entry
stringlengths 6
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stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
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A5JTM5
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CBADH_PSEUC
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4-chlorobenzoyl coenzyme A dehalogenase (4-CBA-CoA dehalogenase) (4-CBCoA dehalogenase) (4-chlorobenzoyl-CoA dehalogenase) (EC 3.8.1.7)
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MYEAIGHRVEDGVAEITIKLPRHRNALSVKAMQEVTDALNRAEEDDSVGAVMITGAEDAFCAGFYLREIPLDKGVAGVRDHFRIGALWWHQMIHKIIRVKRPVLAAINGVAAGGGLGISLASDMAICADSAKFVCAWHTIGIGNDTATSYSLARIVGMRRAMELMLTNRTLYPEEAKDWGLVSRVYPKDDFREVAWKVARELAAAPTHLQVMAKERFHAGWMQPVEECTEFEIQNVIASVTHPHFMPCLTEFLDGHRADRPQVELPAGV
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Dehalogenates 4-chlorobenzoyl-CoA, 4-iodobenzoyl-CoA and 4-bromobenzoyl-CoA, but not 4-fluorobenzoyl-CoA. Inactive towards crotonyl-CoA, alpha-methylcrotonyl-CoA and beta-methylcrotonyl-CoA.
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A5JTM6
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CBACL_PSEUC
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4-chlorobenzoate--CoA ligase (4-CBA:CoA ligase) (EC 6.2.1.33)
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MQTVHEMLRRAVSRVPHRWAIVDAARSTFDICRTGETSRNEGSATARLWPQPARPLAVVSGNSVEAVIAVLALHRLQAVPALMNPRLKPAEISELVARGEMARAVVANDAGVMEAIRTRVPSVCVLALDDLVSGSRVPEVAGKSLPPPPCEPEQAGFVFYTSGTTGLPKGAVIPQRAAESRVLFMATQAGLRHGSHNVVLGLMPLYHTIGFFAVLVAAMAFDGTYVVVEEFDAGNVLKLIERERVTAMFATPTHLDALTTAVEQAGARLESLEHVTFAGATMPDTVLERVNRFIPGEKVNIYGTTEAMNSLYMRAVRIAGTVMRPGFFSEVRIVRVGGDVDDGCPTVKRASWRWRRRMRPFQATLTNLRLLQKSFRKAGTGRAICVRDGSGNIVVLGRVDDMIISGGENIHPSEVERILAAAPGVAEVVVIGVKDERWGQSVVACVVLQPGASASAERLDAFCRASALADFKRPRRYVFLDELPKSAMNKVLRRQLMQHVSATSSAAVVPAPAVKQRTYAPSGRAIAR
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Catalyzes the formation of chlorobenzoyl-CoA via a 2 step reaction. First 4-chlorobenzoyl is adenylated by ATP, followed by acyl transfer from the 4-chlorobenzoyl-AMP intermediate to CoA. Benzoate, 4-bromobenzoate, 4-iodobenzoate and 4-methylbenzoate also act as substrates. Inactive towards 4-aminobenzoate, 4-hydroxybenzoate, 2-aminobenzoate, 2,3-dihydroxybenzoate, 4-coumarate and the aliphatic carboxylic acids palmate, caproate, laurate and butyrate. Negligible activity is detected when ATP is replaced by UTP, CTP or GTP as cosubstrate.
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A5JUY8
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PERL_BUBBU
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Lactoperoxidase (LPO) (WBLP) (EC 1.11.1.7)
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MWVCLQLPVFLASVTLFEVAASDTIAQAASTTTISDAVSKVKIQVNKAFLDSRTRLKTTLSSEAPTTQQLSEYFKHAKGQTRTAIRNGQVWEESFKRLRRDTTLTNVTDPSLDLTALSWEVGCGAPVPLVKCDENSPYRTITGDCNNRRSPALGAANRALARWLPAEYEDGLALPFGWTQRKTRNGFRVPLAREVSNKIVGYLDEEGVLDQNRSLLFMQWGQIVDHDLDFAPETELGSNEHSKTQCEEYCIQGDNCFPIMFPKNDPKLKTQGKCMPFFRAGFVCPTPPYQSLAREQINAVTSFLDASLVYGSEPSLASRLRNLSSPLGLMAVNQEAWDHGLAYLPFNNKKPSPCEFINTTARVPCFLAGDFRASEQILLATAHTLLLREHNRLARELKKLNPHWNGEKLYQEARKILGAFIQIITFRDYLPIVLGSEMQKWIPPYQGYNNSVDPRISNVFTFAFRFGHMEVPSTVSRLDENYQPWGPEAELPLHTLFFNTWRIIKDGGIDPLTRGLLAKKSKLMNQDKMVTSELRNKLFQPTHKIHGFDLAAINLQRCRDHGMPGYNSWRGFCGLSQPKTLKGLQTVLKNKILAKKLMDLYKTPDNIDIWIGGNAEPMVERGRVGPLLACLLGRQFQQIRDGDRFWWENPGVFTEKQRDSLQKFSFSRLICDNTHITKVPLHAFQANNYPHDFVDCSTVDKLDLSPWASREN
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Heme-containing oxidoreductase which catalyzes the conversion of thiocyanate (SCN(-)) into antimicrobial agent hypothiocyanous acid (OSCN(-)) in the presence of hydrogen peroxide (H2O2) (Probable). Also involved in the conversion of iodide (I(-)) into hypoiodite (IO(-)) in the presence of H2O2 (By similarity). Responsible for the inactivation of a wide range of micro-organisms and hence, important component of defense mechanism. Shows antibacterial properties against E.coli, K.pneumoniae, P.aeruginosa, S.sonnei, S.saphrophyticus, S.epidermidis and S.dysenteriae. May protect the udder from infection and may promote growth in newborns (By similarity). May be implicated in airway host defense against infection (By similarity). May contribute to maintaining an appropriate H2O2 cellular level, therefore protecting cells from H2O2-caused injuries and inflammation (By similarity).
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A5JYS0
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PCS1_CAEEL
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Glutathione gamma-glutamylcysteinyltransferase (EC 2.3.2.15) (Phytochelatin synthase) (PC synthase)
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MSQRRHFKMSVTAKNFYRRPLPETCIEFSSELGKKLFTEALVRGSANIYFKLASQFRTQDEPAYCGLSTLVMVLNALEVDPEKVWKAPWRFYHESMLDCCVPLENIRKSGINLQQFSCLAKCNRLKSTVSYGDNSPDFLKKFRTSLVNSVRSDDQVLVASYDRSVLGQTGSGHFSPLAAYHEDSDQVLIMDVARFKYPPHWVKLETLQKALCSVDVTTKLPRGLVELELKKGTRPLIMYGLKAYVNINDSDFATSVISWNQFLLCDPLEDDEEEFQLCCRKFGQCFAPHAMCCTQKTFDADQKNSCTECSTDQNEACKMICSEIRRTRFAEVFSSSAVAALLIAWPFEKGYSERSDRIGNLAEKYKNEFSAETMNEMNQLTTQIRTLISCSKPPVVININKPDATSNKCCKNKIGQSCACANDVNL
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Involved in the synthesis of phytochelatins, which are heavy metal binding proteins required for the detoxification of heavy metals such as cadmium, arsenic and copper.
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A5JYW9
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SIN3_CAEEL
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Paired amphipathic helix protein sin-3 (Histone deacetylase complex subunit sin-3) (Transcriptional corepressor sin-3)
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MYNPPPGGGGGNNGGDQSQQQPTNNATLFLLQMIQQSQHQQQHQNQQQQQLELQIRDQERILIEQQRMQHQQQQNQLLQGLNQFPFNPLGLFQVQAAVQAAQAQFAQNAQGSPIPFHIGSPLQPSHSPAASALQQQYLLPSHSPAITPFARNSEAARNIEQFIAQEEAANVPRANSQQQSPLIRPIPQQQALNIQNLTSTQQAQQILAHHRQVPVQQVQHQQHIPTPPLALPIAQQGPISNEVPSVPPVVPATSAGCPQREPRQQQGGRRQNRPGRRKKPEGPPRVDEALAYLRVIKSTFSSDVPVYHRFLEIMKDFRAQRIETPDVIEQVAELLYDSPELVLGFNTFLPTGYRITLTPDRKYVFSSPQMQPRVLLSPDERRARAIEAGAQAVGAIELGSQEGISKDEDRTIEDEDMDKSKEKDDVDGIDDEDDEESGIEDKNNEEMMEEDNHLIEEIICDDRKKDDCEDSQQEIEMSSELAAHTLNIIELLKKSFLARPTKLVDFMTFIDFFMSDQQYKKDMEKLRKDDEDDEIEENEKIEVDDVPGPSNAPQEIKKPDDIEKKDSSKNLQIEESCSDYLVSMLANCCIGEPDLLAATIDFLPYLGKLLVNGSDAIALKIKTILHFSATNDRNDIPPVNRVNPSDVDMDLVKQMEKCKMGTKKNEKLKLKVAGQGDEGATVELMILKKSYRILYERLKSRTTPNQLSHLMVLINAYANLDITREQLISELPKIMGTSGSDLEMIILQLLGAEKEPKNRPENDMDAVMRKDLPAIQPKRGLRDQKMLQQVKNVEAATVCTLGPSYRFMKDTKATDCSGRVELDDDLKGVLNDTWTSIPSWSSEDTGSQAIKKSNLEEFHFKTEDERYELDIIVDSNRTVIEQLSKTLRDYEAMSDEDKKSFKLDKWLNASSRSTTIRVLAKVFTNSAQDFIDAAQKNPLVGLRRILESLKEKDLLWSRFQQDTNRTWRDALDKQMSAATTILNNQHKNYDQKAFKSKPLVNQIEQICEERRKNNSTDTSPHLILEYTPERKVYRDVNDVTGHFFHDLSGTKCDRDRTKIVLFSYRILMEWLCQEGQQVQIDLDNGEIFKFQGDLNEDENLMTLLNMDGRRICGDRVVPVSTSLESNESSIDHFSENLHQKRTRRTFYGDDSVYMIIRYHHMIQERFAKILSTQAIYAQEHFDNQKKNKRWEDGIGADMHGRKALQENIKQRRAAVNDIRNVRSCPSSSYETTLRELKQLGNAQMDIVAFEEAVKNLFPGDIVLFNNIDKLFSSLAKNIHHATCAEERENPIKLYLKYRQRIMNAERDEDMESVIQEYGQTAEEVLRGKNTYRFEFVEEQNKPFIKIWVIPREEKDDDDDDDEEGNEGGKDEDNVKDEDDGGDGEGRDGPDDDQPPPSNDDGDDEEDEDDEEDGPSGADEPESTSGSGNVPMDHLNIGENFLWSPPEEKVCTGKMTTNEKEQRNSVDYMKVTTTPRLRIHKRMLKEHKGCNVELMTGFQQLSAIVPLM
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Probable transcriptional repressor required for the deposition of dimethylated 'Lys-9' of histone H3 (H3K9me2) on asynapsed chromosome pairs (both autosomes and sex chromosomes) during meiosis, but this does not seem to solely affect the transcriptional status. Plays a role in ray fusion and patterning in the male tail, and this may be through activity of the histone deacetylase complex (HDAC).
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A5JYX5
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DHS3_CAEEL
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Protein dhs-3 (Alcohol dehydrogenase dhs-3) (EC 1.1.1.1)
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MPYVFLLSPQLEIASQWDGYYEKTFEVSDHVHKEIILKVSGQTVLITGSGSGLGRLMAFEFGKLGARLVLWDINEQGNKETLKELEAMGVEAKAYTVDLSEYKEINRTADLVKSEVGKVDILVNNAGIVTGKKLLQCPDELMVKTVSVNTNALFFTTKNFLPGMLESNKGHIVTIASMAGKCGVAGLVDYCASKHGAVGFNDSLASELYALKKDVKTTVVCPIYINTGMFDGIATKWPTLLPILSPEYVVDCIMEAVLTDRAFLAIPKFSYIFIALAGLLPTEVLNLYGDHFGITHSMDHFKGRQSRQA
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May play a role in lipid droplet formation. May modulate triglyceride levels.
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A5JYX8
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NCLN_CAEEL
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Nicalin (Inactive aminopeptidase nra-2) (Nicotinic receptor-associated protein 2)
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MQDEIIDFFRSPALLFYMTLMLTICVVNGSQQVGEVVETEFHAYRLHQYEISGNIYGCKNYRVSYEAVSLGARTLRRTMVTTWRDLLTTDVDDMWALSTGAVLIFIPDNLDELNDIDRKAFIDLEAKLLSAKTDLAVYVAPFNDDAVSILHDVNTRSEKAPTALQHLLQSLSGNTISITSSDQSPELPPSYKPLNIVGRLSSGDRAAPTIAFVAHYDTQSAVPGVSPGADSNGSGIVALLELLAVLSKFYDSPSTRPPYNILFIWTAAGKLNYQGTRHWIDEYQKGFDSADYAKSGLSRKGFSDDRVDLAICIEAIGRKTGGFFMHAGKTPSENSVAAQLLRRLKYFSSISPKKNIELVTKKISLTTVSAWEHEKFNIKRMPAITLSTLPSPSDPARNSILDLPSALDEDELIDNIRLIGEAVLGYILDLPESGPSSDSRVKSEATMLSKDAVDKQRVHHFIRQFASRPRPVGDQRATESITSNLASVAAGYGNVFKSAVTITDAKAFGVTQNRLVAERVKPAVFELVIAAGVFTYLSAFYYIATHSQNTIEGTVAAIRKSIF
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Involved in the recognition and selection of protein complexes to exit the endoplasmic reticulum (ER). In muscles, regulates levamisole-sensitive nicotinic acetylcholine receptor (L-AChR) subunit composition, possibly by allowing only specific L-AChR subunit combinations to exit the ER. Specifically, may promote the inclusion of alpha subunits unc-38 and unc-29 into L-AChR. Regulates L-AChR sensitivity to agonists such as nicotine and levamisole at neuro-muscular junctions. In touch neurons, may prevent ER exit of incorrectly folded mec-4-mec-10 ion channel.
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A5K302
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PLM5_PLAVS
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Plasmepsin V (PvPMV) (EC 3.4.23.-) (Plasmepsin 5)
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MVGASLGPPGRGSLSRLIRLVICVLTLCALSVQGRSESTEGHSKDLLYKYKLYGDIDEYAYYFLDIDIGTPEQRISLILDTGSSSLSFPCAGCKNCGVHMENPFNLNNSKTSSILYCENEECPFKLNCVKGKCEYMQSYCEGSQISGFYFSDVVSVVSYNNERVTFRKLMGCHMHEESLFLYQQATGVLGMSLSKPQGIPTFVNLLFDNAPQLKQVFTICISENGGELIAGGYDPAYIVRRGGSKSVSGQGSGPVSESLSESGEDPQVALREAEKVVWENVTRKYYYYIKVRGLDMFGTNMMSSSKGLEMLVDSGSTFTHIPEDLYNKLNYFFDILCIQDMNNAYDVNKRLKMTNESFNNPLVQFDDFRKSLKSIIAKENMCVKIVDGVQCWKYLEGLPDLFVTLSNNYKMKWQPHSYLYKKESFWCKGIEKQVNNKPILGLTFFKNRQVIFDIQKNRIGFVDANCPSHPTHTRPRTYNEYKRKDNIFLKIPFFYLYSLFVVFALSVLLSLVFYVRRLYHMEYSPLPSEGKAPADA
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During the asexual blood stage, plays an essential role in the export of several proteins into the host erythrocytes by cleaving the pentameric localization motif RxLxE/Q/D (termed Plasmodium export element (PEXEL)) located downstream of the N-terminal secretory signal sequence. Specifically, cleaves after the leucine residue in the RxLxE/Q/D (or RxLxxE) motif of exported proteins including EMP1 (By similarity). Also, by regulating protein export, plays an essential role in gametocyte development and thus parasite transmission to the mosquito vector (By similarity).
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A5K3U9
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AMPL_PLAVS
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Leucine aminopeptidase (PvLAP) (EC 3.4.11.1) (EC 3.4.13.-) (M17 leucyl aminopeptidase) (Pv-M17)
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MPLLRSSQHIKNTYWNIPKKSFRTGVPQFAESKKTRILHLHPLCKSASGVESPPFFDSQTFSSISNRKEFRKMATTVPQVVSLDPTTIPIDYHTPIDDLSIEVKDISAEACPADEGLIVFLLNSAPKHSSSGGSGGNGGSAGSSGNGEGGAQIKINSSVKDNTINEFLKEGNMENFTGKLGTSKSFYIANDQKKYVSLAYVGCGPANEETELEIRKVAYALVTLLHDSKHKKVSIIFEIKIEEALFRFFLEHLFYEYVTDERFKSADKSTETDFIKNLSLHIANADAYKGQIDKARVYFYGTYYAAQLIAAPSNYCNPVSLSNAAVELAQKVNLECKILDVKELEELKMGAYLSVGKGSMYPNKFIHLTYKGAQTGASQNEKKKIALIGKGITFDSGGYNLKAAPGSMIDLMKFDMSGCAAVLGCAYCIGTIKPDNVEVHFLSAVCENMVSKNSYRPGDIITASNGKTIEVGNTDAEGRLTLADALVYAEKLGVDYIVDIATLTGAMLYSLGTSYAGVFGNNDQLINKILSSSKTSNEPVWWLPIINEYRSSLNSKYADLNNISSSVKASSVVASLFLKEFIENTPWAHIDIAGVSWNFKARKPKGFGVRLLTEFVLNDAV
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Aminopeptidase which preferentially cleaves leucine residues from the N-terminus of peptides. Also, has some activity towards tryptophan and methionine and has very low activity towards alanine, arginine, asparagine, phenylalanine and tyrosine. No activity towards histidine, serine, valine, isoleucine, glycine, aspartic acid and glutamic acid. In addition, cleaves the Cys-Gly dipeptide, probably as part of the glutathione regulation pathway cleavage only occurs in the presence of Mn(2+). Plays a role in the final step of host hemoglobin catabolism, by cleaving hemoglobin-derived oligopeptides providing a source of amino acids for the parasite protein synthesis and for the maintenance of osmotic homeostasis.
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A5KE01
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ADA_PLAVS
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Adenosine deaminase (EC 3.5.4.4) (S-methyl-5'-thioadenosine deaminase) (EC 3.5.4.31)
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MNILQEPIDFLKKEELKNIDLSQMSKKERYKIWKRIPKCELHCHLDLCFSADFFVSCIRKYNLQPNLSDEEVLDYYLFAKGGKSLGEFVEKAIKVADIFHDYEVIEDLAKHAVFNKYKEGVVLMEFRYSPTFVAFKYNLDIELIHQAIVKGIKEVVELLDHKIHVALMCIGDTGHEAANIKASADFCLKHKADFVGFDHGGHEVDLKEYKEIFDYVRESGVPLSVHAGEDVTLPNLNTLYSAIQVLKVERIGHGIRVAESQELIDMVKEKNILLEVCPISNVLLKNAKSMDTHPIRQLYDAGVKVSVNSDDPGMFLTNINDDYEELYTHLNFTLEDFMKMNEWALEKSFMDSNIKDKIKNLYF
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Catalyzes the hydrolytic deamination of adenosine to produce inosine. Unlike mammalian adenosine deaminases, also catalyzes the deamination of 5'-methylthioadenosine (MTA), a by-product of polyamine biosynthesis, to produce 5'-methylthioinosine (MTI). Plays an essential role in the purine salvage pathway which allows the parasite to use host cell purines for the synthesis of nucleic acids.
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A5LGW7
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POLG_HAVJ8
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Genome polyprotein [Cleaved into: Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Protein VP1-2A (VPX); Capsid protein VP1 (P1D) (Virion protein 1); Assembly signal 2A (pX); Protein 2BC; Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3ABCD (P3); Protein 3ABC; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD; Protease 3C (P3C) (EC 3.4.22.28) (Picornain 3C); RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48)]
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MNMSRQGIFQTVGSGLDHILSLADVEEEQMIQSVDRTAVTGASYFTSVDQSSVHTAEVGAHQSEPLKTSVDKPGSKRTQGEKFFLIHSADWLTTHALFHEVAKLDVVKLLYNEQFAVQGLLRYHTYARFGIEIQVQINPTPFQQGGLICAMVPGDQSYGSIASLTVYPHGLLNCNINNVVRIKVPFIYTRGAYHFKDPQYPVWELTIRVWSELNIGTGTSAYTSLNVLARFTDLELHGLTPLSTQMMRNEFRVSTTENVVNLSNYEDARAKMSFALDQEDWKSDASQGGGIKITHFTTWTSIPTLAAQFPFNASDSVGQQIKVIPVDPYFFQMTNTNPEQKCITALASICQMFCFWRGDLVFDFQVFPTKYHSGRLLFCFVPGNELIDVSHITLKQATTAPCAVMDITGVQSTLRFRVPWISDTPYRVNRYTKSSHQKGEYTAIGKLIVYCYNRLTSPSNVASHVRVNVYLSAINLECFAPLYHAMDVTTQVGDDSGGFSTTVSTKQNVPDPQVGITTVRDLKGKANQGKMDVSGVQAPVGAITTIEDPVLAKKVPETFPELKPGESRHTSDHMSIYKFMGRSHFLCTFTFNSNNKEYTFPITLSSTSNPPHGLPSTLRWFFNLFQLYRGPLDLTIIITGATDVDGMAWFTPVGLAVDTPWVEKESALSIDYKTALGAVRFNTRRTGNIQIRLPWYSYLYAVSGALDGLGDKTDSTFGLVSIQIANYNHSDEYLSFSCYLSVTEQSEFYFPRAPLNTNAMMSSETMLDRIALGDLESSVDDPRSEEDRKFESHIEKRKPYKELRLEVGKQRLKYAQEELSNEVLPPPRKIKGVFSQAKISLFYTEDHEIMKFSWKGITADTRALRRFGFSLAAGRSVWTLEMDAGVLTGRLVRVNDEKWTEMKDDKIVSLVEKFTSNKHWSKINFPHGMLDLEEIAANSKEFPNMSETDLCFLLHWLNPKKINLADRMLGMSGIQEIKEKGVGLIGECRAFLDSITTTLKSMMFGFHHSVTVEIINTVLCFVKSGILLYVIQQLNQEEHSHIIGLLRVMNYADIGCSVISCGKVFSKMLETVFNWQMDSRMMELRTQSISNWLRDICSGITIFKSFKDAIYWLYTRIREYYDVNYGNKKDVLNILKDNQQKIERAIEEADNFCVLQIQDVEKFEQYQKGVDLIQKLRTVHSMAQVDPGLTVHLAPLRDCIARVHQKLKNLGSINQAMVTRCEPVVCYLYGKRGGGKSLTSIALATKICKHYGVEPEKNIYTKPVASDYWDGYSGQLVCIIDDIGQNTTDEDWSDFCQLVSGCPMRLNMASLEEKGRHFSSPFIIATSNWSNPSPKTVYVKEAIDRRLHFKVEVKPASFFKNPHNDMLNVNLAKTNDAIKDMSCVDLVMDSHNISLSELLSSLVMTVEIRKQNMSEFMELWSQGMSDDDNDSAVAEFFQSFPSGEPSGSKLSRFFQSVTNHKWVAVGAAVGVLGVLVGGWYVYKHFTKKKEEPIPSEGVYHGVTKPKQVIKLDADPVESQSTLEIAGLVRKNLVQFGVGEKNGCVRWVMNALGIKDDWLLVPSHAYKFEKDYEMMEFYFNRGGTYYSISAGNVVIQSLDVGFQDVVLMKVPTIPKFRDITEHFIKKSDVPRALNRLATLVTTVNGTPMLISEGPLKMEEKATYVHKKNDGTTIDLTVDQAWRGKGEGLPGMCGGALISSNQSIQNAILGIHVAGGNSILVAKLVTQEMFQNIDKKIVESQRIMKVEFTQCSMNVVSKTLFKKSPIHHHIDKNMINFPAVMPFSRAEIDPMAVMLSKYSLPIVDEPEDYKDVSVFFQNKILGKSPLVDDFLDIEMAITGAPGIDAINMDSSPGYPYVQEKLTKRDLIWLDDNGMFLGVHPRLAQRILFNTTMMENCSDLDVVFTTCPKDELRPLDKVLESKTRAIDSCPLDYTILCRMYWGPAISYFHLNPGFHTGVAIGIDPDRQWDQLFKTMIRFGDVGLDLDFSAFDASLSPFMIREAGRILTEMSGAPNHFGEALINTIIYSKHLLYNCCYHVYGSMPSGSPCTALLNSIINNVNLYYVFSKIFKKSPVFFCDAIRILCYGDDVLIVFSRQVQFDNLDSIGQRIVDEFRKLGMTATSADKSVPQLKPVSELTFLKRSFNLVDDRIRPAIAEKTIWSLVAWQRSNAEFEQNLENAQWFAFMHGYEFYQDFYHFVQSCLEKEMIEYRLKSYDWWRMKFNDQCFVCDLS
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[Capsid protein VP1]: Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell. [Capsid protein VP2]: Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell. [Capsid protein VP3]: Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell. [Capsid protein VP4]: Plays a role in the assembly of the 12 pentamers into an icosahedral structure. Has not been detected in mature virions, supposedly owing to its small size. [Protein VP1-2A]: Precursor component of immature procapsids that corresponds to an extended form of the structural protein VP1. After maturation, possibly by the host Cathepsin L, the assembly signal 2A is cleaved to give rise to the mature VP1 protein. [Protein 2B]: Functions as a viroporin. Affects membrane integrity and causes an increase in membrane permeability. Involved in host intracellular membrane rearrangements probably to give rise to the viral factories. Does not disrupt calcium homeostasis or glycoprotein trafficking. Antagonizes the innate immune response of the host by suppressing IFN-beta synthesis, which it achieves by interfering with the RIG-I/IFIH1 pathway. [Protein 3ABC]: The precursor 3ABC is targeted to the mitochondrial membrane where protease 3C activity cleaves and inhibits the host antiviral protein MAVS, thereby disrupting activation of IRF3 through the IFIH1/MDA5 pathway. In vivo, the protease activity of 3ABC precursor is more efficient in cleaving the 2BC precursor than that of protein 3C. The 3ABC precursor may therefore play a role in the proteolytic processing of the polyprotein. Possible viroporin. [Protein 3AB]: Interacts with the 3CD precursor and with RNA structures found at both the 5'- and 3'-termini of the viral genome. Since the 3AB precursor contains the hydrophobic domain 3A, it probably anchors the whole viral replicase complex to intracellular membranes on which viral RNA synthesis occurs. [Protease 3C]: Cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease. Cleaves IKBKG/NEMO to impair innate immune signaling. Cleaves host PABPC1 which may participate in the switch of viral translation to RNA synthesis.
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A5LHG2
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ADM5_PIG
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ADM5 [Cleaved into: Adrenomedullin-5 (AM5)]
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MTAHILLLWLFASSILGDPDSAGRLTRHQVSLKSGRLCSLGTCQTHRLPEIIYWLRSASTKELSGKAGRKPQDPYSYGRRRRRRRRRREARLLRRLQDPSLRRAQLAG
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Seems to have a peripheral vasodepressor effect and a central vasopressor effect.
