entry
stringlengths 6
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| entry_name
stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
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E7FI45
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ACDA1_PYRFU
|
Acetate--CoA ligase [ADP-forming] I subunit alpha (EC 6.2.1.13) (ADP-forming acetyl coenzyme A synthetase I subunit alpha) (ACS I subunit alpha)
|
MSLEALFNPKSVAVIGASAKPGKIGYAIMKNLIEYGYEGKIYPVNIKGGEIEINGRKFKVYKSVLEIPDEVDMAVIVVPAKFVPQVLEECGQKGVKVVPIISSGFGELGEEGKKVEQQLVETARKYGMRILGPNIFGVVYTPAKLNATFGPTDVLPGPLALISQSGALGIALMGWTILEKIGLSAVVSVGNKADIDDADLLEFFKDDENTRAILIYMEGVKDGRRFMEVAKEVSKKKPIIVIKAGRSERGAKAAASHTGSLAGSDKVYSAAFKQSGVLRAYTIGEAFDWARALSNLPEPQGDNVVIITNGGGIGVMATDAAEEEGLHLYDNLEELKIFANHMPPFGSYKNPVDLTGMADGKSYEGAIRDALAHPEMHSIAVLYCQTAVLDPRELAEIVIREYNESGRKKPLVVAIVGGIEAKEAIDMLNENGIPAYPEPERAIKALSALYKWSKWKAKHKEK
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Catalyzes the reversible formation of acetate and ATP from acetyl-CoA by using ADP and phosphate. Can use other substrates such as isobutyryl-CoA, propionyl-CoA and butyryl-CoA, but not indoleacetyl-CoA, phenylacetyl-CoA or succinyl-CoA. Seems to be involved primarily in the conversion of acetyl-CoA to acetate. Participates in the degradation of branched-chain amino acids via branched-chain-acyl-CoA esters.
|
E7FKV8
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PK1L1_ORYLA
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Polycystin-1-like protein 1 (Polycystin-1L1) (Polycystic kidney disease 1-like 1) (Protein abecobe)
|
MFCLWIFSLAFLHLHLCSVSSSSLEGSGFFVGWINASSLQLFASIGGCDLSPCMDEGQEGMEALYRSEEPFQCSIRASASPGRRQAGRTCVRKVPGNLAVHCHLLSENEGLEEEDLLRITVMTPRGQSSLQVNVSHGGLLTACSDWIWNTSEKHKNNVPASGLHLGISLEVPCCTSCTRFGSDSELVEEQCSALHVSVSDVLVKDYICCLTPRDKDKTLNRTETPCLYSSNSLKDSLVRGRVYQMSFEECFRWHLLVVLLMLEAQYNHSQEVHEDPSSTVKLCDYAVRIHAEKQAYSTNTDIPLLAVVDILDPVEFLWDFGDFTSARANSRTITKRYTNPGIYKLVVVASWGQMSVRSHVLSLVVQRAVKLNRLVHEPSVLQNHTVTVSCRVNVGTNLTFLWNFGDGTVRTGLSTEQHVFTRTGEFRVMVIASNLVSSASLSSYLFVVDRPCQPPPVKNLGPPNIQVRRNEVVFLGVTFESELNCNVSRELHYSWTVYDSAGLTFPLPLTNTHRQSLVLQSYTLPYGIYKAIARVQIVGSVVYSNYSVRLQVVPNSVVVVIQGGTNIYVNTKSSNEVTLDGQASYDPDFPLNPLRYSWTCQPVSTISSSCFSQSIPTSYPVLKFPTSLLKSNFDQFKFTLTVHSGERSASSEIFLTLTSHLAGKLFVHCPECQGDQVSWDQSFSVRAECEDCNVSAEFIQYSWSLFRVNASSKPVAEIPFCYTVDLNAPSAVLENASTPTPAPEMSPSHHFNADWTRFTEDSLASSSPSRIYKSKNRNSELTDSPVSSVTVGFSGSESFNGPPGVDRGSSQFSNFPGQRDMFSEFQSDPESSAEWEFTFPYLESEDLRGQRGDSRVPFPRPEEGDPGISAGRPKETDMESFPSDSDSFSHSSSNKGEGSNLVDPRPSVRLQKPGLLDLHRDSVDKSLFESYTYTGISSCFLSFRSFSLKPSSTYMLELTAKSQRRFYGQTQLFLKVKPVPKGVACQVQPVRGIELYTHFSIFCTSGREDLIYTYSFSVGGRMPRILYQGRDFLYYFSLPSGDPTDDYKVIIYTEIRSSMYGSAKKLCPVTVRVEPSFVRNASSSYSHHEPDLMISDSGLRNVSVLVQLGNIAEIYNYISLLSTILNRLSLDSQANTHALKHLRNVLICIVCKLEYSAQASPADGIFILNELLRVTSQVTVQSARWVTAHVGALSVQFSESNRSILSALVSLLSSSLQVVTSSPETSDSADSPQPLESHLVTGKSRNAFVDDADHCITDLSETTYNKQSEPVPKRLMMRLVNDLLQTTSDLMLRNFDLQKTKELQVQSDLITLCAGFLNKTSTAINCGLITFFLPASLIKMLLLHDGISAKRGFSQREQPSCVQRIGMELLHNPYEWGRYPIQLKGPVADLSLYSCKTRRKIPVHSFLQPITVELRHPQKTSSMSEYTLLRSQINYHNFSITQEHLQQAVQVTVVFTAPPHMAFPVKILFRMFERPTPSMHHLHRLLNWRNNTILLTLPPSYLSAAGVGHLALLDANFGKTPTRRHLAEQISYSLTVESSLCLSWEDQQGSWTQNGCRAQTNDKTSAVNCSCHHLKPLKVLQQQIQSSHFRADLDQFLSVSRDLTVVFVLLLCVSLNIPVLVWCKKTDATSEENNRAHFLPDNSATDQHFYAVTVHTGLCSAARMSARVYVVLHGEDGCSQTKELHVPGCTLFRRNSQNTFILSVADSLGSVQGVHIWHNNSGPSPEWYLKQVQVSELMPGHMEGRSWQFISQCWLAVNKGDGQVERMLRVSTHGLTFSKMLFLKLFEYMPDYHIWMSVYTCPSPHLFTRAQRLCVCLLLFLGYACVNIIITHQRDDQLPFDLGVIDVTSVSIATGLVSVVAVLPVAMVISFLFRVKSGRMTLENYDNVFSKRPSGKTKYQDTDFLSVSTTNLENKDADDKEAVTPQRNKRRKDSVSFESIHELLFQEVLQVSRRRSLFLKKSKGNDSELSPQSSEFCGALKATKNEAQSVRVKRRYRLASLLYHCVAWTLCLLFCLSCLILSAVLGTRLNSGKILHWIHSLFVSLTFCFFVIHPATILVLAAVVSWRFKRSQDFHCFFNKMNSHLEDLKHQDPDQLRPSAFTRTRAPNAEKILEARQRARYLRRVHPPTRAELRKTRTKRKKQAVIHKMLRDLCLCGSMFFLMVCITYGSPVDEHYPLNAAFRRHFIRAHGDDFMSIKKYEDWWKWAQTSLLSSLYYNESENPQMSFISIGAPLVQKTEVCGTFHSQVSMVTPPRPRYHTGSSSKQEVTVGLGYTRSEGASKLRLLHLSGWLSEQTVALKVQFSLYSPAPNLFSSVTLLSEQSSTGLLQSSATVQSVRLYHSPSMLDYTVMVWQLLFLLLSLVNLYHQTSTAAQHGLMGYWKTTSISVEVSLVIVSLVYYVHYVYHPTMVMEVAEQLRRNHREHVDVSTLANSEQFSRTLRGIILFLLAVKCVTVVRLNRILAPSMPLLSLSSLLWPAISGLLLLSIFSCMGRLLYIERTFHSIQTVLWHFWSLRKSRDLISLWRDFYYFGLLYASSAMLTTMVFAVMIRKAKRSPSTKNDPTIREVLGCISQKFTGMKTQIPDCHTQKTYFLEECESLVDELLFKLNALSNSLHHTLPPKLHTYTDKDSPDASSTTELCKERLQDLVRSLSVGQGEAALTFPHDRSLLELQEEEEVKHQEGRCSVGCKESRLPETLWTADYRESMDEHWTEKKSSNGLGGATYSHVVVVEALVHHEQGTKN
|
Component of a ciliary calcium channel that controls calcium concentration within cilia without affecting cytoplasmic calcium concentration. Forms a heterodimer with pkd2l1 in cilia and forms a calcium-permeant ciliary channel that regulates sonic hedgehog/SHH signaling and gli2 transcription. Does not constitute the pore-forming subunit (By similarity). Also involved in left/right axis specification downstream of nodal flow: forms a complex with pkd2 in cilia to facilitate flow detection in left/right patterning. {ECO:0000250, ECO:0000269|PubMed:21307098}.
|
E8MGH8
|
HYBA1_BIFL2
|
Non-reducing end beta-L-arabinofuranosidase (EC 3.2.1.185) (Beta-L-arabinofuranosidase) (Beta-AFase)
|
MNVTITSPFWKRRRDQIVESVIPYQWGVMNDEIDTTVPDDPAGNQLADSKSHAVANLKVAAGELDDEFHGMVFQDSDVYKWLEEAAYALAYHPDPELKALCDRTVDLIARAQQSDGYLDTPYQIKSGVWADRPRFSLIQQSHEMYVMGHYIEAAVAYHQVTGNEQALEVAKKMADCLDANFGPEEGKIHGADGHPEIELALAKLYEETGEKRYLTLSQYLIDVRGQDPQFYAKQLKAMNGDNIFHDLGFYKPTYFQAAEPVRDQQTADGHAVRVGYLCTGVAHVGRLLGDQGLIDTAKRFWKNIVTRRMYVTGAIGSTHVGESFTYDYDLPNDTMYGETCASVAMSMFAQQMLDLEPKGEYADVLEKELFNGSIAGISLDGKQYYYVNALETTPDGLDNPDRHHVLSHRVDWFGCACCPANIARLIASVDRYIYTERDGGKTVLSHQFIANTAEFASGLTVEQRSNFPWDGHVEYTVSLPASATDSSVRFGLRIPGWSRGSYTLTVNGKPAVGSLEDGFVYLVVNAGDTLEIALELDMSVKFVRANSRVRSDAGQVAVMRGPLVYCAEQVDNPGDLWNYRLADGVTGADAAVAFQADLLGGVDTVDLPAVREHADEDDAPLYVDADEPRAGEPATLRLVPYYSWANREIGEMRVFQRR
|
Beta-L-arabinofuranosidase that removes the beta-L-arabinofuranose residue from the non-reducing end of various substrates, including beta-L-arabinofuranosyl-hydroxyproline (Ara-Hyp), Ara-beta-1,2-Ara-beta-Hyp (Ara(2)-Hyp), Ara-beta-1,2-Ara-beta-1,2-Ara-beta-Hyp (Ara(3)-Hyp), and beta-L-arabinofuranosyl-(1->2)-1-O-methyl-beta-L-arabinofuranose. In the presence of 1-alkanols, shows transglycosylation activity, retaining the anomeric configuration of the arabinofuranose residue.
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E8PLM2
|
OLD_THESS
|
OLD nuclease (EC 3.1.11.3) (Exodeoxyribonuclease OLD) (Overcoming lysogenization defect) (Old)
|
MLKRLQVKNFRCLEDIDLPLGPLTAIVGPNGAGKTTILRAIDLVLGDVWPSLRSFRIPQDFINFDTTRAIEITVHFDPPYTQGSFNITAFRLTCKGEDADFHVDLEPLDEGGNVPRYPSGNPLRVGTDMRNHARVLFLDHRRNLAQHLPSIRGSILGRLLQPVRREFKLQDNFKQVYEQAMDLLRTEQVKQIEKTIAETAKQMLGFLGKDAMKSMEIGFGFADPANPFNSLRLQYRESDLTLPGDELGLGIQSAIVVGIFEAFRQLGEKIGTVIIEEPEMYLHPQAQRYFYRLLCEMADKDQCQIIYSTHSPIFADVNRFEALRLVRKDRDDRVVVSYVREEDKSALDNVRNRFKLGGRFDTARNEVLFAKRALLVEGYGDRVAALQLFNQLEVDPDAECIAVVDCGGKAGIELIVGVCKALDIPFVVVHDEDVWPIDERADEETRRKQEQENKAEQEKNQRIQACAGAERVFVVQPSLEAALGIGRNASDKPYRIAEILKTVDVGQPPDALRPFVEAIRQVTRPMEE
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An exodeoxyribonuclease that degrades linear or supercoiled dsDNA from 5'-3'. Nicks and linearizes circular DNA. Activity is not stimulated by ATP or AMP-PNP, although it has DNA-stimulated ATPase activity.
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E8WYN5
|
MDL_GRATM
|
(R)-mandelonitrile lyase (EC 4.1.2.10) (Hydroxynitrile lyase) (GtHNL)
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MEIKRVGSQASGKGPADWFTGTVRIDPLFQAPDPALVAGASVTFEPGARTAWHTHPLGQTLIVTAGCGWAQREGGAVEEIHPGDVVWFSPGEKHWHGAAPTTAMTHLAIQERLDGKAVDWMEHVTDEQYRR
|
Hydroxynitrile lyase which catalyzes mandelonitrile formation from benzaldehyde and hydrogen cyanide with high stereoselectivity in presence of manganese.
|
E9AE57
|
FUM2_LEIMA
|
Fumarate hydratase 2 (Fumarase 2) (LmFH-2) (EC 4.2.1.2)
|
MSLCDQCEIGCRRVGIKDIEDASAVNADFHFSAIFQPTDPHHHQTEFAKVEGSEKYVEEVEVFGRQALKVNPEALTILAHRAFSDVHHFFRKDHLEGWRRAIEDPEASDNDRYVATTLLKNACIAAGRVLPSCQDTGTAIVLGKRGELCWTGGEDEKYLSKGIWNAYRYHNLRYSQTAALDMFKECNTGDNLPAQLDLLAVPGSDYEFLFIAKGGGSANKAYLYQETKALLNPKSLRAFIEEKLKTLGTAACPPYHIALVIGGTSAEMTMKTVKLASCRYYDSLPTTGDKYGRAFRDPEWEKIVMEVAQKSGIGAQFGGKYFAHQARVIRLPRHGASCPVGLAVSCSADRQILAHINKSGIYIEQLEQNPAQYLPDIPEVHLSTTSVKVDLKRPIDKVRQQLSQYPVGTRVMLNGTLIVARDIAHAKIKEMMDNGEPLPEYMKTSPIYYAGPAKTPEGYASGSFGPTTAGRMDSYVDLFQSHGGSYITLAKGNRSKQVTDACKKHGGFYLGSIGGPAAILAKDSIKQVTCLAFPELGMEAVWKIEVEDFPAFIVVDDKGNDMYSKTLA
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Cytosolic fumarate hydratase that catalyzes the reversible hydration of fumarate to (S)-malate.
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E9F5E9
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SUBD_METRA
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Geranylgeranyl pyrophosphate synthase subD (GGPP synthase) (GGPPSase) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Farnesyltranstransferase) (EC 2.5.1.29) (Geranylgeranyl diphosphate synthase) (Geranyltranstransferase) (EC 2.5.1.10) (Subglutinol biosynthesis cluster protein D)
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MSPSAPNTNELNSPVLETQPLAGDAALLHSSIAAGYEEIIRAPFDYLLNLPGKDVRSKMISAFNEWLCIPADKLEVIKRIVMLLHNASLLIDDIQDSSKLRRGLPVSHHIFGVPQTINAANYAYFLAQQELPKLGDPKAFEIYTEELLSLHRGQGMDIYWREASKCPTEEEYFSMVSHKTGGLFRLAIRLMQLASDKNWFVFHTRDFVPLVNVLGVIFQIRDDYLNLQSHAYTVNKGFGEDLTEGKYSFPIIHSIRSDPTNIQLSSILKQRTTDVDVKLFAVECIKATGSFEHCKEKIAELVAEARQLIKEMGNSVPGSAEAVDRVLDLIGLEPESS
|
Geranylgeranyl pyrophosphate synthase part of the gene cluster that mediates the biosynthesis of the immunosuppressants subglutinols, meroterpenoids consisting of an alpha-pyrone (4-hydroxy-5,6-dimethyl-2-pyrone) moiety attached to a decalin core fused to a five-membered cyclic ether carrying a prenylside chain. The first step of the pathway is the synthesis of the alpha-pyrone moiety by the polyketide synthase subA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations. The alpha-pyrone is then combined with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase subD through the action of the prenyltransferase subC to yield a linear alpha-pyrone diterpenoid. Subsequent steps in the subglutinol biosynthetic pathway involve the decalin core formation, which is thought to be initiated by the epoxidation of the C10-C11 olefin by the FAD-dependent oxidoreductase subE (Probable). The following cyclization cascade would be catalyzed by the terpene cyclase subB (Probable). Lastly, the FAD-dependent dehydrogenase subF probably catalyzes the five-membered cyclic ether formation to complete the formation of subglutinol A (Probable). Subsequent redox reactions appear to give rise to subglutinol C and D, however, it remains unclear which enzymes are responsible for these transformations (Probable). SubD may have secondary function in the conversion of the identified subglutinols to subglutinol analog 45, which seems to be the major product of the cluster.
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E9L7A5
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PAT_PETHY
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Bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase (PhPPA-AT) (EC 2.6.1.1) (EC 2.6.1.78) (EC 2.6.1.79)
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MAATTTTSSSSRIAYSRHNIPGLHSDSLNPKSISFSSNLHTFSLKSSGSRRQLYSRRTGAVVIMQSMDKVEVDISLSPRVNSVKPSKTVAITDQATALVQAGVPVIRLAAGEPDFDTPAPIVEAGINAIREGHTRYTPNAGTMELRSAISHKLKEENGLSYTPDQILVSNGAKQSIIQAVLAVCSPGDEVLIPAPYWVSYPEMARLADATPVILPTSISEDFLLDPKLLESKLTEKSRLLILCSPSNPTGSVYPRKLLEQIAEIVARHPRLLVISDEIYEHIIYAPATHTSFASLPGMWDRTLTVNGFSKAFAMTGWRLGYIAGPKHFIAACNKIQSQFTSGASSISQKAAVAALGLGYAGGELVATMVKSFRERRDYLVKSFGEIEGVKISEPRGAFYLFIDLSSYYGVEVDGFGSINNSESLCRYLLDKAQVALVPGDAFGDDTCIRISYAASLSTLQAAVERIKKALVTIKPPVPV
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Prokaryotic-type aspartate aminotransferase. Has also a prenate transaminase activity. Involved in the aromatic amino acids biosynthesis pathway via the arogenate route. Required for the transamination of prephenate into arogenate. Can use 2-oxoglutarate, oxaloacetate and prephenate as substrates, but not phenylpyruvate or 4-hydroxyphenylpyruvate.
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E9LVH9
|
PETH2_THECS
|
Cutinase 2 (EC 3.1.1.74) (Poly(ethylene terephthalate) hydrolase) (PET hydrolase) (PETase) (EC 3.1.1.101)
|
MANPYERGPNPTDALLEARSGPFSVSEERASRFGADGFGGGTIYYPRENNTYGAVAISPGYTGTQASVAWLGERIASHGFVVITIDTNTTLDQPDSRARQLNAALDYMINDASSAVRSRIDSSRLAVMGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKNWSSVRVPTLIIGADLDTIAPVLTHARPFYNSLPTSISKAYLELDGATHFAPNIPNKIIGKYSVAWLKRFVDNDTRYTQFLCPGPRDGLFGEVEEYRSTCPF
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Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (Ref.1). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (Ref.1, PubMed:23592055). Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world (Ref.1, PubMed:23592055). Capable of degrading the bioplastic poly(lactic acid) (PLLA).
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E9NA96
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IR25A_DROME
|
Ionotropic receptor 25a
|
MILMNPKTSKILWLLGFLSLLSSFSLEIAAQTTQNINVLFINEVDNEPAAKAVEVVLTYLKKNIRYGLSVQLDSIEANKSDAKVLLEAICNKYATSIEKKQTPHLILDTTKSGIASETVKSFTQALGLPTISASYGQQGDLRQWRDLDEAKQKYLLQVMPPADIIPEAIRSIVIHMNITNAAILYDDSFVMDHKYKSLLQNIQTRHVITAIAKDGKREREEQIEKLRNLDINNFFILGTLQSIRMVLESVKPAYFERNFAWHAITQNEGEISSQRDNATIMFMKPMAYTQYRDRLGLLRTTYNLNEEPQLSSAFYFDLALRSFLTIKEMLQSGAWPKDMEYLNCDDFQGGNTPQRNLDLRDYFTKITEPTSYGTFDLVTQSTQPFNGHSFMKFEMDINVLQIRGGSSVNSKSIGKWISGLNSELIVKDEEQMKNLTADTVYRIFTVVQAPFIMRDETAPKGYKGYCIDLINEIAAIVHFDYTIQEVEDGKFGNMDENGQWNGIVKKLMDKQADIGLGSMSVMAEREIVIDFTVPYYDLVGITIMMQRPSSPSSLFKFLTVLETNVWLCILAAYFFTSFLMWIFDRWSPYSYQNNREKYKDDEEKREFNLKECLWFCMTSLTPQGGGEAPKNLSGRLVAATWWLFGFIIIASYTANLAAFLTVSRLDTPVESLDDLAKQYKILYAPLNGSSAMTYFERMSNIEQMFYEIWKDLSLNDSLTAVERSKLAVWDYPVSDKYTKMWQAMQEAKLPATLDEAVARVRNSTAATGFAFLGDATDIRYLQLTNCDLQVVGEEFSRKPYAIAVQQGSHLKDQFNNAILTLLNKRQLEKLKEKWWKNDEALAKCDKPEDQSDGISIQNIGGVFIVIFVGIGMACITLVFEYWWYRYRKNPRIIDVAEANAERSNAADHPGKLVDGVILGHSGEKFEKSKAALRPRFNQYPATFKPRF
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Integral part of various neural sensory systems in the antenna that provide the neural basis for the response to environmental changes in temperature (thermosensation), humidity (hygrosensation) and odor detection. Required for odor-evoked electrophysiological responses in multiple neuron classes in the antenna and is likely to function as part of an olfactory receptor complex with Ir76a and Ir76b. Together with Ir21a and Ir93a, mediates the response of the larval dorsal organ cool cells, a trio of cool-responsive neurons, to cooling and is required for cool avoidance behavior. Required in chordonotal organ neurons for behavioral synchronization to low-amplitude temperature cycles and mediates circadian clock resetting by temperature. Together with Ir40a and Ir93a, mediates the response of the hydrosensory sacculus neurons to changes in relative humidity, and is required for dry detection and humidiy preference behavior.
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E9P860
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ZNFX1_CAEEL
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NFX1-type zinc finger-containing protein 1 homolog (EC 3.6.4.13)
|
MSRDKPPQREVGGRRLPYEMGSLKFDEDPFRGQRRRPWMCFRIGYPTSEFSSEHFMKFVKRCHTSMIEVGILLDDEREFLQYQEVREDYLLLKKLIEEGLQKCETIYEKGPLSTPVVFFILDQCDEDEVQNMLDMFRESCYIFHMKRNEILNWINEMEYEELESDCSKFAQFIKGVENLTESIAMPMEVETEEFIFGKSSIVSTEDFVEDAPHKQIAQDQRETRPIRQPYSMVRNLAPPGLPPPGISISNSSPPGLSSVSPIPRADTRESRYSTPQPPGLSIPAPPGISLPTPPGISLQNHQNDQFEQAHSTISRMSENSSSSRRRFRDEEVQEEEGDHILSSEDVHAARNVCETKILVRGVPQKNDSELSKLINGSKLYVRFERPFVKLAHNLELLYVVNYAISSRKSIVRDHSKAIIRGLFEKDFLLKLKSKFLESSFDNDTWTPEGTELLFEIFHLFFTTARYKGGFMLTLPRFAPSWHDFSMAFDIADMDGLEEAGVGDDELRNLRRLIGYIETWIKRAERERNPSPLALRSYSVYEKAGSSDSGRQVLSESRGAGSSNVYGHDEVDFVDHRRRDEFGHRDNYRTENRRHKSPDNFGEVHRRLDEQQQQRHEDESSRYRDDSRQSRRADDRRDQYQYNESTSMENHLGFHNGGGTVSEHSRDDKFVSPQNCEEKRKYCEEDTDAKPQQPYRFEEIKFEPIWVKCEKSEPPEDFKTLPSVPVLSEYVNPVEPYLRRIQDDGKYKSVHHYLDVQFRLLKEDLVSPLRDGIDLYKKNGTCKGRRIEGAPCSDISIFNVEKVDGKQVTERDGYEMRIIWPAQYDILKLLDNDREMKELGLVMLSCDRFKEDFHLGHIQSSYLMRNGSLHFAVHEETSPFKPNTTYQMAQGTSYLPCYKHVLENLKRISSFKPLPFERYLVHGSKIIFRPNFQQAEKSEYQISEEKKLMKTYNELRSLAACARYTKGKPIPRGVDDDDEDYEFSKSRELSKEDIDLEYRQLQEPIFRPLVGVDIKDSNLIQINKKWYNVSRLLDEFHPDYMDESQRLAFCNTFKYELSLIQGPPGTGKTHIGVQIVKTILQNRSYWKITEPILVVCFTNSGLDNLLERIYQMIENDEELSKDNGRPKIIRFGSKCDSNYLKRQNVMRQDVYEQYKSKVSDGAQKKMSKAGAARRHKADNLAISSYTLFCSRNKLLSYEMLSRVMDPNHQMEIQQFTYDHVDTKGIPLSPDEAIGCWLLERDFGKATKSQTKKAKKPKFQGAQLDSEDENKDYFTVEDSDDEEDELDDEKLLDKLFEKMNLECSGADILSAVHASHADEYYTKGPWEIVQDKRPSVVVLMEKKTKPCNAKFTVDEQINNLVSEIKDMILSSQPVPKKDLNDIKYIFSLARLKRWSLYITWCDALRSIVTENLPRQIREYREACENFKNAQNRVDAEIMRMTMIIGATTTGCSRLRPTLEKVGPRILIVEEAAEVLEAHIISAMISTVEHVVMIGDHKQLRPNPAVHELGVAYGLRISMFERLVERGLPFSQLRQQHRMNLTISDKIVKLSFYDNVTDAENVGLYPDVQGMATNLFFWSHTSMEESPDEVSWLNKHEISMTVALVKHLLKQNYTTNDIVVLATYSAQKNLMYREYANVFGSTPDSNVIPVETVDSFQGKERKIVIVSLVRSHRGGRENTGIGFLAVANRICVALTRAQHGMYIIGNGAYIMNNSELWNKIVNNLRRSNLIEYNLPLKCVAHGNIVTVKDPQDFATKSPEGGCMQKCDTKKFCGHVCERLCHPNMEEEHLQRCLYNCDKKCSNPQFQHRCKKACYEECGSCLYLVEVTLDCGHRITTPCSRINSSKCDQSCTKKLLCGHACAAKCGEECTLVSECSQLVGMPLSCGHIKQLTCSKISANEIDLTCDQRCEKTMLACPHKCAEICGQPCTVECMEVVNVTLGCSHSQDVVCSSFMPGMTDHIECLTKVPKTLSPCKHTELVLCKQAPSTKLCTRRCTSYLEKCGHTCENDCGICFTTKTHICQNMCQKVLNCGHTCSAKCGESCPPCKAFCTNKCEHQSCGAGERGFGRDCSKLCALCVNNCSNKCAHRSCTLKCFEECNVKPCTEPCTDKLKCGHACLGICGEQCPKICGTCERNKYIECVSGTSSTSRVHRLIMIPKCYHVFPVEVLDDHVKKQKEANEKLKCPKCSAFIVGVLRYARYTKKYYLNENMRKLESNIRNIHQSTLEGRVFQAVQDSIGEIRNVTTNLTNASEDILRNFHQKILDIRTSAETFKGKPEHKFKFASLLQVANCCLAITRLLSVSSKFRVSRRKDIPPTFDLMSVRVLGDMPFPKLIDELNRVNIHLSNTYETFMPGAIIPKLKWLISRMTVLQQLTSMCHQLVLEKKDIADSDAHAINDACLNMFRYNEQHNYALNIENFEAIVVKVAPKLLEPTPKFWSWRRLQVPEL
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Epigenetic inheritance factor which, in association with the Argonaute protein wago-4, mediates small RNA-directed transgenerational epigenetic inheritance and thus balances the transgenerational inheritance of epigenetic information. Specifically, maintains a balanced production of small RNAs by preventing the spread of epigenetic signals towards the 5'-end of target mRNAs. Plays a role in small RNA-induced gene silencing in the germline.
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E9P8D2
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MPR1_YEASX
|
N-acetyltransferase MPR1 (EC 2.3.1.271) ((S)-1-pyrroline-5-carboxylate acetyltransferase) (L-azetidine-2-carboxylate acetyltransferase) (AZC acetyltransferase) (Sigma1278b gene for proline-analog resistance 1)
|
MDAESIEWKLTANLRNGPTFFQPLADSIEPLQFKLIGSDTVATAFPVFDTKYIPDSLINYLFKLFNLEIESGKTYPQLHSLTKQGFLNYWFHSFAVVVLQTDEKFIQDNQDWNSVLLGTFYIKPNYAPRCSHNCNAGFLVNGAHRGQKVGYRLAQVYLNWAPLLGYKYSIFNLVFVTNQASWKIWDKLNFQRIGLVPHAGILNGFSEPVDAIIYGKDLTKIEPEFLSME
|
N-acetyltransferase involved in oxidative stress resistance. Acetylates the toxic proline metabolism intermediate (S)-1-pyrroline-5-carboxylate (P5C), or more likely its spontaneously forming tautomer glutamate-5-semialdehyde (GSA) into N-acetyl-GSA for arginine synthesis in the mitochondria. P5C has been shown to increase the levels of reactive oxygen species (ROS) in the cell by inhibiting the function of the respiratory chain in the mitochondria. The enzyme is able to reduce intracellular ROS levels under P5C-induced oxidative stress and protects cells from damage by oxidative stress. Also acetylates and thereby detoxifies the proline analog azetidine-2-carboxylate (AZC), however it is unlikely that AZC is a natural substrate as it occurs only in plants belonging to the Lilaceae family. Does not acetylate proline.
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E9PSK7
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JIP3_RAT
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C-Jun-amino-terminal kinase-interacting protein 3 (JIP-3) (JNK-interacting protein 3) (JNK MAP kinase scaffold protein 3)
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MMEIQMDEGGGVVVYQDDYCSGSVMSERVSGLAGSIYREFERLIHCYDEEVVKELMPLVVNVLENLDSVLSENQEHEVELELLREDNEQLLTQYEREKALRKQAEEKFIEFEDALEQEKKELQIQVEHYEFQTRQLELKAKNYADQISRLEERESEMKKEYNALHQRHTEMIQTYVEHIERSKMQQVGGGGQTESSLPGRSRKERPTSLNVFPLADGMVRAQMGGKLVPAGDHWHLSDLGQLQSSSSYQCPNDEMSESGQSSAAATPSTTGTKSNTPTSSVPSAAVTPLNESLQPLGDYGSVTKNNKRAREKRNSRNMEVQVTQEMRNVSIGMGSSDEWSDVQDIIDSTPELDVCPETRLDRTGSSPTQGIVNKAFGINTDSLYHELSTAGSEVIGDVDEGADLLGEFSGMGKEVGNLLLENSQLLETKNALNVVKNDLIAKVDQLSGEQEVLKGELEAAKQAKVKLENRIKELEEELKRVKSEAVTARREPREEVEDDKIPMAQRRRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASREHPSVQEKKKSTIWQFFSRLFSSSSSPPPAKRSYPSVNIHYKSPTTAGFSQRRNHALCQISAGSRPLEFFPDDDCTSSARREQKREQYRQVREHVRNDDGRLQACGWSLPAKYKQLSPNGGQEDTRMKNVPVPVYCRPLVEKDPSTKLWCAAGVNLSGWKPNEEDSSNGPKPAPGRDPLTCDREGEGEPKSTHPSPEKKKAKEVPEADATSSRVWILTSTLTTSKVVIIDANQPGTVVDQFTVCNAHVLCISSIPAASDSDYPPGDMFLDSDVNPEDSGADGVLAGITLVGCATRCNVPRSNCSSRGDTPVLDKGQGDVAATANGKVNPSQSTEEATEATEVPDPGPSESEATTVRPGPLTEHVFTDPAPTQSSSTQPASENGSESDGSIVQPQVEPSGESSATTSSAAPTMWLGAQNGWLYVHSAVANWKKCLHSIKLKDSVLSLVHVKGRVLVALADGTLAIFHRGEDGQWDLSNYHLMDLGHPHHSIRCMAVVDDRVWCGYKNKVHVIQPKTMQIEKSFDAHPRRESQVRQLAWIGDGVWVSIRLDSTLRLYHAHTHQHLQDVDIEPYVSKMLGTGKLGFSFVRITALLIAGNRLWVGTGNGVVISIPLTETVVLHRGQLLGLRANKTSPTSGEGTRPGGIIHVYGDDSSDKTASSFIPYCSMAQAQLCFHGHRDAVKFFVSVPGNVLATLNGSVLDSPSEGPGPAAPAADAEGQKLKNALVLSGGEGYIDFRIGDGEDDETEEGTGDVNQTKPSLSKAERSHIIVWQVSYTPE
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The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins (By similarity). Promotes neuronal axon elongation in a kinesin- and JNK-dependent manner. Activates cofilin at axon tips via local activation of JNK, thereby regulating filopodial dynamics and enhancing axon elongation. Its binding to kinesin heavy chains (KHC), promotes kinesin-1 motility along microtubules and is essential for axon elongation and regeneration. Regulates cortical neuronal migration by mediating NTRK2/TRKB anterograde axonal transport during brain development. Acts as an adapter that bridges the interaction between NTRK2/TRKB and KLC1 and drives NTRK2/TRKB axonal but not dendritic anterograde transport, which is essential for subsequent BDNF-triggered signaling and filopodia formation.
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E9PSL7
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CTRO_RAT
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Citron rho-interacting kinase (CRIK) (EC 2.7.11.1) (Rho-interacting, serine/threonine-protein kinase 21)
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MLKFKYGVRNPSEASAPEPIASRASRLNLFFQGKPPLMTQQQMSALSREGVLDALFVLLEECSQPALMKIKHVSSFVRKYSDTIAELRELQPSVRDFEVRSLVGCGHFAEVQVVREKATGDVYAMKIMKKAALRAQEQVSFFEEERNILSQSTSPWIPQLQYAFQDKNNLYLVMEYQPGGDLLSLLNRYEDQLDENMIQFYLAELILAVHSVHQMGYVHRDIKPENILIDRTGHIKLVDFGSAAKMNSNKVDAKLPIGTPDYMAPEVLTVMNEDRRGTYGLDCDWWSVGVVAYEMLYGKTPFTEGTSARTFNNIMNFQRFLKFPDDPKVSSELLDLIQSLLCVQKERLKFEGLCCHPFFARTDWNNIRNSPPPFVPTLKSDDDTSNFDEPEKNSWVSSSPCQLSPSGFSGEELPFVGFSYSKALGYLGRSESVVSGLDSPAKISSMEKKLLIKSKELQDSQDKCHKMEQEMARLHRRVSEVEAVLSQKEVELKASETQRSLLEQDLATYITECSSLKRSLEQARMEVSQEDDKALQLLHDIREQSRKLQEIKEQEYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELRESRLAAEEFKRKANECQHKLMKAKDLGKPEVGECSRLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLHNREDSSEGIKKKLVEAEERRHSLENKVKRLETMERRENRLKDDIQTKSEQIQQMADKILELEEKHREAQVSAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKESLETMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKNRLLELETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEEQVMDLEALNDELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQRITESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQMDLQKNHIFRLTQGLQEALDRADLLKTERSDLEYQLENIQVLYSHEKVKMEGTISQQTKLIDFLQAKMDQPAKKKKVPLQYNELKLALEKEKARCAELEEALQKTRIELRSAREEAAHRKATDHPHPSTPATARQQIAMSAIVRSPEHQPSAMSLLAPPSSRRKEASTPEEFSRRLKERMHHNIPHRFNVGLNMRATKCAVCLDTVHFGRQASKCLECQVMCHPKCSTCLPATCGLPAEYATHFTEAFCRDKVSSPGLQSKEPSSSLHLEGWMKVPRNNKRGQQGWDRKYIVLEGSKVLIYDNEAREAGQRPVEEFELCLPDGDVSIHGAVGASELANTAKADVPYILKMESHPHTTCWPGRTLYLLAPSFPDKQRWVTALESVVAGGRVSREKAEADAKLLGNSLLKLEGDDRLDMNCTLPFSDQVVLVGTEEGLYALNVLKNSLTHIPGIGAVFQIYIIKDLEKLLMIAGEERALCLVDVKKVKQSLAQSHLPAQPDVSPNIFEAVKGCHLFAAGKIENSLCICAAMPSKVVILRYNDNLSKFCIRKEIETSEPCSCIHFTNYSILIGTNKFYEIDMKQYTLEEFLDKNDHSLAPAVFASSTNSFPVSIVQANSTGQREEYLLCFHEFGVFVDSYGRRSRTDDLKWSRLPLAFAYREPYLFVTHFNSLEVIEIQARSSLGTPARAYLEIPNPRYLGPAISSGAIYLASSYQDKLRVICCKGNLVKESGTEQHRVPSTSRSSPNKRGPPTYNEHITKRVASSPAPPEGPSHPREPSTPHRYRDREGRTELRRDKSPGRPLEREKSPGRMLSTRRERSPGRLFEDSSRGRLPAGAVRTPLSQVNKVWDQSSV
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Plays a role in cytokinesis (By similarity). Required for KIF14 localization to the central spindle and midbody (By similarity). Putative RHO/RAC effector that binds to the GTP-bound forms of RHO and RAC1 (By similarity). It probably binds p21 with a tighter specificity in vivo (By similarity). Displays serine/threonine protein kinase activity (By similarity). Plays an important role in the regulation of cytokinesis and the development of the central nervous system. Phosphorylates MYL9/MLC2 (By similarity).
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E9PT37
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RBM20_RAT
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RNA-binding protein 20 (RNA-binding motif protein 20)
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MVLAAAMSQDADPSGPEQPDRDACIVPGVQGPPAPQGQQGMQPLPPPLPPPPQPQSSLPQIIQNAAKLLDKNPFSVSSQNPLLTSPASVQLAQIQAQLTLHRLKMAQTAVTNNTAAATVLNQVLSKVAMSQPLFNQLRHPSVLGTTHGPTGVSQHAATVPSAHFPSTAIAFSPPSQAGGPGPSVSLPSQPPNAMVVHTFSGVVPQTPAQPAVILSIGKAGPTPATTGFYDYGKANPGQAYGSETEGQPGFLPASASAAASGGVTYEGHYSHTGQDGQATFSKDFYGPSAQGSHAAGGFPADQAGSMKGDVGGLLQGTNSQWERPSGFSGQNKADITAGPGLWAPPASQPYELYDPEEPTSDRAPPAFGSRLNNSKQGFNCSCRRTKEGQAMLSVRPLQGHQLNDFRGLAPLHLPHICSICDKKVFDLKDWELHVKGKLHAQKCLLFSESAGLRSICATGEGTLSASANSTAVYNPTGNEDYTSTLGTSYAAIPTRAFAQSNPMFPSASSGTNFAQRKGAGRVVHICNLPEGSCTENDVINLGLPFGKVTNYILMKSTNQAFLEMAYTEAAQAMVQYYQEKPALINGEKLLIRMSTRYKELQLKKPGKNVAAIIQDIHSQRERCMLREADRYGPERPRSRSPMSRSLSPRSHSPPGPSRADWGNGRDSYAWRDEDRETVPRRENGEDKRDRLDVWAHDRKHYPRQLDKAELDERLEGGRGYREKYLKSGSPGPLHSASGYKGREDGYHRKETKAKLDKHPKQQQQDVPGRSRRKEEARLREPRHPHPEDSGKEEDLEPKVTRAPEGTKSKQSEKSKTKRADRDQEGADDKKEGRGAENEAGTEEQEGMEESPASVGTQQEGTESSDPENTRTKKGQDCDSGSEPEGDNWYPTNMEELVTVDEVGEEDFIMEPDIPELEEIVPIDQKDKILPEICPCVTATLGLDLAKDFTKQGETLGNGDAELSPKLPGQVPSTSTSCPNDTDMEMAGLNLDAERKPAESETGLSPEVSNCYEKEARGAEGSDVRLAPAAQRMSSPQPADERAQQSSPFLDDCKARGSPEDGPHEVSPLEEKASPTTESDLQSQACQENSRYTETRSLNSRSPEFTEAELKEPLSLPSWEPEVFSELSIPLGVEFVVPRTGFYCKLCGLFYTSEEAAKVSHCRSTVHYRNLQKYLSQLAEEGLKETEGVDSPSPERSGIGPHLERKKL
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RNA-binding protein that acts as a regulator of mRNA splicing of a subset of genes encoding key structural proteins involved in cardiac development, such as TTN (Titin), CACNA1C, CAMK2D or PDLIM5/ENH. Acts as a repressor of mRNA splicing: specifically binds the 5'UCUU-3' motif that is predominantly found within intronic sequences of pre-mRNAs, leading to the exclusion of specific exons in target transcripts. RBM20-mediated exon skipping is hormone-dependent and is essential for TTN isoform transition in both cardiac and skeletal muscles. RBM20-mediated exon skipping of TTN provides substrates for the formation of circular RNA (circRNAs) from the TTN transcripts (By similarity). Together with RBM24, promotes the expression of short isoforms of PDLIM5/ENH in cardiomyocytes.
