFKKRFFRAGQQVPRPTLELSSVWLSKIFYNPEQHHNKQKMIESGITTRMSGIHENPGQSHHTSAQDYRLLTTDPSQLKDELPGDLQSLSWLTSVDVPRLQQIGGGRPDFTSSAQSSLLERQTAQLNSMTVAGGAGSAIHLQSEMQHSPLAINSMPQFSPGFPCAASVYQTAPQQVLTFTQANQQCSPGGLYGNYNSQNLFPQPRITAHSQDLQPKCFPKPIYSYSCLIAMALKNSKTGSLPVSEIYSFMKEHFPYFKTAPDGWKNSVRHNLSLNKCFEKVENKMSGSSRKGCLWALNPAKIDKMEEEMQKWKRKDLPAIRRSMANPDELDKLITDRPESCRQKSVDPGMTRLPSCPPGQTLPLAAQMQPQPVVTLSLQCLPMHQHLQLQLQNQSRLAPSSPAPAQTPPLHTVPDMTNSSLPQHPAKQHTDFYTVHTDVNSEVDALDPSIMDFAWQGNLWEEMKDDSFNLEALGTLSNSPLRLSDCDLDTSSVTPVSSAGGLPYPDLQVTGLYSSYSAIDALSNQYMNTQGGTKPIVLL
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Transcription factor essential for neural and some non-neural tissues development. Binds to an 11-bp consensus sequence containing the invariant tetranucleotide 5'-ACGC-3'. During development of the central nervous system, required to specify the amacrine and horizontal cell fates from multipotent retinal progenitors while suppressing the alternative photoreceptor cell fates. Drives commitment of p2 progenitors to the V2b interneuron fates during spinal cord neurogenesis. In development of non-neural tissues, plays an essential role in the specification of the atrioventricular canal.
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A2BH40
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ARI1A_MOUSE
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AT-rich interactive domain-containing protein 1A (ARID domain-containing protein 1A) (BRG1-associated factor 250) (BAF250) (BRG1-associated factor 250a) (BAF250A) (Osa homolog 1) (SWI-like protein) (SWI/SNF complex protein p270) (SWI/SNF-related, matrix-associated, actin-dependent regulator of chromatin subfamily F member 1)
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MAAQVAPAAASSLGNPPPPPSELKKAEQQQREEAGGEAAAAAAERGEMKAAAGQESEGPAVGPPQPLGKELQDGAESNGGGGGGGAGSGGGPGAEPDLKNSNGNAGPRPALNNNLPEPPGGGGGGGSSSSDGVGAPPHSAAAALPPPAYGFGQAYGRSPSAVAAAAAAVFHQQHGGQQSPGLAALQSGGGGGLEPYAGPQQNSHDHGFPNHQYNSYYPNRSAYPPPPQAYALSSPRGGTPGSGAAAAAGSKPPPSSSASASSSSSSFAQQRFGAMGGGGPSAAGGGTPQPTATPTLNQLLTSPSSARGYQGYPGGDYGGGPQDGGAGKGPADMASQCWGAAAAAAAAAAAVSGGAQQRSHHAPMSPGSSGGGGQPLARTPQSSSPMDQMGKMRPQPYGGTNPYSQQQGPPSGPQQGHGYPGQPYGSQTPQRYPMTMQGRAQSAMGSLSYAQQIPPYGQQGPSAYGQQGQTPYYNQQSPHPQQQPPYAQQPPSQTPHAQPSYQQQPQTQQPQLQSSQPPYSQQPSQPPHQQSPTPYPSQQSTTQQHPQSQPPYSQPQAQSPYQQQQPQQPASSSLSQQAAYPQPQPQQSQQTAYSQQRFPPPQELSQDSFGSQASSAPSMTSSKGGQEDMNLSLQSRPSSLPDLSGSIDDLPMGTEGALSPGVSTSGISSSQGEQSNPAQSPFSPHTSPHLPGIRGPSPSPVGSPASVAQSRSGPLSPAAVPGNQMPPRPPSGQSDSIMHPSMNQSSIAQDRGYMQRNPQMPQYTSPQPGSALSPRQPSGGQMHSGVGSYQQNSMGSYGPQGSQYGPQGGYPRQPNYNALPNANYPNAGMAGSMNPMGAGGQMHGQPGIPPYGTLPPGRMAHASMGNRPYGPNMANMPPQVGSGMCPPPGGMNRKTQESAVAMHVAANSIQNRPPGYPNMNQGGMMGTGPPYGQGINSMAGMINPQGPPYPMGGTMANNSAGMAASPEMMGLGDVKLTPATKMNNKADGTPKTESKSKKSSSSTTTNEKITKLYELGGEPERKMWVDRYLAFTEEKAMGMTNLPAVGRKPLDLYRLYVSVKEIGGLTQVNKNKKWRELATNLNVGTSSSAASSLKKQYIQCLYAFECKIERGEDPPPDIFAAADSKKSQPKIQPPSPAGSGSMQGPQTPQSTSSSMAEGGDLKPPTPASTPHSQIPPLPGMSRSNSVGIQDAFPDGSDPTFQKRNSMTPNPGYQPSMNTSDMMGRMSYEPNKDPYGSMRKAPGSDPFMSSGQGPNGGMGDPYSRAAGPGLGSVAMGPRQHYPYGGPYDRVRTEPGIGPEGNMGTGAPQPNLMPSTPDSGMYSPSRYPPQQQQQQQQQHDSYGNQFSTQGTPSSSPFPSQQTTMYQQQQQNYKRPMDGTYGPPAKRHEGEMYSVPYSAGQGQPQQQQLPAAQSQPASQPQAAQPSPQQDVYNQYSNAYPASATAATDRRPAGGPQNQFPFQFGRDRVSAPPGSSAQQNMPPQMMGGPIQASAEVAQQGTMWQGRNDMTYNYANRQNTGSATQGPAYHGVNRTDEMLHTDQRANHEGPWPSHGTRQPPYGPSAPVPPMTRPPPSNYQPPPSMPNHIPQVSSPAPLPRPMENRTSPSKSPFLHSGMKMQKAGPPVPASHIAPTPVQPPMIRRDITFPPGSVEATQPVLKQRRRLTMKDIGTPEAWRVMMSLKSGLLAESTWALDTINILLYDDNSIMTFNLSQLPGLLELLVEYFRRCLIEIFGILKEYEVGDPGQRTLLDPGRFTKVYSPAHTEEEEEEHLDPKLEEEEEEGVGNDEEMAFLGKDKPSSENNEEKLVSKFDKLPVKIVQRNDPFVVDCSDKLGRVQEFDSGLLHWRIGGGDTTEHIQTHFESKIELLPSRPYVPCPTPPRKHLTTVEGTPGTTEQEGPPPDGLPEKRITATMDDMLSTRSSTLTDEGAKSAEATKESSKFPFGISPAQSHRNIKILEDEPHSKDETPLCTLLDWQDSLAKRCVCVSNTIRSLSFVPGNDFEMSKHPGLLLILGKLILLHHKHPERKQAPLTYEKEEEQDQGVSCDKVEWWWDCLEMLRENTLVTLANISGQLDLSPYPESICLPVLDGLLHWAVCPSAEAQDPFSTLGPNAVLSPQRLVLETLSKLSIQDNNVDLILATPPFSRLEKLYSTMVRFLSDRKNPVCREMAVVLLANLAQGDSLAARAIAVQKGSIGNLLGFLEDSLAATQFQQSQASLLHMQNPPFEPTSVDMMRRAARALLALAKVDENHSEFTLYESRLLDISVSPLMNSLVSQVICDVLFLIGQS
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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. Binds DNA non-specifically. 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.
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A2BIE7
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TAPT1_DANRE
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Transmembrane anterior posterior transformation protein 1 homolog
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MADSVAAGLGDENETENEDKEREKRLFSGVKKMEKQAAASDVTETLGFYERKAKCKDRKTNVSDLSLVRFISAELTRGYFLEHNEAKYTERRERVYTCLRIPKELEKLMIFGYFLCLDVFLYVFTLLPLRVLLALVRLLTLPCCGLSGSRILQPAQVCDVLKGFIMVLCYFMMHYVDYSMMYHLIRGQSVIKLYIIYNMLEVADRLFSSFGQDILDALYWTATEPKERKRAHIGVIPHFFMAVLYVFLHAILIMVQATTLNVAFNSHNKSLLTIMMSNNFVEIKGSVFKKFEKNNLFQMSNSDIKERFTNYTLLLIVCLRNMEQFSWNPDHLWVLFPDVCMVIASEIAVDVVKHAFITKFNDITADVYSEYRASLAFDLVSSRQKNAYTDYSDSVSRRMGFIPLPLALLLIRVVTSSVKIQGSLSIVCVLLFYLGMITLKVLNSIVLLGKSCMYVKEANMEEKLFQNPPSAAPSRVSSRAHRTKHTREPPGDPAEEGMSASVTTQPTQQDECPAPQIPTSESDQFLTTPDESEEKSLIQDDSELKHRAPKKDLLEIDRFTICGNRID
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Plays a role in primary cilia formation. Involved in cartilage and bone development. May play a role in the differentiation of cranial neural crest cells. May act as a downstream effector of hoxc8 during development (By similarity).
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A2BIL7
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BAZ1B_DANRE
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Tyrosine-protein kinase BAZ1B (EC 2.7.10.2) (Bromodomain adjacent to zinc finger domain protein 1B) (Williams syndrome transcription factor homolog)
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MAPLLGRKPYPLVKPLSEPPGPGEEVYTIEHTKEAFRNKEEYEARLRRYGERIWTCKSTGSSQLTHKEAWEEEQEVTELLQEEYPVWFEKPVLEIVHHNTVPLDKLVDQVWVEILTKYAVGEKCDLMVGNDKTLSVEVVKIHPLENPPEENAEKKMEGACDSPSSDKENASQENLKKEPQSKEEESRRESLSDRARRSPRKLPTTMKEEKKKWVMPKFLPHKYDVKLVNEDKVISDVPADNLFRTERPPNKEIMRYFIRHYALRLGSGESAPWVVEDELVKKFSLPSKFSDFLLDPHKFLAENPSTKRKSLSSPEGKPRKRLKNVETGTGGEGAKGDKKKNKDSQNIPLSPTIWSHMQVKKVNGSPLKMKNSGTSKKSDEENVLGTPKSSKKQGDKKSSDPKRRRKSGLNKTPNSQRLSKKEDKSLGGAKKPRMKQMTLLDLAKSPAAAGSPKKQRRSSTTGSAKLGKPFPPMALHLLRFYKENKGKEDKKTTLSSLLSKAAKALSPEDRSRLPEELKELVQKRWELLEQKRRWALMSEEEKQSVLKQKRQEVKQKLREKAKERREKEMQVRREMSRRYEDQELEGKNLPAFRLFDMPEGLPNTIFGDVAMVVEFLHCYSGLLMPDDQYPITSIALLEALAGEKAGFLYLNRVLVVLLQTLLQDELAEGYSELDMPLSEIPLTMHSVSELVRLCLRPSDAHEEESARGSDDWQSGADFDDMVSSEFLEKLETAEVFELDPQEKVSLLLALCHRILMTYSVEDHVEAVHQKSAEMWKERVATLKEANDRKRAEKQKRKEQMETKTDGDVLIKAEKKKESTVKKETPKVLPKEEPEPEDMISTVKSRRLMSIQAKKEKEEQERLNKVRMEKEAEEERIRRQKAATEKAFQDAVTKAKLVLRRTPLGTDRNHNRYWLFSDVVPGLYIEKGWVHESIDYSFTLPPEEEPVLTEEEEEEEEVKKEEETEDGEKEDEGSIISASNDISQQGAPSHESSIETTVPKQGQNLWFVCDTPKDFDELLESLHPQGVRESELKIRLQINYQEILHSIHLTKKGNPGLKTCDGHQELLKFLRSDIIEVASRLQKGGLGYLEDTSEFEEFEERVKTLEKLPEFGECVIALQESVIKKFLQGFMAPKQKKKKKTGGEESTTAEEVDDQKKLAEEARVATAVEKWKTAVREAQTFSRMHVLLGMLDACIKWDMSAENARCKVCRRKGEDDKLILCDECNKAFHLFCLRPALYRIPAGEWLCPACQPTIARRSSRGRNYKEDSEEEEDSEEEDEEESEEEDSEEEHRNTGHSLRSRKKVKTSSKSKMQKKPAKPASRSASKTDTNPSKTSPKSSAKPKSRAAPSSPVDIDELVRQSSKPPSRKKDVELQKCEEILQKIMKFRHSWPFREPVSAEEAEDYQDVITSPMDLTTMQGKFKSSEYHSASDFIEDMKLIFSNAEEYNQPSSNVLTCMSRTEEAFVELLQKSLPGVSYLRRRTRKRAATPSDNSDDDDDDEEEDERSKKQKNGKQGKKASSKRKVEHSRTEKYQTKQK
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Atypical tyrosine-protein kinase that plays a central role in chromatin remodeling and acts as a transcription regulator. Involved in DNA damage response by phosphorylating 'Tyr-142' of histone H2AX (H2AXY142ph). H2AXY142ph plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Essential component of the WICH complex, a chromatin remodeling complex that mobilizes nucleosomes and reconfigures irregular chromatin to a regular nucleosomal array structure. The WICH complex regulates the transcription of various genes, has a role in RNA polymerase I and RNA polymerase III transcription, mediates the histone H2AX phosphorylation at 'Tyr-142', and is involved in the maintenance of chromatin structures during DNA replication processes.
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A2BIX4
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SPEE1_HYPBU
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Polyamine aminopropyltransferase 1 (Caldopentamine synthase) (Norspermidine aminopropyltransferase) (EC 2.5.1.126) (Norspermine aminopropyltransferase) (EC 2.5.1.127) (Norspermine synthase) (Spermidine aminopropyltransferase) (EC 2.5.1.79) (Thermospermine synthase) (Triamine/tetramine aminopropyltransferase)
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MELGMFRLNIYQPGGPIGALYPVEKILYHGRSQYQEIMILVLRGFGKTLVLDGLIQSTESDEHIYHETLVHPAMTVHPNPRRVLILGGGEGATLREVLKHNTVEKAVMVDIDGEVVRVAREYLPEWHQGAFDDPRAQVVIMDGFEYIKEAARRGEDFDVIIMDLTDPFGPKIAAKLYTKEAIGLVKSVLRSDGILVTQAGCAALFPEAFEKVYGSVKSLFAHAEEYGVWVPSFMYVNSFVFASDKYRLTDLSMEEVDRRLRERGVETRFYSGLRHYTLIGLGGIRLLEGRGS
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Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high-temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to norspermidine, spermidine and norspermine to yield norspermine, thermospermine and caldopentamine, respectively. It can also synthesize sym-norspermidine (bis(3-aminopropyl)amine) from 1,3-diaminopropane with a very low activity. The biosynthesis of caldohexamine and caldoheptamine from caldopentamine has been also observed.
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A2CEH0
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POC1B_DANRE
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POC1 centriolar protein homolog B (WD repeat domain 51B)
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MASVMEDPTLERHFKGHKDVISCADFNPNNKQLATGSCDKSLMIWNLAPKARAFRFVGHTDVITGVNFAPSGSLVASSSRDQTVRLWTPSIKGESTVFKAHTASVRSVHFSRDGQRLVTASDDKSVKVWGVERKKFLYSLNRHTNWVRCARFSPDGRLIASCGDDRTVRLWDTSSHQCINIFTDYGGSATFVDFNSSGTCIASSGADNTIKIWDIRTNKLIQHYKVHNAGVNCFSFHPSGNYLISGSSDSTIKILDLLEGRLIYTLHGHKGPVLTVTFSRDGDLFASGGADSQVLMWKTNFDSLNYRELLSKHSKRVTPDPPPHLMDIYPRSHHRHHPQNGTVEINPVADTQSTDPQVVEVGRVVFSTTDARNYDGASSSRAQFTSGMDSGPFRTHTQAREEEDENQEERFAGGMTASPAERSGIPSSLTSTLENIVQQLDILTQTVAVLEERLTLTEDKLRTCLDNQVLLMQQNQQLDRSDEESEGPPL
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Plays an important role in centriole assembly and/or stability and ciliogenesis. Involved in early steps of centriole duplication, as well as in the later steps of centriole length control.
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A2CEI6
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PIWL2_DANRE
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Piwi-like protein 2 (EC 3.1.26.-)
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MDPKRPTFPSPPGVIRAPWQQSTEDQSQLLDQPSLGRARGLIMPIDEPLPGRGRAFSVPGEMPVRFGRGITQSIAAEPLVGMARGVRLPMEEGGFGRGRGFLLPTPEPTVGIGRGAAIGPVPTLDIQKAEVEEKMPELQAEVAPTVAKVGSPGTGSSLVSMFRGLGIEPGKTWGRGAAPVGRGAAGDMGADLQPKPTIIGASLTPEREEVRSEESISFLGRGFTGFGRAAMPHMTVGRGPIGPLSPSPSVAAPFSLISASSASEDAPVAPGTPPKVEVKIETVKEPLQKIGTKGSPIPIGSNYIPICCKNDAVFQYHVTFTPNVESLSMRFGMMKEHRPTTGEVVAFDGSILYLPKRLEEVVHLKAERKTDNQEIDIKIQLTKILPPSSDLCIPFYNVVLRRVMKILGLKLVGRNHYDPNAVVILGKHRLQVWPGYSTSIKHTDGGLYLVVDVSHKVLRNDSVLDVMNLIYQGSRESFQDECTKEFVGSIVITRYNNRTYRIDDIEWSKSPKDTFTLADGSVTTFVDYYRKNYGITIKELDQPLLIHRPKERSRPGGKVITGEILLLPELSFMTGIPEKMRKDFRAMKDLTMHINVGAQQHTQSLKQLLHNINSNNEALSELGRWGLSISQEILVTQGRTLPSETICLHSASFVTSPAVDWSRELVRDPSISTVPLNCWAVFYPRRATDQAEELVTTFSRVAGPMGMRVERPIRVELRDDRTETFVKSIHSQLTSEPRVQLVVCIMTGNRDDLYSAIKKLCCIQSPVPSQAINVRTISQPQKLRSVAQKILLQINCKLGGELWTVNVPLKYLMVIGVDVHHDTSKKSRSVMGFVASLNSMLTKWYSRVTFQMPNEEIINGFRVCLLAALQKYYEVNHAFPEKIVIYRDGVSDGQLKTVEHYEIPQILKCFETIPNYEPKLAFIVVQKRISTTLYSYGSDHFGTPSPGTVLDHTVTNRDWVDFYLMAHSIRQGCGLPTHYITVYNTANLTPDHLQRLTFKMCHLYWNWPGTIRVPAPCKYAHKLAFLSGQYLHSEPAIQLSEKLFFL
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Endoribonuclease that plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Plays an essential role in germ cell differentiation and meiosis, independently of the function in transposable elements repression. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. During piRNA biosynthesis, plays a key role in the piRNA amplification loop, also named ping-pong amplification cycle, by acting as a 'slicer-competent' piRNA endoribonuclease that cleaves primary piRNAs, which are then loaded onto 'slicer-incompetent' piwil4 (By similarity). Piwil2 slicing produces a pre-miRNA intermediate, which is then processed in mature piRNAs, and as well as a 16 nucleotide by-product that is degraded (By similarity). Required for piwil4/miwi2 nuclear localization and association with secondary piRNAs antisense (By similarity). Represses circadian rhythms by promoting the stability and activity of core clock components BMAL1 and CLOCK (By similarity).
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A2CG49
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KALRN_MOUSE
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Kalirin (EC 2.7.11.1) (Protein Duo) (Serine/threonine-protein kinase with Dbl- and pleckstrin homology domain)
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MVLSGSFRNDGLKASDVLPILKEKVAFVSGGRDKRGGPILTFPARSNHDRIRQEDLRKLVTYLASVPSEDVCKRGFTVIIDMRGSKWDLIKPLLKTLQEAFPAEIHVALIIKPDNFWQKQKTNFGSSKFIFETSMVSVEGLTKLVDPSQLTEEFDGSLDYNHEEWIELRLSLEEFFNSAVHLLSRLEDLQEMLARKEFPVDVEGSRRLIDEHTQLKKKVLKAPVEELDREGQRLLQCIRCSDGFSGRNCIPGSADFQSLVPKITSLLDKLHSTRQHLHQMWHVRKLKLDQCFQLRLFEQDAEKMFDWISHNKELFLQSHTEIGVSYQHALDLQTQHNHFAMNSMNAYVNINRIMSVASRLSEAGHYASQQIKQISTQLDQEWKSFAAALDERSTILAMSAVFHQKAEQFLSGVDAWCKMCSEGGLPSEMQDLELAIHHHQSLYEQVTQAYTEVSQDGKALLDVLQRPLSPGNSESLTATANYSKAVHQVLDVVHEVLHHQRRLESIWQHRKVRLHQRLQLCVFQQDVQQVLDWIENHGEAFLSKHTGVGKSLHRARALQKRHDDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIYKAARHLEVRIQDFVRRVEQRKLLLDMSVSFHTHTKELWTWMEDLQKEVLEDVCADSVDAVQELIKQFQQQQTATLDATLNVIKEGEDLIQQLRSAPPSLGEPTEARDSAMSNNKTPHSSSISHIESVLQQLDDAQVQMEELFHERKIKLDIFLQLRIFEQYTIEVTAELDAWNEDLLRQMNDFNTEDLTLAEQRLQRHTERKLAMNNMTFEVIQQGQDLHQYIMEVQASGIELICEKDLDLAAQVQELLEFLHEKQHELELNAEQTHKRLEQCLQLRHLQAEVKQVLGWIRNGESMLNASLVNASSLSEAEQLQREHEQFQLAIEKTHQSALQVQQKAEALLQAGHYDADAIRECAEKVALHWQQLMLKMEDRLKLVNASVAFYKTSEQVCSVLESLEQEYRRDEDWCGGRDKLGPAAEMDHVIPLLSKHLEQKEAFLKACTLARRNAEVFLKYIHRNNVSMPSVASHTRGPEQQVKAILSELLQRENRVLHFWTLKKRRLDQCQQYVVFERSAKQALDWIQETGEYYLSTHTSTGETTEETQELLKEYGEFRVPAKQTKEKVKLLIQLADSFVEKGHIHATEIRKWVTTVDKHYRDFSLRMGKYRYSLEKALGVNTEDNKDLELDIIPASLSDREVKLRDANHEINEEKRKSARKKEFIMAELLQTEKAYVRDLHECLETYLWEMTSGVEEIPPGILNKEHIIFGNIQEIYDFHNNIFLKELEKYEQLPEDVGHCFVTWADKFQMYVTYCKNKPDSNQLILEHAGTFFDEIQQRHGLANSISSYLIKPVQRVTKYQLLLKELLTCCEEGKGELKDGLEVMLSVPKKANDAMHVSMLEGFDENLDVQGELILQDAFQVWDPKSLIRKGRERHLFLFEISLVFSKEIKDSSGHTKYVYKNKLLTSELGVTEHVEGDPCKFALWSGRTPSSDNKTVLKASNIETKQEWIKNIREVIQERIIHLKGALKEPIQLPKTPAKLRNNSKRDGVEDGDSQGDGSSQPDTISIASRTSQNTVESDKLSGGCELTVVLQDFSAGHSSELSIQVGQTVELLERPSERPGWCLVRTTERSPPQEGLVPSSALCISHSRSSVEMDCFFPLKDSYSHSSSENGGKSESVAHLQSQPSLNSIHSSPGPKRSTNTLKKWLTSPVRRLNSGKADGNIKKQKKVRDGRKSFDLGSPKPGDETTPQGDSADEKSKKGWGEDEPDEESHTPLPPPMKIFDNDPTQDEMSSLLAARQAPPDVPTAADLVSAIEKLVKNKLTLEGGSYRGSLKDPTGCLNEGMTPPTPPRNLEEEQKAKALRGRMFVLNELVQTEKDYVKDLGIVVEGFMKRIEEKGVPEDMRGKEKIVFGNIHQIYDWHKDFFLAELEKCIQEQDRLAQLFIKHERKLHIYVWYCQNKPRSEYIVAEYDAYFEEVKQEINQRLTLSDFLIKPIQRITKYQLLLKDFLRYSEKAGLECSDIEKAVELMCLVPKRCNDMMNLGRLQGFEGTLTAQGKLLQQDTFYVIELDAGMQSRTKERRVFLFEQIVIFSELLRKGSLTPGYMFKRSIKMNYLVLEDNVDGDPCKFALMNRETSERVILQAANSDIQQAWVQDINQVLETQRDFLNALQSPIEYQRKERSTAVIRSQPPRVPQASPRPYSSGPVGSEKPPKGSSYNPPLPPLKISTSNGSPGFDYHQPGDKFDASKQNDLGGCNGTSTMTVIKDYYALKENEICVSQGEVVQVLAVNQQNMCLVYQPASDHSPAAEGWVPGSILAPLAKATAAAESSDGSIKKSCSWHTLRMRKRADVENSGKNEATGPRKPKDILGNKVSVKETNSSEESECDDLDPNTSMEILNPNFIQEVAPEFLVPLVDVTCLLGDTVLLQCKACGRPKPSITWKGPDQNILDTDNSSATYTISSCDSGESTLKICNLMPQDSGIYTCIAANDHGTASTSATVKVQGVPAAPNRPIAQERSCTSVILRWLPPASTGNCTISGYTVEYREEGSQVWQQSVASTLDTYLVIEDLSPGCPYQFRVSASNPWGISLPSEPSEFVRLPEYDAAADGATISWKENFDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYVTLHDTYESPTSYILILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQISGHFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPWLQPHNGSYSKIPLDTSRLACFIERRKHQNDVRPIPNVKSYIVNRVNQGTSLSHNP
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Promotes the exchange of GDP by GTP. Activates specific Rho GTPase family members, thereby inducing various signaling mechanisms that regulate neuronal shape, growth, and plasticity, through their effects on the actin cytoskeleton. Induces lamellipodia independent of its GEF activity (By similarity).