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A5LHX3
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PSB11_HUMAN
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Proteasome subunit beta type-11 (EC 3.4.25.1) (Proteasome subunit beta-5t)
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MALQDVCKWQSPDTQGPSPHLPRAGGWAVPRGCDPQTFLQIHGPRLAHGTTTLAFRFRHGVIAAADTRSSCGSYVACPASCKVIPVHQHLLGTTSGTSADCATWYRVLQRELRLRELREGQLPSVASAAKLLSAMMSQYRGLDLCVATALCGWDRSGPELFYVYSDGTRLQGDIFSVGSGSPYAYGVLDRGYRYDMSTQEAYALARCAVAHATHRDAYSGGSVDLFHVRESGWEHVSRSDACVLYVELQKLLEPEPEEDASHAHPEPATAHRAAEDRELSVGPGEVTPGDSRMPAGTETV
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The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Incorporated instead of PSMB5 or PSMB8, this unit reduces the chymotrypsin-like activity of the proteasome (By similarity). Plays a pivotal role in development of CD8-positive T cells (By similarity).
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A5PF10
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NEUR1_PIG
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Sialidase-1 (EC 3.2.1.18) (Acetylneuraminyl hydrolase) (Lysosomal sialidase) (N-acetyl-alpha-neuraminidase 1)
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MTAERPGAVPLGRPGRPPMLGLGEAYRAQVFASIFLLLLSPAGVGARAKNDFNLVHPLVTMEQLLWVSGKQIGSVDTFRIPLITTTPRGTLLAFAEARKMSASDKGAKFIALRRSMDQGSTWSPTAFIVDDGETPDGLNLGAVVSDTTTGVVFLFYSLCAHKAGCRVASTMLVWSKDDGISWSSPRNLSLDIGTEMFAPGPGSGIQKQWAPQKGRLIVCGHGTLERDGVFCLLSDDHGASWRYGSGISGIPYGQPKRENDFNPDECQPYELPDGSVVINARNQNNYHCRCRIVLRSYDACDTLRPRDVTFDPELVDPVVAAGAVATSSGIIFFSNPAHPEFRVNLTLRWSFSNGTSWRKETVQIWPGPSGYSSLATLEGSVGGEDQAPQLYVLYEKGRNRYTESISLAKVSVYGTL
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Catalyzes the removal of sialic acid (N-acetylneuraminic acid) moieties from glycoproteins and glycolipids. To be active, it is strictly dependent on its presence in the multienzyme complex. Appears to have a preference for alpha 2-3 and alpha 2-6 sialyl linkage (By similarity).
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A5PHD6
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PKS1_SARSH
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3-methylorcinaldehyde synthase (MOS) (EC 2.3.1.-) (Non-reducing polyketide synthase 1) (Xenovulene A biosynthesis cluster protein aspks1)
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MAAHGQTSKRGNNTLLLFGALVQSHDVSTLRSMRESIVVQHGEHSWLVDSIKALPQDFEAALPHLPFFDQATTTTIHQLLVDAVSSFLTGSFETLVSPLPAALLIPLAVATQLAHYVEYSRQSPTGLAEGKEALGFCTGILSAFAVASSHDVCDLAKYGAAAMRLGMLVGLVVDCEDAAAGQGRYRSVSAGWDSEEKHAAMLKIVQSFEEAYVSVHFDKNRATITTSPGTISNLTRQLQKEGLVASDMGLLGRFHFAGSTKPREVTVDQLVSFCNSPAGALFRLPDADSLRLATRINDRDGGLITQGSLHEHALQSILVKLAAWFETFSSATTTQANTGAQNGRARPQIVDFGPQNSVPHSLASTVDINSGNGKTRRVKPADAQSSANSTHTRPWLDTDIAIVGMSCKVPGAENLEEFWDLLVSGKSQHQEISGQEGGRFDFGDTAFRTAADQRRRWFANLVSNHDQFDHRFFKKSARESASMDPQQRHILQVAYQAVEGSGYFNKSSSSTPTNANIGCYVGLCLGDYESNVASHPATAFTATGNLQGFVSGKVSHYFGWTGPAVTVNTACSSSLVAVHLACQAILSGECEAALAGGSHIMTSATWFQNLAGGSFLSPTGACKPFDSKADGYCRGEGVGAVFLKRMSQAMADGDMVLGVVAATGVQQNQNCTPIFVPNAPSLENLFSRVMTKARVKPADISVVEGHGTGTAVGDPAEYDAIRKALGGTTHRSADKPLMLSSVKGLVGHMECTSGVIGMIKLLLMMNKGALPPQASFQSINPALGATPADHMFIPTRPQPWVVPAGGFRAALLNNYGASGSNASAVLVQSPSMSFRPEITVGSRPAAGIKFPFWLAAFDKKSLSRYVKALRKWLCRLDGDQSLASLSFNLARQSNRTMQANLVLTARSIEALDQSLADFENGNDGSFIERTPASSQPTVILCFGGQVSCFVGLDKQVYQDMALVRYYLDRVDAVIQCQGGRSIFPGIFNRSPPSKVDIVHLHTMLFAMQYASARCWIDSGVKPAALVGHSFGTLTALCISGILSLEDTIKAIMCRAKLLNEAWGPDQGGMIAVEGDIDVIEELLDEANKNHDDKPATIACYNGPTSFTLAGSTTAMDAVAAQLKNGAKYSKGMKSKRIYVTHAFHSVLVDPLLEELTQRVADSGVRFRKPIIPVELSTEQHMSESELTSEFMANHMRQPVYFHHAVERLARRYAGGSSPCVFLEAGTNSSVCNMASRALGSTEFVTKSSSLSFHGVNIANCDAGWNKLTDTTVNLWETGVRVHHWAHHGVQQMHQTDIKPLLVPPYQFDPDSRHWIDLKVPRKALMETDEADAGGKKQSDAEKLPETILTFHSSDAVGAQKQARFRVNTMLEEYKQLLRGHMTLETAPILSATLQINLVIEAISSTQPEYKSSKSQPQIQDVVYQSPVCFNSANTLWVEVTNVSGQWMFQVFSTTTQELSPKSTRMVHTKGTVAFKNPGDAEIRRQLMSYERLFSHGRATDLLQNSNASTAPIDEMLGNQSIYRIFSEIVSYGPEFRGLQKMVSRGNETAGHVVHLKHQDSASTEAEPWFDPHLADTFCQLGGLWVNCMMPERERGNGHVYLANGIDQWIRGYPAASTDRPEAFNVFAVNKQASEQLTLTDVFVFNAADGALVEVILGIAYVKIARPSMEKLLARLTEPSWVAGGKTTPQTATKPAAAPVVADHTPRTTESASTVNGVNLDDRKPEGTALPQEMLSDTEELRPKAQGQELQDMIARVKAVMADISGLDISEIKDDSNLADLGIDSLVGMEMTHEIESTLKVELPESEIMSVVDMEGLLQCVAGALGLSMTGASSDTLTASSDSGINSAKSSILSGTSTSTSTGTTDTGSDVGQSMKEPSLMLDTVKKAFAQTKEATDARIKAASNQVSYCSTSLPQQNELSVLLTITALEALGAGFSTARPGSQLTRISHAPGHEQFVTHLYKEIETATQIIKIDGHGAQAVITRTAVPLPDVESRQVALCEQMLRGDPEQVGTMELIKHAGENLHRVLSGETDGAKVIFGSKTGSKLVSQWYAQWPLNRSLIAQMGDFLTAVVAGIQADEDMPFSEINPLRIMETGAGTGGTTKQIVPLLARLGLPVVYTFTDLAPSFVAAARKTWGKEYPWMQFRTLDMEKTPPSVEDGLPLQHFIVSANAVHATKSISATTGNLRKALRTDGFLLMMEMTRTPFWVDLIFGLFEGWWLFEDGRKHALTHEALWDQELSKVGFGYVDWTEGMTAESEIQKIILASADANTRLERVRLPASHTDYHLNQVGVENEARELMVADYVSTLTKEFNKTMTQYTDAGLSLSSRTSQTPMSSQKRCILITGGTGGLGAHLVAEAALLPDVNMVICLNRPNRKQEARERQLVSLEKKGLILSPEALAKITVFETDLSQPGSLGLSDDKYNLLRGNVTHIIHNAWLMHSKWPVRRFEPQLRIMAHMLNLAADIATCQRTQGQRQPGPPVSFVFVSSIATVGYHPVVTNPGNPAVPETRIPISSVLPTGYGEAKYICERMLDATLHQYPAQFRASAVRLGQIAGSEINGHWNSAEHISFLVKSSQSIGALPALPGPMGWTPADYVARGLVEIATQPDNIELYPIYHIENPVRQPWDEALAVLADEMGISSEALPFQEWVQTVRDWPRQGDNTAAGANPAYLLVDFLEDHFLRMSCGGLLLGTAKAREHSPSLAGMGPVSDELLRLFVRSWKEVGFLL
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Non-reducing polyketide synthase part of the gene cluster that mediates the biosynthesis of xenovulene A, an unusual meroterpenoid that has potent inhibitory effects on the human gamma-aminobutyrate A (GABAA) benzodiazepine receptor. The first step of xenovulene A biosynthesis is the biosynthesis of 3-methylorcinaldehyde performed by the non-reducing polyketide synthase aspks1. The salicylate hydroxylase asL1 then catalyzes the oxidative dearomatization of 3-methylorcinaldehyde to yield a dearomatized hydroxycyclohexadione. The 2-oxoglutarate-dependent dioxygenase asL3 further catalyzes the oxidative ring expansion to provide the first tropolone metabolite. The cytochrome P450 monooxygenase asR2 allows the synthesis of tropolone hemiacetal. In parallel, a previously unrecognised class of terpene cyclase, asR6, produces alpha-humulene from farnesylpyrophosphate (FPP). The putative Diels-Alderase asR5 probably catalyzes the formation of the tropolone-humulene skeleton by linking humulene and the polyketide moiety. Oxidative-ring contractions catalyzed by asL4 and asL6 then processively remove carbon atoms from the polyketide to yield xenovulene A.
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A5PJM4
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FSP1_BOVIN
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Ferroptosis suppressor protein 1 (FSP1) (EC 1.6.5.-) (Apoptosis-inducing factor homologous mitochondrion-associated inducer of death) (AMID) (p53-responsive gene 3 protein)
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MGSQVSMDAGAVHVVIVGGGFGGIAAASQLQALNIPFVLVDMKDSFHHNVAALRASVESGFAKKTFISYSVTFKENFRQGLVVEIDLKNQTVLLEDGQALPFSHLILATGSTGLFPGKFNQVSSQQMAIQAYEDMVTQVQRSQSIVVVGGGSAGVEMAAEIKTEYPEKEVTLIHSKMALADTELLPCVRQEVKEILLRKGVQLLLSERVSNLEALPVNERRECIKVQTDKGTEVDANLVIVCNGIKINSAAYRSAFGDRLASNGALRVNEYLQVEGYSHIYAIGDCADVREPKMAYHASLHANVAVANIVNSMKQRPLKTYKPGSLTFLLAMGRNDGVGQISGFYVGRLMVRLAKSRDLLVSTSWKTMKQSPP
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A NAD(P)H-dependent oxidoreductase that acts as a key inhibitor of ferroptosis. At the plasma membrane, catalyzes reduction of coenzyme Q/ubiquinone-10 to ubiquinol-10, a lipophilic radical-trapping antioxidant that prevents lipid oxidative damage and consequently ferroptosis. Acts in parallel to GPX4 to suppress phospholipid peroxidation and ferroptosis. This anti-ferroptotic function is independent of cellular glutathione levels. Also acts as a potent radical-trapping antioxidant by mediating warfarin-resistant vitamin K reduction in the canonical vitamin K cycle: catalyzes NAD(P)H-dependent reduction of vitamin K (phylloquinone, menaquinone-4 and menadione) to hydroquinone forms. Hydroquinones act as potent radical-trapping antioxidants inhibitor of phospholipid peroxidation and ferroptosis. May play a role in mitochondrial stress signaling. Upon oxidative stress, associates with the lipid peroxidation end product 4-hydroxy-2-nonenal (HNE) forming a lipid adduct devoid of oxidoreductase activity, which then translocates from mitochondria into the nucleus triggering DNA damage and cell death.
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A5PJN2
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ERO1A_BOVIN
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ERO1-like protein alpha (ERO1-L) (ERO1-L-alpha) (EC 1.8.4.-) (Endoplasmic reticulum oxidoreductase alpha) (Endoplasmic reticulum oxidoreductin-1-like protein) (Oxidoreductin-1-L-alpha)
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MGRRWGFLIGFLVAVGLLGLGHGEQQPSETAAQRCFCQVSGYLDDCTCDVETIDKFNNYRLFPRLQKLLESDYFRYYKVNLKRPCPFWNDINQCGRRDCAVKPCHSDEVPDGIKSASYKYSEEANNLIEECEQAERLGAVDESLSEETQKAVLQWTKHDDSSDNFCEVDDIQSPDAEYVDLLLNPERYTGYKGPDAWKIWNVIYEENCFKPQTIKRPLNPLASGQGKSEENTFYSWLEGLCVEKRAFYRLISGLHASINVHLSARYLLQDTWLEKKWGHNITEFQQRFDGILTEGEGPRRLKNLYFLYLIELRALSKVVPFFERPDFQLFTGNKDQDAENKMLLLEILHEIKSFPLHFDENSFFAGNKKEANKLKEDFRLHFRNISRIMDCVGCLKCRLWGKLQTQGLGTALKILFSEKLIANMPESGPSYEFHLTRQEIVSLFNAFGRISTSVKELENFRNLLQNIH
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Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the proper folding of immunoglobulins. Plays an important role in ER stress-induced, CHOP-dependent apoptosis by activating the inositol 1,4,5-trisphosphate receptor IP3R1.
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A5PJP6
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BRCC3_BOVIN
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Lys-63-specific deubiquitinase BRCC36 (EC 3.4.19.-) (BRCA1-A complex subunit BRCC36) (BRCA1/BRCA2-containing complex subunit 3) (BRCA1/BRCA2-containing complex subunit 36) (BRISC complex subunit BRCC36)
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MAVQVVQAVQAVHLESDAFLVCLNHALSTEKEEVMGLCIGELNDDLRNDPKFTYTGTEMRTVAEKVDTVRIVHIHSVIILRRSDKRKDRVEISPEQLSAASTEAERLAELTGRPMRVVGWYHSHPHITVWPSHVDVRTQAMYQMMDQGFVGLIFSCFIEDKNTKTGRVLYTCFQSIQAQKSSESPRGPRDFWSSSQHISIEGQKEEERYERIEIPIHIVPHVTIGKVCLESAVELPKILCQEEQDAYRRIHSLTHLDSVTKIHNGSVFTKNLCSQMSAVSGPLLQWLEDRLEQNQQHVQELQQEKEELLQELSSLE
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Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not have activity toward 'Lys-48'-linked polyubiquitin chains. Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). In the BRCA1-A complex, it specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX, antagonizing the RNF8-dependent ubiquitination at double-strand breaks (DSBs). Catalytic subunit of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. Mediates the specific 'Lys-63'-specific deubiquitination associated with the COP9 signalosome complex (CSN), via the interaction of the BRISC complex with the CSN complex. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1. Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1 deubiquitination increases IFNAR1 activity by enhancing its stability and cell surface expression (By similarity). Acts as a regulator of the NLRP3 inflammasome by mediating deubiquitination of NLRP3, leading to NLRP3 inflammasome assembly (By similarity). Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination (By similarity). Deubiquitinates HDAC1 and PWWP2B leading to their stabilization (By similarity).
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A5PJS6
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UBP10_BOVIN
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Ubiquitin carboxyl-terminal hydrolase 10 (EC 3.4.19.12) (Deubiquitinating enzyme 10) (Ubiquitin thioesterase 10) (Ubiquitin-specific-processing protease 10)
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MALRSPQYIFGDFSPDEFNQFFVTPRASVELPPYGGTVLCGAQAADDLPDGHDYQRIEFGVNEVIEPSDTLPRTPNYSISSTLNPQAPEFILSCTTSKKLPDDIDKEVNYSSANCQYPGPALALDGGSPAEAEALENDGVSGGLGQRERKKKKKRPPGYYSYLKDGGEGGPSAEALVNGHAGPAVSNSVGAEDTDLMGDVPTAGTPRTWGSPQDATDFVSDAGPAGAFPGALDGGARTAGQLEGCPGADSEASCLPAEAGRDTLLRTAVAQPSVGTDTTENLGVTNGQILESLGEGTAANGVELHTVESSDSDPAKAESAPPPADAPASAAGTVPASQPAKSWASLFHDSKPSSSSLPVVSVETKYSPPATSPLVSEKQAEVKEGLVPVSEDPVAIKIAELLENVTLIHKPVSLQPRGLINKGNWCYINATLQALVACPPMYHLMKLIPLYSKVQRPCTSTPMIDSFVRLMNEFTNMPVPPKPRQALGDKIVRDIRPGAAFEPTYIYRLLTVIKSSLSEKGRQEDAEEYLGFILNGLHEEMLNLKKLLSPNNDKLTISNGPKSHSVNEDEQEEPGEGSEDEWEQVGPRNKTSVTRQADFVQTPITGIFGGHIRSVVYQQSSKESATLQPFFTLQLDIQSDKIRTVQDALESLVARESVQGYTTKTRQEVEISRRVTLEKLPPVLVLHLKRFVYEKTGGCQKLIKNIEYPVDLEISKELLSPGVKNKNFKCHRTYRLFAVVYHHGSSATGGHYTTDVFQIGLNGWLRIDDQTVKVVSQQQVVRPAAERTAYLLYYRRVDLL
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Hydrolase that can remove conjugated ubiquitin from target proteins such as p53/TP53, RPS2/us5, RPS3/us3, RPS10/eS10, BECN1, SNX3 and CFTR. Acts as an essential regulator of p53/TP53 stability: in unstressed cells, specifically deubiquitinates p53/TP53 in the cytoplasm, leading to counteract MDM2 action and stabilize p53/TP53. Following DNA damage, translocates to the nucleus and deubiquitinates p53/TP53, leading to regulate the p53/TP53-dependent DNA damage response. Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes. In turn, PIK3C3/VPS34-containing complexes regulate USP10 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Does not deubiquitinate MDM2. Plays a key role in 40S ribosome subunit recycling when a ribosome has stalled during translation: acts both by inhibiting formation of stress granules, which store stalled translation pre-initiation complexes, and mediating deubiquitination of 40S ribosome subunits. Acts as a negative regulator of stress granules formation by lowering G3BP1 and G3BP2 valence, thereby preventing G3BP1 and G3BP2 ability to undergo liquid-liquid phase separation (LLPS) and assembly of stress granules. Promotes 40S ribosome subunit recycling following ribosome dissociation in response to ribosome stalling by mediating deubiquitination of 40S ribosomal proteins RPS2/us5, RPS3/us3 and RPS10/eS10, thereby preventing their degradation by the proteasome. Part of a ribosome quality control that takes place when ribosomes have stalled during translation initiation (iRQC): USP10 acts by removing monoubiquitination of RPS2/us5 and RPS3/us3, promoting 40S ribosomal subunit recycling. Deubiquitinates CFTR in early endosomes, enhancing its endocytic recycling. Involved in a TANK-dependent negative feedback response to attenuate NF-kappa-B activation via deubiquitinating IKBKG or TRAF6 in response to interleukin-1-beta (IL1B) stimulation or upon DNA damage. Deubiquitinates TBX21 leading to its stabilization.
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A5PJZ1
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SCMC1_BOVIN
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Mitochondrial adenyl nucleotide antiporter SLC25A24 (Small calcium-binding mitochondrial carrier protein 1) (SCaMC-1) (Solute carrier family 25 member 24)
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MLRWLRGFVLPTAACQDVEPPTRYETLFQKLDRNGDGVVDISELQEGLKSLGIPLGQDAEEKIFTTGDVNKDGKLDFEEFMKYLKDHEKKMKLAFKSLDKNNDGKIEASEIVQSLQILGLTISEQQAELILQSIDADGTMTVDWNEWRDYFLFNPVTDIEEIIRFWKHSTGIDIGDSLTIPDEFTEDEKKSGQWWRQLLAGGVAGAVSRTSTAPLDRLKVMMQVHGSKSAKMNIYGGFQQMVKEGGIRSLWRGNGTNVIKIAPETAVKFWAYEQYKKLLTEEGQKIGTFERFVSGSMAGATAQTFIYPMEVLKTRLAVGKTGQYSGMFDCAKKILKYEGMGAFYKGYVPNLLGIIPYAGIDLAVYELLKSHWLDNFAKDSVNPGVMVLLGCGALSSTCGQLASYPLALVRTRMQAQAMIEKSPQLNMVGLFRRILSKEGLPGLYRGITPNFMKVLPAVGISYVVYENMKQTLGVTQK
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Electroneutral antiporter that mediates the transport of adenyl nucleotides through the inner mitochondrial membrane. Originally identified as an ATP-magnesium/inorganic phosphate antiporter, it also acts as a broad specificity adenyl nucleotide antiporter. By regulating the mitochondrial matrix adenyl nucleotide pool could adapt to changing cellular energetic demands and indirectly regulate adenyl nucleotide-dependent metabolic pathways. In vitro, a low activity is also observed with guanyl and pyrimidine nucleotides. May play a role in protecting cells against oxidative stress-induced cell death, by buffering calcium levels in the mitochondrial matrix through the formation of calcium-phosphate precipitates.
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A5PK42
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ODAD4_BOVIN
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Outer dynein arm-docking complex subunit 4 (Tetratricopeptide repeat protein 25) (TPR repeat protein 25)
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MADPENEVLRSTFPSYMAEGERLYLCGEFAKAAHSFSNALHLQSGDKNCLVARSKCFLKMGELEKSLEDAEASLQGDPTFCKGILQKAETLYTMGDFEFALVFYHRGYKLRPDREFKVGIQKAQEAINNSVGSPSSIKLENKGDLSFLSKQAESMRAQQKPHPVRQLIHHPKRESKRKGSLKSEKIVRQLLGELYVDKEYLEKLLLDEDLIKGTIKHGLTVEDLIMTGINYLETRSDFWRQQKPIYARERDRKLMQEKWLRDRKRRPSQTARYILKSLEDIDMLLTSGSAEGSLQKAEKVLKKVLEWNKEEVPNKDELVGNLYSCIGNAQIELGQMVAALQSHRKDLEIAKEYDLPDAKSRALDNIGRVFARVGKFQQAIDTWEEKIPLAKTTLEKTWLFHEIGRCYLELDQAWEAQSYGEKSQQCAEEEGDMEWQLNASVLVAQAQVKLRDFESAVNNFEKALERAKLVHNNEAQQAIINALDDANKGIIEELKKTNYREILKEKKEKENATMLDGQTRTAKEKETRKTKDEPEKVMKQWVQEQTEKQLEGVLSKETLGVTARQPEQRQREDPEKASWRKELGAKERGPGDTAKGQFGEAGRTEQNREETREIYRRPSELDQNLSDESSPRESEGLEKRLSKTDGGELEALGKTESGEIKEMEITENSEKIEKDEKEDEPIE
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Component of the outer dynein arm-docking complex (ODA-DC) that mediates outer dynein arms (ODA) binding onto the doublet microtubule. Plays an essential role for the assembly of ODA-DC and for the docking of ODA in ciliary axoneme.
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A5PK46
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LIPR2_BOVIN
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Pancreatic lipase-related protein 2 (PL-RP2) (Cytotoxic T lymphocyte lipase) (Galactolipase) (EC 3.1.1.26) (Triacylglycerol lipase) (EC 3.1.1.3)
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MLPSWTIGLLLLATVRGKEICYEPFGCFSDEKPWTGILQRPLKLFPWSPEDIDAHFLLYTNENPNNYQRINITDLATVRASNFQLDRKTRFVIHGFIDDGDSGWPTDLCKKMFKVEKVNCICVDWEHGAWTKYTQAVHNTRVVGAEIAFFIQGLSTELGYGPENVHLIGHSLGAQLAAEAGRRLGGQVGRITGLDPAQPCFEGTPEEVRLDPSDAMFVDVIHTDSASIIPFLSLGIRQKVGHLDFYPNGGKEMPGCQKNILSTIIDINGIWQGIQDFVACSHLRSYKYYSSSILNPDGFLGYPCASYEEFQEGGCFPCPAGGCPKMGHYADQFQGKTSAVGQTFFLNTGSSGNFTSWRYRVSVTLAGTKKVRGSIRIALYGSNGNSKQYQIFKGSLQPNASHTHDIDVDLNVGKVQKVKFLWNNNVINLFWPKLGASRVTVQGGEDRTEYNFCSNDTMRENALQTLYPC
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Lipase that primarily hydrolyzes triglycerides and galactosylglycerides. In neonates, may play a major role in pancreatic digestion of dietary fats such as milk fat globules enriched in long-chain triglycerides. Hydrolyzes short-, medium- and long-chain fatty acyls in triglycerides without apparent positional specificity. Can completely deacylate triacylglycerols. When the liver matures and bile salt synthesis increases, likely functions mainly as a galactolipase and monoacylglycerol lipase. Hydrolyzes monogalactosyldiglycerols (MGDG) and digalactosyldiacylglycerols (DGDG) present in a plant-based diet, releasing long-chain polyunsaturated fatty acids. Hydrolyzes medium- and long-chain fatty acyls in galactolipids. May act together with LIPF to hydrolyze partially digested triglycerides. Hydrolyzes long-chain monoglycerides with high efficiency (By similarity). In cytotoxic T cells, contributes to perforin-dependent cell lysis, but is unlikely to mediate direct cytotoxicity (By similarity). Also has low phospholipase activity (By similarity). In neurons, required for the localization of the phospholipid 1-oleoyl-2-palmitoyl-PC (OPPC) to neurite tips through acyl chain remodeling of membrane phospholipids (By similarity). The resulting OPPC-rich lipid membrane domain recruits the t-SNARE protein STX4 by selectively interacting with the STX4 transmembrane domain and this promotes surface expression of the dopamine transporter SLC6A3/DAT at neurite tips by facilitating fusion of SLC6A3-containing transport vesicles with the plasma membrane (By similarity).