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E9PT87
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MYLK3_RAT
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Myosin light chain kinase 3 (EC 2.7.11.18) (Cardiac-MyBP-C-associated Ca/CaM kinase) (Cardiac-MLCK)
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MSGVSEEDPEGLGPQGLPALGGACLVTVDKKLNVLTEKVDRLLHFQEDVTEKLQCVCQGMDHLEQGLHRLEASQELGLAGPGSTSPAAAQAAWPEVLELVRAVRQEGAQHGARLEALFKMVVAVDRAITLVGSTIQNSKVDDFILQGTVPWRKGSLADGPEENKEQAEVAGVKPKHVLNTGSVQAATSRALWEESQKQDTPVGTVEGLPLIIDTSLKGADLTQAGASLRQGVEALDPGQEPPPTEAESRLPALASEDTGTTLELSVAIDRISEVLTSLRMSQSAGEGTSSSKPDCSEPGPQPLGPLTTDSDIHSDEGLPRISVRMREMTTPEELFETQGGSPIGSAEAPGPGTVLEDQIPKGARPFPPLPKRSCNNGGASAEEATGPGAEPIRGPSLVTRDWRDEPVGTTDLQQGRDPGAVSPEPGKDHAAQGPGRTEAGRRVSSAAEAAIVVLDDSAAPPAPFEHRVVSIKDTLISTSYTVSQHEVLGGGRFGQVHRCTERSTGLALAAKIIKVKNIKDREDVKNEINIMNQLSHVNLIQLYDAFESKNSFTLIMEYVDGGELFDRITDEKYHLTELDVVLFTRQICEGVHYLHQHYILHLDLKPENILCVSQTGHQIKIIDFGLARRYKPREKLKVNFGTPEFLAPEVVNYEFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNFIVNCSWDFDADTFKGLSEEAKDFVSRLLVKEKSCRMSATQCLKHEWLNHLIAKASGSNVRLRSQLLLQKYMAQRKWKKHFHVVTAVNRLRKFPTCP
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Calmodulin-dependent kinase that phosphorylates MYL2 in vitro. Promotes sarcomere formation in cardiomyocytes. Increases cardiomyocyte contractility.
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E9PTA2
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TRPM2_RAT
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Transient receptor potential cation channel subfamily M member 2
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MEPLDQRRTDSDQEEGFGVQSRRATDLGMVPNLRRSNSSLCKSRRLLCSFSSEKQENLSSWIPENIKKKECVYFVESSKLSDAGKVVCECGYTHEQHIEVAIKPHTFQGKEWDPKKHVHEMPTDAFGDIVFTGLSQKVGKYVRLSQDTSSIVIYQLMTQHWGLDVPSLLISVTGGAKNFNMKLRLKSIFRRGLVKVAQTTGAWIITGGSHTGVMKQVGEAVRDFSLSSSCKEGDVITIGIATWGTIHNREALIHPMGGFPAEYMLDEEGQGNLTCLDSNHSHFILVDDGTHGQYGVEIPLRTKLEKFISEQTKERGGVAIKIPIVCVVLEGGPGTLHTIYNAITNGTPCVIVEGSGRVADVIAQVAALPVSEITISLIQQKLSVFFQEMFETFTENQIVEWTKKIQDIVRRRQLLTVFREGKDGQQDVDVAILQALLKASRSQDHFGHENWDHQLKLAVAWNRVDIARSEIFTDEWQWKPSDLHPMMTAALISNKPEFVRLFLENGVRLKEFVTWDTLLCLYENLEPSCLFHSKLQKVLAEEHERLAYASETPRLQMHHVAQVLRELLGDSTQLLYPRPRYTDRPRLSLPMPHIKLNVQGVSLRSLYKRSTGHVTFTIDPVRDLLIWAIIQNHRELAGIIWAQSQDCTAAALACSKILKELSKEEEDTDSSEEMLALADEFEHRAIGVFTECYRKDEERAQKLLVRVSEAWGKTTCLQLALEAKDMKFVSHGGIQAFLTKVWWGQLCVDNGLWRIILCMLAFPLLFTGFISFREKRLQALCRLARVRAFFNAPVVIFYLNILSYFAFLCLFAYVLMVDFQPSPSWCEYLIYLWLFSLVCEETRQLFYDPDGCGLMKMASLYFSDFWNKLDVGAILLFIAGLTCRLIPATLYPGRIILSLDFIMFCLRLMHIFTISKTLGPKIIIVKRMMKDVFFFLFLLAVWVVSFGVAKQAILIHNESRVDWIFRGVIYHSYLTIFGQIPTYIDGVNFSMDQCSPNGTDPYKPKCPESDWTGQAPAFPEWLTVTLLCLYLLFANILLLNLLIAMFNYTFQEVQEHTDQIWKFQRHDLIEEYHGRPPAPPPLILLSHLQLLIKRIVLKIPAKRHKQLKNKLEKNEEAALLSWELYLKENYLQNQQYQHKQRPEQKIQDISEKVDTMVDLLDMDRVKRSGSTEQRLASLEEQVTQMGRSLHWIVTTLKDSGFGSGAGALTLAQRAFDEPDAELSIRKKGEEGGDGYHVSARHLLYPDARIMRFPVPNEKVPWEAEFLIYDPPFYTAEKKDATLTDPVGDTAEPLSKINYNVVDGLMDRCSFHGTYVVQYGFPLNPMGRTGLRGRGSLSWFGPNHTLQPVVTRWKRNQGGGICRKSVRKMLEVLVVKLPQSEHWALPGGSREPGKMLPRKLKQVLQQEYWVTFETLLRQGTEVYKGYVDDPRNTDNAWIETVAVSIHFQDQNDVELKRLEENLQTHDPKESARGLEMSTEWQVVDRRIPLYVNHKKILQKVASLFGAHF
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Nonselective, voltage-independent cation channel that mediates Na(+) and Ca(2+) influx, leading to increased cytoplasmic Ca(2+) levels. Functions as ligand-gated ion channel. Binding of ADP-ribose to the cytoplasmic Nudix domain causes a conformation change the channel is primed but still requires Ca(2+) binding to trigger channel opening. Extracellular calcium passes through the channel and increases channel activity (By similarity). Also contributes to Ca(2+) release from intracellular stores in response to ADP-ribose. Plays a role in numerous processes that involve signaling via intracellular Ca(2+) levels (Probable). Besides, mediates the release of lysosomal Zn(2+) stores in response to reactive oxygen species, leading to increased cytosolic Zn(2+) levels. Activated by moderate heat (35 to 40 degrees Celsius). Activated by intracellular ADP-ribose, beta-NAD (NAD(+)) and similar compounds, and by oxidative stress caused by reactive oxygen or nitrogen species. The precise physiological activators are under debate the true, physiological activators may be ADP-ribose and ADP-ribose-2'-phosphate. Activation by ADP-ribose and beta-NAD is strongly increased by moderate heat (35 to 40 degrees Celsius) (By similarity). Likewise, reactive oxygen species lower the threshold for activation by moderate heat (37 degrees Celsius). Plays a role in mediating behavorial and physiological responses to moderate heat and thereby contributes to body temperature homeostasis. Plays a role in insulin secretion, a process that requires increased cytoplasmic Ca(2+) levels. Required for normal IFNG and cytokine secretion and normal innate immune immunity in response to bacterial infection. Required for normal phagocytosis and cytokine release by macrophages exposed to zymosan (in vitro). Plays a role in dendritic cell differentiation and maturation, and in dendritic cell chemotaxis via its role in regulating cytoplasmic Ca(2+) levels (By similarity). Plays a role in the regulation of the reorganization of the actin cytoskeleton and filopodia formation in response to reactive oxygen species via its function in increasing cytoplasmic Ca(2+) and Zn(2+) levels (By similarity). Confers susceptibility to cell death following oxidative stress.
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E9PTT0
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ZDH17_RAT
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Palmitoyltransferase ZDHHC17 (EC 2.3.1.225) (Acyltransferase ZDHHC17) (EC 2.3.1.-) (Zinc finger DHHC domain-containing protein 17)
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MADGPDEYDTETGCVPLLHPEEIKPQSHYNHGYGEPLGRKTHVDDYSTWDIVKATQYGIYERCRELVEAGYDVRQPDKENVTLLHWAAINNRIDLVKYYISKGAIVDQLGGDLNSTPLHWATRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPLMWAAYRTHSVDPTRLLLTFNVSVNLGDKYHKNTALHWAVLAGNTTVISLLLEAGGNVDAQNVKGESALDLAKQRKNVWMINHLQEARQAKGYDNPSFLRKLKADKEFRQKVMLGTPFLVIWLVGFIADLNIDSWLIKGLMYGGVWATVQFLSKSFFDHSMHSALPLGIYLATKFWMYVTWFFWFWNDLSFLSIHLPFLANSVALFYNFGKSWKSDPGIIKATEEQKKKTIVELAETGSLDLSIFCSTCLIRKPVRSKHCGVCNRCIAKFDHHCPWVGNCVGAGNHRYFMGYLFFLLFMICWMIYGCVSYWGLHCETTYTKDGFWTYITQIATCSPWMFWMFLNSVFHFMWVAVLLMCQMYQITCLGITTNERMNARRYKHFKVTTTSIESPFNHGCVRNIIDFFEFRCCGLFRPVIVDWTRQYTIEYDQISGSGYQLV
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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). Palmitoyltransferase specific for a subset of neuronal proteins, including SNAP25, DLG4/PSD95, GAD2, SYT1 and HTT (By similarity). Also palmitoylates neuronal protein GPM6A as well as SPRED1 and SPRED3 (By similarity). Could also play a role in axonogenesis through the regulation of NTRK1 and the downstream ERK1/ERK2 signaling cascade (By similarity). May be involved in the sorting or targeting of critical proteins involved in the initiating events of endocytosis at the plasma membrane (By similarity). May play a role in Mg(2+) transport (By similarity). Could also palmitoylate DNAJC5 and regulate its localization to the Golgi membrane (By similarity). Palmitoylates CASP6, thereby preventing its dimerization and subsequent activation (By similarity).
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E9PU28
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IMDH2_RAT
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Inosine-5'-monophosphate dehydrogenase 2 (IMP dehydrogenase 2) (IMPD 2) (IMPDH 2) (EC 1.1.1.205)
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MADYLISGGTSYVPDDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQVDLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVKKYEQGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISSRDIDFLKEEEHDRFLEEIMTKREDLVVAPAGVTLKEANEILQRSKKGKLPIVNESDELVAIIARTDLKKNRDYPLASKDTKKQLLCGAAIGTHEDDKYRLDLLALAGVDVVVLDSSQGNSIFQINMIKYIKEKYPNLQVIGGNVVTAAQAKNLIDAGVDALRVGMGSGSICITQEVLACGRPQATAVYKVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKYRGMGSLDAMDKHLSSQNRYFSEADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVRAMMYSGELKFEKRTSSAQVEGGVHGLHSYEKRLF
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Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors.
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E9PUL5
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PRRT2_MOUSE
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Proline-rich transmembrane protein 2 (Dispanin subfamily B member 3) (DSPB3)
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MAASSSQVSEMKGVEDSSKTQTEGPRHSEEGLGPVQVVAEIPDQPEALQPGPGITAAPVDSGPKAELAPETTETPVETPETVQATDLSLNPEEGSKASPSPSPSEARQEPASKPDVNRETAAEEGSEPQSTAPPEPTSEPAFQINTQSDPQPTSQPPPKPPLQAEPPTQEDPTTEVLTESTGEKQENGAVVPLQAGDGEEGPAPQPHSPPSTKTPPANGAPPRVLQKLVEEDRIGRAHGGHPGSPRGSLSRHPSSQLAGPGVEGGEGTQKPRDYIILAILSCFCPMWPVNIVAFAYAVMSRNSLQQGDVDGAQRLGRVAKLLSIVALVGGVLIIIASCVINLGVYK
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As a component of the outer core of AMPAR complex, may be involved in synaptic transmission in the central nervous system. In hippocampal neurons, in presynaptic terminals, plays an important role in the final steps of neurotransmitter release, possibly by regulating Ca(2+)-sensing. In the cerebellum, may inhibit SNARE complex formation and down-regulate short-term facilitation.
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E9PUN2
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NRX2B_MOUSE
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Neurexin-2-beta (Neurexin II-beta)
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MPPGGSGQGGCPRRPPALAGPLPPPPPPPPLPLLLGLLLLLGAAEGARVSSSLSTTHHVHHFHSKHGTVPIAINRMPFLTRSGHAGTTYIFGKGGALITYTWPPNDRPSTRMDRLAVGFSTHQRSAVLVRVDSASGLGDYLQLHIDQGTVGVIFNVGTDDITIDEPNAIVSDGKYHVVRFTRSGGNATLQVDSWPVNERYPAGNFDNERLAIARQRIPYRLGRVVDEWLLDKGRQLTIFNSQAAIKIGGRDQGRPFQGQVSGLYYNGLKVLALAAESDPNVRTEGHLRLVGEGPSVLLSAETTATTLLADMATTIMETTTTMATTTTRRGRSPTMRDSTTQNTDDLLVASAECPSDDEDLEECEPSTGGELILPIITEDSLDPPPVATRSPFVPPPPTFYPFLTGVGATQDTLPPPAARRPSSGGPCQAERDDSDCEEPVEASGFASGEVFDSSLPPTDDEDFYTTFPLVTDRTTLLSPRKPRPNLRTDGATGAPGVLFAPSAPAPNLPAGKMNHRDPLQPLLENPPLGPGVPTAFEPRRPPPLRPGVTSAPGFPRLPTANPTGPGERGPPGAVEVIRESSSTTGMVVGIVAAAALCILILLYAMYKYRNRDEGSYQVDQSRNYISNSAQSNGAVVKEKAPAAPKTPSKAKKNKDKEYYV
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Neuronal cell surface protein that may be involved in cell recognition and cell adhesion.
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E9PUQ8
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DGKD_MOUSE
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Diacylglycerol kinase delta (DAG kinase delta) (EC 2.7.1.107)
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MAAAAGAPPPGPPQPPPPPPPEESSDSEPEAEPGSPQKLIRKVSTSGQIRQKTILKEGMLTKQNNSFQRSKRRYFKLRGRTLYYAKTAKSIIFDEVDLTDASVAESSTKNVNNSFTVITPCRKLILCADNRKEMEDWIAALKTVQNKEHFEPTQYSMDHFSGMHNWYACSHARPTYCNVCREVLSGVTSHGLSCEVCKFKAHKRCAVRATSNCKWTTLASIGKDIIEDEDGIAMPHQWLEGNLPVSAKCIVCDKTCGSVLRLQDWRCLWCKAMVHTSCKESLVMKCPLGLCKVSVIPPTALNSIDSDGFWKATCPPSCTSPLLVFVNSKSGDNQGVKFLRRFKQLLNPAQVFDLMNGGPHLGLRLFQKFDTFRILVCGGDGSVGWVLSEIDSLNLHKQCQLGVLPLGTGNDLARVLGWGSACDDDTQLPQILAKLERASTKMLDRWSVMAYETKLPRQASSSTVTEDFSEDSEVQQILFYEDSVAAHLSKILTSDQHSVVISSAKVLCETVKDFVARVGKAYEKTTESSQESEVMAKKCSVLKEKLDSLLKTLDDESQASSSLSNPPPTIAEEAEDGDGSGNICSSTGDHLVGSACPSRPQIFRPREQLMLRANSLKKAIRQIIEHTEKAVDEQNAQTQEQQGFVLGLSESEKKDLKTDNRVCTSSVHSESCVIAKGRSQRKASRAPCEKLVSKGLSLGSSASLPPGTGSRDSLPALNTKILYPSVRAGMSGSLPGGSVISRLLINADPFNAEPENLEYYTEKCVMNNYFGIGLDAKISLDFNNKRDEHPEKCRSRTKNMMWYGVLGTKELLHRTYRNLEQKVLLECDGRPIPLPSLQGIAVLNIPSYAGGTNFWGGTKEDDTFAAPSFDDKILEVVAVFGSMQMAVSRVIKLQHHRIAQCRTVKISILGDEGVPVQVDGEAWIQPPGYIRIVHKNRAQTLTRDRAFENTLKSWEDKQKCELSRPPSFSLHPEILSEEEATQMDQFGQAAGGLIHSIREIAQSHRAMEQELAHAVNASSKAMERVYGKPRTAEGLNCSFVLEMVNNIRALRSETELLLAGKMALQLDPPQKERLGAALIEMDQQLRKLTDTPWLCQPLEPGEEESLQQNVMLDLTKRSRSGKFRLVTKFKKEKNNKNKEVHSNLGGPVHLWGTEEVAAWLEHLSLCEYKDIFTRHDIRGSELLHLERRDLKDLGVTKVGHMKRILCGIKELSRSSPAAEA
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Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids. Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes. By controlling the levels of diacylglycerol, regulates for instance the PKC and EGF receptor signaling pathways and plays a crucial role during development. May also regulate clathrin-dependent endocytosis (By similarity).
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E9PV24
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FIBA_MOUSE
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Fibrinogen alpha chain [Cleaved into: Fibrinopeptide A; Fibrinogen alpha chain]
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MLSLRVTCLILSVASTVWTTDTEDKGEFLSEGGGVRGPRVVERHQSQCKDSDWPFCSDDDWNHKCPSGCRMKGLIDEANQDFTNRINKLKNSLFDFQRNNKDSNSLTRNIMEYLRGDFANANNFDNTYGQVSEDLRRRIEILRRKVIEKAQQIQALQSNVRAQLIDMKRLEVDIDIKIRSCKGSCSRAVNREINLQDYEGHQKQLQQVIAKELLPTKDRQYLPALKMSPVPDLVPGSFKSQLQEAPPEWKALTEMRQMRMELERPGKDGGSRGDSPGDSRGDSRGDFATRGPGSKAENPTNPGPGGSGYWRPGNSGSGSDGNRNPGTTGSDGTGDWGTGSPRPGSDSGNFRPANPNWGVFSEFGDSSSPATRKEYHTGKAVTSKGDKELLIGKEKVTSSGTSTTHRSCSKTITKTVTGPDGRREVVKEVITSDDGSDCGDATELDISHSFSGSLDELSERHPDLSGFFDNHFGLISPNFKEFGSKTHSDSDILTNIEDPSSHVPEFSSSSKTSTVKKQVTKTYKMADEAGSEAHREGETRNTKRGRARARPTRDCDDVLQTQTSGAQNGIFSIKPPGSSKVFSVYCDQETSLGGWLLIQQRMDGSLNFNRTWQDYKRGFGSLNDKGEGEFWLGNDYLHLLTLRGSVLRVELEDWAGKEAYAEYHFRVGSEAEGYALQVSSYRGTAGDALVQGSVEEGTEYTSHSNMQFSTFDRDADQWEENCAEVYGGGWWYNSCQAANLNGIYYPGGTYDPRNNSPYEIENGVVWVPFRGADYSLRAVRMKIRPLVGQ
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Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the immune response via both innate and T-cell mediated pathways.
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E9PV87
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TALD3_MOUSE
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Protein TALPID3
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MKNVEFSLERGQRLKMPARKLREIVSPNQGNKLAVVEDELPRVPPALAANKRLAVETRTSSNGTLCGSLDLTSARLYHQPLLESPPASKKSDFSKDAVVRQLPLNKTEENNAPKANDIFISQYTMGQKDALRTVLKQKAQSMPVFKAVKVHLFEDTSTEKNTVAQETETPPNRIDSATTVAAATAAAIATAAPLIKVQSDLEAKVNCVGELLTKLQETDKQLQRVTEHQASVQSKQEKVHCHDHDKQMNAFMEQHIRHLEKLQQQQIDIQTHFIDAALKASSLQLGMSTSRAVGKYSGKLGSPSVGSSVFSHNTFVSKRVPLSEDTDFDGQKSPLETPAPRRFAPVPVSRDGKITKRESPTEEKENMEMNSPKGNVRLLEQVLNSNECLTRKTESSDITSLTQPKMGWNLEKRDSTETLHSQIFPSSEERGTAQVPVPKYNDVVHDLGQKKQASDMLQIKQSPVTLRLSDHPHNPALLQTTNTRSVLKDAAKILRGVQNNKKVLEENLEAIVRAKDGAAMYSFINALATNREMSEKIRIRKQVDEWIKIISAEIQDELMRKDYEQKRFDPKNQRNKKALTMSRDIKANNQEKTVNRSVIPRSHYQKQTQEQFTSPPVRNLPASGPQKERSGLLKSATTLQDEDYMLQIYGKPVYQGHRSTLKKGPYLRFSSPSPKAKPQRPRVIELVKGTKVKSAKTQTDFHAASRMKMDSKIQHPITALPHADQQYMVSPSREMPTVSGTLEGHLIPMAILLGQTQSNSDSMPPAGVTVNKPRPVTVTTSIPPASRKGNAGVKKPNVAIVEMKSEKKDPPQLSVQILPSVDIDSVSYSSTDGASSPPSPKEASLPPLHTWIQTPDFMKVDEEEVPLPGTNFDEVIDVIQEEEKRDEIPECSAPMLEFNRSVKVVPTKYNGPSFPPVVSAYHPTTDILDKVIERKETLENSLIQWVEQEIMSRIISGLFPLQQQARLDASVSVSEASEPSASDIVAGTSSGALQRMVDARVPVNSDMVSHFVNEALTETIAVMLADREAERQRAAATSVPGDLSGTETNLLARVCAPVATPQPTPPCSPSPVREHVRVKTPDSSPCESDPDAASSIKEIRVEKGSDMPAVMLVSTPTRTPVATPPPAAALTPTLSETSIDKLKLSSPELPKPWDSGDLPLDEENPNSLQELPHPRAVVMSVANEEPESVDFSAQPAPPEPAPSAPLPEGTKAPSLQRVPSSGSSTLENTLSTVTETETLDRHISEGEILFSCGQNLATKRPGDLFLMNINDSLSSTLQDALEMEDDPPSEGQVIRRPHKKRHEDAIVALLTKQQRELLVSQQEEDLDNSVGELSEGQRLVLKAAEDISAGPSGQMLPPTSPAEPSYQHADPRLVLQQSDMASGNICEDLCASHGPMSLRELELQPDSNLILPITHTTTAVSDGNLPEAAEDFSQYQQKQDSDIKQVEHKPIQRHLTSVRNKPDSTLSQHQGGPADLLLIAHVSPARMSVTLPSANLEDCSQSLSTSSMHGGTESSGTDTF
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Required for ciliogenesis and sonic hedgehog/SHH signaling. Required for the centrosomal recruitment of RAB8A and for the targeting of centriole satellite proteins to centrosomes such as of PCM1. May play a role in early ciliogenesis in the disappearance of centriolar satellites that preceeds ciliary vesicle formation (By similarity). Involved in regulation of cell intracellular organization. Involved in regulation of cell polarity (By similarity). Required for asymmetrical localization of CEP120 to daughter centrioles.
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E9PVA8
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GCN1_MOUSE
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Stalled ribosome sensor GCN1 (GCN1 eIF-2-alpha kinase activator homolog) (GCN1-like protein 1) (General control of amino-acid synthesis 1-like protein 1) (Translational activator GCN1)
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MAADTQVSETLKRFAVKVTTASVKERREILSELGRCIAGKDLPEGAVKGLCKLFCLTLHRYRDAASRRALQAAIQQLAEAQPEATAKNLLHSLQSSGVGSKACVPSKSSGSAALLALTWTCLLVRIVFPLKAKRQGDIWNKLVEVQCLLLLEVLGGSHKHAVDGAVKKLTKLWKENPGLVEQYFSAILSLEPSQNYAAMLGLLVQFCTNHKEMDAVSQHKSTLLEFYVKNILMSKAKPPKYLLDNCAPLLRFMSHSEFKDLILPTIQKSLLRSPENVIETISSLLASVTLDLSQYALDIVKGLANQLKSNSPRLMDEAVLALRNLARQCSDSSATEALTKHLFAILGGSEGKLTIIAQKMSVLSGIGSLSHHVVSGPSGQVLNGCVAELFIPFLQQEVHEGTLVHAVSILALWCNRFTTEVPKKLTDWFKKVFSLKTSTSAVRHAYLQCMLASFRGDTLLQALDFLPLLMQTVEKAASQGTQVPTVTEGVAAALLLSKLSVADAQAEAKLSGFWQLVVDEKRQTFTSEKFLLLASEDALCTVLRLTERLFLDHPHRLTNSKVQQYYRVLVAVLLSRTWHVRRQAQQTVRKLLSSLGGVKLANGLLDELKTVLNSHKVLPLEALVTDAGEVTEMGKTYVPPRVLQEALCVISGVPGLKGDIPSTEQLAQEMLIISHHPSLVAVQSGLWPALLTRMKIDPDAFITRHLDQIIPRITTQSPLNQSSMNAMGSLSVLSPDRVLPQLISTITASVQNPALCLVTREEFSIMQTPAGELFDKSIIQSAQQDSIKKANMKRENKAYSFKEQIIEMELKEEIKKKKGIKEEVQLTSKQKEMLQAQMDKEAQIRRRLQELDGELEAALGLLDAIMARNPCGLIQYIPVLVDAFLPLLKSPLAAPRVKGPFLSLAACVMPPRLKTLGTLVSHVTLRLLKPECALDKSWCQEELPVAVRRAVSLLHTHTIPSRVGKGEPDAAPLSAPAFSLVFPMLKMVLTEMPYHSEEEEEQMAQILQILTVHAQLRASPDTPPERVDENGPELLPRVAMLRLLTWVIGTGSPRLQVLASDTLTALCASSSGEDGCAFAEQEEVDVLLAALQSPCASVRETALRGLMELRLVLPSPDTDEKSGLSLLRRLWVIKFDKEDEIRKLAERLWSTMGLDLQSDLCSLLIDDVIYHEAAVRQAGAEALSQAVARYQRQAAEVMGRLMEIYQEKLYRPPPVLDALGRVISESPPDQWEARCGLALALNKLSQYLDSSQVKPLFQFFVPDALNDRNPDVRKCMLDAALATLNAHGKENVNSLLPVFEEFLKDAPNDASYDAVRQSVVVLMGSLAKHLDKSDPKVKPIVAKLIAALSTPSQQVQESVASCLPPLVPAVKEDAGGMIQRLMQQLLESDKYAERKGAAYGLAGLVKGLGILSLKQQEMMAALTDAIQDKKNFRRREGALFAFEMLCTMLGKLFEPYVVHVLPHLLLCFGDGNQYVREAADDCAKAVMSNLSAHGVKLVLPSLLAALEEESWRTKAGSVELLGAMAYCAPKQLSSCLPNIVPKLTEVLTDSHVKVQKAGQQALRQIGSVIRNPEILAIAPVLLDALTDPSRKTQKCLQTLLDTKFVHFIDAPSLALIMPIVQRAFQDRSTDTRKMAAQIIGNMYSLTDQKDLAPYLPSVTPGLKASLLDPVPEVRTVSAKALGAMVKGMGESCFEDLLPWLMETLTYEQSSVDRSGAAQGLAEVMAGLGVEKLEKLMPEIVATASKVDIAPHVRDGYIMMFNYLPITFGDKFTPYVGPIIPCILKALADENEFVRDTALRAGQRVISMYAETAIALLLPQLEQGLFDDLWRIRFSSVQLLGDLLFHISGVTGKMTTETASEDDNFGTAQSNKAIITALGVDRRNRVLAGLYMGRSDTQLVVRQASLHVWKIVVSNTPRTLREILPTLFGLLLGFLASTCADKRTIAARTLGDLVRKLGEKILPEIIPILEEGLRSQKSDERQGVCIGLSEIMKSTSRDAVLFFSESLVPTARKALCDPLEEVREAAAKTFEQLHSTIGHQALEDILPFLLKQLDDEEVSEFALDGLKQVMAVKSRVVLPYLVPKLTTPPVNTRVLAFLSSVAGDALTRHLGVILPAVMLALKEKLGTPDEQLEMANCQAVILSVEDDTGHRIIIEDLLEATRSPEVGMRQAAAIILNMYCSRSKADYSSHLRSLVSGLIRLFNDSSPVVLEESWDALNAITKKLDAGNQLALIEELHKEIRFIGNECKGEHVPGFCLPKRGVTSILPVLREGVLTGSPEQKEEAAKGLGLVIRLTSADALRPSVVSITGPLIRILGDRFNWTVKAALLETLSLLLGKVGIALKPFLPQLQTTFTKALQDSNRGVRLKAADALGKLISIHVKVDPLFTELLNGIRAVEDPGIRDTMLQALRFVIQGAGSKVDAAIRKNLVSLLLSMLGHDEDNTRISTAGCLGELCAFLTDEELNTVLQQCLLADVSGIDWMVRHGRSLALSVAVNVAPSRLCAGRYSNEVQDMILSNAVADRIPIAMSGIRGMGFLMKYHIETGSGQLPPRLSSLLIKCLQNPCSDIRLVAEKMIWWANKEPRPPLEPQTIKPILKALLDNTKDKNTVVRAYSDQAIVNLLKMRRGEELLQSLSKILDVASLEALNECSRRSLRKLACQADSVEQVDDTILT
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Ribosome collision sensor that plays a key role in the RNF14-RNF25 translation quality control pathway, a pathway that takes place when a ribosome has stalled during translation, and which promotes ubiquitination and degradation of translation factors on stalled ribosomes (By similarity). Directly binds to the ribosome and acts as a sentinel for colliding ribosomes: activated following ribosome stalling and promotes recruitment of RNF14, which directly ubiquitinates EEF1A1/eEF1A, leading to its degradation (By similarity). In addition to EEF1A1/eEF1A, the RNF14-RNF25 translation quality control pathway mediates degradation of ETF1/eRF1 and ubiquitination of ribosomal protein (By similarity). GCN1 also acts as a positive activator of the integrated stress response (ISR) by mediating activation of EIF2AK4/GCN2 in response to amino acid starvation. Interaction with EIF2AK4/GCN2 on translating ribosomes stimulates EIF2AK4/GCN2 kinase activity, leading to phosphorylation of eukaryotic translation initiation factor 2 (eIF-2-alpha/EIF2S1). EIF2S1/eIF-2-alpha phosphorylation converts EIF2S1/eIF-2-alpha into a global protein synthesis inhibitor, leading to a global attenuation of cap-dependent translation, and thus to a reduced overall utilization of amino acids, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activator ATF4, and hence allowing ATF4-mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion.
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E9PVD3
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PCD16_MOUSE
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Protocadherin-16 (Protein Dchs1) (Protein dachsous homolog 1)
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MQKELSVALSCPGMKSLRTLLPLLVLLGATVPGSWGQAGSLDLQIDEEQPAGTLIGDISAGLPPGTAPPPMYFISAQEGSGVGTDLAIDEHSGVVRTARVLDRERRDRYRFTAVTPDGATVEVTVRVADINDHAPAFPQARAALQIPEHTALGTRYPLEPARDADAGRLGTQGYALSGDGAGETFRLETRPGPGGAPVPELVIAGELDRENRSHYMLQLEAYDGGSPPRRAQALLDVTLLDINDHAPAFNQSRYHAVVSESLAPGSPVLQVFASDADAGANGAVTYEINRRQSEGDGPFSIDAHTGFLRLERPLDFEQRRVHELVVQARDGGAHPELGSAFVTVHVRDANDNQPSMTVIFLSADGSPRVSEAAPPGQLVARISVSDPDDGDFAHVNVSLEGGEGHFALSTQDSVIYLVCVARRLDREERDVYNLRVTATDSGSPPLRAEAAFVLHVTDVNDNAPAFDRQLYRPEPLPEVALPGSFVVRVTARDPDQGTNGQITYSLAPGTHTHWFSIDPTSGIITTAATLDYELEPQPQLIVVATDGGLPPLVSSATVSVALQDVNDNEPQFQRTFYNASLPEGTQPGTCFLQVTATDADSGPFGLLSYSLGAGLGASGSPPFRIDAHSGDVCTTRTLDRDQGPSSFDFTVTAIDGGGLKSMVYVKVFVADENDNPPQFYPREYAASLSAQSTPGTAVLRVHAHDPDQGPHGRLSYHILAGNSPPLFALDAHSGLLTVAWPLGRRANSVVQLEIGAQDGGGLQAEPIARVNISIVPGTPTPPIFEQLQYVFSVPEDVAPGTSVGIIQAHNPPGRLGPVTLTLSGGDPRGLFSLDSPSGLLKTLRPLDRELLGPVLELEVRAGSGTPPVFAVARIRVLLDDVNDNSPAFPAPEDTVLLPQNTAPGTPIYTLRALDPDSGANSRITFNLLAGGDGLFTVDPTTGHVRLMGPLGPPGGPAHELEVEARDGGSPPRTSHFRLRVVIQDLGIHGLAPRFDSPTYRVDLPSGTTTGTQILQVQAQAPDGSPVTYHLAADGASSPFGLESQSGWLWVRTALDRESQELYTLKVMAVSGSKAELGQQTGTATVRVIILNQNDHSPRLSEEPTFLAVAENQPPGTSVGRVFATDRDSGPNGRLTYSLQQLSEDSKAFRIHPQTGEVTTLQTLDREQQSSFQLLVQVQDGGSPPRSATGTVHVAVLDLNDNSPTFLQASGAAGGGLPIQVPDRVPPGTLVTTLQAKDPDEGENGTILYTLTGPGSELFSLHPHTGELHTAASLVRAERPHYVLTLSAHDQGSPPRSASLQLLVQVLPSTRVVESPDLIEADSAATVPVVLTVTAAEGLRPGSLLGSVAPQEPASVGVLTYTLVGGADPEGTFALDSASGRLYLARPLDFEAGPAWRALTVRAEGPGGAGARLLRVQVRVQDENEHAPTFARDPLALALPENPDPGATLYTFRASDADGPGPNSEVRYRLLRQEPPVPALRLDARTGALSAPRGLDRETTPALLLLVEATDRPANASRRRAARVSARVFVTDENDNAPVFASPSRVRLPEDQPPGPAALHVVARDPDLGEAARVSYRLAAGGDGHFRLHATTGALSVVRPLDREQRAEHVLTVVALDHGSPPRSSTQLLTVSVVDVNDEAPAFPQQEYNVILRENSPPGTSLLTLKATDPDLGANGQVTYGGVSGESFSLDPNTGVLTTLRALDREEQEEIYLTVYARDRGLPPLLTHITVRVTVEDENDHTPTFGNTHLSLEVPEGQDPQTLTTLRASDPDGGLNGQLQYRILDGDSSGAFALDLTSGEFGTMRPLDREVEPAFQLQIEARDGGQPALSATLLVTVTVLDANDHAPVFPVPSYSVEVPEDAPVGTLLLQLQAHDPDDGDNGRVMYYLGAGTAGAFLLEPTSGELSTATALDREHCASYAFSVTAVDGAAAGPLSTTVPITITVRDVNDHAPAFPTSPLRLRLPRPGPSLNKPTLALATLRAEDRDAGANASILYRLAGTPPPGTTVDSYTGEIRVARSPVALGPQDRVLFIVATDLGRPARSATGVVVVGIQGEPERGPRFPRTSSEAVLRENAPPGTPVISPKAVHSGGSNGPITYSILSGNERGIFSIQPSTGAITVRSAEGLDFETSPRLRLVLQAESGGAFAFSVLTLTLQDANDNAPRFLRPHYVAFLPESRPLEGPLLQVEADDLDQGSGGQISYSLAASQPARGLFHVDPATGTITTTAILDREIWAETRLVLMATDRGSPALVGSATLTVMVIDTNDNRPTIPQPWELRVSEDALLGSEIAQVTGNDVDSGPVLWYVLSPSGPQDPFSIGRYGGRVSLTGPLDFEQCDHYHLQLLAHDGPHEGHANLTVLVEDVNDNVPTFSQSLYQVMMLEHTPPGSAILSVSATDRDSGANGHISYHLASPAEGFRVDPNNGTLFTTVGAMALGHEGPGVVDVVLEARDHGAPGRTAQATVHVQLKDQNDHAPSFTLPHYRVAVSEDLPPGSTLLTLEATDADGSRTHATVDYSIISGNRGRVFQLEPRLAEVGDGVGPGPQALGCLVLLEPLDFESLTQYNLTVAAADRGQPPRSSAVPVTVTVLDVNDNPPVFTRASYRVTVPEDMPVGAELLHVEASDADPGPHGLVHFTLSSGDPLGLFELDENSGALRLSRPLDCETQAQHQLVVQAADPAGTHFSLVPVTVEVQDVNDHGPAFPLSLLSTSLAENQPPGTLVTTLHAIDGDAGTFGRLRYSLLEAVPGPEGREAFSLNSSTGELRARVPFDYEHTGSFRLLVGAADAGNLSASVTVSVLITGEDEYDPVFLAPSFHFQVPEGAQRGHSLGHVQATDEDGGADGLVLYSLATSSPYFGINQTTGALYLRVDSRAPGSGTTTSGGGGRTRREAPRELRLEVVARGPLPGSRSATVPVTVDITHTALGLAPDLNLLLVGAVAASLGVVVVLALAALVLGLVRARSRKAEAAPGPMSQTAPIASSSLQKLGREPPSPPPSEHLYHQTLPSYGGPGAGGPYPRGGSLDPSHSSGRGSAEAAEDDEIRMINEFPRVASVASSLAARGPDSGIQQDADGLSDTSCEPPAPDTWYKGRKAGLLLPGAGATLYREEGPPATATAFLGGCGLSPAPAGDYGFPADGKPCVAGALTAIVAGEEELRGSYNWDYLLSWCPQFQPLASVFTEIARLKDEARPCPPAPRIDPPPLITAVAHPGAKSVPPKPASTAVARAIFPPASHRSPISHEGSLSSAAMSPSFSPSLSPLAARSPVVSPFGVAQGPSASALSTESGLEPPDDTELRI
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Calcium-dependent cell-adhesion protein. Mediates functions in neuroprogenitor cell proliferation and differentiation. In the heart, has a critical role for proper morphogenesis of the mitral valve, acting in the regulation of cell migration involved in valve formation.