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A2CG63
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ARI4B_MOUSE
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AT-rich interactive domain-containing protein 4B (ARID domain-containing protein 4B) (180 kDa Sin3-associated polypeptide) (Sin3-associated polypeptide p180) (Histone deacetylase complex subunit SAP180)
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MKALDEPPYLTVGTDVSAKYRGAFCEAKIKTAKRLVKVKVTFRHDSSTVEVQDDHIKGPLKVGAIVEVKNLDGAYQEAVINKLTDASWYTVVFDDGDEKTLRRSSLCLKGERHFAESETLDQLPLTNPEHFGTPVIGKKTNRGRRSNHIPEEESSSSSSDDDEEERKQTDELLGKVVCVDYVSLEKKKAMWFPALVVCPDCSDEIAVKKDNILVRSFKDGKFTSVPRKDVHEITSDTVPKPDAVLKQAFDQALEFHKSRAIPANWKTELKEDSSSSEAEEEEEEEDDEKEKEDNSSEEEEEIEPFPEERENFLQQLYKFMEDRGTPINKRPVLGYRNLNLFKLFRLVHKLGGFDNIESGAVWKQVYQDLGIPVLNSAAGYNVKCAYKKYLYGFEEYCRSANIDFQMALPEKVLNKPCKDCENKEVKVKEESETEIKEVNVEDSKNVMPKEETPAEDESERKENIKPSLGSKKSLLECIPAQSDEEKEAHITKLEENENLEDKDGGRARTEEAFSTEVDGEEEQARSGDETNKEEDEDDEEIEEEEEEDEEEDEDEDDDDNNEEEEFECYPPGMKVQVRYGRGKNQKMYEASIKDSDVEGGEALYLVHYCGWNVRYDEWIKADKIVRPADKNVPKIKHRKKIKNKLDKEKDRDEKYSPKNCKLRRLSKSPFQSNPSPEMVSKLDLADAKNSDTAHIKSIEITSILNGLQASESSAEDSEQEDERCTQDVDNIGKDESKVEHSTHSRNELISKEEQSSPSLLEENKVHTDLVIAKTVSKSPERLRKDMEAISEDTDFEEEDEITKKRKDVKKDTTDKALKPQTKRGKRRYCSADECLQTGSPGKKEDRTKSKEPLCTENSSNSSSDEDEEEKSKAKMTPTKKYNGLEEKRKSLRTTSFYSGFSEVAEKRIKLLNNSDERLQNNRAKDRKDVWSSIQGQWPKKTLKELFSDSDTEAAASPPHPAPDEGAVEESLQTVAEEESCSPIMELEKPLPASVDNKPIEEKPLEVSDRKTEFPSSGSNSVLNTPPTTPESPSSVTITEASQQQSSVTVSVPLPPNQEEVRSIKSETDSTIEVDSVVGELQDLQSEGNSSPAGFDASVSSSSSNQPEPDNPEKACTGQKRVKDTQGVGSSSKKQKRSHKATVVNNKKKGKGTNSSDSEELSAGESVTKTQTIKSVPTGMKTHNSKSPARVQSPGKGGRNGDKDPDLKEPSNRLPKVYKWSFQTSDLENMTSAERISILQEKLQEIRKHYLSLKSEVASIDRRRKRLKKKERESAATSSSSSSPSSSSITAAVMLTLAEPSMSSASQNGMSVECR
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Acts as a transcriptional repressor. May function in the assembly and/or enzymatic activity of the Sin3A corepressor complex or in mediating interactions between the complex and other regulatory complexes (By similarity). Plays a role in the regulation of epigenetic modifications at the PWS/AS imprinting center near the SNRPN promoter, where it might function as part of a complex with RB1 and ARID4A. Involved in spermatogenesis, together with ARID4A, where it functions as a transcriptional coactivator for AR (androgen receptor) and enhances expression of genes required for sperm maturation. Regulates expression of the tight junction protein CLDN3 in the testis, which is important for integrity of the blood-testis barrier. Plays a role in myeloid homeostasis where it regulates the histone methylation state of bone marrow cells and expression of various genes involved in hematopoiesis. May function as a leukemia suppressor.
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A2CI35
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DUSTY_STRPU
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Dual serine/threonine and tyrosine protein kinase (EC 2.7.12.1) (Dusty protein kinase) (Dusty PK) (Receptor-interacting serine/threonine-protein kinase 5)
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MSSRRLGSSRARGRDLAHEVKHFGGLTKHLKKIIFDSNNCLTELKTSDHFEEEVISTLVLPPVADEIVGKVTKNPPALVIFGQTYTSKATLVNKIFREDLFQIVDDSDNNKTWRAVHLKYGSQRNTRLTLTNSFELLNEEPGSPVMRNSWTGIPRVEMLVKEEHQKDACMLSATTEATLNHPLLQCKLQILVTPHNCPGISISQAYNVCTHNVLPVLLYCFDKDQLSEENLRDLQELQNCAGTLPILFVDCREPSEPLVAHRERRLVEDAHEDFDDDSAYDTDERIEGERERHNGLDARLRRRCRPTPNDRPSVIDQLSRAGFISSPEENGRMRGVLDVFTIVNQVEDLHNSAAIVQFIRRSLQYYLIRCCTAMHDLHQHCMNLFITTAFDMQRDILVTPKRIEYARQRENELFDSLKDLTNQKQEQLRSLIQSTVADMTEDLLEQAGNYRFTDLEVSQEGKIQSQKDIKRCTEQIQDLVLARLNACVVEKLIGSVELLRESFLGTLQRCLASLEKIDGDLETSTTVALRQILNAAYQVEVSVRTSSSVVRIIWERMKEFFQSIKPFKTPTRVDTEWKRKVAQTMINNLDESKLAKSICSQFRSRLNNSHESFSTSLRQLEQKHSGRLEKTEEQRMKVRKVYAPRLARLALESTSLRDMVLYGMPKLEREIGRGQYGVVYSCRSWGGVTHCAVKSVVPPDDKHWNDLAMEFHYTRSIAEHDRIVAVIGSVIDHGYGGMGCSPAVLLLMERMQRDLHTAIKANMELPERLHVALDVAEGVRYLHSLGLVHRDIKLKNVLLDKHDRGKITDLGFCKPEAMMSGSIVGTPIHMAPELFSGKYDNSVDTYAFGILLWYVCAGHVKLPQAFEQCANKDHLWTSVKKGVRPERLRPQFDDASWNLMKSSWAGEPSERPLLGEVQSKLQDIYTKALAKREAEGGGGGGAKEQQNLKSDTL
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May act as a positive regulator of ERK phosphorylation downstream of fibroblast growth factor-receptor activation. May induce both caspase-dependent apoptosis and caspase-independent cell death. May play a role in the embryonic development.
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A2D4U1
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OSTCN_ATEGE
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Osteocalcin (Bone Gla protein) (BGP) (Gamma-carboxyglutamic acid-containing protein)
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MRALTLLALLALATLCITGQAGAKPSGAESSKGAAFVSKQEGSEVVKRPRRYLYQWLGAPAPYPDPLEPKREVCELNPDCDELADHIGFQEAYRRFYGPV
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The carboxylated form is one of the main organic components of the bone matrix, which constitutes 1-2% of the total bone protein: it acts as a negative regulator of bone formation and is required to limit bone formation without impairing bone resorption or mineralization. The carboxylated form binds strongly to apatite and calcium. The uncarboxylated form acts as a hormone secreted by osteoblasts, which regulates different cellular processes, such as energy metabolism, male fertility and brain development. Regulates of energy metabolism by acting as a hormone favoring pancreatic beta-cell proliferation, insulin secretion and sensitivity and energy expenditure. Uncarboxylated osteocalcin hormone also promotes testosterone production in the testes: acts as a ligand for G protein-coupled receptor GPRC6A at the surface of Leydig cells, initiating a signaling response that promotes the expression of enzymes required for testosterone synthesis in a CREB-dependent manner. Also acts as a regulator of brain development: osteocalcin hormone crosses the blood-brain barrier and acts as a ligand for GPR158 on neurons, initiating a signaling response that prevents neuronal apoptosis in the hippocampus, favors the synthesis of all monoamine neurotransmitters and inhibits that of gamma-aminobutyric acid (GABA). Osteocalcin also crosses the placenta during pregnancy and maternal osteocalcin is required for fetal brain development.
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A2D5H2
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SIX1_LAGLA
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Homeobox protein SIX1 (Sine oculis homeobox homolog 1)
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MSMLPSFGFTQEQVACVCEVLQQGGNLERLGRFLWSLPACDHLHKNESVLKAKAVVAFHRGNFRELYKILESHQFSPHNHPKLQQLWLKAHYVEAEKLRGRPLGAVGKYRVRRKFPLPRTIWDGEETSYCFKEKSRGVLREWYAHNPYPSPREKRELAEATGLTTTQVSNWFKNRRQRDRAAEAKERENTENNNSSSNKQNQLSPLEGGKPLMSSSEEEFSPPQSPDQNSVLLLQGNMGHARSSNYSLPGLTASQPSHGLQAHQHQLQDSLLGPLTSSLVDLGS
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Transcription factor that is involved in the regulation of cell proliferation, apoptosis and embryonic development (By similarity). Plays an important role in the development of several organs, including kidney, muscle and inner ear (By similarity). Depending on context, functions as transcriptional repressor or activator (By similarity). Lacks an activation domain, and requires interaction with EYA family members for transcription activation (By similarity). Mediates nuclear translocation of EYA1 and EYA2 (By similarity). Binds the 5'-TCA[AG][AG]TTNC-3' motif present in the MEF3 element in the MYOG promoter and CIDEA enhancer (By similarity). Regulates the expression of numerous genes, including MYC, CCNA1, CCND1 and EZR (By similarity). Acts as activator of the IGFBP5 promoter, probably coactivated by EYA2 (By similarity). Repression of precursor cell proliferation in myoblasts is switched to activation through recruitment of EYA3 to the SIX1-DACH1 complex (By similarity). During myogenesis, seems to act together with EYA2 and DACH2 (By similarity). Regulates the expression of CCNA1 (By similarity). Promotes brown adipocyte differentiation (By similarity).
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A2D670
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OSTCN_MACMU
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Osteocalcin (Bone Gla protein) (BGP) (Gamma-carboxyglutamic acid-containing protein)
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MRALTLLALLALATLCITGQAGAKPSGAESSKGAAFVSKQEGSEVVKRPRRYLYQWLGAPAPYPDPLEPKREVCELNPDCDELADHIGFQEAYRRFYGPV
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The carboxylated form is one of the main organic components of the bone matrix, which constitutes 1-2% of the total bone protein: it acts as a negative regulator of bone formation and is required to limit bone formation without impairing bone resorption or mineralization. The carboxylated form binds strongly to apatite and calcium. The uncarboxylated form acts as a hormone secreted by osteoblasts, which regulates different cellular processes, such as energy metabolism, male fertility and brain development. Regulates of energy metabolism by acting as a hormone favoring pancreatic beta-cell proliferation, insulin secretion and sensitivity and energy expenditure. Uncarboxylated osteocalcin hormone also promotes testosterone production in the testes: acts as a ligand for G protein-coupled receptor GPRC6A at the surface of Leydig cells, initiating a signaling response that promotes the expression of enzymes required for testosterone synthesis in a CREB-dependent manner. Also acts as a regulator of brain development: osteocalcin hormone crosses the blood-brain barrier and acts as a ligand for GPR158 on neurons, initiating a signaling response that prevents neuronal apoptosis in the hippocampus, favors the synthesis of all monoamine neurotransmitters and inhibits that of gamma-aminobutyric acid (GABA). Osteocalcin also crosses the placenta during pregnancy and maternal osteocalcin is required for fetal brain development.
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A2ICN5
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MEF2A_PIG
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Myocyte-specific enhancer factor 2A
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MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSSNKLFQYASTDMDKVLLKYTEYNEPHESGTNSDIVEALNKKEHRGCDSPDPDTSYVLTPHTEEKYKKINEEFDNMMRNHKIAPGLPPQNFSMSVTVPVTSPNALSYTNPGSSLVSPSLAASSTLADSSMLSPPQATLHRNVSPGAPQRPPSTGSAGGMLSTSDLTVPNGAGSSPVGNGFVNSRASPNLVGTTGANSLGKVMPTESPPPPGGGNLGMNSRKPDLRVVIPPSSKGMMPPLSEEEELELNTQRISSSQAPQPLATPVVSVTTPSLPQQGLVYSAMPTAYNTDYSLTSADLSALQGFNSPGMLSLGQVSAWQQHHLGQAALSSLVAGGQLSQGSNLSINTNQNINIKSEPISPPRDRMTPSGFQQQQPPPPSQAPQPQPPQPQPQPQPQARQEMGRSPVDSLSSSSSSYDGSDREDPRGDFHSPVVLGRPPNTEDRESPSVKRMRMDAWVT
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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. Also involved in the activation of numerous growth factor- and stress-induced genes. Mediates cellular functions not only in skeletal and cardiac muscle development, but also in neuronal differentiation and survival. Plays diverse roles in the control of cell growth, survival and apoptosis via p38 MAPK signaling in muscle-specific and/or growth factor-related transcription. In cerebellar granule neurons, phosphorylated and sumoylated MEF2A represses transcription of NUR77 promoting synaptic differentiation. Associates with chromatin to the ZNF16 promoter (By similarity).
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A2IDD5
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CCD78_HUMAN
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Coiled-coil domain-containing protein 78 (hsCCDC78)
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MEHAATTGPRPGPPSRRVENVVLRAKDWLPGAPGGTAVWATSLEAEVPPDLALNKEQQLQISKELVDIQITTHHLHEQHEAEIFQLKSEILRLESRVLELELRGDGTSQGCAVPVESDPRHPRAAAQELRHKAQVPGHSDDHRFQVQPKNTMNPENEQHRLGSGLQGEVKWALEHQEARQQALVTRVATLGRQLQGAREEARAAGQRLATQAVVLCSCQGQLRQAEAENARLQLQLKKLKDEYVLRLQHCAWQAVEHADGAGQAPATTALRTFLEATLEDIRAAHRSREQQLARAARSYHKRLVDLSRRHEELLVAYRAPGNPQAIFDIASLDLEPLPVPLVTDFSHREDQHGGPGALLSSPKKRPGGASQGGTSEPQGLDAASWAQIHQKLRDFSRSTQSWNGSGHSCWSGPRWLKSNFLSYRSTWTSTWAGTSTKS
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Component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells that can generate more than 100 centrioles. Deuterosome-mediated centriole amplification occurs in terminally differentiated multiciliated cells (G1/0) and not in S phase. Essential for centriole amplification and is required for CEP152 localization to the deuterosome.
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A2PYH4
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HFM1_HUMAN
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Probable ATP-dependent DNA helicase HFM1 (EC 3.6.4.12) (SEC63 domain-containing protein 1)
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MLKSNDCLFSLENLFFEKPDEVENHPDNEKSLDWFLPPAPLISEIPDTQELEEELESHKLLGQEKRPKMLTSNLKITNEDTNYISLTQKFQFAFPSDKYEQDDLNLEGVGNNDLSHIAGKLTYASQKYKNHIGTEIAPEKSVPDDTKLVNFAEDKGESTSVFRKRLFKISDNIHGSAYSNDNELDSHIGSVKIVQTEMNKGKSRNYSNSKQKFQYSANVFTANNAFSASEIGEGMFKAPSFSVAFQPHDIQEVTENGLGSLKAVTEIPAKFRSIFKEFPYFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPLPWLNIKIVYMAPIKALCSQRFDDWKEKFGPIGLNCKELTGDTVMDDLFEIQHAHIIMTTPEKWDSMTRKWRDNSLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMKTVQSVSQTLKNTSTAIPMRFVAVSATIPNAEDIAEWLSDGERPAVCLKMDESHRPVKLQKVVLGFPCSSNQTEFKFDLTLNYKIASVIQMYSDQKPTLVFCATRKGVQQAASVLVKDAKFIMTVEQKQRLQKYAYSVRDSKLRDILKDGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTMHYAGGLFEEYSETDILQMIGRAGRPQFDTTATAVIMTRLSTRDKYIQMLACRDTVESSLHRHLIEHLNAEIVLHTITDVNIAVEWIRSTLLYIRALKNPSHYGFASGLNKDGIEAKLQELCLKNLNDLSSLDLIKMDEGVNFKPTEAGRLMAWYYITFETVKKFYTISGKETLSDLVTLIAGCKEFLDIQLRINEKKTLNTLNKDPNRITIRFPMEGRIKTREMKVNCLIQAQLGCIPIQDFALTQDTAKIFRHGSRITRWLSDFVAAQEKKFAVLLNSLILAKCFRCKLWENSLHVSKQLEKIGITLSNAIVNAGLTSFKKIEETDARELELILNRHPPFGTQIKETVMYLPKYELKVEQITRYSDTTAEILVTVILRNFEQLQTKRTASDSHYVTLIIGDADNQVVYLHKITDSVLLKAGSWAKKIAVKRALKSEDLSINLISSEFVGLDIQQKLTVFYLEPKRFGNQITMQRKSETQISHSKHSDISTIAGPNKGTTASKKPGNRECNHLCKSKHTCGHDCCKIGVAQKSEIKESTISSYLSDLRNRNAVSSVPPVKRLKIQMNKSQSVDLKEFGFTPKPSLPSISRSEYLNISELPIMEQWDQPEIYGKVRQEPSEYQDKEVLNVNFELGNEVWDDFDDENLEVTSFSTDTEKTKISGFGNTLSSSTRGSKLPLQESKSKFQREMSNSFVSSHEMSDISLSNSAMPKFSASSMTKLPQQAGNAVIVHFQERKPQNLSPEIEKQCFTFSEKNPNSSNYKKVDFFIRNSECKKEVDFSMYHPDDEADEMKSLLGIFDGIF
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Required for crossover formation and complete synapsis of homologous chromosomes during meiosis.
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A2PYL6
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HXK2_HORSE
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Hexokinase-2 (EC 2.7.1.1) (Hexokinase type II) (HK II)
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MIASHLLAYFFTELNHDQVQKVDQYLYHMRLSDETLLEISKRFRKEMEKGLAATTHPTASVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLRVRVTDNGLQKVEMENQIYAIPEDIMQGSGTQLFDHIAGCLANFMDKLQIKDKKLPLGFTFSFPCIQTKLDESFLVSWTKGFKSRGVEGRDVVTLIRKAIQRRGDFDIDIVAMVNDTVATMMTCGYDDQNCEIGLIVGMGSNACYMEEMRYIDTVEGDEGRMCINMEWGAFGDDGTLDDIRTEFDQEIDMGSLNPGQQLFEKMISGMYMGELVRLILVKMAKEELLFRGKLSPELLTTGRFETKDVSEIEGEKDGIQKAREVLVRLGMDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFAKRLQKTVRRLVPNCDIRFLCSEDGSGKGAAMVTAVAYRLAYQHRARLKTLEPLKLSREQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGKRRGVEMHNKIYSIPQDIMHGTGDELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNRLDESILLKWTKGFKASGCEGEDVVTLLKEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNTEWGAFGDNGCLDDFCTEFDVAVDELSLNPGKQRFEKMMSGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCLALQQVRAILQHLGLESTCDDSIIVKEVCTVVAQRAAQLCGAGMAAVVDKIRENRGLDTLKVTVGVDGTLYKLHPHFAKVMRETVKDLAPKCDVSFLESEDGSGKGAALITAVACRIREAGQR
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Catalyzes the phosphorylation of hexose, such as D-glucose and D-fructose, to hexose 6-phosphate (D-glucose 6-phosphate and D-fructose 6-phosphate, respectively). Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate. Plays a key role in maintaining the integrity of the outer mitochondrial membrane by preventing the release of apoptogenic molecules from the intermembrane space and subsequent apoptosis.
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A2PZA5
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FC1_PHOAM
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Fusicoccadiene synthase (FS) (Fusicoccin A biosynthetic gene clusters protein 1) (PaDC4:GGS) [Includes: Fusicocca-2,10(14)-diene synthase (EC 4.2.3.43) (Diterpene cyclase 4) (DC 4); Geranylgeranyl diphosphate synthase (GGDP synthase) (GGS) (EC 2.5.1.29)]
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MEFKYSEVVEPSTYYTEGLCEGIDVRKSKFTTLEDRGAIRAHEDWNKHIGPCGEYRGTLGPRFSFISVAVPECIPERLEVISYANEFAFLHDDVTDHVGHDTGEVENDEMMTVFLEAAHTGAIDTSNKVDIRRAGKKRIQSQLFLEMLAIDPECAKTTMKSWARFVEVGSSRQHETRFVELAKYIPYRIMDVGEMFWFGLVTFGLGLHIPDHELELCRELMANAWIAVGLQNDIWSWPKERDAATLHGKDHVVNAIWVLMQEHQTDVDGAMQICRKLIVEYVAKYLEVIEATKNDESISLDLRKYLDAMLYSISGNVVWSLECPRYNPDVSFNKTQLEWMRQGLPSLESCPVLARSPEIDSDESAVSPTADESDSTEDSLGSGSRQDSSLSTGLSLSPVHSNEGKDLQRVDTDHIFFEKAVLEAPYDYIASMPSKGVRDQFIDALNDWLRVPDVKVGKIKDAVRVLHNSSLLLDDFQDNSPLRRGKPSTHNIFGSAQTVNTATYSIIKAIGQIMEFSAGESVQEVMNSIMILFQGQAMDLFWTYNGHVPSEEEYYRMIDQKTGQLFSIATSLLLNAADNEIPRTKIQSCLHRLTRLLGRCFQIRDDYQNLVSADYTKQKGFCEDLDEGKWSLALIHMIHKQRSHMALLNVLSTGRKHGGMTLEQKQFVLDIIEEEKSLDYTRSVMMDLHVQLRAEIGRIEILLDSPNPAMRLLLELLRV
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Multifunctional diterpene synthase part of the 2 gene clusters that mediate the biosynthesis of fusicoccins, diterpene glucosides that display phytohormone-like activity and function as potent activators of plasma membrane H(+)-ATPases in plants by modifying 14-3-3 proteins and cause the plant disease constriction canker. The first step in the pathway is performed by the fusicoccadiene synthase PaFS that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dimethylallyl diphosphate into geranylgeranyl diphosphate (GGDP) and successively converting GGDP into fusicocca-2,10(14)-diene, a precursor for fusicoccin H. Fusicoccadiene synthase is an allosteric enzyme for GGPP cyclization that generates 64% fusicoccadiene, 9% delta-araneosene, and one additional unidentified diterpene product, when incubated with GGPP. In the absence of isopentenyl diphosphate (IPP), PaFS can also solvolyze the shorter chain geranyl diphosphate (GPP) and farnesyl diphosphate (FPP) as alternative substrates to yield predominantly acyclic products. FPP is converted to farnesol (60.5%), nerolidol (14.0%), and farnesene (14.0%), while GPP is converted to a mixture of geraniol (59.5%) and linalool (35.0%). The second step is the oxidation at the C-8 position by the cytochrome P450 monooxygenase PaP450-2 to yield fusicocca-2,10(14)-diene-8-beta-ol. The cytochrome P450 monooxygenase PaP450-1 then catalyzes the hydroxylation at the C-16 position to produce fusicocca-2,10(14)-diene-8-beta,16-diol. The dioxygenase fc-dox then catalyzes the 16-oxydation of fusicocca-2,10(14)-diene-8-beta,16-diol to yield an aldehyde (8-beta-hydroxyfusicocca-1,10(14)-dien-16-al). The short-chain dehydrogenase/reductase fc-sdr catalyzes the reduction of the aldehyde to yield fusicocca-1,10(14)-diene-8-beta,16-diol. The next step is the hydroxylation at C-9 performed by the cytochrome P450 monooxygenase PaP450-3 that leads to fusicoccin H aglycon which is glycosylated to fusicoccin H by the O-glycosyltransferase PAGT. Hydroxylation at C-12 by the cytochrome P450 monooxygenase PaP450-4 leads then to the production of fusicoccin Q and is followed by methylation by the O-methyltransferase PAMT to yield fusicoccin P. Fusicoccin P is further converted to fusicoccin J via prenylation by the O-glucose prenyltransferase PaPT. Cytochrome P450 monooxygenase PaP450-5 then performs hydroxylation at C-19 to yield dideacetyl-fusicoccin A which is acetylated to 3'-O-deacetyl-fusicoccin A by the O-acetyltransferase PaAT-2. Finally, a another acetylation by the O-acetyltransferase PaAT-1 yields fusicoccin A.
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A2Q0Z0
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EF1A1_HORSE
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Elongation factor 1-alpha 1 (EF-1-alpha-1) (EC 3.6.5.-) (Elongation factor Tu) (EF-Tu) (Eukaryotic elongation factor 1 A-1) (eEF1A-1)
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MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPPYSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGWKVTRKDGNASGTTLLEALDCILPPTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGNVAGDSKNDPPMEAAGFTAQVIILNHPGQISAGYAPVPDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIVDMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKKAAGAGKVTKSAQKAQKAK
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Translation elongation factor that catalyzes the GTP-dependent binding of aminoacyl-tRNA (aa-tRNA) to the A-site of ribosomes during the elongation phase of protein synthesis. Base pairing between the mRNA codon and the aa-tRNA anticodon promotes GTP hydrolysis, releasing the aa-tRNA from EEF1A1 and allowing its accommodation into the ribosome. The growing protein chain is subsequently transferred from the P-site peptidyl tRNA to the A-site aa-tRNA, extending it by one amino acid through ribosome-catalyzed peptide bond formation. Also plays a role in the positive regulation of IFNG transcription in T-helper 1 cells as part of an IFNG promoter-binding complex with TXK and PARP1.
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A2Q0Z1
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HSP7C_HORSE
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Heat shock cognate 71 kDa protein (EC 3.6.4.10) (Heat shock 70 kDa protein 8)
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MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAFNMKATVEDEKLQGKINDEDKQKILDKCNEIINWLDKNQTAEKEEFEHQQKELEKVCNPIITKLYQSAGGMPGGMPGGFPGGGAPPSGGASSGPTIEEVD
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Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, chaperone-mediated autophagy, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle of HSP70, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity of HSP70 for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The HSP70-associated co-chaperones are of three types: J-domain co-chaperones HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1. Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70. Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Substrate recognition component in chaperone-mediated autophagy (CMA), a selective protein degradation process that mediates degradation of proteins with a -KFERQ motif: HSPA8/HSC70 specifically recognizes and binds cytosolic proteins bearing a -KFERQ motif and promotes their recruitment to the surface of the lysosome where they bind to lysosomal protein LAMP2. KFERQ motif-containing proteins are eventually transported into the lysosomal lumen where they are degraded. Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1. Interacts with VGF-derived peptide TLQP-21.