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A5PK74
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RIOX1_BOVIN
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Ribosomal oxygenase 1 (Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66) (EC 1.14.11.27, EC 1.14.11.79) (Histone lysine demethylase NO66)
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MDGLRASAGLLRRGRLRRRRQQQPHSGSVLALPLRPRKIRRQLRRSVSSRMAALRAQTLQSEDSEDSRVESTVGEPGDPLAGGTAALSDATGREPHGQLGPVELLEASPASRSLQTPRALVEAQTPAARLVEAQTPAARLVEAHTPAARLVEAHTPPARLVEASALPARLVETSALLCSTQHLAAVPPSVAPAMLSGPQGESTGEELPWDSPLQRILAELNRIPSSRRRAARLFEWLISPMPPDHFYRRLWEREAVLVRRQDHSYYQGLFSTAVLDSILRNEEVQFGQHLDAARYINGRRETLNPPGRALPAAAWSLYRAGCSLRLLCPQAFSTTVWQFLAVLQEQFGSMAGSNVYLTPPNSQGFAPHYDDIEAFVLQLEGRKLWRVYRPRVPTEELALTSSPNFSQDDLGEPVLQTVLEPGDLLYFPRGFIHQAECQDGVHSLHLTLSTFQRNTWGDFLEAVLPLAVQAAMEENVEFRRGLPRDFMDYMGAQHSDSKDPRRTAFMEKVRVLVARLGHFAPVDAVADQRAKDFIHDSLPPVLTDRERALSVYGLPIRWEAGEPVNVGAQLTTETEVHMLQDGIARLVGEGGHLFLYYTVENSRVYHLEEPKCLEIYPQQADAMELLLRSYPEFVRVGDLPCDTVEDQLSLATMLYDKGLLLTKMPLT
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Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase (By similarity). Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' (H3K4me3) and monomethylated H3 'Lys-4' (H3K4me1) residues, while it has weaker activity for dimethylated H3 'Lys-36' (H3K36me2). Acts as a regulator of osteoblast differentiation via its interaction with SP7/OSX by demethylating H3K4me and H3K36me, thereby inhibiting SP7/OSX-mediated promoter activation. Also catalyzes demethylation of non-histone proteins, such as CGAS: demethylation of monomethylated CGAS promotes interaction between CGAS and PARP1, followed by PARP1 inactivation (By similarity). Also catalyzes the hydroxylation of 60S ribosomal protein L8 on 'His-216', thereby playing a role in ribosome biogenesis. Participates in MYC-induced transcriptional activation (By similarity).
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A5PKJ4
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MK07_BOVIN
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Mitogen-activated protein kinase 7 (MAP kinase 7) (MAPK 7) (EC 2.7.11.24)
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MAEPLKEDDGEDGSGEPPGPVKAEPAGTAASVAAKNLALLKARSFDVTFDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYGEFKSVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPAEHQYFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMTVLGTPSPAVIQAVGAERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARVSAAAALRHPFLAKYHDPDDEPDCAPPFDFAFDREALTRERIKEAIVAEIEDFHARREGIRQQIRFQPSLQPVASEPGCPDVEMPSPWAPSGDCAMESPPPAPLPCPGPAPDTIDLTLQPPPPASEPAPPKKEGAISDNTKAALKAALLKSLRSRLRDGPSAPLEAPEPRKPVTAQERQREREEKRRRRQERAKEREKRRQERERKERGAGVSGGPSADPLAGLVLSDNDRSLLERWTRMAQPPAPAPATARPPSPPAGPATQPTGPLPQPACPPPAPAAGPAAPQTTAASGLLAPQPLVPPPGLPGPSALSVLPYFPSGPPPPDPGGAPQPSTSESPDVTLVTQQLSKSQVEDPLPPVFSGTPKGSGAGYGVGFDLEEFLNQSFDMGVADGPQDGQADSASLSASLLADWLEGHGMNPADIESLQREIQMDSPMLLADLPDLQEP
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Plays a role in various cellular processes such as proliferation, differentiation and cell survival. The upstream activator of MAPK7 is the MAPK kinase MAP2K5. Upon activation, it translocates to the nucleus and phosphorylates various downstream targets including MEF2C. EGF activates MAPK7 through a Ras-independent and MAP2K5-dependent pathway. May have a role in muscle cell differentiation. May be important for endothelial function and maintenance of blood vessel integrity. MAP2K5 and MAPK7 interact specifically with one another and not with MEK1/ERK1 or MEK2/ERK2 pathways. Phosphorylates SGK1 at Ser-78 and this is required for growth factor-induced cell cycle progression (By similarity). Involved in the regulation of p53/TP53 by disrupting the PML-MDM2 interaction (By similarity).
|
A5PKP9
|
UB2D4_XENLA
|
Ubiquitin-conjugating enzyme E2 D4 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme D4) (Ubiquitin carrier protein D4) (Ubiquitin-protein ligase D4)
|
MALKRIQKELMDLQRDPPAQCSAGPVGEDLFHWQATIMGPNDSPFQGGVFFLTIHFPTDYPFKPPKVAFTTKIYHPNINSNGSICLDILRSQWSPALTVSKVLLSICSLLCDPNPDDPLVPEIAHTYKADREKYNRLAREWTQKYAM
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Catalyzes the covalent attachment of ubiquitin to other proteins. Regulates pronephros development, possibly by promoting ubiquitination and thus inactivation or degradation of map3k10/mlk2. {ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000269|PubMed:18021256}.
|
A5PKW4
|
PSD1_HUMAN
|
PH and SEC7 domain-containing protein 1 (Exchange factor for ADP-ribosylation factor guanine nucleotide factor 6) (Exchange factor for ARF6) (Exchange factor for ARF6 A) (Pleckstrin homology and SEC7 domain-containing protein 1)
|
MAQGAMRFCSEGDCAISPPRCPRRWLPEGPVPQSPPASMYGSTGSLLRRVAGPGPRGRELGRVTAPCTPLRGPPSPRVAPSPWAPSSPTGQPPPGAQSSVVIFRFVEKASVRPLNGLPAPGGLSRSWDLGGVSPPRPTPALGPGSNRKLRLEASTSDPLPARGGSALPGSRNLVHGPPAPPQVGADGLYSSLPNGLGGPPERLATLFGGPADTGFLNQGDTWSSPREVSSHAQRIARAKWEFFYGSLDPPSSGAKPPEQAPPSPPGVGSRQGSGVAVGRAAKYSETDLDTVPLRCYRETDIDEVLAEREEADSAIESQPSSEGPPGTAYPPAPRPGPLPGPHPSLGSGNEDEDDDEAGGEEDVDDEVFEASEGARPGSRMPLKSPVPFLPGTSPSADGPDSFSCVFEAILESHRAKGTSYTSLASLEALASPGPTQSPFFTFELPPQPPAPRPDPPAPAPLAPLEPDSGTSSAADGPWTQRGEEEEAEARAKLAPGREPPSPCHSEDSLGLGAAPLGSEPPLSQLVSDSDSELDSTERLALGSTDTLSNGQKADLEAAQRLAKRLYRLDGFRKADVARHLGKNNDFSKLVAGEYLKFFVFTGMTLDQALRVFLKELALMGETQERERVLAHFSQRYFQCNPEALSSEDGAHTLTCALMLLNTDLHGHNIGKRMTCGDFIGNLEGLNDGGDFPRELLKALYSSIKNEKLQWAIDEEELRRSLSELADPNPKVIKRISGGSGSGSSPFLDLTPEPGAAVYKHGALVRKVHADPDCRKTPRGKRGWKSFHGILKGMILYLQKEEYKPGKALSETELKNAISIHHALATRASDYSKRPHVFYLRTADWRVFLFQAPSLEQMQSWITRINVVAAMFSAPPFPAAVSSQKKFSRPLLPSAATRLSQEEQVRTHEAKLKAMASELREHRAAQLGKKGRGKEAEEQRQKEAYLEFEKSRYSTYAALLRVKLKAGSEELDAVEAALAQAGSTEDGLPPSHSSPSLQPKPSSQPRAQRHSSEPRPGAGSGRRKP
|
Guanine nucleotide exchange factor for ARF6. Induces cytoskeletal remodeling (By similarity).
|
A5PLL7
|
PDES1_HUMAN
|
Plasmanylethanolamine desaturase 1 (EC 1.14.19.77) (Transmembrane protein 189)
|
MAGAENWPGQQLELDEDEASCCRWGAQHAGARELAALYSPGKRLQEWCSVILCFSLIAHNLVHLLLLARWEDTPLVILGVVAGALIADFLSGLVHWGADTWGSVELPIVGKAFIRPFREHHIDPTAITRHDFIETNGDNCLVTLLPLLNMAYKFRTHSPEALEQLYPWECFVFCLIIFGTFTNQIHKWSHTYFGLPRWVTLLQDWHVILPRKHHRIHHVSPHETYFCITTGWLNYPLEKIGFWRRLEDLIQGLTGEKPRADDMKWAQKIK
|
Plasmanylethanolamine desaturase involved in plasmalogen biogenesis in the endoplasmic reticulum membrane. Plasmalogens are glycerophospholipids with a hydrocarbon chain linked by a vinyl ether bond at the glycerol sn-1 position, and are involved in antioxidative and signaling mechanisms.
|
A5PN09
|
UBP20_DANRE
|
Ubiquitin carboxyl-terminal hydrolase 20 (EC 3.4.19.12) (Deubiquitinating enzyme 20) (Ubiquitin thioesterase 20) (Ubiquitin-specific-processing protease 20)
|
MTDSGDLCPHLDSIGEVTKEELIQKSKGTCQSCGVGGPNLWACLQCDCPYVGCGESYSDHSTIHAQAKKHNLTVNLTTFRVWCYVCEREVFLEPKPVTPVSSAHRCKPHDQDPVSQTTCYPLKAVPIAVADEEGSESEEDELKPRGLTGMKNIGNSCYMNAALQALSNCPPLTQFFQDCSGLVRTDKKPALCKSYQKLISELWHKKRPSYVVPTTLFHGIKLVNPMFRGYAQQDTQEFLRCLMDQLHEELKEPLFDCSGGISEVEPDLSLDSCNLVDGDRSPSEDEFLSCDSGSGSERGDGERAGGEAELLIQDECVAVRGTGGISEKERLKERRGEERTREMDEDADVDTAAQDGQAERETETATPATAVPAPGNTEPDNEASMHCPSSRPCSPAHSVQELHSRLSSNPPRSSPLRTGPTYTFKKAQMLLSTKKKKQSRFRSVISDIFDGSILSLVQCLTCDRVSTTVETFQDLSLPIPGKEDLAKLHSSIHQSAPVKAGVCTDGYAAQGWISYIMDSIRRFVVSCIPSWFWGPMVTLEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLRLPEILCIHLKRFRHEVMYSFKINSHVSFPLEGLDLKPFLAKESPSQITTYDLLSVICHHGTAGSGHYIAYCQNVINGQWYEFDDQYVTEVHETVVQNAEAYVLFYRKSSEESVRERQRVVALANLKEPSLLQFYISREWLNKFNTFTEPGPITNHTFLCQHGGIPPTKYHYVDDLVVILPQNVWEYLYNRFGGGPAVNHLYVCAICQVEIETLAKRRKLEIDTFIKLNKEFQAEEAPTVILCISMQWFREWENFVKGKDNEPPGPIDNSKIAVMKGGHIQLKQGADYGQISEETWQYLLSIYGGGPEIAVRQTISPPDTDTHGERKIEAETRAL
|
Deubiquitinating enzyme involved in beta-2 adrenergic receptor (adrb2) recycling. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination beta-2 adrenergic receptor (adrb2). Plays a central role in adrb2 recycling and resensitization after prolonged agonist stimulation by constitutively binding adrb2, mediating deubiquitination of adrb2 and inhibiting lysosomal trafficking of adrb2. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity).
|
A5PN28
|
OTO1A_DANRE
|
Otolin-1-A (zOtolin1)
|
MPNILHPFIIIMTLLVVATGNQASIDKTTQWPRMKPTKKPPPRDEGPSKLGSISTTVSPTAIGITEEVTDAMMDAYTITSTGSTTFSSDTYSADYHTEAMVPPGVGPGNYTLDYNECFFNFCECCPPERGPPGPVGEKGLPGIPGGKGEMGPPGPPGQEGLTGAPGTHGVKGEKGDTGASGLPGIPGVTGKQGEKGESGPKGDKGDTGFPGLKGDPGERGEPGWNGTKGGMGEPGKQGLTGPPGPDGIKGEKGDKGDCPFGEKGQKGSIGEPGPQGPKGDPGVPGTNGTDGLPGSKGPKGDPGPLSKQGEPGPPGPQGPPGQRGMPGMKGTRGLKGARGIRGFKGFKGEPAVQKRSAFSVGLFPSRSFPPPGLPIRFDKIIYNEEAHWDPNASKFNCTHGGVYVFSYYITVRNRPLRAALVVNGIRKLRTRDSLYGQDIDQASNMAVLRLSSGDQVWLETLRDWNGVYSSSEDDSTFSGFLLYADATKD
|
Collagen-like protein, which provides an organic scaffold for otoliths onto the sensory epithelium of the inner ear. Acts as a scaffold for biomineralization by sequestering calcium.
|
A5TY85
|
PKNA_MYCTA
|
Serine/threonine-protein kinase PknA (EC 2.7.11.1)
|
MSPRVGVTLSGRYRLQRLIATGGMGQVWEAVDNRLGRRVAVKVLKSEFSSDPEFIERFRAEARTTAMLNHPGIASVHDYGESQMNGEGRTAYLVMELVNGEPLNSVLKRTGRLSLRHALDMLEQTGRALQIAHAAGLVHRDVKPGNILITPTGQVKITDFGIAKAVDAAPVTQTGMVMGTAQYIAPEQALGHDASPASDVYSLGVVGYEAVSGKRPFAGDGALTVAMKHIKEPPPPLPPDLPPNVRELIEITLVKNPAMRYRSGGPFADAVAAVRAGRRPPRPSQTPPPGRAAPAAIPSGTTARVAANSAGRTAASRRSRPATGGHRPPRRTFSSGQRALLWAAGVLGALAIIIAVLLVIKAPGDNSPQQAPTPTVTTTGNPPASNTGGTDASPRLNWTERGETRHSGLQSWVVPPTPHSRASLARYEIAQ
|
Protein kinase that regulates many aspects of mycobacterial physiology. Is a key component of a signal transduction pathway that regulates cell growth, cell shape and cell division via phosphorylation of target proteins such as FtsZ and MurD. Shows a strong preference for Thr versus Ser as the phosphoacceptor.
|
A5U1U6
|
KGD_MYCTA
|
Multifunctional 2-oxoglutarate metabolism enzyme (2-hydroxy-3-oxoadipate synthase) (HOA synthase) (HOAS) (EC 2.2.1.5) (2-oxoglutarate carboxy-lyase) (2-oxoglutarate decarboxylase) (Alpha-ketoglutarate decarboxylase) (KG decarboxylase) (KGD) (EC 4.1.1.71) (Alpha-ketoglutarate-glyoxylate carboligase) [Includes: 2-oxoglutarate dehydrogenase E1 component (ODH E1 component) (EC 1.2.4.2) (Alpha-ketoglutarate dehydrogenase E1 component) (KDH E1 component); Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (EC 2.3.1.61) (2-oxoglutarate dehydrogenase complex E2 component) (ODH E2 component) (OGDC-E2) (Dihydrolipoamide succinyltransferase)]
|
MANISSPFGQNEWLVEEMYRKFRDDPSSVDPSWHEFLVDYSPEPTSQPAAEPTRVTSPLVAERAAAAAPQAPPKPADTAAAGNGVVAALAAKTAVPPPAEGDEVAVLRGAAAAVVKNMSASLEVPTATSVRAVPAKLLIDNRIVINNQLKRTRGGKISFTHLLGYALVQAVKKFPNMNRHYTEVDGKPTAVTPAHTNLGLAIDLQGKDGKRSLVVAGIKRCETMRFAQFVTAYEDIVRRARDGKLTTEDFAGVTISLTNPGTIGTVHSVPRLMPGQGAIIGVGAMEYPAEFQGASEERIAELGIGKLITLTSTYDHRIIQGAESGDFLRTIHELLLSDGFWDEVFRELSIPYLPVRWSTDNPDSIVDKNARVMNLIAAYRNRGHLMADTDPLRLDKARFRSHPDLEVLTHGLTLWDLDRVFKVDGFAGAQYKKLRDVLGLLRDAYCRHIGVEYAHILDPEQKEWLEQRVETKHVKPTVAQQKYILSKLNAAEAFETFLQTKYVGQKRFSLEGAESVIPMMDAAIDQCAEHGLDEVVIGMPHRGRLNVLANIVGKPYSQIFTEFEGNLNPSQAHGSGDVKYHLGATGLYLQMFGDNDIQVSLTANPSHLEAVDPVLEGLVRAKQDLLDHGSIDSDGQRAFSVVPLMLHGDAAFAGQGVVAETLNLANLPGYRVGGTIHIIVNNQIGFTTAPEYSRSSEYCTDVAKMIGAPIFHVNGDDPEACVWVARLAVDFRQRFKKDVVIDMLCYRRRGHNEGDDPSMTNPYVYDVVDTKRGARKSYTEALIGRGDISMKEAEDALRDYQGQLERVFNEVRELEKHGVQPSESVESDQMIPAGLATAVDKSLLARIGDAFLALPNGFTAHPRVQPVLEKRREMAYEGKIDWAFGELLALGSLVAEGKLVRLSGQDSRRGTFSQRHSVLIDRHTGEEFTPLQLLATNSDGSPTGGKFLVYDSPLSEYAAVGFEYGYTVGNPDAVVLWEAQFGDFVNGAQSIIDEFISSGEAKWGQLSNVVLLLPHGHEGQGPDHTSARIERFLQLWAEGSMTIAMPSTPSNYFHLLRRHALDGIQRPLIVFTPKSMLRHKAAVSEIKDFTEIKFRSVLEEPTYEDGIGDRNKVSRILLTSGKLYYELAARKAKDNRNDLAIVRLEQLAPLPRRRLRETLDRYENVKEFFWVQEEPANQGAWPRFGLELPELLPDKLAGIKRISRRAMSAPSSGSSKVHAVEQQEILDEAFG
|
Shows three enzymatic activities that share a first common step, the attack of thiamine-PP on 2-oxoglutarate (alpha-ketoglutarate, KG), leading to the formation of an enamine-thiamine-PP intermediate upon decarboxylation. Thus, displays KGD activity, catalyzing the decarboxylation from five-carbon 2-oxoglutarate to four-carbon succinate semialdehyde (SSA). Also catalyzes C-C bond formation between the activated aldehyde formed after decarboxylation of alpha-ketoglutarate and the carbonyl of glyoxylate (GLX), to yield 2-hydroxy-3-oxoadipate (HOA), which spontaneously decarboxylates to form 5-hydroxylevulinate (HLA). And is also a component of the 2-oxoglutarate dehydrogenase (ODH) complex, that catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). The KG decarboxylase and KG dehydrogenase reactions provide two alternative, tightly regulated, pathways connecting the oxidative and reductive branches of the TCA cycle (By similarity).
|
A5U493
|
BLAC_MYCTA
|
Beta-lactamase (EC 3.5.2.6) (Ambler class A beta-lactamase)
|
MRNRGFGRRELLVAMAMLVSVTGCARHASGARPASTTLPAGADLADRFAELERRYDARLGVYVPATGTTAAIEYRADERFAFCSTFKAPLVAAVLHQNPLTHLDKLITYTSDDIRSISPVAQQHVQTGMTIGQLCDAAIRYSDGTAANLLLADLGGPGGGTAAFTGYLRSLGDTVSRLDAEEPELNRDPPGDERDTTTPHAIALVLQQLVLGNALPPDKRALLTDWMARNTTGAKRIRAGFPADWKVIDKTGTGDYGRANDIAVVWSPTGVPYVVAVMSDRAGGGYDAEPREALLAEAATCVAGVLA
|
Extended spectrum beta-lactamase (ESBL) that inactivates beta-lactam antibiotics by hydrolyzing the amide group of the beta-lactam ring. Exhibits predominant penicillinase activity. Also displays high levels of cephalosporinase activity as well as measurable activity with carbapenems, including imipenem and meropenem. Plays a primary role in the intrinsic resistance of M.tuberculosis to beta-lactam antibiotics.
|
A5U4N0
|
ADOK_MYCTA
|
Adenosine kinase (ADK) (AK) (EC 2.7.1.20)
|
MTIAVTGSIATDHLMRFPGRFSEQLLPEHLHKVSLSFLVDDLVMHRGGVAGNMAFAIGVLGGEVALVGAAGADFADYRDWLKARGVNCDHVLISETAHTARFTCTTDVDMAQIASFYPGAMSEARNIKLADVVSAIGKPELVIIGANDPEAMFLHTEECRKLGLAFAADPSQQLARLSGEEIRRLVNGAAYLFTNDYEWDLLLSKTGWSEADVMAQIDLRVTTLGPKGVDLVEPDGTTIHVGVVPETSQTDPTGVGDAFRAGFLTGRSAGLGLERSAQLGSLVAVLVLESTGTQEWQWDYEAAASRLAGAYGEHAAAEIVAVLA
|
Catalyzes the phosphorylation of adenosine to adenosine monophosphate (AMP). Can also catalyze the phosphorylation of the adenosine analog 2-methyladenosine (methyl-Ado) to methyl-AMP, the first step in the metabolism of this compound to an active form that displays antitubercular activity. Is not active on guanosine, inosine, deoxyadenosine, cytidine, uridine, or thymidine. Prefers dGTP and GTP to ATP as phosphate donors in vitro.
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A5U654
|
PPGK_MYCTA
|
Polyphosphate glucokinase (Poly(P) glucokinase) (EC 2.7.1.63) (ATP-dependent glucokinase) (EC 2.7.1.2) (Polyphosphate--glucose phosphotransferase)
|
MTSTGPETSETPGATTQRHGFGIDVGGSGIKGGIVDLDTGQLIGDRIKLLTPQPATPLAVAKTIAEVVNGFGWRGPLGVTYPGVVTHGVVRTAANVDKSWIGTNARDTIGAELGGQQVTILNDADAAGLAETRYGAGKNNPGLVVLLTFGTGIGSAVIHNGTLIPNTEFGHLEVGGKEAEERAASSVKEKNDWTYPKWAKQVIRVLIAIENAIWPDLFIAGGGISRKADKWVPLLENRTPVVPAALQNTAGIVGAAMASVADTTH
|
Catalyzes the phosphorylation of glucose using polyphosphate or ATP as the phosphoryl donor. Polyphosphate, rather than ATP, seems to be the major phosphate donor for the enzyme in M.tuberculosis. GTP, UTP and CTP can replace ATP as phosphoryl donor.
|
A5U6Z7
|
DBH_MYCTA
|
DNA-binding protein HupB (HupB) (MtbHU) (EC 1.16.3.1) (DNA-binding protein HU homolog) (Histone-like protein)
|
MNKAELIDVLTQKLGSDRRQATAAVENVVDTIVRAVHKGDSVTITGFGVFEQRRRAARVARNPRTGETVKVKPTSVPAFRPGAQFKAVVSGAQRLPAEGPAVKRGVGASAAKKVAKKAPAKKATKAAKKAATKAPARKAATKAPAKKAATKAPAKKAVKATKSPAKKVTKAVKKTAVKASVRKAATKAPAKKAAAKRPATKAPAKKATARRGRK
|
A nucleoid-associated protein (NAP) that plays a role in local chromosome architecture (Probable). Binds DNA non-sequence specifically in vitro phosphorylation of an N-terminal fragment decreases DNA-binding. Stimulates supercoiling relaxation by topoisomerase 1 (Top1, topA), at higher than 80 uM inhibits relaxation, has no effect on DNA gyrase the effect is independent of DNA-binding. Increases the intervening strand passage activity of Top1 that occurs between the two catalytic trans-esterification reactions. Does not bind ssDNA, probably helps condense chromosomes. Binds dsDNA in vitro acetylated protein binds 10-fold less well to DNA (note in vitro acetylated protein is more heavily modified than in vivo modified protein). In vitro acetylated protein compacts DNA less well than unmodified protein. Has ferroxidase activity, converts Fe(2+) into Fe(3+). Binds Fe(3+) but not Fe(2+) prevents the generation of hydroxyl radicals by the Fenton reaction and thus protects DNA from damage. May function in iron storage.
|
A5U8S6
|
PAND_MYCTA
|
Aspartate 1-decarboxylase (EC 4.1.1.11) (Aspartate alpha-decarboxylase) [Cleaved into: Aspartate 1-decarboxylase beta chain; Aspartate 1-decarboxylase alpha chain]
|
MLRTMLKSKIHRATVTCADLHYVGSVTIDADLMDAADLLEGEQVTIVDIDNGARLVTYAITGERGSGVIGINGAAAHLVHPGDLVILIAYATMDDARARTYQPRIVFVDAYNKPIDMGHDPAFVPENAGELLDPRLGVG
|
Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. {ECO:0000255|HAMAP-Rule:MF_00446}. Overexpression of wild-type or mutant proteins confers resistance to pyrazinoic acid (POA), the active form of the anti-tuberculosis prodrug pyrazinamide (PZA), when grown on agar plates.
|
A5W059
|
HMGA_PSEP1
|
4-hydroxy-4-methyl-2-oxoglutarate aldolase/4-carboxy-4-hydroxy-2-oxoadipate aldolase (HMG/CHA aldolase) (EC 4.1.3.17) (Oxaloacetate decarboxylase) (OAA decarboxylase) (EC 4.1.1.112)
|
MNTLIGKTGIVVRNIQRAELDSIDALGRLGVATVHEAQNRKGLLSSKMRPIQQGTSLAGSAVTVLVAPGDNWMFHVAVEQCRPGDVLVVSPSSPCTDGYFGDLLATSLQARGVRALIVDAGVRDTQTLRDMGFAVWARAINAQGTVKETLGSVNLPVICGGQLINPGDIVVADDDGVVVVRRDECESTLVAAAERAGLEEEKRLRLAAGELGLDIYKMRERLEAKGLRYVDNIEDLEG
|
Catalyzes the last step of the bacterial protocatechuate 4,5-cleavage pathway. The preferred substrates of the enzyme are 2-keto-4-hydroxy acids with a 4-carboxylate substitution. Catalyzes the conversion of 4-hydroxy-4-methyl-2-oxoglutarate (HMG) to pyruvate. Also catalyzes the conversion of 4-carboxy-4-hydroxy-2-oxoadipic acid (CHA) to pyruvate and oxaloacetate.
|
A5WVX9
|
ZDH17_DANRE
|
Palmitoyltransferase ZDHHC17 (EC 2.3.1.225) (Acyltransferase ZDHHC17) (EC 2.3.1.-) (DHHC domain-containing cysteine-rich protein 17) (Zinc finger DHHC domain-containing protein 17)
|
MADALVGYEKEAGCVPILHPEEIKPQSHYNHGYNESRKSHVDDYSTWDIVKATQYGIFERCRELVEAGYDVRQPDKENVTLLHWAAINNRVDLVKYYISKGAIVDQLGGDLNSTPLHWATRQGHLSMVVQLMKYGADPSLIDGEGCSCVHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPLMWAAYRTHSVDPTRLLLTFNVSVNLGDKYHKNTALHWAVLAGNTTVISLLLEANANVDAQNIKGETPLDLAKQRKNVWMINHLQEARQAKGYDSPSYLKRLKMDKEFRQKVMLGTPFLVIWLVGFIADLDIDSWLIKGVMYAVMWLVVQFLSKSFFDHSMHSALPLGIYLATKFWMYITWFYWFWNDLPFVTIHLPFLLNSLALFYNFGKSWKSDPGIIKASEEQKKKTIVELAETGSLDLSIFCSTCLIRKPIRSKHCAVCNRCIAKFDHHCPWVGNCVGSGNHRYFMGYLFFLLCMICWMMYGCICYWRIHCATSYTKDGFWIYITQIATCSPWMFWMFLNSVFHFMWVAVLIMCQLYQIAVLGITTNERMNARRYKHFKVTATSIESPFNHGCMRNLIDFFELRCCGLLRPVPIDWTSQYTIEYDQTSGSGYQLV
|
Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates and is involved in a variety of cellular processes. Has no stringent fatty acid selectivity and in addition to palmitate can also transfer onto target proteins myristate from tetradecanoyl-CoA and stearate from octadecanoyl-CoA (By similarity). Plays a role in axonogenesis.