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E9PVX6
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KI67_MOUSE
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Proliferation marker protein Ki-67 (Antigen identified by monoclonal antibody Ki-67 homolog) (Antigen KI-67 homolog) (Antigen Ki67 homolog)
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MASSAHLVTIKRSGDDGAHFPLSLSSCLFGRSIECDIRIQLPVVSKRHCKIEVKEQEAILYNFSSTNPTQVNGVTIDEPVRLRHGDIITIIDRSFRYEDGNHEDGSKPTEFPGKSLGKEPSRRASRDSFCADPDGEGQDTKASKMTASRRSFVYAKGLSADSPASDGSKNSVSQDSSGHVEQHTGRNIVEPTSGDLFKKSRSTGSSYREPKSSPTQSLSNSNEKESPFEKLYQSMKEELDVKSQKSCRKSEPQPDRAAEESRETQLLVSGRARAKSSGSTPVTAASSPKVGKIWTERWRGGMVPVQTSTETAKMKTPVRHSQQLKDEDSRVTGRRHSVNLDEGESAQAVHKTVTPGKLATRNQAAVEAGDVASPADTPEHSSSKKRSIPAKVEAPSAETQKRLSLTQRLVPGEKKTPKGSFSKPEKLATAAEQTCSGLPGLSSVDISNFGDSINKSEGMPMKRRRVSFGGHLRPELFDENLPPNTPLKRGETPTKRKSLGTHSPAVLKTIIKERPQSPGKQESPGITPPRTNDQRRRSGRTSSGSKFLCETDIPKKAGRKSGNLPAKRASISRSQHGILQMICSKRRSGASEANLIVAKSWADVVKLGVKQTQTKVAKHVPQKQTSKRQRRPSTPKKPTSNLHNQFTTGHANSPCTIVVGRAQIEKVSVPARPYKMLNNLMLNRKVDFSEDLSGLTEMFKTPVKEKQQQMSDTGSVLSNSANLSERQLQVTNSGDIPEPITTEILGEKVLSSTRNAAKQQSDRYSASPTLRRRSIKHENTVQTPKNVHNITDLEKKTPVSETEPLKTASSVSKLRRSRELRHTLVETMNEKTEAVLAENTTARHLRGTFREQKVDQQVQDNENAPQRCKESGELSEGSEKTSARRSSARKQKPTKDLLGSQMVTQTADYAEELLSQGQGTIQNLEESMHMQNTSISEDQGITEKKVNIIVYATKEKHSPKTPGKKAQPLEGPAGLKEHFETPNPKDKPITEDRTRVLCKSPQVTTENITTNTKPQTSTSGKKVDMKEESSALTKRIHMPGESRHNPKILKLECEDIKALKQSENEMLTSTVNGSKRTLEKSKKKAQPLEDLTCFQELFISPVPTNIIKKIPSKSPHTQPVRTPASTKRLSKTGLSKVDVRQEPSTLGKRTKSPGRAPGTPAPVQEENDSTAFMETPKQKLDFAGNSSGSKRRSRTSKNRSQPLEDLDGFQELFQTPAGASDSVTVEESAKISLESSQAEPVKTPASTKRRSKMSLMKVDMKELSILEKQTQSRGRDAGTPAPMQEGNGTTAIMETPKQKLDFTGNSTGHKRRPRTPKIRAQPLEDLDGFQELFQTPAGANDSVTVEESAKMSLESSQAEPVKTPASTKRLSKTDLSKVDVREDPSILGKKTKSPGRAPGTPAPVQEENDCTAYMETPKQKLESIENLTGLRKQSRTPKDITGFQDSFQIPDHANGPLVVVKTKKMFFNSPQPESAITRKSRERQSRASISKIDVKEELLESEEHLQLGEGVDTFQVSTNKVIRSSRKPAKRKLDSTAGMPNSKRMRCSSKDNTPCLEDLNGFQELFQMPGYANDSLTTGISTMLARSPQLGPVRTQINKKSLPKIILRKMDVTEEISGLWKQSLGRVHTTQEQEDNAIKAIMEIPKETLQTAADGTRLTRQPQTPKEKVQPLEDHSVFQELFQTSRYCSDPLIGNKQTRMSLRSPQPGFVRTPRTSKRLAKTSVGNIAVREKISPVSLPQCATGEVVHIPIGPEDDTENKGVKESTPQTLDSSASRTVSKRQQGAHEERPQFSGDLFHPQELFQTPASGKDPVTVDETTKIALQSPQPGHIINPASMKRQSNMSLRKDMREFSILEKQTQSRGRDAGTPAPMQEENGTTAIMETPKQKLDFIGNSTGHKRRPRTPKNRAQPLEDLDGFQELFQTPAGASDPVSVEESAKISLASSQAEPVRTPASTKRRSKTGLSKVDVRQEPSTLGKRMKSLGRAPGTPAPVQEENDSTAFMETPKQKLDFTGNSSGHKRRPQTPKIRAQPLEDLDGFQELFQTPAGANDSVTVEESVKMSLESSQAEPVKTPASTKRLSKTGLSKVDVREDPSILEKKTKSPGTPAPVQEENDCTAFMETPKQKLDFTGNSSGHKRRPRTPKIRAQPLEDLDGFQELFQTPAGASDSVTVEESAKMSLESSQAKPVKTPASTKRLSKTGLSKVDVREDPSTLGKKTKSPGRAPGTPAPVQEENDSTAFMETPKQKLDFAENSSGSKRRSRTSKNRSQPLEDLDGFQELFQTPAGASNPVSVEESAKISLESSQAEPVRTRASTKRLSKTGLNKMDVREGHSPLSKSSCASQKVMQTLTLGEDHGRETKDGKVLLAQKLEPAIYVTRGKRQQRSCKKRSQSPEDLSGVQEVFQTSGHNKDSVTVDNLAKLPSSSPPLEPTDTSVTSRRQARTGLRKVHVKNELSGGIMHPQISGEIVDLPREPEGEGKVIKTRKQSVKRKLDTEVNVPRSKRQRITRAEKTLEDLPGFQELCQAPSLVMDSVIVEKTPKMPDKSPEPVDTTSETQARRRLRRLVVTEEPIPQRKTTRVVRQTRNTQKEPISDNQGMEEFKESSVQKQDPSVSLTGRRNQPRTVKEKTQPLEELTSFQEETAKRISSKSPQPEEKETLAGLKRQLRIQLINDGVKEEPTAQRKQPSRETRNTLKEPVGDSINVEEVKKSTKQKIDPVASVPVSKRPRRVPKEKAQALELAGLKGPIQTLGHTDESASDKGPTQMPCNSLQPEQVDSFQSSPRRPRTRRGKVEADEEPSAVRKTVSTSRQTMRSRKVPEIGNNGTQVSKASIKQTLDTVAKVTGSRRQLRTHKDGVQPLEVLGDSKEITQISDHSEKLAHDTSILKSTQQQKPDSVKPLRTCRRVLRASKEDPKEVLVDTRDHATLQSKSNPLLSPKRKSARDGSIVRTRALRSLAPKQEATDEKPVPEKKRAASSKRHVSPEPVKMKHLKIVSNKLESVEEQVSTVMKTEEMEAKRENPVTPDQNSRYRKKTNVKQPRPKFDASAENVGIKKNEKTMKTASQETELQNPDDGAKKSTSRGQVSGKRTCLRSRGTTEMPQPCEAEEKTSKPAAEILIKPQEEKGVSGESDVRCLRSRKTRVALDSEPKPRVTRGTKKDAKTLKEDEDIVCTKKLRTRS
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Required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly. Associates with the surface of the mitotic chromosome, the perichromosomal layer, and covers a substantial fraction of the chromosome surface. Prevents chromosomes from collapsing into a single chromatin mass by forming a steric and electrostatic charge barrier: the protein has a high net electrical charge and acts as a surfactant, dispersing chromosomes and enabling independent chromosome motility. Binds DNA, with a preference for supercoiled DNA and AT-rich DNA (By similarity). Does not contribute to the internal structure of mitotic chromosomes. May play a role in chromatin organization. It is however unclear whether it plays a direct role in chromatin organization or whether it is an indirect consequence of its function in maintaining mitotic chromosomes dispersed.
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E9PX95
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ABCAH_MOUSE
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ATP-binding cassette sub-family A member 17
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MEVLKKLKLLLWKNFILKRRKTLITLLEMLMPLLFCAIVLYLRLNSMPRKKSSTNYPAVDVSLLPVYFYNYPLKSKFQLAYIPSKSETLKAVTEVVEQTFAVDFEVLGFPSVPLFEDYIIKDPKSFYILVGIIFHHDFNSSNEPLPLVVKYDLRFSYVQRNFVSPPRHLFFQEEIEGWCTAFLYPPNLSQAPREFSYADGGNPGYNKEGFLAIQHAVDKAIMRHHAPKAALNMFKDLHVLVQRFPFGPHIQDPFLVILQNEFPLLLMLSFICVELIITNSVLSEKERKQKEYMSMMGVESWLHWVAWFITFFISVSITVSVMTVLFCTKINRVAVFRNSNPTLIFIFLMCFAIATIFFAFMMSTFFQRAHVGTVIGGTVFFFTYLPYMYITFSYHQRTYTQKILSCLFSNVAMATGVRFISLFEAEGTGIQWRNIGSVWGDFSFAQVLGMLLLDSFLYCLIAFLVESLFPRKFGIPKSWYIFAKKPVPEIPPLLNIGDPEKPSKGNFMQDEPTNQMNTIEIQHLYKVFYSGRSKRTAIRDLSMNLYKGQVTVLLGHNGAGKTTVCSVLTGLITPSKGHAYIHGCEISKDMVQIRKSLGWCPQHDILFDNFTVTDHLYFYGQLKGLSPQDCHEQTQEMLHLLGLKDKWNSRSKFLSGGMKRKLSIGIALIAGSKVLILDEPTSGLDSPSRRAIWDLLQQQKGDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGSPSFLKQKYGAGYYMTIIKTPLCDTSKLSEVIYHHIPNAVLESNIGEEMIVTLPKKTIHRFEALFNDLELRQTELGISTFATSVTTMEEVFIRVCKLADPSTNVLTEKRHSLHPLPRHHRVPVDRIKCLHSGTFPVSTEQPMRLNTGFCLLCQQFYAMLLKKITYSRRNWMLVLSVQVLLPLAIIMLSLTFFNFKLRKLDNVPLELTLQTYGQTIVPFFIAENSHLDPQLSDDFVKMLVAAGQVPLRIQGSVEDFLLKKAKEAPEGFDKLYVVAASFEDVNNHTTVKALFNNQAYHSPSLALTLVDNLLFKLLSGANASITTTNYPQPQTAIEVSESILYQGPKGHYLVVNFLFGIAFLSSSFSILTVGEKSVKSKSLQFVSGVSTAVFWLSALLWDLISFLVPTLLLVLVFLWYKEEAFAHHESIPAVVLIMMLYGWAVIPLVYTVSFSFNTPGSACVKLVVMLTFLSISPVVLVTVTSEKDLGYTELSDSLDHIFLILPGHCLGMALSNLYYNFELKKFCSAKNLSDIDCNDVLEGYVVQENIYAWESLGIGKYLTALAVLGPVYITMLFLTEANAFYVLKSRLSGFFPSFWKEKSGMIFDVAEPEDEDVLEEAETIKRYLETLVKKNPLVVKEVSKVYKDKVPLLAVNKVSFVVKEEECFGLLGLNGAGKTSIFNMLTSEQPITSGDAFVKGFNIKSDIAKVRQWIGYCPEFDALLNFMTGREMLVMYARIRGIPECHIKACVDLILENLLMCVCADKLVKTYSGGNKRMLSTGIALVGEPAVILLDEPSTGMDPVARRLLWDTVERVRESGKTIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHLKSKFGISYSLQAKVRRKWQQQMLEEFKAFVDLTFPGSNLEDEHQNMLQYYLPGPNLSWAKVFSIMEQAKKDYMLEDYSISQLSLEDIFLNFTRPESSTKEQIQQEQAVLASPSPPSNSRPISSPPSRLSSPTPKPLPSPPPSEPILL
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Promotes cholesterol efflux from sperm which renders sperm capable of fertilization. Has also been shown to decrease levels of intracellular esterified neutral lipids including cholesteryl esters, fatty acid esters and triacylglycerols.
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E9PXF8
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MTMRD_MOUSE
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Myotubularin-related protein 13 (Inactive phosphatidylinositol 3-phosphatase 13) (SET-binding factor 2)
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MARLADYFIVVGYDHEKPAGPGEGLGKIIQRFPQQDWDDTPFPQGIELFCQPGGWHLSRERKQPTFFVVVLTDIDSDRHYCSCLTFYEAEINLQGTKKEEIEGEEVSGLIQPAEVFAPKSLVLVSRLDYPEIFRACLGLIYTVYVDSMSVSLESLIANLCACLVPAAGGSQKLFSLGAGDRQLIQTPLHDSLPVTGTSVALLFQQLGIQNVLNLFCAVLTENKVLFHSASFQRLSDACRALESLMFPLKYSYPYIPILPAQLLEVLSSPTPFIIGVHSIFKTDVHELLDVIIADLDGGTIKIPECIHLSSLPEPLLHQTQSALSLILHPDLEVADHAFPPPRTALSHSKMLDKEVRAVFLRLFAQLFQGYRSCLQLIRIHAEPVIHFHKTAFLGQRGLVENDFLTKVLNGMAFAGFVSERGPPYRACDLFDELVAFEVERIKVEEKNPLKMIKHIRELAEQLFKNENPNPHMAFQKVPRPTEGSHLRVHILPFPKINEARVQELIQENLAKNQNAPPATRIEKKCVVPAGPPVVSIMEKVITVFNSAQRLEVVRNCISFIFENKTLETEKTLPAALRALKGKAARQCLTDELGLHVQQNRAILDHQQFDYIIRMMNCTLQDCSSLEEYNIAAALLPLTSAFYRKLAPGVSQFAYTCVQDHPIWTNQQFWETTFYNAVQEQVRSLYLSAKDDNHIPHLKQKLPDGQHQEKTAMDLAAEQLRLWPTLSKSTQQELVQHEESTVFSQAIHFANLMVNLLVPLDTSKNKLLRASAPGDWESGSNSIVTNSIAGSVAESYDTESGFEDSENSDVANSVVRFIARFIDKVCTESGVTQDHIRSLHCMIPGIVAMHIETLEAVHRESRRLPPIQKPKILRPALLPGEEIVCEGLRVLLDPDGREEATGGLLGGPQLLPAEGALFLTTYRILFRGTPHDQLVGEQTVVRSFPIASITKEKKITMQNQLQQSVQEGLQITSASFQLIKVAFDEEVSPEVVDIFKKQLMKFRYPQSIFSTFAFAAGQTTPQIILPKQKEKNTSFRTFSKTIVKGAKKAGKMTIGRQYLLKKRTGTIVEERVNRPGWNEEDDISVSDDSELPTSTTLKASEKSTMEQLVEKACFRDYQRLGLGTISGNSSRSKPEYFRVTASNRLYSLCRSYPGLLVIPQAVQDSSLPRVARCYRHNRLPVVCWKNSRSGTLLLRSGGFHGKGVVGLFKSQNSPQAVSTSSLESSSSIEQEKYLQALLTAVIVHQKLRGSSTLTVRPALALSPVHGYRDKSFTQSNPKSSAKEPVHNQGVWASLRSSTRLISSPTSFIDVGARLAGKDHSASFSNSTYLQNQLLKRQAALYIFGEKSQLRSSKVEFAFNCEFVPVEFHEIRQVKASFKKLMRACIPSTIPTDSEVTFLKALGDSEWFPQLHRIMQLAVVVSEVLENGSSVWVCLEEGWDITTQVTSLAQLLSDPFYRTIAGFRTLVEKEWLSFGHKFSQRSSLALNSQGGGFAPIFLQFLDCVHQVHNQYPTEFEFNLYYLKFLAFHYVSNRFKTFLLDSDYERLEHGTLFDDKGDKHAKKGVCIWECIDKMHTRSPIFFNYLYSPVEVEALKPNVNVSSLKKWDYYTEETLSAGPSYDWMMLTPKHFPYEESDVAGGAGPQSQRKTVWPCYDDVTCSQPDALTRLFSEIEKLEHKLNQTPERWHQLWEKVTTDLKEEPRTAHSLRHSAGSPGIASTNVPSYQKRPALHPLHRGLGEDQSTTTAPSNGVEHRAATLYSQYTSKNDENRSFEGTLYKRGALLKGWKPRWFVLDVTKHQLRYYDSGEDTSCKGHIDLAEVEMVIPAGPSMGAPKYTSDKAFFDLKTSKRVYNFCAQDGQSAQQWMDRIQSCISDA
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Guanine nucleotide exchange factor (GEF) which activates RAB21 and possibly RAB28 (By similarity). Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form (By similarity). In response to starvation-induced autophagy, activates RAB21 which in turn binds to and regulates SNARE protein VAMP8 endolysosomal transport required for SNARE-mediated autophagosome-lysosome fusion (By similarity). Acts as an adapter for the phosphatase MTMR2. Increases MTMR2 catalytic activity towards phosphatidylinositol 3,5-bisphosphate and to a lesser extent towards phosphatidylinositol 3-phosphate.
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E9PXX9
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S28A1_MOUSE
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Sodium/nucleoside cotransporter 1 (Concentrative nucleoside transporter 1) (CNT 1) (Na(+)/nucleoside cotransporter 1) (Sodium-coupled nucleoside transporter 1) (Solute carrier family 28 member 1)
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MADDTPRQRESISLTPVAHGLENMGAEFLEIMEEGQLPHRHSSLPEGGGSRSKAVWKPFSRWRSLQPTVQARSLCREHWQLFEWISKGLLSTAYIGFLIVACLLDFPRALALFVITCVVLVFLAYNLLKRLLGSKLKKCVKFQGHSCLSLWLKRGLALAAGLGVILWLSLDTAQRPEQLVSFAGICVFLVLLFAGSKHHRAVSWRAVSWGLGLQFVLGLFVIRTEPGFVAFQWLGDQIRVFLSYTEAGSSFVFGEALVKDVFAFQVLPIIVFFSCVMSVLYYLGLMQWVILKIAWLMQVTMGTSATETLSVAGNIFVSQTEAPLLIRPYLADMTLSEVHVVMTGGYATIAGSLLGAYISFGIDASSLIAASVMAAPCALALSKLVYPEVEESKFRSEEGVKLTYGDAQNLVEAASAGAAISVKVVANIAANLIAFLAVLAFINAALSWLGDMVDIQGLSFQLICSYVLRPVAFLMGVAWEDCPVVAELLGIKLFLNEFVAYQELSQYKQRRLAGAEEWLGDKKQWISVRAEILTTYALCGFANFSSIGIMLGGLTSMVPQRRSDFSQIVLRALITGAFVSLVNACVAGILYVPRGVEVDCMSLLNQTVSSSSFEVYLCCRQVFQNTSLEFGQEALHNCCRFYNHTVCT
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Sodium and pyrimidine nucleoside symporter of the plasma membrane that imports uridine, thymidine and cytidine into cells by coupling their transport to the transmembrane sodium electrochemical gradient. Also transports adenosine, an atypical substrate transported with high apparent affinity, but low maximum velocity. Therefore, exhibits the transport characteristics of the nucleoside transport system cit or N2 subtype (N2/cit). Involved in renal nucleoside (re)absorption.
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E9PY46
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IF140_MOUSE
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Intraflagellar transport protein 140 homolog (WD and tetratricopeptide repeats protein 2)
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MALYFDHRIKAPDTPSSPSHITWHPTHPFLAVASISPSSGGNVDIYLEQGEPVPDTHIERSFQATSLCWHPTRLILAIGWETGEVIMFNKQDKEQHTVPLPHTTDIAILSWSTSGSCLVSGDKLGVLLLWRLDQRGRVQGTPLLKHEYGKALTHCIFRLPPPGEDLVQLAKAAVSGDEKALDMFNWRKSSFGSFLKTGSQEGLSFFVSLMDGTVHYVDEKGKTAQVASTDSSIQTLFYIERREALVVVTENLLLSLYVVTPEGEAEEVMKVKLSGKTGCRADITLIEGSLLVTAIGEPVLRFWDLERGENYILSLQEKFGFEKGESINCVCFCKAKGLLAAGTNKGRVAMWKKVPSFPNGRGAEGKDMWALQTPTELEGNITQIKWGSRKNLLAVSSTESVSILSEQAMSSHFHQQVAAVQISPSLVNVSFLSTGGTHSLHTDMHISGVFATKDAVAVWNGKQVAIFEPSGSTLRNAGTFLCETSVLAMHEESIYTVEPNRLQVRTWQGTVKQLLLFSETEGSPCFLDVCGTFLVAGTDLAHFKSFDLSRREAKVHCSCKNLAQLVPDVGSITSLRCNANGNKISILLSKVNNSPDSKIYIYDVEMDTVNVFNFTTGQIGQIQTLPFNEPPTNETRSFMDKSLAGYTPVNHFWDQSEPRLFVCEALQEAPGAQPQAVDKQPRVEEGTCHKEEVLILSFFASEEHGFLLHDSFPRPSTYQSLLGMEVPHYYFTKKPGEADKEDRVDSGYYHIPQMVAKRPLRDFVGLEDCDKSTRDAMLNFSFFVTIGDMDEAFKSIKLIKSEAVWENMARMCVKTQRLDVAKVCLGNMGHARGARALREAEQEPELEARVAMLAIQLGMLEEAEQLYKKCKRYDLLNKFYQASDQWQKAVEVAELHDRVHLRTTYYNYAKHLEASADCGQALSYYEKSDTHRFEVPRMLSEDLQSLELYINRMKDKTLWRWWAQYLESQAEMDTALRYYELAQDYFSLVRIHCFQGNIQKAAEIANETGDWAASYHLARQYESQDEVKQAVHFYTRAQAFNNAIRLCKENGLDDQLMNLALLSSPEDMIEAARYYEEKGEQMDRAVMLYHKAGHFSKALELAFTTQQFAALQLIAEDLDEKSDPALLARCSDFCIEHRQFEKAVELLLAAKKYHEALQLCLEQNMTITEDMAEKMTVSKDSKDMSEESRRELLEQIANCCMRQGNYHLATKKYTQAGNKLKAMRALLKSGDTEKIVFFAGVSRQKEIYIMAANYLQSLDWRKEPEIMKSIISFYTKGRALDLLAGFYDACAQVEIDEYQNYDKAHGALTEAYKCLSKAKTKNPLDQETKLAQLQSKMTLVKRFIQARRTYTEDPKESLRQCELLLEEPDLDSTIRVGDVYGFLVEHHVQMEEYQMAYKYLEEMRKRLPSANMSYYVDQRTVDTVHQGLGLLPPSRIMPERVRHNSMEDHKEVYEEVIEEVDNDP
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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) (By similarity). Plays a pivotal role in proper development and function of ciliated cells through its role in ciliogenesis and/or cilium maintenance. Required for the development and maintenance of the outer segments of rod and cone photoreceptor cells. Plays a role in maintenance and the delivery of opsin to the outer segment of photoreceptor cells.
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E9PY61
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GP179_MOUSE
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G-protein coupled receptor 179
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MGARAVVISSLAWGLLSCCFLCSGALGSQRPLRSLPPLPSQAKPRSEPMWMPPKGAEAALAFLYSGDVQRLSGANCSEKYEVRGAEGKAGVPPVLQRAAGTLAQAANFLNMLLQANDIRESSVEEDVEWYQALVRSVAEGDPKAYRALLTFNPAPGASHLQLALQATRMGDETVLQDLSGNKVQEETPGEDLDRPVLQKRVLTNDLRSLDSPKWPRGDGYVGDIQQVKLSPPFLECHEGQLRPGWLVTVSATFYGLKPDLTPEVRGQVQMDIDLQSVDINQCASGPGWYSNTHLCDLNSTQCVPLESQGFVLGRYLCRCRPGFYGASGSGGLEESATQAAGQFGSPQDSLGKLLRCQPCPEGCTSCLDATPCLVEEALALRTAVLACQACCMLAVFLSMLVAYRCRGSKRIRASGIVLLETILFGSLLLYFPVFILYFKPSVFRCVALRWVRLLGFAVVYGTIILKLYRVLQLFLSRTAQRVPHPSSGQLLRRLGQLLLLVLGFLVVWTAGALEPGTQHTALVTRGHTPTGRHFYLCHHDHWDYIMVVAEMLLLCWGSFLCYATRAVPSAFHEPRYMSIALHNELLLSTAFHTARFVLVPSLHPDWTLLLFFLHTHSTVTATLALIFIPKFWKPGAPPREEILDEVYEDELDLQRSGSYLNSSIASAWSERSLEPGDIRDELKKLYAQLEIRKTKEMAANNPHLPKKRGSSHQGLGRSFMRYLAEFPEALARQHSRDSGSLGLGSLPGSSRRRLLSSSLQETEKPPALRKTRSTYDHHREHNTLPFDSTLRRTLSKKASPTDGRESLADGPPALGFRSASAHNLTVGERLPRARPISLQKSLSVAAGSREKALLVASQAYLEETYRQAKEREERKKAEAAMVSPVRRPSTRRLEWPLRAPLSAPPSPGKSSSMDSSQTTARPHEEAGRRLPHPPIRHQVSTPVLALSGICLGEPRMLSPTPASTLAPILLPAPAPAPAPVLAPVSKPPQSPTLLTFICPWENAELPGKKENVVQEDPAGPERSGHSPASARTKIWRALSVAVEKRGTGESEALTEGGHVQGEADDTDEEKPKVFSKSHSLKTPLQQGSVRSLGLAIKALTRSRSTYKEKDGGEGTPETEKGKPTEVSTGAPLRSPRLGRPKAVSKQVALAPCEDEESLQNQQNAHTSRMLHVCQKEGSREQEDRNKRVAPGPGERKVERTGKITMTTLRQVFGEKNAEQAKESPAGYQEVPNPALQSLGSADHRVAEVCPWEVTEPESGMDPPESVNKAKVYSWERTEGGSLEKKPSRQVLSRSWEEREKVLAESETEGVGAIPRKKPERLVRSQEAVCPWESPDSGGLSPQLVHQESDRTGGRFVVVSKGDAHPEALPSHAAKAELCLWEMSDVGEGTSTQRVQELPEERQKSPKKATFWGERNLGGDLVSLCPWESTDFRGPSAVSLQAPGSSGSLGSGIAEVCPWEAENIANDKKAEVCPWELGEELAGSDGLNPGADGKSLPGKETPSRKGCLAESGEQTVRAKPTVPQGQESVCPWEDEAPERSSPQPDKASSKAGEKLLSHGGSQVLQVCPWEAVKPEEKQATLSTAEICPWEVDGQPETRTSEHPSKGEVHKDEEKMPGRARIKAQEEAEGRIQKQEAICPWESMAPGSTPQRDTEKAQASLQRQGSVAGRAAEICPWEVGTEVGEERTIGAEASEARPNDAGHASTDSGSRQVAASAPKKSERLGSEKEVVCPWDSLSPGDSSQQPDTPNTEKLKDELQEHGSSRPIEVCPWEAEEVPTGEKAKICPWELNEGTVGKGLEREPGCEPERQRRQNLEEAGLPFQEEGTSKGDTKLCREQEGEAICPWKPPAQVPKVSDLPLSTVGQGVEGQSLEASDRASEKGELRQDLKMGSLPEYITQVVPVDGGGASSELQPISLQEGMVLAGSSSHPHIQCPDQPRVSSQPLVSTGDGTAEVCPWDAPDSDSDTKVEPCAQKVTGRVTETEMSRQDEKEKSQEEKERAPETRDHEGVAVQKMPQTSNFGKQEAVCPRESQDFGVQAATDASDGSKGGSEKVCPWEVEEVPSIKEAEICPWEASPGAVGEGALDLGQDGESQGEGRAERHLLKAAETVCPLEGTMSSGLFTQEDVVDTDLPKVGLHGASSPGKGLAELCVWEVTDPEGNKIKGTMADICPWEETRAQSDESGPLALPVTQAGVPAAPEKSVCLSVHGPLESFLPESKSVRPDISKPPGSSRPEGVREQEPLELETGAKSVPKPSPTETEAPESFTLTDDQGLMASEGEAGELSPPPDYPWDCE
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Orphan receptor involved in vision. Required for signal transduction through retinal depolarizing bipolar cells. Acts as an atypical G-protein coupled receptor that recruits and regulates the R7 group RGS-GNB5 complexes instead of activating G proteins: promotes the GTPase activator activity of R7 RGS proteins, increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. Associates with components of metabotropic signaling cascade in retina ON-bipolar neurons, such as TRPM1 and GRM6: may control the ability of the GRM6 cascade to gate TRPM1.
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E9PYH6
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SET1A_MOUSE
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Histone-lysine N-methyltransferase SETD1A (EC 2.1.1.364) (SET domain-containing protein 1A)
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MDQEGGGDGQKAPSFQWRNYKLIVDPALDPALRRPSQKVYRYDGVHFSVSDSKYTPVEDLQDPRCHVRSKARDFSLPVPKFKLDEFYIGQIPLKEVTFARLNDNVRETFLKDMCRKYGEVEEVEILLHPRTRKHLGLARVLFTSTRGAKETVKNLHLTSVMGNIIHAQLDIKGQQRMKYYELIVNGSYTPQTVPTGGKALSEKFQGSGAAAETTEARRRSSSDTAAYPAGTTVGGTPGNGTPCSQDTNFSSSRQDTPSSFGQFTPQSSQGTPYTSRGSTPYSQDSAYSSSTTSTSFKPRRSENSYQDSFSRRHFSTSSAPATTATATSATAAATAASSSSSSSSSSSSSSSSSSSASQFRGSDSSYPAYYESWNRYQRHTSYPPRRATREDPSGASFAENTAERFPPSYTSYLAPEPNRSTDQDYRPPASEAPPPEPPEPGGGGGGSGGGGGGGGGGGGGAPSPEREEARTPPRPASPARSGSPAPETTNESVPFAQHSSLDSRIEMLLKEQRSKFSFLASDTEEEEENSSAGPGARDAGAEVPSGAGHGPCTPPPAPANFEDVAPTGSGEPGAARESPKANGQNQASPCSSGEDMEISDDDRGGSPPPAPTPPQQPPPPPPPPPPPPPPYLASLPLGYPPHQPAYLLPPRPDGPPPPEYPPPPPPPPPHIYDFVNSLELMDRLGAQWGGMPMSFQMQTQMLTRLHQLRQGKGLTAASAGPPGGAFGEAFLPFPPPQEAAYGLPYALYTQGQEGRGSYSREAYHLPLPMAAEPLPSSSVSGEEARLPHREEAEIAESKVLPSAGTVGRVLATLVQEMKSIMQRDLNRKMVENVAFGAFDQWWESKEEKAKPFQNAAKQQAKEEDKEKMKLKEPGMLSLVDWAKSGGITGIEAFAFGSGLRGALRLPSFKVKRKEPSEISEASEEKRPRPSTPAEEDEDDPEREKEAGEPGRPGTKPPKRDEERGKTQGKHRKSFTLDSEGEEASQESSSEKDEDDDDEDEEDEEQEEAVDATKKEAEASDGEDEDSDSSSQCSLYADSDGENGSTSDSESGSSSSSSSSSSSSSSSSSSESSSEEEEQSAVIPSASPPREVPEPLPAPDEKPETDGLVDSPVMPLSEKETLPTQPAGPAEEPPPSVPQPPAEPPAGPPDAAPRLDERPSSPIPLLPPPKKRRKTVSFSAAEEAPVPEPSTAAPLQAKSSGPVSRKVPRVVERTIRNLPLDHASLVKSWPEEVARGGRNRAGGRVRSTEEEEATESGTEVDLAVLADLALTPARRGLATLPTGDDSEATETSDEAERPSPLLSHILLEHNYALAIKPPPTTPAPRPLEPAPALAALFSSPADEVLEAPEVVVAEAEEPKQQLQQQHPEQEGEEEEEDEEEESESSESSSSSSSDEEGAIRRRSLRSHTRRRRPPLPPPPPPPPSFEPRSEFEQMTILYDIWNSGLDLEDMSYLRLTYERLLQQTSGADWLNDTHWVQHTITNLSTPKRKRRPQDGPREHQTGSARSEGYYPISKKEKDKYLDVCPVSARQLEGGDTQGTNRVLSERRSEQRRLLSAIGTSAIMDSDLLKLNQLKFRKKKLRFGRSRIHEWGLFAMEPIAADEMVIEYVGQNIRQMVADMREKRYVQEGIGSSYLFRVDHDTIIDATKCGNLARFINHCCTPNCYAKVITIESQKKIVIYSKQPIGVDEEITYDYKFPLEDNKIPCLCGTESCRGSLN
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Histone methyltransferase that catalyzes methyl group transfer from S-adenosyl-L-methionine to the epsilon-amino group of 'Lys-4' of histone H3 (H3K4) via a non-processive mechanism. Part of chromatin remodeling machinery, forms H3K4me1, H3K4me2 and H3K4me3 methylation marks at active chromatin sites where transcription and DNA repair take place (By similarity). Responsible for H3K4me3 enriched promoters and transcriptional programming of inner mass stem cells and neuron progenitors during embryogenesis. Required for H3K4me1 mark at stalled replication forks. Mediates FANCD2-dependent nucleosome remodeling and RAD51 nucleofilaments stabilization at reversed forks, protecting them from nucleolytic degradation. Does not methylate 'Lys-4' of histone H3 if the neighboring 'Lys-9' residue is already methylated (By similarity).
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E9PYI1
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ZN568_MOUSE
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Zinc finger protein 568
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MERLSQMAGRRAWCAEDSVPRQEEEDRTRPSKTVTFKDVAVDLTQEEWQQMKPAQRALYRDVMLETYSNLVTVGCQVTKPDVIFKLEQAEEPWVLEEEMFWRRSPEAARGRMKSFAFKDMAKDLRFEDVVIYFSLEEWECLRHSHRNLYRAVMLDNYSNLLSLSLADTKPRVVSLLEQGKEPWMVMRNETKIWHPDWVSRTEAKDSSKIKTLQEKMAKKHTCPTLEDSKTRGDREVTRELEGQQVHQEGHLRQAAVTSVERPDSVQCTAHREAHPGGKPCSSEKSQKTSLCQPPPIEREQLHSKAKASEHAQHGKVFNSCTSDTAVHPRPQESRKDSERKKSALAGGPDTSKPQSAQGSERPHKCKECGKAFHTPSQLSHHQKLHVGEKPYKCQECGKAFPSNAQLSLHHRVHTDEKCFECKECGKAFMRPSHLLRHQRIHTGEKPHKCKECGKAFRYDTQLSLHLLTHAGARRFECKDCDKVYSCASQLALHQMSHTGEKPHKCKECGKGFISDSHLLRHQSVHTGETPYKCKECGKGFRRGSELARHQRAHSGDKPYKCKECGKSFTCTTELFRHQKVHTGDRPHKCKECGKAFIRRSELTHHERSHSGEKPYECKECGKTFGRGSELSRHQKIHTGEKPYKCQQCGKAFIRGSHLTQHQRIHTGRRSE
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Has transcriptional repression activity, partially through the recruitment of the corepressor TRIM28 but has also repression activity independently of this interaction. Essential during embryonic development, where it acts as direct repressor of IGF2-P0, placental-specific transcript of IGF2, in early development and regulates convergent extension movements required for axis elongation and tissue morphogenesis in all germ layers. Also important for normal morphogenesis of extraembryonic tissues including the yolk sac, extraembryonic mesoderm and placenta. May enhance proliferation or maintenance of neural stem cells.
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E9PYK3
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PARP4_MOUSE
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Protein mono-ADP-ribosyltransferase PARP4 (EC 2.4.2.-) (ADP-ribosyltransferase diphtheria toxin-like 4) (ARTD4) (Poly [ADP-ribose] polymerase 4) (PARP-4) (Vault poly(ADP-ribose) polymerase) (VPARP) (mVparp)
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MTLGIFANCIFCLKVKYLPRQQKKKLQTDIKENGGKFSFLLNPQCTHVIVDSADVLSRCHLNSIQKNDVQIANPAFIQDSVRQRRLLDVRNYDPLSPAPAAPPAERSRSEVQSEYLPSDNTPEKENTEVTEVSAENVEIPPFLQDFEVVKYNILEKVGGPETVVVELQSSQDPESCPFVITAHFLLADQKTRRESTGKQTSEGAIEYYESYVEDLKRQGFLLQEHFTAEATQLASEKLQALLLEEVISSGALSQEVSDLLEVIWTEALGHLENTLLKPVNSMSLNDVSKAEGILLLVKTALKNGDSPGQLQKTMAEFYRLLPHRHPASEEVNLRLLAQKEDLCQLVRDMVNVCETNLSKPNPPSLAKYRALRCKIEHVDQNTEEFSRVRKEVLQNNRSEQPVDILQIFRVGRVNEATEFLSKLGNVRLLFHGSPVRNILGILSRGLLLPKVAEDRGVQRTDVGNLGSGIYFSDSLSTSIKYAHAGETDGSRLLVVCDVALGKCVNLFKKDFSLTEAPPGYDSVHGVSETTSVPTDFQDDEFVVYKTNQVKMKYIVKFCTPGDQIKEFHPHENTEVEEQRAEPSSVPEAGDFQLPDIKPFTNIKAGLQDASANPVPLDSVHIKGRVIDFVAQVIVFQTYTNQSHVPIEAKYIFPLDDKAAVCGFEAFINGKHIVGEIKEKEEARQEYREAVSQGHGAYLMDQDTPDVFTVSVGNLPPRAKVLIKITYITELSIQSPVAIFFIPGTVAPWQQDKALNENLQDTVETIRIKEIGAEQSFSLAMSIEMPYMIEFISSDTHELRQKSTDCKAVVSTVEGSSLDSGGFSLHIGLRDAYLPRMWVEKHPEKESEACMLVFQPELADVLPDLRGKNEVIICLDCSSSMEGVTFTQAKQVALYALSLLGEEQKVNIMQFGTGYKELFSYPKCITDSKMATEFIMSAAPSMGNTDFWKVLRYLSLLYPSEGFRNILLISDGHLQSESLTLQLVKRNIQHTRVFTCAVGSTANRHILRTLSQCGAGVFEYFNSKSKHSWKKQIEAQMTRIRSPSCHSVSVKWQQLSRDAPEPLQAPAWVPSLFHNDRLLVYGFIPHCTQATLQAFIQEKEFCTMVSTTELQKTTGTMIHKLAARALIRDYEDGILHDDETNHEMKKNIMKSLIIELSKENSLITQFTSFVAVEKRDVNEIPFANVPNISELVAKEDVDFLPYVSWQEKQPEASISQTEIDSSRLKHNKLSDGHGVLQPVSVSSEVNEKPSLLLAAKKRKIKTIKKCSLDISEDFEDRTAVAQSPATAQSLNFHLPLSVRPQLKAVEQQLHGNRLEPKQRGGFRKLLMAKKCRNVPDSLVSSAPAVTAEFSYLSACSSSSAFLSPLCDIPSSLPPHPLGGTHPPPPLPLPDGTHLPSPLFGSTHPPPPLFGGTLIPPPSSLFGGTHLPPPPPLPGGTHIPPPPPIPGGTLIPPSSSLFGGTHLPPPPLLSAGTHIPPPPLLSAGTHLPPPPLLPAGTHIPPPPPITGSTHPPPPSSLFGGTHLPPPPPLPGGTHIPPPPPIPGGTLIPSPSSLFGGTHLPPPPLLPAGTHIPPPPPITGSTHPPPPSSLFGGTHLPPPPPAGTQFSLSPIGFIPPKLGPPKLSHSHKLVGDTNIHDSEPPLLGFKDLCSRDMGFSCGTAFSGSFASSKDFDPGKFSQGPNNISFSPKAPEMGVLHQSPFCSPPKPPSAPPLVTNVLCSEAPQSYFLNLQSAAVHQSPNNRVSEIIMESVESSLPSDYSSRDASSYLALEGAEDSLLGGSSFETDTDEAAAFIANDLLTSIETSSDEECAFCDEDQESPVPWASLFALQTENGFWKLTPELGLILNLNVNALLTSLEEKGIRSLGTKGRERLLDLIATLLVLQFLYTKLEQEGMVAKSLIKMDDAFISRNIPWAFENIKKAREWARKTEGQYPSICQRLELGKDWESATKQLLGIQPQANTSLHRILYYSQG
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Mono-ADP-ribosyltransferase that mediates mono-ADP-ribosylation of target proteins.
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E9PYY5
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DNAI4_MOUSE
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Dynein axonemal intermediate chain 4 (WD repeat-containing protein 78)
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MHSSPTSTRKQASFAASASAQPRKSISFINPSKSSAGKGYAASNPNKLAVSRTMGFLTDMKPAEKLNVPSAKTVQVLDSKGVDVTPRPLYHPDPHAASAKPNKLLTSQEGSLGSDYISSYSLYQNTLNPSMLGQYTRSVLGSSSVSKSSISTTESMSEDLEDSSYKRDRLASFTDVRVLRSTAEAAISKEELEKTIEIILTETETLRFFDLPTVMFSTESEEAEKIIEKNKKYETLCRNRLGNDLYVERMMQTFNGAPKNKEVQCEKIILEEKGVVATTWDLYDSYNIPETLLAAKRSGYSSKGSLPAKDRDPKIQDSESSSLMDIENVILAKVQEDEEDNSEAILKSDKLHQDLFYMERVLMENVFQPKLAAYRQLPVYKEHEPEEPEETLQVENLKVAEDEPKKEDEEEVEMELELEIATEQSTIPANLERLWSFSCDLTKGLNVSSLSWNKANPDLLAVGYGNFGFREQKKGMACCWSIKNPMWPERIYQSSYGVTSVDFSNSSPNLLAVGYHNGTVAIYNVQSSHNIPVLDSSESPQKHLGPVWQVQWIEQDRGTTGDDKREILVSISADGRISKWIIRKGLDCHDLMRLKRTTATGGKKGGEKEKKGEALISRQAPGMCFAFHPKDTNIYLAGTEEGLIHKCSCSYNEQYLETYRGHKGPVYKVTWNPFCPDVFLSCSADWGVMIWHQDTVKPFLSFYPTTYVVYDVSWSPKSAYIFAAANENRVEIWDLQISTLDPLIVNVANPGIKFTTVLFAKETDCLLVGDSDGQVAVYELRNMPTASDTSRGDVINILLGPKTNHTG
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Plays a critical role in the assembly of axonemal dynein complex, thereby playing a role in ciliary motility.