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A2Q5W1
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ERN1_MEDTR
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Ethylene-responsive transcription factor ERN1 (ERF transcription factor ERN1) (NF box-binding protein 1) (Protein ERF REQUIRED FOR NODULATION 1)
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MEIQFQQPNMQNQKAGISVTNKGGKFKGRNRNSNNTNKFVGVRQRPSGRWVAEIKDTTQKIRMWLGTFETAEEAARAYDEAACLLRGSNTRTNFITHVSLDSPLASRIRNLLNNRKGDKKQEDGAVASAPSNSKTTISNTSTITSNDDNKESTLSTCATRNTELFEDAYKPDLSNCKEVFESGSQSNISCGFGPFFDHFSFTQLLDMAKNDDITDASSLELSEFERMKVERQISASLYAINGVHEYMETVQESNEALWDLPPLCSLFC
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Transcription factor involved in symbiotic nodule signaling in response to rhizobial Nod factors (NFs). Binds to the GCC-box (NF-responsive box) of ENOD11 promoter. Acts as transcriptional activator of NF-responsive box-containing target gene promoters in root hairs. Functions as a transcriptional regulator required for root infection by symbiotic rhizobia, infection thread (IT) formation and maintenance, and nodule development. Necessary for NF-induced gene expression and spontaneous nodulation activated by CCAMK. Functions downstream of CCAMK to activate nodulation gene expression. Involved in early stages of root nodule development. Functions redundantly with ERN2. Is essential with ERN2 for the initiation of root hair infection, and nodule organogenesis and development. Required for accurate expression of the NF signaling genes ENOD11 and ENOD12.
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A2QAC0
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LAD_ASPNC
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L-arabinitol 4-dehydrogenase (LAD) (EC 1.1.1.12)
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MATATVLEKANIGVFTNTKHDLWVADAKPTLEEVKNGQGLQPGEVTIEVRSTGICGSDVHFWHAGCIGPMIVTGDHILGHESAGQVVAVAPDVTSLKPGDRVAVEPNIICNACEPCLTGRYNGCENVQFLSTPPVDGLLRRYVNHPAIWCHKIGDMSYEDGALLEPLSVSLAGIERSGLRLGDPCLVTGAGPIGLITLLSARAAGASPIVITDIDEGRLEFAKSLVPDVRTYKVQIGLSAEQNAEGIINVFNDGQGSGPGALRPRIAMECTGVESSVASAIWSVKFGGKVFVIGVGKNEMTVPFMRLSTWEIDLQYQYRYCNTWPRAIRLVRNGVIDLKKLVTHRFLLEDAIKAFETAANPKTGAIKVQIMSSEDDVKAASAGQKI
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Catalyzes the NAD-dependent oxidation of L-arabinitol to L-xylulose in the fungal L-arabinose catabolic pathway. L-arabinose catabolism is important for using plant material as a carbon source. Not active with NADP as cosubstrate.
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A2QAN3
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BGALA_ASPNC
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Beta-galactosidase A (An-beta-gal) (EC 3.2.1.23) (Lactase A)
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MKLSSACAIALLAAQAAGASIKHRINGFTLTEHSDPAKRELLQKYVTWDDKSLFINGERIMIFSGEFHPFRLPVKELQLDIFQKVKALGFNCVSFYVDWALVEGKPGEYRADGIFDLEPFFDAASEAGIYLLARPGPYINAESSGGGFPGWLQRVNGTLRSSDKAYLDATDNYVSHVAATIAKYQITNGGPIILYQPENEYTSGCCGVEFPDPVYMQYVEDQARNAGVVIPLINNDASASGNNAPGTGKGAVDIYGHDSYPLGFDCANPTVWPSGDLPTNFRTLHLEQSPTTPYAIVEFQGGSYDPWGGPGFAACSELLNNEFERVFYKNDFSFQIAIMNLYMIFGGTNWGNLGYPNGYTSYDYGSAVTESRNITREKYSELKLLGNFAKVSPGYLTASPGNLTTSGYADTTDLTVTPLLGNSTGSFFVVRHSDYSSEESTSYKLRLPTSAGSVTIPQLGGTLTLNGRDSKIHVTDYNVSGTNIIYSTAEVFTWKKFADGKVLVLYGGAGEHHELAISTKSNVTVIEGSESGISSKQTSSSVVVGWDVSTTRRIIQVGDLKILLLDRNSAYNYWVPQLATDGTSPGFSTPEKVASSIIVKAGYLVRTAYLKGSGLYLTADFNATTSVEVIGVPSTAKNLFINGDKTSHTVDKNGIWSATVDYNAPDISLPSLKDLDWKYVDTLPEIQSSYDDSLWPAADLKQTKNTLRSLTTPTSLYSSDYGFHTGYLLYRGHFTATGNESTFAIDTQGGSAFGSSVWLNGTYLGSWTGLYANSDYNATYNLPQLQAGKTYVITVVIDNMGLEENWTVGEDLMKTPRGILNFLLAGRPSSAISWKLTGNLGGEDYEDKVRGPLNEGGLYAERQGFHQPEPPSQNWKSSSPLEGLSEAGIGFYSASFDLDLPKGWDVPLFLNIGNSTTPSPYRVQVYVNGYQYAKYISNIGPQTSFPVPEGILNYRGTNWLAVTLWALDSAGGKLESLELSYTTPVLTALGEVESVDQPKYKKRKGAY
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Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.
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A2QHE5
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FDC1_ASPNC
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Ferulic acid decarboxylase 1 (EC 4.1.1.102) (Phenacrylate decarboxylase)
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MSAQPAHLCFRSFVEALKVDNDLVEINTPIDPNLEAAAITRRVCETNDKAPLFNNLIGMKNGLFRILGAPGSLRKSSADRYGRLARHLALPPTASMREILDKMLSASDMPPIPPTIVPTGPCKENSLDDSEFDLTELPVPLIHKSDGGKYIQTYGMHIVQSPDGTWTNWSIARAMVHDKNHLTGLVIPPQHIWQIHQMWKKEGRSDVPWALAFGVPPAAIMASSMPIPDGVTEAGYVGAMTGSSLELVKCDTNDLYVPATSEIVLEGTLSISETGPEGPFGEMHGYIFPGDTHLGAKYKVNRITYRNNAIMPMSSCGRLTDETHTMIGSLAAAEIRKLCQQNDLPITDAFAPFESQVTWVALRVDTEKLRAMKTTSEGFRKRVGDVVFNHKAGYTIHRLVLVGDDIDVYEGKDVLWAFSTRCRPGMDETLFEDVRGFPLIPYMGHGNGPAHRGGKVVSDALMPTEYTTGRNWEAADFNQSYPEDLKQKVLDNWTKMGFSN
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Catalyzes the reversible decarboxylation of aromatic carboxylic acids like ferulic acid, p-coumaric acid or cinnamic acid, producing the corresponding vinyl derivatives 4-vinylphenol, 4-vinylguaiacol, and styrene, respectively, which play the role of aroma metabolites. {ECO:0000255|HAMAP-Rule:MF_03196, ECO:0000269|PubMed:26083754}.
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A2QQ28
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RSP5_ASPNC
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Probable E3 ubiquitin-protein ligase hulA (EC 2.3.2.26) (HECT ubiquitin ligase A) (HECT-type E3 ubiquitin transferase hulA)
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MGSNLPAQPNLRVTIIAADGLYKRDVFRFPDPFAVATVGGEQTHTTSVIKKTLNPYWNEMFDLRVNEDSILAIQIFDQKKFKKKDQGFLGVINVRIGDVIDLQMGGDEMLTRDLKKSNDNLVVHGKLIINLSTNLSTPIPNQANGLHRSHAQSSTSSGLVPQVSSASHPSVSPGQAEPSAAASNVSLHPQRVPSTTRPTSTVGPVNGGPAPPPNGPQGSRTNLSSFEDSQGRLPAGWERREDNLGRTYYVDHNTRTTTWTRPSSNYNEQTQRTQREANMQLERRAHQSRMLPEDRTGANSPNLQESPQPQPQQAHTPPAGGSASAVSMMATGATTAGTGELPPGWEQRTTPEGRPYFVDHNTRTTTWVDPRRQQYIRMYGHNANGGNTTIQQQPVSQLGPLPSGWEMRLTNTARVYFVDHNTKTTTWDDPRLPSSLDQGVPQYKRDFRRKLIYFRSQPALRIMSGQCHVKVRRNNIFEDSYAEIMRQSASDLKKRLMIKFDGEDGLDYGGLSREFFFLLSHEMFNPFYCLFEYSAHDNYTLQINPHSGVNPEHLNYFKFIGRVVGLAIFHRRFLDSFFIGAFYKMMLRKKVSLQDMEGVDEDLHRNLAWTLENDIEGIIELTFSVDDEKFGERTTIDLKPGGRDIPVTNENKGEYVELVTEWKIVKRVEEQFNAFMSGFNELIPADLVNVFDERELELLIGGIADIDVDDWKKHTDYRGYQEQDEVIQNFWKIVRTWDAEQKSRLLQFTTGTSRIPVNGFKDLQGSDGPRRFTIEKSGDPIALPKSHTCFNRLDLPPYKTHDVLEHKLSIAVEETLGFGQE
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E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Probably involved in the regulatory network controlling carbon source utilization.
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A2QTW5
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BPHA_ASPNC
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Benzoate 4-monooxygenase bphA (EC 1.14.14.92) (Benzoate-para-hydroxylase A) (BpH) (Cytochrome P450 monooxygenase cyp53A1)
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MLALLLSPYGAYLGLALLVLYYLLPYLKRAHLRDIPAPGLAAFTNFWLLLQTRRGHRFVVVDNAHKKYGKLVRIAPRHTSIADDGAIQAVYGHGNGFLKSDFYDAFVSIHRGLFNTRDRAEHTRKRKTVSHTFSMKSIGQFEQYIHGNIELFVKQWNRMADTQRNPKTGFASLDALNWFNYLAFDIIGDLAFGAPFGMLDKGKDFAEMRKTPDSPPSYVQAVEVLNRRGEVSATLGCYPALKPFAKYLPDSFFRDGIQAVEDLAGIAVARVNERLRPEVMANNTRVDLLARLMEGKDSNGEKLGRAELTAEALTQLIAGSDTTSNTSCAILYWCMRTPGVIEKLHKVLDEAIPQDVDVPTHAMVKDIPYLQWVIWETMRIHSTSAMGLPREIPAGNPPVTISGHTFYPGDVVSVPSYTIHRSKEIWGPDAEQFVPERWDPARLTPRQKAAFIPFSTGPRACVGRNVAEMELLVICGTVFRLFEFEMQQEGPMETREGFLRKPLGLQVGMKRRQPGSA
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Cytochrome P450 monooxygenase part of the benzoic acid degradation pathway also known as the protocatechuic acid pathway (PubMed:11594739, Ref.5). Benzoic acid debradation begins with the conversion of benzoic acid into 4-hydroxybenzoic acid through hydroxylation by the benzoate-4-monooxygenase bphA, and its partner NADPH-cytochrome P450 reductase cprA which act as a mediator in electron donation from NADPH. 4-Hydroxybenzoic acid is then converted into 3,4-dihydroxybenzoic acid (also called protocatechuic acid) by the p-hydroxybenzoate-m-hydroxylase phhA (Ref.5). Protocatechuic acid is converted into 3-carboxy-cis,cis-muconic acid by the intradiol ring-cleavage dioxygenase prcA, which is further metabolized through the 3-oxoadipate pathway to finally enter the tricarboxylic acid cycle (TCA) (Ref.5).
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A2R2V4
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OTASE_ASPNC
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Ochratoxinase (OTase) (EC 3.4.17.-) (Amidohydrolase 2) (Amidase 2) (Carboxypeptidase Am2)
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MVRRIASATPMVQSPMSPLGTTYCVRPNPVSLNLQRRPLVIASTDEAKVTIIYAGLLIPGDGEPLRNAALVISDKIIAFVGSEADIPKKYLRSTQSTHRVPVLMPGLWDCHMHFGGDDDYYNDYTSGLATHPASSGARLARGCWEALQNGYTSYRDLAGYGCEVAKAINDGTIVGPNVYSSGAALSQTAGHGDIFALPAGEVLGSYGVMNPRPGYWGAGPLCIADGVEEVRRAVRLQIRRGAKVIKVMASGGVMSRDDNPNFAQFSPEELKVIVEEAARQNRIVSAHVHGKAGIMAAIKAGCKSLEHVSYADEEVWELMKEKGILYVATRSVIEIFLASNGEGLVKESWAKLQALADSHLKAYQGAIKAGVTIALGTDTAPGGPTALELQFAVERGGMTPLEAIKAATANAPLSVGPQAPLTGQLREGYEADVIALEENPLEDIKVFQEPKAVTHVWKGGKLFKGPGIGPWGEDARNPFL
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Carboxypeptidase that catalyzes the release of a C-terminal amino acid with specific catalytic activity for aromatic amino acids such as phenylalanine. Is able to degrade ochratoxin A, one of the five major mycotoxins most harmful to humans and animals that is produced by Aspergillus and Penicillium species and occurs in a wide range of agricultural products.
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A2R3H4
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UBA4_ASPNC
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Adenylyltransferase and sulfurtransferase uba4 (Common component for nitrate reductase and xanthine dehydrogenase protein F) (Ubiquitin-like protein activator 4) [Includes: Molybdopterin-synthase adenylyltransferase (EC 2.7.7.80) (Adenylyltransferase uba4) (Sulfur carrier protein MOCS2A adenylyltransferase); Molybdopterin-synthase sulfurtransferase (EC 2.8.1.11) (Sulfur carrier protein MOCS2A sulfurtransferase) (Sulfurtransferase uba4)]
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MNGVEQTCASLRTQIAATEAKLADLKRELEIAEQAAASHKQNAADAEGGSERRWPLLDEEYRRYGRQMIVPQLGIQGQLKLRSAKVLIVGAGGLGCPAALYLAGAGVGTLGLVDGDAVESSNLHRQVLHRTRNIGKLKVDSAIEYLKELNPHSKYIAHREHLAPEAAPEIFSNYDLILDCTDNPATRYLISDTAVLLGKPLVSASALRTEGQLMVLNNPPRPAGDKTGGPCYRCVFPKPPPANTVTSCADGGIVGPVVGTMGVLQALEAIKVITADETTTPPPPSLHIFSAYSTPLFRTIKLRSRRPNCAVCSAEASVTVDTVRSGSTDYIFFCGTTGPENLLSPEERITPLEYRTRHHDKEEKEPTIIDVREKVQYDICSLENSINIPISTILASASSSMSNGDSLADGVPALPSWVPPDVASSQSTDPVYVVCRLGNDSQVAVKKLKELGLDQGGKRVVADIRGGFRAWKEQVDPEWPEY
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Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers urm1 and mocs2a. Its N-terminus first activates urm1 and mocs2a as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to urm1 and mocs2a to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards urm1 and mocs2a. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor nfs1 probably acting as a sulfur donor for thiocarboxylation reactions (By similarity).
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A2R6H1
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OTAA_ASPNC
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Highly reducing polyketide synthase otaA (EC 2.3.1.-) (Ochratoxin biosynthesis cluster protein 1) (Ochratoxin biosynthesis cluster protein A)
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MSSAPIPQSEPLAIIGLACKYANGIDSPEALYEQVMAARCMHGAMPSNRMDASFYYHPTSEATGTSYSKGGYFLNCDLNAFDSPFFQLSEIDVMAMDPQQKMLLENVYHALENAGIPLKNAISSPTSVFVGCSNNDHLALANSDLLLSLKGKGTGTSPSILANRVSWFYDFQGTSQTIDTACSSSLVAFHQGCMDVRAGKSAMSIISGINLIEHPGPTLYLSSLGVLSPDGKSMSFDARANGYGRGEGVGTVIVKPLQAALRDGNRIRAIVRSTGSNQDGRTPGITVPNPSAQERLIHDVYRVADLDPRRTGYVEAHGTGTQVGDPLEVQAILAALGVARDSPLYVGSVKSVLGHLEGGAGLAGLISATLAVESKMIPPVAGLQSLNPKIPQRDDLKFAREATPWPRWDVRRASINSFGFGGTNAHAVVEDVEGFFADLFGQYIPGALPAPEVDTSLETTPMLSKPLMSGNASNQSVQSWSTSRLFVISAFDEAGIQRNTSALAEYLDSKSTTADTDGEDRLLNNLCHTLNEKRTRFDWRSYHVADSIASLRESLQHSRAIRQSSAPKPIRFVFTGQGANWAGMACDMLKYPLFRRRIQEAAAYLRELGSGWDLFERMTSKAGELDEPTFAQSSCVAVQVALVDLLASWKVVPETVVGHSSGEIAAAYCAGHISRQAAWKVAFCRGKVCARRTDGQGRMLAAAMPVHQLERVVARVNKGQPTSVKIGCYNSPRNLTLTGRYDDILRLKLELDDVGALNRMLPVKVAYHSDYMQDAAPEYLSLLGEILDGGDTIHKDASIQMISSVTGQPVPAGDVQQASYWVKNLVSPVRFCTALLASMEFPGTTGKREDTLIEIGPHSTLRSAIKESFAEVPEYQSVQYGSLLKRYETNGSTILHTLGMMFCSGHEISLAAINDRRVGTRKIPMLLTGLPGYAFDHSRSVRGTSRRIEQVKFPTYNRHELLGVPVEDSNPYEQRWRNVLRPDDLPWLRMNRMKGQIHFPGVAYILMATEALQQRVARTMTIPRVRIANMSILAPLQVPDSPSGVEIQVSIYPTNVRANGATDWATFRIISYDTAEKTWVEHCVGSVRAETGPPDLCVNTALRKQCAEPVDIAQMYHGFTAAGMDFGENLRNIQAMKVSPDRTACTATITAPSIAPQAHDQYPLHPCSFESILHALLYLCEASQSPMVTNYIEEVVIVNPNDTGAREFESFARRQRTSATTWTCDVSITTNVGDQDIQIKGLDLVQLPANNDDAVDAESFYTVNWRPDVKLLASADALHNSAPVDAAQHLPTFDEHEGYQLASAIFLQEAKEYVTRTGLPPLPTHHQAFMDWMEEEYQSINNGTTPLLDKSLLDGIRADPDRRKSLLDRVARQSARGELLVRVGTRMIDILEQKIDCLEVMFGPDNLMERTYEEGLPGQIAPAVAGYLHCLAHAQTGIKILEVGAGTGSATKVMLDSLRPTEAQDGGGLVSSVSSYDFTDISAAFFEKARARFHDWADILRPKLLNIEQDPAAQGFELGSYDLVIATHVLHATADLNVSLKNIRALLKEGGDLIVIENIQPKFMCSQLPFGLLPGWWRSVEPYRKTNPLILKEHWTEELQNAGLRPRLIINDTDDGINEMSAFVASPMPKVLDGSQPCSIIYSSTYPGQQQLALEVADRLPRSCTAAVVDLADISLDHSDTVGIVLVGCQGLDLSELTSSEYDRVKFILTSFQKLLWVTCDPTDVPKSALATGLVRSTRWEREHDNVNIILLSVSLSRPTPLTISSEIVRLCENAFISCKRVPPNSEYRIEGSNGVLLTNRLFPAAGINECIGLGSRPRSRQVPLGTVDHPIKLTSIGSQQPNGFHFIEDPQAHEPLDPDEVKIRIHAAGLDEEDADQLSRLIPGHGFGDQGSGTVVEIGHGVQGIQVGDQVMALRTGPSCALQTFFRTHSATVAKIPDGIRLSDAAALPLPWVTAYHSLVTVARLDSQEKVLIHPAIGATGQAAVQVASMLGATVYATVETDAQRQTLAEYGVEESHILDSASVEKQFGTQTSTQGVDVLLNLRRDGLEFLHLSCLSPFGRLVDISGSRAFPSQVNSPSNQSYYRVNMRELSQLKPESIRQTLRTVAQLLASPTIRPVAPFRVGYSQLQRVLSEIRRGSRGPWVIQPLPNDPIPPLGSHQFDPSASYLLIGGFGGLGRSVARWMHHRGAKHFIFFSRSGASSAAARELCADLRAAGCAVSDMICDTTDAQAVAKAMAQCEASMPPIRGCLQASMVLEDSMLSNMDHTRFLGAITPKVQGTINVASALAPIKSNLDFFVMLSSSAGIVGNRGQANYAAANTFLDAFAGQLVTQGYPATSVSLGSVLSVGWVAENQHKLRIAFAFGALSEDLLLSILEYHMDPAWGAAQSIQTCHTVVGVRSARDFQRQSIPLPGFMAHPLFSPLLAIAGRSQTAEQAAEAPVSQGLREASSMEAAVEVVTRAIVHKLARIMALSVQEIDPQRSLGSYGVDSLVTVDLKAWFQREVGVSIGSGELLGEMAMTQLAQQAADASQFLPAELRGKLRKNTDIHV
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Highly reducing polyketide synthase part of the gene cluster that mediates the biosynthesis of ochratoxin A (OTA), a mycotoxin composed of a chlorinated type I polyketide dihydroisocoumarin moiety linked to L-phenylalanine, and demonstrated to have nephrotoxic, immunotoxic, genotoxic, neurotoxic, and teratogenic properties. OtaA catalyzes the condensation of one acetate and 4 malonate units to form the isocoumarin group. The pathway begins with the highly reducing polyketide synthase otaA that catalyzes the formation of the isocoumarin group during the initial stages of biosynthesis, starting from one acetate and 4 malonate units, to originate the characteristic pentaketide skeleton 7-methylmellein (7-MM) of the OTA molecule. The newly identified cyclase otaY might be involved in the polyketide cyclization reaction during the initial steps of the OTA biosynthesis. 7-MM is then oxidized into 7-carboxymellein (also called ochratoxin beta) by the cytochrome P450 monooxygenase otaC. The NRPS encoded by the otaB gene is involved in the linking of phenylalanine to the dihydroisocoumarin ring. The reaction catalyzed by NRPS results in the production of ochratoxin B (OTB), which is the non-chlorinated analog of OTA and which subsequently serves as the substrate of the halogenase otaD for chlorination activity to form the final molecular structure of OTA, containing a chlorine atom in the C-5 position of the molecule (Probable).
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A2RJT9
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PYRDA_LACLM
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Dihydroorotate dehydrogenase A (fumarate) (DHOD A) (DHODase A) (DHOdehase A) (EC 1.3.98.1)
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MLNTTFANAKFANPFMNASGVHCMTIEDLEELKASQAGAYITKSSTLEKREGNPLPRYVDLELGSINSMGLPNLGFDYYLDYVLKNQKENAQEGPIFFSIAGMSAAENIAMLKKIQESDFSGITELNLSCPNVPGKPQLAYDFEATEKLLKEVFTFFTKPLGVKLPPYFDLVHFDIMAEILNQFPLTYVNSVNSIGNGLFIDPEAESVVIKPKDGFGGIGGAYIKPTALANVRAFYTRLKPEIQIIGTGGIETGQDAFEHLLCGATMLQIGTALHKEGPAIFDRIIKELEEIMNQKGYQSIADFHGKLKSL
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Catalyzes the conversion of dihydroorotate to orotate with fumarate as the electron acceptor. Molecular oxygen can replace fumarate in vitro, but cannot use NAD(+) as an electron acceptor.
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A2RRP1
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NBAS_HUMAN
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NBAS subunit of NRZ tethering complex (Neuroblastoma-amplified gene protein) (Neuroblastoma-amplified sequence)
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MAAPESGPALSPGTAEGEEETILYDLLVNTEWPPETEVQPRGNQKHGASFIITKAIRDRLLFLRQYIWYSPAPFLLPDGLVRLVNKQINWHLVLASNGKLLAAVQDQCVEIRSAKDDFTSIIGKCQVPKDPKPQWRRVAWSYDCTLLAYAESTGTVRVFDLMGSELFVISPASSFIGDLSYAIAGLIFLEYKASAQWSAELLVINYRGELRSYLVSVGTNQSYQESHCFSFSSHYPHGINTAIYHPGHRLLLVGGCETAEVGMSKASSCGLSAWRVLSGSPYYKQVTNGGDGVTAVPKTLGLLRMLSVKFYSRQGQEQDGIFKMSLSPDGMLLAAIHFSGKLSIWAIPSLKQQGEWGQNEQPGYDDLNPDWRLSTEKRKKIKDKESFYPLIDVNWWADSAVTLARCSGALTVSSVKTLKNLLGKSCEWFEPSPQVTATHDGGFLSLECEIKLAPKRSRLETRAGEEDEGEEDSDSDYEISAKARYFGYIKQGLYLVTEMERFAPPRKRPRTITKNYRLVSLRSTTPEELYQRKIESEEYEEALSLAHTYGLDTDLVYQRQWRKSAVNVASIQNYLSKIKKRSWVLHECLERVPENVDAAKELLQYGLKGTDLEALLAIGKGADDGRFTLPGEIDIDSISYEELSPPDEEPAKNKKEKELKKRQELLKLVNFSKLTLEQKELCRCRRKLLTYLDRLATYEEILGVPHASEQRYDAEFFKKFRNQNIVLSARTYAQESNVQALEILFTYHGSDLLPHRLAILSNFPETTSPHEYSVLLPEACFNGDSLMIIPWHEHKHRAKDWCEELACRMVVEPNLQDESEFLYAAQPELLRFRMTQLTVEKVMDWYQTRAEEIEHYARQVDCALSLIRLGMERNIPGLLVLCDNLVTLETLVYEARCDVTLTLKELQQMKDIEKLRLLMNSCSEDKYVTSAYQWMVPFLHRCEKQSPGVANELLKEYLVTLAKGDLKFPLKIFQHSKPDLQQKIIPDQDQLMAIALECIYTCERNDQLCLCYDLLECLPERGYGDKTEATTKLHDMVDQLEQILSVSELLEKHGLEKPISFVKNTQSSSEEARKLMVRLTRHTGRKQPPVSESHWRTLLQDMLTMQQNVYTCLDSDACYEIFTESLLCSSRLENIHLAGQMMHCSACSENPPAGIAHKGKPHYRVSYEKSIDLVLAASREYFNSSTNLTDSCMDLARCCLQLITDRPPAIQEELDLIQAVGCLEEFGVKILPLQVRLCPDRISLIKECISQSPTCYKQSTKLLGLAELLRVAGENPEERRGQVLILLVEQALRFHDYKAASMHCQELMATGYPKSWDVCSQLGQSEGYQDLATRQELMAFALTHCPPSSIELLLAASSSLQTEILYQRVNFQIHHEGGENISASPLTSKAVQEDEVGVPGSNSADLLRWTTATTMKVLSNTTTTTKAVLQAVSDGQWWKKSLTYLRPLQGQKCGGAYQIGTTANEDLEKQGCHPFYESVISNPFVAESEGTYDTYQHVPVESFAEVLLRTGKLAEAKNKGEVFPTTEVLLQLASEALPNDMTLALAYLLALPQVLDANRCFEKQSPSALSLQLAAYYYSLQIYARLAPCFRDKCHPLYRADPKELIKMVTRHVTRHEHEAWPEDLISLTKQLHCYNERLLDFTQAQILQGLRKGVDVQRFTADDQYKRETILGLAETLEESVYSIAISLAQRYSVSRWEVFMTHLEFLFTDSGLSTLEIENRAQDLHLFETLKTDPEAFHQHMVKYIYPTIGGFDHERLQYYFTLLENCGCADLGNCAIKPETHIRLLKKFKVVASGLNYKKLTDENMSPLEALEPVLSSQNILSISKLVPKIPEKDGQMLSPSSLYTIWLQKLFWTGDPHLIKQVPGSSPEWLHAYDVCMKYFDRLHPGDLITVVDAVTFSPKAVTKLSVEARKEMTRKAIKTVKHFIEKPRKRNSEDEAQEAKDSKVTYADTLNHLEKSLAHLETLSHSFILSLKNSEQETLQKYSHLYDLSRSEKEKLHDEAVAICLDGQPLAMIQQLLEVAVGPLDISPKDIVQSAIMKIISALSGGSADLGGPRDPLKVLEGVVAAVHASVDKGEELVSPEDLLEWLRPFCADDAWPVRPRIHVLQILGQSFHLTEEDSKLLVFFRTEAILKASWPQRQVDIADIENEENRYCLFMELLESSHHEAEFQHLVLLLQAWPPMKSEYVITNNPWVRLATVMLTRCTMENKEGLGNEVLKMCRSLYNTKQMLPAEGVKELCLLLLNQSLLLPSLKLLLESRDEHLHEMALEQITAVTTVNDSNCDQELLSLLLDAKLLVKCVSTPFYPRIVDHLLASLQQGRWDAEELGRHLREAGHEAEAGSLLLAVRGTHQAFRTFSTALRAAQHWV
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Involved in Golgi-to-endoplasmic reticulum (ER) retrograde transport the function is proposed to depend on its association in the NRZ complex which is believed to play a role in SNARE assembly at the ER. Required for normal embryonic development (By similarity). May play a role in the nonsense-mediated decay pathway of mRNAs containing premature stop codons (By similarity).