|
A5X5Y0
|
5HT3E_HUMAN
|
5-hydroxytryptamine receptor 3E (5-HT3-E) (5-HT3E) (Serotonin receptor 3E)
|
MEGSWFHRKRFSFYLLLGFLLQGRGVTFTINCSGFGQHGADPTALNSVFNRKPFRPVTNISVPTQVNISFAMSAILDVNEQLHLLSSFLWLEMVWDNPFISWNPEECEGITKMSMAAKNLWLPDIFIIELMDVDKTPKGLTAYVSNEGRIRYKKPMKVDSICNLDIFYFPFDQQNCTLTFSSFLYTVDSMLLDMEKEVWEITDASRNILQTHGEWELLGLSKATAKLSRGGNLYDQIVFYVAIRRRPSLYVINLLVPSGFLVAIDALSFYLPVKSGNRVPFKITLLLGYNVFLLMMSDLLPTSGTPLIGVYFALCLSLMVGSLLETIFITHLLHVATTQPPPLPRWLHSLLLHCNSPGRCCPTAPQKENKGPGLTPTHLPGVKEPEVSAGQMPGPAEAELTGGSEWTRAQREHEAQKQHSVELWLQFSHAMDAMLFRLYLLFMASSIITVICLWNT
|
This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. This receptor is a ligand-gated ion channel, which when activated causes fast, depolarizing responses. It is a cation-specific, but otherwise relatively nonselective, ion channel.
|
A5Y5L5
|
CIN_NICSU
|
1,8-cineol synthase, chloroplastic (EC 4.2.3.108) ((E)-beta-ocimene synthase) (EC 4.2.3.106) (Alpha-pinene synthase) (EC 4.2.3.-) (Alpha-terpineol synthase) (EC 4.2.3.111) (Beta-myrcene synthase) (EC 4.2.3.15) (Limonene synthase) (EC 4.2.3.-) (Sabinene synthase) (EC 4.2.3.-)
|
MNHHLIITPIFHLQIMLPVATLKRPPPPAATCSIYSFSRGTPSLVSKARLSTAAVGGMKNEPSPNHYSDISSSDLNLTRRSGNYGPTMWDFEYIQSIHNDYTEKKYMNRLNKLKEEMKKMIMAEGSQELEKLELIDNLQRLGVSYHFKHEIMQILSSIKQHSTPADSLYATALKFRLFREYGFHISQEIFGGLSETHTEDTKGMLYLYEASFLATEGESELEKARNWTEKHLREYLENKNDDQNVAELVHHALELPLHWRMLRIEARWFINFYKKKQDMIPLLLELAILDFNIVQAAHIEDLKYVARWWKETCLAENLPFARDRLVENFFWTIGVNFLPQYGYFRRIETKVNALVTTIDDVYDVFGTMDELQCFTHAFQRWNIDELDNLPDNMKMCYFALDNFINEVAGDAFEEHRVPILSYLRNAWTDLCKAYLREAKWYFSKYIPTMEEYMDNAWISISAPVILVHAYFLVANPVNKEVLHYLENYHDIIRWSALILRLANDLGTSSEELKRGDVPKSIQCYMNEKKVSEEEARQHIRLLISETWKKLNEAHNVAAHPFPKMFVKCAMNLARMAQCMYQHGDGHGHGDLNSETTNHIMALLFESIPPA
|
Monoterpene synthase involved in the biosynthesis of monoterpene natural products of the 'cineole cassette', volatile compounds present in floral scent. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into 1,8-cineole and, as minor products, limonene, sabinene, (E)-beta-ocimene, beta-myrcene, alpha-pinene and alpha-terpineol.
|
A5YKK6
|
CNOT1_HUMAN
|
CCR4-NOT transcription complex subunit 1 (CCR4-associated factor 1) (Negative regulator of transcription subunit 1 homolog) (NOT1H) (hNOT1)
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MNLDSLSLALSQISYLVDNLTKKNYRASQQEIQHIVNRHGPEADRHLLRCLFSHVDFSGDGKSSGKDFHQTQFLIQECALLITKPNFISTLSYAIDNPLHYQKSLKPAPHLFAQLSKVLKLSKVQEVIFGLALLNSSSSDLRGFAAQFIKQKLPDLLRSYIDADVSGNQEGGFQDIAIEVLHLLLSHLLFGQKGAFGVGQEQIDAFLKTLRRDFPQERCPVVLAPLLYPEKRDILMDRILPDSGGVAKTMMESSLADFMQEVGYGFCASIEECRNIIVQFGVREVTAAQVARVLGMMARTHSGLTDGIPLQSISAPGSGIWSDGKDKSDGAQAHTWNVEVLIDVLKELNPSLNFKEVTYELDHPGFQIRDSKGLHNVVYGIQRGLGMEVFPVDLIYRPWKHAEGQLSFIQHSLINPEIFCFADYPCHTVATDILKAPPEDDNREIATWKSLDLIESLLRLAEVGQYEQVKQLFSFPIKHCPDMLVLALLQINTSWHTLRHELISTLMPIFLGNHPNSAIILHYAWHGQGQSPSIRQLIMHAMAEWYMRGEQYDQAKLSRILDVAQDLKALSMLLNGTPFAFVIDLAALASRREYLKLDKWLTDKIREHGEPFIQACMTFLKRRCPSILGGLAPEKDQPKSAQLPPETLATMLACLQACAGSVSQELSETILTMVANCSNVMNKARQPPPGVMPKGRPPSASSLDAISPVQIDPLAGMTSLSIGGSAAPHTQSMQGFPPNLGSAFSTPQSPAKAFPPLSTPNQTTAFSGIGGLSSQLPVGGLGTGSLTGIGTGALGLPAVNNDPFVQRKLGTSGLNQPTFQQSKMKPSDLSQVWPEANQHFSKEIDDEANSYFQRIYNHPPHPTMSVDEVLEMLQRFKDSTIKREREVFNCMLRNLFEEYRFFPQYPDKELHITACLFGGIIEKGLVTYMALGLALRYVLEALRKPFGSKMYYFGIAALDRFKNRLKDYPQYCQHLASISHFMQFPHHLQEYIEYGQQSRDPPVKMQGSITTPGSIALAQAQAQAQVPAKAPLAGQVSTMVTTSTTTTVAKTVTVTRPTGVSFKKDVPPSINTTNIDTLLVATDQTERIVEPPENIQEKIAFIFNNLSQSNMTQKVEELKETVKEEFMPWVSQYLVMKRVSIEPNFHSLYSNFLDTLKNPEFNKMVLNETYRNIKVLLTSDKAAANFSDRSLLKNLGHWLGMITLAKNKPILHTDLDVKSLLLEAYVKGQQELLYVVPFVAKVLESSIRSVVFRPPNPWTMAIMNVLAELHQEHDLKLNLKFEIEVLCKNLALDINELKPGNLLKDKDRLKNLDEQLSAPKKDVKQPEELPPITTTTTSTTPATNTTCTATVPPQPQYSYHDINVYSLAGLAPHITLNPTIPLFQAHPQLKQCVRQAIERAVQELVHPVVDRSIKIAMTTCEQIVRKDFALDSEESRMRIAAHHMMRNLTAGMAMITCREPLLMSISTNLKNSFASALRTASPQQREMMDQAAAQLAQDNCELACCFIQKTAVEKAGPEMDKRLATEFELRKHARQEGRRYCDPVVLTYQAERMPEQIRLKVGGVDPKQLAVYEEFARNVPGFLPTNDLSQPTGFLAQPMKQAWATDDVAQIYDKCITELEQHLHAIPPTLAMNPQAQALRSLLEVVVLSRNSRDAIAALGLLQKAVEGLLDATSGADADLLLRYRECHLLVLKALQDGRAYGSPWCNKQITRCLIECRDEYKYNVEAVELLIRNHLVNMQQYDLHLAQSMENGLNYMAVAFAMQLVKILLVDERSVAHVTEADLFHTIETLMRINAHSRGNAPEGLPQLMEVVRSNYEAMIDRAHGGPNFMMHSGISQASEYDDPPGLREKAEYLLREWVNLYHSAAAGRDSTKAFSAFVGQMHQQGILKTDDLITRFFRLCTEMCVEISYRAQAEQQHNPAANPTMIRAKCYHNLDAFVRLIALLVKHSGEATNTVTKINLLNKVLGIVVGVLLQDHDVRQSEFQQLPYHRIFIMLLLELNAPEHVLETINFQTLTAFCNTFHILRPTKAPGFVYAWLELISHRIFIARMLAHTPQQKGWPMYAQLLIDLFKYLAPFLRNVELTKPMQILYKGTLRVLLVLLHDFPEFLCDYHYGFCDVIPPNCIQLRNLILSAFPRNMRLPDPFTPNLKVDMLSEINIAPRILTNFTGVMPPQFKKDLDSYLKTRSPVTFLSDLRSNLQVSNEPGNRYNLQLINALVLYVGTQAIAHIHNKGSTPSMSTITHSAHMDIFQNLAVDLDTEGRYLFLNAIANQLRYPNSHTHYFSCTMLYLFAEANTEAIQEQITRVLLERLIVNRPHPWGLLITFIELIKNPAFKFWNHEFVHCAPEIEKLFQSVAQCCMGQKQAQQVMEGTGAS
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Scaffolding component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Its scaffolding function implies its interaction with the catalytic complex module and diverse RNA-binding proteins mediating the complex recruitment to selected mRNA 3'UTRs. Involved in degradation of AU-rich element (ARE)-containing mRNAs probably via association with ZFP36. Mediates the recruitment of the CCR4-NOT complex to miRNA targets and to the RISC complex via association with TNRC6A, TNRC6B or TNRC6C. Acts as a transcriptional repressor. Represses the ligand-dependent transcriptional activation by nuclear receptors. Involved in the maintenance of embryonic stem (ES) cell identity.
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A5YM72
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CRNS1_HUMAN
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Carnosine synthase 1 (EC 6.3.2.11) (ATP-grasp domain-containing protein 1)
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MLLCLSPAWLMKVPAPGQPGEAALLVSKAVSFHPGGLTFLDDFVPPRRATYFLAGLGLGPGRGREAAELARDLTCPTGASAELARLLEDRLLTRQLLAQQGGVAVPATLAFTYKPPGLLRGGDASLGLRLVELSGKEGQETLVKEEVEAFLRSEALGDILQVAVKLSGWRWRGRQAWRLHPRAELGAVVDTVLALLEKLEEEESVLVEAVYPPAQLPCSDGPSPGPGLAVRICAVVCRTQGDRPLLSKVVCGVGRGDRPLRHHNSLPRTLEVALAQCGLGEEAQVAAVRQRVKAAAEAALAAVLALEAGLSAEQRGGRRAHTDFLGVDFALTAAGGVLTPVALELNGGLCLEACGALEGLWAAPRLGPAADEAVAAPLVETMLRRSARCLMEGKQLLVVGAGGVSKKFVWEAARDYGLQLHLVESDPNHFASQLVQTFIHFDMTEHRRDEENARLLAELVRARGLKLDGCFSYWDDCLVLTALLCQELGLPCSSPAAMRLAKQKSLTQLHLLHHHGPPWPAPSLHAVPCCPLESEADVERAVHQVPLPGVMKLEFGAGAVGVRLVEDAPQCHEHFSRITRDLQGEADHPGIGLGWGNAMLLMEFVEGTEHDVDLVLFGGRLLAAFVSDNGPTRLPGFTETAACMPTGLAPEQEAQMVQAAFRCCLGCGLLDGVFNVELKLTGAGPRLIEINPRMGGFYLRDWILELYGVDLLLAAVMVACGLRPALPTRPRARGHLVGVMCLVSQHLQALSSTASRETLQALHDRGLLRLNLLEEALVPGEYEEPYCSVACAGPSPTEARLRLLGLCQGLGIDGPSYPVAHFLSHFK
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Catalyzes the synthesis of carnosine and homocarnosine. Carnosine is synthesized more efficiently than homocarnosine.
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A5YVK8
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ERVA_TABDI
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Ervatamin-A (ERV-A) (EC 3.4.22.-)
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AVIPLKNQGKCGSCWAFSTVTTVESINQIRTGNLISLSEQQLVDCSKKNHGCKGGYFDRAYQYIIANGGIDTEANYPYKAFQGPCRAAKKVVRIDGCKGVPQCNENALKNAVASQPSVVAIDASSKQFQHYKSGIFTGPCGTKLNHGVVIVGYGKDYWIVRNSWGRHWGEQGYTRMKRVGGCGL
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Cysteine proteinase.
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A5Z1X6
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ITB1_CAMBA
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Integrin beta-1 (Fibronectin receptor subunit beta) (VLA-4 subunit beta) (CD antigen CD29)
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MNLQLIFWIGLISSVCCVFGQADEDRCLKANAKSCGECIQAGPNCGWCTNSTFLQEGMPTSARCDDLEALKKKGCHPNDTENPRGSKDIKKNKNVTNRSKGTAEKLQPEDITQIQPQQLVLQLRSGEPQTFTLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTDLMNEMRRITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTNEQNCTSPFSYKNVLSLTDKGEVFNELVGKQRISGNLDSPEGGFDAIMQVAVCGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQCHLKNDVYTMSHYYDYPSIAHLVQKLSENNIQTIFAVTEEFQPVYKELKNLIPKSAVGTLSANSSNVIQLIIDAYNSLSSEVILENSKLPEGVTINYKSYCKNGVNGTGENGRKCSNISIGDEVQFEISITANKCPDKNSETIKIKPLGFTEEVEIILQFICECECQGEGIPGSPKCHDGNGTFECGACRCNEGRVGRHCECSTDEVNSEDMDAYCRKENSSEICSNNGECVCGQCVCRKRDNTNEIYSGKFCECDNFNCDRSNGLICGGNGVCKCRVCECNPNYTGSACDCSLDTTSCMAVNGQICNGRGVCECGACKCTDPKFQGPTCEMCQTCLGVCAEHKECVQCRAFNKGEKKDTCAQECSHFNITKVENRDKLPQPGQVDPLSHCKEKDVDDCWFYFTYSVNGNNEATVHVVETPECPTGPDIIPIVAGVVAGIVLIGLALLLIWKLLMIIHDRREFAKFEKERMNAKWDTGENPIYKSAVTTVVNPKYEGK
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Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha-10/beta-1, alpha-11/beta-1 and alpha-V/beta-1 are receptors for fibronectin. Alpha-4/beta-1 recognizes one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. Integrin alpha-5/beta-1 is a receptor for fibrinogen. Integrin alpha-1/beta-1, alpha-2/beta-1, alpha-6/beta-1 and alpha-7/beta-1 are receptors for lamimin. Integrin alpha-6/beta-1 (ITGA6:ITGB1) is present in oocytes and is involved in sperm-egg fusion. Integrin alpha-4/beta-1 is a receptor for VCAM1 and recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-9/beta-1 is a receptor for VCAM1, cytotactin and osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in cytotactin. Integrin alpha-3/beta-1 is a receptor for epiligrin, thrombospondin and CSPG4. Integrin alpha-3/beta-1 provides a docking site for FAP (seprase) at invadopodia plasma membranes in a collagen-dependent manner and hence may participate in the adhesion, formation of invadopodia and matrix degradation processes, promoting cell invasion. Alpha-3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of endothelial cells migration. Integrin alpha-V/beta-1 is a receptor for vitronectin. Beta-1 integrins recognize the sequence R-G-D in a wide array of ligands. When associated with alpha-7/beta-1 integrin, regulates cell adhesion and laminin matrix deposition. Involved in promoting endothelial cell motility and angiogenesis. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process and the formation of mineralized bone nodules. May be involved in up-regulation of the activity of kinases such as PKC via binding to KRT1. Together with KRT1 and RACK1, serves as a platform for SRC activation or inactivation. Plays a mechanistic adhesive role during telophase, required for the successful completion of cytokinesis (By similarity). ITGA4:ITGB1 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling. ITGA4:ITGB1 and ITGA5:ITGB1 bind to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1. ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1. ITGA5:ITGB1 is a receptor for IL1B and binding is essential for IL1B signaling (By similarity). ITGA5:ITGB3 is a receptor for soluble CD40LG and is required for CD40/CD40LG signaling (By similarity). Plays an important role in myoblast differentiation and fusion during skeletal myogenesis (By similarity).
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A6BM07
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I7GT1_SOYBN
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Isoflavone 7-O-glucosyltransferase 1 (EC 2.4.1.170) (UDP-glucose:isoflavone 7-O-glucosyltransferase)
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MKDTIVLYPNLGRGHLVSMVELGKLILTHHPSLSITILILTPPTTPSTTTTTLACDSNAQYIATVTATTPSITFHRVPLAALPFNTPFLPPHLLSLELTRHSTQNIAVALQTLAKASNLKAIVIDFMNFNDPKALTENLNNNVPTYFYYTSGASTLALLLYYPTIHPTLIEKKDTDQPLQIQIPGLSTITADDFPNECKDPLSYACQVFLQIAETMMGGAGIIVNTFEAIEEEAIRALSEDATVPPPLFCVGPVISAPYGEEDKGCLSWLNLQPSQSVVLLCFGSMGRFSRAQLKEIAIGLEKSEQRFLWVVRTELGGADDSAEELSLDELLPEGFLERTKEKGMVVRDWAPQAAILSHDSVGGFVTHCGWNSVLEAVCEGVPMVAWPLYAEQKMNRMVMVKEMKVALAVNENKDGFVSSTELGDRVRELMESDKGKEIRQRIFKMKMSAAEAMAEGGTSRASLDKLAKLWKQS
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Involved in the biosynthesis of isoflavonoids. Specific for UDP-glucose. Can use genistein > daidzein > formononetin > quercetin > kaempferol > 4,2',4',6'-tetrahydroxychalcone > apigenin > aureusidin > esculetin > naringenin as substrates, but not cyanidin, trans-p-coumaric acid, caffeic acid, benzoic acid, m- and p-hydroxybenzoic acids, salicylic acid, salicyl alcohol, and hydroquinone.
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A6BM72
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MEG11_HUMAN
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Multiple epidermal growth factor-like domains protein 11 (Multiple EGF-like domains protein 11)
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MVLSLTGLIAFSFLQATLALNPEDPNVCSHWESYAVTVQESYAHPFDQIYYTRCTDILNWFKCTRHRISYKTAYRRGLRTMYRRRSQCCPGYYESGDFCIPLCTEECVHGRCVSPDTCHCEPGWGGPDCSSGCDSDHWGPHCSNRCQCQNGALCNPITGACVCAAGFRGWRCEELCAPGTHGKGCQLPCQCRHGASCDPRAGECLCAPGYTGVYCEELCPPGSHGAHCELRCPCQNGGTCHHITGECACPPGWTGAVCAQPCPPGTFGQNCSQDCPCHHGGQCDHVTGQCHCTAGYMGDRCQEECPFGSFGFQCSQHCDCHNGGQCSPTTGACECEPGYKGPRCQERLCPEGLHGPGCTLPCPCDADNTISCHPVTGACTCQPGWSGHHCNESCPVGYYGDGCQLPCTCQNGADCHSITGGCTCAPGFMGEVCAVSCAAGTYGPNCSSICSCNNGGTCSPVDGSCTCKEGWQGLDCTLPCPSGTWGLNCNESCTCANGAACSPIDGSCSCTPGWLGDTCELPCPDGTFGLNCSEHCDCSHADGCDPVTGHCCCLAGWTGIRCDSTCPPGRWGPNCSVSCSCENGGSCSPEDGSCECAPGFRGPLCQRICPPGFYGHGCAQPCPLCVHSSRPCHHISGICECLPGFSGALCNQVCAGGYFGQDCAQLCSCANNGTCSPIDGSCQCFPGWIGKDCSQACPPGFWGPACFHACSCHNGASCSAEDGACHCTPGWTGLFCTQRCPAAFFGKDCGRVCQCQNGASCDHISGKCTCRTGFTGQHCEQRCAPGTFGYGCQQLCECMNNSTCDHVTGTCYCSPGFKGIRCDQAALMMEELNPYTKISPALGAERHSVGAVTGIMLLLFLIVVLLGLFAWHRRRQKEKGRDLAPRVSYTPAMRMTSTDYSLSGACGMDRRQNTYIMDKGFKDYMKESVCSSSTCSLNSSENPYATIKDPPILTCKLPESSYVEMKSPVHMGSPYTDVPSLSTSNKNIYEVEPTVSVVQEGCGHNSSYIQNAYDLPRNSHIPGHYDLLPVRQSPANGPSQDKQS
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May regulate the mosaic spacing of specific neuron subtypes in the retina through homotypic retinal neuron repulsion. Mosaics provide a mechanism to distribute each cell type evenly across the retina, ensuring that all parts of the visual field have access to a full set of processing elements (By similarity).
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A6BMK7
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NEUR1_BOVIN
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Sialidase-1 (EC 3.2.1.18) (Acetylneuraminyl hydrolase) (Lysosomal sialidase) (N-acetyl-alpha-neuraminidase 1)
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MTEEGPGIVSLGKLRRPRMLRLWGICRVQIFSAIFMLMSPAGVGAGAKDDFSLVHPLVTMEQLLWVSGKQIGSVDTFRIPLITTTPRGTLLAFAEARKMSTSDKGAKFIALRRSMDQGSTWSPTAFIVDDGETPDGLNLGAVVSDTTTGVVFLFYSLCAHKAGCQVASTMLVWSKDDGVSWSSPRNLSLDIGTEMFAPGPGSGIQKQREPRKGRLIVCGHGTLERDGVFCLLSDDHGVSWRYGGGVSGIPYGQPKRENDFNPDECQPYELPDGSVVINARNQNNYHCHCRIILRSYDACDTLRPRDVTFDTELVDPVVAAGAVATSSGIVFFSNPAHPEFRVNLTLRWSFSNGTSWRKETVQLWPGPSGYSSLTTLEGNVDGKDEAPQLYVLYEKGRNQYMESISLVKVSVYGTL
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Catalyzes the removal of sialic acid (N-acetylneuraminic acid) moieties from glycoproteins and glycolipids. To be active, it is strictly dependent on its presence in the multienzyme complex. Appears to have a preference for alpha 2-3 and alpha 2-6 sialyl linkage (By similarity).
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A6H5Y3
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METH_MOUSE
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Methionine synthase (MS) (EC 2.1.1.13) (5-methyltetrahydrofolate--homocysteine methyltransferase) (Cobalamin-dependent methionine synthase) (Vitamin-B12 dependent methionine synthase)
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MKKTLQDEIEAILRKRIMVLDGGMGTMIQRYKLSEEHFQGQEFKDHSRPLKGNNDILSITQPDIIYQIHKEYLLAGADIIETNTFSSTSIAQADYGLEHLAYRMNKCSADVARKAAEEITLQTGVKRFVAGALGPTNKTLSVSPSVERPDYRNITFDELVDAYQEQAKGLLDGRVDILLIETIFDTANAKAALFAIQNLFEENYAPPRPIFISGTIVDKSGRTLSGQTGEAFVTSVSHSDPLCIGLNCSLGAAEMRPFIETIGKCTTAYVLCYPNAGLPNTFGDYDETPSTMATHLKDFAVDGLVNIVGGCCGSTPDHIREIAEAVKKCKPRVPPASVFEGHMLLSGLEPFRIGPYTNFVNIGERCNVAGSRKFAKLIMAGNYEEALSIAKAQVEMGAQVLDINMDDGMLDGPSAMTRFCNSIASEPDIAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEGDFLEKARKIKKFGAAVVVMAFDEEGQATETDVKVNVCTRAYHLLVDKVGFNPNDIIFDPNILTIGTGMEEHNLYAINFIHATRVIKETLPGVRISGGLSNLSFSFRGMEAIREAMHGVFLYHAIKFGMDMGIVNAGNLPVYDAIHKDLLQLCEDLIWNKDSEATEKLLRYAQTHGTGGKKVIQTDEWRNGSIEERLEYALVKGIEKHIVEDTEEARLNGEKYPRPLNIIEGPLMNGMKVVGDLFGAGKMFLPQVIKSARVMKKAVGHLIPFMEKEREEARLINGSVEEEDPYQGTIVLATVKGDVHDIGKNIVGVVLACNNFRVIDLGVMTPCDKILQAALDHKADIIGLSGLITPSLDEMIFVAKEMERLAIKIPLLIGGATTSRTHTAVKIAPRYSAPVIHVLDASKSVVVCSQLLDENLRDDYFEEILEEYEDIRQDHYESLKERKYVPLSQARKHGFHIDWLSEPHPVKPTFIGTQVFEDYNLQKLVDYIDWKPFFDVWQLRGKYPNRGFPKIFNDKAVGEEARKVYNDAQNMLNILISQKKLQARGVVGFWPAQSVQDDIHLYAEGVVPQAAEPIATFYGLRQQAEKDSSSTDPYHCLSDFIAPLHSGVCDYLGLFAVACFGVEELSKTYEDDGDDYSSIMVKALGDRLAEAFAEELHERVRRELWAYSRSEQLGVPDLRRLRYEGIRPAPGYPSQPDHTEKLTMWRLASIEQATGIRLTESLAMAPASAVSGLYFSNVKAKYFAVGKISKDQTEDYALRKNMPVAEVEKWLGPILGYDTD
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Catalyzes the transfer of a methyl group from methylcob(III)alamin (MeCbl) to homocysteine, yielding enzyme-bound cob(I)alamin and methionine in the cytosol. MeCbl is an active form of cobalamin (vitamin B12) used as a cofactor for methionine biosynthesis. Cob(I)alamin form is regenerated to MeCbl by a transfer of a methyl group from 5-methyltetrahydrofolate. The processing of cobalamin in the cytosol occurs in a multiprotein complex composed of at least MMACHC, MMADHC, MTRR (methionine synthase reductase) and MTR which may contribute to shuttle safely and efficiently cobalamin towards MTR in order to produce methionine.