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E9PZ19
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TUTLB_MOUSE
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Protein turtle homolog B (Immunoglobulin superfamily member 9B)
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MIWYVATLIASVISTRGLVAQGAHGLREEPEFVTARAGEGVVLRCDVIHPVTGQPPPYVVEWFKFGVPIPIFIKFGYYPPHVDPEYAGRASLHDKASLRLEQVRSEDQGWYECKVLMLDQQYDTFHNGSWVHLTINAPPTFTETPPQYIEAKEGGSITMTCTAFGNPKPIVTWLKEGTLLGASAKYQVSDGSLTVTSVSREDRGAYTCRAYSIQGEAVHTTHLLVQGPPFIVSPPENITVNISQDALLTCRAEAYPGNLTYTWYWQDENVYFQNDLKLRVRILIDGTLIIFRVKPEDAGKYTCVPSNSLGRSPSASAYLTVQYPARVLNMPPVIYVPVGIHGYIRCPVDAEPPATVVKWNKDGRPLQVEKNLGWTLMEDGSIRIEEATEEALGTYTCVPYNTLGTMGQSAPARLVLKDPPYFTVLPGWEYRQEAGRELLIPCAAAGDPFPVITWRKVGKPSRSKHNALPSGSLQFRALSKEDHGEWECVATNVVTSITASTHLTVIGTSPHAPGSVRVHVSMTTANVSWEPGYDGGYEQTFSVWMKRAQFGPHDWLSLSVPPGPSWLLVDSLEPETAYQFSVLAQNRLGTSAFSEVVTVNTLAFPVTTPEPLVLVTPPRCLTANRTQQGVLLSWLPPANHSFPIDRYIMEFRVGERWEMLDDAIPGTDGDFFAKDLSQDTWYEFRVLAVMQDLISEPSNIAGVSSTDIFPQPDLTDDGLARPVLAGIVATICFLAAAILFSTLAACFVNKQRKRKLKRKKDPPLSITHCRKSLESPLSSGKVSPESIRTLRAPSESSDDQGQPAAKRMLSPTREKELSLYKKTKRAISSRKYSVAKAEAEAEATTPIELISRGPDGRFVMGPSEMEPSVKGRRIEGFPFAEETDMYPEFRQSDEENEDPLVPTSVAALKPQLTPMSSSQDSYLPPPAYSPRFQPRGLEGPSGLGGRLQATGQARPPAPRPFQHGQYYGYLSSSSPGEVEPPPFYMPEVGSPLSSVMSSPPLHTEGPFGHPTIPEENGENASNSTLPLTQTPTGGRSPEPWGRPEFPFGGLETPAMMFPHQLHPCDVAESLQPKACLPRGLPPAPLQVPAAYPGMLSLEAPKGWVGKSPGRGPIPAPPATKWQERPMQPLVSQGQLRHTSQGMGIPVLPYPEPAEPGGHGGPSTFGLDTRWYEPQPRPRPSPRQARRAEPSLHQVVLQPSRLSPLTQSPLSSRTGSPELAARARPRPGLLQQAEMSEITLQPPAAVSFSRKSTPSSTGSPSQSSRSGSPSYRPTMGFTTLATGYPSPPPGPAPPAPGDTLDVFGQTPSPRRMGEEPLRPEPPTTLPTSG
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Transmembrane protein which is abundantly expressed in interneurons, where it may regulate inhibitory synapse development (By similarity). May mediate homophilic cell adhesion.
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E9PZ36
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PKHD1_MOUSE
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Fibrocystin (Polycystic kidney and hepatic disease 1 protein) (Polyductin)
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MMLAWLVSLLSMEVLLLAKPYSSFQFEPAEGSLAGGTWITVVFDGLDRSILYPNNGSQLQIDLVSVAIPTLRIPCDVSPAFVDLPVVTCQTRSLPSEADAGPYSLEMRSGEQVLGTPCPGSLDSCTFKFSKDQTPVLYQVYPASGVPGEVVSVYGRVITTWLETFDPDVDYIESPLILEAREDKWLTPCSLINRQTGSCFPIQEEHGLGNVQCRVEGDYIGSQNVSFSVFNKGRSMVHKEAWLISAKQELFLYQTYPEILSVFPKVGSLGGRTDIIITGDFFDPSARVTIAGIPCDIRYVSPRKIECTTRAPGNEARLTAPQAGNRGLRFEVGDATKDVELTEATPGYRWQIVPNASSPSGFWSKEGRPFRARLSGFFVAPQTNNYTFWIQADSQASLCFSSSEEPRTKVEVASVGVGTADWFDSWEQIGNEGSWHQKTTKLELQGGAKYYLEAEQHGIAPSRGMRIGVQIHNTWLNPDVVNTYLLEKHQIRARAQRLPEIQVLHVSGKGNFFLTWGNVSSQPVPANATAQQIQTTIEELLVVKCNLAPFSAHVLLRLGFEQGLEGSRSDGVRTSSTEPFCGRFSLGQLGHLILIPEAADKGYQLDRYPYLCLAYRGHMNKTLDMTVSFLFGFQTIMKNITCDWSLTDPHPESWQFTCINLWDTCLCHSEDIQSSLANTPLLAHRIDIRPVVPEAGLLYVDEIILADTNVTVSQADSGRACPGGNVVESVSVVGVPPVYSISSWLAGCGSELPLITACSVSTEGTGDGSELIEVTAQRLQRTSPPLGGHFFLYLSDTVIPDVPVRMSARQLHKLLQDSADESTSGYLNAGDFTVTEDLNSCYEHVWTLSWTTQTGDLPNFIRVSDQNLTGVNPTVTARVVYDGGVFLGPIFGDMLATANQQTQVAVQVNDIPAYCSGSCSFQYQQESTPSVDHVWYSLGSDVNLLVHFTGTGFPRDTQFLQVTVNKTSCEVLFSNETNVACELALLPVGVHQIFMLVIPSGLAVHASGEDLLLHVEPRLDAVEPSTAAEIGGRWVTLRGSSLEGVSLVLFGTQSCVIDAIRSNSQQIQCKVPPRGKDGYTVNVTVISGDHSTVLARAFTYVSSLNPVIVSLSRNRSSIAGGEILFLGMSLLVNYTDLDVQIHVQDTSAQVLSQTAWGLEVVLPPLVPGIHVISAFINGVSIRSQGVDLYIQYLTEVFSVEPCSGSLLGGTLLSLLGTGLGRDPALIRVLVDNHPCDIVNLTEVNIWCETPPAVLPPRADVLTVLASVEIWAGNTSFFHGPSLVGKGFTFTYEAAATPVVTAMWGEFRNNSVRFYVEGSNISDSVILLGSLKCELEVQFFGDSMNLSGCFFPLHSLEAGVYTLQVRHKRMGFANMSVVPQKFELSPQIIAIFPTHGSKCGGTVLTVKGMAFSSRKRSVHVDISGPFACMILSLEDHTVLCQTRFVGDQFSEASLALNITVLVNGLTSKCKGNCTLFIEEAATPIVDALTISISGSLTMVLMRGRRLATTADEPIAFVDDQLPCHTTFFNTSHVACQIRDLAPGFHYLSAVHTSAGYACLNSVSRNFFIVPQVLDYFPKDFSIHGGSLLTIKGTALRGWKATVVYVGRQACLTVNFSSDFIQCIVPAGNGSAALEIDVNGVLYHIGLVDYSSIFTPELLSVSRSQDILTFTVARISGAANVDIFIGTSPCLGVAGNRTVLQCMVPLLPAGEYLVTGYDHSRGWASSTLILVLRATVTSVTKNYGCLGGRLLHVLGAGFSPGNISAAVCGAPCQVLANATVSAFSCLVLPLHVSLAFLCDLRHAEDSCKVRSSTYLRCDLTVSMGTERLPGSWPYVYLCEESSLCLFEPDHWTESVFPSFSGLFLSPKVERDEVLIYNSSCNITMETEAEMECEMPNQPITAKITEIQKSWGQNTQGNFSFQFCRRWSRPHSWFPQRVPHDGDSVTVETGHLLLLDANTSFLNSLHIKGGKLIFMDPGPIELRAHSILITDGGELHIGSEEKPFQGKARIKIYGSVHSTPFFPYGVKFLAVRNGTLSLHGSVPEVTVTYLQAAAHAGDKVLTLGEAVDWKPGDEAVITSGMTVAGAEATEVVVVETVHNADLHLRNPLRYSYDFRENWVAGENPILKPTVALLSRNIIIQGNFTLERVKLLNSCQEANTAKGNLKHCLYSKSEKMLGARDLGARVIIQSFPEEPSFVKLKGVQFRDLGQAFHKHLSSLALVGAMRGSYIQSCSVWNSFSRGLSMHRTWGLKVDSNVFYKIVGHALLLGSYLDGRFSTSETVTGRKNGWWEQGSTIRNNVIISVSAAEGLSGSEMLAPAGIYTFSPTNVMEGNRVCAAGYGYVFHLVTSQTLQAPLLSFNWNTAHSCTRYGLLVYPKFQPPWNNDTGFTLFQNFMVWGSAGGAQIFRSNNLHLKNFQVYACRDFGIDILESDANTLITDSFLLGHFTHKGSLCMSAGIKTPQRWELTISNTTFVNFDGNCVAIRTCSGCFQGQGGYTVKTRQLKFVNSSNLVAFPFPHAAVLEDLDGSLSGKNGSHVLASMETLSDTCLTNASFSQIVPGSVCGEAVLFHRMSIALANSLDVPKNLTITDISNKTITVNYVEDTLSNYYGWMALLLDQETYSLQFESPWMNRSLQYSATFDSFAPGNYLLIMHRDLPPYPDILLRCGSQVGHSLPFHPLPSQDRACDWFFNRQLRQLTYLVSGEGQVKVFLQLKPGVPPSVSASTSVPESASRWSLPETWQDVEKGWGGYNHTIPGPGDDVLILPNKTVLVDTDLPVLRCLYVMGTLEFPVDRSNVLSVACLLIAGGELKVGTLENPLEKDQRLLIFLRASEEVVCDYFEGIHVDPGTIGVYGKLRLHSAYPKKSWVHLGADIAPGNERIIVHNAVDWQPHDTIVLSSSSYEAHEAEVLTVKEVKGHHIRIYERLKHRHIGSTHTMEDGQQVHLAAEVGLLTRNIRIQPDSSCRGRLLVGSFRKSSGEDFSGVLQLLNVEIQNMGLPLYSSIEFTGVSAGSWVISSTVHQSCSVGIHASSSHGVILTDNVVFGTNGHGIDVEGQNYSLTNNLVILTMQSANSSPWVAGIKVNYAEDIILHGNVVAGSERLGFHVGGHGCSSEVLWSDNVVHSSLHGLHLYKKHESNNCTGVSGFMAFKNFDYGAMVQTENSVDIQNITLVDNTVGLLAITYVSSALLSSVSTVQITLRNSVIVATSSSFDCIHDRKAPQSANWTSTDRAPSNPRGGRIGILWPVSASEPNAWPQEPWHKVRSRHSVPGIMKLQDVTFSSFVKSCYSNDLDVCILPNEYSTGVMYPITAERTRMLGIKDKNKFYFPVLQSSKDLVGTICPTLVCEYPRKYLFTDLDGRTLGLPPPVSVFPRTEEEWTGSFLNTGIFREEQKCTFRAMNQGFFCKQTEHAVLILDNVDATWTIPKSHPLVSVTNGFVDTFSIVKDSDLCPPTSSLSTFYSILPTRQMTKVCFPEQTPPFLRFLLLGNQRASKLILAVFYNEIQSPHVFLDKSFIPPTPLESAFSLLAEPSGANYFDIMNNLLYVVLQGEEPVEIHSSVSIHLALTVTFSVLEKGWERAMLESLSDFFQIDPNQIRLTLEMPGNKETLEAIANSERKRKRNCPSVTCGGPSIRYGQRRPLMAEMTSLKITPATTLETFSKVIVIEVGDLPNIRNSEPIQSLPSNRLQRLVNQVITAQQTGALENVLGMTVGALLVTQSKGVTGYRNASSLITGNLIYTRPSELSILVQPSDGEVGIELPVQPRLVFLDEKNERVESLGLPSEPWIISVSLEGASESVLKGCTLAETRDGYVTFSRLAVLISGSNWHLFFTVISPPGTNFTARSRTFVVLPVASKERSTIILALSLCSVASWVALSCLVCCWFKKSKTRKIKPEDISESQAKEQKKNTHNSSKPRGLQAKTAKENTLMGEDMRMKVMQGMQSQFPQHSMDGVSKRKVSRLAVTEERTTTPAPKIPRITCVPGSLAQQLTLQEPGNWQEAQQQLLRYQLAGRNQLLLLRPDLRQERKQGQEPSQLDKGSDCTGLSQEKATCIPTETFSLHTAPPETIQ
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Promotes ciliogenesis in renal epithelial cells and therefore participates in the tubules formation and/or ensures the maintenance of the architecture of the lumen of the kidney. Has an impact on cellular symmetry by ensuring correct bipolar cell division through the regulation of centrosome duplication and mitotic spindle assembly and by maintaining oriented cell division (OCD) during tubular elongation through planar cell polarity (PCP) pathway. During epithelial cell morphogenesis regulates also cell-cell and cell-matrix adhesion and participates in cell motility (By similarity). Promotes cell-cell contact through the positive regulation of PTK2 kinase activity leading to either positive regulation of epithelial cell proliferation through the HRAS/RAF1 pathways, or negative regulation of apoptosis through the PDK1/AKT1 pathway. May act in collecting-duct and biliary differentiation (By similarity). May participate in the regulation of the cholangiocytes proliferation and the CCN2 production in an CXCL8-dependent manner (By similarity).
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E9PZJ8
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ASCC3_MOUSE
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Activating signal cointegrator 1 complex subunit 3 (EC 3.6.4.12)
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MALPRLTGALRSFSNVTKQDNYNEEVADLKLKRSKLHEQVLDFGLTWKKIVKFLNEKLEKNKMQNINEDLKDILQAAKQIVGTDNGREAIESGAAFLFMTFHMTDSVGYMETKAIRQTFGPFPSSSATSACNATNRIISHFSQDDLTAFVQMAENPCNDRVVFGKNLAFSFDMYDLDHFDELPINGESQKTISLDYKKFLNEQFQEPYTPELKPVEKTNGSLLWCEVEKYLNATLKEMTEAARVEDLCCTLYDMLASAKSGDELQDELFELLGPEGLDLIEKLLQNRITIVDRFLNSSSDHKFQVLQDSCKKILGENSKPNYGCQVTIQSEQEKQLMKQYRREEKRIARREKKAGEDGEVSGEGVLPFDPKELRIQREHALLNARNAPILGRQRDVEFEKIRYPHVYDSQAQARETSAFIAGAKMILPEGIQRENTKLYEEVRIPYGEPMPVGFEEKPVYIKDLDEVGQLAFKGMKRLNRIQSIVFETAYNTNENMLICAPTGAGKTNIAMLTILHEIRQHFHQGVIKKNEFKIVYVAPMKALAAEMTNYFSKRLEPLGIVVKELTGDMQLSKSEILRTQMLVTTPEKWDVVTRKSVGDVALSQIVKLLILDEVHLLHEDRGPVLESIVARTLRQVESTQSMIRILGLSATLPNYLDVATFLHVNPYIGLFYFDGRFRPVPLGQTFLGIKSTNKMQQLNNMDEVCYESVLKQVKAGHQVMVFVHARNATVRTAMSLIERAKNSGQISCFLPTEGPEYGHALKQVQKSRNKQVRELFSDGFSIHHAGMLRQDRNLVENLFSNGHIKVLVCTATLAWGVNLPAHAVVIKGTQIYAAKRGSFVDLGILDVMQIFGRAGRPQFDKFGEGIIITTHDKLSHYLSLLTQQNPIESQFLESLADNLNAEIALGTVTNVEEAVRWMSYTYLYVRMRANPLAYGISHKAYQIDPTLRKHREQLLIEVGQKLDKAKMIRFEERTGYFSSTDLGRTASHFYIKYNTIETFNELFDAHKTEGDIFAIVSKAEEFDQIKVREEEIEELDALLNNFCELSAPGGVENSYGKINILLQTYISRGEMDSFSLISDSAYVAQNAARIVRALFEIALRKRWPTMTYRLLNLSKVIDKRLWGWASPLRQFSVLPPHILTRLEEKNLTVDKLKDMRKDEIGHILHHVNIGLKVKQCVHQIPSVTMEASIQPITRTVLRVSLNIHPDFSWNDQVHGTVGEPWWIWVEDPTNDHIYHSEYFLALKKQVINKEAQLLVFTIPIFEPLPSQYYIRAVSDRWLGAEAVCIINFQHLILPERHPPHTELLDLQPLPITALGCKAYEALYNFSHFNPVQTQIFHTLYHTDCNVLLGAPTGSGKTVAAELAIFRVFNKYPTSKAVYIAPLKALVRERMDDWKIRIEEKLGKKVIELTGDVTPDMKSIAKADLIVTTPEKWDGVSRSWQNRSYVQQVNILIIDEIHLLGEERGPVLEVIVSRTNFISSHTEKPVRIVGLSTALANARDLADWLNIKQMGLFNFRPSVRPVPLEVHIQGFPGQHYCPRMASMNKPAFQAIRSHSPAKPVLIFVSSRRQTRLTALELIAFLATEEDPKQWLNMDEQEMDNIIGTVRDSNLKLTLAFGIGMHHAGLHERDRKTVEELFVNCKVQVLIATSTLAWGVNFPAHLVIIKGTEYYDGKTRRYVDFPITDVLQMMGRAGRPQFDDQGKAVILVHDIKKDFYKKFLYEPFPVESSLLGVLSDHLNAEIAGGTITSKQDAMDYITWTYFFRRLIMNPSYYSLGDVSQDSINKFLSHLIGQSLVELELSHCIEVGEDNRTIEPLTCGRIASYYYLKHKTVKMFKDRLKPECSTEELLSILSDAEEYTDLPVRHNEDHTNNELAKCLPIELNPHSFDSPHTKAHLLLQAHLSRAMLPCPDYDTDTKTVLDQALRVCQAMLDVAASQGWLVTVLNITHLIQMVIQGRWLKDSSLLTIPNIEQHHLHLFRKWKPPVKSSHAKCRTSIECLPELIHACEGKDHVFSSMVEKELQPAKTKQAWNFLSRLPVINVGISVKGSWDDLVEGHNELSISTLTADKRDENKWIKLHADQEYVLQVSLQRVHFGLPKGKHENHAVTPRFPKLKDEGWFLILGEVDKRELMAVKRVGFVRTHHDASISFFTPETPGRYIFTLYLMSDCYLGLDQQYDIYLNVIKANISTKDSDVFTDLSV
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ATPase involved both in DNA repair and rescue of stalled ribosomes. 3'-5' DNA helicase involved in repair of alkylated DNA: promotes DNA unwinding to generate single-stranded substrate needed for ALKBH3, enabling ALKBH3 to process alkylated N3-methylcytosine (3mC) within double-stranded regions. Also involved in activation of the ribosome quality control (RQC) pathway, a pathway that degrades nascent peptide chains during problematic translation. Drives the splitting of stalled ribosomes that are ubiquitinated in a ZNF598-dependent manner, as part of the ribosome quality control trigger (RQT) complex. Part of the ASC-1 complex that enhances NF-kappa-B, SRF and AP1 transactivation.
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E9PZM4
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CHD2_MOUSE
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Chromodomain-helicase-DNA-binding protein 2 (CHD-2) (EC 3.6.4.12) (ATP-dependent helicase CHD2)
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MMRNKDKSQEEDSSLHSNASSRSASEEVSGSDSGSQSESEQGSEPGSGHGSESNSSSESSESQSESESESAGSKSQPVLPEAKEKPASKKERIADVKKMWEEYPDVYGVRRSNRSRQEPSRFNVKEEASSGSESGSPKRRGQRQLKKQEKWKQDPSEDEQEQGTSAESEAEQKKGKARRPVPRRTVPKPQVKKQPKIQRGKRKKQESSDDDDDDDEAPKRQTRRRAAKNVSYKEDDDFETDSDDLIEMTGEGGDEQQDNSETIEKVLDSRLGKKGATGASTTVYAVEANGDPSDDFDTEREEGEVQYLIKWKGWSYIHSTWESEDSLQQQKVKGLKKLENFKKKEDEVKQWLGKVSPEDVEYFSCQQELASELNKQYQIVERVIAVKTSKSTLGQTDFPAHSRKPAPSNEPEYLCKWMGLPYSECSWEDEALIGKKFQNCIDSFHSRNNSKTIPTRECKALKQRPRFVALKKQPAYLGGESLELRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLIVVPLSTLTSWQREFEIWAPEINVVVYIGDLMSRNTIREYEWIHSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENGYQSLHKVLEPFLLRRVKKDVEKSLPAKVEQILRVEMSALQKQYYKWILTRNYKALAKGTRGSTSGFLNIVMELKKCCNHCYLIKAPEDSERESGQEVLQSLIRSSGKLILLDKLLTRLRERGNRVLIFSQMVRMLDILAEYLTIKHYPFQRLDGSIKGEIRKQALDHFNADGSEDFCFLLSTRAGGLGINLASADTVVIFDSDWNPQNDLQAQARAHRIGQKKQVNIYRLVTKGTVEEEIIERAKKKMVLDHLVIQRMDTTGRTVLENNSGRSNSNPFNKEELTAILKFGAEDLFKEIEGEESEPQEMDIDEILRLAETRENEVSTSATDELLSQFKVANFATMEDEEELEERPHKDWDEIIPEEQRKKVEEEERQKELEEIYMLPRIRSSTKKAQTNDSDSDTESKRQAQRSSASESETDDSDDDKKPKRRGRPRSVRKDLVEGFTDAEIRRFIKAYKKFGLPLERLECIARDAELVDKSVADLKRLGELIHNSCVSAMQEYEEQLKESTSEGKGPGKRRGPTIKISGVQVNVKSIIQHEEEFEMLHKSIPVDPEEKKKYCLTCRVKAAHFDVEWGVEDDSRLLLGIYEHGYGNWELIKTDPELKLTDKILPVETDKKPQGKQLQTRVDYLLKLLRKGLEKKGTVASGEEAKLKKRKPRVKKENKAPRLKDEHGLEPASPRHSDNPSEEGEVKDDGLEKSPTKKKQKKKENKENKEKPVSSRKDREGDKERKKSKDKKEKVKGGDGKSSSKSKRSQGPVHITAGSEPVPIGEDEDDDLDQETFSICKERMRPVKKALKQLDKPDKGLSVQEQLEHTRNCLLKIGDRIAECLKAYSDQEHIKLWRRNLWIFVSKFTEFDARKLHKLYKMAHKKRSQEEEEQKKKDDSLGGKKPFRPEASGSSRDSLISQSHTSHNLHPQKPHLPASHGPQMHGHPRDNYSHPNKRHFSNADRGDWQRERKFNYGGGNSAPWGGDRHHQYEQHWYKDHHYGDRRHMDAHRSGSYRPNNMSRKRPYEQYNSDRDHRGHRDYYDRHHHDSKRRRSDDFRPQNYHQQDFRRMSDHRPTMGYHGQGPSDHYRSFHTDKLGEYKQPMPSLHTALSDPRSPPSQKSPHDSKSPLDHRSPLERSLEQKNNPDYNWNVRKT
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DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. Involved in myogenesis via interaction with MYOD1: binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to the onset of myogenic gene expression, promoting their expression.
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E9PZQ0
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RYR1_MOUSE
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Ryanodine receptor 1 (RYR-1) (RyR1) (Skeletal muscle calcium release channel) (Skeletal muscle ryanodine receptor) (Skeletal muscle-type ryanodine receptor) (Type 1 ryanodine receptor)
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MGDGGGEGEDEVQFLRTDDEVVLQCSATVLKEQLKLCLAAEGFGNRLCFLEPTSNAQNVPPDLAICCFILEQSLSVRALQEMLANTVEAGVESSQGGGHRTLLYGHAILLRHAHSRMYLSCLTTSRSMTDKLAFDVGLQEDATGEACWWTMHPASKQRSEGEKVRVGDDLILVSVSSERYLHLSTASGELQVDASFMQTLWNMNPICSGCEEGFVTGGHVLRLFHGHMDECLTISPSDSDDQRRLVYYEGGPVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHVTTGRYLGLTEDQGLVVVDASKAHTKATSFCFRISKEKLDVAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKALRLGVLKKKAMLHQEGHMDDALSLTRCQQEESQAARMIYSTAGLYNQFIKGLDSFSGKPRGSGPPAGSALPIEGVILSLQDLIGYFEPPSEELQHEEKQTKLRSLRNRQSLFQEEGMLSLVLNCIDRLNVYTTAAHFAEFAGEEAAESWKEIVNLLYELLASLIRGNRTNCALFSTNLDWLVSKLDRLEASSGILEVLYCVLIESPEVLNIIQENHIKSIISLLDKHGRNHKVLDVLCSLCVCNGVAVRSNQDLITENLLPGRELLLQTNLINYVTSIRPNIFVGRAEGSTQYGKWYFEVMVDEVAPFLTAQATHLRVGWALSEGYSPYPGGGEGWGGNGVGDDLYSYGFDGLHLWTGHVARPVTSPGQHLLAPEDVVSCCLDLSVPSISFRINGCPVQGVFESFNLDGLFFPVVSFSAGIKVRFLLGGRHGEFKFLPPPGYAPCHEAVLPRERLHLQPIKEYRREGPRGPHLVGPSRCLSHLDFVPCPVDTIQIVLPPHLERIREKLAENIHELWALTRIEQGWTYGPVRDDNKRLHPCLVNFHSLPEPERNYNLQMSGETLKTLLALGCHVGMADEKAEDNLKKTKLPKTYMMSNGYKPAPLDLSHVRLTPAQTTLVDRLAENGHNVWARDRVAQGWSYSAVQDIPARRNPRLVPYRLLDEATKRSNRDSLCQAVRTLLGYGYNIEPPDQEPSQVDSQSRGDRARIFRAEKSYAVQSGRWYFEFEAVTTGEMRVGWARPELRPDVELGADDLAYVFNGHRGQRWHLGSEPFGRPWQSGDVVGCMIDLTENTIIFTLNGEVLMSDSGSETAFRDIEIGDGFLPVCSLGPGQVGHLNLGQDVSSLRFFAICGLQEGFEPFAINMQRPVTTWFSKSLPQFEPVPLEHPHYEVARMDGTVDTPPCLRLTHRTWGSQNSLVEMLFLRLSLPVQFHQHFRCTAGATPLASPGLQPPAEDEARAAEPDTDYENLRRSAGGWGEAEGGKDGTAKEGTPGGTAQAGVEAQPARAENEKDATTEKNKKRGFLFKAKKVAMMTQPPSTPALPRLPRDVVPADNRDDPEIILNTTTYYYSVRVFAGQEPSCVWVGWVTPDYHQHDMSFDLSKVRAVTVTMGDEQGNVHSSLKCSNCYMVWGGDFVSPGQQGRISHTDLVIGCLVDLATGLMTFTANGKESNTFFQVEPNTKLFPAVFVLPTHQNVVQFELGKQKNIMPLSAAMFLSERKNPAPQCPPRLEVQMLMPVSWSRMPNHFLQVDTRRAGERLGWAVQCQEPLMMMALHIPEENRCMDILELSERLDLQRFHSHTLSLYRSVCALGNNRVAHALCSHVDQAQLLHALEDARLPGPLRAGYYDLLISIHLESACRSRRSMLSEYIVPLTPETRAITLFPPGRSAEDGPRRHGLPGVGVTTSLRPPHHFSPPCFVVALPAAGATEAPARLSPAIPLEALRDKALRMLGEAVRDGGQHARDPVGGSVEFQFVPVLKLVSTLLVMGVFSDEDVKQILKMIEPEVFREEEEVEEEGEEEEEDEEEKEEDEEEEAHEKEDEEKEEAEDAAEEEKEELEEGLLQMKLPESVKLQMCHLLEYFCDQELQHRVESLAAFAECYVDKMQGNQRGRYGLLMKAFTMSAAETARRTREFRSPPQEQINMLLHFKNGADEEECPLPEEIRQELVNFHQDLLAHCGIQLEGEEEEPEEESTLGSRLMSLLEKVKLVKKTEEKPEEEPAPEEHKPQSLQELVSHTVVRWAQEDFVQSPELVRAMFSLLHRQYDGLGELLRALPRAYTISVSSVEDTMSLLECLGQIRSLLIVQMGPQEENLMIQSIGNIMNNKVFYQHPNLMRALGMHETVMEVMVNVLGGGESKEIRFPKMVTSCCRFLCYFCRISRQNQRSMFDHLSYLLENSGIGLGMQGSTPLDVAAASVIDNNELALALQEQDLEKVVSYLAGCGLQSCPMLLAKGYPDIGWNPCGGERYLDFLRFAVFVNGESVEENANVVVRLLIRKPECFGPALRGEGGSGLLAAIEEAIRISEDPARDGPGVRRDRRREHFGEEPPEENRVHLGHAIMSFYAALIDLLGRCAPETHLIQAGKGEALRIRAILRSLVPLDDLVGIISLPLQIPTLGKDGALVQPKMSASFVPDHKASMVLFLDRVYGIENQDFLLHVLDVGFLPDMRAAASLDTATFSTTEMALALNRYLCLAVLPLITKCAPLFAGTEHRAIMVDSMLHTVYRLSRGRSLTKAQRDVIEDCLMALCRYIRPSMLQHLLRRLVFDVPILNEFAKMPLKLLTNHYERCWKYYCLPTGWANFGVTSEEELHLTRKLFWGIFDSLAHKKYDQELYRIAMPCLCAIAGALPPDYVDASYSSKTEKKATVDAEGNFDPRPVETLNVIIPEKLDSFINKFAEYTHEKWAFDKIQNNWSYGENIDEELKTHPMLRPYKTFSEKDKEIYRWPIKESLKAMIAWEWTVEKAREGEEEKTEKKKTRKISQTAQTYDPREGYNPQPPDLSVVTLSRELQAMAEQLAENYHNTWGRKKKQELEAKGGGSHPLLVPYDTLTAKEKARDREKAQELLKFLQMNGYAVTRGLKDMELDTSSIEKRFAFGFLQQLLRWMDISQEFIAHLEAVVSSGRVEKSPHEQEIKFFAKILLPLINQYFTNHCLYFLSTPAKVLGSGGHASNKEKEMITSLFCKLAALVRHRVSLFGTDAPAVVNCLHILARSLDARTVMKSGPEIVKAGLRSFFESASEDIEKMVENLRLGKVSQARTQVKGVGQNLTYTTVALLPVLTTLFQHIAQHQFGDDVILDDVQVSCYRTLCSIYSLGTTRNPYVEKLRPALGECLARLAAAMPVAFLEPELNEYNACSVYTTKSPRERAILGLPNSVEEMCPDIPVLERLMAEIGGLAESGARYTEMPHVIEITLPMLCSYLPRWWERGPEAPPPALPAGAPPPCTAVTSDHLNSLLGNILRIIVNNLGIDEASWMKRLAVFAQPIVSRARPELLRSHFIPTIGRLRKRAGKVVAEEEQLRLEAKAEAEEGELLVRDEFSVLCRDLYALYPLLIRYVDNNRAHWLTEPNPNAEELFRMVGEIFIYWSKSHNFKREEQNFVVQNEINNMSFLTADNKSKMAKAGDVQSGGSDQERTKKKRRGDRYSVQTSLIVATLKKMLPIGLNMCAPTDQDLIVLAKARYALKDTDEEVREFLQNNLNLQGKVEGSPSLRWQMALYRGVPGREEDADDPEKIVRRVQEVSAVLYHLDQTEHPYKSKKAVWHKLLSKQRRRAVVACFRMTPLYNLPTHRACNMFLESYKASWILTEDHSFEDRMIDDLSKAGEQEEEEEEVEEKKPDPLHQLVLHFSRTALTEKSKLDEDYLYMAYADIMAKSCHLEEGGENGEEGGEEEEVEVSFEEKEMEKQRLLYQQSRLHNRGAAEMVLQMISACKGETGAMVSSTLKLGISILNGGNAEVQQKMLDYLKDKKEVGFFQSIQALMQTCSVLDLNAFERQNKAEGLGMVNEDGTVINRQNGEKVMADDEFTQDLFRFLQLLCEGHNNDFQNYLRTQTGNTTTINIIICTVDYLLRLQESISDFYWYYSGKDVIEEQGKRNFSKAMSVAKQVFNSLTEYIQGPCTGNQQSLAHSRLWDAVVGFLHVFAHMMMKLAQDSSQIELLKELLDLQKDMVVMLLSLLEGNVVNGMIARQMVDMLVESSSNVEMILKFFDMFLKLKDIVGSEAFQDYVTDPRGLISKKDFQKAMDSQKQFTGPEIQFLLSCSEADENEMINCEEFANRFQEPARDIGFNVAVLLTNLSEHVPHDPRLRNFLELAESILEYFRPYLGRIEIMGASRRIERIYFEISETNRAQWEMPQVKESKRQFIFDVVNEGGESEKMEMFVSFCEDTIFEMQIAAQISEPEGEPEEDEDEGAEEAEEGAAGSDGSGSAAAAGVWVWLAATAGRTLRGLSYRSLRRRVRRLRRLTAREAATAVAALLWALVTRAGGAGAGAAAGALRLLWGSLFGGGLVDSAKKVTVTELLAGMPDPTGDEVHGQQPSGAGSDAEGEGEGEGEGDAADGAGDEEAAADQAGTGGADGAVAVADGSPFRPEGAGGLGDMGDTTPVEPPTPEGSPILKRKLGVDGEEEEPPPEPEPEPEPEPEKADTENGEKEVPEPPPEPPKKTPPPPPPKKEEAGGAGLEEFWGELEVQRVKFLNYLSRNFYTLRFLALFLAFAINFILLFYKVSDSPPGEDDIEGSGAGDMSGAGSGDGSGWGSRAGEEVEGDEDENMVYYFLEESTGYMEPALRCLSLLHTLVAFLCIIGYNCLKVPLVIFKREKELARKLEFDGLYITEQPEDDDVKGQWDRLVLNTPSFPSNYWDKFVKRKVLDKHGDIFGRERIAELLGMDLASLEITAHNERKPDPPPGLLTWIMSIDVKYQIWKFGVIFTDNSFLYLGWYMVMSLLGHYNNFFFAAHLLDIAMGVKTLRTILSSVTHNGKQLVMTVGLLAVVVYLYTVVAFNFFRKFYNKSEDEDEPDMKCDDMMTCYLFHMYVGVRAGGGIGDEIEDPAGDEYELYRVVFDITFFFFVIVILLAIIQGLIIDAFGELRDQQEQVKEDMETKCFICGIGSDYFDTTPHGFETHTLEEHNLANYMFFLMYLINKDETEHTGQESYVWKMYQERCWDFFPAGDCFRKQYEDQLS
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Calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules. Repeated very high-level exercise increases the open probability of the channel and leads to Ca(2+) leaking into the cytoplasm. Can also mediate the release of Ca(2+) from intracellular stores in neurons, and may thereby promote prolonged Ca(2+) signaling in the brain. Required for normal embryonic development of muscle fibers and skeletal muscle. Required for normal heart morphogenesis, skin development and ossification during embryogenesis.
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E9PZZ1
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PRD13_MOUSE
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PR domain zinc finger protein 13 (EC 2.1.1.-) (PR domain-containing protein 13)
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MPAHVTPRTEDARRGAGPSSACGCSWFCHLRPVEDPASPSVCLAAVATMHGTSRTSATSVNADCCIPAGLRLGPVPGTFKLGKYLSDRREPGPKKKVRMVRGELVDESGGSPLEWIGLIRAARNPQEQTLEAIADLPGGQIFYRALRDVQPGEELTVWYSNSLAQWFDIPTTATPTHDEKGEERYICWYCWRTFRYPNSLKAHLRFHCVLSGGGGRAFLPQEHAARPGASPVAEGLGLPPKPTVPDLTAPVQAIALRPQAPAAQLAQACGARESIKREASLAPLATSPPPGKWGTPKKGKEQPDRAHSQFLGIVGGSSGGGGGLPFYPGVRSAFKPAGLARAAAQSDPYREEGGGKGPGLALGRLLGGGRAGGRPGSGESPAGHHHHHHHAHHHHHHHPKCLLAGEPPPAGLPCPGALRAFPLLAGHPEEASAFKHVERAPPAAATTSLPSARYAALPAPGLPVERCALQPLDGGSLKAYPGGGGGGECSPLPAVMPAFTVYSGDLLYGPPAAYYPLKLHLGGLLKYPESISYLSGPAAAAAAAAAAAAAAAAIGPAELGSLASIDREIAMHTQQLSEMAAGKSRARLDSGTLPPAVVAATGPGGGGGGGSAAGKPKTGHLCLYCGKLYSRKYGLKIHMRTHTGYKPLKCKVCLRPFGDPSNLNKHIRLHAEGNTPYRCEFCGKVLVRRRDLERHVKSRHPGQSLMAKAGDGPGPEPSYALEPGDPKSEDSDVDVCFTDDQSDPEAGGRGEHDS
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May be involved in transcriptional regulation. Is required for the differentiation of Kiss1-expressing neurons in the arcuate (Arc) nucleus of the hypothalamus. Is a critical regulator of GABAergic cell fate in the cerebellum, required for normal postnatal cerebellar development. {ECO:0000250, ECO:0000269|PubMed:34730112}.
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E9Q0N2
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PTPRH_MOUSE
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Receptor-type tyrosine-protein phosphatase H (R-PTP-H) (EC 3.1.3.48) (Stomach cancer-associated protein tyrosine phosphatase 1) (SAP-1)
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MARAGGNCGVWRSLVLLGLYGCSVVRAAGTSVTVDRHAPASSYEFSMWVEKDGVSSSPQIPVTTAAPNPVRNLRVEGQNNISISLSWEPPDQSSLQGLTYWTQCSRHGGQTETRNTTDTSVTVDGLDPGSSYECSVWVEKDGLYSKNETLNTSTAPNPVRNLRVEGQNNISISLSWEPPDQPSLQGLTYWAQCSRHGGQTETRNTADTSVTVDGLDPGSSYECSVWVEKDGVYSTNETLNTSTAPNPVRNLRVEGQNNISISLSWEPPDQPSLQGLTYWAQCSRHGGQTETRNTTDTSITVDGLDPGSSYECSVWVEKDGVYSTNETLSNTTAPNPVRNLRVKSQNNFSISLSWEPPDQPSLQGLIYWAQCSRHGGQTETRNTTDTSVTVDGLDPGFLYKCSVWVEKDGVYSTNETLNTSTVPISASNPVRNLRVEGQNNFSISLSWEPPDQSSLQGLTYWAQCSRHGGQTETRNTADTSVTVDGLDPGSSYECSVWVEKDGVYSTNETLNTSTVPAAVNITSCISTSGGYGVLLTWSCPSGGYESFEVKVGRKWRSENGSLCGKGVTVSDLEPAQSYTATVTTVFKDLKAQSLSTTCHTESAAIIAGAIVGILLLFILVGLLIVFLKRRRKKRQPKEVPKDLVCSCPGDILAKDFADHVRENEKDSNCGFAEEYQQLALEGQGQSQITASALENRSKNRYRNVLPYDWSRVPLQPLQEEPGSDYINASFMPGLWSPKEFIATQGPLPNTVGDFWRMVWEQQSHTLVMLTNCMESGRVKCEHYWPLDAQPCIHGQLQVMLISEEASENWTVRHLQLFHMKEQQTLSLRQFHYLAWPDHGVPYSPDPLLAFRKMLRQWMDQTTDGGPPIVHCSAGVGRTGTLIALDVLLRQLECEGLVGPFSFVKKMRESRPLMVQTEAQYVFLHQCILKSLQKPAPALVPEEAMYENVASLVYENASAIMAHESEFSASGC
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Protein phosphatase that may contribute to contact inhibition of cell growth and motility by mediating the dephosphorylation of focal adhesion-associated substrates and thus negatively regulating integrin-promoted signaling processes. Induces apoptotic cell death by at least two distinct mechanisms: inhibition of cell survival signaling mediated by PI 3-kinase, Akt, and ILK and activation of a caspase-dependent proapoptotic pathway. Inhibits the basal activity of LCK and its activation in response to TCR stimulation and TCR-induced activation of MAP kinase and surface expression of CD69. Inhibits TCR-induced tyrosine phosphorylation of LAT and ZAP70. Inhibits both basal activity of DOK1 and its CD2-induced tyrosine phosphorylation. Induces dephosphorylation of BCAR1, focal adhesion kinase and SRC. Reduces migratory activity of Jurkat cells (By similarity). Reduces tyrosine phosphorylation of CEACAM20 and thereby contributes to suppress the intestinal immune response.