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A2RRU4
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SCAP_RAT
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Sterol regulatory element-binding protein cleavage-activating protein (SCAP) (SREBP cleavage-activating protein)
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MTLTERLREKISQAFYNHGLLCASYPIPIILFTGLCILACCYPLLKLPLPGTGPVEFSTPVKGYSPPPADSDHKQGEPSEQPEWYVGAPVAYIQQIFVKSSVSPWHRNLLAVDVFRSPLSRAFQLVEEIRNHVLRDSSGTKSLEEVCLQVTDLLPGLRKLRSLLPEHGCLLLSPGNFWQNDWERFHADPDIIGTIHQHEPKTLQTSATLKDLLFGVPGKYSGVSLYTRKRMVSYTITLVFQRYHAKFLSSLRARLMLLHPSPNCSLRAENLVHVHFKEEIGIAELIPLVTTYIILFAYIYFSTRKIDMVKSKWGLALAAVVTVLSSLLMSVGLCTLFGLTPTLNGGEIFPYLVVVIGLENVLVLTKSVVSTPVDLEVKLRIAQGLSSESWSIMKNVATELGIILIGYFTLVPAIQEFCLFAVVGLVSDFFLQMLFFTTVLSIDIRRMELADLNKRLPPESCLPSAKPVGRPARYERQLAVRPSTPHTITLQPSSFRNLRLPKRLRVIYFLARTRLAQRLIMAGTVVWIGILVYTDPAGLRTYLAAQVTEQSPLGEGSLGPMPVPSGVLPASHPDPAFSIFPPDAPKLPENQTLPGELPEHAVPAEGVQDSRAPEVTWGPEDEELWRKLSFRHWPTLFNYYNITLAKRYISLLPVIPVTLHLNPREALEGRHPQDGRTAWAPPEPLPAGLWETGPKGPGGTQTHGDITLYKVAALGLAAGIVLVLLLLCLYRVLCPRNYGQPGGGAGRRRRGELPCDDYGYAPPETEIVPLVLRGHLMDIECLASDGMLLVSCCLAGQVCVWDAQTGDCLTRIPRPGPRRDSCGGGAFEAQENWERLSDGGKASPEEPGDSPPLRRRPRGPPPPSLFGDQPDLTCLIDTNFSVQLPPEPTQPEPRHRAGCGRSRDSGYDFSRLVQRVYQEEGLAAVHMSALRPPSPGPPLPQASQEEGTAPEKGSPPLAWAPSTAGSIWSLELQGSLIVVGRSSGRLEVWDAIEGVLCCSNEEISSGITALVFLDRRIVAARLNGSLDFFSLETHTSLSPLQFRGTPGRGSSPSSPVYSSSNTVACHLTHTVPCAHQKPITALRAAAGRLVTGSQDHTLRVFRLEDSCCLFTLQGHSGAITTVYIDQTMVLASGGQDGAICLWDVLTGSRVSHTFAHRGDVTSLTCTTSCVISSGLDDFINIWDRSTGIKLYSIQQDLGCGASLGVISDNLLVTGGQGCVSFWDLNYGDLLQTVYLGKNSEAQPARQILVLDNAAIVCNFGSELSLVYVPSVLEKLD
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Escort protein required for cholesterol as well as lipid homeostasis. Regulates export of the SCAP-SREBP complex from the endoplasmic reticulum to the Golgi upon low cholesterol, thereby regulating the processing of sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2. At high sterol concentrations, formation of a ternary complex with INSIG (INSIG1 or INSIG2) leads to mask the ER export signal in SCAP, promoting retention of the complex in the endoplasmic reticulum. Low sterol concentrations trigger release of INSIG, a conformational change in the SSD domain of SCAP, unmasking of the ER export signal, promoting recruitment into COPII-coated vesicles and transport of the SCAP-SREBP to the Golgi: in the Golgi, SREBPs are then processed, releasing the transcription factor fragment of SREBPs from the membrane, its import into the nucleus and up-regulation of LDLR, INSIG1 and the mevalonate pathway. Binds cholesterol via its SSD domain.
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A2RST1
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MGST2_MOUSE
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Microsomal glutathione S-transferase 2 (Microsomal GST-2) (EC 2.5.1.18) (Glutathione peroxidase MGST2) (EC 1.11.1.-) (Leukotriene C4 synthase MGST2) (EC 4.4.1.20) (Microsomal glutathione S-transferase II) (Microsomal GST-II)
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MAGDSSLLAAVSLLSACQQSYFAWRVGRARLKHKIAPPAVTGPLEFERIFRAQQNSLEFYPVFIVMLWMAGWYFNQVFAACLGLLYIYARHKYFWGYAEAAEKRITGFRLSLGILTLLPVLAVLGVASRFLNEYLDFHVAKKLRKPF
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Catalyzes several different glutathione-dependent reactions. Catalyzes the glutathione-dependent reduction of lipid hydroperoxides, such as 5-HPETE. Has glutathione transferase activity, toward xenobiotic electrophiles, such as 1-chloro-2, 4-dinitrobenzene (CDNB). Catalyzes also the conjugation of leukotriene A4 with reduced glutathione to form leukotriene C4 (LTC4) (By similarity). Involved in oxidative DNA damage induced by ER stress and anticancer agents by activating LTC4 biosynthetic machinery in nonimmune cells.
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A2RSY6
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TRM1L_MOUSE
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TRMT1-like protein (EC 2.1.1.-)
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MENMAEEELLPQEKEEAQVRVPTPAPDSAPVPAPAADTALDSAPTPDSDPAPALAPAPAPALSPSLASVPEEAESKRHISIQRRLADLEKLAFGTEGDVDSASSLNSDNPGTENSQTCPLCPKEKFRAYSSHKLRRHLQNLHWKISVEFEGYRMCICHLACRPVKPTIVGEQISSKLGAHYHCIICSATITRRTDMLGHVKRHVNKGETKSRYIAASTAKSSNEILKETDTDIQVFPNYSIPQKTDSYFNPKMKLNRQIIFCTLAALAKERKPLECLDAFGATGIMGLQWAKHLGNAVKVTINDLNENSVTLIQKNCHLNKLKVVVDSEEKEEGDALEDDGTLGDIQVTRMDANVLMHLRSFDFIHLDPFGTSVNYLDSAFRNVRNLGIVSVTSTDISSLYAKAQHVARRHYGCNIVRTEYYKELAARIVVAAVARAAARCNKGIEVLFAVALEHFVLVVVRVLRGPTSADETAKKIQYLIHCQWCEERIFQKDGNMVEENPYRQLPCNCHGSMPGKTAIELGPLWSSSLFNTGFLKRMLFESIHHGLDDIQPLIKTLIFESECTPQSQCSTHAPSNTNKQEENGVFVKTTDDTTIDIYSAQGKRKSNEMAINLAKKQKTDASTAHPPFYYNIHRHSIKGMNMPKLKKFLCCLSQAGFRVSRTHFDPMGIRTDAPLMQFKSILLKYSTPTYTGAQSEGQMPPAAEDTVTDRVEMSVSDKAEASGCRRW
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May play a role in motor coordination and exploratory behavior.
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A2RT67
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DEND3_MOUSE
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DENN domain-containing protein 3
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MAEPAARHLSLPSGLLELCALLGASQDSLRGLEQIAQKRGVKSASSLVPEVLSVFVPPFTTKEDGQVPGASCALGKGRRRSFRKKREKPRMEPWKSHPGDSKGPDSEDVTIPGGVDLLALPQLCFPGCVCVASEPKEDYIHFLVLTDVCGNRTYGVVAQYYRPLHDEYCFYNGKSHWEPSVISARCFVPFAVCVVSRFPYYNSLKDCLSCLLTHLKLCKDFEVDNHIKDFAARLSLIPSPPPGPLHLIFNMKPLQVVFPSRADPESPIVDLDLHLPLLCFRPEKVLQILTCILTEQRIVFFSSDWALLTLMAECFVAYLHPLQWQHTFVPILSGQMLDFVMAPTSFLMGCHLDHFEEVRKEADGLVLIDIDHGSVTCSKSSDDNIDIPDVPLLLAQTFIQRVQSLQLHPDLHLAHLSASTDLNEGRARRRAWQQTLNCKIQHITLQLLVGIFREVKNHLNYEHRVFNSEEFLKTRAAGDQQFYKQVLDTYMFHSFLKARLNGRMDAFARMDLDTQSEEDRIDRMLISPRRPTVEKMASRKASPLHITHRRMVVSMPNLQDISLPELPPRNSSLRIMDTSNCRSSSPVLKVTPKSTYMFKIPDIHFPLESQCVQAYYTDFVTLLSKAMALLGPGDSLLLARYFYLRGLLHLMQGQLLSALLDFQNLYKTDIGIFPADLVKRTVESMSASERAQAERTPELRRLITEVFDKHGEAPKADDAVKNFELPKKHMQLNDFVKRVQESGIVKDAVIIHRLFDALTFGHEKQIDPETFRDFYTCWKETEAEAQEVSLPALLMEHLDKNECVYKLSSSVKTNRGVGKIAMTQKRLFLLTEGRPGYVEIATFRNIEEVKNSTVAFLLLRIPTLKIKTVAKKEVFEANLKSECDLWHLMVKEMWAGKQLADDHKDPQYVQQALTNVLLMDAVVGTLQSPSAIHAASKLAYFDNMKKKSPMAVPKTTSETLKHKINPSAGETAPQAIEVLLYTPGRLDPAEKVEDAHPKLWCALNEGKVVVFDASSWTVHQHCFKVGSSKVNCMVMAEHNQVWVGSEDSVIYIINVHSMSCNKQLTDHRSPVTGLAVHNGKKPSEIYSCSLDGTVIAWNVSTLRVISRFQLSYGDLLSISLHNDRIWCCTVHKILVVTPQGFVRQELKHPKDASFLAFQLLPEEQQLWAASTGVSELYMWSLKDLDQPPQKTYLQDCSEVTCMIRVKRQIWVGGRGLSQGKTRGKIYVMDVEKVTVEKELVAHLDTVRTLCSAEDRYVLSGAGQEEGKIAIWKVE
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Guanine nucleotide exchange factor (GEF) activating Rab12. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab12 into its active GTP-bound form. Regulates autophagy in response to starvation through Rab12 activation. Starvation leads to ULK1/2-dependent phosphorylation of Ser-554 and Ser-572, which in turn allows recruitment of 14-3-3 adapter proteins and leads to up-regulation of GEF activity towards Rab12. Also plays a role in protein transport from recycling endosomes to lysosomes, regulating, for instance, the degradation of the transferrin receptor and of the amino acid transporter PAT4. Starvation also induces phosphorylation at Tyr-940, which leads to up-regulated GEF activity and initiates autophagy.
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A2RTF1
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CTSRB_MOUSE
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Cation channel sperm-associated auxiliary subunit beta (CatSper-beta)
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MESPLIYVMLVLLNVFVFSSGVIHNKGKERTYFSCSGEGILTGLHTIKLFLTMDNLKVRCFFRNENQSPSKEILGLFTSGGLAPNMIITNSTFYGGYYFKLTPFSNRLEWLIDIPRQNITVNTDIAAVEQWMIKITMHEGLNIYDTEGTLLDLVREPILQWNLGRVLTEMEVRDLYPEVNDIKVTKSPCANDVALIGFMMKPSSNGVFIGKTISGFWTYKECIWHDLTEIIYAELKDEHQGLTVIDLVLTNHFLVILTSLGLYVSSDLRYPTTSQIKLSRAEFCGFERVDYIRGNLWYNEKCFANRESFEVDYVTITFNRNRTLSESSSCFFSKEPFLHWLPCVFSTIKNEKSIPRVITFLIDQETDSGIYLFNVQDTKETYVTVAMLKDGKPSPRPKFPSFHFPSTFTLPLGMIFHPRSHFLYVYGSQIWVSMDGGNTFEMLCNLFSHHVTKTSNSFYTSDIVFIVEDGRILTTKAGLTTYSELGILKDAIFTLYYDQLGYIHKLTPENFDAGSKLLGHGNSGSIFGKRPDLGFEAILVPQYISTNEMYFFAHVPLTMPTNIQWKKRFKTIHLGKTIEFSKTGLANIKNVYMHKTEPVGFQTSIHTEIIVPFGIENSKDSPCLLSDLEITYSGKLYYTIKLLSKNPLHELKSTDVEKSVLIPGYSSFLIMNITDKWTASALATMPQAIKSNLKFLTGSWFLYNFGTAGGRKWSISTRQCNYWIQQDSLDFMSLNLVKYIDVGNTIDFQFKIIPKAMSTFPIPPVSMVVGNPGLVEVKTQGVFDLNENYYLDIHVSGRFFQKGSTSIALVLWEGSSKCYAITLLPTIKSSCSYLRTMHHTPGRHIPPEDWISGVHKDSQGFNMIKTLPINYRPPSHMGISIPLTDNFYHADPSKPIPRNQFHKSKETGKYKQCANVTSRAMCNCSEHQKFSHAVAFSDCKEKVHRFKFPVTQYPVVLEIFNERDKISAEPPYLVTMTEVNMRKNWQLKHNEPENVKKMKHYLEPLLKTPVYNPLGLNLTIQGSELFHFKVSVVPGVSFCELSEEFQIYVDEVPLPFPGHALIAVATSVVLGVLIFIAFVFQLRNIHPLKALKKSIRGNPGLTSSTTVSS
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Auxiliary component of the CatSper complex, a complex involved in sperm cell hyperactivation. Sperm cell hyperactivation is needed for sperm motility which is essential late in the preparation of sperm for fertilization.
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A2RTX5
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SYTC2_HUMAN
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Threonine--tRNA ligase 2, cytoplasmic (EC 6.1.1.3) (Threonyl-tRNA synthetase) (ThrRS) (Threonyl-tRNA synthetase protein 3)
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MAAEALAAEAVASRLERQEEDIRWLWSEVERLRDEQLNAPYSCQAEGPCLTREVAQLRAENCDLRHRLCSLRLCLAEERSRQATLESAELEAAQEAGAQPPPSQSQDKDMKKKKMKESEADSEVKHQPIFIKERLKLFEILKKDHQLLLAIYGKKGDTSNIITVRVADGQTVQGEVWKTTPYQVAAEISQELAESTVIAKVNGELWDLDRPLEGDSSLELLTFDNEEAQAVYWHSSAHILGEAMELYYGGHLCYGPPIENGFYYDMFIEDRAVSSTELSALENICKAIIKEKQPFERLEVSKEILLEMFKYNKFKCRILNEKVNTATTTVYRCGPLIDLCKGPHVRHTGKIKTIKIFKNSSTYWEGNPEMETLQRIYGISFPDNKMMRDWEKFQEEAKNRDHRKIGKEQELFFFHDLSPGSCFFLPRGAFIYNTLTDFIREEYHKRDFTEVLSPNMYNSKLWEASGHWQHYSENMFTFEIEKDTFALKPMNCPGHCLMFAHRPRSWREMPIRFADFGVLHRNELSGTLSGLTRVRRFQQDDAHIFCTVEQIEEEIKGCLQFLQSVYSTFGFSFQLNLSTRPENFLGEIEMWNEAEKQLQNSLMDFGEPWKMNPGDGAFYGPKIDIKIKDAIGRYHQCATIQLDFQLPIRFNLTYVSKDGDDKKRPVIIHRAILGSVERMIAILSENYGGKWPFWLSPRQVMVIPVGPTCEKYALQVSSEFFEEGFMADVDLDHSCTLNKKIRNAQLAQYNFILVVGEKEKIDNAVNVRTRDNKIHGEILVTSAIDKLKNLRKTRTLNAEEAF
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Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged tRNA(Thr) via its editing domain, at the post-transfer stage.
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A2RU14
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TM218_HUMAN
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Transmembrane protein 218
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MAGTVLGVGAGVFILALLWVAVLLLCVLLSRASGAARFSVIFLFFGAVIITSVLLLFPRAGEFPAPEVEVKIVDDFFIGRYVLLAFLSAIFLGGLFLVLIHYVLEPIYAKPLHSY
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May be involved in ciliary biogenesis or function.
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A2RU30
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TESP1_HUMAN
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Protein TESPA1 (Thymocyte-expressed positive selection-associated protein 1)
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MEASVLSPTSWEKRRAWLRQSRNWQTQVLEEEAAAALQDVPDPEPSSLDDVFQEGNPINKIEDWLQDCGYSEEGFSEEAGQFIYNGFCSHGTSFEDDLTLGAEATLLAANGKLFSRSFLETARPCQLLDLGCSLASSSMTGGTNKTSSSISEILDKVQEDAEDVLFSLGFGQEDHKDTSRIPARFFTTPSQAKGIDFQLFLKSQVRRIEMEDPCLMLASRFKQVQTLAVTADAFFCLYSYVSKTPVQKFTPSHMFWNCNHPTDVPSIRILSREPEPQSPRDRLRKAISKMCLYTCPRDRPPPPHNTPKRNSLDQVVLEVMDKVKEEKQFLQQDSDLGQFSQEDPVPPAEGKKLPTSPYPCVFCCEEETQQRMSTVLAPSQTLDSNPKVPCCTHSLPIEDPQWSTDPAQIRRELCSLPATNTETHPAKDETFWKRKSRARKSLFQKNLMGRKVKSLDLSITQQKWKQSVDRPELRRSLSQQPQDTFDLEEVQSNSEEEQSQSRWPSRPRHPHHHQTFAGKDS
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Required for the development and maturation of T-cells, its function being essential for the late stages of thymocyte development (By similarity). Plays a role in T-cell antigen receptor (TCR)-mediated activation of the ERK and NFAT signaling pathways, possibly by serving as a scaffolding protein that promotes the assembly of the LAT signalosome in thymocytes. May play a role in the regulation of inositol 1,4,5-trisphosphate receptor-mediated Ca(2+) release and mitochondrial Ca(2+) uptake via the mitochondria-associated endoplasmic reticulum membrane (MAM) compartment. {ECO:0000250, ECO:0000269|PubMed:22561606}.
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A2RU49
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HYKK_HUMAN
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Hydroxylysine kinase (5-hydroxy-L-lysine kinase) (EC 2.7.1.81) (Aminoglycoside phosphotransferase domain-containing protein 1)
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MSSGNYQQSEALSKPTFSEEQASALVESVFGLKVSKVRPLPSYDDQNFHVYVSKTKDGPTEYVLKISNTKASKNPDLIEVQNHIIMFLKAAGFPTASVCHTKGDNTASLVSVDSGSEIKSYLVRLLTYLPGRPIAELPVSPQLLYEIGKLAAKLDKTLQRFHHPKLSSLHRENFIWNLKNVPLLEKYLYALGQNRNREIVEHVIHLFKEEVMTKLSHFRECINHGDLNDHNILIESSKSASGNAEYQVSGILDFGDMSYGYYVFEVAITIMYMMIESKSPIQVGGHVLAGFESITPLTAVEKGALFLLVCSRFCQSLVMAAYSCQLYPENKDYLMVTAKTGWKHLQQMFDMGQKAVEEIWFETAKSYESGISM
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Catalyzes the GTP-dependent phosphorylation of 5-hydroxy-L-lysine.
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A2RUB1
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MEIOC_HUMAN
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Meiosis-specific coiled-coil domain-containing protein MEIOC (Meiosis-specific with coiled-coil domain protein)
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MEVRRGDTCPRPHPSGLREEGLEPKVAFPGGANRCWNLGADAGSRLTDVFGSVMLTGSASFYDCYTSQSEDNVDLRQTYTPFSSTEYSSSVDSSLFCAPWSTYGDDIKQPSNSQISIKNRIQTERNDYGSETDLYGLVSNILEEQDKSQPYFAEGTCSSNLKSVWPMNTSRFADHHDLLTETKRPIDTVISQQAFYSDESVSAMEKQYLRNSNLTPQQKIDELHHGFTGLDLEEQWMYPSRSDHSNCHNIQTNDTAKTTFQEYPLIKNCFTPQTGLSDIMKESGVDIYHYGRDRICTKGLEAPLQQKRAEMFLSQFNRYNENVDYCRYPEYVHPNKAKLNKCSNFSVQDSKKLANGTPETPTVEADTYTKLFQVKPANQKKMEETIPDQQNFTFPKTTPHLTEKQFAKEAVFTADFGLTSEYGLKPHTACPANDFANVTEKQQFAKPDPPHSEYFKSVNLLSNSATSSGGINLNRPTWMNVQTKNNTPIPYRNQGNLMKLNSHLSAASKGSNHSSDFPQLSSTNLTPNSNLFQKYCQENPSAFSSFDFSYSGAERIQSVNHIEGLTKPGEENLFKLVTDKKIKQPNGFCDNYSAQKYGIIENVNKHNFQAKPQSGHYDPEEGPKHLDGLSQNTYQDLLESQGHSNSHRTRGGDNSRVNRTQVSCFSNNYMMGDLRHNQCFQQLGSNGFPLRSTHPFGHSVVPLLDSYDLLSYDDLSHLYPYFNMMYGDNSFSGLMPTFGFQRPIKTRSGPASELHIRLEECCEQWRALEKERKKTELALAKNYPGKKVSSTNNTPVPRLTSNPSRVDRLIVDELRELARVVTLLGKMERLRSSLLHASISTALDRHLESIHIVQSRRKDEIVNASNRQRQGVPRCQDDRDVFALASAIKEMCVATRKTRTALWCALQMTLPKTASTADVVKPLQDTVNCEDKVHESINSSNPMNQRGETNKH
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Is required for meiosis completion in both male and female germ cells. Confers stability to numerous meiotic mRNAs in gonads allowing proper initiation and progression into meiosis prophase I. The function may involve YTHDC2 and is independent of induction by retinoic acid (RA). Maintains an extended meiotic prophase I by properly promoting the transition from a mitotic to a meiotic cell cycle program by binding transcripts through its interaction with YTHDC2 that regulate the mitotic cell cycle.
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A2RUB6
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CCD66_HUMAN
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Coiled-coil domain-containing protein 66
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MNLGDGLKLETELLDGKTKLILSPYEHKSKISVKMGNKAKIAKCPLRTKTGHILKSTQDTCIGSEKLLQKKPVGSETSQAKGEKNGMTFSSTKDLCKQCIDKDCLHIQKEISPATPNMQKTRNTVNTSLVGKQKPHKKHITAENMKSSLVCLTQDQLQQILMTVNQGNRSLSLTENGKEAKSQYSLYLNSISNQPKDENIMGLFKKTEMVSSVPAENKSVLNEHQETSKQCEQKIAIENEWKPADIFSTLGERECDRSSLEAKKAQWRKELDEQVALKKKEKEVSEKWNDPWKKSESDKIIWEKHQILDQSRETVLLEHPFSAVKQELQRKWIEELNKQIEDDRQRKIEEKIIYSKGEEHDRWAMHFDSLKSYPGSQSQLFSQSTHKQPEYFCVSPDTQELADVSSVCTPTTGSQVEPSEEEHIAKPIKDVVMANSKKTNFLRSMTALLDPAQIEERDRRRQKQLEHQKAITAQVEEKRRKKQLEEEQRKKEEQEEELRLAQEREEMQKQYEEDILKQKQKEEIMTLKTNELFQTMQRAQELAQRLKQEQRIRELAQKGHDTSRLIKNLGVDTIQMEYNASNISNSRHDSDEISGKMNTYMNSTTSKKDTGVQTDDLNIGIFTNAESHCGSLMERDITNCSSPEISAELIGQFSTKKNKQELTQDKGASLEKENNRCNDQCNQFTRIEKQTKHMKKYPKRPDWNINKPPKRYIPASEKYPKQLQKQREEKKVRRQMELLHLVEKNNPGHLSQNRGISPEIFHSSHQETESKLRWHLVKKEEEPLNIHSFSKERSPSSPVPVVKNRTQQTQNTLHLPLKNSSYERENLISGSNQTELSSGISESSHFIPYVRTNEIYYLDPDAPLSGPSTQDPQYQNSQDCGQKRQLFDSDCVRDPLLNPNMVKNRDRQQAILKGLSELRQGLLQKQKELESSLLPLAENQEESFGSSF
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Microtubule-binding protein required for ciliogenesis. May function in ciliogenesis by mediating the transport of proteins like BBS4 to the cilium, but also through the organization of the centriolar satellites. Plays a role in retina morphogenesis and/or homeostasis (By similarity).