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A6H630
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ARMT1_MOUSE
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Damage-control phosphatase ARMT1 (EC 3.1.3.-) (Acidic residue methyltransferase 1) (Protein-glutamate O-methyltransferase) (EC 2.1.1.-) (Sugar phosphate phosphatase ARMT1)
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MAESPAFLSAKDEGSFAYLTIKDRTPQILTKVIDTLHRHKSEFFEKHGEEGIEAEKKAISLLSKLRNELQTDKPITPLVDKCVDTHIWNQYLEYQRSLLNEGDGEPRWFFSPWLFVECYMYRRIHEAIMQSPPIHDFDVFKESKEENFFESQGSIDALCSHLLQLKPVKGLREEQIQDEFFKLLQISLWGNKCDLSLSGGESSSQKANIINCLQDLKPFILINDTESLWALLSKLKKTVETPVVRVDIVLDNSGFELITDLVLADFLFSSELATEIHFHGKSIPWFVSDVTEHDFNWIVEHMKSSNLESMSTCGACWEAYARMGRWAYHDHAFWTLPHPYCVMPQVAPDLYAELQKAHLILFKGDLNYRKLMGDRKWKFTFPFHQALSGFHPAPLCSIRTLKCELQVGLQPGQAEQLTASDPHWLTTGRYGILQFDGPL
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Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate (By similarity). Its preference for fructose-1-phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-control function in hexose phosphate metabolism (By similarity). Has also been shown to have O-methyltransferase activity that methylates glutamate residues of target proteins to form gamma-glutamyl methyl ester residues (By similarity). Possibly methylates PCNA, suggesting it is involved in the DNA damage response (By similarity).
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A6H639
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DRC5_MOUSE
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Dynein regulatory complex subunit 5 (T-complex-associated testis-expressed protein 1) (Tcte-1)
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MQETPSVPSNSSSHSQSVLTIQRQVSALGSSSTGPTSLKTSSTPTPGQLKTKVPNVRRMRRIISEDAEWSLAIVPLLTELCIQHIVKNFQNNPILKQLPLEHQKKVLSNLPPELPLTVTANLIDDENYWHRCCIKRWSVCHVSRHGGSWKRMFFERHLENLLKLFIPGTTDPNVILDLLPLCRNYVRRIHVDQFLPPVRMPTPLQGEEQSDSGSEGEGSEPEKDHYQLQTLVGGLKHLEELDLVYGVKDCGMNFEWNLFLFTYRDCYSLAATIKACHTLKIFKLTRSKVDDDKARILIRSLLDHPALEELDLSHNLIGDRGARAAAKLLSHSRLRVLNLANNQLQAPGAQSLAHALAHNTNLVFLNLRLNCIEDEGGQAIAHALETNKCLSVLHLGGNKLSEPTATLLSQMLTVNTTLVSLNLSCNHIGQDGGKQLLEGISDNKTILEFDLRLSDVSQESEYLIGQVLHANREAARQRTLNPGHFSSPTNNCTENSVV
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Component of the nexin-dynein regulatory complex (N-DRC) a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. May play a role in the assembly of N-DRC (By similarity). Required for sperm motility.
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A6H687
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SAC31_MOUSE
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SAC3 domain-containing protein 1 (SAC3 homology domain-containing protein 1)
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MGRFKGENRSQARWIMGGVSKGRGSGKSRKPRQAAFGQTGARVCPSSPQQDAVPRFRWPGDAECASSTHTPTMSGCKLPMGLCPDMCPAAERARRERERRLHRLEVEPGGRGNAPRADPKRTVKEYSRPAAGKPRPPPSLLRPPPVLLATVRYLAGEVAGRGDVSCAEVASFVADRLRAVRLDLSLQGVDDADAATVLEAALATLLAVVARVRPEETRGAADPVLLQTQVQEGFGSLRRCYARGKGPYPRQAAFQGLFLLYNLGSVEALQEVLQLPAALRACPPLQAALAVDAAFREDNHARLFRLLRTLPYLQSCAVQEHIGYARRKALARLSRALSTPKGQTLPLDFIEHFLALDGLQEARDLCQAHGLTLDKDRVVFLRGQYSEEGLPPPGAYHILVGNKLQGHTLEDVVMAEEGDIHRPGSAA
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Involved in centrosome duplication and mitotic progression.
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A6H6A9
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RBG1L_MOUSE
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Rab GTPase-activating protein 1-like
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MEVRASFQKVSGSSDSVATLNSEEFVLVSQHTDATSIKDDGKPQLKIASNGDEQLEKAMEEILRDSEKGQSGLPVDCQGSSEISDCPFGDVPASQTTKPPLQLILDPSNTEISTPRPSSPSRFPEEDSVLFNKLTYLGCMKVSSPRSEVEALRAMATMRASSQYPFAVTLYVPNVPEGSVRIIDQSSNVEIASFPIYKVLFCARGHDGTAESNCFAFTESSHGSEEFQIHVFSCEIKEAVSRILYSFCTAFKRSSRQVSDVKDSVIPTPDSDVFTFSVSLEVKEDDGKGNFSPVPKDRDKFYFKIKQGIEKKVVITVQQLSNKELAIERCFGMLLSPGRNVKNSDMHLLDMESMGKSYDGRAYVITGMWNPNAPIFLALNEETPKDKRVYMTVAVDMVVTEVVEPVRFLLETVVRVYPANERFWYFSRKTFTETFFMRLKQSEGKGHSSAGDAIYEVVSLQRESDKEEPITPTSAGGPMSPQEDEAEEESDNELSSGTGDVSKDCPEKILYSWGELLGRWHNNLGGRPKGLFTLVKSGVPEALRAEVWQLLAGCHDNQEMLDKYRILITKDSAQESVITRDIHRTFPAHDYFKDTGGDGQESLYKICKAYSVFDEDIGYCQGQSFLAAVLLLHMPEEQAFCVLVTIMYGYKLRDLYRNNFEDLHCKFYQLEKLMQEQLPDLYSHFCDLNLEAHMYASQWFLTLFTAKFPLCMVFHIIDLLLCEGLNIIFHVALALLKTSKEDLLQADFEGALKFFRVQLPKRYRAEENARRLMEQACNIKVPTKKLKKYEKEYQAMRENQLQQEDPMDRYKFVYL
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GTP-hydrolysis activating protein (GAP) for small GTPase RAB22A, converting active RAB22A-GTP to the inactive form RAB22A-GDP (By similarity). Plays a role in endocytosis and intracellular protein transport. Recruited by ANK2 to phosphatidylinositol 3-phosphate (PI3P)-positive early endosomes, where it inactivates RAB22A, and promotes polarized trafficking to the leading edge of the migrating cells. Part of the ANK2/RABGAP1L complex which is required for the polarized recycling of fibronectin receptor ITGA5 ITGB1 to the plasma membrane that enables continuous directional cell migration.
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A6H6E2
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MMRN2_MOUSE
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Multimerin-2
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MIPTLLLGFGVYLSWGLLGSWAQDPGTKFSHLNRPGMPEGWRLGAEDTSRDPIRRNWCPYQKSRLVTFVAACKTEKFLVHSQQPCPQGAPDCQGVRVMYRVAQKPVYQVQQKVLISVDWRCCPGFQGPDCQDHNPTANPEPTEPSGKLQETWDSMDGFELGHPVPEFNEIKVPQEQQENLLQNLQNDAQSVEDGFPGSWEAPPSNLTDEMTEANLTEFEFPGRTSEHLLQPHIDAFLKAHFSPIWKNFNDSLHSLSQAIRNLSLDVEANHQAIKMIQEGTVARADFQELGAKFEAKVQQNSQRLGQLWQDVEDQLHAQRRSVHHALSDVQAEVSTKLKQLVKAQELPGANGSLVMASAAAAARPEPESLQARLGQLQRNLSALHMVTSQREEELQSTLKNMDSVLKQHAEEIKELYSESDETFDQISKVERQVEELLVNHTGLRELRVILMEKSLIMEENKEEIERQLLELNLTLQHLHAGHADLIKYVKDCNCQRVNSDVDVAPEGHRDVMHTLEETQVSLDEQHQLDGSSLQALQSTVDAMSSAMDAYRGEGERARAERARIRSQLRALDHAVEALKTAANGTRKEIRLLHGSFTALLEDALRHQAVLAALFGEEMIDEMSEEAPRPLPLDYEQIRLALQDAASGLQEQAIGWEDLATRVEALEKAAGGFVEQHPQLAEGLEPSHDSGREEEAMTLAELEQEIRRLSSDVKQIGQCCEASWAASLNSSLEDLHSMLLDTQHGLRQHRQLFHNLFQNFQGLVASNISLDLGKLQAMLSKKDKKQPRGPGESRKRDKKQVVMSTDAHAKGLELWETGSPVAFYAGSSEGATALQMVKFNTTSINVGSSYFPEHGYFRAPKRGVYLFAVSITFGPGPGMGQLVFEGHHRVPVYSTEQRGGSTATTFAMVELQKGERAWFELIQGSATKGSQPGTAFGGFLMFKT
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Inhibits endothelial cells motility and acts as a negative regulator of angiogenesis it down-regulates KDR activation by binding VEGFA.
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A6H730
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PPAP_BOVIN
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Prostatic acid phosphatase (EC 3.1.3.2) (Protein tyrosine phosphatase ACP3) (EC 3.1.3.48)
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MRNAALLMTRATSLRLSLLLLLSFLPDLDGGVRAKELRFVTLVFRHGDRSPIETFPNDPIKESSWPQGFGQLTQLGMAQHYELGQYIRKRYENFLNESYKREQVHVRSTDIDRTLMSAMTNLAALFPPEGISIWNPSLPWQPIPVHTVPVSEDQLLYLPFRNCPRFQELQSETLISEEFQKRLQPYKDFIEVLPKLTGYHDQDLLGIWSKVYDPLFCEGVHNFTLPSWATEDTMTKLKEISELSLLSLYGIHKQKEKSRLQGGVLINEILNHMKSATQPSNRRKLIMYSAHDTTVSGLQMALDVYNGILPPYASCHMMELYFQDGEYFVEMYYRNETRYEPHPLTLPGCTPSCPLAKFVELVAPVISQDWSMECAIRNHKGTEDIIN
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A non-specific tyrosine phosphatase that dephosphorylates a diverse number of substrates under acidic conditions (pH 4-6) including alkyl, aryl, and acyl orthophosphate monoesters and phosphorylated proteins. Has lipid phosphatase activity and inactivates lysophosphatidic acid in seminal plasma (By similarity).
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A6H737
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LOXL2_BOVIN
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Lysyl oxidase homolog 2 (EC 1.4.3.13) (Lysyl oxidase-like protein 2)
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MERRGSSCLCRCLALLALLPTLSLAQYESWRHYPEYFQEPAPEYHRPEVPSDVAKIQLRLAGQKRKHSEGRVEVYYDGQWGTVCDDDFTIHAAHVVCRELGYVEAKSWTASSSYGKGEGPIWLDNVYCTGSEATLAACSSNGWGVTDCKHTEDVGVVCSEKRIPGFKFDNSLINSIENMNIQVEDIRIRAILSAFRKRTPVTEGYVEVKEGKTWKQICDKHWTAKNSRVVCGMFGFPGEKTYNTKVYKMFAARKKQRYWPYSMDCTGTEAHISSCKLGPQVSLDPVKNVTCENGLPAVVSCVPGQVFSPDGPSRFRKAYKPEQPLVRLRGGANVGEGRVEVLKNGEWGTVCDDKWDLVSASVVCRELGFGSAKEAITGSRLGQGIGPIHLNEIECTGNEKSIIDCKFNAESQGCNHEEDAAVRCNIPAMGFQKKLRLNGGRNPYEGRVEVLVERNGSLVWGMVCGENWGIVEAMVVCRQLGLGFASNAFQETWYWHGNINANKVVMSGVKCSGTELSLAHCRHDGEDVACPEGGVRYGAGVACSETAPDLVLNAEIVQQSTYLEDRPMFMLQCAMEENCLSASAAQTNPTTGYRRLLRFSSQIHNNGQSDFRPKNGRHAWIWHDCHRHYHSMEVFTHYDLLNLNGTKVAEGHKASFCLEDTECEGDIQKSYECANFGEQGITMGCWDMYRHDIDCQWVDITDVPPGDYLFQVVINPNYEVAESDYTNNIMKCRTRYDGHRIWMYNCHIGGSFSEETEKKFEHFSGLINNQVSKR
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Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine). Acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation. Shows no activity against histone H3 when it is trimethylated on 'Lys-9' (H3K9me3) or 'Lys-27' (H3K27me3) or when 'Lys-4' is monomethylated (H3K4me1) or dimethylated (H3K4me2). Also mediates deamination of methylated TAF10, a member of the transcription factor IID (TFIID) complex, which induces release of TAF10 from promoters, leading to inhibition of TFIID-dependent transcription. LOXL2-mediated deamination of TAF10 results in transcriptional repression of genes required for embryonic stem cell pluripotency including POU5F1/OCT4, NANOG, KLF4 and SOX2. Involved in epithelial to mesenchymal transition (EMT) via interaction with SNAI1 and participates in repression of E-cadherin CDH1, probably by mediating deamination of histone H3. During EMT, involved with SNAI1 in negatively regulating pericentromeric heterochromatin transcription. SNAI1 recruits LOXL2 to pericentromeric regions to oxidize histone H3 and repress transcription which leads to release of heterochromatin component CBX5/HP1A, enabling chromatin reorganization and acquisition of mesenchymal traits. Interacts with the endoplasmic reticulum protein HSPA5 which activates the IRE1-XBP1 pathway of the unfolded protein response, leading to expression of several transcription factors involved in EMT and subsequent EMT induction. When secreted into the extracellular matrix, promotes cross-linking of extracellular matrix proteins by mediating oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. Acts as a regulator of sprouting angiogenesis, probably via collagen IV scaffolding. Acts as a regulator of chondrocyte differentiation, probably by regulating expression of factors that control chondrocyte differentiation.
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A6H772
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PP4C_BOVIN
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Serine/threonine-protein phosphatase 4 catalytic subunit (PP4C) (Pp4) (EC 3.1.3.16)
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MAEISDLDRQIEQLRRCELIKESEVKALCAKAREILVEESNVQRVDSPVTVCGDIHGQFYDLKELFRVGGDVPETNYLFMGDFVDRGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYGSVTVWRYCTEIFDYLSLSAIIDGKIFCVHGGLSPSIQTLDQIRTIDRKQEVPHDGPMCDLLWSDPEDTTGWGVSPRGAGYLFGSDVVAQFNAANDIDMICRAHQLVMEGYKWHFNETVLTVWSAPNYCYRCGNVAAILELDEHLQKDFIIFEAAPQETRGIPSKKPVADYFL
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Protein phosphatase that is involved in many processes such as microtubule organization at centrosomes, maturation of spliceosomal snRNPs, apoptosis, DNA repair, tumor necrosis factor (TNF)-alpha signaling, activation of c-Jun N-terminal kinase MAPK8, regulation of histone acetylation, DNA damage checkpoint signaling, NF-kappa-B activation and cell migration. The PPP4C-PPP4R1 PP4 complex may play a role in dephosphorylation and regulation of HDAC3. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically dephosphorylates H2AX phosphorylated on Ser-140 (gamma-H2AX) generated during DNA replication and required for DNA double strand break repair. Dephosphorylates NDEL1 at CDK1 phosphorylation sites and negatively regulates CDK1 activity in interphase. In response to DNA damage, catalyzes RPA2 dephosphorylation, an essential step for DNA repair since it allows the efficient RPA2-mediated recruitment of RAD51 to chromatin.
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A6H7G2
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DBNL_BOVIN
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Drebrin-like protein
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MAVNLSRNGPALLEAYQQVVNEKSSTDWALFTYEGNSNDIRVAGTGEGGLEEMVEELNSGKVMYAFCRVKDPNSGLPKFVLINWTGEGVNDVRKGACANHVSTMAGFLKGAHVTINARAEEDVEPECIMQKVARASGANYTFHKESSRFQDTGPQAPVGSVYQKTNAVSEIKRVGKDSFWAKAEKEEENRRLEEKRRAEEERQQLEQERRERELREAALREQRYQEQGGEAGLQRKYEQHEVLSRNREEQPAHPREIFKQKERAMSTTSISSPQPGKLKSPFLQKQLTQPDTPISRESPHATSRPRADLREEPVPSIPPCSVQVEEEAVYEEPPEQETFYEEPPAVQQQDASSEPIDHYPGLSGKGLCARALYDYQAADETEISFDPENLITGIEVIDEGWWRGYGPDGHFGMFPANYVELIE
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Adapter protein that binds F-actin and DNM1, and thereby plays a role in receptor-mediated endocytosis. Plays a role in the reorganization of the actin cytoskeleton, formation of cell projections, such as neurites, in neuron morphogenesis and synapse formation via its interaction with WASL and COBL. Does not bind G-actin and promote actin polymerization by itself. Required for the formation of organized podosome rosettes. May act as a common effector of antigen receptor-signaling pathways in leukocytes. Acts as a key component of the immunological synapse that regulates T-cell activation by bridging TCRs and the actin cytoskeleton to gene activation and endocytic processes (By similarity).
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A6H7I5
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DYN2_BOVIN
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Dynamin-2 (EC 3.6.5.5)
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MGNRGMEELIPLVNKLQDAFSSIGQSCHLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIFSKTEYAEFLHCKSRKFTDFEEVRQEIEAETDRVTGTNKGISPVPINLRIYSPHVLNLTLIDLPGITKVPVGDQPQDIEYQIKDMILQFISRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIEGKKDIRTALAAERKFFLSHPAYRHIADRMGTPHLQKTLNQQLTNHIRESLPALRSKLQSQLLSLEKEVEEYKNFRPDDPTRKTKALLQMVQQFGVDFEKRIEGSGDQVDTLELSGGARINRIFHERFPFELVKMEFDEKDLRREISYAIKNIHGVRTGLFTPDLAFEAIVKKQVVKLKEPCLKCVDLVIQELINTVRQCTSKLSSYPRLREETERIVTTYIREREGRTKDQILLLIDIEQSYINTNHEDFIGFANAQQRSTQLNKKRAVPNQVIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKDLRQIELACDSQEDVDSWKASFLRAGVYPEKDQAENEDGAQENTFSMDPQLERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHYELLAYLYSSADQSSLMEESADQAQRRDDMLRMYHALKEALNIIGDISTSTVSTPVPPPVDDTWIQNTSSHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPVPVGPASFSAPPIPSRPGPHPGVFANNDPFSAPPQIPSRPARIPPGIPPGVPSRRPPAAPSRPTIIRPAEPSLLD
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Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones (By similarity). Plays an important role in vesicular trafficking processes, in particular endocytosis. Involved in cytokinesis. Regulates maturation of apoptotic cell corpse-containing phagosomes by recruiting PIK3C3 to the phagosome membrane.
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A6H7J1
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INSM1_BOVIN
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Insulinoma-associated protein 1 (Zinc finger protein IA-1)
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MPRGFLVKRSKKSTPVSYRIRGGEDGDRALLLLPGCGGARASPPAPGPGPVPGPLQPPPPTERAHAALAAALACAPGPPPPPPGLRAAHFGNPEAAHPAPLYSPTRPVSREHEKHKYFERSFNLGSPVSAESFPTPAALLVGGGGGGGGGGANGAGGGGTCSGDPLLFAPAELKMGTAFSAAAEAARGPGPGPPLPPAAALRPPGKRPSPPASAAAAAEPPAKVAKAPGSKKPKAIRKLHFEDEVTTSPVLGLKIKEGPVEAPRGRAGGAARPLGEFICQLCKEEYADPFALAQHKCSRIVRVEYRCPECAKVFSCPANLASHRRWHKPRPAPAAARACEPETPARAEAREATGGGGSDRDTPSPGGVSESGSEDGLYECHHCAKKFRRQAYLRKHLLAHHQALQAKGAPPPAPPAEDLLALYPGPDEKVPQEAAGDGEAAGVLGLSASAECHLCPVCGETFPSKGAQERHLRLLHAAQVFPCKYCPATFYSSPGLTRHINKCHPSENRQVILLQVPVRPAC
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Sequence-specific DNA-binding transcriptional regulator that plays a key role in neurogenesis and neuroendocrine cell differentiation during embryonic and/or fetal development. Binds to the consensus sequence 5'-[TG][TC][TC][TT][GA]GGG[CG]A-3' in target promoters. Acts as a transcriptional repressor of NEUROD1 and INS expression via its interaction with cyclin CCND1 in a cell cycle-independent manner. Negatively regulates skeletal muscle-specific gene expression in endocrine cells of the pituitary by inhibiting the Notch signaling pathway. Represses target gene transcription by recruiting chromatin-modifying factors, such as HDAC1, HDAC2, HDAC3, KDM1A and RCOR1 histone deacetylases. Binds to its own promoter, suggesting autoregulation as a self-control feedback mechanism. Competes with histone H3 for the same binding site on the histone demethylase complex formed by KDM1A and RCOR1, and thereby inhibits demethylation of histone H3 at 'Lys-4'. Promotes the generation and expansion of neuronal basal progenitor cells in the developing neocortex. Involved in the differentiation of endocrine cells of the developing anterior pituitary gland, of the pancreas and intestine, and of sympatho-adrenal cells in the peripheral nervous system. Promotes cell cycle signaling arrest and inhibition of cellular proliferation.
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A6H8H2
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DEN4C_MOUSE
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DENN domain-containing protein 4C
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MIEDKGPRVTDYFVVAGLTDTSTLLDQEINRTDTNSIGPKAPITDIAVIIKSAGETVPEGYTCVEATPSALQANLNYGSLKSPELFLCYRRGRDKPPLTDIGVLYEGKERLMPGCEVIQATPYGRCANVNNSSTTSQRIFITYRRAPPVRSQNSLAVTDICVIITSKGETPPHTFCKVDKNLNCGMWGSNVFLCYKKSVPASNAIAYKAGLIFRYPEEDYESFPLSPSVPLFCLPMGATIECWDPQIKYPLPVFSTFVLTGSSAEKVYGAAIQFYEPYSQERLTEKQLTQLGLLTLVEKRVVSKPINSNKCICLLSHWPFFEAFKNFLMFIYKVSVSGPHPLPIEKHISHFMQNIPFPSPQRPRILIQLSVHDAFILSQPVSTPLPLSGANFSSLLMNLGPENCATLLLLVLLESKILLHSLRPAVLTGVAEAVVAMIFPFQWQCPYIPLCPLSLAGVLSAPLPFIVGVDSRYFDLHDPPQDVVCIDLDTNTLYVADERKNINWKQLPKRPCKSLLGTLRRLYQQLCSVHRKPQESSAIEMTPIEADYSWQKKMTQLEMEIQETFLRFMASILKGYRSYLRPITEAPSNKATAADSLFDRQGFLKSRDRAYTKFYTLLSKTQIFIRFIEECSFVSDKDTGLAFFDDCIEKLFPDKGVERTEKVDLDSAEDTRLIELDDSQRSEHTVFIMPPEPPPDDGNNLSPQYSYTYFPRLDLKLFDSPQKLKLCFNRHPPGSSITNSPALMAKRTKQEIKTAHKLAKRCYTNPPQWAKYLFSHCYSLWFICLPAYVRVSHPKVRALQQAHDVLVKMRKTDVDPLDEVCYRVVMQLCGLWVNPVLAVRVLFEMKTARIKPNAITYGYYNKVVLESPWPSSTRSGIFLWTKVRNVVHGLAQFRQPLKKTGQKSQVFSISGGQSDQGYGSKDELVKEGADGHAPEEHTPPELTTTELHIEEECDISAIVSKHLQPTPEPQSPTEPPAWGSSIVKVPSGLFDTNNRTSTGSTSTVLFSTQAPVEDAVFSEVTNFKKNGDRGEKKQKHFPERSCSFSSESRAGMLLKKSSLDLNSSEMAIMMGADAKILTAALTCPKTSPPHVTRTHSFENVNCHLADSRTRMSEGTRDSEHRSSPVLEMLEESQELLEPVVGDNVAETAAEMTCNSLQSNSHSDQSRDTQAGAQDPVNKRSSSYATRKAIEREDVETGLDPLSLLATECVEKTSDSEDKLFSPVISRNLADEIESYMNLKSPLGSKSCSMELHGEGNQEPGSPAVFAHPLERSSSLPSDRGPPARDSTETEKSSPAVSSSKTLTGRFKPQSPYRAYKDRSTSLSALVRSSPNSSLGSVVNSLSGLKLDNILSGPKIDVLKSSMKQAATVASKMWVAVASAYSYSDDEEETNKDYSFPAGLEDHHIVGETLSPNTSVSGLVPSELTQSNTSLGSSSSSGDVGKLQCPAGEVPFSRNIKGQDFEKSDHGSSQNTSMSSIYQNCAMEVLMSSCSQCRACGALVYDEEIMAGWTADDSNLNTTCPFCKSNFLPLLNVEFKDLRGSASFFLKPSTSGDSLQSGSIPSASEPSEHKPTSSSAEPDLISFMDFSKHSETITEEASYTVESSDEIKKTNGDVQSVKMSSVPNSLSKRNVSLTRSHSVGGPLQNIDFSQRPFHGVSTVSLPSSLQEDVDHLGKRPSPPPVSVPYLSPLVLRKELESLLENEGDQVIHTSSFINQHPIIFWNLVWYFRRLDLPSNLPGLILTSEHCNGGVQLPLSSLSQDSKLVYIQLLWDNINLHQEPGEPLYVSWRNLNSEKKPSLLSEQQQAASALVETIRQSIQQNDVLKPINLLSQQMKPGTKRQRSLYREILFLSLVSLGRENIDIEAFDNEYGLAYRSLPSESLERLQRIDAPPSISVEWCRKCFGAPLI
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Guanine nucleotide exchange factor (GEF) activating RAB10. Promotes the exchange of GDP to GTP, converting inactive GDP-bound RAB10 into its active GTP-bound form. Thereby, stimulates SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane in response to insulin.
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A6H8H5
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KCNB2_MOUSE
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Potassium voltage-gated channel subfamily B member 2 (Voltage-gated potassium channel subunit Kv2.2)
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MAEKAPPGLNRKTSRSTLSLPPEPVDIIRSKTCSRRVKINVGGLNHEVLWRTLDRLPRTRLGKLRDCNTHESLLEVCDDYNLNENEYFFDRHPGAFTSILNFYRTGKLHMMEEMCALSFGQELDYWGIDEIYLESCCQARYHQKKEQMNEELRREAETMREREGEEFDNTCCPEKRKKLWDLLEKPNSSVAAKILAIVSILFIVLSTIALSLNTLPELQENDEFGQPSDNRKLAHVEAVCIAWFTMEYLLRFLSSPNKWKFFKGPLNVIDLLAILPYYVTIFLTESNKSVLQFQNVRRVVQIFRIMRILRILKLARHSTGLQSLGFTLRRSYNELGLLILFLAMGIMIFSSLVFFAEKDEDATKFTSIPASFWWATITMTTVGYGDIYPKTLLGKIVGGLCCIAGVLVIALPIPIIVNNFSEFYKEQKRQEKAIKRREALERAKRNGSIVSMNLKDAFARSMELIDVAVEKAGESANTKDSVDDNHLSPSRWKWARKALSETSSNKSYENKYQEVSQNDSHEHLNNTSSSSPQHLSAQKLEMLYNEITKTQPHSHPNPDCQEQPERPCVYEEEIEMEEVICPQEQLAVAQTEVIVDMKSTSSIDSFTSCATDFTETERSPLPPPSASHLQMKFPTDLPGTDEHQRARAPPFLTLSRDKGPAAREAAVDYAPIDITVNLDAGASHGPLQPDSASDSPKSSLKGSNPLKSRSLKVNFQENRASAPQTPPSTARPLPVTTADFPLTTPQHMSTILLEEALPQGQPPLLEADDSAHCQGPSKGFSPRFPKQKLFPFSSRERRSFTEIDTGEDEDFLDLQRSRPDKQADPSPNCLADKPGDARDSLREEGCVGSSSPQNTDHNCRQDIYQAVGEVKKDSSQEGYKMENHLFAPEIHSNPGDTGHCPTRETSM
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Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain and smooth muscle cells. Channels open or close in response to the voltage difference across the membrane, letting potassium ions pass in accordance with their electrochemical gradient. Homotetrameric channels mediate a delayed-rectifier voltage-dependent outward potassium current that display rapid activation and slow inactivation in response to membrane depolarization. Can form functional homotetrameric and heterotetrameric channels that contain variable proportions of KCNB1 channel properties depend on the type of alpha subunits that are part of the channel. Can also form functional heterotetrameric channels with other alpha subunits that are non-conducting when expressed alone, such as KCNS1 and KCNS2, creating a functionally diverse range of channel complexes. In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Contributes to the delayed-rectifier voltage-gated potassium current in cortical pyramidal neurons and smooth muscle cells.