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E9Q0S6
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TENS1_MOUSE
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Tensin-1 (EC 3.1.3.-)
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MGCTVSLVCCEALEPLPSCGPQPPGTPPGPARPERCEPGGAAPDPRRRLLLQPEDLEAPKTHHFKVKAFKKVKPCGICRQAITREGCVCKVCSFSCHRKCQAKVAAPCVPPSSHELVPITTETVPKNVVDVGEGDCRVGSSPKNLEEGGSMRVSPSIQPQPQSQPTSLSRNTSVSRAMEDSCELDLVYVTERIIAVSFPSTANEENFRSNLREVAQMLKSKHGGNYLLFNLSEQRPDITKLHAKVLEFGWPDLHTPALEKICSVCKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYLHYSNISASADQALDRFAMKRFYEDKIVPIGQPSQRRYVHYFSGLLSGSIKMNNKPLFLHHVIMHGIPNFESKGGCRPFLRIYQAMQPVYTSGIYNIPGDSQASICITIEPGLLLKGDILLKCYHKKFRSPARDVIFRVQFHTCAIHDLGVVFGKEDLDEAFKDDRFPDYGKVEFVFSYGPEKIQGMEHLENGPSVSVDYNTSDPLIRWDSYDNFSGHREDGMEEVVGHTQGPLDGSLYAKVKKKDSLNGSSGPVTTARPALSATPNHVEHTLSVSSDSGNSTASTKTDKTDEPVSGATTAPAALSPQEKKELDRLLSGFGVDREKQGAMYRAQQLRSHPGGGPTVPSPGRHIVPAQVHVNGGALASERETDILDDELPIQDGQSGGSMGTLSSLDGVTNTSESGYPETLSPLTNGLDKPYSTEPVLNGGGYPYEAANRVIPVHSSHSAPIRPSYSAQEGLAGYQREGPHPAWSQQVTSAHCGCDPSGLFRSQSFPDVEPQLPQAPTRGGSSREAVQRGLNSWQQQQPHPPPRQQERSPLQSLARSKPSPQLSAETPVAALPEFPRAASQQEIEQSIETLNMLMLDLEPASAAAPLHKSQSVPGAWPGASPLSSQPLLGSSRQSHPLTQSRSGYIPSGHSLGTPELVSSGRPYSPYDYQLHPAGSNQSFHPKSPASSTFLPSPHSSAGPQEPPASLPGLIAQPQLPPKETTSDPSRTPEEEPLNLEGLVAHRVAGVQARERQPAEPPGPLRRRAASDGQYENQSPEATSPRSPGVRSPVQCVSPELALTIALNPGGRPKEPHLHSYKEAFEEMEGTSPSSPPHSVARSPPGLAKTPLSALGLKPHNPADILLHPTGVARRLIQPEEDEGEEVTKPPEEPRSYVESVARTAVAGPRAQDVEPKSFSAPAAHAYGHETPLRNGTPGGSFVSPSPLSTSSPILSADSTSVGSFPSVVSSDQGPRTPFQPMLDSSIRSGSLGQPSPAALSYQSSSPVPVGGSSYNSPDYSLQPFSSSPESQGQPQYSAASVHMVPGSPQARHRTVGTNTPPSPGFGRRAVNPTMAAPGSPSLSHRQVMGPSGPGFHGNVVSGHPASAATTPGSPSLGRHPVGSHQVPGLHSSVVTTPGSPSLGRHPGAHQGNLASSLHSNAVISPGSPSLGRHLGGSGSVVPGSPSLDRHAAYGGYSTPEDRRPTLSRQSSASGYQAPSTPSFPVSPAYYPGLSSPATSPSPDSAAFRQGSPTPALPEKRRMSVGDRAGSLPNYATINGKVSSSPVANGMASGSSTVSFSHTLPDFSKYSMPDNSPETRAKVKFVQDTSKYWYKPEISREQAIALLKDQEPGAFIIRDSHSFRGAYGLAMKVSSPPPTITQQGKKGDMTHELVRHFLIETGPRGVKLKGCPNEPNFGSLSALVYQHSVIPLALPCKLVIPSRDPTDESKDSSGPANSTTDLLKQGAACNVLFVNSVDMESLTGPQAISKATSETLAADPTPAATIVHFKVSAQGITLTDNQRKLFFRRHYPLNTVTFCDLDPQERKWMKTEGGAPAKLFGFVARKQGSTTDNACHLFAELDPNQPASAIVNFVSKVMLSAGQKR
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May act as a protein phosphatase and/or a lipid phosphatase (By similarity). Involved in fibrillar adhesion formation (By similarity). Essential for myofibroblast differentiation and myofibroblast-mediated extracellular matrix deposition (By similarity). Enhances RHOA activation in the presence of DLC1. Plays a role in cell polarization and migration (By similarity). May be involved in cartilage development and in linking signal transduction pathways to the cytoskeleton (By similarity).
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E9Q236
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MRP4_MOUSE
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ATP-binding cassette sub-family C member 4 (EC 7.6.2.-) (EC 7.6.2.2) (EC 7.6.2.3) (Multidrug resistance-associated protein 4)
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MLPVHTEVKPNPLQDANLCSRVFFWWLNPLFKTGHKRRLEEDDMFSVLPEDRSKHLGEELQRYWDKELLRAKKDSRKPSLTKAIIKCYWKSYLILGIFTLIEEGTRVVQPLFLGKIIEYFEKYDPDDSVALHTAYGYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMCHMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVLLWVEIGISCLAGLAVLVILLPLQSCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLIANLRKKEISKILGSSYLRGMNMASFFIANKVILFVTFTSYVLLGNEITASHVFVAMTLYGAVRLTVTLFFPSAIERGSEAIVSIRRIKNFLLLDELPQRKAHVPSDGKAIVHVQDFTAFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRIAYVSQQPWVFSGTVRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSGVDFGSLLKKENEEAEPSTAPGTPTLRKRTFSEASIWSQQSSRPSLKDGAPEGQDAENTQAVQPEESRSEGRIGFKAYKNYFSAGASWFFIIFLVLLNMVGQVFYVLQDWWLSHWANKQGALNNTRNANGNITETLDLSWYLGIYAGLTAVTVLFGIARSLLVFYILVNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWILIPLVPLSVVFLVLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICAIFVIVVAFGSLVLAKTLNAGQVGLALSYALTLMGMFQWSVRQSAEVENMMISVERVIEYTDLEKEAPWECKKRPPPGWPHEGVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPEGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNLDPFNEHTDEELWRALEEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKNNRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQNPESLFYKMVQQLGKGEAAALTETAKQVYFRRNYPDITFTSPAVMNTSNGQPSALTIFETAL
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ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds and xenobiotics from cells. Transports a range of endogenous molecules that have a key role in cellular communication and signaling, including cyclic nucleotides such as cyclic AMP (cAMP) and cyclic GMP (cGMP), bile acids, steroid conjugates, urate, and prostaglandins. Mediates also the ATP-dependent efflux of glutathione conjugates such as leukotriene C4 (LTC4) and leukotriene B4 (LTB4). The presence of GSH is necessary for the ATP-dependent transport of LTB4, whereas GSH is not required for the transport of LTC4. Mediates the cotransport of bile acids with reduced glutathione (GSH). Transports a wide range of drugs and their metabolites, including anticancer, antiviral and antibiotics molecules (Probable). Confers resistance to anticancer agents (Probable).
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E9Q2M9
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WDFY4_MOUSE
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WD repeat- and FYVE domain-containing protein 4
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MEAEDLSKTEDRPEDPGFQNEGQSPAVKPSFSLEGQSPGPSVLWDMLEQKFLDYQQLMPRNPEERRKNLLSLLPLFLKAWEHSVGIICFRSLQRLAEDVSDQLAQEIQQALAGKPAEQARAAAGQLLQWKSDADQDGNLLLKSVYVLTGTDSETLGRVVDSGLPALLLQCLYLFFAFPVEKDDLLESDVQGQRMFVQMLLNICSESQGLEGLLSGSELQSLLIATTCLREHSCLFWKQPTFCVLRAISKAQSPSVIQYLRTADCVRLSVQNLSKLADTLPAPEVSEAVSLILNFVRDSYPISSALLLEFENGEGYPLLLKVLLRYNGLTQGVVEPHLEELIELVMWLTTCGRSELKVFDSVTYPQLEGFKFHQEASGVTVKNLQAFQVLQNLFHRASDSVLCIQVLLAIKTMWAWNPRNFFLLEWTLQPISQFAEIIPLKPTPVQEHFFQLLETLVFKLLYVPHEVLAKVQRLIKESSELSCTLVALRSILRITASDRLFTDIFRDSGLLGLLLAQLRKQAKIMRKSGNKECSPDVQDPERELTYVMLSTVVTLLQGSVRNAVVLKDHGMVPFIKIFLDDECYRGPSLSILEQLSVINAEEYMSIIVGALCSSTQGELQLKLDLLKSLLRILETPKGHAAFRVSSGFNGLLSLLSDLEGSLQVPEVTTCGAVSPSQTLELVLHTLCVVSAALHLDPVNEHFFRSNGLFEKLAEDLCLLGCFGTPEEERTRWDSSSDMKARPFMDLLSCAFSSSCQFPPRLQSCLQILSFLESMASGTLHLRGDLMEPARAGQEPSVDAQKAEAGGRQGKFKQWPDMEDRMDEGDVMIMHPGIICIMVRLLPRLYLEDHPQLSEEIQCSVARHLLSLVKSEKNRQVMCEAGMLRTLMTFCPRTLSTGGSDLHSILIRIFEKLGSQAIEPDVLRQFLGLGIRPPRSAAVKSLHLPPGHEDNPGCSGSCAATAEKPTDSSPRPGGSQALRPSWASQYSATALQTTLSLISMTSPRNLQPQRAALTPSFVEFDMSSEGYGCLFTPTLSTVMGTSTEHSISGGTGSGAPRPFPPPGGLTFSCWFLISRQANVMEGHPLRFLTLVRHLARTEQPFVCFSISLCMDDLSLVVSTEEKEFQPLDAMEPEDEAEPSAGRQLQVRCSQLLTCGQWYHLAVVVSKEMKRNCSVTTYLDGQAIGSAKMLYIQALPGSFFSMDPSSFVDVYGYIGTPRVWKQKSSLTWRLGPAYLFEEDISADTLALIIKLGPRYCGNFQAVHLQGEDPDGEATPLIAEERVSFGLYVPSSSITSIMNIRNTYNEVDSRLIAKEMNISSRDNATPVFLLRNCAGHLSGPLRTLGAVAVGQLGVRVFHSSPAASSLDYIGGPAILLGLISLATDDHTMYAAMKVLHSVLTSNAMCDYLMQHICGYQILAFLLRKKTSFLNHRIFQLILSVAGTAELGFRPSAVTNMCIFQHVLCNFELWTNTADNLELTLFSHLLEILQSPREGPRNAEVAHQAQLLPKLLFLFNEPSLALSKVSTIIAILGCQLKGHFNIQDLLRVGLFVIYTLKPSSVNERQICLDGAQDPSRPAGSQTSGKAIWLRNQLLEMLFGVISSSQLHLTSELKEQVFLSLGPDWFLLLLQGHLHPSTTTLALKLLLYFLSSPPLRGRFRDGLSAGCWVENCMDGVDIVMDNLKSRPAVPDQSPCLLPGFRVLNDFLAYHVLIPEVYLIVSSFFLQTPLTELTNGPRENLDLMLQWLLQKHHQQEVLQAGLCIEGALLLLGMLKAIMNQPPAGSGDGAWEQTLPSSVLQFLRLVHRSYPQDSAWRTPDFLQTVAIITFPLETQKETTSESSRNTSSPGASAEASHAAEGFQASFQPHPALRQLREFMQVLLRELLLGGSNPKQWLPLEVILEASPDGATSQQKRDFQTEVLLSTMDIFQVPSGDGMPTLRGSKEPLPNAEAGAVPSLASVSYFTQKLVEKIYSGVFSADPRHILLFITEHIIAVIENPSSQKDTVMSALYSSLNKVILHCLSKPQQSLSECLGLLTILDFLQEHWDIIFATYNSNVSFLLCLMHCLLLLNARSYPEGFGLEPKPRITPYHQVFLSPNEEVKDKKEEGLPSLGDVQHSIQKSVRALWQQLVAQRRQTLEDAFKIDLSVKAGEIEVKIEEITPLWEETMLRAWQHYLASEKKSLASRSSVMHHSKVTSWSGSLSSAMRLMPGRQAKDPECRAEDFVSCIENYRRKGQELYASIYKDYVQRRKSGSIKAATAWARMREQLFGELGLWGQMTESTRCSRWELDGREGPARMRKRIRHLLAWEPLNLGYKESQEGKGDVSQTNTGNQVFMTADELTTEEAESRPDEVGVDCTQLTFFPALHESLHSEDFLELCRERQVILQELLDGEKVSQKVPMVIVQGHLVSEGILLFGQHHFYICENFTLSPTGDVYCTHHCLSNISDPFIFNMCSKDRSSDHYSCQRHAYSDLRELRQARFLLQDIALEIFFQNGYSKLLVFYNSDRSKALKSFSTFQPSLKGKGTTEDPFNLRKHPGFDRTMLQRWQKREISNFEYLMYLNTLAGRTYNDYMQYPVFPWVLADYTSEMLNLTNPKTFRDLSKPMGAQTKERKLKFTQRFKDVEKIEGDMTVQCHYYTHYSSAIIVASYLVRMPPFTQAFCSLQGGSFDVADRMFHSVKSTWESASKENMSDVRELTPEFFYLPEFLTNCNAVEFGCMQDGTTLGDVQLPPWADGDPRKFISLHRQALESDFVSSNLHHWIDLIFGYKQQGPAAVEAVNTFHPYFYGDRIDLGSITDPLIKSTILGFISNFGQVPKQIFTKPHPSRNTTGKNPGPGKDASTPVGLPGHSQSFLHSLPALRPSQVTVKDMYLFSLGSESPKGAIGHIVPTEKSILAVEKNKLLMPPLWNRTFSWGFDDFSCCLGSYGSDKILMTFENLAAWGPCLCAVCPSPTMIVTSGASAVVCIWELSLVKGRPRGLKLRQALYGHTQAVTCLTASVTFSLLVSGSQDRTCILWDLDHLSRVACLPVHREGISAIAISDVSGTIVSCAGAHLSLWNVNGQPLASITTAWGPEGTITCCCIVEGPAWDASHVIITGSKDGMVRIWKTEDVKMPVPRQAVMEEPSTEPLSPRGHKWAKNLALSRELDVSVALSGKPSKASPAVTALAITRNQSKLLVGDEKGRIFCWSADG
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Plays a critical role in the regulation of cDC1-mediated cross-presentation of viral and tumor antigens in dendritic cells. Mechanistically, acts near the plasma membrane and interacts with endosomal membranes to promote endosomal-to-cytosol antigen trafficking. Also plays a role in B-cell survival through regulation of autophagy.
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E9Q2Z1
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CECR2_MOUSE
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Chromatin remodeling regulator CECR2 (Cat eye syndrome critical region protein 2 homolog)
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MCPEEGGAAGLGELRSWWEVPAIAHFCSLFRTAFRLPDFEIEELEAALHRDDVEFISDLIACLLQGCYQRRDITPQTFHSYLEDIINYRWELEEGKPNPLREASFQDLPLRTRVEILHRLCDYRLDADDVFDLLKGLDADSLRVEPLGEDNSGALYWYFYGTRMYKEDPVQGRSNGELSLCRESERQKNVSNVPGKTGKRRGRPPKRKKLQEEIISSEKQEENSLTSDLQTRNGSRGPGQGTWWLLCQTEEEWRQVTESFRERTSLRERQLYKLLSEDFLPEICNMIAQKGKRPQRTKPELQHRFMSDHLSIKSIKLEETPMLTKIEKQKRREEEEERQLLLAVQKKEQEQMLKEERKREMEEKVKAVEDRAKRRKLREERAWLLAQGKELPPELSHLDLNSPMREGKKTKDLFELDDDFTAMYKVLDVVKAHKDSWPFLEPVDESYAPNYYQIIKIPMDISSMEKKLNGGLYCNKEEFVNDMKTMFRNCRKYNGDSSEYTKMSDNLERCFHRAMTKHFPGEDGDTDEEFWIKEDEKREKRRSRSGRSSGSHVWTRSRDTEGSSRKQPPVENGGKSLPPARRAASSGDDQSRSSIQLPPEVGTSHGQGFSRPLHCGRVPSHAPPLNQMRPAAPGTFGSLQGSDPTNLHGSSRIPEAPPGEPLQHPPFAIQAPVGISNHRGSLLSAPDLSNMGSHVPSLQLGQMNCPSQDGNMYPPAPFQAGFIPSRHGGTPARPPDFPESSEIPPGHIYHSYKYLNRAHPAVWNGNHGTTNPGRLGPDEKPHLGPGPSHHPHTLGHMMDGRVMRQPIPPNQWTKQSSFLPHGVPSSGYMQPPCKSAGHRLQPPPTPAPSPRFRGPSQALRGAQGGESMMDSPEMIAMQQLSSRVCPPGVPYHPRQPTPPQLPGPFPQVAHSASVCVSAPKPALDNPGSTQEMTETHEPEEDPAEPLPGHEEKAASICSSEGVYLKQLPHPAPPLQASCTRQSSPQERETEDSQLKSDASDSADTYKTSKNKNTWPLDNSYSSPAVQGCLRDLSIVAETGNLPENGVVGEASPCRSEGKGLDGSGSEKPLCPRGKTLQEAVPCTGPNATTPPCTDPSLMAATVNQFSPLYMPGIEYSNSATQYPMSPSLQGLASMMGGKSSGSQPQSFPPRGFQANGPHPGLFPRYRPQQGMRYSYQPPSQPSYHPYQRTPYYTCPQGFSDWQRSLPSQRSPSGPPGSHPPRSLFSEKNVLSSLQGCETLNTALTSPTQMDVVTAKVVPPDGHNSGPEEEKMDESVERPESPKEFLDLDNHNAATKRQNSLSTSDYLYGTPPPSLSSGMTFGSSAFPPHSVMLQTGSPYTPQRSASHFQPRAYPSPVPAHPPPHPVATQPNGLSPEDSLYCCQEEGLGHFQASMMEQTGTGSGLRGSFQEVHRPPGLQMHPVQSQSLFPKTPAPAASPEQLPPHKTPTLPLDQS
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Regulatory subunit of the ATP-dependent CERF-1 and CERF-5 ISWI chromatin remodeling complexes, which form ordered nucleosome arrays on chromatin and facilitate access to DNA during DNA-templated processes such as DNA replication, transcription, and repair (By similarity). The complexes do not have the ability to slide mononucleosomes to the center of a DNA template (By similarity). The CERF-1 ISWI chromatin remodeling complex has a lower ATP hydrolysis rate than the CERF-5 ISWI chromatin remodeling complex (By similarity). Plays a role in various processes during development: required during embryogenesis for neural tube closure and inner ear development. In adults, required for spermatogenesis, via the formation of ISWI-type chromatin complexes. In histone-modifying complexes, CECR2 recognizes and binds acylated histones: binds histones that are acetylated and/or butyrylated (By similarity). May also be involved through its interaction with LRPPRC in the integration of cytoskeletal network with vesicular trafficking, nucleocytosolic shuttling, transcription, chromosome remodeling and cytokinesis (By similarity).
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E9Q394
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AKP13_MOUSE
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A-kinase anchor protein 13 (AKAP-13) (AKAP-Lbc)
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MKLSPQQAPLYGDCVVTVLLAEEDKVEDDAIFYLIFSGSTLYHCTSTRKVSSDTLETIAPGHDCCETVKVLLCASREGLPVFVVAEEDFHFVQDEAYDAAQFLATSAGNQQALNFTRFLDRSGPPSRDVNSLDEKVALAFRHLKLPAEWNVLGTDHTLHDGGPRETLMHFAVRLGLLRLTWFLLQKPGGRGALSIHNKEGATPVSLALERGYHELHQLLTEENAGEPDSWSSLSYEIPYGDCSVRHHRELDIYTLTSESESHREPHGDSCTGHISKLMNIQQQLMKTNLKQMDNLMPLMVTAQDSSCVPSVPETDGLFLPCVPEPSDHQHPPFEETKSTLCCQRSPGRMAESSCDLSSMVEEENVICSHKKNKDVGRKGEEAEPASAMDSGSASHQDSCLQSVPDCGVKGREGLPSCGNRNEVTGTNYSGVATCQQPLSSRSSVLQDAMVTEPDACQHSSGRELPDSSSTDVGAPEKAGELEHSLLTPDATTQNNKPQVGEGTKERLENSDSSTTETTAVQVLSEPMEKADITNHVFATSAVGVNTPAEASPALSSEEIPTEKPGMETQERGCEGGTTSDQSSPVLPAAAIENKVLGGQEPDTSIAGFCKTASPLDLTMPGPSSDGMPEQNSESHARPAQSLSGQALLCSTAEAGTPSAEATHQPSTVTSSGRLEECGSGKASLPESTMVQPSTQELCTTLCPEDPQADTVTSDTVKNTQKSVGVCHLCVSDAKNQGNGLKQDTPLTNVLEDVPRLPSVVSQTEKELAPDQVSPPASSFSLASSPESESVTKDDALSLVPSQKEKGTATPQLHRTTACRDGPDGRDLSDTDKVGDGATDPPPSSAVELRTSMGNTSPVGIGGEQEGSSPTATLEVLSDSLLHNVDKAALVSDFTLPEEGVSVVVPESSTALGQDGKDRAMSCSSVKEDVHSSEMSREDQRTPPSGQEIPGLCEKPMSALCAEEKAQQHTPSACLKTETKDIKEVAPQVSLLTEGGAAKSLVPPRTSLSADSKQKASSTEQSGSSLLPSGLPGASEALHCNQPSALDVVVENTQFQGETNACEVSRSAMEDVTVADASPATAEPRKKDASHCIKDIPISELLNQEKQMTPSLPEAFLDKGVTDLQEVITPEIEPLDCKRETLEGTDLNCATSNSKETPIEKPMQPLARDLPTETGLSVINNNVPQADMKQVAQASIPAEESNATTVSTQAADVPTRADSIEETATRIVEAVIRQVRASNALMAKVETQNPSLSSPETKQLENAYTESACAFLPGETPQIEKTHEDTTGQCGAETEEPEKIILPESAPGKQGKMPDTRTGDEVDLLSRISAASEEEAVGNGAATPKMKQGPGTQAINRESWCAIEPCPEAASLLASKQSSECRSFIDVGLGTECASKEGMLQRVSGSESDLFHSPSDEMDSIIFPKPEEEQLLCDTTGSSSSTDDTASLDRHSSHGSDVSLPQTSKLNRSRNHQSANGFFSPGVEAPESRESESEPAGSGEMEEEEMDSITEVPANCSFLRSSMRSLSPFRRHSWGPGKNAASDAEMNQRSSMRALGHVVRRPPIHRRSFSLEGLTGGGVGNKPSSSLEMSSANSSELRNPFGGEEQRNSLMSLSEEHLEPDQRQHHRMFDQQTCYRSKQQGFNYCTSAISSPLTKSISLMTISHPGLDSSRPFHSTSANLTESITEENCNFLPPSPSKKNFEEKSGTKVSRTFSYIRNKMSSSKKSKEKEKEKDKIKEKEKDSKEKEKDKKTLNGHTFSPIPIVGPISCSQCMKPFTNKDAYTCAGCGAFVHKGCRENLASCAKVKMKQPKGSLQAHDTSSLPTVIMRNKSSQPKERPRSAVLLADEATAAPMFTNRRSQQSVSLSKSVSIQNITGVGNDENMSNTWKFLSHSTDSLNKICKVNESTESLTDEGVGTDMNEGQLMGDFESDSKQLEAESWSRTVDSKFLKQQKKDVVKRQEVIYELMQTELHHIRTLKIMSDVYSRGMMTDLLFEQQMVEKLFPCLDELISIHSQFFQRILERKKESLVDKSEKNFLIKRIGDVLVSQFSGESAERLKKTYGKFCGQHNQSVNYFKDLYTKDKRFQAFVKKKMSSSVVRRLGIPECILLVTQRITKYPVLFQRILQCTKDNEVEQEDLTQSLSLVKDVIGAVDSKVASYEKKVRLGEIYTKTDSKSIMRMKSGQMFAKEDLRRKKLVRDGSVFLKSTTGRLKEVQAVLLTDILVFLQEKDQKYVFASLDHKSTVISLKKLIVREVAHEEKGLFLISMGVKDPEMVEVHASSREERNSWIQIIQDTINSLNRDEDEGIPSENEEEKKLLDTKARELKEQLQQKDQQILLLLEEKEMIFRDMTECSTPLPEDCSPTHSPRVLFRSNTEEALKGGPLMKSAINEVEILQSLVSGSLGGTLGQSISSPVEQEVMAAPISLPRRAETFGGFDCHQMNASKGGEKEEGDDGQDLRRTESDSGLKKGGNGNLVFMLKRNSEQVVQSIVHLHELLSMLQGVVLQQDSYIEDQKLVLTEKVLTRSASRPSSLIEQEKQRSLEKQRQDLANLQKQQAQHLEEKRRREREWEAREQELRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCDLERLRAAQKQLEREQEQLRRDTERLSQRQMDQNLCQVSNKHGRLMRIPSFLPNSDEFSSPSAPSVTKSGSLDSELSVSPKRNSISRTQKDKGPFHILGSASQTKVPEGQSQAPSSTSTSTRLFGLSKPKEKKEKKKKSKGSRTQPGDGPASEVPAEGEEIFC
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Scaffold protein that plays an important role in assembling signaling complexes downstream of several types of G protein-coupled receptors. Activates RHOA in response to signaling via G protein-coupled receptors via its function as Rho guanine nucleotide exchange factor. May also activate other Rho family members. Part of a kinase signaling complex that links ADRA1A and ADRA1B adrenergic receptor signaling to the activation of downstream p38 MAP kinases, such as MAPK11 and MAPK14. Part of a signaling complex that links ADRA1B signaling to the activation of RHOA and IKBKB/IKKB, leading to increased NF-kappa-B transcriptional activity. Part of a RHOA-dependent signaling cascade that mediates responses to lysophosphatidic acid (LPA), a signaling molecule that activates G-protein coupled receptors and potentiates transcriptional activation of the glucocorticoid receptor NR3C1 (By similarity). Part of a signaling cascade that stimulates MEF2C-dependent gene expression in response to lysophosphatidic acid (LPA) (By similarity). Part of a signaling pathway that activates MAPK11 and/or MAPK14 and leads to increased transcription activation of the estrogen receptors ESR1 and ESR2. Part of a signaling cascade that links cAMP and EGFR signaling to BRAF signaling and to PKA-mediated phosphorylation of KSR1, leading to the activation of downstream MAP kinases, such as MAPK1 or MAPK3 (By similarity). Functions as scaffold protein that anchors cAMP-dependent protein kinase (PKA) and PRKD1. This promotes activation of PRKD1, leading to increased phosphorylation of HDAC5 and ultimately cardiomyocyte hypertrophy. Has no guanine nucleotide exchange activity on CDC42, Ras or Rac (By similarity). Required for normal embryonic heart development, and in particular for normal sarcomere formation in the developing cardiomyocytes. Plays a role in cardiomyocyte growth and cardiac hypertrophy in response to activation of the beta-adrenergic receptor by phenylephrine or isoproterenol. Required for normal adaptive cardiac hypertrophy in response to pressure overload. Plays a role in osteogenesis.
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E9Q3E1
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AL3B2_MOUSE
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Aldehyde dehydrogenase family 3 member B2 (EC 1.2.1.3) (Aldehyde dehydrogenase 8)
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MSAAETGSEPSQGAGPSEATLHSLREAFNAGRTRPTEFRTAQLRSLGRFLQENKELLQDALAKDVGKSGFESDMSEIILCENEVDLALKNLQTWMKDEPVSTNLLTKLSSAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQYLDQSCFAVMLGGPEETRQLLEHKFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCSQEMQERLVPALQNSITRFYGDNPQTSPNLGRIINQKHFKRLQGLLGCGRVAIGGQSDEGERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFINRREKPLALYAFSNNNQVVNQMLERTSSGGFGGNDGFLYLTLPALPLGGVGNSGMGRYHGKFSFDTFSHHRACLLRSPGMEKLNDLRYPPYGPWNQQLISWAIGSRSCTLL
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Oxidizes medium and long chain aldehydes into non-toxic fatty acids.
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E9Q3L2
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PI4KA_MOUSE
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Phosphatidylinositol 4-kinase alpha (PI4-kinase alpha) (PI4K-alpha) (PtdIns-4-kinase alpha) (EC 2.7.1.67)
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MAAAGARGGGGGGGGGGGGGSGSSSGSSTSRGFYFNTVLSLARSLAVQRPASLEKVQKLLCMCPVDFHGIFQLDERRRDAVIALGIFLIESDLQHKDCVVPYLLRLLRGLPKVYWVEESTARKGRGNLPVAESFSFCLVTLLSDVACRDPSLRDEILEAILQVLHVLLGMCQALEIQEKEYLCKYAIPCLIGISRSFGRYSNSEESLLSKLFPKVSPHSLRIPEELEGVRRRSFNDFRSILPSNLLTVCQEGTLKRKTSSVSSISQVSPERGIPPPSSPGGSAFHYFEASCLPDGTALEPEYYFSTISSSFSISPLFNGITYKEFCIPLEMLRELLNLVKKIVEEPVLKSLDAIVAGVMEANPSADLYYTTFSDPLYLTMFKMLRDTLYYMKDLPTSFVKEIHDFVLEQFNMSQGELQKILHDADRIHSEMSPLKLRCQANAACVDLMVWAVKDEQGAENLCIKLSEKLQSKTSSKVIIAHLPLLICCLQGLGRLCERFPVVVHSVTPSLRDFLVIPSPVLVKLYKYHSQYHTVAGSDIKISVTNEHSESTLNVLPGKKNQPSMYEQLRDIAIDNICRCLKAGLTVDPVIVEAFLASLSNRLYISQESDKDAHLIPDHTIRALGHIAVALRDTPKVMEPILQILQQKFCQPPSPLDVLIIDQLGCLVITGNQYIYQEVWNLFQQISVKASSVVYSATKDYKDHGYRHCSLAVINALANIAANIQEEHLVDELLMNLLELFVQLGLEGKRASERASEKGPALKASSSAGNLGVLIPVIAVLTRRLPPIKEAKPRLQKLFRDFWLYSVLMGFAVEGSGLWPEEWYEGVCEIATKSPLLTFPSKEPLRSVLQYNSAMKNDTVTPAELSELRSTIINLLDPPPEVSALINKLDFAMSTYLLSVYRLEYMRVLRSTDPDRFQVMFCYFEDKAIQKDKSGMMQCVIAVADKVFDAFLNMMAEKAKTKENEEELERHAQFLLVNFNHIHKRIRRVADKYLSGLVDKFPHLLWSGTVLKTMLDILQTLSLSLSADIHKDQPYYDIPDAPYRITVPDTYEARESIVKDFAARCGMILQEAMKWAPTVTKSHLQEYLNKHQNWVSGLSQHTGLAMATESILHFAGYNKQNTTLGATQLTERPACVKKDYSNFMASLNLRNRYAGEVHGMIRFSGATGQMSDLNKMMVQDLITALDHSHPQHYTQAMFKLTAMLISSKDCDPQLLHHLCWGPLRMFNEHGMETALACWEWLLAGKNGVEVPFMREMAGAWHMTVEQKFGLFSVETKEADPLAASEASQPRPCPPEVTPHYIWIDFLVQRFEIAKYCSSDQVEIFSSLLQRSMSLNIGGARGSMNRHVAAIGPRFKLLTLGLSLLHADVVPNATIRNVLREKIYSTAFDYFSCPPKFPTQGEKRLREDISIMIKFWTAMFSDKKYLTASQLVPPDNQDTRSNLDITVGSRQQATQGWINTYPLSSGMSTISKKSGMSKKTNRGSQLHKYYMKRRTLLLSLLATEIERLITWYNPLSAPELELDQAGENSVANWRSKYISLSEKQWKDNVNLAWSISPYLAVQLPARFKNTEAIGNEVTRLVRLDPGAVSDVPEAIKFLVTWHTIDADAPELSHVLCWAPTDPPTGLSYFSSMYPPHPLTAQYGVKVLRSFPPDAILFYIPQIVQALRYDKMGYVREYILWAAAKSQLLAHQFIWNMKTNIYLDEEGHQKDPDIGDLLEQLVEEITGSLSGPAKDFYQREFDFFNKITNVSAIIKPYPKGDERKKACLSALSEVKVQPGCYLPSNPEAIVLDIDYKSGTPMQSAAKAPYLAKFKVKRCGVSELEKEGLQCRSDAEDECFSQEADGKKICWQAAIFKVGDDCRQDMLALQIIDLFKNIFQLVGLDLFVFPYRVVATAPGCGVIECIPDCTSRDQLGRQTDFGMYDYFTRQYGDESTLAFQQARYNFIRSMAAYSLLLFLLQIKDRHNGNIMLDKKGHIIHIDFGFMFESSPGGNLGWEPDIKLTDEMVMIMGGKMEATPFKWFMEMCVRGYLAVRPYMDAVVSLVTLMLDTGLPCFRGQTIKLLKHRFSPNMTEREAANFIMKVIQNCFLSNRSRTYDMIQYYQNDIPY
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Acts on phosphatidylinositol (PtdIns) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate.
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E9Q3M5
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S4A5_MOUSE
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Electrogenic sodium bicarbonate cotransporter 4 (Anion exchange protein) (Solute carrier family 4 member 5)
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MKVDEEKAGVKKLDPTSYKRRQPEQDFPSIHIGFPVPSYSQRKSDSKGHLSGLQKVQWSLKPGKPQQELAGPGIRASSQGGAVDFTKRTRSPAAEQLQDILGEEDEAPNPTLFTEMDTLQHDGDQMEWKESARWIKFEEKVEEGGERWSKPHVSTLSLHSLFELRTCLQTGTVLLDLDSCSLPQIIDDVIEKQIEDGLLRPELRERVSYVLLRKHRHQTKKPIHRSLADIGKSVSTTNRSSARSSSAGPTLHRSTEDLRIRQSTSYGHLCHAQSRSMNDISHTPNTDQRKNKFMKKIPKDSEASNVLVGEVDFLDQPFIAFVRLVQSAMLGGVTEVPVPTRFLFILLGPSGRAKSYNEIGRAIATLMVDDLFSDVAYKARNREDLIAGIDEFLDEVIVLPPGEWDPNIRIEPPKKVPSADKRKSVFSLAEPGQMNGSVGGGGASAGGGGSGGGAGGSGAGGVGSGDEAEMPAMHEIGEELIWTGRFFGGLCLDVKRKLPWFPSDFYDGFHLQSISAVLFIYLGCITNAITFGGLLGDATDNYQGVMESFLGTAMAGSLFCLFSGQPLIILSSTGPILIFEKLLFDFSKANGLDYMEFRLWIGLHSAIQCLILVATDASFIIKYITRFTEEGFSTLISFIFIYDAIKKMIGAFKYYPINTDFKPDFITTYKCECVAPDTVNTTTVNASAPLAPNTNTSLYTPLNLTALDWSLLSKKECLSYGGRLLGSSCQFVPDLALMSFILFFGTYSMTLTLKKFKFSRYFPTKVRTLVADFSIVFSILLFCGIDACFGLQTPKLHVPSVIKPTRPDRGWFVAPFGKNPWWVYPASILPALLVTILIFMDQQITAVIVNRKENKLRKAAGYHLDLFWVGILMALCSFTGLPWYVAATVISIAHIDSLKMETETSAPGEQPQFLGVREQRVTGVMVFILTGISVFLAPILKYIPMPVLYGVFLYMGVASLNGIQFWERCKLFLMPAKHQPDHAFLRHVPLRRIHLFTLVQILCLALLWILKSTMAAIIFPVMILGLIIVRRLLDLIFSQHDLAWIDNILPEKDKKETDKKKKRRKEVHETAEKEVAMPQFLPPSVVKIPMEGIPSDPQNGIHCVARKRSSSWSYSL
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Mediates sodium- and bicarbonate-dependent electrogenic sodium bicarbonate cotransport, with a Na(+):HCO3(-) stoichiometry varying from 1:2 to 1:3.
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E9Q3T6
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PRD14_MOUSE
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PR domain zinc finger protein 14 (EC 2.1.1.-) (PR domain-containing protein 14)
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MALPPSGETQSQDKANYLPQSNPHHLTTYYAHAPGYSHFRNLATTEEEFQPWKLAAAVLESQAMAPLDAFRMTAPLLNPGLAVQSEPLYNLPWYKLSPWNRIPQFTPEVPRFLDSTEHRSSGSSNQNLVLGGGGGQISGQRWEAENLLLPSPVIASLLPDGIKSSQSISVPQTLNQEGKLPFCGFNFTEEELSFVLYGAIASPEHPTDLQHAISGILVPTESSGSNHLHKTLDKDSLQLPEGLCLMQTSFGDVPHFGVFCSDFIAKGVRFGPFRGRVVNASEVKAHRDNSRMWEIFEDGHLSHFIDGKGSGNWMSYVNCARFPKEQNLLAVQHQGQIFYESCRDIQRNQELLVWYGNGYEKFLGVPMNLRVTEQGGQQLSESSEESAEGYRCERCGKVFTYKYYRDKHLKYTPCVDKGDRKFPCSLCQRSFEKRDRLRIHILHVHERHRPYLCSTCGKSFSQSSSLNKHMRVHSGDRPYQCVYCTKKFTASSILRTHIRQHSGEKPFKCKHCGKAFASHAAHDSHVRRSHKDNGRSSCDICGKGFLDQEAFYAHMRLHKTC
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Transcription factor that has both positive and negative roles on transcription (By similarity). Plays a role in cellular pluripotency. Essential for germ cell development at 2 levels: the reacquisition of potential pluripotency, including SOX2 up-regulation, and successful epigenetic reprogramming, characterized by EHMT1 repression. Its association with CBFA2T2 is required for the functions in pluripotency and germ cell formation. {ECO:0000250, ECO:0000269|PubMed:18622394, ECO:0000269|PubMed:26523391}.