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A2RUC4
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TYW5_HUMAN
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tRNA wybutosine-synthesizing protein 5 (hTYW5) (tRNA yW-synthesizing protein 5) (EC 1.14.11.42) (tRNA(Phe) (7-(3-amino-3-carboxypropyl)wyosine(37)-C(2))-hydroxylase)
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MAGQHLPVPRLEGVSREQFMQHLYPQRKPLVLEGIDLGPCTSKWTVDYLSQVGGKKEVKIHVAAVAQMDFISKNFVYRTLPFDQLVQRAAEEKHKEFFVSEDEKYYLRSLGEDPRKDVADIRKQFPLLKGDIKFPEFFKEEQFFSSVFRISSPGLQLWTHYDVMDNLLIQVTGKKRVVLFSPRDAQYLYLKGTKSEVLNIDNPDLAKYPLFSKARRYECSLEAGDVLFIPALWFHNVISEEFGVGVNIFWKHLPSECYDKTDTYGNKDPTAASRAAQILDRALKTLAELPEEYRDFYARRMVLHIQDKAYSKNSE
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tRNA hydroxylase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the hydroxylation of 7-(a-amino-a-carboxypropyl)wyosine (yW-72) into undermodified hydroxywybutosine (OHyW*). OHyW* being further transformed into hydroxywybutosine (OHyW) by LCMT2/TYW4. OHyW is a derivative of wybutosine found in higher eukaryotes.
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A2RUH7
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MBPHL_HUMAN
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Myosin-binding protein H-like
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MEAATAPEVAAGSKLKVKEASPADAEPPQASPGQGAGSPTPQLLPPIEEHPKIWLPRALRQTYIRKVGDTVNLLIPFQGKPKPQAIWTHDGCALDTRRVSVRNGEQDSILFIREAQRADSGRYQLRVQLGGLEATATIDILVIERPGPPQSIKLVDVWGFSATLEWTPPQDTGNTALLGYTVQKADTKSGLWFTVLEHYHRTSCIVSDLIIGNSYAFRVFAENQCGLSETAPITTDLAHIQKAATVYKTKGFAQRDFSEAPKFTQPLADCTTVTGYNTQLFCCVRASPRPKIIWLKNKMDIQGNPKYRALTHLGICSLEIRKPGPFDGGIYTCKAVNPLGEASVDCRVDVKVPN
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Myosin-binding protein which plays a role in cardiac function. Seems to regulate conduction in the atria and ventricular conduction systems.
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A2RUV0
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NOTC1_XENTR
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Neurogenic locus notch homolog protein 1 (Notch 1) [Cleaved into: Notch 1 extracellular truncation (NEXT); Notch 1 intracellular domain (NICD)]
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MYRIGLLVLIWSLLGLAQGLRCTQTAEMCLNGGRCEMTPGGTGVCLCSSSYFGERCQYPNPCALKNQCMNFGTCEPVLLGNAIDFTCHCPVGFTDKVCLTPVDNACVNNPCRNGGTCELLSSVSDYRCRCPPGWTGDSCQQADPCASNPCANGGKCLPFETQYICKCPSGFHGATCKQDINECSQNPCRNGGQCLNEFGSYRCNCQNRFTGRNCEEPYVPCNPSPCLNGGTCRQTDDTSYECTCLPGFSGQNCEENIDDCPSNNCRNGGTCVDGVNTYNCQCPPDWTGQYCTEDVDECQLMPNACQNGGTCHNTYGGYNCVCVNGWTGEDCSENIDDCANAACHSGATCHDRVASFFCECPHGRTGLLCHLDNACISNPCNEGSNCDTNPVNGKAICTCPPGYTGPACNNDVDECSLGANPCEHGGRCTNTLGSFQCNCPQGYAGPRCEIDVNECLSNPCQNDATCLDQIGEFQCICMPGYEGLYCETNIDECASNPCLHNGKCVDKINEFHCECPTGFNGNLCQHDVDECASTPCKNGAKCLDGPNSYTCQCTEGFTGRHCEQDINECIPDPCHYGTCKDGIATFTCLCRPGYTGRLCDNDINECLSQPCQNGGQCTDRENGYICTCPKGTTGVNCETNLDDCASNPCDYGKCIDKIDGYECTCEPGYTGKMCNINIDECASNPCRNGGTCKDKINGFTCVCPDGYHDHMCLSEVNECNSNPCIHGTCHDGINGYKCDCDAGWSGSNCDVNNNECESNPCMNGGTCKDMTGAYICTCRAGFSGPNCQTNINECASNPCLNRGTCIDDVAGYKCNCMLPYTGAICEAVLAPCSGSPCKNGGRCKESEDYETFSCECPPGWQGQTCEIDMNECVNRPCRNGAMCQNTNGSYKCNCKPGYAGRHCETDIDDCQPNPCHNGGSCSDGINMFFCNCPAGFRGPKCEEDINECASNPCKNGANCTDCVNSYTCTCQPGFSGIHCENNTPDCTESSCFNGGTCIDGINTFSCQCPPGFTGNYCQHDINECDSKPCLNGGTCQDSYGAYKCTCPQGYTGLNCQNLVRWCDSSPCKNGGKCWQTNNFYRCECKSGWTGVYCDVPSVSCEVAAKQQGVDIAHLCRNSGMCVDTGNTHFCRCQAGYTGSYCEEQVDECSPNPCQNGATCTDYLGGYSCECVAGYHGVNCSEEINECLSHPCHNGGTCIDLINTYKCSCPRGTQGVHCEINVDDCTPFYDSVSLEPKCFNNGKCFDRVGGYNCICPPGFVGERCEGDVNECLSNPCDPRGTQNCIQLVNDYRCECRQGFTGRRCDSVVDGCKGLPCRNGGTCAVASNTERGFICKCPPGFDGATCEYDARTCGNLRCQNGGTCISVLKSSKCVCSEGYTGATCQYPVVSPCASRPCYNGGTCQFSPEEPFFQCFCPTNFNGLFCHILDYGFIGGLGKNITPPDNEEICENEQCAELADNKICNANCNNHACGWDGGDCSLNFNDPWKNCTQSLQCWKYFNDGKCDSQCNNSGCLYDGFDCQKVEVQCNPLYDQYCRDHFQDGHCDQGCNNAECEWDGLDCDNMPENLAEGTLLIVVLMPPEKLKNNSVNFLRELSRVLHTNVVFKKDSKGEYKIYPYYGNEEELKKHHIKKRSAASWSDAPTAIFSTMKESVLPGRRRRELDQMEVRGSIVYLEIDNRQCYKSSSQCFTSATDVAAFLGALATHGNLNIPYKIEAVKSEIVETAKPPPPLYAMFSMLVIPLLIIFVIMVVIVNKKRRREHGQLWFPEGFIPKEPSKKKRREPLGEDSVGLKPLKNLTDGSFMDDNQNEWGDEETLENKRFRFEEQVMLPELVDDQTDHRQWTQQHLDAADLRIPSMAPTPPQGEIDADCMDVNVRGPDGFTPLMIAACSGGGLETGNSEEEEDASANMISDFIGQGAQLHNQTDRTGETALHLAARYARADAAKRLLESSADANVPDNMGRTPLHAAVAADAQGVFQILIRNRATDLDARMCDGTTPLILAARLAVEGMVEELINAHADVNAVDEFGKSALHWAAAVNNVDAAAVLLKSSANKDMQNNKEETPLFLAAREGSYETAKVLLDHYANRDITDHMDRLPRDIAQERMHHDIVHLLDEHNLVKSPTLHGGPLGAPTLSPPICSPNGYMGNMKPSVQSKKARKPSIKGNGCKEAKELKARRKKSQDGKTSLLDSGSSGVLSPVDSLESPHGYLSDVASPPLMTSPFQQSPSMPLNHLTSMQDSHLGLNHMTMANKQEMASNRMAFDGMTPRLTHLNVSSPNTIMTNGSMHFTVGGAPAMNGQCDWFARLQNGMVQNQYNPIRNGIQQGNAQQALQHGLMSSLHNGLPATTLSQMMTYQAMPNTRMANQPHLMQAQQMQQQQNLQLHQSVQQQQHQNSNATSTHIGSPFCSNDISQTDLQQMSGNNIHSVMPQDTQIFTNSLPPTLTQSMATTQFLTPPSQHSYSSPMDNTPSHQLQVPDHPFLTPSPESPDQWSSSSPHSNMSDWSEGISSPPTSMQPQRTHIPEAFK
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Functions as a receptor for membrane-bound ligands Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs. Involved in angiogenesis negatively regulates endothelial cell proliferation and migration and angiogenic sprouting. Involved in the maturation of both CD4(+) and CD8(+) cells in the thymus. Important for follicular differentiation and possibly cell fate selection within the follicle. During cerebellar development, functions as a receptor for neuronal DNER and is involved in the differentiation of Bergmann glia. Represses neuronal and myogenic differentiation. May play an essential role in postimplantation development, probably in some aspect of cell specification and/or differentiation. May be involved in mesoderm development, somite formation and neurogenesis (By similarity). Involved in determination of left/right symmetry by modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO).
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A2RUV9
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AEBP1_RAT
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Adipocyte enhancer-binding protein 1 (AE-binding protein 1) (Aortic carboxypeptidase-like protein)
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MAAVRTASLLCGLLALLALCPEGSPQTVLTDDEIQEFLEGFLSEFETQSPPREDDVEAQPLPEPTQRARKSKAGGKPRADAEAPPEKNKDKEKKGKKDKGPKAAKHLEGSTRPTKKPKEKPPKATKKPKEKPPKATKKPKEKPPKATKKPKEKPPKATKRPSAGKRFSTVAPLETPERSLTSPSNPGTRELPEERGRTSLNTWQGQGEETQVEARQHRPEPEEETEMPTLDYNDQIEREDYEDFEYIRRQKQPRPTPSRKRIWPEPPEEKTQEPEERKEVDPPLKPLLPPDYGDGYLIPNYDDLDYYFPHPPPQKPDVGQEVDEEKEELKKPKKEGSSPKEDTEDKWAAEKNKDHKAGPRKGEELEEEWGPVEKIKCPPIGMESHRIEDNQIRASSMLRHGLGAQRGRLNMQAGANEDDYYDGAWCAEDESQTQWIEVDTRRTTRFTGVITQGRDSSIHDDFVTTFFVGFSNDSQTWVMYTNGYEEMTFHGNVDKDTPVLSELPEPVVARFIRIYPLTWNGSLCMRLEVLGCPVTPVYSYYAQNEVVTTDSLDFRHHSYKDMRQLMKVVNEECPTITRTYSLGKSSRGLKIYAMEISDNPGEHELGEPEFRYTAGMHGNEVLGRELLLLLMQYLCHEYRDGNPRVRNLVQDTRIHLVPSLNPDGYEVAAQMGSEFGNWALGLWTEEGFDIFEDFPDLNSVLWAAEEKKWVPYRVPNNNLPIPERYLSPDATVSTEVRAIISWMEKNPFVLGANLNGGERLVSYPYDMARTPSQEQLLAAALAAARGEDEDEVSEAQETPDHAIFRWLAISFASAHLTMTEPYRGGCQAQDYTSGMGIVNGAKWNPRSGTFNDFSYLHTNCLELSIYLGCDKFPHESELPREWENNKEALLTFMEQVHRGIKGVVTDEQGIPIANATISVSGINHGVKTASGGDYWRILNPGEYRVTAHAEGYTSSAKICNVDYDIGATQCNFILARSNWKRIREILAMNGNRPILRVDPSRPMTPQQRRLQQRRLRYRLRMREQMRLRRLNSTTGPATSPTPALTLPPSPTPGSTSRLWEILPTTAAGWEESETETYTEVVTEFETEYGPDLEVEELEEEEEEEEEMDTGLTFPVTTVETYTVNFGDF
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As a positive regulator of collagen fibrillogenesis, it is probably involved in the organization and remodeling of the extracellular matrix (By similarity). May positively regulate MAP-kinase activity in adipocytes, leading to enhanced adipocyte proliferation and reduced adipocyte differentiation. May also positively regulate NF-kappa-B activity in macrophages by promoting the phosphorylation and subsequent degradation of I-kappa-B-alpha (NFKBIA), leading to enhanced macrophage inflammatory responsiveness. Can act as a transcriptional repressor.
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A2RUW1
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TOLIP_RAT
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Toll-interacting protein
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MATTVSTQRGPVYIGELPQDFLRITPTQQQQQIQLDAQAAQQLQYGGAVGTVGRLSITVVQAKLAKNYGMTRMDPYCRLRLGYAVYETPTAHNGAKNPRWNKVIQCTVPPGVDSFYLEIFDERAFSMDDRIAWTHITIPESLKQGQVEDEWYSLSGRQGDDKEGMINLVMSYTSLPAAMMMPPQPVVLMPTVYQQGVGYVPIAGMPAVCSPGMVPMAMPPPAVAPQPRCNEEDLKAIQDMFPNMDREVIRSVLEAQRGNKDAAINSLLQMGEES
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Component of the signaling pathway of IL-1 and Toll-like receptors (By similarity). Inhibits cell activation by microbial products (By similarity). Recruits IRAK1 to the IL-1 receptor complex (By similarity). Inhibits IRAK1 phosphorylation and kinase activity. Connects the ubiquitin pathway to autophagy by functioning as a ubiquitin-ATG8 family adapter and thus mediating autophagic clearance of ubiquitin conjugates (By similarity). The TOLLIP-dependent selective autophagy pathway plays an important role in clearance of cytotoxic polyQ proteins aggregates (By similarity). In a complex with TOM1, recruits ubiquitin-conjugated proteins onto early endosomes (By similarity). Binds to phosphatidylinositol 3-phosphate (PtdIns(3)P) (By similarity).
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A2RVJ8
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HIT4_ARATH
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Protein HEAT INTOLERANT 4
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MKKGAKRKGVSKAGRKAAVAETQNDEVIEETTKTTQEESQQHEEEVVDEVKENGEEEEAKGDQEEEEDAKPDSLEEDEENQEDEVKAEEVKEEVEKKPVARRGGKRKRATKKDTEIKDEKKPVPKAKKPRAAKVKEEPVYFEEKRSLEDLWKVAFPVGTEWDQLDALYEFNWDFQNLEEALEEGGKLYGKKVYVFGCTEPQLVPYKGANKIVHVPAVVVIESPFPPSDKIGITSVQREVEEIIPMKKMKMDWLPYIPIEKRDRQVDKMNSQIFTLGCTQRRSALRHMKEDQLKKFEYCLPYFYQPFKEDELEQSTEVQIMFPSEPPVVCEFDWEFDELQEFVDKLVEEEALPAEQADEFKEYVKEQVRAAKKANREAKDARKKAIEEMSEDTKQAFQKMKFYKFYPQPSPDTPDVSGVQSPFINRYYGKAHEVL
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Essential protein required for basal thermotolerance, especially during heat-induced chromocentre decondensation, thus regulating transcriptional gene silencing (TGS).
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A2RVK7
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RP41L_ARATH
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Exosome complex component RRP41-like (Protein SLOWER GROWTH) (Ribosomal RNA-processing protein 41-like)
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MAAKPGAATPTYSPKIVGRSRLPIFKDSDLDWSRPDGRGFHQCRPALLQTGAVSSASGSAYAEFGNTKVIVSVFGPRESKKAMVYSDVGRLNCNVSYTNFASPTLGQGTDHKEYSSMLHKALEGVIMMETFPKTTVDVFALVLESGGSDLSVLISCASLALADAGIMMYDLITAVSVSCIGKSLMIDPVTEEEGCEDGSFMMTCMPSRYEITQLTITGEWTTPNINEAMQLCLDASSKLGEIMRDCLKQSASASDE
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Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing, maturation and degradation events. In vitro, is a processive phosphorolytic exonuclease and requires a single-stranded poly(A) tail on the substrate RNA for its activity (By similarity). Plays an important role in seed germination and early seedling growth by mediating specific cytoplasmic mRNA decay of transcripts coding for the abscisic acid (ABA) biosynthetic enzymes NCED5 and NCED6, and the ABA signaling transcription factors ABI3 and ABI4.
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A2RVM0
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TIC32_ARATH
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Short-chain dehydrogenase TIC 32, chloroplastic (EC 1.1.1.-) (Translocon at the inner envelope membrane of chloroplasts 32) (AtTIC32)
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MWFFGSKGASGFSSRSTAEEVTHGVDGTGLTAIVTGASSGIGVETARVLSLRGVHVVMAVRNTDSGAKVKEDIVKQVPGAKLDVMELDLSSMQSVRKFASEYKSTGLPLNLLINNAGIMACPFMLSKDNIELQFATNHLGHFLLTKLLLDTMKSTSRESKREGRIVNLSSEAHRFSYPEGVRFDKINDKSSYSSMRAYGQSKLCNVLHANELTKQLKEDGVNITANSLHPGAIMTNLGRYFNPYLAVAVGAVAKYILKSVPQGAATTCYVALNPQVAGVSGEYFQDSNIAKPLPLVKDTELAKKVWDFSTKLTDSQSGESSS
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Involved in protein precursor import into chloroplasts. Part of the redox regulon consisting of TIC32, TIC 55 and TIC62.
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A2RVQ5
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AGL16_ARATH
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Agamous-like MADS-box protein AGL16
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MGRGKIAIKRINNSTSRQVTFSKRRNGLLKKAKELAILCDAEVGVIIFSSTGRLYDFSSSSMKSVIERYSDAKGETSSENDPASEIQFWQKEAAILKRQLHNLQENHRQMMGEELSGLSVEALQNLENQLELSLRGVRMKKDQMLIEEIQVLNREGNLVHQENLDLHKKVNLMHQQNMELHEKVSEVEGVKIANKNSLLTNGLDMRDTSNEHVHLQLSQPQHDHETHSKAIQLNYFSFIA
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Probable transcription factor involved in the regulation of flowering time in long-day photoperiod. Participates in the repression of FT expression and floral transition, by interacting closely with the FLC-SVP pathways. Functions in the satellite meristemoid lineage of stomatal development.
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A2RVU1
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MWL1_ARATH
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Protein MODIFYING WALL LIGNIN-1 (MWL-1)
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MFIFLFGLAAFFLCLSAEFQKAKALLRAQVFLKGKDLKWDGESCYLPENRAFGLGIAALVCVSVAQIVGNVVICRGFTKTDKTRTTIFCIILLLFSWVNFAVAVTLISVGASMNREQIYGKGWLNRECYLVKDGVFAASGFLSVTTMAAILGAFAFKVKPSLQVENHDKRHTQNV
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Together with MWL2, contributes to secondary cell wall biology, specifically lignin biosynthesis.
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A2SWM2
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SPNS2_DANRE
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Sphingosine-1-phosphate transporter SPNS2 (Protein spinster homolog 2) (Protein two of hearts)
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MCVESDGCEIEGCSSSDEVHTLSGSMSPALKSRDLHHCRPGQKFHAALLRCRTPLVAAGILSFGNVLNYMDRYTVAGVLLDIQKQFKVGDSSAGLLQTVFICSFMVAAPIFGYLGDRFNRKIILSCGIFFWSAVTLLSSFITKEYYWLLVLSRCLVGIGESSYSSISPTIIGDLFTNNKRTVMLSVFYLAIPLGSGLGYILGSIAKDAGGHWYWALRVSPMLGLTAGTLILIFVSEPKRGSADQPGGRLKTRTSWVCDMKALAKNRSYVFSSLASAAVSFATGAFGIWIPQYLVRAQVVQKSAESCTYQPCSSRDSLIFGAITCVTGLLGVVIGAVTTRLCRQKTERADPLVCAVSMLGSAIFICLIFVVAKKSIVGAYICIFIGETLLFLNWAITADILMYVVIPTRRATAVAFQGFTSHLLGDAGSPYLIGLISDSLQESYATSEIWQFLSLGYALMLCPFVIVLGGMFFLATALFFLDDRDKAAKQVNQLARPPSTVKVTK
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Lipid transporter that specifically mediates export of sphingosine-1-phosphate (sphing-4-enine 1-phosphate, S1P) and sphinganine-1-phosphate, which play critical roles in regulating heart development. Mediates the export of S1P from cells in the extraembryonic yolk syncytial layer (YSL), thereby regulating myocardial precursor migration.
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A2SZS3
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L_RVFV
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RNA-directed RNA polymerase L (Protein L) (EC 2.7.7.48) (Large structural protein) (Replicase) (Transcriptase) [Includes: cap-snatching endonuclease (EC 3.1.-.-)]
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MDSILSKQLVDKTGFVRVPIKHFDCTMLTLALPTFDVSKMVDRITIDFNLDDIQGASEIGSTLLPSMSIDVEDMANFVHDFTFGHLADKTDRLLMREFPMMNDGFDHLSPDMIIKTTSGMYNIVEFTTFRGDERGAFQAAMTKLAKYEVPCENRSQGRTVVLYVVSAYRHGVWSNLELEDSEAEEMVYRYRLALSVMDELRTLFPELSSTDEELGKTERELLAMVSSIQINWSVTESVFPPFSREMFDRFRSSPPDSEYITRIVSRCLINSQEKLINSSFFAEGNDKALRFSKNAEECSLAVERALNQYRAEDNLRDLNDHKSTIQLPPWLSYHDVDGKDLCPLQGLDVRGDHPMCNLWREVVTSANLEEIERMHDDAAAELEFALSGVKDRPDERNRYHRVHLNMGSDDSVYIAALGVNGKKHKADTLVQQMRDRSKQPFSPDHDVDHISEFLSACSSDLWATDEDLYNPLSCDKELRLAAQRIHQPSLSERGFNEIITEHYKFMGSRIGSWCQMVSLIGAELSASVKQHVKPNYFVIKRLLGSGIFLLIKPTSSKSHIFVSFAIKRSCWAFDLSTSRVFKPYIDAGDLLVTDFVSYKLSKLTNLCKCVSLMESSFSFWAEAFGIPSWNFVGDLFRSSDSAAMDASYMGKLSLLTLLEDKAATEELQTIARYIIMEGFVSPPEIPKPHKMTSKFPKVLRSELQVYLLNCLCRTIQRIAGEPFILKKKDGSISWGGMFNPFSGRPLLDMQPLISCCYNGYFKNKEEETEPSSLSGMYKKIIELEHLRPQSDAFLGYKDPELPRMHEFSVSYLKEACNHAKLVLRSLYGQNFMEQIDNQIIRELSGLTLERLATLKATSNFNENWYVYKDVADKNYTRDKLLVKMSKYASEGKSLAIQKFEDCMRQIESQGCMHICLFKKQQHGGLREIYVMGAEERIVQSVVETIARSIGKFFASDTLCNPPNKVKIPETHGIRARKQCKGPVWTCATSDDARKWNQGHFVTKFALMLCEFTSPKWWPLIIRGCSMFTRKRMMMNLNYLKILDGHRELDIRDDFVMDLFKAYHGEAEVPWAFKGKTYLETTTGMMQGILHYTSSLLHTIHQEYIRSLSFKIFNLKVAPEMSKGLVCDMMQGSDDSSMLISFPADDEKVLTRCKVAAAICFRMKKELGVYLAIYPSEKSTANTDFVMEYNSEFYFHTQHVRPTIRWIAACCSLPEVETLVARQEEASNLMTSVTEGGGSFSLAAMIQQAQCTLHYMLMGMGVSELFLEYKKAVLKWNDPGLGFFLLDNPYACGLGGFRFNLFKAITRTDLQKLYAFFMKKVKGSAARDWADEDVTIPETCSVSPGGALILSSSLKWGSRKKFQKLRDRLNIPENWIELINENPEVLYRAPRTGPEILLRIAEKVHSPGVVSSLSSGNAVCKVMASAVYFLSATIFEDTGRPEFNFLEDSKYSLLQKMAAYSGFHGFNDMEPEDILFLFPNIEELESLDSIVYNKGEIDIIPRVNIRDATQTRVTIFNEQKTLRTSPEKLVSDKWFGTQKSRIGKTTFLAEWEKLKKIVKWLEDTPEATLAHTPLNNHIQVRNFFARMESKPRTVRITGAPVKKRSGVSKIAMVIRDNFSRMGHLRGVEDLAGFTRSVSAEILKHFLFCILQGPYSESYKLQLIYRVLSSVSNVEIKESDGKTKTNLIGILQRFLDGDHVVPIIEEMGAGTVGGFIKRQQSKVVQNKVVYYGVGIWRGFMDGYQVHLEIENDIGQPPRLRNVTTNCQSSPWDLSIPIRQWAEDMGVTNNQDYSSKSSRGARYWMHSFRMQGPSKPFGCPVYIIKGDMSDVIRLRKEEVEMKVRGSTLNLYTKHHSHQDLHILSYTASDNDLSPGIFKSISDEGVAQALQLFEREPSNCWVRCESVAPKFISAILEICEGKRQIRGINRTRLSEIVRICSESSLRSKVGSMFSFVANVEEAHDVDYDALMDLMIEDAKNNAFSHVVDCIELDVSGPYEMESFDTSDVNLFGPAHYKDISSLSMIAHPLMDKFVDYAISKMGRASVRKVLETGRCSSKDYDLSKVLFRTLQRPEESIRIDDLELYEETDVADDMLG
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RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate (Probable). During transcription, synthesizes subgenomic RNAs and assures their capping by a cap-snatching mechanism, which involves the endonuclease activity cleaving the host capped pre-mRNAs (By similarity). These short capped RNAs are then used as primers for viral transcription. The 3'-end of subgenomic mRNAs molecules are not polyadenylated. During replication, the polymerase binds the 5' and 3' vRNA extremities at distinct sites (By similarity). In turn, significant conformational changes occur in the polymerase and in vRNA to initiate active RNA synthesis (By similarity). As a consequence of the use of the same enzyme for both transcription and replication, these mechanisms need to be well coordinated (By similarity).
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A2T1U1
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ORANG_BRAOB
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Protein ORANGE, chloroplastic (BoOr) (DnaJ-like cysteine-rich domain-containing protein Or)
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MSCLGRILSVSYPPDPYGSRLSVSKLSSPGRNRRLRWRFTALDSDSSSLDSDSSDKFAAGFCIIEGPETVQDFAKMQLQEIQDNIRSRRNKIFLHMEEVRRLRIQQRIRNTELGIIDEEQEHELPNFPSFIPFLPPLTAANLRVYYATCFSLIAGIILFGGLLAPTLELKLGIGGTSYKDFIQSLHLPMQLSQVDPIVASFSGGAVGVISALMVVEVNNVKQQEHKRCKYCLGTGYLACARCSSTGSLIISEPVSAIAGGNHSVSTSKTERCSNCSGAGKVMCPTCLCTGMAMASEHDPRIDPFL
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Involved in chromoplast differentiation. Is associated with a cellular process that triggers the differentiation of pro-plastids or other non-colored plastids into chromoplasts for carotenoid accumulation. Associated with carotenoid accumulation in de-etiolated cotyledons. Controls leaf petiole elongation by suppressing the expression of ERF1 genes.