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A6H8Y1
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BDP1_HUMAN
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Transcription factor TFIIIB component B'' homolog (Transcription factor IIIB 150) (TFIIIB150) (Transcription factor-like nuclear regulator)
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MFRRARLSVKPNVRPGVGARGSTASNPQRGRESPRPPDPATDSASKPAEPTDVPTVDFGGAEPQEKAPRSSTEKTGGDNDVEESSRSSSTVSQRRKRISSTSSLVKSSVSVPSESHPLSTINQEAPQPTATSTKEKQPCSDRYRIYKAQKLREMLKEELRKEKKQWKNKYAINESQRPPDRSKMTMRDFIYYLPDNNPMTSSLEQEKKTEKPSTPVQTREQEGKSTPNAEDNEMEEETDDGPLLVPRVKVAEDGSIILDEESLTVEVLRTKGPCVVEENDPIFERGSTTTYSSFRKNYYSKPWSNKETDMFFLAISMVGTDFSMIGQLFPHRARIEIKNKFKREEKTNGWRIDKAFQEKRPFDFDFFAHLLQKVLAEEEKRKQKSVKNHSLKEKKSTKPRKNVKVKKVACEGVNNDPDESMSSRISDTERSQKDAQTVEEESLTLSREDAEQVALEVDLNQKKRRRKKQDGANELGVNNLLENATVQAGPSKGEKHKNKCQAIRPELKEGECSKEQMLSCTQNIDGIVGFASTEKVEKRTDPILSLSNQQDATSVATESSESSTSDLPSFEVGIRALCEVNNAEGSCIEERNVDLKNNSLEIDQTENVKPMLRGRFQRPKPNLSRAGKKSVLSQGKTESESKNSHSKTSVEKNHVEKDKMNTLDILRMETTERENPEAETVSVLGEKNCLQEGSQLKALRPVQVRGRLQKPKPNAGKAAERKEILISQEEIGANVEKNENESCADRDTPQHMEDQSRKDFEEEDVILQPEKNDSFQNVQPDEPKVLNECLSVQENNKANKLNQVPILRTRFQKPKPNIGRGTGRREISSKEEVLEKILVSGEMAAALRETVRLDTSPKEMVPAEINTKEMQSDLKETGRRAISPREKILDVIDDTIEMETGLKAMGREICLREKTPEVIDATEEIDKDLEEAGRREISPQKNGPEEVKPLGEVETDLKATGNESSPREKTPEVTDATEEIDKNLEETGRRKISPRENGPEEVKPVDEMETDLNATGRESSPREKTPEVIDATEEIDLEETEREVSPQENGLEEVKPLGEMETDLKATGRDSFPRGKTPEVIDAIEEIEIDLEETEREISPQENGLEEVKPLGEMQTDLKATGREISPREKTPEVIDATEEIDKDLEETGRREISPEENGPEEVKPVDEMETDLKTTGREGSSREKTREVIDAAEVIETDLEETEREISPQENGPEEVKPVGKMETDLKEIREEISQREKVLAEFSAIREKEIDLKETGKRDIPIMEKVSGKMAVVEEMEADLKETGKENFRERGSEEICVTEEKVAELKQTGKTDISPRENELEETSTSRQTDTHLMQSGSNDFSAVPSLDIQNISSEVLSMMHTPVEEKRNSEKEVSSHFSHFKISSQTHESDKTEVQGIQSPDVPEQFSDINLSKSLPQEQKPLEIKPAPFVRSRFKRPKPNLARAALKRETTESEKYIYEKKSETKKMETIVMQENNEQTDTLPSQHDEASLMISREKDTLGHRNEEAVILPCTQTERNLSPSNSCEPKEESQSAPVQKNDSVVSVGTNNVNTFQQEMKESVIQTARQVRGRLQRPRPNIRKTGQRQIVDKGEAKGIIKEGRTILPKDETEKKVLTVSNSQIETEIEVPSSAVPEHRMYENQSQVVLVENLHVNKTNETIRHENKPYVPSSAQMTRRKFQKAKPNLGRAHSKKEEPVLEKVTTDQSKEGKPEDHLLQKGASNTQLLLKEKAELLTSLEVSARKDCVGSKESALAKIDAELEEVGPSRRVGEETVGDNSPSSVVEEQYLNKLTSCPQPLNETSYSKIALDGKTTISSTSEYERNRGERRSHKKFKPNVTRGRGSKRVRGKTSKKEPRASKAMLVTLRASQEEDDDADDFESDYEEESYHLAPEEVNKAPVFVPVGLRSPEPVSAQIEETMEELEITVNVPDVGCIAVVEHELPNTDVTTEEMKQEENLSVPFEMTTSEHIQDEPGTNDGSTEAAITLLTMGDLVLQSEISSEQGDVGVCIIPHVHSKDKSHIPSSLDNVNHKIVHECQELSSPVITTSPASFEENKIVLEEQSSREEISLMEKVKENATPTRNTISKVTSNLRIRSRLAKPKPNLEKTLGTNRLDDYQEVSSLCVTKGAEMETQRETEKNASKATELENKNLGPVTTAENKDQSKLACVHGIKGTSISSEVNLTERNENQEESSQEVHMLSVAPVASSETGPCTLGLDRGLGENSVEEPQIKDSKGDSVLTLPVPEYTPTSIPEVQQENIINPQDLTVNLVANVPQDGEDEQAFILTLVEIPANAVEEFTDATAQFMPNPLLPAPILVKSVNTEERGDMSICLPATSVGQDAMGLSISGRDNSKKPPDNLDLVSRKRFQCRLDKNDHIPPAKKRSLTLRDDCQEYTTEVHSKELTNVFEETGESHKGQDIFLTSGSTLTTPEPQRQQVEAAFQSRGSRSPDACMDKNVPQLPQDEMIVSDKEERTDAAPKSQQMDSRTSSSKASLSRPGRRPLGFLSLICSKNSLESDEPMQVHSKKRLKPLIPGLRKKLKRSNPFNESQEKNRESSDLLPSPSVITTQSENISSSATQVSCDQPLLKEGYKSAQKRAPQGEATTVSEYFFNDIFIEVDETE
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General activator of RNA polymerase III transcription. Requires for transcription from all three types of polymerase III promoters. Requires for transcription of genes with internal promoter elements and with promoter elements upstream of the initiation site.
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A6M931
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IF4A3_PIG
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Eukaryotic initiation factor 4A-III (eIF-4A-III) (eIF4A-III) (EC 3.6.4.13) (ATP-dependent RNA helicase DDX48) (ATP-dependent RNA helicase eIF4A-3) (DEAD box protein 48) (Eukaryotic translation initiation factor 4A isoform 3) [Cleaved into: Eukaryotic initiation factor 4A-III, N-terminally processed]
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MAATATMATSGSARKRLLKEEDMTKVEFETSEEVDVTPTFDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILAPTRELAVQIQKGLLALGDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKEQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRILVKRDELTLEGIKQFFVAVEREEWKFDTLCDLYDTLTITQAVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINYDLPNNRELYIHRIGRSGRYGRKGVAINFVKNDDIRILRDIEQYYSTQIDEMPMNVADLI
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ATP-dependent RNA helicase. Involved in pre-mRNA splicing as component of the spliceosome. Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Its RNA-dependent ATPase and RNA-helicase activities are induced by CASC3, but abolished in presence of the MAGOH-RBM8A heterodimer, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The inhibition of ATPase activity by the MAGOH-RBM8A heterodimer increases the RNA-binding affinity of the EJC. Involved in translational enhancement of spliced mRNAs after formation of the 80S ribosome complex. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. Shows higher affinity for single-stranded RNA in an ATP-bound core EJC complex than after the ATP is hydrolyzed. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes) specifically inhibits formation of proapoptotic isoforms the function is different from the established EJC assembly. Involved in craniofacial development.
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A6M9B7
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GLCT_ECOLX
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O-antigen biosynthesis glycosyltransferase WclY (EC 2.4.1.-) (Alpha-1,4-glucosyltransferase) (Glucosyltransferase) (Glc-T) (Glycosyltransferase)
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MKIAYVVSSKKKCGPNIVILNIVKELANKHEMEIFFLDESDDDVFECVNVKSTQIKKASDLKEHLKRFDIIHSSGIRPDALVVLCKVIYRVKCKIITTIHNYVFQDLYYSYGLVKSLIGGLLWCSIWLFFDKLVILSKNADNYYWFLPSAKKNIIYNGIDDNDCLQNKKCNYRKEFNIPDDGILAGSCANLTKRKGIDLVIQTLTKEHKIYYIVAGNGIEKHNLINLVKARKLHERVYFIDFLDEPESFMSQLDVFLMPSRSEGFGLTVLESTKLGIPVITSNIPIFMELFDQMCLTFDIKNPSTLIDVITYAKKNRLHLSQKFHAIFQDRFTSSKMATKYENVYNNLFREVL
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Involved in the assembly of the O-repeating unit during O-antigen biosynthesis. Glucosyltransferase accountable for the alpha-D-Glc-1,4-beta-D-Gal linkage within the O-antigen. Transfers alpha-1,4-Glc to the Gal moiety of a specific Gal-beta1-3GalNAc-alpha-OPO3-PO3-phenoxyundecyl (Gal-beta1-3GalNAc-PP-PhU) synthetic natural acceptor substrate analog. Requires both Gal-beta1-3GalNAc-alpha and the diphosphate moiety in the acceptor. Not active with GalNAc-PP-PhU, GlcNAc-PP-PhU, Gal-beta1-3GalNAc-alpha-O-benzyl, D-Rha-alpha1-3GlcNAc-alpha-PP-PhU or D-Man-alpha1-3Man-alpha-5-benzamidopentyl (BAP), nor with glycopeptides TTTVTP (Gal-beta1-3GalNAc-alpha-)TPTG or TT (Gal-beta1-3GalNAc-alpha-)TVTPTPTG as acceptor substrates. Has a broad nucleotide sugar donor substrate specificity with ADP-Glc, TDP-Glc and UDP-Glc as superior donors. Gal, GlcNAc, and GalNAc residues are transferred from UDP-sugars, but with low activity. UDP-Xyl, UDP-GlcA, GDP-Fuc or GDP-K-Rha do not act as donors.
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A6N6J5
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WDR35_RAT
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WD repeat-containing protein 35 (Naofen)
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MFFYLSKKIAVPNNVKLKCISWNKDQGFIACGGEDGLLKVLRLETQTDDSKLRGLAAPSNLSMNQNLEGHSGAVQVVTWNEQYQKLTTSDQNGLIIVWMLYKGSWYEEMINNRNKSVVRSMSWNADGQKICIVYEDGAVIVGSVDGNRIWGKDLKGIQLCHVTWSADSKILLFGMANGEIHIYDNQGNFIMKMKLNCLVNVTGAISIAGIHWYHGTEGYVEPDCPCLAICFDNGRCQIMRHENDQNPVLIDTGMYVVGIQWNHIGSVLAVAGSQKVVTQDKDVNIVQFYTPFGEHLGTLKVPGKQMCSLSWEGGGLKIALAVDSFIYFANIRPDYKWGYCSNTVVYAYTRPDRPEYCVVFWDTKNNEKYVKYVKSLISITTCGDFCILATKADENHPQFVLVLCNSIGTPLDPKYIDLVPLFVAMTKTHVIAASKEALYTWQYRVAKKLTALEINQITRSRKEGRERIYHVDDVPSGSVDGVFDYSKAIQGTRDPICAITASDKTLIVGRESGVIQRYSFPNVALIQKYSLDCRACQLSLNCNSSRLAIIDIAGVLTFFDLDTRVTDSTGQQVVGELLKLERKDVWDMKWAKDNPDLFAMMEKTRMYVFRNLDPEEPIQTSGYICNFEDLEIKSVLLDEILKNPEHPSKDYIMNFEIRSLRDSRALIEKVGIEDASQFIEDNPHPRLWRLLAEAALQKLDLYTAQQAFVRCKDYQGIKFVKRLGNLQSESMKQAEVIAYFGRFEEAERMYLDMDRRDLAIGLRLKLGDWFRVLQLLKTGSGDADDSLLEQAHNAIGDYFADRQKWMNAVQYYVKGRNQERLAECYYMLEDYEGLENLANSLPENHKLLPEIAQMFVRVGMCEQAVSAFLKCNQPKAAVDTCVHLNQWNKAVELAKSHSMKEIGSLLARYASHLLEKNKTLDAIELYRKASYFFDAAKLMYKIADEEAKKRTKPLRVKKLYVLSALLIEQYHEQMKNAQRGKVKGKNSEATSALAGLLEEEVLSTTSRFTDNAWRGAEAYHFFILAQRQLYEGYVDTALKTALHLRDYEDIIPSVEIYSLLALCACASRAFGTCSKAFIKLESLETLSAEQKQQYEDLALEIFTKHTPKDNRKSELNSLLEGGEGKLPTCIATGSPIIEYQFWVCKVCKHYVLAQEISNYNFCPLCHSSVE
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As a component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors (GPCRs), it is involved in ciliogenesis and ciliary protein trafficking (By similarity). May promote CASP3 activation and TNF-stimulated apoptosis.
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A6NC98
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CC88B_HUMAN
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Coiled-coil domain-containing protein 88B (Brain leucine zipper domain-containing protein) (Gipie) (Hook-related protein 3) (HkRP3)
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MEGGKGPRLRDFLSGSLATWALGLAGLVGEAEDSEGEEEEEEEEPPLWLEKRFLRLSDGALLLRVLGIIAPSSRGGPRMLRGLDGPAAWRVWNLNHLWGRLRDFYQEELQLLILSPPPDLQTLGFDPLSEEAVEQLEGVLRLLLGASVQCEHRELFIRHIQGLSLEVQSELAAAIQEVTQPGAGVVLALSGPDPGELAPAELEMLSRSLMGTLSKLARERDLGAQRLAELLLEREPLCLRPEAPSRAPAEGPSHHLALQLANAKAQLRRLRQELEEKAELLLDSQAEVQGLEAEIRRLRQEAQALSGQAKRAELYREEAEALRERAGRLPRLQEELRRCRERLQAAEAYKSQLEEERVLSGVLEASKALLEEQLEAARERCARLHETQRENLLLRTRLGEAHAELDSLRHQVDQLAEENVELELELQRSLEPPPGSPGEAPLAGAAPSLQDEVREAEAGRLRTLERENRELRGLLQVLQGQPGGQHPLLEAPREDPVLPVLEEAPQTPVAFDHSPQGLVQKARDGGPQALDLAPPALDSVLEASAECPQAPDSDPQEAESPLQAAAMDPQASDWSPQESGSPVETQESPEKAGRRSSLQSPASVAPPQGPGTKIQAPQLLGGETEGREAPQGELVPEAWGLRQEGPEHKPGPSEPSSVQLEEQEGPNQGLDLATGQAEAREHDQRLEGTVRDPAWQKPQQKSEGALEVQVWEGPIPGESLASGVAEQEALREEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQARLREAVEAAGQELESASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLESEGRQHLEEAERERREKEALQAELEKAVVRGKELGDRLEHLQRELEQAALERQEFLREKESQHQRYQGLEQRLEAELQAAATSKEEALMELKTRALQLEEELFQLRQGPAGLGPKKRAEPQLVETQNVRLIEVERSNAMLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSVLEIQGQELHRKLEVLEEEVRAARQSQEETRGQQQALLRDHKALAQLQRRQEAELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERERLMQDGHRQRGLEEELRRLQSEHDRAQMLLAELSRERGELQGERGELRGRLARLELERAQLEMQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALRREKQKLVEKIMDQYRVLEPVPLPRTKKGSWLADKVKRLMRPRREGGPPGGLRLGADGAGSTESLGGPPETELPEGREADGTGSPSPAPMRRAQSSLCLRDETLAGGQRRKLSSRFPVGRSSESFSPGDTPRQRFRQRHPGPLGAPVSHSKGPGVGWENSAETLQEHETDANREGPEVQEPEKRPLTPSLSQ
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Acts as a positive regulator of T-cell maturation and inflammatory function. Required for several functions of T-cells, in both the CD4(+) and the CD8(+) compartments and this includes expression of cell surface markers of activation, proliferation, and cytokine production in response to specific or non-specific stimulation (By similarity). Enhances NK cell cytotoxicity by positively regulating polarization of microtubule-organizing center (MTOC) to cytotoxic synapse, lytic granule transport along microtubules, and dynein-mediated clustering to MTOC. Interacts with HSPA5 and stabilizes the interaction between HSPA5 and ERN1, leading to suppression of ERN1-induced JNK activation and endoplasmic reticulum stress-induced apoptosis.
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A6NCS4
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NKX26_HUMAN
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Homeobox protein Nkx-2.6 (Homeobox protein NK-2 homolog F)
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MLLSPVTSTPFSVKDILRLERERSCPAASPHPRVRKSPENFQYLRMDAEPRGSEVHNAGGGGGDRKLDGSEPPGGPCEAVLEMDAERMGEPQPGLNAASPLGGGTRVPERGVGNSGDSVRGGRSEQPKARQRRKPRVLFSQAQVLALERRFKQQRYLSAPEREHLASALQLTSTQVKIWFQNRRYKCKRQRQDKSLELAGHPLTPRRVAVPVLVRDGKPCLGPGPGAPAFPSPYSAAVSPYSCYGGYSGAPYGAGYGTCYAGAPSGPAPHTPLASAGFGHGGQNATPQGHLAATLQGVRAW
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Acts as a transcriptional activator. In conjunction with NKX2-5, may play a role in both pharyngeal and cardiac embryonic development.
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A6ND01
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JUNO_HUMAN
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Sperm-egg fusion protein Juno (Folate receptor 4) (Folate receptor delta) (FR-delta) (IZUMO1 receptor protein JUNO)
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MACWWPLLLELWTVMPTWAGDELLNICMNAKHHKRVPSPEDKLYEECIPWKDNACCTLTTSWEAHLDVSPLYNFSLFHCGLLMPGCRKHFIQAICFYECSPNLGPWIQPVGSLGWEVAPSGQGERVVNVPLCQEDCEEWWEDCRMSYTCKSNWRGGWDWSQGKNRCPKGAQCLPFSHYFPTPADLCEKTWSNSFKASPERRNSGRCLQKWFEPAQGNPNVAVARLFASSAPSWELSYTIMVCSLFLPFLS
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Receptor for IZUMO1 present at the cell surface of oocytes (oolemma), which is essential for species-specific gamete recognition and fertilization. The IZUMO1:IZUMO1R/JUNO interaction is a necessary adhesion event between sperm and egg that is required for fertilization but is not sufficient for cell fusion. The ligand-receptor interaction probably does not act as a membrane 'fusogen'. Does not bind folate.
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A6ND36
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FA83G_HUMAN
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Protein FAM83G (Protein associated with SMAD1)
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MAFSQVQCLDDNHVNWRSSESKPEFFYSEEQRLALEALVARGRDAFYEVLKRENIRDFLSELELKRILETIEVYDPGSEDPRGTGPSQGPEDNGVGDGEEASGADGVPIEAEPLPSLEYWPQKSDRSIPQLDLGWPDTIAYRGVTRASVYMQPPIDGQAHIKEVVRKMISQAQKVIAVVMDMFTDVDIFKDLLDAGFKRKVAVYIIVDESNVKYFLHMCERACMHLGHLKNLRVRSSGGTEFFTRSATKFKGALAQKFMFVDGDRAVCGSYSFTWSAARTDRNVISVLSGQVVEMFDRQFQELYLMSHSVSLKGIPMEKEPEPEPIVLPSVVPLVPAGTVAKKLVNPKYALVKAKSVDEIAKISSEKQEAKKPLGLKGPALAEHPGELPELLPPIHPGLLHLERANMFEYLPTWVEPDPEPGSDILGYINIIDPNIWNPQPSQMNRIKIRDTSQASAQHQLWKQSQDSRPRPEPCPPPEPSAPQDGVPAENGLPQGDPEPLPPVPKPRTVPVADVLARDSSDIGWVLELPKEEAPQNGTDHRLPRMAGPGHAPLQRQLSVTQDDPESLGVGLPNGLDGVEEEDDDDYVTLSDQDSHSGSSGRGPGPRRPSVASSVSEEYFEVREHSVPLRRRHSEQVANGPTPPPRRQLSAPHITRGTFVGPQGGSPWAQSRGREEADALKRMQAQRSTDKEAQGQQFHHHRVPASGTRDKDGFPGPPRYRSAADSVQSSTRNAGPAMAGPHHWQAKGGQVPRLLPDPGSPRLAQNARPMTDGRATEEHPSPFGIPYSKLSQSKHLKARTGGSQWASSDSKRRAQAPRDRKDP
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Substrate for type I BMP receptor kinase involved in regulation of some target genes of the BMP signaling pathway. Also regulates the expression of several non-BMP target genes, suggesting a role in other signaling pathways.
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A6NDB9
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PALM3_HUMAN
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Paralemmin-3
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MAESSLYRQRLEVIAEKRRLQEEIRAARREVEEEKLRVERLKRKSLRERWLMDGAAAVPEPSEDPTSKDPQSPEGQAQARIRNLEDSLFTLQSQLQLLQSASTGAQHKPSGRPSWRRQGHRPLSQSIVEAGSVGQTDLNKRASLPAGLVGTPPESPSEPREDVLGFLPGPRQVPGAAGDSSEANGPCPSPIPTPEQGLSQRAVPSEGRVGEAKGGGVVSVVWEGLRATEDCATGATGPELEAKVEEVVLEAIGDRKGAGSLELPAWVKEDRGIVEVVWEGVGGSDAEAMGEIGRVPEVVQTSSPRLQERLEAAASIEGEDVPQGSPEGDGQGGSGGEEGSFIWVERVTLSEEWEELLVEGLEGPEVAGRERGDESPLGAEGAKTGGGEETWEAEKRKAEESMGIGSEEKPGTGRDEAEMSPVVERKGGEKKLELESRGSAEKLGTEREGGEEPLGIERKVEGHLRAEKEGDEEKRGAEEEEVEEPLGVEKKGGEEEPEATKEPLEAERKGGEETLEAEKRGGEESLETEKTQGTEGDLNLEQGSREGSESQAEEMNEAGPPLEANTETRPEKEGPQPQEKPVGALEEEGVKPQTAAEGQGPLGDATPLLAETPAPEQPAECQPLLQGEGPSANPSAHPVPTYAPARQPEPSAPTEGEEASGPKQKTCQCCAVM
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ATP-binding protein, which may act as a adapter in the Toll-like receptor (TLR) signaling.
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A6NDE4
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RBY1B_HUMAN
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RNA-binding motif protein, Y chromosome, family 1 member B
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MVEADHPGKLFIGGLNRETNEKMLKAVFGKHGPISEVLLIKDRTSKSRGFAFITFENPADAKNAAKDMNGKSLHGKAIKVEQAKKPSFQSGGRRRPPASSRNRSPSGSLRSARGSRGGTRGWLPSQEGHLDDGGYTPDLKMSYSRGLIPVKRGPSSRSGGPPPKKSAPSAVARSNSWMGSQGPMSQRRENYGVPPRRATISSWRNDRMSTRHDGYATNDGNHPSCQETRDYAPPSRGYAYRDNGHSNRDEHSSRGYRNHRSSRETRDYAPPSRGHAYRDYGHSRRDESYSRGYRNRRSSRETREYAPPSRGHGYRDYGHSRRHESYSRGYRNHPSSRETRDYAPPHRDYAYRDYGHSSWDEHSSRGYSYHDGYGEALGRDHSEHLSGSSYRDALQRYGTSHGAPPARGPRMSYGGSTCHAYSNTRDRYGRSWESYSSCGDFHYCDREHVCRKDQRNPPSLGRVLPDPREAYGSSSYVASIVDGGESRSEKGDSSRY
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RNA-binding protein which may be involved in spermatogenesis. Required for sperm development, possibly by participating in pre-mRNA splicing in the testis.
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A6NDG6
|
PGP_HUMAN
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Glycerol-3-phosphate phosphatase (G3PP) (EC 3.1.3.21) (Aspartate-based ubiquitous Mg(2+)-dependent phosphatase) (AUM) (EC 3.1.3.48) (Phosphoglycolate phosphatase) (PGP)
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MAAAEAGGDDARCVRLSAERAQALLADVDTLLFDCDGVLWRGETAVPGAPEALRALRARGKRLGFITNNSSKTRAAYAEKLRRLGFGGPAGPGASLEVFGTAYCTALYLRQRLAGAPAPKAYVLGSPALAAELEAVGVASVGVGPEPLQGEGPGDWLHAPLEPDVRAVVVGFDPHFSYMKLTKALRYLQQPGCLLVGTNMDNRLPLENGRFIAGTGCLVRAVEMAAQRQADIIGKPSRFIFDCVSQEYGINPERTVMVGDRLDTDILLGATCGLKTILTLTGVSTLGDVKNNQESDCVSKKKMVPDFYVDSIADLLPALQG
|
Glycerol-3-phosphate phosphatase hydrolyzing glycerol-3-phosphate into glycerol. Thereby, regulates the cellular levels of glycerol-3-phosphate a metabolic intermediate of glucose, lipid and energy metabolism. Was also shown to have a 2-phosphoglycolate phosphatase activity and a tyrosine-protein phosphatase activity. However, their physiological relevance is unclear. In vitro, has also a phosphatase activity toward ADP, ATP, GDP and GTP (By similarity).