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E9Q401
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RYR2_MOUSE
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Ryanodine receptor 2 (RYR-2) (RyR2) (Cardiac muscle ryanodine receptor) (Cardiac muscle ryanodine receptor-calcium release channel) (Type 2 ryanodine receptor)
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MADAGEGEDEIQFLRTDDEVVLQCTATIHKEQQKLCLAAEGFGNRLCFLESTSNSKNVPPDLSICTFVLEQSLSVRALQEMLANTVEKSEGQVDVEKWKFMMKTAQGGGHRTLLYGHAILLRHSYSGMYLCCLSTSRSSTDKLAFDVGLQEDTTGEACWWTIHPASKQRSEGEKVRVGDDLILVSVSSERYLHLSYGNSSWHVDAAFQQTLWSVAPISSGSEAAQGYLIGGDVLRLLHGHMDECLTVPSGEHGEEQRRTVHYEGGAVSVHARSLWRLETLRVAWSGSHIRWGQPFRLRHVTTGKYLSLMEDKNLLLMDKEKADVKSTAFAFRSSKEKLDVGVRKEVDGMGTSEIKYGDSICYIQHVDTGLWLTYQAVDVKSARMGSIQRKAIMHHEGHMDDGLNLSRSQHEESRTARVIRSTVFLFNRFIRGLDALSKKVKLPTIDLPIESVSLSLQDLIGYFHPPDEHLEHEDKQNRLRALKNRQNLFQEEGMINLVLECIDRLHVYSSAAHFADVAGREAGESWKSILNSLYELLAALIRGNRKNCAQFSGSLDWLISRLERLEASSGILEVLHCVLVESPEALNIIKEGHIKSIISLLDKHGRNHKVLDVLCSLCVCHGVAVRSNQHLICDNLLPGRDLLLQTRLVNHVSSMRPNIFLGVSEGSAQYKKWYYELMVDHTEPFVTAEATHLRVGWASTEGYSPYPGGGEEWGGNGVGDDLFSYGFDGLHLWSGCIARTVSSPNQHLLRTDDVISCCLDLSAPSISFRINGQPVQGMFENFNIDGLFFPVVSFSAGIKVRFLLGGRHGEFKFLPPPGYAACYEAVLPKEKLKVEHSREYKQERTYTRDLLGPTVSLTQAAFTPVPVDTSQIVLPPHLERIRERLAENIHELWVMNKIELGWQYGPVRDDNKRQHPCLVEFCKLPEQERNYNLQMSLETLKTLLALGCHVGIADEHAEEKVKKMKLPKNYQLTSGYKPAPMDLSFIKLTPSQEAMVDKLAENAHNVWARDRIRQGWTYGIQQDVKNRRNPRLVPYTLLDDRTKKSNKDSLREAVRTLLGYGYHLEAPDQDHASRAEVCSGTGERFRIFRAEKTYAVKAGRWYFEFEAVTAGDMRVGWSRPGCQPDLELGSDDRAFAFDGFKAQRWHQGNEHYGRSWQAGDVVGCMVDMNEHTMMFTLNGEILLDDSGSELAFKDFDVGDGFIPVCSLGVAQVGRMNFGKDVSTLKYFTICGLQEGYEPFAVNTNRDITMWLSKRLPQFLQVPSNHEHIEVTRIDGTIDSSPCLKVTQKSFGSQNNNTDIMFYRLSMPIECAEVFSKSVAGGLPGAGFYGPKNDLEDFDVDSDFEVLMKTAHGHLVPDRIDKDKETPKPEFNNHKDYAQEKPSRLKQRFLLRRTKPDYSTGHSARLTEDVLADDRDDYEYLMQTSTYYYSVRIFPGQEPANVWVGWITSDFHQYDTGFDLDRVRTVTVTLGDEKGKVHESIKRSNCYMVCAGESMSPGQGRNNSNGLEIGCVVDAASGLLTFIANGKELSTYYQVEPSTKLFPAVFAQATSPNVFQFELGRIKNVMPLSAGLFKSEHKNPVPQCPPRLHVQFLSHVLWSRMPNQFLKVDVSRISERQGWLVQCLDPLQFMSLHIPEENRSVDILELTEQEELLQFHYHTLRLYSAVCALGNHRVAHALCSHVDEPQLLYAIENKYMPGLLRAGYYDLLIDIHLSSYATARLMMNNEFIVPMTEETKSITLFPDENKKHGLPGIGLSTSLRPRMRFSSPSFVSISNDCYQYSPEFPLDILKAKTIQMLTEAVKEGSLHARDPVGGTTEFLFVPLIKLFYTLLIMGIFHNEDLKHILQLIEPSVFKEAAVPEEEGGTPEKEISIEDAKLEGEEEAKGGKRPKEGLLQMKLPEPVKLQMCLLLQYLCDCQVRHRIEAIVAFSDDFVAKLQDNQRFRYNEVMQALNMSAALTARKTREFRSPPQEQINMLLNFKDDKSECPCPEEIRDQLLDFHEDLMTHCGIELDEDGSLDGSNDLTIRGRLLSLVEKVTYLKKKQAEKPVASDSRKCSSLQQLISETMVRWAQESVIEDPELVRAMFVLLHRQYDGIGGLVRALPKTYTINGVSVEDTINLLASLGQIRSLLSVRMGKEEEKLMIRGLGDIMNNKVFYQHPNLMRALGMHETVMEVMVNVLGGGESKEITFPKMVANCCRFLCYFCRISRQNQKAMFDHLSYLLENSSVGLASPAMRGSTPLDVAAASVMDNNELALALREPDLEKVVRYLAGCGLQSCQMLVSKGYPDIGWNPVEGERYLDFLRFAVFCNGESVEENANVVVRLLIRRPECFGPALRGEGGNGLLAAMEEAIKIAEDPSRDGPSPTSGSSKTLDIEEEEDDTIHMGNAIMTFYAALIDLLGRCAPEMHLIHAGKGEAIRIRSILRSLIPLGDLVGVISIAFQMPTIAKDGKVVEPDMSAGFCPDHKAAMVLFLDRVYGIEVQDFLLHLLEVGFLPDLRAAASLDTAALSATDMALALNRYLCTAVLPLLTRCAPLFAGTEHHASLIDSLLHTVYRLSKGCSLTKAQRDSIEVCLLSICGQLRPSMMQHLLRRLVFDVPLLNEHAKMPLKLLTNHYERCWKYYCLPGGWGNFGAASEEELHLSRKLFWGIFDALSQKKYEQELFKLALPCLSAVAGALPPDYMESNYVSMMEKQSSMDSEGNFNPQPVDTSNITIPEKLEYFINKYAEHSHDKWSMDKLANGWIYGEIYSDSSKIQPLMKPYKLLSEKEKEIYRWPIKESLKTMLAWGWRIERTREGDSMALYNRTRRISQTSQVSIDAAHGYSPRAIDMSNVTLSRDLHAMAEMMAENYHNIWAKKKKLELESKGGGNHPLLVPYDTLTAKEKAKDREKAQDIFKFLQISGYVVSRGFKDLDLDTPSIEKRFAYSFLQQLIRYVDEAHQYILEFDGGSRSKGEHFPYEQEIKFFAKVVLPLIDQYFKNHRLYFLSAASRPLCTGGHASNKEKEMVTSLFCKLGVLVRHRISLFGNDATSIVNCLHILGQTLDARTVMKTGLDSVKSALRAFLDNAAEDLEKTMENLKQGQFTHTRSQPKGVTQIINYTTVALLPMLSSLFEHIGQHQFGEDLILEDVQVSCYRILTSLYALGTSKSIYVERQRSALGECLAAFAGAFPIAFLETHLDKHNVYSIYNTRSSRERAALSLPANVEDVCPNIPSLEKLMTEIIELAESGIRYTQMPYMMEVVLPMLCSYMSRWWEHGPENHPERAEMCCTALNSEHMNTLLGNILKIIYNNLGIDEGAWMKRLAVFSQPIINKVKPQLLKTHFLPLMEKLKKKAAMVVSEEDHLKAEARGDMSEAELLILDEFTTLARDLYAFYPLLIRFVDYNRAKWLKEPNPEAEELFRMVAEVFIYWSKSHNFKREEQNFVVQNEINNMSFLITDTKSKMSKAAISDQERKKMKRKGDRYSMQTSLIVAALKRLLPIGLNICAPGDQELIALAKNRFSLKDTEEEVRDIIRSNIHLQGKLEDPAIRWQMALYKDLPNRTEDPSDPERTVERVLGIANVLFHLEQKSKYTGRGYFSLVEHPQRSKKAVWHKLLSKQRKRAVVACFRMAPLYNLPRHRAVNLFLQGYEKSWIETEEHYFEDKLIEDLAKPGAELPEEDEAMKRVDPLHQLILLFSRTALTEKCKLEEDFLYMAYADIMAKSCHDEEDDDGEEEVKSFEEKEMEKQKLLYQQARLHDRGAAEMVLQTISASKGETGPMVAATLKLGIAILNGGNSTVQQKMLDYLKEKKDVGFFQSLAGLMQSCSVLDLNAFERQNKAEGLGMVTEEGSGEKVLQDDEFTCDLFRFLQLLCEGHNSDFQNYLRTQTGNNTTVNIIISTVDYLLRVQESISDFYWYYSGKDIIDEQGQRNFSKAIQVAKQVFNTLTEYIQGPCTGNQQSLAHSRLWDAVVGFLHVFAHMQMKLSQDSSQIELLKELMDLQKDMVVMLLSMLEGNVVNGTIGKQMVDMLVESSNNVEMILKFFDMFLKLKDLTSSDTFKEYDPDGKGVISKRDFHKAMESHKHYTQSETEFLLSCAETDENETLDYEEFVKRFHEPAKDIGFNVAVLLTNLSEHMPNDTRLQTFLELAESVLNYFQPFLGRIEIMGSAKRIERVYFEISESSRTQWEKPQVKESKRQFIFDVVNEGGEKEKMELFVNFCEDTIFEMQLAAQISESDLNERLANKEESEKERPEEQAPRMGFFSLLTIQSALFALRYNVLTLVRMLSLKSLKKQMKRMKKMTVKDMVLAFFSSYWSVFVTLLHFVASVCRGFFRIVSSLLLGGSLVEGAKKIKVAELLANMPDPTQDEVRGDEEEGERKPLESALPSEDLTDLKELTEESDLLSDIFGLDLKREGGQYKLIPHNPNAGLSDLMTNPVPVPEVQEKFQEQKAKEEKEEKEETKSEPEKAEGEDGEKEEKAKDEKSKQKLRQLHTHRYGEPEVPESAFWKKIIAYQQKLLNYFARNFYNMRMLALFVAFAINFILLFYKVSTSSVVEGKELPTRTSSDTAKVTNSLDSSPHRIIAVHYVLEESSGYMEPTLRILAILHTIISFFCIIGYYCLKVPLVIFKREKEVARKLEFDGLYITEQPSEDDIKGQWDRLVINTQSFPNNYWDKFVKRKVMDKYGEFYGRDRISELLGMDKAALDFSDAREKKKPKKDSSLSAVLNSIDVKYQMWKLGVVFTDNSFLYLAWYMTMSVLGHYNNFFFAAHLLDIAMGFKTLRTILSSVTHNGKQLVLTVGLLAVVVYLYTVVAFNFFRKFYNKSEDGDTPDMKCDDMLTCYMFHMYVGVRAGGGIGDEIEDPAGDEYEIYRIIFDITFFFFVIVILLAIIQGLIIDAFGELRDQQEQVKEDMETKCFICGIGNDYFDTVPHGFETHTLQEHNLANYLFFLMYLINKDETEHTGQESYVWKMYQERCWEFFPAGDCFRKQYEDQLN
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Calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering cardiac muscle contraction. Aberrant channel activation can lead to cardiac arrhythmia. In cardiac myocytes, calcium release is triggered by increased Ca(2+) levels due to activation of the L-type calcium channel CACNA1C. The calcium channel activity is modulated by formation of heterotetramers with RYR3. Required for cellular calcium ion homeostasis. Required for embryonic heart development.
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E9Q414
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APOB_MOUSE
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Apolipoprotein B-100 (Apo B-100) [Cleaved into: Apolipoprotein B-48 (Apo B-48)]
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MGPRKPALRTPLLLLFLLLFLDTSVWAQDEVLENLSFSCPKDATRFKHLRKYVYNYEAESSSGVQGTADSRSATKINCKVELEVPQICGFIMRTNQCTLKEVYGFNPEGKALMKKTKNSEEFAAAMSRYELKLAIPEGKQIVLYPDKDEPKYILNIKRGIISALLVPPETEEDQQELFLDTVYGNCSTQVTVNSRKGTVPTEMSTERNLQQCDGFQPISTSVSPLALIKGLVHPLSTLISSSQTCQYTLDPKRKHVSEAVCDEQHLFLPFSYKNKYGIMTRVTQKLSLEDTPKINSRFFSEGTNRMGLAFESTKSTSSPKQADAVLKTLQELKKLSISEQNAQRANLFNKLVTELRGLTGEAITSLLPQLIEVSSPITLQALVQCGQPQCYTHILQWLKTEKAHPLLVDIVTYLMALIPNPSTQRLQEIFNTAKEQQSRATLYALSHAVNSYFDVDHSRSPVLQDIAGYLLKQIDNECTGNEDHTFLILRVIGNMGRTMEQVMPALKSSVLSCVRSTKPSLLIQKAALQALRKMELEDEVRTILFDTFVNGVAPVEKRLAAYLLLMKNPSSSDINKIAQLLQWEQSEQVKNFVASHIANILNSEELYVQDLKVLIKNALENSQFPTIMDFRKFSRNYQISKSASLPMFDPVSVKIEGNLIFDPSSYLPRESLLKTTLTVFGLASLDLFEIGLEGKGFEPTLEALFGKQGFFPDSVNKALYWVNGRVPDGVSKVLVDHFGYTTDGKHEQDMVNGIMPIVDKLIKDLKSKEIPEARAYLRILGKELSFVRLQDLQVLGKLLLSGAQTLQGIPQMVVQAIREGSKNDLFLHYIFMDNAFELPTGAGLQLQVSSSGVFTPGIKAGVRLELANIQAELVAKPSVSLEFVTNMGIIIPDFAKSSVQMNTNFFHESGLEARVALKAGQLKVIIPSPKRPVKLFSGSNTLHLVSTTKTEVIPPLVENRQSWSTCKPLFTGMNYCTTGAYSNASSTESASYYPLTGDTRYELELRPTGEVEQYSATATYELLKEDKSLVDTLKFLVQAEGVQQSEATVLFKYNRRSRTLSSEVLIPGFDVNFGTILRVNDESAKDKNTYKLILDIQNKKITEVSLVGHLSYDKKGDGKIKGVVSIPRLQAEARSEVHTHWSSTKLLFQMDSSATAYGSTISKRVTWRYDNEIIEFDWNTGTNVDTKKVASNFPVDLSHYPRMLHEYANGLLDHRVPQTDVTFRDMGSKLIVATNTWLQMATRGLPYPQTLQDHLNSLSELNLLKMGLSDFHIPDNLFLKTDGRVKYTMNRNKINIDIPLPLGGKSSKDLKMPESVRTPALNFKSVGFHLPSREVQVPTFTIPKTHQLQVPLLGVLDLSTNVYSNLYNWSASYTGGNTSRDHFSLQAQYRMKTDSVVDLFSYSVQGSGETTYDSKNTFTLSCDGSLHHKFLDSKFKVSHVEKFGNSPVSKGLLTFETSSALGPQMSATVHLDSKKKQHLYVKDIKVDGQFRASSFYAQGKYGLSCERDVTTGQLSGESNMRFNSTYFQGTNQIVGMYQDGALSITSTSDLQDGIFKNTASLKYENYELTLKSDSSGQYENFAASNKLDVTFSTQSALLRSEHQANYKSLRLVTLLSGSLTSQGVELNADILGTDKINTGAHKATLKIARDGLSTSATTNLKYSPLLLENELNAELGLSGASMKLSTNGRFKEHHAKFSLDGRAALTEVSLGSIYQAMILGADSKNIFNFKLSREGLRLSNDLMGSYAEMKLDHTHSLNIAGLSLDFFSKMDNIYSGDKFYKQNFNLQLQPYSFITTLSNDLRYGALDLTNNGRFRLEPLKLNVGGNFKGTYQNNELKHIYTISYTDLVVASYRADTVAKVQGVEFSHRLNADIEGLTSSVDVTTSYNSDPLHFNNVFHFSLAPFTLGIDTHTSGDGKLSFWGEHTGQLYSKFLLKAEPLALIVSHDYKGSTSHSLPYESSISTALEHTVSALLTPAEQTSTWKFKTKLNDKVYSQDFEAYNTKDKIGVELSGRADLSGLYSPIKLPFFYSEPVNVLNGLEVNDAVDKPQEFTIIAVVKYDKNQDVHTINLPFFKSLPDYLERNRRGMISLLEAMRGELQRLSVDQFVRKYRAALSRLPQQIHHYLNASDWERQVAGAKEKITSFMENYRITDNDVLIAIDSAKINFNEKLSQLETYAIQFDQYIKDNYDPHDLKRTIAEIIDRIIEKLKILDEQYHIRVNLAKSIHNLYLFVENVDLNQVSSSNTSWIQNVDSNYQVRIQIQEKLQQLRTQIQNIDIQQLAAEVKRQMDAIDVTMHLDQLRTAILFQRISDIIDRVKYFVMNLIEDFKVTEKINTFRVIVRELIEKYEVDQHIQVLMDKSVELAHRYSLSEPLQKLSNVLQRIEIKDYYEKLVGFIDDTVEWLKALSFKNTIEELNRLTDMLVKKLKAFDYHQFVDKTNSKIREMTQRINAEIQALKLPQKMEALKLLVEDFKTTVSNSLERLKDTKVTVVIDWLQDILTQMKDHFQDTLEDVRDRIYQMDIQRELEHFLSLVNQVYSTLVTYMSDWWTLTAKNITDFAEQYSIQNWAESIKVLVEQGFIVPEMQTFLWTMPAFEVSLRALQEGNFQTPVFIVPLTDLRIPSIRINFKMLKNIKIPLRFSTPEFTLLNTFHVHSFTIDLLEIKAKIIRTIDQILSSELQWPLPEMYLRDLDVVNIPLARLTLPDFHVPEITIPEFTIPNVNLKDLHVPDLHIPEFQLPHLSHTIEIPAFGKLHSILKIQSPLFILDANANIQNVTTSGNKAEIVASVTAKGESQFEALNFDFQAQAQFLELNPHPPVLKESMNFSSKHVRMEHEGEIVFDGKAIEGKSDTVASLHTEKNEVEFNNGMTVKVNNQLTLDSHTKYFHKLSVPRLDFSSKASLNNEIKTLLEAGHVALTSSGTGSWNWACPNFSDEGIHSSQISFTVDGPIAFVGLSNNINGKHLRVIQKLTYESGFLNYSKFEVESKVESQHVGSSILTANGRALLKDAKAEMTGEHNANLNGKVIGTLKNSLFFSAQPFEITASTNNEGNLKVGFPLKLTGKIDFLNNYALFLSPRAQQASWQASTRFNQYKYNQNFSAINNEHNIEASIGMNGDANLDFLNIPLTIPEINLPYTEFKTPLLKDFSIWEETGLKEFLKTTKQSFDLSVKAQYKKNSDKHSIVVPLGMFYEFILNNVNSWDRKFEKVRNNALHFLTTSYNEAKIKVDKYKTENSLNQPSGTFQNHGYTIPVVNIEVSPFAVETLASSHVIPTAISTPSVTIPGPNIMVPSYKLVLPPLELPVFHGPGNLFKFFLPDFKGFNTIDNIYIPAMGNFTYDFSFKSSVITLNTNAGLYNQSDIVAHFLSSSSFVTDALQYKLEGTSRLMRKRGLKLATAVSLTNKFVKGSHDSTISLTKKNMEASVRTTANLHAPIFSMNFKQELNGNTKSKPTVSSSIELNYDFNSSKLHSTATGGIDHKFSLESLTSYFSIESFTKGNIKSSFLSQEYSGSVANEANVYLNSKGTRSSVRLQGASKVDGIWNVEVGENFAGEATLQRIYTTWEHNMKNHLQVYSYFFTKGKQTCRATLELSPWTMSTLLQVHVSQLSSLLDLHHFDQEVILKANTKNQKISWKGGVQVESRVLQHNAQFSNDQEEIRLDLAGSLDGQLWDLEAIFLPVYGKSLQELLQMDGKRQYLQASTSLLYTKNPNGYLLSLPVQELADRFIIPGIKLNDFSGVKIYKKLSTSPFALNLTMLPKVKFPGIDLLTQYSTPEGSSVPIFEATIPEIHLTVSQFTLPKSLPVGNTVFDLNKLANMIADVDLPSVTLPEQTIVIPPLEFSVPAGIFIPFFGELTARAGMASPLYNVTWSAGWKTKADHVETFLDSMCTSTLQFLEYALKVVETHKIEEDLLTYNIKGTLQHCDFNVEYNEDGLFKGLWDWQGEAHLDITSPALTDFHLYYKEDKTSLSASAASSTIGTVGLDSSTDDQSVELNVYFHPQSPPEKKLSIFKTEWRYKESDGERYIKINWEEEAASRLLGSLKSNVPKASKAIYDYANKYHLEYVSSELRKSLQVNAEHARRMVDEMNMSFQRVARDTYQNLYEEMLAQKSLSIPENLKKRVLDSIVHVTQKYHMAVMWLMDSFIHFLKFNRVQFPGYAGTYTVDELYTIVMKETKKSLSQLFNGLGNLLSYVQNQVEKSRLINDITFKCPFFSKPCKLKDLILIFREELNILSNIGQQDIKFTTILSSLQGFLERVLDIIEEQIKCLKDNESTCVADHINMVFKIQVPYAFKSLREDIYFVLGEFNDFLQSILQEGSYKLQQVHQYMKALREEYFDPSMVGWTVKYYEIEENMVELIKTLLVSFRDVYSEYSVTAADFASKMSTQVEQFVSRDIREYLSMLTDINGKWMEKIAELSIVAKETMKSWVTAVAKIMSDYPQQFHSNLQDFSDQLSSYYEKFVGESTRLIDLSIQNYHVFLRYITELLRKLQVATANNVSPYIKLAQGELMITF
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Apolipoprotein B is a major protein constituent of chylomicrons (apo B-48), LDL (apo B-100) and VLDL (apo B-100). Apo B-100 functions as a recognition signal for the cellular binding and internalization of LDL particles by the apoB/E receptor.
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E9Q4F7
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ANR11_MOUSE
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Ankyrin repeat domain-containing protein 11
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MPKGGCSKTPQQEDFALSNDMVEKQTGKKDKDKVSLTKTPKLDRSDGGKEVRERATKRKLPFTVGANGEQKDSDTEKQGPERKRIKKEPVARKSGLLFGMGLSGIRAGYPLSERQQVALLMQMTAEESANSPVDTTPKHPSQSTVCQKGTPNSASKTKDKVNKRNERGETRLHRAAIRGDARRIKELISEGADVNVKDFAGWTALHEACNRGYYDIAKQLLAAGAEVNTKGLDDDTPLHDAANNGHYKVVKLLLRYGGNPQQSNRKGETPLKVANSPTMVNLLLGKGTYTSSEESSTESSEEEDAPSFAPSSSVDGNNTDSEFEKGLKLKAKNPEPQKTVTPVKDEYEFDEDDEQDRVPPVDDKHLLKKDYRKEAKANSFISIPKMEVKSYSKNNTLAPKKAAHRILSDTSDEEDVSVSIGAGEKLRLSAHTMLPGSKARESSSSRQQKEKNKLKKKRKKETKGKEVRFGKRSDKFCSSGSESESSESEEDDGDSVGSSGCLKGSPLVLKDPSLFSSLSASSTSSHGSAVAQKHGSGHTDQHTKHWRTDNWKAISSPAWSEVSSLSDSSRTGLTSESDCSSEGSSVESLKPTRRKQEHRKRGVLQSAPSEKRSSFHPCTDGAVPKLDKEGKVVKKHKTKHKHKHKEKGQCSVSQELKLKSFTYEYEDSKQKSDKAILLESDLSTENKLKVLKHDREHLKKEDKLGRMKPEDKDWLFKDEKVLKRIKDANKDMSRAFREDKDRASKAERERATKDKSPKEEKLRLYKEERKKKSKDRASRLERKNDMKEDKLSKEKEKAFKEDKEKLKKEKLYREDAAFDDYCNKSQFLDHEDTKFSLSDDQQERWFSDLSDSSFDFKGEDSWDSVTDYRDIKNDSVAKLILETVKEDSKEKKRDNKIREKRDFKDSFFRKRDRDCLDKNSEKRRDQTEKHKSIPSYLSEKDKKRRESAEGGRDRRDGRIRSEEVHREDLKECGFESSFKDKSDCDFPKNLEPWERPHAAREKEKKDALEKERKEKGRADKYKEKSSERERSDKSTLDKCQKDKEFEKCFKEKKDGKEKHKDIHSKDRKASFDQLREKKEKVFSSIISEDFSERKDDRKGKEKSWYIADIFTDESEDEKDDCVAGSFKATEASDTQRVDGLPEKEEGREHPSDRHRKSSSDRQHTEKPRDKEPKEKKKDRGASEGGKDKKEKMEKIFEKHKEKKDKECAERYKDRKERASADSAPEKKNKQKLPEKVEKKHFAEDKVKSKHKEKPEKEHSRERERKPSRGPDVEKSLLEKLEEEALHDYREDSNDKISEVSSDSFADHGQEPSLSTLLEVSFSEPPAEDKARDSACLSEKLREKERHRHSSSSSKKSHERERAKKEKAEKKEKSEDYKDSISSVRKDASQFEKDFLDAETYGVSYPTKADVEEELDKAIELFSSEKKDRSDPEREPAKRIEKELKPYGSSAISILKEKKKREKHRERWREEKERHRDKHVDGFLRHHKDEPKPAAKDKDNPPNSFKEKSREESLKLSETKLKEKFKENTEREKGDSIKMSNGNDKLVPSRDSGKKDSRPREKLLGDGDLMMTSFERMLSQKDLEIEERHKRHKERMKQMEKMRHRSGDPKLKEKKPTEDGRKKSLDFPSKKALGLDKKVKEPAPTLTTGESKPHSGPGTESKDWLSGQPLKEVLPASPRTEQSRPTGVPTPTSVVSCPSYEEVMHTPRTPSCSADDYPDLVFDCTDSQHSMPVSTASTSACSPPFFDRFSVASSVVSENAAGQTPTRPISTNLYRSISVDIRRTPEEEFSAGDKLFRQQSVPAPSSFDSPVQHLLEEKAPLPPVPAEKFACLSPGYYSPDYGIPSPKVDTLHCPPTAVVSATPPPDSVFSNLPPKSSPSPRGELLSPAIEGTLPPDLGLPLDATEDQQATAAILPQEPSYLEPLDEGPFTTVITEEPVEWTHTAAEQGLSSSSLIASASENPVSWPVGSELMLKSPQRFAESPKHFCPGESLHSTTPGPYSAAEPTYPVSPGSYPLPAPEPALEEVKDGGTGAIPVAISAAEGAAPYAAPARLESFFSNCKSHPDAPLDTAPEPTGVTAVAQVEALGPLESSFLDSNPSISTLSQVEPVSWHEAFTSPEDDLDLGPFSLPELPLQAKDASDVEAEAAKASPVPPAESPPGPTGVLGGGDVPAPAAEEPPAPPPQEASPQLSTEPEPSEEPKLDVVLEATVETEVLADDSAPEASISNSVPAPSPPQQQPPGGGDEEAETEDPSATPCCAPDGPTTDGLAQAHNSAEASCVVAAAEGPPGNVQAEATDPEPKPTSEVPKAPKVEEVPQRMTRNRAQMLASQSKQGIPAAEKDPMPTPASRAKGRASEEEDAQAQHPRKRRFQRSSQQLQQQLNTSTQQTREVIQQTLAAIVDAIKLDAIEPYHSDRSNPYFEYLQIRKKIEEKRKILCCITPQAPQCYAEYVTYTGSYLLDGKPLSKLHIPVIAPPPSLAEPLKELFKQQEAVRGKLRLQHSIEREKLIVSCEQEILRVHCRAARTIANQAVPFSACTMLLDSEVYNMPLESQGDENKSVRDRFNARQFISWLQDVDDKYDRMKTCLLMRQQHEAAALNAVQRMEWQLKAQELDPAGHKSLCVNEVPSFYVPMVDVNDDFVLLPA
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Chromatin regulator which modulates histone acetylation and gene expression in neural precursor cells. May recruit histone deacetylases (HDACs) to the p160 coactivators/nuclear receptor complex to inhibit ligand-dependent transactivation (By similarity). Has a role in proliferation and development of cortical neural precursors. May also regulate bone homeostasis.
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E9Q4N7
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ARI1B_MOUSE
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AT-rich interactive domain-containing protein 1B (ARID domain-containing protein 1B) (BRG1-associated factor 250b) (BAF250B)
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MAARAAAAARARAGSGERRAPSGPRPAPGARDLETGARGAVAAPGPILGGGDGGLNNVHHHPLHPRHDLNMAHSASAAAAASSNSAQSGRSEAALKEGGSAAALSSSAAVAASSSSAGPGSTMETGLLPNHKLKAVGEAPAAPPHQQHHHHHAHHHHHHHAHHLHHLHHHHALQQQLNQFQQPQPPQPQQQQPPPPPQQQHPTANNSLGGAGGGAPQPGPDMEQPQHGGAKDSVAGNQADPQGQPLLSKPGDEDDAPPKMGEPAGSRYEHPGLGAQQQPAPVAVPGGGGGPAAVSEFNNYYGSAAPASGGPGGRAGPCFDQHGGQQSPGMGMMHSASAAAGAPSSMDPLQNSHEGYPNSQYNHYPGYSRPGAGGGGGGGGGGGGSGGGGGGGGAGGAGGAAAAAAGAGAVAAAAAAAAAAAAAAGGGGGGGYGSSSSGYGVLSSPRQQGGGMMMGPGGGGAASLSKAAAGAAAAAGGFQRFAGQNQHPSGATPTLNQLLTSPSPMMRSYGGSYPDYSSSSAPPPPSQPQSQAAAGAAAGGQQAAAGMGLGKDLGAQYAAASPAWAAAQQRSHPAMSPGTPGPTMGRSQGSPMDPMVMKRPQLYGMGTHPHSQPQQSSPYPGGSYGPPGAQRYPLGMQGRAPGALGGLQYPQQQMPPQYGQQAVSGYCQQGQQPYYNQQPQPSHLPPQAQYLQPAAAQSQQRYQPQQDMSQEGYGTRSQPPLAPGKSNHEDLNLIQQERPSSLPDLSGSIDDLPTGTEATLSSAVSASGSTSSQGDQSNPAQSPFSPHASPHLSSIPGGPSPSPVGSPVGSNQSRSGPISPASIPGSQMPPQPPGSQSESSSHPALSQSPMPQERGNYSRTPTYSGVPSASYSGPGPGMGINANNQMHGQGPAQPCGAMPLGRMPSAGMQNRPFPGTMSSVTPSSPGMSQQGGPGMGPPMPTVNRKAQEAAAAVMQAAANSAQSRQGSFPGMNQSGLVASSSPYSQSMNNNSSLMSTQAQPYSMTPTMVNSSTASMGLADMMSPSESKLSVPLKADGKEEGVSQPESKSKDSYGSQGISQPPTPGNLPVPSPMSPSSASISSFHGDESDSISSPGWPKTPSSPKSSSSSTTGEKITKVYELGNEPERKLWVDRYLTFMEERGSPVSSLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVGTSSSAASSLKKQYIQYLFAFECKTERGEEPPPEVFSTGDSKKQPKLQPPSPANSGSLQGPQTPQSTGSNSMAEVPGDLKPPTPASTPHGQMTPMQSGRSSTVSVHDPFSDVSDSAYPKRNSMTPNAPYQQGMGMPDMMGRMPYEPNKDPFSGMRKVPGSSEPFMTQGQVPNSGMQDMYNQSPSGAMSNLGMGQRQQFPYGTSYDRRHEAYGQQYPGQGPPTGQPPYGGHQPGLYPQQPNYKRHMDGMYGPPAKRHEGDMYNMQYGSQQQEMYNQYGGSYSGPDRRPIQGQYPYPYNRERMQGPGQMQPHGIPPQMMGGPMQSSSSEGPQQNMWATRNDMPYPYQSRQGPGGPAQAPPYPGMNRTDDMMVPEQRINHESQWPSHVSQRQPYMSSSASMQPITRPPQSSYQTPPSLPNHISRAPSPASFQRSLESRMSPSKSPFLPTMKMQKVMPTVPTSQVTGPPPQPPPIRREITFPPGSVEASQPILKQRRKITSKDIVTPEAWRVMMSLKSGLLAESTWALDTINILLYDDSTVATFNLSQLSGFLELLVEYFRKCLIDIFGILMEYEVGDPSQKALDHRSGKKDDSQSLEDDSGKEDDDAECLVEEEEEEEEEEEDSEKIESEGKSSPALAAPDASVDPKETPKQASKFDKLPIKIVKKNKLFVVDRSDKLGRVQEFSSGLLHWQLGGGDTTEHIQTHFESKMEIPPRRRPPPPLSSTGKKKELEGKGDSEEQPEKSIIATIDDVLSARPGALPEDTNPGPQTDSGKFPFGIQQAKSHRNIRLLEDEPRSRDETPLCTIAHWQDSLAKRCICVSNIVRSLSFVPGNDAEMSKHPGLVLILGKLILLHHEHPERKRAPQTYEKEEDEDKGVACSKDEWWWDCLEVLRDNTLVTLANISGQLDLSAYTESICLPILDGLLHWMVCPSAEAQDPFPTVGPNSVLSPQRLVLETLCKLSIQDNNVDLILATPPFSRQEKFYATLVRYVGDRKNPVCREMSMALLSNLAQGDTLAARAIAVQKGSIGNLISFLEDGVTMAQYQQSQHNLMHMQPPPLEPPSVDMMCRAAKALLAMARVDENRSEFLLHEGRLLDISISAVLNSLVASVICDVLFQIGQL
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Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth. Binds DNA non-specifically.
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E9Q4P1
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WDFY1_MOUSE
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WD repeat and FYVE domain-containing protein 1 (WD40- and FYVE domain-containing protein 1)
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MAAEIHSRPQSSRPVLLSKIEGHQDAVTAALLIPKEDGVITASEDRTIRVWLKRDSGQYWPSIYHTMASPCSAMAYHHDSRRIFVGQDNGAVMEFHVSEDFNKMNFIKTYPAHQNRVSAIIFSLAAEWVISTGHDKCVSWMCTRSGNMLGRHFFSSWASCLQYDLDTQHAFVGDYSGQITLLKLEQNTCSVITTLKGHEGSIACLWWDPIQRLLFSGASDNSVIMWDIGGRKGRTLLLQGHHDRVQSLCYLQLTRQLVSCSADGGIAVWNMDVSREEAPQWLESDSCQKCEQPFFWNIKQMWDTKTLGLRQHHCRKCGQAVCGKCSSKRSSYPVMGFEFQVRVCDSCYDSIKDEDRTSLATFHEGKHNISHMSMDIARGLMVTCGTDRVVKIWDMTPVVGCSLATGFSPH
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Positively regulates TLR3- and TLR4-mediated signaling pathways by bridging the interaction between TLR3 or TLR4 and TICAM1. Promotes TLR3/4 ligand-induced activation of transcription factors IRF3 and NF-kappa-B, as well as the production of IFN-beta and inflammatory cytokines.
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E9Q4S1
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PDE8B_MOUSE
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High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B (PDE8B) (EC 3.1.4.53) (Cell proliferation-inducing gene 22 protein)
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MGCAPSIHVSQSGVIYCRDSDESNSPRQTSSVSQGPTAPLHGLFVQTDAADAMPPSRAAGPPGAVRVRRSRAELGSGSSTGSSGPATTTCRGRRRHCCSSAEAETQTSYTSVKVLLIFAKEDSQSDGFWWACDRAGYRCNIARTPESALECFLDKHHEIIVIDHRQSRNFDAEAVCRSIRATNPSEHTVILAVVSQASDDHEEASVLPLLHAGFNRRFMENSSIIACYNELIQIEHGEVRSQFKLRACNSVFTALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLPKSDKNRADLLDTINTCIKKGKEWQGVYYARRKSGDSIQQHVKITPVIGQGGKIRHFVSLKKLCCTTDSNKQIHRIHRDSGDNSQTEPHSFRHKSRRKESIDVKSISSRGSDAPSLQNRRYPSMARIHSMTIEAPITKVINIINAAQENSPVTVAEALDRVLEILRTTELYSPQLGTKDEDPHTSDLVGGLMTDGLRRLSGNEYVFTKNVHHSHSHLSMPITINDVPPSIAQLLDNEESWDFNIFELEAVTHKRPLVYLGLKVFSRFGVCEFLNCTETTLRAWLQVIEANYHSSNAYHNSTHAADVLHATAFFLGKERVKGSLDQLDEVAALIAATVHDVDHPGRTNSFLCNAGSELAVLYNDTAVLESHHTALAFQLTVKDTKCNIFKNIDRNHYRTLRQAIIDMVLATEMTKHFEHVNKFVNSINKPLAAESEGSDCECNPTGKNFPENQILIKRMMIKCADVANPCRPLDLCIEWAGRISEEYFAQTDEEKRQGLPVVMPVFDRNTCSIPKSQISFIDYFITDMFDAWDAFAHLPALMQHLADNYKHWKTLDDLKCKTLRLPSDS
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Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in specific signaling in the thyroid gland (By similarity).
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E9Q4Z2
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ACACB_MOUSE
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Acetyl-CoA carboxylase 2 (EC 6.4.1.2) (ACC-beta)
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MVLLLFLTCLVFSCLTFSWLKIWGKMTDSKPLTNSKVEANLLSSEESLSASELSGEQLQEHGDHSCLSYRGPRDASQQRNSLPSSCQRPPRNPLSSNDTWPSPELQTNWTAAPGPEVPDANGLSFPARPPSQRTVSPSREDRKQAHIKRQLMTSFILGSLDDNSSDEDPSAGSFQNSSRKSSRASLGTLSQEAALNTSDPESHAPTMRPSMSGLHLVKRGREHKKLDLHRDFTVASPAEFVTRFGGNRVIEKVLIANNGIAAVKCMRSIRRWAYEMFRNERAIRFVVMVTPEDLKANAEYIKMADQYVPVPGGPNNNNYANVELIIDIAKRIPVQAVWAGWGHASENPKLPELLCKHEIAFLGPPSEAMWALGDKIASTIVAQTLQIPTLPWSGSGLTVEWTEDSRHQGKCISVPEDVYEQGCVKDVDEGLQAAEKIGFPLMIKASEGGGGKGIRKAESAEDFPMLFRQVQSEIPGSPIFLMKLAQNARHLEVQVLADQYGNAVSLFGRDCSIQRRHQKIIEEAPATIAAPAVFEFMEQCAVLLAKMVGYVSAGTVEYLYSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLHRLKDIRLLYGESPWGVTPIPFETPLSPPIARGHVIAARITSENPDEGFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGDFRTTVEYLVNLLETESFQNNDIDTGWLDHLIAQRVQAEKPDIMLGVVCGALNVADAMFRTCMTEFLHSLERGQVLPADSLLNIVDVELIYGGIKYALKVARQSLTMFVLIMNGCHIEIDAHRLNDGGLLLSYNGSSYTTYMKEEVDSYRITIGNKTCVFEKENDPTVLRSPSAGKLMQYTVEDGDHVEAGSSYAEMEVMKMIMTLNVQESGRVKYIKRPGVILEAGCVVARLELDDPSKVHAAQPFTGELPAQQTLPILGEKLHQVFHGVLENLTNVMSGYCLPEPFFSMKLKDWVQKLMMTLRHPSLPLLELQEIMTSVAGRIPAPVEKAVRRVMAQYASNITSVLCQFPSQQIATILDCHAATLQRKADREVFFMNTQSIVQLVQRYRSGTRGYMKAVVLDLLRKYLNVEHHFQQAHYDKCVINLREQFKPDMTQVLDCIFSHSQVAKKNQLVTMLIDELCGPDPTLSDELTSILCELTQLSRSEHCKVALRARQVLIASHLPSYELRHNQVESIFLSAIDMYGHQFCPENLKKLILSETTIFDVLPTFFYHENKVVCMASLEVYVRRGYIAYELNSLQHRELPDGTCVVEFQFMLPSSHPNRMAVPISVSNPDLLRHSTELFMDSGFSPLCQRMGAMVAFRRFEEFTRNFDEVISCFANVQTDTLLFSKACTSLYSEEDSKSLREEPIHILNVAIQCADHMEDEALVPVFRAFVQSKKHILVDYGLRRITFLVAQEREFPKFFTFRARDEFAEDRIYRHLEPALAFQLELSRMRNFDLTAVPCANHKMHLYLGAAKVKEGLEVTDHRFFIRAIIRHSDLITKEASFEYLQNEGERLLLEAMDELEVAFNNTSVRTDCNHIFLNFVPTVIMDPLKIEESVRDMVMRYGSRLWKLRVLQAEVKINIRQTTSDSAIPIRLFITNESGYYLDISLYREVTDSRSGNIMFHSFGNKQGSLHGMLINTPYVTKDLLQAKRFQAQSLGTTYVYDFPEMFRQALFKLWGSPEKYPKDILTYTELVLDSQGQLVEMNRLPGCNEVGMVAFKMRFKTPEYPEGRDAVVIGNDITFQIGSFGIGEDFLYLRASEMARTEGIPQIYLAANSGARMGLAEEIKQIFQVAWVDPEDPHKGFRYLYLTPQDYTQISSQNSVHCKHIEDEGESRYVIVDVIGKDANLGVENLRGSGMIAGEASLAYEKTVTISMVTCRALGIGAYLVRLGQRVIQVENSHIILTGAGALNKVLGREVYTSNNQLGGVQIMHTNGVSHVTVPDDFEGVCTILEWLSFIPKDNRSPVPITTPSDPIDREIEFTPTKAPYDPRWMLAGRPHPTLKGTWQSGFFDHGSFKEIMAPWAQTVVTGRARLGGIPVGVIAVETRTVEVAVPADPANLDSEAKIIQQAGQVWFPDSAYKTAQVIRDFNKERLPLMIFANWRGFSGGMKDMYEQMLKFGAYIVDGLRLYEQPILIYIPPCAELRGGSWVVLDSTINPLCIEMYADKESRGGVLEPEGTVEIKFRKKDLVKTIRRIDPVCKKLVGQLGKAQLPDKDRKELEGQLKAREELLLPIYHQVAVQFADLHDTPGHMLEKGIISDVLEWKTARTFFYWRLRRLLLEAQVKQEILRASPELNHEHTQSMLRRWFVETEGAVKAYLWDSNQVVVQWLEQHWSAKDGLRSTIRENINYLKRDSVLKTIQSLVQEHPEVIMDCVAYLSQHLTPAERIQVAQLLSTTESPASS
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Mitochondrial enzyme that catalyzes the carboxylation of acetyl-CoA to malonyl-CoA and plays a central role in fatty acid metabolism (By similarity). Catalyzes a 2 steps reaction starting with the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain followed by the transfer of the carboxyl group from carboxylated biotin to acetyl-CoA (By similarity). Through the production of malonyl-CoA that allosterically inhibits carnitine palmitoyltransferase 1 at the mitochondria, negatively regulates fatty acid oxidation. Together with its cytosolic isozyme ACACA, which is involved in de novo fatty acid biosynthesis, promotes lipid storage.