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A2T2X4
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IFT46_CHLRE
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Intraflagellar transport protein 46 (Flagellar-associated protein 32) (IFT complex B protein)
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MDDSMDYPDRDGDDLDQFQGTARSQVVQNQPHDEEVNLSESESFAGADEPPAAPRDASLIESHDMDEGPAAPARTLSPTGYEAGKHAPGGIANSDEAPPGAYNAQEYKHLNVGEDVRELFSYIGRYKPQTVELDTRIKPFIPDYIPAVGGIDEFIKVPRPDTKPDYLGLKVLDEPAAKQSDPTVLTLQLRQLSKEAPGAKADMVGRLEHTDENKAKKIQQWIASINDIHKAKPAATVNYSKRMPEIEALMQEWPPEVETFLKTMHMPSGDVELDIKTYARLVCTLLDIPVYDDPVESLHVLFTLYLEFKNNPIFRQHMEMENKLDGMSGGGGGMMGGGADVLGL
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Forms part of a complex involved in intraflagellar transport (IFT), the bi-directional movement of particles required for the assembly, maintenance and functioning of primary cilia. Plays a role in maintaining IFT complex B stability.
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A2T3P0
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NSP2_ROTSH
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Non-structural protein 2 (NSP2) (EC 3.6.4.-) (NCVP3) (Non-structural RNA-binding protein 35) (NS35)
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MAELACFCYPHLENDSYKFIPFNNLAIKAMLTAKVDKKDMDKFYDSIIYGIAPPPQFKKRYNTNDNSRGMNFETIMFTKVAMLICEALNSLKVTQANVSNVLSRVVSIRHLENLVIRKENPQDILFHSKDLLLKSTLIAIGQSKEIETTITAEGGEIVFQNAAFTMWKLTYLEHQLMPILDQNFIEYKVTLNEDKPISDVHVKELVAELRWQYNKFAVITHGKGHYRIVKYSSVANHADRVYATFKSNVKTGVNNDFNLLDQRIIWQNWYAFTSSMKQGNTLDVCKRLLFQKMKPEKNPFKGLSTDRKMDEVSQVGV
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Participates in replication and packaging of the viral genome. Plays a crucial role, together with NSP5, in the formation of virus factories (viroplasms) which are large inclusions in the host cytoplasm where replication intermediates are assembled and viral RNA replication takes place. Displays ssRNA binding, NTPase, RNA triphosphatase (RTPase) and ATP-independent helix-unwinding activities. The unwinding activity may prepare and organize plus-strand RNAs for packaging and replication by removing interfering secondary structures. The RTPase activity plays a role in the removal of the gamma-phosphate from the rotavirus RNA minus strands of dsRNA genome segments. {ECO:0000255|HAMAP-Rule:MF_04089, ECO:0000269|PubMed:14699117}.
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A2T3P5
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VP7_ROTSH
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Outer capsid glycoprotein VP7
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MYGIEYTTVLTFLISIILLNYILKSLTRIMDFIIYRFLFIIVILSPFLRAQNYGINLPITGSMDTAYANSTQEETFLTSTLCLYYPTEAATEINDNSWKDTLSQLFLTKGWPTGSVYFKEYTNIASFSVDPQLYCDYNVVLMKYDATLQLDMSELADLILNEWLCNPMDITLYYYQQTDEANKWISMGSSCTIKVCPLNTQTLGIGCLTTDATTFEEVATAEKLVITDVVDGVNHKLDVTTATCTIRNCKKLGPRENVAVIQVGGSDILDITADPTTAPQTERMMRINWKKWWQVFYTVVDYVDQIIQVMSKRSRSLNSAAFYYRV
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Calcium-binding protein that interacts with rotavirus cell receptors once the initial attachment by VP4 has been achieved. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. Following entry into the host cell, low intracellular or intravesicular Ca(2+) concentration probably causes the calcium-stabilized VP7 trimers to dissociate from the virion. This step is probably necessary for the membrane-disrupting entry step and the release of VP4, which is locked onto the virion by VP7 (By similarity). {ECO:0000255|HAMAP-Rule:MF_04131, ECO:0000269|PubMed:10590110, ECO:0000269|PubMed:9144247, ECO:0000303|PubMed:15165605}.
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A2T3Q9
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NSP5_ROTSH
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Non-structural protein 5 (NSP5) (NS26)
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MSLSIDVTSLPSIPSTIYKNESSSTTSTLSGKSIGRSEQYISPDAEAFNKYMLSKSPEDIGPSDSASNDPLTSFSIRSNAVKTNADAGVSMDSSAQSRPSSNVGCDQVDFSLNKGLKVKANLDSSISISTDTKKEKSKQNHKSRKHYPRIEAESDSDDYVLDDSDSDDGKCKNCKYKKKYFALRMRMKQVAMQLIEDL
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Plays an essential role in the viral genome replication. Participates, together with NSP2, in the formation of viral factories (viroplasms) which are large inclusions in the host cytoplasm where replication intermediates are assembled and viral RNA replication takes place. Orchestrates the recruitment of viroplasmic proteins such as capsid proteins to these factories. {ECO:0000255|HAMAP-Rule:MF_04092, ECO:0000269|PubMed:11884570, ECO:0000269|PubMed:17825341}.
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A2T3S5
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VP3_ROTSH
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Protein VP3 [Includes: 2',5'-phosphodiesterase (EC 3.1.4.-); mRNA guanylyltransferase (EC 2.7.7.50); mRNA (guanine-N(7))-methyltransferase (EC 2.1.1.56)]
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MKVLALRHSVAQVYADTQVYVHDDTKDSYENAFLISNLTTHNILYLNYSIKTLEILNKSGIAAIALQSLEELFTLIRCNFTYDYELDIIYLHDYSYYTNNEIRTDQHWITKTNIEEYLLPGWKLTYVGYNGSETRGHYNFSFKCQNAATDDDLIIEYIYSEALDFQNFMLKKIKERMTTSLPIARLSNRVFRDKLFPSLLKEHKNVVNVGPRNESMFTFLNYPTIKQFSNGAYLVKDTIKLKQERWLGKRISQFDIGQYKNMLNVLTAIYYYYNLYKSKPIIYMIGSAPSYWIYDVRHYSDFFFETWDPLDTPYSSIHHKELFFINDVKKLKDNSILYIDIRTDRGNADWKKWRKTVEEQTINNLDIAYEYLRTGKAKVCCVKMTAMDLELPISAKLLHHPTTEIRSEFYLLLDTWDLTNIRRFIPKGVLYSFINNIITENVFIQQPFKVKVLNDSYIVALYALSNDFNNRSEVIKLINNQKQSLITVRINNTFKDEPKVGFKNIYDWTFLPTDFDTKEAIITSYDGCLGLFGLSISLASKPTGNNHLFILSGTDKYYKLDQFANHTSISRRSHQIRFSESATSYSGYIFRDLSNNNFNLIGTNIENSVSGHVYNALIYYRYNYSFDLKRWIYLHSIDKVDIEGGKYYELAPIELIYACRSAKEFATLQDDLTVLRYSNEIENYINTVYSITYADDPNYFIGIQFRNIPYKYDVKIPHLTFGVLHISDNMVPDVIDILKIMKNELFKMDITTSYTYMLSDGIYVANVSGVLSTYFKIYNVFYKNQITFGQSRMFIPHITLSFNNMRTVRIETTKLQIKSIYLRKIKGDTVFDMVE
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Multifunctional enzyme involved in mRNA capping. Catalyzes the formation of the 5' cap structure on the viral plus-strand transcripts. Specifically binds to GTP and displays guanylyltransferase and methyltransferase activities. Has affinity for ssRNA but not for dsRNA. Capping activity is non-specific and caps RNAs that initiate with either a G or an A residue. Together with VP1 polymerase, forms a VP1-VP3 complex positioned near the channels situated at each of the five-fold vertices of the core. Following infection, the outermost layer of the virus is lost, leaving a double-layered particle (DLP) made up of the core and VP6 shell. VP1 then catalyzes the transcription of fully conservative plus-strand genomic RNAs that are capped by VP3 and extruded through the DLP's channels into the cytoplasm where they function as mRNAs for translation of viral proteins. DLPs probably have an RNA triphosphatase activity as well, whereas open cores do not. {ECO:0000255|HAMAP-Rule:MF_04128, ECO:0000305|PubMed:10603323}. Counteracts the host innate immune response thanks to its phosphodiesterase that degrades the 5'-triphosphorylated, 2'-5' linked adenylate oligomers produced by the host cell IFN-inducible 2',5'-oligoadenylate synthetase (OAS). The host RNaseL is therefore not activated. {ECO:0000255|HAMAP-Rule:MF_04128, ECO:0000269|PubMed:23878220}.
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A2T3T2
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VP4_ROTSH
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Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
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MASLIYRQLLTNSYTVDLSDEIQEIGSTKSQNVTINPGPFAQTGYAPVNWGPGEINDSTTVEPLLDGPYQPTTFNPPVDYWMLLAPTTPGVIVEGTNNTDRWLATILIEPNVQSENRTYTIFGIQEQLTVSNTSQDQWKFIDVVKTTANGSIGQYGPLLSSPKLYAVMKHNEKLYTYEGQTPNARTAHYSTTNYDSVNMTAFCDFYIIPRSEESKCTEYINNGLPPIQNTRNVVPLSLTARDVIHYRAQANEDIVISKTSLWKEMQYNRDITIRFKFANTIIKSGGLGYKWSEISFKPANYQYTYTRDGEEVTAHTTCSVNGVNDFSFNGGYLPTDFVVSKFEVIKENSYVYIDYWDDSQAFRNVVYVRSLAANLNSVMCTGGSYNFSLPVGQWPVLTGGAVSLHSAGVTLSTQFTDFVSLNSLRFRFRLAVEEPHFKLTRTRLDRLYGLPAADPNNGKEYYEIAGRFSLISLVPSNDDYQTPIANSVTVRQDLERQLGELREEFNALSQEIAMSQLIDLALLPLDMFSMFSGIKSTIDAAKSMATNVMKKFKKSGLANSVSTLTDSLSDAASSISRGSSIRSIGSSASAWTDVSTQITDISSSVSSVSTQTSTISRRLRLKEMATQTEGMNFDDISAAVLKTKIDKSTQISPNTIPDIVTEASEKFIPNRAYRVINNDDVFEAGIDGKFFAYKVDTFEEIPFDVQKFADLVTDSPVISAIIDFKTLKNLNDNYGITKQQAFNLLRSDPRVLREFINQDNPIIRNRIEQLIMQCRL
|
[Outer capsid protein VP4]: Spike-forming protein that mediates virion attachment to the host epithelial cell receptors and plays a major role in cell penetration, determination of host range restriction and virulence. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. It is subsequently lost, together with VP7, following virus entry into the host cell. Following entry into the host cell, low intracellular or intravesicular Ca(2+) concentration probably causes the calcium-stabilized VP7 trimers to dissociate from the virion. This step is probably necessary for the membrane-disrupting entry step and the release of VP4, which is locked onto the virion by VP7. During the virus exit from the host cell, VP4 seems to be required to target the newly formed virions to the host cell lipid rafts (By similarity). {ECO:0000255|HAMAP-Rule:MF_04132, ECO:0000269|PubMed:1649333, ECO:0000269|PubMed:9144247, ECO:0000303|PubMed:15165605}. [Outer capsid protein VP5*]: Forms the spike 'foot' and 'body' and acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm. During entry, the part of VP5* that protrudes from the virus folds back on itself and reorganizes from a local dimer to a trimer. This reorganization may be linked to membrane penetration by exposing VP5* hydrophobic region. In integrin-dependent strains, VP5* targets the integrin heterodimer ITGA2/ITGB1 for cell attachment. {ECO:0000255|HAMAP-Rule:MF_04132}. [Outer capsid protein VP8*]: Forms the head of the spikes and mediates the recognition of specific host cell surface glycans. It is the viral hemagglutinin and an important target of neutralizing antibodies. In sialic acid-dependent strains, VP8* binds to host cell sialic acid, most probably a ganglioside, providing the initial contact. In some other strains, VP8* mediates the attachment to histo-blood group antigens (HBGAs) for viral entry. {ECO:0000255|HAMAP-Rule:MF_04132}.
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A2T6K4
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OSTCN_MACNE
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Osteocalcin (Bone Gla protein) (BGP) (Gamma-carboxyglutamic acid-containing protein)
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MRALTLLALLALATLCITGQAGAKPSGAESSKGAAFVSKQEGSEVVKRPRRYLYQWLGAPAPYPDPLEPKREVCELNPDCDELADHIGFQEAYRRFYGPV
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The carboxylated form is one of the main organic components of the bone matrix, which constitutes 1-2% of the total bone protein: it acts as a negative regulator of bone formation and is required to limit bone formation without impairing bone resorption or mineralization. The carboxylated form binds strongly to apatite and calcium. The uncarboxylated form acts as a hormone secreted by osteoblasts, which regulates different cellular processes, such as energy metabolism, male fertility and brain development. Regulates of energy metabolism by acting as a hormone favoring pancreatic beta-cell proliferation, insulin secretion and sensitivity and energy expenditure. Uncarboxylated osteocalcin hormone also promotes testosterone production in the testes: acts as a ligand for G protein-coupled receptor GPRC6A at the surface of Leydig cells, initiating a signaling response that promotes the expression of enzymes required for testosterone synthesis in a CREB-dependent manner. Also acts as a regulator of brain development: osteocalcin hormone crosses the blood-brain barrier and acts as a ligand for GPR158 on neurons, initiating a signaling response that prevents neuronal apoptosis in the hippocampus, favors the synthesis of all monoamine neurotransmitters and inhibits that of gamma-aminobutyric acid (GABA). Osteocalcin also crosses the placenta during pregnancy and maternal osteocalcin is required for fetal brain development.
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A2T6Y4
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APEX1_PANTR
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DNA-(apurinic or apyrimidinic site) endonuclease (EC 3.1.11.2) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) endonuclease, mitochondrial]
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MPKRGKKGAVAEDGDELRTEPEAKKSKTAAKKNDKEAAGEGPALYEDPPDQKTSPSGKPATLKICSWNVDGLRAWIKKKGLDWVKEEAPDILCLQETKCSENKLPAELQELPGLSHQYWSAPSDKEGYSGVGLLSRQCPLKVSYGIGEEEHDQEGRVIVAEFDSFVLVTAYVPNAGRGLVRLEYRQRWDEAFRKFLKGLASRKPLVLCGDLNVAHEEIDLRNPKGNKKNAGFTPQERQGFGELLQAVPLADSFRHLYPNTPYAYTFWTYMMNARSKNVGWRLDYFLLSHSLLPALCDSKIRSKALGSDHCPITLYLAL
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Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 are DNA repair and redox regulation of transcriptional factors. Functions as a apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Does also incise at AP sites in the DNA strand of DNA/RNA hybrids, single-stranded DNA regions of R-loop structures, and single-stranded RNA molecules. Has a 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER. Possesses a DNA 3' phosphodiesterase activity capable of removing lesions (such as phosphoglycolate) blocking the 3' side of DNA strand breaks. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. Acts as a loading factor for POLB onto non-incised AP sites in DNA and stimulates the 5'-terminal deoxyribose 5'-phosphate (dRp) excision activity of POLB. Plays a role in the protection from granzymes-mediated cellular repair leading to cell death. Also involved in the DNA cleavage step of class switch recombination (CSR). On the other hand, APEX1 also exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain, such as the FOS/JUN AP-1 complex after exposure to IR. Involved in calcium-dependent down-regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs). Together with HNRNPL or the dimer XRCC5/XRCC6, associates with nCaRE, acting as an activator of transcriptional repression. Stimulates the YBX1-mediated MDR1 promoter activity, when acetylated at Lys-6 and Lys-7, leading to drug resistance. Acts also as an endoribonuclease involved in the control of single-stranded RNA metabolism. Plays a role in regulating MYC mRNA turnover by preferentially cleaving in between UA and CA dinucleotides of the MYC coding region determinant (CRD). In association with NMD1, plays a role in the rRNA quality control process during cell cycle progression. Associates, together with YBX1, on the MDR1 promoter. Together with NPM1, associates with rRNA. Binds DNA and RNA (By similarity).
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A2T756
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PDX1_PANTR
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Pancreas/duodenum homeobox protein 1 (Homeodomain protein PDX1) (Insulin promoter factor 1) (IPF-1)
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MNGEEQYYAATQLYKDSCAFQRGPAPEFSAGPPACLYMGRQPPPPPPHPFPGALGALEQGSPPDISPYEVPPLADDPAVAHLHHHLPAQLALPHPPAGPFPEGAEPGVLEEPNRVQLPFPWMKSTKAHAWKGQWAGGAYAAEPEENKRTRTAYTRAQLLELEKEFLFNKYISRPRRVELAVMLNLTERHIKIWFQNRRMKWKKEEDKKRGGGTAVGGGGVAEPEQDCAVTSGEELLALPPPPPPGGAVPPAAPVAAREGRLPPGLSASPQPSSVAPRRPQEPR
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Activates insulin and somatostatin gene transcription. Key regulator of islet peptide hormone expression but also responsible for the development of the pancreas, most probably by determining maturation and differentiation of common pancreatic precursor cells in the developing gut. As part of a PDX1:PBX1b:MEIS2b complex in pancreatic acinar cells is involved in the transcriptional activation of the ELA1 enhancer the complex binds to the enhancer B element and cooperates with the transcription factor 1 complex (PTF1) bound to the enhancer A element. Binds the DNA sequence 5'-CC[CT]TAATGGG-3' (By similarity).
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A2T7I6
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APEX1_PONPY
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DNA-(apurinic or apyrimidinic site) endonuclease (EC 3.1.11.2) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) endonuclease, mitochondrial]
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MPKRGKKGAVAEDGDELKTEPEAKKSKTTAKKNDKEAAGEGPALYEDPPDQKTSPSGKPATLKICSWNVDGLRAWIKKKGLDWVKEEAPDILCLQETKCSENKLPAELQELPGLSHQYWSAPSDKEGYSGVGLLSRQCPLKVSYGIGEEEHDQEGRVIVAEFDSFVLVTAYVPNAGRGLVRLEYRQRWDEAFRRFLKGLASRKPLVLCGDLNVAHEEIDLRNPKGNKKNAGFTPQERQGFGELLQAVPLADSFRHLYPNTPYAYTFWTYMMNARSKNVGWRLDYFLLSHSLLTALCDSKIRSKALGSDHCPITLYLAL
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Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 are DNA repair and redox regulation of transcriptional factors. Functions as a apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Does also incise at AP sites in the DNA strand of DNA/RNA hybrids, single-stranded DNA regions of R-loop structures, and single-stranded RNA molecules. Has a 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER. Possesses a DNA 3' phosphodiesterase activity capable of removing lesions (such as phosphoglycolate) blocking the 3' side of DNA strand breaks. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. Acts as a loading factor for POLB onto non-incised AP sites in DNA and stimulates the 5'-terminal deoxyribose 5'-phosphate (dRp) excision activity of POLB. Plays a role in the protection from granzymes-mediated cellular repair leading to cell death. Also involved in the DNA cleavage step of class switch recombination (CSR). On the other hand, APEX1 also exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain, such as the FOS/JUN AP-1 complex after exposure to IR. Involved in calcium-dependent down-regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs). Together with HNRNPL or the dimer XRCC5/XRCC6, associates with nCaRE, acting as an activator of transcriptional repression. Stimulates the YBX1-mediated MDR1 promoter activity, when acetylated at Lys-6 and Lys-7, leading to drug resistance. Acts also as an endoribonuclease involved in the control of single-stranded RNA metabolism. Plays a role in regulating MYC mRNA turnover by preferentially cleaving in between UA and CA dinucleotides of the MYC coding region determinant (CRD). In association with NMD1, plays a role in the rRNA quality control process during cell cycle progression. Associates, together with YBX1, on the MDR1 promoter. Together with NPM1, associates with rRNA. Binds DNA and RNA (By similarity).
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A2T7L5
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MYC_PONPY
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Myc proto-oncogene protein (Proto-oncogene c-Myc) (Transcription factor p64)
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MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSPRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDSSLPKSCTSPDSSAFSPSSDSLLSSTESSPQASPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHIKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRVKLDSVRVLRQISNNRKCTSPRSSDAEENDKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSIQAEEQKLISEKDLLRKRREQLKHKLEQLRNSCA
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Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes. Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis. Regulator of somatic reprogramming, controls self-renewal of embryonic stem cells. Functions with TAF6L to activate target gene expression through RNA polymerase II pause release (By similarity). Positively regulates transcription of HNRNPA1, HNRNPA2 and PTBP1 which in turn regulate splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (By similarity).
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A2T928
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RARGB_DANRE
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Retinoic acid receptor gamma-B (RAR-gamma-B) (Nuclear receptor subfamily 1 group B member 3-B)
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MRDVFREATPMTCRSPLPDLRDMMEKLTVFEPTIDSTVETQSTSSEEMIPSSPSPPPPPRVYKPCFVCQDKSSGYHYGVSSCEGCKGFFRRSIQKNMVYTCHRDKNCQINKVTRNRCQYCRLRKCFEVGMSKEAVRNDRNKKKKDVKEEVVLPESYELSGELEELVNKVSKAHRETFPSLCQLGKYTTNSSADHRVQLDLGLWDKFSELSTKCIIKIVEFAKRLPGFTSLTIADQITLLKSACLDILMLRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFAFAGQLLPLEMDDTETGLLSAICLICGDRMDLEEPHRVDQLQEPLLEALKIYARRRRPNKPHMFPRMLMKVTDLRGISTKGAERAITLKMEIPGPMPPLIREMLENPEIFEDSSDSNDSGAAAVVPAPNIKRMGQRQAAWVKGERPEWVRGRRRGSKSRYKAGFKAGKARSRDSPDNNGEIRQGDERSEMSVRAEQDFALE
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Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The rar/rxr heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 (By similarity). Required for hindbrain development. {ECO:0000250, ECO:0000269|PubMed:18929555}.
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A2TGX5
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CLM8_RAT
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CMRF35-like molecule 8 (CLM-8) (CD300 antigen-like family member A) (CD antigen CD300a)
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MTQLASAVWPPTLLLLLLFWVPGCVPLRGPSSVTGTVGESLNVTCQYEERFKMNKKYWCRGSLVLLCKDIVRTGGSEEARNGRVSIRDDRDNLTFTVTLQNLTLEDAGTYMCAVDIPLIDHSFKVELSVVPGNIPVSSPGTTRETTVVPTSFSTKGPTQGSIPEGHHEHYEPQGLSLPVLLSVLALLLLLLVGTSLLAWRMFQKRSVKADKHPEMSQNLRQAEEQSESQYVNLQLHTLPLREEPVPPSQVEVEYSTLALPQEELHYTSVVFDSQRQNSHANGDPPCQSPDQKTEYSEIRKPREGLSDPHP
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Inhibitory receptor which may contribute to the down-regulation of cytolytic activity in natural killer (NK) cells, and to the down-regulation of mast cell degranulation. Negatively regulates the Toll-like receptor (TLR) signaling mediated by MYD88 but not TRIF through activation of PTPN6.
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A2TK72
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VM3A2_DEIAC
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Zinc metalloproteinase recombinant fibrinogenase II (FIIa) (rF II) (EC 3.4.24.-) (Snake venom metalloproteinase) (SVMP)
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KREAEANRTPEQQIYDPYKYVETVFVVDKAMVTKYNGDLDKIKTRMYEAANNMNEMYRYMFFRVVMVGLIIWTEEDKITVKPDVDYTLNAFAEWRKTYLLAEKKHDNAQLITGIDFRGSIIGYAYIGSMCHPKRSVGIIQDYSPINLVLAVIMAHEMGHNLGIHHDDGYCYCGGYPCIMGPSISPEPSKFFSNCSYIQCWDFIMNHNPECIDNEPLGTDIISPPLCGNELLEA
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Snake venom zinc metalloprotease that acts at several levels. It has direct fibrino(geno)lytic activity (Aalpha chain of fibrinogen is cleaved quickly, Bbeta chain slowly, and gamma chain even more slowly) and degradation of TNF-alpha. These activities permit to protect against sepsis and disseminated intravascular coagulation. It inhibits ADP-induced platelet aggregation in human platelet-rich plasma (IC(50)=65.4 ug/ml). It decreases the activity of complement by degrading human C5, C6 and C9 in vitro, decreasing serum levels of C1q, C3 and C4 in rat, and inhibiting the MAC deposition on HUVECs membrane. This inhibition of complement protects against hyperacute rejection that is the main barrier in xenotransplantation. Has preference for Lys at the P1 position. Cleaves insulin B chain at '36-Val-|-Glu-37', '39-Leu-|-Tyr-40', and '48-Phe-|-Phe-49' bonds. Also cleaves fibronectin and type IV collagen.
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A2VBC4
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PA1_POLPI
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Phospholipase A1 (PLA1) (EC 3.1.1.32) (allergen Poly p 1)
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MNFKYSILFICFGTLDRGLIPECPFNEYDILFFVYTRQQRDGIVLTEETLQNYDLFKKSTISRQVVFIDHGFLSNGNNENFIAMAKALIEKDNFLVISVDWKKGACNAFASTLDYLGYSTAVGNTRHVGKYVADFTKLLVEQYKVSMSNIRLIGHSLGAHTSGFAGKEVQELKLNKYSNIDGLDPAGPSFDSNDCPERLCETDAEYVQIIHTSNILGVYSKIGTVDFYMNYGSHQPGCGRFFSPSCSHTKAVKYLTECIKHECCLIGTPWKKYFSTPKPISQCTKDTCVCVGLNAKSYPARGSFYVPVEATAPYCHNEGIKL
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Catalyzes the hydrolysis of phosphatidylcholine with phospholipase A1 activity. Shows hemolytic activity. Acts as an allergen.
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A2VCW5
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S38A5_RAT
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Sodium-coupled neutral amino acid transporter 5 (Solute carrier family 38 member 5) (System N transporter 2)
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MAISCAVGMEMQEPKMNGTLSTGAAAGYRQEREGFLPTTHGPAPGRKPVQFLDFEGKTSFGMSVFNLSNAIMGSGILGLAYAMAHTGVIFFLALLLCIALLSSYSIHLLLTCASVVGIRAYEQLGQRAFGPAGKVVVAIIICLHNVGAMSSYLFIIKSELPLVIGTFLHMDPEGDWFLKGNLLIILVSLLIILPLALMKHLGYLGYTSSLSLTCMLFFLISVIYKKFQLGCVVSHNDTVVESEPAPLQAFNSSCEAKLFTVDSQMSYTVPIMAFAFVCHPEVLPIYTELCCPTQRRMQAVANMSIGAMFIMYGLTATFGYLTFYSTVKAEMLEMYTQEDLLILCVRLAVLLAVTLTVPVVLFPIRRALQQLLFPSKAFSWPRHVAIALILLILVNILVICVPTIRDIFGFIGSTSAPSLIFILPSVFYLRIVPADMEPLFSWPKIQALCFGVLGVLFMAISLGFMFANWATGQSRMSGH
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Symporter that cotransports neutral amino acids and sodium ions, coupled to an H(+) antiporter activity. Releases L-glutamine and glycine from astroglial cells and may participate in the glutamate/GABA-glutamine cycle and the NMDA receptors activation. In addition contributes significantly to L-glutamine uptake in retina, namely in ganglion and Mueller cells and, therefore participates in the retinal glutamate-glutamine cycle. The transport activity is pH sensitive, Li(+) tolerant, bidirectional and associated with large uncoupled fluxes of protons. The transport is electroneutral coupled to the cotransport of 1 Na(+) and the antiport of 1 H(+). May have particular importance for modulation of net hepatic glutamine flux.