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A6NDV4
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TMM8B_HUMAN
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Transmembrane protein 8B (Nasopharyngeal carcinoma-associated gene 6 protein) (Protein NAG-5) (Protein NGX6)
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MNMPQSLGNQPLPPEPPSLGTPAEGPGTTSPPEHCWPVRPTLRNELDTFSVHFYIFFGPSVALPPERPAVFAMRLLPVLDSGGVLSLELQLNASSVRQENVTVFGCLTHEVPLSLGDAAVTCSKESLAGFLLSVSATTRVARLRIPFPQTGTWFLALRSLCGVGPRFVRCRNATAEVRMRTFLSPCVDDCGPYGQCKLLRTHNYLYAACECKAGWRGWGCTDSADALTYGFQLLSTLLLCLSNLMFLPPVVLAIRSRYVLEAAVYTFTMFFSTFYHACDQPGIVVFCIMDYDVLQFCDFLGSLMSVWVTVIAMARLQPVVKQVLYLLGAMLLSMALQLDRHGLWNLLGPSLFALGILATAWTVRSVRRRHCYPPTWRRWLFYLCPGSLIAGSAVLLYAFVETRDNYFYIHSIWHMLIAGSVGFLLPPRAKTDHGVPSGARARGCGYQLCINEQEELGLVGPGGATVSSICAS
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May function as a regulator of the EGFR pathway. Probable tumor suppressor which may function in cell growth, proliferation and adhesion.
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A6NED2
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RCCD1_HUMAN
|
RCC1 domain-containing protein 1
|
MAEERPGAWFGFGFCGFGQELGSGRGRQVHSPSPLRAGVDICRVSASWSYTAFVTRGGRLELSGSASGAAGRCKDAWASEGLLAVLRAGPGPEALLQVWAAESALRGEPLWAQNVVPEAEGEDDPAGEAQAGRLPLLPCARAYVSPRAPFYRPLAPELRARQLELGAEHALLLDAAGQVFSWGGGRHGQLGHGTLEAELEPRLLEALQGLVMAEVAAGGWHSVCVSETGDIYIWGWNESGQLALPTRNLAEDGETVAREATELNEDGSQVKRTGGAEDGAPAPFIAVQPFPALLDLPMGSDAVKASCGSRHTAVVTRTGELYTWGWGKYGQLGHEDTTSLDRPRRVEYFVDKQLQVKAVTCGPWNTYVYAVEKGKS
|
Plays a role in transcriptional repression of satellite repeats, possibly by regulating H3K36 methylation levels in centromeric regions together with KDM8. Possibly together with KDM8, is involved in proper mitotic spindle organization and chromosome segregation. Plays a role in regulating alpha-tubulin deacetylation and cytoskeletal microtubule stability, thereby promoting cell migration and TGF-beta-induced epithelial to mesenchymal transition (EMT), potentially through the inhibition of KDM8.
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A6NFA1
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TIKI2_HUMAN
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Metalloprotease TIKI2 (EC 3.4.-.-) (Heart, kidney and adipose-enriched transmembrane protein homolog) (TRAB domain-containing protein 2B)
|
MHAALAGPLLAALLATARARPQPPDGGQCRPPGSQRDLNSFLWTIRRDPPAYLFGTIHVPYTRVWDFIPDNSKAAFQASTRVYFELDLTDPYTISALASCQLLPHGENLQDVLPHELYWRLKRHLDYVKLMMPSWMTPAQRGKGLYADYLFNAIAGNWERKRPVWVMLMVNSLTERDVRFRGVPVLDLYLAQQAEKMKKTTGAVEQVEEQCHPLNNGLNFSQVLFALNQTLLQQESVRAGSLQASYTTEDLIKHYNCGDLSAVIFNHDTSQLPNFINTTLPPHEQVTAQEIDSYFRQELIYKRNERMGKRVMALLRENEDKICFFAFGAGHFLGNNTVIDILRQAGLEVDHTPAGQAIHSPAPQSPAPSPEGTSTSPAPVTPAAAVPEAPSVTPTAPPEDEDPALSPHLLLPDSLSQLEEFGRQRKWHKRQSTHQRPRQFNDLWVRIEDSTTASPPPLPLQPTHSSGTAKPPFQLSDQLQQQDPPGPASSSAPTLGLLPAIATTIAVCFLLHSLGPS
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Metalloprotease that acts as a negative regulator of the Wnt signaling pathway by mediating the cleavage of the 8 N-terminal residues of a subset of Wnt proteins. Following cleavage, Wnt proteins become oxidized and form large disulfide-bond oligomers, leading to their inactivation. Able to cleave WNT3A, WNT5, but not WNT11. Required for head formation.
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A6NFQ2
|
TCAF2_HUMAN
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TRPM8 channel-associated factor 2 (TRP channel-associated factor 2)
|
MATIAAAAFEALMDGVTCWDVPRGPIPSELLLIGEAAFPVMVNDKGQVLIAASSYGRGRLVVVSHEGYLSHTGLAPFLLNAVSWLCPCPGAPVGVHPSLAPLVNILQDAGLEAQVKPEPGEPLGVYCINAYNDTLTATLIQFVKHGGGLLIGGQAWYWASQHGPDKVLSRFPGNKVTSVAGVYFTDTYGDRDRFKVSKKVPKIPLHVRYGEDVRQDQQQLLEGISELDIRTGGVPSQLLVHGALAFPLGLDASLNCFLAAAHYGRGRVVLAAHECLLCAPKMGPFLLNAVRWLARGQTGKVGVNTNLKDLCPLLSEHGLQCSLEPHLNSDLCVYCCKAYSDKEAKQLQEFVAEGGGLLIGGQAWWWASQNPGHCPLAGFPGNIILNCFGLSILPQTLKAGCFPVPTPEMRSYHFRKALSQFQAILNHENGNLEKSCLAKLRVDGAAFLQIPAEGVPAYISLHRLLRKMLRGSGLPAVSRENPVASDSYEAAVLSLATGLAHSGTDCSQLAQGLGTWTCSSSLYPSKHPITVEINGINPGNNDCWVSTGLYLLEGQNAEVSLSEAAASAGLRVQIGCHTDDLTKARKLSRAPVVTHQCWMDRTERSVSCLWGGLLYVIVPKGSQLGPVPVTIRGAVPAPYYKLGKTSLEEWKRQMQENLAPWGELATDNIILTVPTTNLQALKDPEPVLRLWDEMMQAVARLAAEPFPFRRPERIVADVQISAGWMHSGYPIMCHLESVKEIINEMDMRSRGVWGPIHELGHNQQRHGWEFPPHTTEATCNLWSVYVHETVLGIPRAQAHEALSPPERERRIKAHLGKGAPLCDWNVWTALETYLQLQEAFGWEPFTQLFAEYQTLSHLPKDNTGRMNLWVKKFSEKVKKNLVPFFEAWGWPIQKEVADSLASLPEWQENPMQVYLRARK
|
[Isoform 2]: Negatively regulates the plasma membrane cation channel TRPM8 activity. Involved in the recruitment of TRPM8 to the cell surface. Promotes prostate cancer cell migration stimulation in a TRPM8-dependent manner.
|
A6NFX1
|
MFS2B_HUMAN
|
Sphingosine-1-phosphate transporter MFSD2B (Major facilitator superfamily domain-containing protein 2B) (hMfsd2b)
|
MAAPPAPAAKGSPQPEPHAPEPGPGSAKRGREDSRAGRLSFCTKVCYGIGGVPNQIASSATAFYLQLFLLDIAQIPAAQVSLVLFGGKVSGAAADPVAGFFINRSQRTGSGRLMPWVLGCTPFIALAYFFLWFLPPFTSLRGLWYTTFYCLFQALATFFQVPYTALTMLLTPCPRERDSATAYRMTVEMAGTLMGATVHGLIVSGAHRPHRCEATATPGPVTVSPNAAHLYCIAAAVVVVTYPVCISLLCLGVKERPDPSAPASGPGLSFLAGLSLTTRHPPYLKLVISFLFISAAVQVEQSYLVLFCTHASQLHDHVQGLVLTVLVSAVLSTPLWEWVLQRFGKKTSAFGIFAMVPFAILLAAVPTAPVAYVVAFVSGVSIAVSLLLPWSMLPDVVDDFQLQHRHGPGLETIFYSSYVFFTKLSGACALGISTLSLEFSGYKAGVCKQAEEVVVTLKVLIGAVPTCMILAGLCILMVGSTPKTPSRDASSRLSLRRRTSYSLA
|
Lipid transporter that specifically mediates export of sphingosine-1-phosphate in red blood cells and platelets. Sphingosine-1-phosphate is a signaling sphingolipid and its export from red blood cells into in the plasma is required for red blood cell morphology (By similarity). Sphingosine-1-phosphate export from platelets is required for platelet aggregation and thrombus formation (By similarity). Mediates the export of different sphingosine-1-phosphate (S1P) species, including S1P(d18:0) (sphinganine 1-phosphate), S1P (d18:1) (sphing-4-enine 1-phosphate) and S1P (d18:2) (sphinga-4E,14Z-dienine-1-phosphate) (Probable). Release of sphingosine-1-phosphate is facilitated by a proton gradient (By similarity). In contrast, cations, such as sodium, are not required to drive sphingosine-1-phosphate transport (Probable). In addition to export, also able to mediate S1P import (By similarity). Does not transport lysophosphatidylcholine (LPC) (Probable).
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A6NFY7
|
SDHF1_HUMAN
|
Succinate dehydrogenase assembly factor 1, mitochondrial (SDH assembly factor 1) (SDHAF1) (LYR motif-containing protein 8)
|
MSRHSRLQRQVLSLYRDLLRAGRGKPGAEARVRAEFRQHAGLPRSDVLRIEYLYRRGRRQLQLLRSGHATAMGAFVRPRAPTGEPGGVGCQPDDGDSPRNPHDSTGAPETRPDGR
|
Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Promotes maturation of the iron-sulfur protein subunit SDHB of the SDH catalytic dimer, protecting it from the deleterious effects of oxidants. May act together with SDHAF3. Contributes to iron-sulfur cluster incorporation into SDHB by binding to SDHB and recruiting the iron-sulfur transfer complex formed by HSC20, HSPA9 and ISCU through direct binding to HSC20.
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A6NGG8
|
PCARE_HUMAN
|
Photoreceptor cilium actin regulator
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MGCTPSHSDLVNSVAKSGIQFLKKPKAIRPGCQGGSERGSIPLLVKNSTCYDAGEGLAEEQPSPRRNQTTAKGLCQLMGDPASGKRKDMEGLIPGTKTSSSQLNKSQSHMAKDIPFKTQGSHGSQGADFSGDESEESSTQDTSKWKRTAKCHTSSTQSHCYQTIHPAHEPEGKVDFPEPLVKAHQQAYTYLHSSLSKYEAILCIIHQATQTRELLQPMVSFLLLCFEEISQLLGEISKDGEVLLQEVREDLAWPLKKREPQEQPNLLQQLLQYTVSKLQVLNGTVASLTGSFLEGSSSYLHSTATHLENKLSTKRNVDERLLRALRQLESLASGCGDPGVQGLPLCSEDSGIGADNESVQSVDKLGKQTSWDLAPEPEEWKSVTSPHTEARQSGHTWQQSPFCLGSGRPQDCLLSGAPMAKVQPRAQDEARSPCLSSTSPENITSPPLKLGTSTPCDSFGIGVSVEPHLSKTSRPMDASSLSDSEDSSPEEEEEDKMSSMSLCAWQEKTPHSRPQSSPADRESPFQARTRRLRSLQAQEMILKMKESISERIKFVPVPCGHQDWSEEEEGRTVVPPRPSTVSGSRRAPERQTRSQSESCLQSHVEDPTFQELRRVQRDLSQKLEAFYALGAKGQGQSQEQILQPRAAAVWPNGTCRVSPSNTTSRLKASLTKNFSILPSQDKSILQKCNPHPEDEQGKAGKLPNAIPSGEVSEAAKATDWNVRGCPTRTSVKKLIETFSPTESLRMLGDSKDAGASPCLRNCIMPPRFPKYTGLAPLYPKPQISPASGRESLKMGIGWKPLAPIFPPLPKAEAAKSEELSCEMEGNLEHLPPPPMEVLMDKSFASLESPESSKSTENSPKETQEPGPGEAGPTRRTWASPKLRASVSPLDLLPSKSTASLTKPHSTGPGSGRSSCQPRKPALDLSSPPATSQSPEVKGGTWSQAEKATSLYRQPRKAIAWHHSGPPSGQNRTSESSLARPRQSRERSPPVGRKASPTRTHWVPQADKRRRSLPSSYRPAQPSPSAVQTPPSPPVSPRVLSPPTTKRRTSPPHQPKLPNPPPESAPAQCKVPSPPTQHPEASPPFSIPSPSPPMSPSQEHKETRDSEDSQAVIAKVSGNTHSIFCPATSSLFEAKPPLSTAHPLTPPSLPPEAGGPLGNPAECWKNSSGPWLRADSQRRAALCALNPLPFLRRTASDRQPGGRPQPPTLDPTSTSYESQLGQNSSSEESPKKDTEPGSSPCSPELQGGTRRASPPEFCVLGHGLQPEPRTGHIQDKSQPEAQPQQEEVS
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Plays an essential role for normal photoreceptor cell maintenance and vision.
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A6NGQ2
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OOEP_HUMAN
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Oocyte-expressed protein homolog (KH homology domain-containing protein 2) (Oocyte- and embryo-specific protein 19) (hOEP19)
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MVDDAGAAESQRGKQTPAHSLEQLRRLPLPPPQIRIRPWWFPVQELRDPLVFYLEAWLADELFGPDRAIIPEMEWTSQALLTVDIVDSGNLVEITVFGRPRVQNRVKSMLLCLAWFHREHRARAEKMKHLEKNLKAHASDPHSPQDPVA
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As part of the OOEP-KHDC3L scaffold, recruits BLM and TRIM25 to DNA replication forks, thereby promoting the ubiquitination of BLM by TRIM25, enhancing BLM retainment at replication forks and therefore promoting stalled replication fork restart (By similarity). Positively regulates the homologous recombination-mediated DNA double-strand break (DSB) repair pathway by regulating ATM activation and RAD51 recruitment to DSBs in oocytes (By similarity). Thereby contributes to oocyte survival and the resumption and completion of meiosis (By similarity). As a member of the subcortical maternal complex (SCMC), plays an essential role for zygotes to progress beyond the first embryonic cell divisions via regulation of actin dynamics (By similarity). Required for the formation of F-actin cytoplasmic lattices in oocytes which in turn are responsible for symmetric division of zygotes via the regulation of mitotic spindle formation and positioning (By similarity).
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A6NGU5
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GGT3_HUMAN
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Putative glutathione hydrolase 3 proenzyme (EC 3.4.19.13) (Gamma-glutamyltransferase 3) (Putative gamma-glutamyltranspeptidase 3) (GGT 3) (EC 2.3.2.2) [Cleaved into: Putative glutathione hydrolase 3 heavy chain; Putative glutathione hydrolase 3 light chain]
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MKKKLVVLGLLAVVLVLVIVGLCLWLPSASKEPDNHVYTRAAVAADAKQCLEIGRDTLRDGGSAVDAAIAALLCVGLMNAHSMGIGVGLFLTIYNSTTRKAEVINAREVAPRLAFASMFNSSEQSQKGGLSVAVPGEIRGYELAHQRHGRLPWARLFQPSIQLARQGFPVGKGLAAVLENKRTVIEQQPVLCEVFCRDRKVLREGERLTLPRLADTYEMLAIEGAQAFYNGSLMAQIVKDIQAAGGIVTAEDLNNYCAELIEHPLNISLGDAVLYMPSARLSGPVLALILNILKGYNFSRESVETPEQKGLTYHRIVEAFRFAYAKRTLLGDPKFVDVTEVVRNMTSEFFAAQLRSQISDHTTHPISYYKPEFYTPDDGGTAHLSVVAEDGSAVSATSTINLYFGSKVCSPVSGILFNNMDDFSSPSITNEFGAPPSPANFIQPGKQPLLSMCPTIMVGQDGQVRMVVGAAGGTQITTDTALAIIYNLWFGYDVKRAVEEPRLHNKLLPNVTTVERNIDQAVTAALETRHHHTQIASTFIAVVQAIVRTAGGWAAASDSRKGGEPAGY
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Hydrolyzes and transfers gamma-glutamyl moieties from glutathione and other gamma-glutamyl compounds to acceptors.
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A6NHL2
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TBAL3_HUMAN
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Tubulin alpha chain-like 3 (EC 3.6.5.-)
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MRECLSIHIGQAGIQIGDACWELYCLEHGIQPNGVVLDTQQDQLENAKMEHTNASFDTFFCETRAGKHVPRALFVDLEPTVIDGIRTGQHRSLFHPEQLLSGKEDAANNYARGRYSVGSEVIDLVLERTRKLAEQCGGLQGFLIFRSFGGGTGSGFTSLLMERLTGEYSRKTKLEFSVYPAPRISTAVVEPYNSVLTTHSTTEHTDCTFMVDNEAVYDICHRKLGVECPSHASINRLVVQVVSSITASLRFEGPLNVDLIEFQTNLVPYPRIHFPMTAFAPIVSADKAYHEQFSVSDITTACFESSNQLVKCDPRLGKYMACCLLYRGDVVPKEVNAAIAATKSRHSVQFVDWCPTGFKVGINNRPPTVMPGGDLAKVHRSICMLSNTTAIVEAWARLDHKFDLMYAKRAFLHWYLREGMEEAEFLEAREDLAALERDYEEVAQSF
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Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
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A6NHR9
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SMHD1_HUMAN
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Structural maintenance of chromosomes flexible hinge domain-containing protein 1 (SMC hinge domain-containing protein 1) (EC 3.6.1.-)
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MAAADGGGPGGASVGTEEDGGGVGHRTVYLFDRREKESELGDRPLQVGERSDYAGFRACVCQTLGISPEEKFVITTTSRKEITCDNFDETVKDGVTLYLLQSVNQLLLTATKERIDFLPHYDTLVKSGMYEYYASEGQNPLPFALAELIDNSLSATSRNIGVRRIQIKLLFDETQGKPAVAVIDNGRGMTSKQLNNWAVYRLSKFTRQGDFESDHSGYVRPVPVPRSLNSDISYFGVGGKQAVFFVGQSARMISKPADSQDVHELVLSKEDFEKKEKNKEAIYSGYIRNRKPSDSVHITNDDERFLHHLIIEEKEKDSFTAVVITGVQPEHIQYLKNYFHLWTRQLAHIYHYYIHGPKGNEIRTSKEVEPFNNIDIEISMFEKGKVPKIVNLREIQDDMQTLYVNTAADSFEFKAHVEGDGVVEGIIRYHPFLYDRETYPDDPCFPSKLKDEDDEDDCFILEKAARGKRPIFECFWNGRLIPYTSVEDFDWCTPPKKRGLAPIECYNRISGALFTNDKFQVSTNKLTFMDLELKLKDKNTLFTRILNGQEQRMKIDREFALWLKDCHEKYDKQIKFTLFKGVITRPDLPSKKQGPWATYAAIEWDGKIYKAGQLVKTIKTLPLFYGSIVRFFLYGDHDGEVYATGGEVQIAMEPQALYDEVRTVPIAKLDRTVAEKAVKKYVEDEMARLPDRLSVTWPEGDELLPNEVRPAGTPIGALRIEILNKKGEAMQKLPGTSHGGSKKLLVELKVILHSSSGNKEIISHISQHGGKWPYWFKKMENIQKLGNYTLKLQVVLNESNADTYAGRPLPSKAIKFSVKEGKPEKFSFGLLDLPFRVGVPFNIPLEFQDEFGHTSQLVTDIQPVLEASGLSLHYEEITKGPNCVIRGVTAKGPVNSCQGKNYNLKVTLPGLKEDSQILKIRLLPGHPRRLKVKPDSEILVIENGTAFPFQVEVLDESDNITAQPKLIVHCKFSGAPNLPVYVVDCSSSGTSILTGSAIQVQNIKKDQTLKARIEIPSCKDVAPVEKTIKLLPSSHVARLQIFSVEGQKAIQIKHQDEVNWIAGDIMHNLIFQMYDEGEREINITSALAEKIKVNWTPEINKEHLLQGLLPDVQVPTSVKDMRYCQVSFQDDHVSLESAFTVRPLPDEPKHLKCEMKGGKTVQMGQELQGEVVIIITDQYGNQIQAFSPSSLSSLSIAGVGLDSSNLKTTFQENTQSISVRGIKFIPGPPGNKDLCFTWREFSDFIRVQLISGPPAKLLLIDWPELKESIPVINGRDLQNPIIVQLCDQWDNPAPVQHVKISLTKASNLKLMPSNQQHKTDEKGRANLGVFSVFAPRGEHTLQVKAIYNKSIIEGPIIKLMILPDPEKPVRLNVKYDKDASFLAGGLFTDFMISVISEDDSIIKNINPARISMKMWKLSTSGNRPPANAETFSCNKIKDNDKEDGCFYFRDKVIPNKVGTYCIQFGFMMDKTNILNSEQVIVEVLPNQPVKLVPKIKPPTPAVSNVRSVASRTLVRDLHLSITDDYDNHTGIDLVGTIIATIKGSNEEDTDTPLFIGKVRTLEFPFVNGSAEIMSLVLAESSPGRDSTEYFIVFEPRLPLLSRTLEPYILPFMFYNDVKKQQQMAALTKEKDQLSQSIVMYKSLFEASQQLLNEMKCQVEEARLKEAQLRNELKIHNIDIPTTQQVPHIEALLKRKLSEQEELKKKPRRSCTLPNYTKGSGDVLGKIAHLAQIEDDRAAMVISWHLASDMDCVVTLTTDAARRIYDETQGRQQVLPLDSIYKKTLPDWKRSLPHFRNGKLYFKPIGDPVFARDLLTFPDNVEHCETVFGMLLGDTIILDNLDAANHYRKEVVKITHCPTLLTRDGDRIRSNGKFGGLQNKAPPMDKLRGMVFGAPVPKQCLILGEQIDLLQQYRSAVCKLDSVNKDLNSQLEYLRTPDMRKKKQELDEHEKNLKLIEEKLGMTPIRKCNDSLRHSPKVETTDCPVPPKRMRREATRQNRIITKTDV
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Non-canonical member of the structural maintenance of chromosomes (SMC) protein family that plays a key role in epigenetic silencing by regulating chromatin architecture (By similarity). Promotes heterochromatin formation in both autosomes and chromosome X, probably by mediating the merge of chromatin compartments (By similarity). Plays a key role in chromosome X inactivation in females by promoting the spreading of heterochromatin. Recruited to inactivated chromosome X by Xist RNA and acts by mediating the merge of chromatin compartments: promotes random chromatin interactions that span the boundaries of existing structures, leading to create a compartment-less architecture typical of inactivated chromosome X (By similarity). Required to facilitate Xist RNA spreading (By similarity). Also required for silencing of a subset of clustered autosomal loci in somatic cells, such as the DUX4 locus. Has ATPase activity may participate in structural manipulation of chromatin in an ATP-dependent manner as part of its role in gene expression regulation. Also plays a role in DNA repair: localizes to sites of DNA double-strand breaks in response to DNA damage to promote the repair of DNA double-strand breaks. Acts by promoting non-homologous end joining (NHEJ) and inhibiting homologous recombination (HR) repair.
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A6NI15
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MSGN1_HUMAN
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Mesogenin-1 (Paraxial mesoderm-specific mesogenin1) (pMesogenin1) (pMsgn1)
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MDNLRETFLSLEDGLGSSDSPGLLSSWDWKDRAGPFELNQASPSQSLSPAPSLESYSSSPCPAVAGLPCEHGGASSGGSEGCSVGGASGLVEVDYNMLAFQPTHLQGGGGPKAQKGTKVRMSVQRRRKASEREKLRMRTLADALHTLRNYLPPVYSQRGQPLTKIQTLKYTIKYIGELTDLLNRGREPRAQSA
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Involved in specifying the paraxial, but not dorsal, mesoderm. May regulate the expression of T-box transcription factors required for mesoderm formation and differentiation (By similarity).
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A6NI61
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MYMK_HUMAN
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Protein myomaker (Myoblast fusion maker) (Transmembrane protein 226) (Transmembrane protein 8C)
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MGTLVAKLLLPTLSSLAFLPTVSIAAKRRFHMEAMVYLFTLFFVALHHACNGPGLSVLCFMRHDILEYFSVYGTALSMWVSLMALADFDEPKRSTFVMFGVLTIAVRIYHDRWGYGVYSGPIGTAILIIAAKWLQKMKEKKGLYPDKSVYTQQIGPGLCFGALALMLRFFFEDWDYTYVHSFYHCALAMSFVLLLPKVNKKAGSPGTPAKLDCSTLCCACV
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Myoblast-specific protein that mediates myoblast fusion, an essential step for the formation of multi-nucleated muscle fibers. Actively participates in the membrane fusion reaction by mediating the mixing of cell membrane lipids (hemifusion) upstream of MYMX. Acts independently of MYMX (By similarity). Involved in skeletal muscle regeneration in response to injury by mediating the fusion of satellite cells, a population of muscle stem cells, with injured myofibers (By similarity). Also involved in skeletal muscle hypertrophy, probably by mediating the fusion of satellite cells with myofibers (By similarity).
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A6NI73
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LIRA5_HUMAN
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Leukocyte immunoglobulin-like receptor subfamily A member 5 (CD85 antigen-like family member F) (Immunoglobulin-like transcript 11) (ILT-11) (Leukocyte immunoglobulin-like receptor 9) (LIR-9) (CD antigen CD85f)
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MAPWSHPSAQLQPVGGDAVSPALMVLLCLGLSLGPRTHVQAGNLSKATLWAEPGSVISRGNSVTIRCQGTLEAQEYRLVKEGSPEPWDTQNPLEPKNKARFSIPSMTEHHAGRYRCYYYSPAGWSEPSDPLELVVTGFYNKPTLSALPSPVVTSGENVTLQCGSRLRFDRFILTEEGDHKLSWTLDSQLTPSGQFQALFPVGPVTPSHRWMLRCYGSRRHILQVWSEPSDLLEIPVSGAADNLSPSQNKSDSGTASHLQDYAVENLIRMGMAGLILVVLGILIFQDWHSQRSPQAAAGR
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May play a role in triggering innate immune responses. Does not seem to play a role for any class I MHC antigen recognition.
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A6NIH7
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U119B_HUMAN
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Protein unc-119 homolog B
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MSGSNPKAAAAASAAGPGGLVAGKEEKKKAGGGVLNRLKARRQAPHHAADDGVGAAVTEQELLALDTIRPEHVLRLSRVTENYLCKPEDNIYSIDFTRFKIRDLETGTVLFEIAKPCVSDQEEDEEEGGGDVDISAGRFVRYQFTPAFLRLRTVGATVEFTVGDKPVSNFRMIERHYFREHLLKNFDFDFGFCIPSSRNTCEHIYEFPQLSEDVIRLMIENPYETRSDSFYFVDNKLIMHNKADYAYNGGQ
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Myristoyl-binding protein that acts as a cargo adapter: specifically binds the myristoyl moiety of a subset of N-terminally myristoylated proteins and is required for their localization. Binds myristoylated NPHP3 and plays a key role in localization of NPHP3 to the primary cilium membrane. Does not bind all myristoylated proteins. Probably plays a role in trafficking proteins in photoreceptor cells.