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E9Q555
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RN213_MOUSE
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E3 ubiquitin-protein ligase RNF213 (EC 2.3.2.27) (EC 3.6.4.-) (E3 ubiquitin-lipopolysaccharide ligase RNF213) (EC 2.3.2.-) (Mysterin) (RING finger protein 213)
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MECPQCGHVSSEKAPKFCSECGQKLPSAATVQGDLKNDNTLVVSSTPEGKTEQGAVLREEEVLLSSTDPGKELEKPEESDSNASWTTQMSKKEKRRRKRQGTISSSEAPSSGLWSLDMPPSPGSHNSALPQNQAQQGGAASQPGHPLDTENMPMEDGFVHTEGSGSPLQGQAAERTDAQSNLAPSDLAEVKDLNTSKPSVDKGLPLDGGPALSAFKGHPKMTDASQKAPLPESKGETSGQEKKVPPIDAAASPVKTAGKETGEDVRKPKPSPVSPVASKHGDQEAELKGKLATPVRKSNEGGNTQPEDQRKPGEGRNFAAAVKTQQAAAPQQAAAPEPTSAFNPRDTVTVYFHAIVSRHFGFNPEEHKVYVRGGEGLGQKGWTDACEMYCTQDLHDLGSLVEGKMDIPRQSLDKPIPYKYVIHRGGSSKDTVEYEFIYEQAQKKGEHVNRCLRVVSTSLGNGDWHQYDDIICMRSTGFFQQAKNRILDSTRKELLKGKKQAAVVMLDRIFSVLQPWSDINLQSFMTQFLQFYSVVREPMIHDGRARKWTSLQYEEKEVWTNLWEHVKKQMAPFLEGKSGESLPADCPVRSKLTLGLSILFMVEAAEFTVPKKDLDSLCYLLIPSAGSPEALHSDLSPVLRIRQRWRIYLTNLCLRCIDERCDRWLGILPLLHTCMQKSPPKKNSKSQPEDTWAGLEGISFSEFRDKAPTRSQPLQFMQSKMALLRVDEYLFRSWLSVVPLESLSSYLENSIDYLSDVPVRVLDCLQGISYRLPGLRKISNQNMKKDVENVFKMLMHLVDIYQHRIFGENLLQIYLTECLTLHETVCNITANHQFFEIPALSAELICKLLELSPPGHTDEGLPEKSYEDLVTSTLQEALATTRNWLRSLFKSRMLSISSAYVRLTYSEEMAVWRRLVEIGFPEKHGWKGSLLGDMEGRLKQEPPRLQISFFCSSQCRDGGLHDSVSRSFEKCVIEAVSSACQSQTSVLEGLSCQDLQKFGTLLSAVITKSWPVHNGEPVFDVDEIFKYLLKWPDVRQLFELCGTNEKIIDNITEEGRQLMATAESVFQKVAGELENGTIVVGQLELILEHQSQFLDIWNLNRRRLPSQEKACDVRSLLKRRRDDLLFLKQEKRYVESLLRQLGRVKHLVQVDFGNIEIIHSQDLSNKKLNEAVIKLPNSSSYKRETHYCLSPDIREMASKLDSLKDSHIFQDFWQETAESLNTLDKDPRELKVSLPEVLEYLYNPCYDNFYTLYENLKSGKITFAEVDAIFKDFVDKYDELKNDLKFMCTMNPQDQKGWISERVGQIKEYHTLHQAVSSAKVILQVRRALGVTGDFSVLNPLLNFADSFEDFGNEKLDQISPQFIKAKQLLQDISEPRQRCLEELARQTELVAWLHKALEDINELKVFVDLASISAGENDIDVDRVACFHDAVQGYASLLYKMDERTNFSDFMNHLQELWRALDNDQHLPDKLKDSARNLEWLKTVKESHGSVELSSLSLATAINSRGVYVIEAPKDGQKISPDTVLRLLLPDGHGYPEALRTYSTEELKELLNKLMLMSGKKDHNSNTEVEKFSEVFSNMQRLVHVFIKLHCAGNMLFRTWTAKVYCCPDGGIFMNFGLELLSQLTEKGDVIQLLGALCRQMEDFLDNWKTVVAQKRAEHFYLNFYTAEQLVYLSSELRKPRPSEAALMMLSFIKGKCTVQDLVQATSACESKADRYCLREVMKKLPQQLLSEPSLMGKLQVIMMQSLVYMSAFLPHCLDLDALGRCLAHLATMGGTPVERPLPKGLQAGQPNLILCGHSEVLPAALAIYMQAPRQPLPTFDEVLLCTPATTIEEVELLLRRCLTSGSQGHKVYSLLFADQLSYEVGCQAEEFFQSLCTRAHREDYQLVILCDAAREHCYIPSTFSQYKVPLVPQAPLPNIQAYLQSHYQVPKRLLSAATVFRDGLCVGIVTSERAGVGKSLYVNTLHTKLKAKLRDETVPLKIIRLTEPHLDENQVLSALLPFLKEKYQKMPVIFHIDISTSVQTGIPIFLFKLLILQYLMDINGKIWRRSPGHLYLVEIPQGLSVQPKRSSKLNARAPLFKFLDLFPKVTCRPPKEVIDMELTPERSHTDPAMDPVEFCSEAFQRPYQYLKRFHQQQNLDTFQYEKGSVEGSPEECLQHFLIYCGLINPSWSELRNFAWFLNCQLKDCEASIFCKSAFTGDTLRGFKNFVVTFMILMARDFATPTLHTSDQSPGRQSVTIGEVVEEDLAPFSLRKRWESEPHPYVFFNGDHMTMTFIGFHLETNNNGYVDAINPSNGKVIKKDVMTKELFDGLRLQRVPFNIDFDNLPRYEKLERLCLALGIEWPIDPDETYELTTDNMLKILAIEMRFRCGIPVIIMGETGCGKTRLIKFLSDLKRGSVEAETMKLVKVHGGTTPSMIYSKVKEAERTAFSNKAQHKLDTILFFDEANTTEAVSCIKEILCDRTVDGEHLHEDSGLHIIAACNPYRKHSQEMILRLESAGLGYRVSAEETADRLGSIPLRQLVYRVHALPPSLIPLVWDFGQLNDSAEKLYIQQIVQRLVDSVSVNPSETCVIADVLSASQMFMRKRENECGFVSLRDVERCVKVFRWFHDHSDMLLKELDKFLHESSDSTHTFERDPVLWSLVMAIGVCYHASLEEKASYRTAIARCFPKPYNSSRAILDEVTHVQDLFLRGAPIRTNIARNLALKENVFMMVICIELKIPLFLVGKPGSSKSLAKIIVADAMQGQAAFSELFRCLKQVHLVSFQCSPHSTPQGIISTFKQCARFQQGKDLGQYVSVVVLDEVGLAEDSPKMPLKTLHPLLEDGCIEDDPAPYKKVGFVGISNWALDPAKMNRGIFVSRGSPNEKELIESAEGICSSDRLVQDKIRGYFAPFAKAYETVCQKQDKEFFGLRDYYSLIKMVFAKAKASKRGLSPQDITHAVLRNFSGKDNIQALSIFTASLPEARYKEEVSTVELIKQNIYPGPQASSRGLDGAESRYLLVLTRNYVALQILQQTFFEGQQPEIIFGSSFPQDQEYTQICRNINRVKICMETGKMVVLLNLQNLYESLYDALNQYYVYLGGQKYVDLGLGTHRVKCRVHTAFRLIVIEEKDVVYKQFPVPLINRLEKHYLDMNTVLQPWQKSIVQELQQWAHEFADVKADQFIARHKYSPADVFIGYHSDACASVVLQAVERQGCRDLTEELYRKVSEEARSILLDCATPDAVVRLSGSSLGSFTAKQLSQEYYYAQQHNSFVDFLQAHLRMTHHECRAVFTEITTFSRLLTGNDCDVLASELRGLASKPVVLSLQQYDTEYSFLKDVRSWLTNPGKRKVLVIQADFDDGTRSAQLVASAKYTAINEINKTQGTKDFVFVYFVTKLSRMGSGTSYVGFHGGLWRSVHIDDLRRSTIMASDVTKLQNVTISQLFKPEDKPEQEEMEIETSQSKELAEEQMEVEDSEEMKKASDPRSCDCSQFLDTTRLVQSCVQGAVGMLRDQNESCARNMRRVTILLDLLNEDNTRNASFLRESKMRLHVLLNKQEENQVRSLKEWVTREAANQDALQEAGTFRHTLWKRVQDVVTPILASMIAHIDRDGNLELLAQPDSPAWVQDLWMFIYSDIKFLNISLVLNNTRSNSEMSFILVQSHMNLLKDAYNAVPFSWRIRDYLEELWVQAQYITDTEGLSKKFVEIFQKTPLGVFLAQFPVAQQQKLLQSYLKDFLLLTMKVSSREELMFLQMALWSCLRELQEASGTPDETYKFPLSLPWVHLAFQHFRTRLQNFSRILTIHPQVLSSLSQAAEKHSLAGCEMTLDAFAAMACAEMLKGDLLKPSPKAWLQLVKNLSTPLELVCSEGYLCDSGSMTRSVIQEVRALWNRIFSIALFVEHVLLGTESHIPELSPLVTTYVSLLDKCLEEDSNLKTCRPFVAVMTTLCDCKDKASKKFSRFGIQPCFICHGDAQDPVCLPCDHVYCLRCIQTWLIPGQMMCPYCLTDLPDKFSPTVSQDHRKAIEKHAQFRHMCNSFFVDLVSTMCFKDNTPPEKSVIDTLLSLLFVQKELLRDASQKHREHTKSLSPFDDVVDQTPVIRSVLLKLLLKYSFHEVKDYIQNYLTQLEKKAFLTEDKTELYLLFISCLEDSVHQKTSAGCRNLEQVLREEGHFLRTYSPGLQGQEPVRIASVEYLQEVARVRLCLDLAADFLSELQEGSELAEDKRRFLKHVEEFCTRVNNDWHRVYLVRKLSSQRGMEFVQSFSKQGHPCQWVFPRKVIAQQKDHVSLMDRYLVHGNEYKAVRDATAKAVLECKTLDIGNALMACRSPKPQQTAYLLLALYTEVAALYRSPNGSLHPEAKQLEAVNKFIKESKILSDPNIRCFARSLVDNTLPLLKIRSANSILKGTVTEMAVHVATILLCGHNQILKPLRNLAFYPVNMANAFLPTMPEDLLVHARTWRGLENVTWYTCPRGHPCSVGECGRPMQESTCLDCGLPVGGLNHTPHEGFSAIRNNEDRTQTGHVLGSPQSSGVAEVSDRGQSPVVFILTRLLTHLAMLVGATHNPQALTVIIKPWVQDPQGFLQQHIQRDLEQLTKMLGRSADETIHVVHLILSSLLRVQSHGVLNFNAELSTKGCRNNWEKHFETLLLRELKHLDKNLPAINALISQDERISSNPVTKIIYGDPATFLPHLPQKSIIHCSKIWSCRRKITVEYLQHIVEQKNGKETVPVLWHFLQKEAELRLVKFLPEILALQRDLVKQFQNVSRVEYSSIRGFIHSHSSDGLRKLLHDRITIFLSTWNALRRSLETNGEIKLPKDYCCSDLDLDAEFEVILPRRQGLGLCGTALVSYLISLHNNMVYTVQKFSNEDNSYSVDISEVADLHVISYEVERDLNPLILSNCQYQVQQGGETSQEFDLEKIQRQISSRFLQGKPRLTLKGIPTLVYRRDWNYEHLFMDIKNKMAQSSLPNLAISTISGQLQSYSDACEALSIIEITLGFLSTAGGDPGMDLNVYIEEVLRMCDQTAQVLKAFSRCQLRHIIALWQFLSAHKSEQRLRLNKELFREIDVQYKEELSTQHQRLLGTFLNEAGLDAFLLELHEMIVLKLKGPRAANSFNPNWSLKDTLVSYMETKDSDILSEVESQFPEEILMSSCISVWKIAATRKWDRQSR
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Atypical E3 ubiquitin ligase that can catalyze ubiquitination of both proteins and lipids, and which is involved in various processes, such as lipid metabolism, angiogenesis and cell-autonomous immunity. Acts as a key immune sensor by catalyzing ubiquitination of the lipid A moiety of bacterial lipopolysaccharide (LPS) via its RZ-type zinc-finger: restricts the proliferation of cytosolic bacteria, such as Salmonella, by generating the bacterial ubiquitin coat through the ubiquitination of LPS. Also acts indirectly by mediating the recruitment of the LUBAC complex, which conjugates linear polyubiquitin chains (By similarity). Ubiquitination of LPS triggers cell-autonomous immunity, such as antibacterial autophagy, leading to degradation of the microbial invader (By similarity). Involved in lipid metabolism by regulating fat storage and lipid droplet formation act by inhibiting the lipolytic process (By similarity). Also regulates lipotoxicity by inhibiting desaturation of fatty acids (By similarity). Also acts as an E3 ubiquitin-protein ligase via its RING-type zinc finger: mediates 'Lys-63'-linked ubiquitination of target proteins (By similarity). Involved in the non-canonical Wnt signaling pathway in vascular development: acts by mediating ubiquitination and degradation of FLNA and NFATC2 downstream of RSPO3, leading to inhibit the non-canonical Wnt signaling pathway and promoting vessel regression (By similarity). Also has ATPase activity ATPase activity is required for ubiquitination of LPS.
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E9Q557
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DESP_MOUSE
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Desmoplakin (DP)
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MSCNGGSHPRINTLGRMTRAESGPDLRYEMTYSGGGGGGGGGGGGGTSRTFYSHSRRCTVNDQNSDGYCQTGTMSRHQNQNTIQEMLQNCSDCLMRAELIAQPELKFGEGMQLAWNRELDEYFTQANDQMEIIDGLIREMRQMGQPCDAYQKRLLQLQEQMRALYKAISVPRVRRASSKGAGGYTCQSGSGWDEFTKRLTGECLGWMRQQREEMDLMAWGVDAGSVEQHINSHRSIHNTIGDYRWQLDKIKADLREKSAIYQLEEEYENLLKASFERMDHLRQLQNIIQATSREIMWINDCEEEELLYDWSDKNTNIAQKQEAFSIRMSQLEVKEKELNKLKQESDQLVLNQHPASDKIEAYMDTLQTQWSWILQITKCIDVHLKENAAYFQFFEEAQSTEAYLKGLQDSIRKKYPCDKNMPLQHLLEQIKELEKEREKIIEYKRQVQNLVNKSKKIVQLKPRNPDYRSNKPIILRALCDYKQDQKIVHKGDECILKDNNERSKWYVTGPGGVDMLVPSVGLIIPPPNPLAVDLSCKIEQYYEAILALWNQLYINMKSLVSWHYCMIDIEKIRAMTIAKLKTMRQEDYMKTIEDLELHYQDFIKNSQGSEMFGDDDKRRMQSQFTDAQKHYQTLVIQLPGHPQHQTVTKTEITHLGTCQDVNHNKVIETNRENDKQETWLLMELQKIRRQMEHCEARMTLKNLLLAEQGSTHHITVKINELKSVQNDSQALAEVLNQLKDMLANFRGSEKYCYLQNEIFGLFQKLENINGVSDGYLNSLCSVRALLQAILQTEDMLKVYEARLTEEETVCLDLDKVEAYRCGLKKIKNDLNLKKSLLATMKTELQKAQQIHSQSSQQYPLYDLDLGKFTEKVTQLTDRWQKIDKQIDFRLWDLEKQIKQLRNYRDNYQSFCKWLYDAKRRQDSLESMKFGDSNTVMRFLNEQKNLHSEISGKRDKSEEVHKIAELCANSIKDYELQLASYTSGLETLLNIPIKRTMVQSPSGVILQEAADIHARYIELLTRSGDYYRFLSEMLKSLEDLKLKNTKIEVLEEELRLARDANSENCNKNKFLDQNLQKYQAECSQFKAKLVSLEELKRQAELDGKSAKQNLDKCYGQIKELNEKITRLTYEIEDEKRRRKTVEDRFDQQKNDYDQLQKARQCEKENLSWQKLESEKAIKEKEYEIERLRVLLQEEGARKREYENELAKVRNHYNEEMSNLRNKYETEINITKTTIKEISMQKEDDSKNLRNQMDRLSRENRDLKDEIVRLNDSILQATEQRRRAEENALQQKACGSETMQKKQRLEIELKQVIQQRSEDNARHKQSLEEAAKTIQDKNKEIERLKAEYQEEAKRRWEYENELSKVRNSYDEEIISLKNQFETEINITKTTIHQLTMQKEEDTSGYRAQIDNLTRENRSLCEEVKRLKNTLAQTTENLRRVEENAQQQKATGSEMSQRKQQLEIELRQVTQMRTEESMRYKQSLDDAAKTIQDKNKEIERLKQLVDKETNERKCLEDENSKLQRVQYDLQKANNSATEAMSKLKVQEQELTRLRIDYERVSQERTVKDQDITRIQSSLKDLQLQKQKAEEELSRLKRTASDESSKRKMLEEELEAMRRSLKEQAVKITNLTQQLEQASIVKKRSEDDLRQQRDVLDGHVREKQRTQEELRRLSLDVEALRRQLVQEQENVKQAHLRNEHFQKAIEDKSRSLNESKIEIERLQSLTENLTKEHLMLEEELRNLRLEYDDLRRGRSEADSDKNSTISELRSQLQISNNRTLELQGLINDLQRERENLRQEIEKFQKQALEASNRIQESKSQCTQVVQERESLLVKIKVLEQDKARLQRLEDELNRAKATLEAESRVKQRLECEKQQIQNDLNQWKTQYSRKEETIRKIESEREKSEREKNSLRSEIERLQAEIKRIEERCRRKLEDSSRETQSQLESERCRLQKEIEKLRQRPYGSHRETQTEYEWTVDSSKLVFDGLRKKVTAMQLYECQLIDKTTLDKLLKGKKSVEEVASEIQPFLRGAGAIAGASASPKEKYSLVEAKRKKFITPESTVMLLEAQAATGGIIDPHRNEKLTVDNAVARDLIDFDDRQQIYTAEKAITGFDDPFSGKTVSVSEAIKKNLIDRETGMRLLEAQLASGGVVDPVNSVFLPKDVALARGLIDRDLYRSLNDPRDSQKNFVDPITKKKVSYMQLRERCRIEPHTGLLLLSVQKRSMSFQGIRQPVTVTELVDSGILRPSTVNELESGQISYDEVGERIKDFLQGSSCIAGIYNETTKQKLGIYEAMKIGLVRPGTALELLEAQAATGFIVDPVSNLRLPVEEAYKRGLVGIEFKEKLLSAERAVTGYNDPETGNIISLFQAMNKELIEKGHGIRLLEAQIATGGIIDPKESHRLPVDMAYKRGYFNEELSEILSDPSDDTKGFFDPNTEENLTYLQLKERCIKDEETGLCLLPLKEKKKQVQTSQKNTLRKRRVVIVDPETNKEMSVQEAYKKGLIDYDTFKELCEQECEWEEITITGSDGSTRVVLVDRKTGSQYDIQDAIDKGLVDRKFFDQYRSGSLSLTQFADMISLKNGVGNSSGLGGSVNDDVFSSSRHDSVSKISTISSVRNLTIRSSSLSDPLEESSPIAAIFDTENLEKISIAEGIERGIVDSITGQRLLEAQACTGGIIHPTTGQKLSLQDAVNQGLIDQDMATRLKPAQKAFIGFEGVKGKKKMSAAEAVKEKWLPYEAGQRFLEFQFLTGGLVDPEVHGRISTEEAIRKGFIDGRAAQRLQDISSYAKILTCPKTKLKISYKDAMNRSMVEDITGLRLLEAASVSSKGLPSPYNMSAPGSRSGSRSGSRSGSRSGSRSGSRRGSFDATGNSSYSYSYSFSSSSIGGY
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Major high molecular weight protein of desmosomes. Regulates profibrotic gene expression in cardiomyocytes via activation of the MAPK14/p38 MAPK signaling cascade and increase in TGFB1 protein abundance (By similarity).
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E9Q5C9
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NOLC1_MOUSE
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Nucleolar and coiled-body phosphoprotein 1 (140 kDa nucleolar phosphoprotein) (Nopp140)
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MADTGLRRVVPSDLYPLVLRFLRDSQLSEVASKFAKATGATQQDANASSLLDIYSFWLNRSTKAPKVKLQSNGPVTKKAKKETSSSDSSEDSSEDEDKKAQGLPTQKAAAQVKRASVPQHAGKAAAKASESSSSEESSEEEEEDKKKKPVQQKAAKPQAKAVRPPAKKAESSESDSDSDSDSSSEEETPQTQKPKAAVAAKAQTKAEAKPGTPAKAQPKVANGKAAASSSSSSSSDDSEEEKKAAAPPKKTVPKKQVVAKAPVKVAAAPTQKSSSSEDSSSEEEEGQRQPMKKKAGPYSSVPPPSVPLPKKSPGTQAPKKAAAQTQPADSSDDSSDDSDSSSEEEKKPPAKTVVSKTPAKAAPVKKKAESSSDSSDSDSSEDEAPAKPVSTTKSPKPAVTPKPSAAKAVTTPKQPAGSNQKPQSRKADSSSSEEESSSSEEEEASKKSATTPKAKVTAKAAPAKQAPQAAGDSSSDSDSSSSEEEEKTPKPPAKKKAAGGAVSTPAPGKKAEAKSSSSSSSSSSEDSSEEEKKKKPKATTPKIQASKANGTPASLNGKAAKESEEEEEEEETEEKKKAAGTKPGSGKKRKQNETADEATTPQAKKVKLETPNTFPKRKKGERRASSPFRRVREEEIEVDSRVADNSFDAKRGAAGDWGERANQVLKFTKGKSFRHEKTKKKRGSYRGGSISVQVNSVKFDSE
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Nucleolar protein that acts as a regulator of RNA polymerase I by connecting RNA polymerase I with enzymes responsible for ribosomal processing and modification (By similarity). Required for neural crest specification: following monoubiquitination by the BCR(KBTBD8) complex, associates with TCOF1 and acts as a platform to connect RNA polymerase I with enzymes responsible for ribosomal processing and modification, leading to remodel the translational program of differentiating cells in favor of neural crest specification (By similarity). Involved in nucleologenesis, possibly by playing a role in the maintenance of the fundamental structure of the fibrillar center and dense fibrillar component in the nucleolus. It has intrinsic GTPase and ATPase activities (By similarity).
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E9Q5F9
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SETD2_MOUSE
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Histone-lysine N-methyltransferase SETD2 (EC 2.1.1.359) (Lysine N-methyltransferase 3A) (Protein-lysine N-methyltransferase SETD2) (EC 2.1.1.-) (SET domain-containing protein 2)
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MKPLPSQQPPPKMGDFYDPEHPTPEEEENEAKIENVQKTGFIKGPVFKGVASSRFLPKGTKTKVNLEEQGRQKVSFSFSFTKKTLQNRFLTALSNEKQSDSPNSPAPPLQVDSNPKVKMDAGDTFPATEESSPPKSRVELGRIHFKKHLLHVTSRPQLAASTTAASPLPPTTQLPAVLAESMIDSPPSSPPPPPPPPQASSPSPPAQISEPVALPQPPATALMTSPPGPLPGDVAVRAQKESPVKSGPEVLEVDTKQDIVSNSLEEHTVQTLKEQADHLLQKEDSHIGKEEEVSDGSKISLSSKKASSKKKSSQFEGTFLGSESDEDSVRTSSSQRSHDLKSSTSIDKERDFKKSSAPSKSEDLGKSSRSKTERDDRYCSYSKLERDTRYVSSRCRSERDRRRSRSRSRSDRASRTSLSYSRSERSHYYDSERRYHRSSPYRERTRYSRPYTDNRARESSDSEDEYKKTYPRRTSAHSYRDLRTSSSYSKFDRDCKTETSYLEMERRGKYTSKLERESKRTSEHETIKRCCSPPNELGFRRGSSYSKHDNSTSRYKSALSKSISKNDKFKNSFCCTELNEENKQSHSFSLQTPCSKGSELRTINKISEREKTGSPTPSNQLNDSPTFKKLDESPVLKPEFIGHDGRESIKELELSKVKNDQLRNFCSIELNVNGSPETEADVATFCTSKTDAISMTSDDSVTGSEVSPLIKACMLSSNGFQNVGRCRERDSDDTCRQHNTSKSPFREMEPLLSPHHDKLMSLPVKTIDYPKTLIKEPVDKRHSCCKTKDSDIYCSPNENPEAENAEPSAMTISSHSFVNVHLESKTVICDNREPTDRHSENTCDEYKQSIGSTSSASHNHFDGLYEPIGSSGISSLQSPPSGIRCEENTSPTLDAVESKKGIDFLKYARKETDVGSALPDSGKGFSWENRHNNVLSGQSLQEAQEEGNSILHERRGRPEIPLDEEQRGHTHISDDSEVVFPYDLNLTMEDSDGITYTLKCDSSGNAPEIVSTVHEDYSGSSASSSDESDSEDTESDDSSIPRNRLQSVVVVPKNSTLPMEETSPCSSRSSQSYKHYSDRWEDGLETRRHAYEEEYESKGCSQTEKYFLHKGTERSAESCYSQFGRKADNHLPDIAHAQSDGVDSTSQTDSRSDHLGHLNPEDTLRAKTSRPQELPVYSDDFEDLPNKSRQQMIFSNRPDSSRLGKTELSFSSSCDISRMDGLHSSEELRNLGWDFSQQERPTTTYQQPDSSYGTCGTHKYQQSTEHYGGTHNYWQGNGYWDPRSAGRPPGTGLAYDRIQGQVPDSLTDDREEEEHWDQRSGSHFSSPSNKFFFHQKDKGSVQAPEISSNSIKDALVMNERKDFSKNFEKNDIKERGPPKKRRQELESDSESDGELQARKKVRVEMEQGESSVPQHSELMGPSCAMDDFRDPQRWKEFAKLGKMPCYFDLIEENVYLTERKKNKSHRDIKRMQCECTPLSKDERAQGEVACGEDCLNRLLMIECSSRCPNGDYCSNRRFQRKQHADVEVILTEKKGWGLRAAKDLPSNTFVLEYCGEVLDHKEFKARVKEYARNKNIHYYFMALKNDEIIDATQKGNCSRFMNHSCEPNCETQKWTVNGQLRVGFFTTKLVPSGSELTFDYQFQRYGKEAQKCFCGSANCRGYLGGENRVSIRAAGGKMKKERSRKKDSVDGELEALMENGEGLSDKNQVLSLSRLMVRIETLEQKLTCLKLIQNTHSQSCLKSFLERHGLSLLWIWMAELGDGRESNQKLQEEIIKTLEHLPIPTKNMLEESKVLPIIQRWSQTKTAVPQLSEGDGYSSENTSRAHTPLNTPDPSAKPSTEMDTDTPKKLIFRRLKIISENSMDSAVSDVTSELECKDGKEDLDQLETVTVEEDEELQSQQLLPQQLCESKVESEATIEVSKLPTSEPEADTETEPKDSNGTKLEETIAEETPSQDEEEGVSDVESERSQEPPDKTVDISDLATKLLDSWKDLKEVYRIPKKSQTEKESTVAERGRDAAAFRDQTAPKTPNRSRERDPDKQSQNKEKRKRRGSLSPPSSAYERGTKRPDDRYDTPTSKKKVRIKDRNKLSTEERRKLFEQEVAQREAQKQQQQMQNLGMTSPLPFDSLGYNASHHPFAGYPPGYPMQAYVDPSNPNAGKVLLPTPSMDPVCSPAPYDHAQPLVGHSTESLAAPPSVPVVPHVAASVEVSSSQYVAQNESVVHQDSNVPVMPVQAPGPVQGQNYNVWESNQQSVSVQQQYSPAQSQTTIYYQGQTCSTVYSVTSPYSQTTPPIVQSYAQPSLQYIQGQQIFTAHPQGVVVQPTAAVTSIVAPGQPQSLQPPEMVVTNNLLDLPPPSPPKPKTIVLPPNWKTARDPEGKIYYYHVITRQTQWDPPTWESPGDDASLEHEAEMDLGTPTYDENPMKTSKKPKTAEADTSSELAKKSKEVFRKEMSQFIVQCLNPYRKPDCKVGRITTTEDFKHLARKLTHGVMNKELKYCKNPEDLECNENVKHKTKEYIKKYMQKFGAVYKPKEDTELE
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Histone methyltransferase that specifically trimethylates 'Lys-36' of histone H3 (H3K36me3) using dimethylated 'Lys-36' (H3K36me2) as substrate. It is capable of trimethylating unmethylated H3K36 (H3K36me0) in vitro (By similarity). Represents the main enzyme generating H3K36me3, a specific tag for epigenetic transcriptional activation. Plays a role in chromatin structure modulation during elongation by coordinating recruitment of the FACT complex and by interacting with hyperphosphorylated POLR2A (By similarity). Acts as a key regulator of DNA mismatch repair in G1 and early S phase by generating H3K36me3, a mark required to recruit MSH6 subunit of the MutS alpha complex: early recruitment of the MutS alpha complex to chromatin to be replicated allows a quick identification of mismatch DNA to initiate the mismatch repair reaction (By similarity). Required for DNA double-strand break repair in response to DNA damage: acts by mediating formation of H3K36me3, promoting recruitment of RAD51 and DNA repair via homologous recombination (HR) (By similarity). Acts as a tumor suppressor (By similarity). H3K36me3 also plays an essential role in the maintenance of a heterochromatic state, by recruiting DNA methyltransferase DNMT3A (By similarity). H3K36me3 is also enhanced in intron-containing genes, suggesting that SETD2 recruitment is enhanced by splicing and that splicing is coupled to recruitment of elongating RNA polymerase (By similarity). Required during angiogenesis. Required for endoderm development by promoting embryonic stem cell differentiation toward endoderm: acts by mediating formation of H3K36me3 in distal promoter regions of FGFR3, leading to regulate transcription initiation of FGFR3. In addition to histones, also mediates methylation of other proteins, such as tubulins and STAT1. Trimethylates 'Lys-40' of alpha-tubulins such as TUBA1B (alpha-TubK40me3) alpha-TubK40me3 is required for normal mitosis and cytokinesis and may be a specific tag in cytoskeletal remodeling. Involved in interferon-alpha-induced antiviral defense by mediating both monomethylation of STAT1 at 'Lys-525' and catalyzing H3K36me3 on promoters of some interferon-stimulated genes (ISGs) to activate gene transcription (By similarity).
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E9Q5G3
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KIF23_MOUSE
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Kinesin-like protein KIF23
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MKSAKAKTVRKPVIKKGSQTNLKDPVGVYCRVRPLSFPDQECCVEVINSTTLQLHTPEGYRLNRNGDYKETQYSFKRVFGTHTTQKELFDVVANPLVDDLIHGKNGLLFTYGVTGSGKTYTMTGSPGSGGLLPRCLNMIFNSIGSFQAKRYVFKSNDRNSMEIQCEVDALLERQKREALPIPKTPSSKRQADPEFADMINVQEFCKAEEVDEDSVYGVFVSYIEIYNNYIYDLLEEVQFDPIKPKLPQSKTLREDKNHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFSIKLVQAPLDADGDNVLQEKEQITISQLSLVDLAGSERTNRTKAEGNRLREAGNINQSLMTLRTCMEVLRENQTYGTNKMVPYRDSKLTHLFKNYFDGEGKVRMIVCVNPKAEDYEESLQVMRFAEVTQEVEVARPVDKVICGLTPGRRYRNLPRGGPVGDEPLVPEVILQSFPPLPPCKLLDINDEETLPKLADTLEKRHHLRQLMTEDLNKKCLAFKALLKEFDNSLSNKENYVQEKLNEREKVISGQKLEIERLEKKNKTLEYKIEILEKTTTIYEEDKRNLQQELESQNQKLQRQFSDKRRLEARLQGMVTETSMKWQKECERRVAATQLEMQNKLWVKDEKLKQLKAIVTEPKPEKPERPSRERDREKIIPRSVSPSPLPLSSNNIAQISNGQQLMSQPQLHRRSNSCSSISVASCISEWEQKLSPFSTPVNVTSLARHRQQEPGQSKTCIVSDRRRGMCWTEGREMVPTFSSEIGVEEDHCRRNTPIPVRHRRSRSAGSRWVDHKPASNVQTETVMQPHVPHAITVSVANEKALAKCEKYMLTHQELASDGEIQTKVIKGDVYKTRGGGQSVQFTDIETLKQELPTGSRKRRSSTLAPAQPDGTESEWTDVETRCSVAVEMRAGSQLGPGYQHHAQPKRKKP
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Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Essential for cytokinesis in Rho-mediated signaling. Required for the localization of ECT2 to the central spindle. Plus-end-directed motor enzyme that moves antiparallel microtubules in vitro (By similarity).
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E9Q5G7
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OOG1_MOUSE
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Oogenesin-1
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MVICLHCPDQDDSLEEVTEECYSPPTLQNLAIQSLLRDEALAISALTDLPQSLFPVIFEEAFTDGYIGILKAMIPVWPFPYLSLGKQINNCNLETLKAMLEGLDILLAQKVQTSRCKLRVINWREDDLKIWAGSHEGEGLPDFRTEKQPIENSAGCEVKKELKVTTEVLRMKGRLDESTTYLLQWAQQRKDSIHLFCRKLLIEGLTKASVIEIFKTVHADCIQELILRCICIEELAFLNPYLKLMKSLFTLTLDHIIGTFSLGDSEKLDEETIFSLISQLPTLHCLQKLYVNDVPFIKGNLKEYLRCLKKPLETLCISNCDLSQSDLDCLPYCLNICELKHLHISDIYLCDLLLEPLGFLLERVGDTLKTLELDSCCIVDFQFSALLPALSQCSHLREVTFYDNDVSLPFLKQLLHHTALLSQLIYECYPAPLECYDDSGVILTHRLESFCPELLDILRAKRQLHSVSFQTTKCSKCGGCYIYDRHTQCCRFVELL
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May down-regulate the expression of spermatogenesis-associated genes in female germ cells allowing their normal differentiation into oocytes. May act as a Ras-mediated signaling protein in early embryogenesis.
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E9Q5K4
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CP2CN_MOUSE
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Cytochrome P450 2C44 (EC 1.14.14.-) (Arachidonic acid epoxygenase)
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MELLGLPTLALLVLVMSLSLLSVWTKMRTGGRLPPGPTPLPIIGNILQLDLKDIPASLSKLAKEYGPVYTLYFGSWPTVVLHGYDVVKEALLNQGDEFLGRGPLPIIEDSQKGHGIVFSEGERWKLLRRFSLMTLKNFGMGKRSLEERVQEEARCLVEELHKTEAQPFDPTFILACAPCNVICSILFNERFPYNDKTFLNLMDLLNKNFYQLNSIWIQMYNLWPTIMKYIPGKHREFSKRLGGVKNFILEKVKEHQESLDPANPRDYIDCFLSKIEEEKHNLKSDFNLENLAICGSNLFTAGTETTSTTLRFGLLLLVKHPEVQAKVHEELDRVIGRHQPPSMKDKMKLPYTDAVLHEIQRYITLLPSSLPHAVVQDTKFRHYVIPKGTAVFPFLSSILLDQKEFPNPEKFDPGHFLDKNGCFKKTDYFVPFSLGKRSCVGEGLARMELFLFFTTILQKFSLKALVEPKDLDIKPVTTGLFNLPPPYKLRLVPR
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A cytochrome P450 monooxygenase involved in polyunsaturated fatty acids (PUFAs) metabolism and signaling. Catalyzes preferentially the epoxidation of double bonds of PUFAs. Converts arachidonic acid (ARA, C20:4(n-6)) primarily to stereospecific products 8R,9S-epoxyeicosatrienoate (EET) and 11R,12S-EET. Plays a major role in the formation of EETs and hydroxy-EETs (HEETs) in kidney. Via EETs may inhibit the epithelial sodium channels (ENaCs) in nephron segments, preventing excessive sodium absorption during high dietary salt intake. Participates in the formation of anti-inflammatory hydroxyepoxyeicosatrienoic acids (HEETs) by converting 20-hydroxyeicosatetraenoic acid (20-HETE) to 20,8,9-HEET, an activator of PPARA (By similarity). Metabolizes eicosapentaenoic acid (EPA, C20:5(n-3)) to epoxyeicosatetraenoic acid (EETeTr) regioisomers, 8,9-, 11,12-, 14,15-, and 17,18- EETeTr, preferentially producing 17R,18S enantiomer (By similarity). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR NADPH-ferrihemoprotein reductase).
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E9Q5K9
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YTDC1_MOUSE
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YTH domain-containing protein 1
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MAADSREEKDGELNVLDDILTEVPEQDDELYNPESEQDKNEKKGSKRKSERMESTDTKRQKPSIHSRQLISKPLSSSVSNNKRIVSTKGKSVTEYKNEEYQRSERNKRLDADRKIRLSSSSSREPYKSQPEKTCLRKRDSERRAKSPTPDGSERIGLEVDRRASRSSQSSKEEVNSEDYGSDHETGSSGSSEQGNNTENEEEGGEEDVEEDEEVDEDAEDDEEVDEDAEEEEEEDEEEEEDEDEDEEEEEYEQDERDQKEEGNDYDTRSEASDSGSESVSFTDGSVRSGSGTDGSDEKKKERKRARGISPIVFDRSGSSASESYAGSEKKHEKLSSSVRAVRKDQTSKLKYVLQDARFFLIKSNNHENVSLAKAKGVWSTLPVNEKKLNLAFRSARSVILIFSVRESGKFQGFARLSSESHHGGSPIHWVLPAGMSAKMLGGVFKIDWICRRELPFTKSAHLTNPWNEHKPVKIGRDGQEIELECGTQLCLLFPPDESIDLYQLIHKMRHKRRMHSQPRSRGRPSRREPVRDVGRRRPEDYDIHNSRKKPRIDYPPEFHQRPGYVKDPRYQEVDSFTNLIPNRRFSGVRRDVFLNGSYNDYVREFHNMGPPPPWQGMPPYPGIEQPPHHPYYQHHAPPPQAHPPYSGHHPVPHEARYRDKRVHDYDMRVDDFLRRTQAVVSGRRSRPRERDRERERDRPRDNRRDRERDRGRDRERERERICDRDRDRGERGRYRR
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Regulator of alternative splicing that specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs. M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in the efficiency of mRNA splicing, processing and stability. Acts as a key regulator of exon-inclusion or exon-skipping during alternative splicing via interaction with mRNA splicing factors SRSF3 and SRSF10 (By similarity). Specifically binds m6A-containing mRNAs and promotes recruitment of SRSF3 to its mRNA-binding elements adjacent to m6A sites, leading to exon-inclusion during alternative splicing (By similarity). In contrast, interaction with SRSF3 prevents interaction with SRSF10, a splicing factor that promotes exon skipping: this prevents SRSF10 from binding to its mRNA-binding sites close to m6A-containing regions, leading to inhibit exon skipping during alternative splicing (By similarity). May also regulate alternative splice site selection (By similarity). Also involved in nuclear export of m6A-containing mRNAs via interaction with SRSF3: interaction with SRSF3 facilitates m6A-containing mRNA-binding to both SRSF3 and NXF1, promoting mRNA nuclear export (By similarity). Involved in S-adenosyl-L-methionine homeostasis by regulating expression of MAT2A transcripts, probably by binding m6A-containing MAT2A mRNAs. Also recognizes and binds m6A on other RNA molecules (By similarity). Involved in random X inactivation mediated by Xist RNA: recognizes and binds m6A-containing Xist and promotes transcription repression activity of Xist (By similarity). Also recognizes and binds m6A-containing single-stranded DNA (By similarity). Involved in germline development: required for spermatogonial development in males and oocyte growth and maturation in females, probably via its role in alternative splicing.
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E9Q5R7
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NAL12_MOUSE
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NACHT, LRR and PYD domains-containing protein 12 (Monarch-1) (PYRIN-containing APAF1-like protein 7) (PYPAF7)
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MLPSTARDGLYRLSTYLEELEAGELKKFKLFLGIAEDLSQDKIPWGRMEKAGPLEMAQLMVAHMGTREAWLLALSTFQRIHRKDLWERGQGEDLVRVTPNNGLCLFESQSACPLDVSPNAPRKDLQTTYKDYVRRKFQLMEDRNARLGECVNLSNRYTRLLLVKEHSNPIWTQQKFVDVEWERSRTRRHQTSPIQMETLFEPDEERPEPPHTVVLQGAAGMGKSMLAHKVMLDWADGRLFQGRFDYVFYISCRELNRSHTQCSVQDLISSCWPERGISLEDLMQAPDRLLFIIDGFDKLHPSFHDAQGPWCLCWEEKQPTEVLLGSLIRRLLLPQVSLLITTRPCALEKLHGLLEHPRHVEILGFSEEARKEYFYRYFHNTGQASRVLSFLMDYEPLFTMCFVPMVSWVVCTCLKQQLESGELLRQTPRTTTAVYMFYLLSLMQPKPGTPTFKVPANQRGLVSLAAEGLWNQKILFDEQDLGKHGLDGADVSTFLNVNIFQKGIKCEKFYSFIHLSFQEFFAAMYCALNGREAVRRALAEYGFSERNFLALTVHFLFGLLNEEMRCYLERNLGWSISPQVKEEVLAWIQNKAGSEGSTLQHGSLELLSCLYEVQEEDFIQQALSHFQVVVVRSISTKMEHMVCSFCARYCRSTEVLHLHGSAYSTGMEDDPPEPSGVQTQSTYLQERNMLPDVYSAYLSAAVCTNSNLIELALYRNALGSQGVRLLCQGLRHASCKLQNLRLKRCQISGSACQDLAAAVIANRNLIRLDLSDNSIGVPGLELLCEGLQHPRCRLQMIQLRKCLLEAAAGRSLASVLSNNSYLVELDLTGNPLEDSGLKLLCQGLRHPVCRLRTLWLKICHLGQASCEDLASTLKMNQSLLELDLGLNDLGDSGVLLLCEGLSHPDCKLQTLRLGICRLGSVACVGIASVLQVNTCLQELDLSFNDLGDRGLQLLGEGLRHQTCRLQKLWLDNCGLTSKACEDLSSILGISQTLHELYLTNNALGDTGVCLLCKRLRHPGCKLRVLWLFGMDLNKKTHRRMAALRVTKPYLDIGC
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Plays an essential role as an potent mitigator of inflammation. Primarily expressed in dendritic cells and macrophages, inhibits both canonical and non-canonical NF-kappa-B and ERK activation pathways. Functions as a negative regulator of NOD2 by targeting it to degradation via the proteasome pathway. In turn, promotes bacterial tolerance. Inhibits also the RIGI-mediated immune signaling against RNA viruses by reducing the E3 ubiquitin ligase TRIM25-mediated 'Lys-63'-linked RIGI activation but enhancing the E3 ubiquitin ligase RNF125-mediated 'Lys-48'-linked RIGI degradation (By similarity). Acts also as a negative regulator of inflammatory response to mitigate obesity and obesity-associated diseases in adipose tissue.