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A2VD12
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PBIP1_RAT
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Pre-B-cell leukemia transcription factor-interacting protein 1 (Hematopoietic PBX-interacting protein)
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MASCPDSDNSWVLAGSETLPVETLGPESRVDPESEEAPQALQDSSKADGKESAGTLNGEEMLFQTESSQGEGAALPEESEAKGALGGDDGHGTKRPGDTAVQEDLQETPMVTSLGPDTQDLERNIHPQNLPSSPRAVWKEHGCSSSDDDTDVDVEGLRRRRGREPSPPQPTAAVDGEDQAKGEGIGELGISLNMCFLGALVLLGLGILLFSGALLEPETEPVEEAELQVFPETELVQTVGNRQDEVEQLQASVPPDSVPSLQSMGLLLDKLAKENQDIRLLQAQLQAQKEELQSLLHQPKGLEEENARLREALQQGKTSHQALESELQQLRARLQGLEANCVRGVDGVCLNWGGSPQGGKATTEQGHKGQEPDTSLLEQHKQLEAEAKALRQELQKQWQLLGSVHRNLQRGLQDAGQGAPAHAGLAELGHMLAQTLQGLESQGINTGRSSNDSEAWHQKKPRFQHPREWSGREKWRGGQRDQKAEHWKLKKEESGQDRKKSWRDEGREFTGHWKENRPRAEESGSRKDSKRQDPKVHPRKSGNSHSGERQKHSWGKDNSPDSVSWEELLRRKYRPPQGCSGVADCARQEGLALFGVELAPVRQQELASVLREYLARLPWAGQLTKELPLSPAYFGEDGIFRHDRLRFRDFVDALEDSLEEVALKQTGDDDEVDDFEDFIFSHFFGDKALKRRSKKKEKQPWNHRAVGPREEHSRHPHHYHQG
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Regulator of pre-B-cell leukemia transcription factors (BPXs) function. Inhibits the binding of PBX1-HOX complex to DNA and blocks the transcriptional activity of E2A-PBX1. Tethers estrogen receptor-alpha (ESR1) to microtubules and allows them to influence estrogen receptors-alpha signaling (By similarity).
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A2VDJ0
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T131L_HUMAN
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Transmembrane protein 131-like
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MAGLRRPQPGCYCRTAAAVNLLLGVFQVLLPCCRPGGAQGQAIEPLPNVVELWQAEEGELLLPTQGDSEEGLEEPSQEQSFSDKLFSGKGLHFQPSVLDFGIQFLGHPVAKILHAYNPSRDSEVVVNSVFAAAGHFHVPPVPCRVIPAMGKTSFRIIFLPTEEGSIESSLFINTSSYGVLSYHVSGIGTRRISTEGSAKQLPNAYFLLPKVQSIQLSQMQAETTNTSLLQVQLECSLHNKVCQQLKGCYLESDDVLRLQMSIMVTMENFSKEFEENTQHLLDHLSIVYVATDESETSDDSAVNMYILHSGNSLIWIQDIRHFSQRDALSLQFEPVLLPTSTTNFTKIASFTCKATSCDSGIIEDVKKTTHTPTLKACLFSSVAQGYFRMDSSATQFHIETHENTSGLWSIWYRNHFDRSVVLNDVFLSKETKHMLKILNFTGPLFLPPGCWNIFSLKLAVKDIAINLFTNVFLTTNIGAIFAIPLQIYSAPTKEGSLGFEVIAHCGMHYFMGKSKAGNPNWNGSLSLDQSTWNVDSELANKLYERWKKYKNGDVCKRNVLGTTRFAHLKKSKESESFVFFLPRLIAEPGLMLNFSATALRSRMIKYFVVQNPSSWPVSLQLLPLSLYPKPEALVHLLHRWFGTDMQMINFTTGEFQLTEACPYLGTHSEESRFGILHLHLQPLEMKRVGVVFTPADYGKVTSLILIRNNLTVIDMIGVEGFGARELLKVGGRLPGAGGSLRFKVPESTLMDCRRQLKDSKQILSITKNFKVENIGPLPITVSSLKINGYNCQGYGFEVLDCHQFSLDPNTSRDISIVFTPDFTSSWVIRDLSLVTAADLEFRFTLNVTLPHHLLPLCADVVPGPSWEESFWRLTVFFVSLSLLGVILIAFQQAQYILMEFMKTRQRQNASSSSQQNNGPMDVISPHSYKSNCKNFLDTYGPSDKGRGKNCLPVNTPQSRIQNAAKRSPATYGHSQKKHKCSVYYSKHKTSTAAASSTSTTTEEKQTSPLGSSLPAAKEDICTDAMRENWISLRYASGINVNLQKNLTLPKNLLNKEENTLKNTIVFSNPSSECSMKEGIQTCMFPKETDIKTSENTAEFKERELCPLKTSKKLPENHLPRNSPQYHQPDLPEISRKNNGNNQQVPVKNEVDHCENLKKVDTKPSSEKKIHKTSREDMFSEKQDIPFVEQEDPYRKKKLQEKREGNLQNLNWSKSRTCRKNKKRGVAPVSRPPEQSDLKLVCSDFERSELSSDINVRSWCIQESTREVCKADAEIASSLPAAQREAEGYYQKPEKKCVDKFCSDSSSDCGSSSGSVRASRGSWGSWSSTSSSDGDKKPMVDAQHFLPAGDSVSQNDFPSEAPISLNLSHNICNPMTVNSLPQYAEPSCPSLPAGPTGVEEDKGLYSPGDLWPTPPVCVTSSLNCTLENGVPCVIQESAPVHNSFIDWSATCEGQFSSAYCPLELNDYNAFPEENMNYANGFPCPADVQTDFIDHNSQSTWNTPPNMPAAWGHASFISSPPYLTSTRSLSPMSGLFGSIWAPQSDVYENCCPINPTTEHSTHMENQAVVCKEYYPGFNPFRAYMNLDIWTTTANRNANFPLSRDSSYCGNV
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[Isoform 1]: Membrane-associated form that antagonizes canonical Wnt signaling by triggering lysosome-dependent degradation of Wnt-activated LRP6. Regulates thymocyte proliferation.
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A2VDL4
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SATT_BOVIN
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Neutral amino acid transporter A (Solute carrier family 1 member 4)
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MEKSSETNGYLDSAQEGPAAGPGEPGTTARRAGRCAGFLRRHGLVLLTVSGVVAGAGLGAALRGLQLNRTQVTYLAFPGEMLLRMLRMIILPLVVCSLVSGAASLDASSLGRLGGIAIAYFGLTTLGASALAVALAFIIKPGSGSQTLQSSDLGLEDSGPPPVPKETVDSFLDLTRNLFPSNLVVAAFRTYATDYREVTYNTSAGKVTIEKIPIGTEIEGMNILGLVLFALVLGVALKKLGSEGEELIRFFNAFNEATMVLVSWIMWYVPVGIMFLVGSKIVEMKDIIMLVTSLGKYIFTSILGHFIHGGIVLPLIYFVFTRKNPFRFLLGLLTPFATAFATCSSSATLPSMMKCIEENNGVDKRISRFILPIGATVNMDGAAIFQCVAAVFIAQLNNVELRAGQIFTILVTATASSVGAAGVPAGGVLTIAIILEAIGLPTHDLSLILAVDWIVDRTTTVVNVEGDALGAGILHHLNQKAMKRGEQELSEVKVEAIPNSKSEEETSPLVTHPNPTGPAASTPESKESVL
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Sodium-dependent neutral amino-acid transporter that mediates transport of alanine, serine, cysteine, proline, hydroxyproline and threonine.
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A2VDL6
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AT1A2_BOVIN
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Sodium/potassium-transporting ATPase subunit alpha-2 (Na(+)/K(+) ATPase alpha-2 subunit) (EC 7.2.2.13) (Sodium pump subunit alpha-2)
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MGRGAGREYSPAATTAENGGGKKKQKEKELDELKKEVAMDDHKLSLDELGRKYQVDLSKGLTNQRAQDILARDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGAILCFLAFGIQAAMEDEPSNDNLYLGVVLAAVVIVTGCFSYYQEAKSSKIMDSFKNMVPQQALVVREGEKMQINAEEVVVGDLVEVKGGDRVPADLRIISSHGCKVDNSSLTGESEPQTRSPEFTHENPLETRNICFFSTNCVEGTARGIVIATGDRTVMGRIATLASGLEVGRTPIAMEIEHFIQLITGVAVFLGVSFFVLSLILGYSWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTEDQSGATFDKRSPTWTALSRIAGLCNRAVFKAGQENISVSKRDTAGDASESALLKCIELSCGSVRKMRDRNPKVAEIPFNSTNKYQLSIHEREDSPQSHVLVMKGAPERILDRCSSILVQGKEIPLDKEMQDAFQNAYLELGGLGERVLGFCQLNLPSAKFPRGFKFDTDELNFPTEKLCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPREAKACVVHGSDLKDMTSEQLDEILKNHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGIAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLLFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEAAESDIMKRQPRNPQTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPSRLLGIRLDWDDRSMNDLEDSYGQEWTYEQRKVVEFTCHTAFFASIVVVQWADLIICKTRRNSVFQQGMKNKILIFGLLEETALAAFLSYCPGMGVALRMYPLKVTWWFCAFPYSLLIFIYDEVRKLILRRYPGGWVEKETYY
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This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium, providing the energy for active transport of various nutrients (By similarity).
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A2VDN5
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SPAST_BOVIN
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Spastin (EC 5.6.1.1)
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MNSPGGRGKKKGSGGPSSPVPPRPPPPCQARSRPAPKPAPPPQSPHKRNLYYFSYPLFLGFALLRLVAFHLGLLFVWLCQRFSRALMAAKRSSGAAPASASPPAPVPGGEAERVRAFHKQAFEYISVALRIDEDEKVGQKDQAVEWYKKGIEELEKGIAVVVTGQGEQCERARRLQAKMMTNLVMAKDRLQLLEKLQPSLQFSKSQTDVYNDSTNLTCRNGHLQSESGAVPKRKDPLTHASNSLPRSKTVMKTGPTGLSGHHRAPSCSGLSMVSGVRQGPGSAAATHKSTPKTNRTNKPSTPTTAARKKKDLKNFRNVDSNLANLIMNEIVDNGTAVKFDDIAGQELAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDDRVLVMGATNRPQELDEAVLRRFTKRVYVSLPNEETRLLLLKNLLCKQGSPLTQKELAQLARMTNGYSGSDLTALAKDAALGPIRELKPEQVKNMSASEMRNIRLSDFTESLKKIKRSVSPQTLEAYIRWNKDFGDTTV
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ATP-dependent microtubule severing protein that specifically recognizes and cuts microtubules that are polyglutamylated. Preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold. Severing activity is not dependent on tubulin acetylation or detyrosination. Microtubule severing promotes reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. It is critical for the biogenesis and maintenance of complex microtubule arrays in axons, spindles and cilia. SPAST is involved in abscission step of cytokinesis and nuclear envelope reassembly during anaphase in cooperation with the ESCRT-III complex. Recruited at the midbody, probably by IST1, and participates in membrane fission during abscission together with the ESCRT-III complex. Recruited to the nuclear membrane by IST1 and mediates microtubule severing, promoting nuclear envelope sealing and mitotic spindle disassembly during late anaphase. Required for membrane traffic from the endoplasmic reticulum (ER) to the Golgi and endosome recycling. Recruited by IST1 to endosomes and regulates early endosomal tubulation and recycling by mediating microtubule severing. Probably plays a role in axon growth and the formation of axonal branches. {ECO:0000255|HAMAP-Rule:MF_03021}.
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A2VDP1
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BRE1A_BOVIN
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E3 ubiquitin-protein ligase BRE1A (BRE1-A) (EC 2.3.2.27) (RING finger protein 20) (RING-type E3 ubiquitin transferase BRE1A)
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MSGIGSKRAAGEPGTSVPPEKKTAVEDSGTTVETIKLGGVSSTEELDIRTLQTKNRKLAEMLDQRQAIEDELREHIEKLERRQATDDASLLIVNRYWSQFDENIRIILKRYDLEQGLGDLLTERKALVVPEPEPDSDSNQERKDDRERGEGQEPAFSFLATLASSSSEEMESQLQERVESSRRAVSQIVTVYDKLQEKVELLSRKLNSGDSLMVEEAVQELNSFLAQENTRLQELTDLLQEKHCTMSQEFSKLQSKVETAESRVSVLESMIDDLQWDIDKIRKREQRLNRHLAEVLERVNSKGYKVYGAGSSLYGGTITINARKFEEMNAELEENKELAQNRHCELEKLRQDFEEVTSQNEKLKVELRSAVEEVVKETPEYRCMQSQFSVLYNESLQLKAHLDEARTLLHGTRGTHQRQVELIERDEVSLHKKLRTEVIQLEDTLAQVRKEYEMLRIEFEQTLAANEQAGPINREMRHLISSLQNHNHQLKGEVLRYKRKLREAQSDLNKTRLRSGSALLQSQSSTEDPKDEPAELKQDSEDLATQSAASKASQEEVNEIKSKRDEEERERERREKEREREREREKEKEREREKQKLKESEKERESAKDKEKGKHDDGRKKEAEIIKQLKIELKKAQESQKEMKLLLDMYRSAPKEQRDKVQLMAAEKKSKAELEDLRQRLKDLEDKEKKENKKMADEDALRKIRAVEEQIEYLQKKLAMAKQEEEALLSEMDVTGQAFEDMQEQNIRLMQQLREKDDANFKLMSERIKSNQIHKLLKEEKEELADQVLTLKTQVDAQLQVVRKLEEKEHLLQSNIGTGEKELGLRTQALEMNKRKAMEAAQLADDLKAQLEMAQKKLHDFQDEIVENSVTKEKDMFNFKRAQEDISRLRRKLETTKKPDNVPKCDEILMEEIKDYKARLTCPCCNMRKKDAVLTKCFHVFCFECVKTRYDTRQRKCPKCNAAFGANDFHRIYIG
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Component of the RNF20/40 E3 ubiquitin-protein ligase complex that mediates monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1). H2BK120ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me, respectively). It thereby plays a central role in histone code and gene regulation. The RNF20/40 complex forms a H2B ubiquitin ligase complex in cooperation with the E2 enzyme UBE2A or UBE2B reports about the cooperation with UBE2E1/UBCH are contradictory. Required for transcriptional activation of Hox genes. Recruited to the MDM2 promoter, probably by being recruited by p53/TP53, and thereby acts as a transcriptional coactivator. Mediates the polyubiquitination of PA2G4 leading to its proteasome-mediated degradation.
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A2VDT1
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TP4A3_BOVIN
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Protein tyrosine phosphatase type IVA 3 (EC 3.1.3.48) (Protein-tyrosine phosphatase 4a3)
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MARMNRPAPVEVSYKNMRFLITHNPTNATLSSFIEDLKKYGATTVVRVCEVTYDKAPLEKDGITVVDWPFDDGAPPPGKVVEDWLSLLKNKFCDDPGSCVAVHCVAGLGRAPVLVALALIESGMKYEDAIQFIRQKRRGAINSKQLTYLEKYRPKQRLRFKDPHAHKTKCCIM
|
Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. Enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. May be involved in the progression of cardiac hypertrophy by inhibiting intracellular calcium mobilization in response to angiotensin II (By similarity).
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A2VDU3
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M3K7_BOVIN
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Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25)
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MSTASAASSSSSSSAGEMIEAPSQVLNFEEIDYKEIEVEEVVGRGAFGVVCKAKWRAKDVAIKQIESESERKAFIVELRQLSRVNHPNIVKLYGACLNPVCLVMEYAEGGSLYNVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSMQPKALIHRDLKPPNLLLVAGGTVLKICDFGTACDIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLMRYFPGADEPLQYPCQYSDEGQSNSATSTGSFMDITSTNTSNKSDTNMEQVPATNDTIKRLESKLLKNQAKQQSESGRLSLGASRGSSVESLPPTSEGKRMSADMSEIEARIAATTGNGQPRRRSIQDLTVTGTDPGQVSSRSSSPSVRMITTSGPTSEKPARSHPWTPDDSTDTNGSDNSIPMAYLTLDHQLQPLAPCPNSKESMAVFEQHCKMAQEYMKVQTEIALLLQRKQELVAELDQDEKDQQNTSRLVQEHKKLLDENKSLSTYYQQCKKQLEVIRSQQQKRQGTS
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Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Mediates signal transduction of TRAF6, various cytokines including interleukin-1 (IL-1), transforming growth factor-beta (TGFB), TGFB-related factors like BMP2 and BMP4, toll-like receptors (TLR), tumor necrosis factor receptor CD40 and B-cell receptor (BCR). Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade and the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases like MAP2K1/MEK1, MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7. These MAP2Ks in turn activate p38 MAPKs and c-jun N-terminal kinases (JNKs) both p38 MAPK and JNK pathways control the transcription factors activator protein-1 (AP-1). Independently of MAP2Ks and p38 MAPKs, acts as a key activator of NF-kappa-B by promoting activation of the I-kappa-B-kinase (IKK) core complex. Mechanistically, recruited to polyubiquitin chains of RIPK2 and IKBKG/NEMO via TAB2/MAP3K7IP2 and TAB3/MAP3K7IP3, and catalyzes phosphorylation and activation of IKBKB/IKKB component of the IKK complex, leading to NF-kappa-B activation. In osmotic stress signaling, plays a major role in the activation of MAPK8/JNK1, but not that of NF-kappa-B. Promotes TRIM5 capsid-specific restriction activity (By similarity). Phosphorylates RIPK1 at 'Ser-321' which positively regulates RIPK1 interaction with RIPK3 to promote necroptosis but negatively regulates RIPK1 kinase activity and its interaction with FADD to mediate apoptosis (By similarity).
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A2VDV2
|
STK38_BOVIN
|
Serine/threonine-protein kinase 38 (EC 2.7.11.1)
|
MAMTGSTPCSSMSSHTKERVTMTKVTLENFYSNLIAQHEEREMRQKKLEKVMEEEGLKDEEKRLRRSAHARKETEFLRLKRTRLGLEDFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVGHIRAERDILVEADSLWVVKMFYSFQDKLNLYLIMEFLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCTGLKKAHRTEFYRNLNHSLPSDFTFQNMNSKRKAETWKRNRRQLAFSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETPQETYKKVMNWKETLTFPPEVPISEKAKDLILRFCCEWEHRIGAPGVEEIKNNSFFEGVDWEHIRERPAAISIEIKSIDDTSNFDEFPESDILKPTVATSNHPDTDYKNKDWVFINYTYKRFEGLTARGAIPSYMKAAK
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Negative regulator of MAP3K1/2 signaling. Converts MAP3K2 from its phosphorylated form to its non-phosphorylated form and inhibits autophosphorylation of MAP3K2 (By similarity).
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A2VDW9
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IKZF3_BOVIN
|
Zinc finger protein Aiolos (Ikaros family zinc finger protein 3)
|
MEDIKPNVELKSTQEQSVPTEGSELLNDYDLTKAHETENVDGTEGPANEDEDIGDDSMKVKDEYSERDENVLKPEPMGNAEEPEIPYSYSREYNEYENIKLERHVVSYDSSRPTSGKMNCDVCGLSCISFNVLMVHKRSHTGERPFQCNQCGASFTQKGNLLRHIKLHTGEKPFKCHLCNYACQRRDALTGHLRTHSVEKPYKCEFCGRSYKQRSSLEEHKERCRTFLQSTDLGETASVEARHIKAEMGSERALVLDRLASNVAKRKSSMPQKFIGEKRHCFDVSYNPSYMYEKESEMIQTRMMDQAINNAISYLGAEALRPLVQTPPAPTSEMVPVISSMYPIALTRAEMPNGAPQELEKKNIHLPEKSLPSERGLSPTNSGHDSTDTDSNHEERQNHIYQQNPMVPPRARNGMPLLKEGPRSYDLLKPPPICPRDSIKVINKEGEVTDVYRCDHCRVLFLDYVMFTIHMGCHGFRDPFECNMCGYRSHDRYEFSSHIARGEHRAMLK
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Transcription factor that plays an important role in the regulation of lymphocyte differentiation. Plays an essential role in regulation of B-cell differentiation, proliferation and maturation to an effector state. Involved in regulating BCL2 expression and controlling apoptosis in T-cells in an IL2-dependent manner (By similarity).
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A2VDY3
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CHM4A_BOVIN
|
Charged multivesicular body protein 4a (Chromatin-modifying protein 4a) (CHMP4a)
|
MSGLGRLFGRGKKEKGPTPEEAIQKLKETEKILIKKQEFLEQKIEQELQAAKKHGTKNKRAALQALRRKKRLEQQLAQTDGTLSTLEFQREAIENATTNAEVLRTMELAAQGLKKAYQDMDIDKVDELMADITEQQEVAQQISDAISRPVGFGDDVDEDELLEELEELEQEELARELLHVGDEEEEPPVALPSAPSTHLPAEPAPKADEDEAELKQLAEWVS
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Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. When overexpressed, membrane-assembled circular arrays of CHMP4A filaments can promote or stabilize negative curvature and outward budding. CHMP4A/B/C are required for the exosomal release of SDCBP, CD63 and syndecan (By similarity).
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A2VDZ3
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MEF2A_BOVIN
|
Myocyte-specific enhancer factor 2A
|
MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSSNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVEALNKKEHRGCDSPDPDTSYVLTPHTEEKYKKINEEFDNMMRNHKIAPGLPPQNFSMSVTVPVTSPSALSYTNPGSSLVSPSLAASSALADTSMLSPPQATLHRNVSPGAPQRPPSTGSAGGMLSTSDLTVPNGAGSSPVGNGFVNSRASPNLIGTTGANSLGKVMPTKSPPPPGGGSLGMNSRKPDLRVVIPPSSKGMMPPLNTQRISSSQATQPLATPVVSVTTPSLPPQGLVYSAMPTAYNTDYSLTSADLSALQGFNSPGMLSLGQVSAWQQHHLGQAALNSLVAGGQLSQGSNLSINTNQNINIKSEPISPPRDRMTPSGFQQQQQPQPPPPPPQAPQPQPRQEVGRSPVDSLSSSSSSYDGSDREDPRGDFHSPVVLGRPPNSEDRESPSVKRMRMDAWVT
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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. Also involved in the activation of numerous growth factor- and stress-induced genes. Mediates cellular functions not only in skeletal and cardiac muscle development, but also in neuronal differentiation and survival. Plays diverse roles in the control of cell growth, survival and apoptosis via p38 MAPK signaling in muscle-specific and/or growth factor-related transcription. In cerebellar granule neurons, phosphorylated and sumoylated MEF2A represses transcription of NUR77 promoting synaptic differentiation. Associates with chromatin to the ZNF16 promoter (By similarity).
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A2VDZ4
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PLK4_BOVIN
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Serine/threonine-protein kinase PLK4 (EC 2.7.11.21) (Polo-like kinase 4) (PLK-4) (Serine/threonine-protein kinase Sak)
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MATCIGEKIEDFRVGNLLGKGSFAGVYRAESIHTGLEVAIKMIDKKAMYKAGMVQRVQNEVKIHCQLKHPSILELYNYFEDNNYVYLVLEMCHNGEMNRYLKNRRKPFSENEARHFMHQIITGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLAAQLKMPHEKHYTLCGTPNYISPEIATRSAHGLESDIWSLGCMFYTLLIGRPPFDTDTVKNTLNKVVLADYEMPTFLSREAKDLIHQLLRRNPADRLSLSSVLDHPFMSRNSSKKSKDLGTVEDSIDSGHATISTAITASSSTSISGSLFDRRRLLIEQPLPNKMTIFPKNKNPSDFSSSGDGISFYTSWGNQEQETSNSGRGRVIQEAEERPHSRYLRRAHSSDRSETSHGQSRVKTYTMERCYSAEMLSKSKRSGVEENERYSPTNNDANIFHFFKEKTSNSSGSFEGPDNNQALSNHLCPGKTPFPFPEQTPQTEMVQQWFGNLQINDPSCEQSKTRGVEPPLVYQKRTLRSITSPLTAYRLKPIRQKTKKAVVSILDSEEVCVELLKDYASQEYVKEVLQISSDGSMITIYYPNDGRGFLLADRPPSPTDNISRYSFDNLPEKYWRKYQYASRFVQLVRSKSPKITYFTRYAKCVLMENSPGADFEVWFYDGAKIHKTEDLIQVIEKTGRSYTLKGESEVNSLKEEVKMYMNHANEGHRICLALESIISEEEKKSGSAPFFPIIVGRRPSSTSSPKALTPPPPVDPNYPMRETPSLNRMIINSAASPKQAPVLNPPVVTNEGLGLMGAASETNSSPRSLKDCLPKSAQLLKSVFVKNVGWATQLTSGAVWVQFNDGSQLVVQAGVSSISYTSPDGQTTRYGENEKLPEYIKQKLQCLSSILLMFSNPTPSFH
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Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the parental centriole cylinder, leading to the recruitment of centriole biogenesis proteins such as SASS6, CENPJ/CPAP, CCP110, CEP135 and gamma-tubulin. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Phosphorylates 'Ser-151' of FBXW5 during the G1/S transition, leading to inhibit FBXW5 ability to ubiquitinate SASS6. Its central role in centriole replication suggests a possible role in tumorigenesis, centrosome aberrations being frequently observed in tumors. Also involved in deuterosome-mediated centriole amplification in multiciliated that can generate more than 100 centrioles. Also involved in trophoblast differentiation by phosphorylating HAND1, leading to disrupt the interaction between HAND1 and MDFIC and activate HAND1. Phosphorylates CDC25C and CHEK2. Required for the recruitment of STIL to the centriole and for STIL-mediated centriole amplification (By similarity). Phosphorylates CEP131 and PCM1 which is essential for proper organization and integrity of centriolar satellites (By similarity).