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A6NIX2
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WTIP_HUMAN
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Wilms tumor protein 1-interacting protein (WT1-interacting protein)
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MQRSRAGADEAALLLAGLALRELEPGCGSPGRGRRGPRPGPGDEAAPALGRRGKGSGGPEAGADGLSRGERGPRRAAVPELSAQPAGSPRASLAGSDGGGGGGSARSSGISLGYDQRHGSPRSGRSDPRPGPGPPSVGSARSSVSSLGSRGSAGAYADFLPPGACPAPARSPEPAGPAPFPLPALPLPPGREGGPSAAERRLEALTRELERALEARTARDYFGICIKCGLGIYGAQQACQAMGSLYHTDCFTCDSCGRRLRGKAFYNVGEKVYCQEDFLYSGFQQTADKCSVCGHLIMEMILQALGKSYHPGCFRCSVCNECLDGVPFTVDVENNIYCVRDYHTVFAPKCASCARPILPAQGCETTIRVVSMDRDYHVACYHCEDCGLQLSGEEGRRCYPLAGHLLCRRCHLRRLQPGPLPSPTVHVTEL
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Adapter or scaffold protein which participates in the assembly of numerous protein complexes and is involved in several cellular processes such as cell fate determination, cytoskeletal organization, repression of gene transcription, cell-cell adhesion, cell differentiation, proliferation and migration. Positively regulates microRNA (miRNA)-mediated gene silencing. Negatively regulates Hippo signaling pathway and antagonizes phosphorylation of YAP1. Acts as a transcriptional corepressor for SNAI1 and SNAI2/SLUG-dependent repression of E-cadherin transcription. Acts as a hypoxic regulator by bridging an association between the prolyl hydroxylases and VHL enabling efficient degradation of HIF1A. In podocytes, may play a role in the regulation of actin dynamics and/or foot process cytoarchitecture (By similarity). In the course of podocyte injury, shuttles into the nucleus and acts as a transcription regulator that represses WT1-dependent transcription regulation, thereby translating changes in slit diaphragm structure into altered gene expression and a less differentiated phenotype. Involved in the organization of the basal body (By similarity). Involved in cilia growth and positioning (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:A9LS46, ECO:0000269|PubMed:20303269, ECO:0000269|PubMed:20616046, ECO:0000269|PubMed:21834987, ECO:0000269|PubMed:22286099}.
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A6NJ46
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NKX63_HUMAN
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Homeobox protein Nkx-6.3
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MESNLQGTFLLNNTPLAQFPEMKAPVCQYSVQNSFYKLSPPGLGPQLAAGTPHGITDILSRPVAAPNNSLLSGYPHVAGFGGLSSQGVYYSPQVGNFSKAGNEYPTRTRNCWADTGQDWRGGRQCSNTPDPLSDSIHKKKHTRPTFTGHQIFALEKTFEQTKYLAGPERARLAYSLGMTESQVKVWFQNRRTKWRKKSALEPSSSTPRAPGGAGAGAGGDRAPSENEDDEYNKPLDPDSDDEKIRLLLRKHRAAFSVLSLGAHSV
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Putative transcription factor, which may be involved in patterning of central nervous system and pancreas.
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A6NJ78
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MET15_HUMAN
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12S rRNA N4-methylcytidine (m4C) methyltransferase (12S rRNA m4C methyltransferase) (EC 2.1.1.-) (Methyltransferase 5 domain-containing protein 1) (Methyltransferase-like protein 15)
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MLRYPYFCRMYKECLSCWLESGIPNLGVWPNRIHTTAEKYREYEAREQTDQTQAQELHRSQDRDFETMAKLHIPVMVDEVVHCLSPQKGQIFLDMTFGSGGHTKAILQKESDIVLYALDRDPTAYALAEHLSELYPKQIRAMLGQFSQAEALLMKAGVQPGTFDGVLMDLGCSSMQLDTPERGFSLRKDGPLDMRMDGGRYPDMPTAADVVNALDQQALASILRTYGEEKHAKKIASAIVQARSIYPITRTQQLASIVAGAFPPSAIYTRKDLLQRSTHIATKTFQALRIFVNNELNELYTGLKTAQKFLRPGGRLVALSFHSLEDRIVKRFLLGISMTERFNLSVRQQVMKTSQLGSDHENTEEVSMRRAPLMWELIHKKVLSPQDQDVQDNPRGRSAKLRAAIKL
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N4-methylcytidine (m4C) methyltransferase responsible for the methylation of position C839 in mitochondrial 12S rRNA. Involved in the stabilization of 12S rRNA folding, therefore facilitating the assembly of the mitochondrial small ribosomal subunits.
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A6NK06
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IRG1_HUMAN
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Cis-aconitate decarboxylase (CAD) (EC 4.1.1.6) (Aconitate decarboxylase) (Aconitate decarboxylase 1) (Cis-aconitic acid decarboxylase) (Immune-responsive gene 1 protein)
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MMLKSITESFATAIHGLKVGHLTDRVIQRSKRMILDTLGAGFLGTTTEVFHIASQYSKIYSSNISSTVWGQPDIRLPPTYAAFVNGVAIHSMDFDDTWHPATHPSGAVLPVLTALAEALPRSPKFSGLDLLLAFNVGIEVQGRLLHFAKEANDMPKRFHPPSVVGTLGSAAAASKFLGLSSTKCREALAIAVSHAGAPMANAATQTKPLHIGNAAKHGIEAAFLAMLGLQGNKQVLDLEAGFGAFYANYSPKVLPSIASYSWLLDQQDVAFKRFPAHLSTHWVADAAASVRKHLVAERALLPTDYIKRIVLRIPNVQYVNRPFPVSEHEARHSFQYVACAMLLDGGITVPSFHECQINRPQVRELLSKVELEYPPDNLPSFNILYCEISVTLKDGATFTDRSDTFYGHWRKPLSQEDLEEKFRANASKMLSWDTVESLIKIVKNLEDLEDCSVLTTLLKGPSPPEVASNSPACNNSITNLS
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Cis-aconitate decarboxylase that catalyzes production of itaconate and is involved in the inhibition of the inflammatory response. Acts as a negative regulator of the Toll-like receptors (TLRs)-mediated inflammatory innate response by stimulating the tumor necrosis factor alpha-induced protein TNFAIP3 expression via reactive oxygen species (ROS) in LPS-tolerized macrophages. Involved in antimicrobial response of innate immune cells ACOD1-mediated itaconic acid production contributes to the antimicrobial activity of macrophages by generating itaconate, leading to alkylation of proteins, such as TFEB. Involved in antiviral response following infection by flavivirus in neurons: ACOD1-mediated itaconate production inhibits the activity of succinate dehydrogenase, generating a metabolic state in neurons that suppresses replication of viral genomes (By similarity). Plays a role in the embryo implantation (By similarity).
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A6NK58
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LIPT2_HUMAN
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Putative lipoyltransferase 2, mitochondrial (EC 2.3.1.181) (Lipoate-protein ligase B) (Lipoyl/octanoyl transferase) (Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase)
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MRQPAVRLVRLGRVPYAELLGLQDRWLRRLQAEPGIEAPSGTEAGALLLCEPAGPVYTAGLRGGLTPEETARLRALGAEVRVTGRGGLATFHGPGQLLCHPVLDLRRLGLRLRMHVASLEACAVRLCELQGLQDARARPPPYTGVWLDDRKICAIGVRCGRHITSHGLALNCSTDLTWFEHIVPCGLVGTGVTSLSKELQRHVTVEEVMPPFLVAFKEIYKCTLISEDSPN
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Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes, which catalyze essential redox reactions. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate (By similarity). {ECO:0000250, ECO:0000269|PubMed:28757203}.
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A6NK89
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RASFA_HUMAN
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Ras association domain-containing protein 10
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MDPSEKKISVWICQEEKLVSGLSRRTTCSDVVRVLLEDGCRRRRRQRRSRRLGSAGDPHGPGELPEPPNEDDEDDDEALPQGMLCGPPQCYCIVEKWRGFERILPNKTRILRLWAAWGEEQENVRFVLVRSEASLPNAGPRSAEARVVLSRERPCPARGAPARPSLAMTQEKQRRVVRKAFRKLAKLNRRRQQQTPSSCSSTSSSTASSCSSSPRTHESASVERMETLVHLVLSQDHTIRQQVQRLHELDREIDHYEAKVHLDRMRRHGVNYVQDTYLVGAGIELDGSRPGEEPEEVAAEAEEAAAAPPLAGEAQAAALEELARRCDDLLRLQEQRVQQEELLERLSAEIQEELNQRWMRRRQEELAAREEPLEPDGGPDGELLLEQERVRTQLSTSLYIGLRLNTDLEAVKSDLDYSQQQWDSKKRELQGLLQTLHTLELTVAPDGAPGSGSPSREPGPQACADMWVDQARGLAKSGPGNDEDSDTGLSSMHSQDSDSLPMCESLV
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Plays an important role in regulating embryonic neurogenesis.
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A6NKB5
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PCX2_HUMAN
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Pecanex-like protein 2 (Pecanex homolog protein 2)
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MVSQVLQLLRQGVWAALTGGWYHDPEQSKFTNSCHLYLWLFLLLLPLALHLAFPPNAIIVFFYCSAVTIFFTIIKLVSYRLHLMFDKGEVIQQKPSRKEEKPNKDKEAKGEHITNHRNPSNNRQIHNGKKEEASRNLSTPPLRCSSRGQSITSHHSSGPLELSAQETVEDLKGVILLEDHPIAPVSSTSPGIKVESLPASQAHMLETTTKSVIPVKPVATETLINGKGKERGGKGQPPLRHRSEGGLVDKGPLKKLPHLSLSQYDLLETDVSFQPWGSENSVLIPEPVSCPRGSIRERVQSKSPQDSLSSSCPQCDTIVAKPVEEPADTSCQVDTSCQGDLPLHQEVDSSDSEVAVTLIDTSQPGDPLSLHEPIKIVITMSSTPNSMTDLESSLHLRVVGTEKTSVKSDAEPTNPGAAGSPNAEQISIPVITLDLPEGGGGGVPCPEGNGSERTPERLKTRVSTNQCSGYGSGEGGNAIKDHSSSSREPWESVSRLTPDTGSESKVGKEGQTNLDPSSCKSSHEKRHARVLSVDSGTDVFLSKSSAEIVNDTEKTMPTSKSDLEAKEGQMPNESNFLEFVSLLESINTSKMTASSQLNGSAEQNEESGLLRDNCSQEKKEEILENEKPSGHSSKQGKPDLQSQDHTSTGPACTQPAKTTAFFQGNRQRQIIYRVTSQQDSSVLQVISGPETSVQEEISVDAMHVFIDEHGEIRSCYLKSGNQKEGPLQPLPSNNDCLSQAREMQVSSSSTTTSESQDPSSGDPAVSALQQQLLLMVARRTQSETPRHVSQDLEASSCSSTQGKFNREQFYKFIIFPGKWIKVWYDRLTLLALLDRTEDIKENVLAILLIVLVSLLGFLTLSQGFCKDMWVLLFCLVMASCQYSLLKSVQPDPASPIHGHNQIITYSRPIYFCVLCGLILLLDTGAKARHPPSYVVYGLKLFSPVFLQSARDYLIVFLYCFPAISLLGLFPQINTFCTYLLEQIDMLFFGGSAVSGITSAVYSVARSVLAAALLHAVCFSAVKEPWSMQHIPALFSAFCGLLVALSYHLSRQSSDPSVLMSFIQCRLFPKFLHQNLAESAADPLPKKMKDSVTDVLKWDLIVCAVVAVLSFAVSASTVFLSLRPFLSIVLFALAGAVGFVTHYVLPQLRKHHPWMWISHPILKNKEYHQREVRDVAHLMWFERLYVWLQCFEKYILYPALILNALTIDAFLISNHRRLGTHWDIFLMIIAGMKLLRTSFCNPVYQFINLSFTVIFFHFDYKDISESFLLDFFMVSILFSKLGDLLHKLQFVLTYVAPWQMAWGSSFHVFAQLFAIPHSAMLFFQTIATSIFSTPLSPFLGSVIFITSYVRPVKFWEKNYNTRRVDNSNTRLAVQIERDPGNDDNNLNSIFYEHLTRTLQESLCGDLVLGRWGNYSSGDCFILASDDLNAFVHLIEIGNGLVTFQLRGLEFRGTYCQQREVEAIMEGDEEDRGCCCCKPGHLPHLLSCNAAFHLRWLTWEITQTQYILEGYSILDNNAATMLQVFDLRRILIRYYIKSIIYYMVTSPKLLSWIKNESLLKSLQPFAKWHYIERDLAMFNINIDDDYVPCLQGITRASFCNVYLEWIQHCARKRQEPSTTLDSDEDSPLVTLSFALCTLGRRALGTAAHNMAISLDSFLYGLHVLFKGDFRITARDEWVFADMDLLHKVVAPAIRMSLKLHQDQFTCPDEYEDPAVLYEAIQSFEKKVVICHEGDPAWRGAVLSNKEELLTLRHVVDEGADEYKVIMLHRSFLSFKVIKVNKECVRGLWAGQQQELIFLRNRNPERGSIQNNKQVLRNLINSSCDQPLGYPMYVSPLTTSYLGTHRQLKNIWGGPITLDRIRTWFWTKWVRMRKDCNARQHSGGNIEDVDGGGAPTTGGNNAPSGGSQESSAEQPRKGGAQHGVSSCEGTQRTGRRKGRSQSVQAHSALSQRPPMLSSSGPILESRQTFLQTSTSVHELAQRLSGSRLSLHASATSLHSQPPPVTTTGHLSVRERAEALIRSSLGSSTSSTLSFLFGKRSFSSALVISGLSAAEGGNTSDTQSSSSVNIVMGPSARAASQATRHLSEPCEPPDATEQGQLHDRCLAEAVADTLGVVCRRASQEDMGLDDTASQQSVSDEQ
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May play a role in tumorigenesis of colorectal carcinomas with high microsatellite instability (MSI-H).
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A6NL88
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SHSA7_HUMAN
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Protein shisa-7 (Cystine-knot AMPAR modulating protein of 59 kDa) (CKAMP59) (GABA(A) receptor auxiliary subunit Shisa7) (Protein shisa-6-like)
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MPALLLLVLLASSAGQARARPSNATSAEPAGPLPALLAHLRRLTGALTGGGGAASPGANGTRTGPAGGAGAAARAPPPAELCHGYYDVMGQYDATFNCSTGSYRFCCGTCHYRFCCEHRHMRLAQASCSNYDTPRWATTPPPLAGGAGGAGGAGGGPGPGQAGWLEGGRTGGAGGRGGEGPGGSTAYVVCGVISFALAVGVGAKVAFSKASRAPRAHRDINVPRALVDILRHQAGPGTRPDRARSSSLTPGIGGPDSMPPRTPKNLYNTVKTPNLDWRALPPPSPSLHYSTLSCSRSFHNLSHLPPSYEAAVKSELNRYSSLKRLAEKDLDEAYLKRRPLELPRGTLPLHALRRPGTGGGYRMEAWGGPEELGLAPAPNPRRVMSQEHLLGDGGRSRYEFTLPRARLVSQEHLLLSSPEALRQSREHLLSPPRSPALPPDPTARASLAASHSNLLLGPGGPPTPLRGLPPPSSLHAHHHHALHGSPQPAWMSDAGGGGGTLARRPPFQRQGTLEQLQFIPGHHLPQHLRTASKNEVTV
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Transmembrane protein that regulates gamma-aminobutyric acid type A receptor (GABA(A)R) trafficking, channel deactivation kinetics and pharmacology, necessary for fast inhibitory transmission in the brain. Enhances the action of benzodiazepine, a primary GABA(A)Rs target drug, in the brain. May affect channel kinetics of AMPA-type glutamate receptors (AMPAR), the brain's main excitatory neurotransmitter, necessary for synaptic hippocampal plasticity, and memory recall. May regulate the induction and maintenance of long-term potentiation at Schaffer collaterals/CA3-CA1 excitatory synapses.
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A6NMY6
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AXA2L_HUMAN
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Putative annexin A2-like protein (Annexin A2 pseudogene 2) (Lipocortin II pseudogene)
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MSTVHEILCKLSLEGDHSTPPSAYGSVKAYTNFDAERDALNIETAIKTKGVDEVTIVNIVTNRDNAQRQDIVFSYQRRTKKELASALKSALSGHLETVILGLLKTPAQYDASELKASMKGLGTDEDSLIEIICSRTNQELQEINRVYKEMYKTDLEKDIISDTSGDFRKLMVALAKGRRAEDGSVIDYELIDQDAQDLYDAGVKRKGTDVPKWISIMTERSVPHLQKVFDRYKSYSPYDMLESIRKEVKGDLENAFLNLVQRIQNKPLYFADQLYDSMKGKGTRDKVLIRIMVSRSEVDMLKIRSEFKRKYGKSLYYYIQQDTKGDYQKALLYLCGGDD
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Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response.
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A6NMZ7
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CO6A6_HUMAN
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Collagen alpha-6(VI) chain
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MMLLILFLVIICSHISVNQDSGPEYADVVFLVDSSDRLGSKSFPFVKMFITKMISSLPIEADKYRVALAQYSDKLHSEFHLSTFKGRSPMLNHLRKNFGFIGGSLQIGKALQEAHRTYFSAPANGRDKKQFPPILVVLASSESEDNVEEASKALRKDGVKIISVGVQKASEENLKAMATSQFHFNLRTVRDLSMFSQNMTHIIKDVIKYKEGAVDDIFVEACQGPSMADVVFLLDMSINGSEENFDYLKGFLEESVSALDIKENCMRVGLVAYSNETKVINSLSMGINKSEVLQHIQNLSPRTGKAYTGAAIKKLRKEVFSARNGSRKNQGVPQIAVLVTHRDSEDNVTKAAVNLRREGVTIFTLGIEGASDTQLEKIASHPAEQYVSKLKTFADLAAHNQTFLKKLRNQITHTVSVFSERTETLKSGCVDTEEADIYLLIDGSGSTQATDFHEMKTFLSEVVGMFNIAPHKVRVGAVQYADSWDLEFEINKYSNKQDLGKAIENIRQMGGNTNTGAALNFTLSLLQKAKKQRGNKVPCHLVVLTNGMSKDSILEPANRLREEHIRVYAIGIKEANQTQLREIAGEEKRVYYVHDFDALKDIRNQVVQEICTEEACKEMKADIMFLVDSSGSIGPENFSKMKTFMKNLVSKSQIGPDRVQIGVVQFSDINKEEFQLNRFMSQSDISNAIDQMAHIGQTTLTGSALSFVSQYFSPTKGARPNIRKFLILITDGEAQDIVKEPAVVLRQEGVIIYSVGVFGSNVTQLEEISGRPEMVFYVENFDILQRIEDDLVFGICSPREECKRIEVLDVVFVIDSSGSIDYDEYNIMKDFMIGLVKKADVGKNQVRFGALKYADDPEVLFYLDDFGTKLEVISVLQNDQAMGGSTYTAEALGFSDHMFTEARGSRLNKGVPQVLIVITDGESHDADKLNATAKALRDKGILVLAVGIDGANPVELLAMAGSSDKYFFVETFGGLKGIFSDVTASVCNSSKVDCEIDKVDLVFLMDGSTSIQPNDFKKMKEFLASVVQDFDVSLNRVRIGAAQFSDTYHPEFPLGTFIGEKEISFQIENIKQIFGNTHIGAALREVEHYFRPDMGSRINTGTPQVLLVLTDGQSQDEVAQAAEALRHRGIDIYSVGIGDVDDQQLIQITGTAEKKLTVHNFDELKKVNKRIVRNICTTAGESNCFVDVVVGFDVSTQEKGQTLLEGQPWMETYLQDILRAISSLNGVSCEVGTETQVSVAFQVTNAMEKYSPKFEIYSENILNSLKDITVKGPSLLNANLLDSLWDTFQNKSAARGKVVLLFSDGLDDDVEKLEQKSDELRKEGLNALITVALDGPADSSDLADLPYIEFGKGFEYRTQLSIGMRELGSRLSKQLVNVAERTCCCLFCKCIGGDGTMGDPGPPGKRGPPGFKGSEGYLGEEGIAGERGAPGPVGEQGTKGCYGTKGPKGNRGLNGQEGEVGENGIDGLNGEQGDNGLPGRKGEKGDEGSQGSPGKRGTPGDRGAKGLRGDPGAPGVDSSIEGPTGLKGERGRQGRRGWPGPPGTPGSRRKTAAHGRRGHTGPQGTAGIPGPDGLEGSLGLKGPQGPRGEAGVKGEKGGVGSKGPQGPPGPGGEAGNQGRLGSQGNKGEPGDLGEKGAVGFPGPRGLQGNDGSPGYGSVGRKGAKGQEGFPGESGPKGEIGDPGGPGETGLKGARGKMISAGLPGEMGSPGEPGPPGRKGVKGAKGLASFSTCELIQYVRDRSPGRHGKPECPVHPTELVFALDHSRDVTEQEFERMKEMMAFLVRDIKVRENSCPVGAHIAILSYNSHARHLVRFSDAYKKSQLLREIETIPYERSSASREIGRAMRFISRNVFKRTLPGAHTRKIATFFSSGQSADAHSITTAAMEFGALEIIPVVITFSNVPSVRRAFAIDDTGTFQVIVVPSGADYIPALERLQRCTFCYDVCKPDASCDQARPPPVQSYMDAAFLLDASRNMGSAEFEDIRAFLGALLDHFEITPEPETSVTGDRVALLSHAPPDFLPNTQKSPVRAEFNLTTYRSKRLMKRHVHESVKQLNGDAFIGHALQWTLDNVFLSTPNLRRNKVIFVISAGETSHLDGEILKKESLRAKCQGYALFVFSLGPIWDDKELEDLASHPLDHHLVQLGRIHKPDHSYGVKFVKSFINSIRRAINKYPPINLKIKCNRLNSIDPKQPPRPFRSFVPGPLKATLKEDVLQKAKFFQDKKYLSRVARSGRDDAIQNFMRSTSHTFKNGRMIESAPKQHD
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Collagen VI acts as a cell-binding protein.
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A6NNB3
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IFM5_HUMAN
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Interferon-induced transmembrane protein 5 (Bone-restricted interferon-induced transmembrane protein-like protein) (BRIL) (Dispanin subfamily A member 1) (DSPA1)
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MDTAYPREDTRAPTPSKAGAHTALTLGAPHPPPRDHLIWSVFSTLYLNLCCLGFLALAYSIKARDQKVVGDLEAARRFGSKAKCYNILAAMWTLVPPLLLLGLVVTGALHLARLAKDSAAFFSTKFDDADYD
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Required for normal bone mineralization.
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A6NNM8
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TTL13_HUMAN
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Tubulin polyglutamylase TTLL13 (EC 6.3.2.-) (Tubulin tyrosine ligase like 13) (Tubulin tyrosine ligase-like family member 13 pseudogene) (Tubulin--tyrosine ligase-like protein 13)
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MEPSTCRTMESEEDYVEEKESEKCVKEGVTNPSNSSQQALLKADYKALKNGVPSPIMATKIPKKVIAPVDTGDLEAGRRKRRRKRRSLAINLTNCKYESVRRAAQMCGLKEVGEDEEWTLYWTDCAVSLERVMDMKRFQKINHFPGMTEICRKDLLARNLNRMYKLYPSEYNIFPRTWCLPADYGDFQSYGRQRKARTYICKPDSGCQGRGIFITRNPREIKPGEHMICQQYISKPLLIDGFKFDMRVYVLITSCDPLRIFTYEEGLARFATTPYMEPSHNNLDNVCMHLTNYAINKHNENFVRDGAVGSKRKLSTLNIWLQEHSYNPGELWGDIEDIIIKTIISAHSVLRHNYRTCFPQYLNGGTCACFEILGFDILLDHKLKPWLLEVNHSPSFTTDSCLDQEVKDALLCDAMTLVNLRGCDKRKVMEEDKRRVKERLFQCYRQPRESRKEKTESSHVAMLDQERYEDSHLGKYRRIYPGPDTEKYARFFKHNGSLFQETAASKAREECARQQLEEIRLKQEQQETSGTKRQKARDQNQGESAGEKSRPRAGLQSLSTHLAYRNRNWEKELLPGQLDTMRPQEIVEEEELERMKALLQRETLIRSLGIVEQLTRLQHPGPQGQKKLHESRDRLGSQELKSMSLVLLVLLRGAATEQGAPHFLHPVLPHESIPRILGALPSMNAAIPHVPRYHLQPKNFNWTGEPAAINSCSLSMKKAGRCYFSSARIRLTSQGQASRRLEAINRVLAGSVPPTLTPKQGYFLQPERVASDSWTECTLPSMVNSEHRAAKVPLCPASAPMLQRSRALLNINQFR
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Polyglutamylase which modifies tubulin, generating polyglutamate side chains of variable lengths on the gamma-carboxyl group of specific glutamate residues within the C-terminal tail of tubulin. Mediates ATP-dependent polyglutamate side-chain elongation of the polyglutamylation reaction but not the initiation step. Preferentially modifies the alpha-tubulin tail over a beta-tail.
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A6NNY8
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UBP27_HUMAN
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Ubiquitin carboxyl-terminal hydrolase 27 (EC 3.4.19.12) (Deubiquitinating enzyme 27) (Ubiquitin carboxyl-terminal hydrolase 22-like) (Ubiquitin thioesterase 27) (Ubiquitin-specific-processing protease 27) (X-linked ubiquitin carboxyl-terminal hydrolase 27)
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MCKDYVYDKDIEQIAKEEQGEALKLQASTSTEVSHQQCSVPGLGEKFPTWETTKPELELLGHNPRRRRITSSFTIGLRGLINLGNTCFMNCIVQALTHTPILRDFFLSDRHRCEMPSPELCLVCEMSSLFRELYSGNPSPHVPYKLLHLVWIHARHLAGYRQQDAHEFLIAALDVLHRHCKGDDVGKAANNPNHCNCIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISLDLPGSCTSFWPMSPGRESSVNGESHIPGITTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMNKLPVVACFHFKRFEHSAKQRRKITTYISFPLELDMTPFMASSKESRMNGQLQLPTNSGNNENKYSLFAVVNHQGTLESGHYTSFIRHHKDQWFKCDDAVITKASIKDVLDSEGYLLFYHKQVLEHESEKVKEMNTQAY
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Deubiquitinase involved in innate antiviral immunity by mediating deubiquitination of CGAS and RIGI. Negatively regulates RIGI by mediating 'Lys-63'-linked deubiquitination of RIGI, inhibiting type I interferon signaling. Also regulates 'Lys-63'-linked ubiquitination level of MDA5/IFIH1. Acts as a positive regulator of the cGAS-STING pathway by catalyzing 'Lys-48'-linked deubiquitination of CGAS, thereby promoting its stabilization. Can reduce the levels of BCL2L11/BIM ubiquitination and stabilize BCL2L11 in response to the RAF-MAPK-degradation signal (By similarity). By acting on BCL2L11 levels, may counteract the anti-apoptotic effects of MAPK activity (By similarity).
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