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A2VE08
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IMA5_BOVIN
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Importin subunit alpha-5 (Karyopherin subunit alpha-1) [Cleaved into: Importin subunit alpha-5, N-terminally processed]
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MTTPGKENFRLKSYKNKSLNPDEMRRRREEEGLQLRKQKREEQLFKRRNVATAEEETEEEVMSDGGFHEAQINNMEMAPGGVITSDMIEMIFSNSPEQQLSATQKFRKLLSKEPNPPIDEVISTPGVVARFVEFLKRKENCTLQFESAWVLTNIASGNSLQTRIVIQAGAVPIFIELLSSEFEDVQEQAVWALGNIAGDSTMCRDYVLDCNILPPLLQLFSKQNRLTMTRNAVWALSNLCRGKSPPPEFAKVSPCLNVLSWLLFVSDTDVLADACWALSYLSDGPNDKIQAVIDAGVCRRLVELLMHNDYKVVSPALRAVGNIVTGDDVQTQVILNCSALQSLLHLLSSPKESIKKEACWTISNITAGNRAQIQTVIDANIFPALISILQTAEFRTRKEAAWAITNATSGGSAEQIKYLVELGCIKPLCDLLTVMDSKIVQVALNGLENILRLGEQEAKRNGTGINPYCALIEEAYGLDKIEFLQSHENQEIYQKAFDLIEHYFGTEDEDSSIAPQVDLSQQQYIFQQCEAPMEGFQL
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Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity).
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A2VE31
|
S38A2_BOVIN
|
Sodium-coupled neutral amino acid symporter 2 (Amino acid transporter A2) (Protein 40-9-1) (Solute carrier family 38 member 2) (System A amino acid transporter 2) (System A transporter 1) (System N amino acid transporter 2)
|
MKKAEMGRFNISPDEDSSSYSSNSDFNYSYPTKQAALKSHYADVDPENQNFLLESNLGKKKYETDFHPGTTSFGMSVFNLSNAIVGSGILGLSYAMANTGIALFIILLTFVSIFSLYSVHLLLKTANEGGSLLYEQLGHKAFGMVGKLTASGSITMQNIGAMSSYLFIVKYELPLVIQALMNIEDTNGLWYLNGDYLVLLVSLVLILPLSLLRNLGYLGYTSGLSLLCMMFFLIVVIFKKFQISCPAEIAFLVNETVNSSLTQPATFLPDMGFNRTESDSCQPRYFIFNSQTVYAVPILTFSFVCHPAILPIYEELKGRSRRRMMNVSKISFFAMFLMYLLAALFGYLTFYGHVESELLHTYSSVMETDILLLIVRLAVLVAVTLTVPVVIFPIRSSITHLLCASKEFSWWRHSVITVSILVFTNLLVIFVPNIRDIFGFIGASAAAMLIFILPSAFYIKLVKKEPMKSVQKIGAMFFLLSGIVVMTGSMALIVLDWVHNAPGGGH
|
Symporter that cotransports neutral amino acids and sodium ions from the extraccellular to the intracellular side of the cell membrane. The trasnport is pH-sensitive, Li(+)-intolerant, electrogenic, driven by the Na(+) electrochemical gradient and cotransports of neutral amino acids and sodium ions with a stoichiometry of 1:1. May function in the transport of amino acids at the blood-brain barrier (By similarity). May function in the transport of amino acids in the supply of maternal nutrients to the fetus through the placenta (By similarity). Maintains a key metabolic glutamine/glutamate balance underpinning retrograde signaling by dendritic release of the neurotransmitter glutamate (By similarity). Transports L-proline in differentiating osteoblasts for the efficient synthesis of proline-enriched proteins and provides proline essential for osteoblast differentiation and bone formation during bone development (By similarity).
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A2VE79
|
NUDT3_BOVIN
|
Diphosphoinositol polyphosphate phosphohydrolase 1 (DIPP-1) (EC 3.6.1.52) (Diadenosine hexaphosphate hydrolase) (Ap6A hydrolase) (EC 3.6.1.61) (Endopolyphosphatase) (EC 3.6.1.10) (Nucleoside diphosphate-linked moiety X motif 3) (Nudix motif 3) (m7GpppN-mRNA hydrolase) (EC 3.6.1.62) (m7GpppX diphosphatase) (EC 3.6.1.59)
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MMKLKSNQTRTYDGDGYKKRAACLCFRSESEEEVLLVSSSRHPDRWIVPGGGMEPEEEPGTAAVREVCEEAGVKGTLGRLVGIFENQERKHRTYVYVLIVTEVLEDWEDSVSIGRKREWFKIEDAINVLQCHKPVQASYFETLRQGYSANNGTPLVAPTYSVSAQSSMPGIR
|
Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate) and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a role in signal transduction (By similarity). InsP6 (inositol hexakisphosphate) is not a substrate (By similarity). Also able to catalyze the hydrolysis of dinucleoside oligophosphates, with diadenosine 5',5'''-P1,P6-hexaphosphate (Ap6A) and diadenosine 5',5'''- P1,P5-pentaphosphate (Ap5A) being the preferred substrates (By similarity). The major reaction products are ADP and p4a from Ap6A and ADP and ATP from Ap5A (By similarity). Also able to hydrolyze 5- phosphoribose 1-diphosphate (By similarity). Acts as a decapping enzyme that can hydrolyze both monomethylated and unmethylated capped RNAs (By similarity). Hydrolyzes monomethylated capped RNA after both the alpha- and beta-phosphates generating m7GMP + ppRNA and m7GDP + pRNA (By similarity). Modulates the stability of a subset of mRNAs implicated in cell motility (By similarity). Divalent cations zinc, magnesium and manganese determine its substrate specificity (By similarity). Exhibits diphosphoinositol polyphosphate phosphohydrolase in the presence of magnesium ions, diadenosine hexaphosphate hydrolase activity in the presence of manganese ions and endopolyphosphatase activity in the presence of zinc ions (By similarity). Plays an important role in limiting DNA damage and maintaining cell survival upon oxidative stress via its endopolyphosphatase activity (By similarity).
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A2VEA3
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ARI1_BOVIN
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E3 ubiquitin-protein ligase ARIH1 (EC 2.3.2.31) (Protein ariadne-1 homolog) (ARI-1) (RING-type E3 ubiquitin transferase ARIH1)
|
MDSDEGYNYEFDEDEECSEEDSGAEEEEDEDDDEPDDDNLDLGEVELVEPGLGVGGERDGLLCGETGGGGGSALGPGGGGGGGGGGGGPGHEQEEDYRYEVLTAEQILQHMVECIREVNEVIQNPATITRILLSHFNWDKEKLMERYFDGNLEKLFAECHVINPSKKSRTRQMNTRSSAQDMPCQICYLNYPNSYFTGLECGHKFCMQCWSEYLTTKIMEEGMGQTISCPAHGCDILVDDNTVMRLITDSKVKLKYQHLITNSFVECNRLLKWCPAPDCHHVVKVQYPDAKPVRCKCGRQFCFNCGENWHDPVKCKWLKKWIKKCDDDSETSNWIAANTKECPKCHVTIEKDGGCNHMVCRNQNCKAEFCWVCLGPWEPHGSAWYNCNRYNEDDAKAARDAQERSRAALQRYLFYCNRYMNHMQSLRFEHKLYAQVKQKMEEMQQHNMSWIEVQFLKKAVDVLCQCRATLMYTYVFAFYLKKNNQSIIFENNQADLENATEVLSGYLERDISQDSLQDIKQKVQDKYRYCESRRRVLLQHVHEGYEKDLWEYIED
|
E3 ubiquitin-protein ligase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 UBE2L3. Acts as an atypical E3 ubiquitin-protein ligase by working together with cullin-RING ubiquitin ligase (CRL) complexes and initiating ubiquitination of CRL substrates: associates with CRL complexes and specifically mediates addition of the first ubiquitin on CRLs targets. The initial ubiquitin is then elongated by CDC34/UBE2R1 and UBE2R2. E3 ubiquitin-protein ligase activity is activated upon binding to neddylated cullin-RING ubiquitin ligase complexes. Plays a role in protein translation in response to DNA damage by mediating ubiquitination of EIF4E2, the consequences of EIF4E2 ubiquitination are however unclear. According to a report, EIF4E2 ubiquitination leads to promote EIF4E2 cap-binding and protein translation arrest. According to another report EIF4E2 ubiquitination leads to its subsequent degradation. Acts as the ligase involved in ISGylation of EIF4E2. In vitro, controls the degradation of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex member SUN2 and may therefore have a role in the formation and localization of the LINC complex, and as a consequence, may act in nuclear subcellular localization and nuclear morphology.
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A2VEC9
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SSPO_HUMAN
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SCO-spondin (SCO-spondin pseudogene)
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MLLPALLFGMAWALADGRWCEWTETIRVEEEVAPRQEDLVPCASLDHYSRLGWRLDLPWSGRSGLTRSPAPGLCPIYKPPETRPAKWNRTVRTCCPGWGGAHCTEALAKASPEGHCFAMWQCQLQAGSANASAGSLEECCARPWGQSWWDGSSQACRSCSSRHLPGSASSPALLQPLAGAVGQLWSQHQRPSATCASWSGFHYRTFDGRHYHFLGRCTYLLAGAADSTWAVHLTPGDRCPQPGHCQRVTMGPEEVLIQAGNVSVKGQLVPEGQSWLLHGLSLQWLGDWLVLSGGLGVVVRLDRTGSISISVDHELWGQTQGLCGLYNGWPEDDFMEPGGGLAMLAATFGNSWRLPGSESGCLDAVEVAQGCDSPLGLIDADVEPGHLRAEAQDVCHQLLEGPFGQCHAQVSPAEYHEACLFAYCAGAMAGSGQEGRQQAVCATFASYVQACARRHIHIRWRKPGFCERLCPGGQLYSDCVSLCPPSCEAVGQGEEESCREECVSGCECPRGLFWNGTLCVPAAHCPCYYCRQRYVPGDTVRQLCNPCVCRDGRWHCAQALCPAECAVGGDGHYLTFDGRSYSFWGGQGCRYSLVQDYVKGQLLILLEHGACDAGSCLHAISVSLEDTHIQLRDSGAVLVNGQDVGLPWIGAEGLSVRRASSAFLLLRWPGAQVLWGLSDPVAYITLDPRHAHQVQGLCGTFTQNQQDDFLTPAGDVETSIAAFASKFQVAGKGRCPSEDSALLSPCTTHSQRHAFAEAACAILHSSVFQECHRLVDKEPFYLRCLAAVCGCDPGSDCLCPVLSAYARRCAQEGASPPWRNQTLCPVMCPGGQEYRECAPACGQHCGKPEDCGELGSCVAGCNCPLGLLWDPEGQCVPPSLCPCQLGARRYAPGSATMKECNRCICQERGLWNCTARHCPSQAFCPRELVYAPGACLLTCDSPSANHSCPAGSTDGCVCPPGTVLLDERCVPPDLCPCRHSGQWYLPNATIQEDCNVCVCRGRQWHCTGQRRSGRCQASGAPHYVTFDGLAFTYPGACEYLLVREASGLFTVSAQNLPCGASGLTCTKALAVRLEGTVVHMLRGRAVTVNGVSVTPPKVYTGPGLSLRRAGLFLLLSTHLGLTLLWDGGTRVLVQLSPQFRGRVAGLCGDFDGDASNDLRSRQGVLEPTAELAAHSWRLSPLCPEPGDLPHPCTMNTHRAGWARARCGALLQPLFTLCHAEVPPQQHYEWCLYDACGCDSGGDCECLCSAIATYADECARHGHHVRWRSQELCSLQCEGGQVYEACGPTCPPTCHEQHPEPGWHCQVVACVEGCFCPEGTLLHGGACLEPASCPCEWGRNSFPPGSVLQKDCGNCTCQEGQWHCGGDGGHCEELVPACAEGEALCQENGHCVPHGWLCDNQDDCGDGSDEEGCAAPGCGEGQMTCSSGHCLPLALLCDRQDDCGDGTDEPSYPCPQGLLACADGRCLPPALLCDGHPDCLDAADEESCLGQVTCVPGEVSCVDGTCLGAIQLCDGVWDCPDGADEGPGHCPLPSLPTPPASTLPGPSPGSLDTASSPLASASPAPPCGPFEFRCGSGECTPRGWRCDQEEDCADGSDERGCGGPCAPHHAPCARGPHCVSPEQLCDGVRQCPDGSDEGPDACGGLPALGGPNRTGLPCPEYTCPNGTCIGFQLVCDGQPDCGRPGQVGPSPEEQGCGAWGPWSPWGPCSRTCGPWGQGRSRRCSPLGLLVLQNCPGPEHQSQACFTAACPVDGEWSTWSPWSVCSEPCRGTMTRQRQCHSPQNGGRTCAALPGGLHSTRQTKPCPQDGCPNATCSGELMFQPCAPCPLTCDDISGQVTCPPDWPCGSPGCWCPEGQVLGSEGWCVWPRQCPCLVDGARYWPGQRIKADCQLCICQDGRPRRCRLNPDCAVDCGWSSWSPWAKCLGPCGSQSIQWSFRSSNNPRPSGRGRQCRGIHRKARRCQTEPCEGCEHQGQVHRVGERWHGGPCRVCQCLHNLTAHCSPYCPLGSCPQGWVLVEGTGESCCHCALPGENQTVQPMATPAAAPAPSPQIRFPLATYILPPSGDPCYSPLGLAGLAEGSLHASSQQLEHPTQAALLGAPTQGPSPQGWHAGGDAYAKWHTRPHYLQLDLLQPRNLTGILVPETGSSNAYASSFSLQFSSNGLHWHDYRDLLPGILPLPKLFPRNWDDLDPAVWTFGRMVQARFVRVWPHDVHHSDVPLQVELLGCEPGSPPAPLCPGVGLRCASGECVLRGGPCDGVLDCEDGSDEEGCVLLPEGTGRFHSTAKTLALSSAQPGQLLHWPREGLAETEHWPPGQESPTSPTETRPVSPGPASGVPHHGESVQMVTTTPIPQMEARTLPPGMAAVTVVPPHPVTPATPAGQSVAPGPFPPVQCGPGQTPCEVLGCVEQAQVCDGREDCLDGSDERHCARNLLMWLPSLPALWAASTVPFMMPTMALPGLPASRALCSPSQLSCGSGECLSAERRCDLRPDCQDGSDEDGCVDCVLAPWSVWSSCSRSCGLGLTFQRQELLRPPLPGGSCPRDRFRSQSCFVQACPVAGAWAMWEAWGPCSVSCGGGHQSRQRSCVDPPPKNGGAPCPGASQERAPCGLQPCSGGTDCELGRVYVSADLCQKGLVPPCPPSCLDPKANRSCSGHCVEGCRCPPGLLLHDTRCLPLSECPCLVGEELKWPGVSFLLGNCSQCVCEKGELLCQPGGCPLPCGWSAWSSWAPCDRSCGSGVRARFRSPSNPPAAWGGAPCEGDRQELQGCHTVCGTEVFGWTPWTSWSSCSQSCLAPGGGPGWRSRSRLCPSPGDSSCPGDATQEEPCSPPVCPVPSIWGLWAPWSTCSAPCDGGIQTRGRSCSSLAPGDTTCPGPHSQTRDCNTQPCTAQCPENMLFRSAEQCHQEGGPCPRLCLTQGPGIECTGFCAPGCTCPPGLFLHNASCLPRSQCPCQLHGQLYASGAMARLDSCNNCTCVSGKMACTSERCPVACGWSPWTLWSLCSCSCNVGIRRRFRAGTAPPAAFGGAECQGPTMEAEFCSLRPCPGPGGEWGPWSPCSVPCGGGYRNRTRGSSRSLMEFSTCGLQPCAGPVPGMCPRDKQWLDCAQGPASCAELSAPRGTNQTCHPGCHCPSGMLLLNNVCVPTQDCPCAHEGHLYPPGSTVVRPCENCSCVSGLIANCSSWPCAEGEPTWSPWTPWSQCSASCGPARCHRHRFCARSPSAVPSTVAPLPLPATPTPLCSGPEAEEEPCLLQGCDRAGGWGPWGPWSHCSRSCGGGLRSRTRACDQPPPQGLGDYCEGPRAQGEVCQALPCPVTNCTAIEGAEYSPCGPPCPRSCDDLVHCVWRCQPGCYCPPGQVLSSNGAICVQPGHCSCLDLLTGQRHHPGARLARPDGCNHCTCLEGRLNCTDLPCPVPGGWCPWSEWTMCSQPCRGQTRSRSRACACPTPQHGGAPCTGEAGEAGAQHQREACPSYATCPVDGAWGPWGPWSPCDMCLGQSHRSRACSRPPTPEGGRPCPGNHTQSRPCQENSTQCTDCGGGQSLHPCGQPCPRSCQDLSPGSVCQPGSVGCQPTCGCPLGQLSQDGLCVPPAHCRCQYQPGAMGIPENQSRSAGSRFSSWESLEPGEVVTGPCDNCTCVAGILQCQEVPDCPDPGVWSSWGPWEDCSVSCGGGEQLRSRRCARPPCPGPARQSRTCSTQVCREAGCPAGRLYRECQPGEGCPFSCAHVTQQVGCFSEGCEEGCHCPEGTFQHRLACVQECPCVLTAWLLQELGATIGDPGQPLGPGDELDSGQTLRTSCGNCSCAHGKLSCSLDDCFEADGGFGPWSPWGPCSRSCGGLGTRTRSRQCVLTMPTLSGQGCRGPRQDLEYCPSPDCPGAEGSTVEPVTGLPGGWGPWSSWSPCSRSCTDPARPAWRSRTRLCLANCTMGDPLQERPCNLPSCTELPVCPGPGCGAGNCSWTSWAPWEPCSRSCGVGQQRRLRAYRPPGPGGHWCPNILTAYQERRFCNLRACPVPGGWSRWSPWSWCDRSCGGGQSLRSRSCSSPPSKNGGAPCAGERHQARLCNPMPCEAGCPAGMEVVTCANRCPRRCSDLQEGIVCQDDQVCQKGCRCPKGSLEQDGGCVPIGHCDCTDAQGHSWAPGSQHQDACNNCSCQAGQLSCTAQPCPPPTHCAWSHWSAWSPCSHSCGPRGQQSRFRSSTSGSWAPECREEQSQSQPCPQPSCPPLCLQGTRSRTLGDSWLQGECQRCSCTPEGVICEDTECAVPEAWTLWSSWSDCPVSCGGGNQVRTRACRAAAPHHRSPPCLGPDTQTRQQPCPGLLEACSWGPWGPCSRSCGPGLASRSGSCPCLMAKADPTCNSTFLHLDTQGCYSGPCPEECVWSSWSSWTRCSCRVLVQQRYRHQGPASRGARAGAPCTRLDGHFRPCLISNCSEDSCTPPFEFHACGSPCAGLCATHLSHQLCQDLPPCQPGCYCPKGLLEQAGGCIPPEECNCWHTSAAGAGMTLAPGDRLQLGCKECECRRGELHCTSQGCQGLLPLSEWSEWSPCGPCLPPSALAPASRTALEEHWLRDPTGLSPTLAPLLASEQHRHRLCLDPATGRPWTGAPHLCTAPLSQQRLCPDPGACPDSCQWSLWGPWSPCQVPCSGGFRLRWREAEALCGGGCREPWAQESCNGGPCPESCEAQDTVFTLDCANQCPHSCADLWDRVQCLQGPCRPGCRCPPGQLVQDGRCVPISSCRCGLPSANASWELAPAQAVQLDCQNCTCVNESLVCPHQECPVLGPWSAWSSCSAPCGGGTMERHRTCEGGPGVAPCQAQDTEQRQECNLQPCPECPPGQVLSACATSCPCLCWHLQPGAICVQEPCQPGCGCPGGQLLHNGTCVPPTACPCTQHSLPWGLTLTLEEQAQELPPGTVLTRNCTRCVCHGGAFSCSLVDCQVPPGETWQQVAPGELGLCEQTCLEMNATKTQSNCSSARASGCVCQPGHFRSQAGPCVPEDHCECWHLGRPHLPGSEWQEACESCLCLSGRPVCTQHCSPLTCAQGEEMVLEPGSCCPSCRREAPEEQSPSCQLLTELRNFTKGTCYLDQVEVSYCSGYCPSSTHVMPEEPYLQSQCDCCSYRLDPESPVRILNLRCLGGHTEPVVLPVIHSCQCSSCQGGDFSKR
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Involved in the modulation of neuronal aggregation (By similarity). May be involved in developmental events during the formation of the central nervous system (By similarity).
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A2VEI2
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MICU1_DROME
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Calcium uptake protein 1 homolog, mitochondrial (Mitochondrial calcium uptake 1)
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MSVLRFLVTRQALAALTRPRTLNIIQNPAQIAYASTLCNQNSNHNAKDLTKSSANLSLMQTRGHKRFGHQEEKTPSVTKYFHMFILSLFLISVMDWGKVKRMLTPKVDADAGQRPSSAADVNGEDKSSESESEDSEDEEAGSDLHLHEGKKIREKVGFRERKIIEYENRIRQFSTPDKVFRYFATIQVPVADDRHEVYMTPTDFLTSMTPGMKQPDGLGLDQYRRYDPKSVGEQLNLHLEKNSIFYKLGSYGLITFSDYIFLLTVLSISRRHFEIAFRMFDLNGDGDVDCEEFEMVATLVRQQTSMGTRHRDHANTGNTFKGVNSALITYFFGPNMDEKLTIEKFLDFQEQLQREILSLEFERKEPNDEGNITEADFAELLLAYAGYPLKKKQKKLKRVKRRFRDHGKGISKQDYLDFFHFLNNINDVDTALTFYHIAGASIDQQTLQHVAKTVAMVNLSDHVVDVVFTIFDENNDNQLSNKEFISVMKNRVQRGLEKPKDTGFLKMMRSVFKCAKETKPVLLDI
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Key regulator of mitochondrial calcium uniporter (MCU) that senses calcium level via its EF-hand domains (Probable). During development, required in alpha/beta or gamma mushroom body neurons to support olfactory intermediate-term memory in the adult.
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A2VEY9
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APP_DROME
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Palmitoyltransferase app (EC 2.3.1.225) (Protein approximated)
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MNLLCCCCCSNMAPNQRVTRKWELFAGRNKFYCDGLLMSAPHTGVFYLTCILITGTSALFFAFDCPFLADSINPAIPIVGAVLYFFTMSSLLRTTFTDPGVIPRASNDEAAYIEKQIEVPNSLNSPTYRPPPRTKEVLVKGQTVKLKYCFTCKIFRPPRASHCSLCDNCVDRFDHHCPWVGNCVGKRNYRFFYLFLVSLAFLAVFIFSCSVTHLVLLMKKEHEVFNVIKAAPFTVIVVFICFFSIWSVIGLAGFHTYLTTSDQTTNEDLKGSFSSKGGPRTQNPYSRGNICLNCCHILCGPMTPSLIDRRGIATDEFIQQMQHQSSPRHALSDVLSASHMVTTSQPMMGGLGGGGIGGAGGGISIGGAELKPRFYDESNPSSSTLEGNGGAINGHGNGHGNGFDHPPPSYDLVQNGNSNSLAQLVDNEIPLVQMDIPAYTHQTATQARQYRHRHHKQRQICNGGTVSYENQLANASSEDELDDPDVVVVGSPEVVAAVAAIASNKAREMRNRSGSYSNLFDADFEAALVNSSLADNHVRGEGASSSGKPSAGAALLAAAISGKTENMYSNVLPVDNDTDPADSTLHVYSNIIDERKQQEQANNVLSSTLLCDDLDLDDPVSASCHVKRKSLGDGAEQVKSAERLRMLHDNTMIDTALDLDSLDGSSMGNNSQSCLVKSGKPNATSVTTNVAIV
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Palmitoylates Dlish which is required for the apical cell cortex localization, total cellular level and full activity of dachs.
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A2WV32
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CESA4_ORYSI
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Cellulose synthase A catalytic subunit 4 [UDP-forming] (EC 2.4.1.12) (OsCesA4)
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MMESGVPPCAACGDDAHAACRACSYALCKACLDEDAAEGRTTCARCGGEYGAPDPAHGQGAVVEEEVEESHEPVASGVRERVTMASQLSDHQDEGVHARTMSTHARTISSVSGVGSELNDESGKPIWKNRVESWKEKKKEKKASAKKAAAKAQAPPVEEQIMDEKDLTDAYEPLSRIIPISKNKLTPYRAVIIMRLVVLGLFFHYRITNPVYSAFGLWMTSVICEIWFGFSWILDQFPKWCPINRETYVDRLIARYGDGEDSGLAPVDFFVSTVDPLKEPPLITANTVLSILAVDYPVEKISCYVSDDGSAMLTFESLAETAEFARRWVPFCKKYSIEPRAPEFYFSQKIDYLKDKIHPSFVKERRAMKRDYEEYKVRINALVAKAQKTPEEGWIMQDGTPWPGNNPRDHPGMIQVFLGETGARDFDGNELPRLVYVSREKRPGYQHHKKAGAMNALVRVSAVLTNAPYILNLDCDHYVNNSKAVREAMCFMMDPSVGRDVCYVQFPQRFDGIDRSDRYANRNVVFFDVNMKGLDGLQGPVYVGTGCCFYRQALYGYGPPSLPALPKSSVCSWCCCCCPKKKAEKSEKEMHRDSRREDLESAIFNLREIDNYDEYERSMLISQMSFEKSFGLSSVFIESTLMENGGVPESANPSTLIKEAIHVISCGYEEKTEWGKEIGWIYGSVTEDILTGFKMHCRGWRSIYCMPIRPAFKGSAPINLSDRLHQVLRWALGSVEIFLSRHCPLWYGYGGGRLKWLQRLSYINTIVYPFTSLPLIAYCCLPAICLLTGKFIIPTLSNAATIWFLGLFISIIVTSVLELRWSGIGIEDWWRNEQFWVIGGVSAHLFAVFQGILKMIAGLDTNFTVTAKATDDTEFGELYVFKWTTVLIPPTSILVLNLVGVVAGFSDALNSGYESWGPLFGKVFFAMWVIMHLYPFLKGLMGRQNRTPTIVVLWSVLLASVFSLLWVKIDPFIGSSETTTTNSCANFDC
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Catalytic subunit of cellulose synthase terminal complexes ('rosettes'), required for beta-1,4-glucan microfibril crystallization, a major mechanism of the cell wall formation (By similarity). Involved in the secondary cell wall formation.
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