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E9Q612
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PTPRO_MOUSE
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Receptor-type tyrosine-protein phosphatase O (R-PTP-O) (EC 3.1.3.48) (Glomerular epithelial protein 1) (Protein tyrosine phosphatase U2) (PTP-U2) (PTPase U2)
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MGHLPRGTLGGRRLLPLLGLFVLLKIVTTFHVAVQDDNNIVVSLEASDIVSPASVYVVRVAGESKNYFFEFEEFNSTLPPPVVFKATYHGLYYIITLVVVNGNVVTKPSRSITVLTKPLPVTSVSIYDYKPSPETGVLFEIHYPEKYNVFSRVNISYWEGRDFRTMLYKDFFKGKTVFNHWLPGLCYSNITFQLVSEATFNKSTLVEYSGVSHEPKQHRTAPYPPRNISVRFVNLNKNNWEEPSGSFPEDSFIKPPQDSIGRDRRFHFPEETPETPPSNVSSGSPPSNVSSAWPDPNSTDYESTSQPFWWDSASAAPENEEDFVSALPADYDTETTLDRTEKPTADPFSAFPVQMTLSWLPPKPPTAFDGFNILIEREENFTDYLTVDEEAHEFVAELKEPGKYKLSVTTFSSSGACETRKSQSAKSLSFYISPTGEWIEELTEKPQHVSVHVLSSTTALMSWTSSQENYNSTIVSVVSLTCQKQKESQRLEKQYCTQVNSSKPVIENLVPGAQYQVVMYLRKGPLIGPPSDPVTFAIVPTGIKDLMLYPLGPTAVVLSWTRPILGVFRKYVVEMFYFNPTTMTSEWTTYYEIAATVSLTASVRIASLLPAWYYNFRVTMVTWGDPELSCCDSSTISFITAPVAPEITSVEYFNSLLYISWTYGDATTDLSHSRMLHWMVVAEGRKKIKKSVTRNVMTAILSLPPGDIYNLSVTACTERGSNTSLPRLVKLEPAPPKSLFAVNKTQTSVTLLWVEEGVADFFEVFCQQLGSGHNGKLQEPVAVSSHVVTISSLLPATAYNCSVTSFSHDTPSVPTFIAVSTMVTEVNPNVVVISVLAILSTLLIGLLLVTLVILRKKHLQMARECGAGTFVNFASLEREGKLPYSWRRSVFALLTLLPSCLWTDYLLAFYINPWSKNGLKKRKLTNPVQLDDFDSYIKDMAKDSDYKFSLQFEELKLIGLDIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSHIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMVSEEEEEDWASRHFRINYADEAQDVMHFNYTAWPDHGVPPANAAESILQFVFTVRQQAAKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCVQLMWLRKKQQFCISDVIYENVSKS
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Possesses tyrosine phosphatase activity. Plays a role in regulating the glomerular pressure/filtration rate relationship through an effect on podocyte structure and function.
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E9Q634
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MYO1E_MOUSE
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Unconventional myosin-Ie (Unconventional myosin 1E)
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MGSKGAYRYHWQSHNVKHSGVDDMVLLSKITESSIVENLKKRYMDDYIFTYIGSVLISVNPFKQMPYFGEKEVEMYQGAAQYENPPHIYALADSMYRNMIIDRENQCVIISGESGAGKTVAAKYIMSYVSRVSGGGPKVQHVKDIILQSNPLLEAFGNAKTVRNNNSSRFGKYFEIQFSPGGEPDGGKISNFLLEKSRVVMRNPGERSFHIFYQLIEGASPEQKQSLGITSMDYYYYLSLSGSYKVDDIDDKRDFQETLHAMNVIGIFSEEQTLVLQIVAGILHLGNISFKEVGNYAAVESEEFLAFPAYLLGINQDRLKEKLTSRQMDSKWGGKSESIHVTLNVEQACYTRDALAKALHARVFDFLVDSINKAMEKDHEEYNIGVLDIYGFEIFQKNGFEQFCINFVNEKLQQIFIELTLKAEQEEYVQEGIRWTPIEYFNNKIVCDLIESKVNPPGIMSILDDVCATMHAVGEGADQTLLQKLQMQIGSHEHFNSWNQGFIIHHYAGKVSYDMDGFCERNRDVLFMDLIELMQSSELPFIKSLFPENLQADKKGRPTTAGSKIKKQANDLVSTLMKCTPHYIRCIKPNETKKPKDWEESRVKHQVEYLGLKENIRVRRAGYAYRRVFQKFLQRYAILTKATWPVWRGDEKQGVLHLLQSVNMDSDQFQLGRSKVFIKAPESLFLLEEMRERKYDGYARVIQKTWRKFVARKKYVQMREEASDLLLNKKERRRNSINRNFIGDYIGMEERPELQQFVGKREKIDFADTVTKYDRRFKGVKRDLLLTPKCLYLIGREKVKQGPDKGVVKEVLKRRIEVERILSVSLSTMQDDIFILHEQEYDSLLESVFKTEFLSLLAKRYEEKTQKQLPLKFSNTLELKLKKENWGPWSAGGSRQVQFHQGFGDLAILKPSNKVLQVSIGPGLPKNSRPTRRNTVTSRGYPGGTKNNYPMRAAPAPPGCHQNGVIRNQFVPPPHAFGNQRSNQKSLYTSMARPPLPRQQSTGSDRLSQTPESLDFLKVPDQGVAGVRRQTSSRPPPAGGRPKPQPKPKPQVPQCKALYAYDAQDTDELSFNANDIIDIIKEDPSGWWTGRLRGKQGLFPNNYVTKI
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Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which are then moved relative to actin filaments. Binds to membranes containing anionic phospholipids via its tail domain (By similarity). Involved in clathrin-mediated endocytosis and intracellular movement of clathrin-coated ve (By similarity)sicles. Required for normal morphology of the glomerular basement membrane, normal development of foot processes by kidney podocytes and normal kidney function. In dendritic cells, may control the movement of class II-containing cytoplasmic vesicles along the actin cytoskeleton by connecting them with the actin network via ARL14EP and ARL14 (By similarity). {ECO:0000250, ECO:0000269|PubMed:19005011}.
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E9Q649
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GCNT4_MOUSE
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Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 4 (EC 2.4.1.102) (Core 2-branching enzyme 3) (Core2-GlcNAc-transferase 3) (C2GnT3)
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MKIFRCCFKYTLQQKLFILLLTLWLFSLLKLLNVGRLLFPQRDIYLVEYSLSTSPFVRNRFPESGDAARDNVNCSGVYEHEPLEIGKSLEIRRRSIIDLEDGDVVAMTSDCDVYQTLRQYHEKLVSREEEDFPIAYSLVVHKDAIMVERLIRAIYNQHNLYCIHYDLKSPDTFKAAMNNLAKCFPNIFIASKLETVEYAHISRLQADWNCLSDLLKSSVQWKYVINLCGQDFPLKSNFELVTELKSLQGRNMLETVRPPSAKTERFTYHHELRQVPYDYMKLPVKTNVSKGAPPHNIQVFVGSAYFVLSRAFVKYIFNSSLVEDFFAWSKDTYSPDEHFWATLIRIPGIPGGISSSSQDVSDLQSKTRLVKWFYYEGFLYPNCTGSHLRSVCIYGAAELRWLLNEGHWFANKFDSKVDPILMKCLAEKLEEQQRKLIALSSEKFMTEGTRQSHTL
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Glycosyltransferase that mediates core 2 O-glycan branching, an important step in mucin-type biosynthesis. Does not have core 4 O-glycan or I-branching enzyme activity.
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E9Q6W4
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ZN296_MOUSE
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Zinc finger protein 296 (Hepatocellular carcinoma-associated antigen MHCA108)
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MSRRKAGRVPRRVDPDTDTDIEMPDLVMDVKPDLDLRSLAQGPWIARDMPISDVKRQLQTASRPLGAPSTCAPRMPLSSKSSDRQPWTDKHPDLLTCGRCGKIFPLGAIIAFMDHKKQGCQLLQVSDPISESKELKALSCLQCGRQYTSPWKLLCHAQWDHGLCIYQTQHLDTPEAPLLGLAEVAAAMSAVAVVAPVESKPPPVSSAARRSPTCDVCKKTLSSFSNLKVHMRSHTGERPYSCDQCSYACAQSSKLNRHKKTHRQLAPGSPSTSASSRGVSPAAPPEPAAYAAAPASTLPSQTVEKAGAAATAGVQEPGAPGSGAQGGPGFVGWGAPAKVERTDPVKIEKTAPRKSHGPGGKCEFCGKSFTNSSNLTVHRRSHTGERPYTCDQCPYACAQSSKLNRHRRTHGLGTGKTVKCPHCLVPFGLQATLDKHLRQKHPEMA
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May be a transcriptional corepressor with KLF4.
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E9Q784
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ZC3HD_MOUSE
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Zinc finger CCCH domain-containing protein 13
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MSKIRRKVTVENTKTISESTSRRPSVFERLGPSTGSTTETQCRNWLKTGSCLYGNTCRFIHGPSPRGKGYSSNYRRSPERPTGDLRERMKNKRQDVDSESQKRNTEEPSSPVRKESSRGRHRDKEDIKIVKERTPESEEENVEWETNRDDSDNGDINYDYVHELSLEMKRQKIQRELMKLEQENMDKREEIIIQKEVSPEVVRSKLSPSPSLRKSSKSPKRKSSPKASSAGKKERKAAVVASPLLDQQRNSKGNQSKKKGPRTPSPPPPILEDIILGKKYKEKYKVKDRIEEKPRDGKDRGRDFEKQREKRDKPRSSSPGQHHSPLSSRHHSSSSQSGSSIQRHSPSPRRKRTPSPSYQRTLTPSLRRSASPYPTHCLSSPQRKQSPPRHRSPMREKGRHDHERTSQSHDRRHERREETRGKRDREKDTREERESEHDHRDDREPRDSRDRRDTRDRRELRDSRDMRDSREMRDYSRDAKESRDPRDSRSARDVHDYRDREARDAHARDVRDARDARDARDARDIRDVRDVRDVRDVRDVRDVRDVRDVRDVRDARDVRDVRDARDVRDVRDVRDGHRKEDVYQEEARSYGRNHLREESSRVELRNDSRNESRSEIRNDRMGRSRGRGPELPEKGSRGTRGSQMDSHSSGSNYHDSWETRSSYPERDRYPERDTRDPARDSSFERRHGERDRRDNRERDQRPSSPIRHQGRSEELERDERREERRIDRVDERRDDRVRDRDRDREREREREREREREREKERERELERERAREREREREKERERERERERDQRDRDHDREREREREREREKEREREREERERERERERERERERERERERERERERERERAREREKERERQREWEDKDKGRDDRREKREDIHVREDRIPRDSHEERKSKKRYRNEGSPSPRQSPKRRREHSPDSDTYHSGDDKNEKHRLLSQVVRPQESRSLSPSHLTEDRQGRWKEEDRKSERKESSRRYEEQELKEKLSCGDRQREQAESVDSSRVRAQDLLSHRQAEDRDRDGSDRAHDEKKKAKAPKKPVKKKKEEDVGVERGNLETHEDSQVFSPKKGQKKKNIEKKRKRSKGDSDVSDEEAAPQNKKKRGPRTPPLAIKEELADISTDKDGVLEDPLKKENTAFSDWSDEDVPDRTEGLEAEHTAATATPGSTPSPLSSLLPPPPPVAAASTAATALASSAVSATTSATSSSSAATSNTNGSEDSHRKCHRARGEKVEVSHVTLEDTPHRKLVDQKRSSSLGSNRSHRSHTSGRLRSPSNDSAHRSGDDQGSRKRVLHSGSRDREKTKSLEITGERKSRIDQLKRGEPSRSTSSDRQDSRSHSSRRSSPESDRQVHSRSGSFDSRDRLQERDRYEHDRERERDRRDPRQREWDREAEKEWPRTRDRDRLRERDRDRDRRRDLDRERERLISDPMERDRERERTFETSQLESGKRSEVKLESEHERDLEGSSRDSVALDKERMDRDLGSVQGFEDVSKAERTESLEGDDESKLDDAHSLGSGAGEGYEPISDDELDEILAGDAEKREDQQEEEKMPDPLDVIDVDWSGLMPKHPKEPREPGAALLKFTPGAVLLRVGISKKLAGSELFTKVKETCQQLVEKPKDADSLFEHELGALNMAALLRKEERASLLSDLGPCCKALCFRRDSAIRKQLVKNEKGTVKQAYTNTPMVDNELLRLSLRLFKKKATCHAPGQEKTEDGKLGPCSIQQELCVS
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Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing. Acts as a key regulator of m6A methylation by promoting m6A methylation of mRNAs at the 3'-UTR. Controls embryonic stem cells (ESCs) pluripotency via its role in m6A methylation. In the WMM complex, anchors component of the MACOM subcomplex in the nucleus. Also required for bridging WTAP to the RNA-binding component RBM15 (RBM15 or RBM15B).
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E9Q7D5
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ARHG5_MOUSE
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Rho guanine nucleotide exchange factor 5
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MEAEEPEYGVSTEVPDIEELKTIPEGIMRSSQIPALDPEAQEDRDPSYKWTDGHRPVMNQSKVLRDMGDHTPNSMAIFFKKESSDMETSQEILLAEACNTPDQQEAVIQSLKDRLSRTIAAPELLACAVQEEWLDIPSKLDNRVGAELQSELMSLTLAVSKEKEEEETSPDTSIPRGSWPPCKTHPGETEQTQGSGSELLRQGKQLQLEATQENQGQEGFLQSQEAQGLEEQEGQEVEIQEEGTLNEGICFGGLLGEQEEVEEGFNGNEEEQKQGQIQSYMLLGGQWENEGLSGELEGLNYSERGQENRERRVWVLRDSEEEGQDQESREVEERRVATQYTENQRLVEKSEIVKRKQRDHDQTGKVMPVRDQKEVVDSGDRVQGNGDSGGQTAVEGSRPGEDSKPSLPVASVDPEVLSPGTLFPGISSSVADIPQIQKEPVCEELSPQAPALEPTEWSHQPISPPASFAPEESLDNRTHNSQQEEFRLRKGIEVVSASTSVAPSGTRDSPPFSPPNVFSSTATLSPVSSSVILPEETPTASASADTPHHCGPCETPPLPAKSSRYPCATSDTANPHSPLSSYTGVTQHLRSNSFPGSHRTEQTPDSLGMSLSFSHLELPQRPPKPAIYGSLTPRRNRRSRDGIVFSDSSTALFALKQDSEEFTSNPERPSSPHGSPTWGSPQNSAFAIGSPANVSSPPTVSMDMTIREALLPIPPEKRHSYSHIVERDGLLHEVASTLKRHSHPPPLTLSSGLHRSSKGSFSLVPDSTVARQHRPLPSTPESPNHTQTSIPSRLRYNKPLPPTPDMPEFYHPSISSSYISRMYRPLPPVPIIDPSSEPPPLPPKSRGRSKSIQGGVIHSGGQAKPRPNNQDWTASTLSVGRTSWPPATGRSTESLPLTSRCNNEVSPGLAFSNMTNLLSPSSPTTPWIPDLQRPTTKDESGLTEESEPPVRGSFRRSAPQEEFNNTRRSALGSRKNSEKPLHHQLEKASSWPHRRDPARTSESSSEQVVLGQVPNKQKGWNRQGLRRPSILPESSSDLRNPAAGRLPGSSDSVVFREKKPKEGMGGFSRRCSKLISSQLLYQEYSDVVLNKEIQSQQRLDSLAEPHGLSSPRHRRKALVSSDSYLQRLSMASSGSLWQEIPVVRNSTVLLSMTHEDQKLQEAKFELIVSEASYLRSLNIAVDHFQHSAQLRGTLSNQDHQWLFSRLQDVRDVSTTFLSDLEENFENNIFSFQVCDVVLNHAADFHRVYLPYVTNQTYQERTFQSLMNSNSSFREVLEKLESDPICQRLSLKSFLILPFQRITRLKLLLQNILKRTQPGSSEEAEATKAHHALEKLIRDCNSNVQRMRRTEELIYLSQKIEFECKIFPLISQSRWLVKSGELTALEFSVSPGLRRKLTTRPVHLHLFNDCLLLSRPREGSRFLVFDHAPFSSIRGEKCEMKLHGPHKNLFRLFLLHNAQGTQVEFLFRTETQSEKLRWISALAMPREELDLLECYDSPQVQCLRAYKPRENDELALEKADVVMVTQQSSDGWLEGVRLSDGEQGWFPVQQVEFISNPEVRAQNLKEAHRVKTAKLQLVEQQV
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Guanine nucleotide exchange factor which activates Rho GTPases. Strongly activates RHOA. Also strongly activates RHOB, weakly activates RHOC and RHOG and shows no effect on RHOD, RHOV, RHOQ or RAC1. Involved in regulation of cell shape and actin cytoskeletal organization. Plays a role in actin organization by generating a loss of actin stress fibers and the formation of membrane ruffles and filopodia (By similarity). Required for SRC-induced podosome formation. Involved in positive regulation of immature dendritic cell migration.
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E9Q7E2
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ARID2_MOUSE
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AT-rich interactive domain-containing protein 2 (ARID domain-containing protein 2) (BRG1-associated factor 200) (BAF200) (Zinc finger protein with activation potential) (Zipzap/p200)
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MANSTGKAPPDERRKGLAFLDELRQFHHSRGSPFKKIPAVGGKELDLHGLYTRVTTLGGFAKVSEKNQWGEIVEEFNFPRSCSNAAFALKQYYLRYLEKYEKVHHFGEDDDEVPPGNPKPQLPIGAIPSSYNYQQHSVSDYLRQSYGLSMDFNSPNDYNKLVLSLLSGLPNEVDFAINVCTLLSNESKHVMQLEKDPKIITLLLANAGVFDDTLGSFSSVFGEEWREKTDRDFVKFWKDIVDDNEVRDLISDRNKAHEDTPGEWIWESLFHPPRKLGINDIEGQRVLQIAVILRNLSFEESNVKLLAANRTCLRFLLLSAHSHFISLRQLGLDTLGNIAAELLLDPVDFRTTHLMFHTVTKCLMSRDRFLKMRGMEILGNLCKAEDNGVLICEYVDQDSYREIICHLTLPDVLLVTSTLEVLYMLTEMGDVACTKIAKVEKSIDVLVCLVSMDAQMFGPDALAAVKLIEHPSSSHQVLSEIRPQAIEQVQTQTHIASGPASRAVVAQHAAPPPGIVEIDSEKFACQWLNAHFEVNPDCSVSRAEMYSEYLSTCSKLARGGILTSTGFYKCLRTVFPNHTVKRVEDSTSSGQAHIHVIGVKRRALPLPIQMYYQQQPISTPVVRVDAVADLSPTPSPAGIPHGPQAAGNHFQRTPVTNQSSNLTATQMSFPVQGIHTVAQTVSRIPPNPSVHTHQQQNSPVTVIQNKAPIPCEVVKATVIQNSVPQTAVPVSISVGGAPAQNSVGQNHSAGPQPVTVVNSQTLLHHPSVMPQPSPLHTVVPGQVPSGTPVTVIQQTVPQSRMFGRVQSIPACTSTVSQGQQLITTSPQPMHTSSQQTAAGSQPQDTVIIAPPQYVTTSASNIVSATSVQNFQVATGQVVTIAGVPSPQPSRVGFQNIAPKPLPSQQVSPSVVQQPIQQPQQPAQQSVVIVSQPAQQGQAYAPAIHQIVLANPAALPAGQTVQLTGQPNITPSSSPSPVPPTNNQVPTAMSSSSTLQSQGPPPTVSQMLSVKRQQQQQHSPAAPAQQVQVQVQQPQQVQVQVQPQQPSAGVGQPAPNESSLIKQLLLPKRGPSTPGGKLILPAPQIPPPNNARAPSPQVVYQVANNQAAGFGVQGQTPAQQLLVGQQNVQLVQSAMPPAGGVQTVPISNLQILPGPLISNSPATIFQGTSGNQVTITVVPNTSFATATVSQGNAAQLIAPAGLSMSGAQASAGLQVQTLPAGQSACTTAPLPFKGDKIICQKEEEAKEATGLHVHERKIEVMENPSCRRGTTNTSNGDTSESELQVGSLLNGRKYSDSSLPPSNSGKLQSETSQCSLISNGPSLELGENGAPGKQNSEPVDMQDVKGDLKKALVNGICDFDKGDGSHLSKNIPNHKTSNHVGNGEISPVEPQGTSGATQQDTAKGDQLERVSNGPVLTLGGSPSTSSMQEAPSVATPPLSGTDLPNGPLASSLNSDVPQQRPSVVVSPHSTAPVIQGHQVIAVPHSGPRVTPSALSSDARSTNGTAECKTVKRPAEDNDRDTVPGIPNKVGVRIVTISDPNNAGCSATMVAVPAGADPSTVAKVAIESAAQQKQQHPPTYMQSVAPQNTPMPPSPAVQVQGQPSSSQPSPVSASSQHADPVRKPGQNFMCLWQSCKKWFQTPSQVFYHAATEHGGKDVYPGQCLWEGCEPFQRQRFSFITHLQDKHCSKDALLAGLKQDEPGQVANQKSSTKQPTVGGTGSAPRAQKAIASHPSAALMALRRGSRNLVFRDFTDEKEGPITKHIRLTAALILKNIGKYSECGRRLLKRHENNLSVLAISNMEASSTLAKCLYELNFTVQSKEQEKDSEML
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Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Required for the stability of the SWI/SNF chromatin remodeling complex SWI/SNF-B (PBAF). May be involved in targeting the complex to different genes. May be involved in regulating transcriptional activation of cardiac genes.
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E9Q7F2
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RN169_MOUSE
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E3 ubiquitin-protein ligase RNF169 (EC 2.3.2.27) (RING finger protein 169) (RING-type E3 ubiquitin transferase RNF169)
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MAAAGPSTRASSAAAAAALSRRGRRGRCDEMAAAKAGAPGPASSPALLVLRSAPRPEESGCTGCLETPGEVAALPCSHSRCRGCASRAAGPGCRRCRPRGSGWARRRARDDGQAAAELMGERARRGQPEPCRPRRDGGAAASGPRPEPEPLAEPEFIFRTPIKLSKPGELSEEYGCLRKLRGEKLQEEKDCDDQIHKLLQEDSEMGKRKADEQKKRDEAVVLKTSLEQCPARLSDSENEEPSRGQMMQTHRSAFVSKNSSCSLAFLAGKLNTKVQRSQSCSDTVQDRVRSRLRTAPPNRAKITTITPGSTPIIGVLLSTQNNRCLSAPDLTIEKRLPFGSLSSLASLHKPERSISPESNDSISEELNHFKPIVCSPCTPPKRLPDGRVLSPLIIKSTPRNLTRSLQKQTSYEASPRILKKWEQIFQERQIKKTLSKATLTSLAPEAGEEFPGSDTIHSSKERPSLAFNTRLSRVQVLSECAGPTSTALECFPSVNQTKVEQDCVRKRSREFSLETCHSSEHGGASSGPSLEREQCEESGSTVDATLVKTCISTVMKTAAVNSLLPKNDVLGGVLKTKQQLKTLNHFDLGNGILVNSLGEEPIPSLRRGRKRRCKTKHLEQNGVKKLRPPSSDMDLAPKDPGLLEVGRKLQQEEEDQQLALQSHRMFDSERRTMSRRKGSVDQYLLRSSSLAGAK
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Probable E3 ubiquitin-protein ligase that acts as a regulator of double-strand breaks (DSBs) repair following DNA damage. Functions in a non-canonical fashion to harness RNF168-mediated protein recruitment to DSB-containing chromatin, thereby contributing to regulation of DSB repair pathway utilization. Once recruited to DSB repair sites by recognizing and binding ubiquitin catalyzed by RNF168, competes with TP53BP1 and BRCA1 for association with RNF168-modified chromatin, thereby favouring homologous recombination repair (HRR) and single-strand annealing (SSA) instead of non-homologous end joining (NHEJ) mediated by TP53BP1. E3 ubiquitin-protein ligase activity is not required for regulation of DSBs repair.
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E9Q7G0
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NUMA1_MOUSE
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Nuclear mitotic apparatus protein 1 (Nuclear mitotic apparatus protein) (NuMA protein)
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MTLHATRAATLLSWVNSLHVADPVETVLQLQDCSIFIKIINTIHDTKEGQQILQQPLPERLDFVCSFLQKNRKHPSSTQCLVSVQKVIEGSEMELAKMIMLFLYQSTMSSRNLRDWEQFEYGVQAELAVILKFMLDHEESLNLTEDLESFLEKVPYTHASTLSEELSPPSHQTKRKIRFLEIQRIASSSSENNFLSGSPSSPMGDILQTPQFQMRRLKKQLADERSNRDDLELELSESLKLLTEKDAQIAMMQQRIDHLALLNEKQAASSQEPSELEELRGKNESLTVRLHETLKQCQNLKTEKSQMDRKISQLSEENGDLSFKVREFANHLQQLQGAFNDLIEEHSKASQEWAEKQARLENELSTALQDKKCLEEKNEILQGKLSQLEDQATRLQESPAPEKGEVLGDALQLDTLKQEAAKLATDNTQLQTRVETLECERGKQEAQLLAERSRFEDEKQQLASLIADLQSSVSNLSQAKEELEQASQAQGAQLTAQLTSMTGLNATLQQRDQELASLKEQAKKEQAQMLQTMQEQEQAAQGLRQQVEQLSSSLKLKEQQLEEAAKEQEATRQDHAQQLAIVAEAREASLRERDTARQQLETVEKEKDAKLESLQQQLQAANDARDNAQTSVTQAQQEKAELSQKIGELHACIEASHQEQRQVQARVTELEAQLKAEQQKTTEREKVVQEKAQLQEQLRALEESLKITKGSLEEEKRRAADALKEQQCRATEMEAESRSLMEQREREQKELEQEKAGRKGLEARIQQLEEAHQAETEALRHELAEATASQHRAESECERLIREVESRQKRFEARQQEEARYGAMFQEQLMALKGEKTGQEVQEEAVEIHSEGQPGQQQSQLAQLHASLAKAIQQVQEKEVRAQKLVDDLSALQEKMAATNKEVACLKTLVLKAGEQQETASLELLKEPPRAANRASDQLGEQQGRPFSSTHAAVKAMEREAEQMGGELERLRAALIKSQGQQQEERGQQEREVARLTQERGQAQADLAQEKAAKAELEMRLQNTLNEQRVEFAALQEALAHALTEKEGTDQELAKLRGQEAAQRTELKELQQTLEQLKIQLVKKEKEHPAGGASGEDASGPGTQSETAGKTDAPGPELQALRAEISKLEQQCQQQQQQVEGLTHSLKSERACRAEQDKALETLQGQLEEKARELGHNQAASASAQRELQALRAKAQDHSKAEEEWKAQVARGQQEAERKSSLISSLEEEVSILNRQVLEKEGESKELKRLVVAESEKSQKLEERLRLLQVETASNSARAAERSSALREEVQSLREEVEKQRVVSENSRQELASQAERAEELGQELKAWQEKFFQKEQALSALQLEHTSTQALVSELLPAKHLCQQLQAEQAAAEKRFREELEQSKQAAGGLQAELMRAQRELGELGSLRQKIVEQERAAQQLRAEKASYAEQLSMLKKAHGLLAEENRGLGERANLGRQFLEVELDQAREKYVQELAAVRTDAETHLAEMRQEAQSTSRELEVMTAKYEGAKVKVLEERQRFQEERQKLTAQVEELSKKLTEHDQASKVQQQKLKAFQAQRGESQQEVQRLQTQLNELQAQLSQKEQAAEHYKLQMEKAKTHYDAKKQQNQKLQEQLQDLEELQKENKELRSEAERLGRELQQAGLKTKEAEQTCRHLTAQVRSLEAQVAHADQQLRDLGKFQVATDALKSREPQVKPQLDLSIDSLDLSLEEGTPCSVASKLPRTQPDGTSVPGEPASPISQRLPPKVESLESLYFTPTPARGQAPLETSLDSLGDAFPDSGRKTRSARRRTTQIINITMTKKLELEEPDSANSSFYSTQSAPASQANLRATSSTQSLARLGSPDDGNSALLSLPGYRPTTRSSARRSQARMSSGAPQGRNSFYMGTCQDEPEQLDDWNRIAELQQRNRVCPPHLKTCYPLESRPTLSLATITDEEMKTGDPRETLRRASMQPAQIAEGVGITTRQQRKRVSSETHQGPGTPESKKATSCFPRPMTPRDRHEGRKQSSTADTQKKAAPVLKQADRRQSMAFSILNTPKKLGNSLLRRGASKKTPAKVSPNPRSGTRRSPRIATTTTGTATVATTPRAKGKVKH
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Microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignement and the segregation of chromosomes during mitotic cell division. Functions to tether the minus ends of MTs at the spindle poles, which is critical for the establishment and maintenance of the spindle poles. Plays a role in the establishment of the mitotic spindle orientation during metaphase and elongation during anaphase in a dynein-dynactin-dependent manner. In metaphase, part of a ternary complex composed of GPSM2 and G(i) alpha proteins, that regulates the recruitment and anchorage of the dynein-dynactin complex in the mitotic cell cortex regions situated above the two spindle poles, and hence regulates the correct oritentation of the mitotic spindle. During anaphase, mediates the recruitment and accumulation of the dynein-dynactin complex at the cell membrane of the polar cortical region through direct association with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), and hence participates in the regulation of the spindle elongation and chromosome segregation. Binds also to other polyanionic phosphoinositides, such as phosphatidylinositol 3-phosphate (PIP), lysophosphatidic acid (LPA) and phosphatidylinositol triphosphate (PIP3), in vitro (By similarity). Also required for proper orientation of the mitotic spindle during asymmetric cell divisions. Plays a role in mitotic MT aster assembly. Involved in anastral spindle assembly. Positively regulates TNKS protein localization to spindle poles in mitosis. Highly abundant component of the nuclear matrix where it may serve a non-mitotic structural role, occupies the majority of the nuclear volume (By similarity). Required for epidermal differentiation and hair follicle morphogenesis.
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E9Q7R9
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CFA43_MOUSE
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Cilia- and flagella-associated protein 43
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MSQDPERDDVTASATASASASAPASASAHYSGSSLSVRWVQGFPSQNVHFVNDQTICYPSGNFVIFINLETKKKTVLQCINGIVGVMATNVPSEVVAFSDRRFKPVIYIYSFPSLTRKNKLKGDILLDYTLLCFSYCGTYLASYSSLPEFELALWNWEASAILCKKSNPGMDVSQMSFNPMNWHQMCLSSSSAMSVWTIERSNQEHHFRIRSVKLPLEDATFLNEPDMLFPTTLPKDLIYGPVLPLSAIAGLVGEEAETFRPKDDIYPLLHPTMHCWTPSSDLYVGCEEGHLLMINTETLKVTVLQKAEEFPLPDGAPLINPLTLVYQKDGILASGIDGVIYSFIIKDSKYQVKTFLEFDGPVTHLVFSPSYKMLLIQTDKGSVYIYTFGAEMPLDKLLDACDGKVQAVSFITPGTKYFLTLTSSGEVSTVSLEDCNCTSRIFLKTQATALACSPSSPTAAVGTVDGYVYFLNILDVESPQMIHQAFLSQSPVKIVTYDQRGIFLLVGTEEGNIFVIDARPSKSFQIFGFTETGKDILQISTVSVMESDVVEVLVLYPLPDMGRSRLEYFTLPVMLPEVVPENFSDERGRLKDDLTHKYLYEVEHTLSSAVLGFTGSKIFGFCSQVPYICSYVMPVKEHTGVLVLKPHQKVQSKQYGSGTIYLSSHGLWLMTIAKCGILCIRDMFSMETFVRCRSHSHQGRGIQNMKMSLDGQHILVNGKDDNTLVCLKWKRLGANIASEIFEHSRPLVLHLSQTVESESVYLALSRESTNEQQEETTESQKHLNSDSSEEEAVIDHKMIPWIQQKMEEAIKKEVRIFSPRRKEIKRGIKELAQVIAMMMEENEKVDIIAKLDEQEFCLDADELERLHDECEEEVAKIRKDVEMHNLAQSYLTELIKEECWNSMAVKGRALKCFHIPYVVDNFPMKERTEEELQELSKVMQQKKTEIECLKLRKEIVEVQATTTIAKKHHEEEEEEEEDEERTIKTTSLPNYLLGSLSTDFGADTSLLTSQLDLHSREEKINQIILLKDIIYNIKRNFNSEFDAAYKQKEIEIARVKEKNVRIAEIISDLELEETVWQPVFEDSEKPERALVVEDDEISFKKYIAPWQRAKIKEVVSTYEMERLQQARISDERQRGLMDMMGGVLEVKKEDILRMVIPQPPFMAKADALWSEDERKQFKEYEKKVKELNEERDKYRKSLEAELKKLQNSIQESTQNFDDHLKRLFERRVKAEMVINQEELKINNIIFSLLLDEELSSREQFLNNYLLKKQEEKTKTAEAIQKAREDLDVFKEHHDMLVAEDKILDRSFKKEFSDILGHQVDVLYKLFKRRPRVHKQKTQADVTSLVPYGERPGSAKLNKENLAQLMKSMDELDNINNMPEGLDPSVWEHFCSTRRAKVENEYKVKQKAACLLEMTTFLRKRMEEDDVVHHEIEKVFHELIRLQDEKVRFQVNLTVQILLKQGQVELENFQLMLEYSDAILINKNIIEDLNSVIRTQGQKKVASMMESKEVHKGIYQIEWEHKKMEMEMEDLNQRAWDIEMLFFSRDRQKYLNEPNYENVIAIQIGIMEQTISVIDKTHKKNVENCKKLLKKLGKYSNQKDVANYTLSCNLREELVAVSERQDICNEIGSKLTCEKIARERYDNQLKQQKLLNISKQQAEQISILQAEVERLRMKTFPALIPM
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Flagellar protein involved in sperm flagellum axoneme organization and function. Involved in the regulation of the beating frequency of motile cilia on the epithelial cells of the respiratory tract.
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E9Q7X6
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HEG1_MOUSE
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Protein HEG homolog 1
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MATPRAPRWPPPSLLLLLLLPLLLLPPAAPGARGSLPSPAHRTLLPVAGPLSPPGAGHTAPGPGVATRRGRSGRVPRGVSAAAARNRWLESNNPEPHIGCSPSYQSQEDHSGSRKGVTAQNARMSHSSSEGPENPPLLPETSAEWSNMASSHRADIAGLRRGPSPEITTAPTAHSSLLSLESLPESPSSSRSQRRITPSQTESGTSLGFLERTRELPEEGTVHTQVAGTWVSRQASHPALEPGEPTVLSQKRNSSGQEHSGPPFSWSQSHPPPSDHPSSSGSIKNGNNFTALQNPSVTQTKSMLITDTYTNGVPRTLRSLPVGVDPADETEGFPEHSRLGITSMSVRSSPSVKDSRTNSGLTEHLGDGEGTELSTENGYGLPSIHWQSDAPSFGGRQLASSSEAGDGRAMPLTEAVFRSDPSIGGGESTGRWILTKKKTSTDAAESSALHPEAGGAGGLTQSSHAAQQPRGGGEDSGMGGRSYAESSSSSSSTSSSESLDSSAPLREHSLTGLSYTREHGSDAGQRTSSDHTDHGYVPSTFTKGERTLLSITDNTSYSEASESSTSSVKISDSPSQAQPKQSSMSSDDDEPAQSSTESPVLHTSNLPTYTSTVNMPNTLVLDTGTKPVEDPSDSRVPSTQPSPSQPQPFSSALPSTRSPGSTSETTTSSPSPSPISLLVSTLAPYSVSQTTFPHPSSTLVPHRPREPRVTSVQMSTAISAIALIPSNQTANPKNQSTPQQEKPITEAKSPSLVSPPTDSTKAVTVSLPPGAPWSPALTGFSTGPALPATSTSLAQMSPALTSAMPQTTHSPVTSPSTLSHVEALTSGAVVVHTTPKKPHLPTNPEILVPHISTEGAITTEGNREHTDPTTQPIPLTTSTTSAGERTTELGRAEESSPSHFLTPSSPQTTDVSTAEMLTSRYITFAAQSTSQSPTALPPLTPVNSCTVNPCLHDGKCIVDLTGRGYRCVCPPAWQGENCSVDVNECLSSPCPPLATCNNTQGSFTCRCPVGYQLEKGICNLVRTFVTEFKLKKTFLNTTAENHSNTQELENEIAQTLNVCFSTLPGYIRTTAHVSREPSTVFISLKTTFALASNVTLFDLADRIQKYVNSCRSSAEVCQLLGSQRRVFRAGSLCKRKSPECDKETSICTDLDGVALCQCKSGYFQFNKMDHSCRACEDGYRLENETCMSCPFGLGGLNCGNPYQLITVVIAAAGGGLLLILGVALIVTCCRKSKNDISKLIFKSGDFQMSPYTDVPKNPRSQEWGREAIEMHENGSTKNLLQMTDVYYSPTNVRNPELERNGLYPAYTGLPGSRHSCIFPGQYNPSFISDESRRRDYF
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Receptor component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity. May be acting by stabilizing endothelial cell junctions.
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E9Q7X7
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NRX2A_MOUSE
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Neurexin-2 (Neurexin II-alpha) (Neurexin-2-alpha)
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MALGSRWQPPPQLPPLLLLLALAAGVRGLEFGGGPGQWARYARWAGAASTGELSFSLRTNATRALLLYLDDGGDCDFLELLLVDGRLRLRFTLSCAEPATLQLDTPVADDRWHMVLLTRDARRTALAVDGEARAAEVRSKRREMQVASDLFVGGIPPDVRLSALTLSTVKYEPPFRGLLANLKLGERPPALLGSQGLRGAAADPLCAPARNPCANGGLCTVLAPGEVGCDCSHTGFGGKFCSEEEHPMEGPAHLTLNSEVGSLLFSEGGAGRGGAGDVHQPTKGKEEFVATFKGNEFFCYDLSHNPIQSSTDEITLAFRTLQRNGLMLHTGKSADYVNLSLKSGAVWLVINLGSGAFEALVEPVNGKFNDNAWHDVRVTRNLRQHAGIGHAMVNKLHYLVTISVDGILTTTGYTQEDYTMLGSDDFFYIGGSPNTADLPGSPVSNNFMGCLKDVVYKNNDFKLELSRLAKEGDPKMKLQGDLSFRCEDVAALDPVTFESPEAFVALPRWSAKRTGSISLDFRTTEPNGLLLFSQGRRAGAGVGSHSSTQRADYFAMELLDGYLYLLLDMGSGGIKLRASSRKVNDGEWCHVDFQRDGRKGSISVNSRSTPFLATGESEVLDLESELYLGGLPEGGRVDLPLPPEVWTAALRAGYVGCVRDLFIDGRSRDLRGLAEAQGAVGVAPFCSRETLKQCASAPCRNGGICREGWNRFVCDCIGTGFLGRVCEREATVLSYDGSMYMKIMLPTAMHTEAEDVSLRFMSQRAYGLMMATTSRESADTLRLELDGGQMRLTVNLDCLRVGCAPSKGPETLFAGHKLNDNEWHTVRVVRRGKSLQLSVDNVTVEGQMAGAHTRLEFHNIETGIMTERRFISVVPSNFIGHLSGLVFNGQPYMDQCKDGDITYCELNARFGLRAIVADPVTFKSRSSYLALATLQAYASMHLFFQFKTTAPDGLLLFNSGNGNDFIVIELVKGYIHYVFDLGNGPSLMKGNSDKPVNDNQWHNVVVSRDPGNVHTLKIDSRTVTQHSNGARNLDLKGELYIGGLSKNMFSNLPKLVASRDGFQGCLASVDLNGRLPDLIADALHRIGQVERGCDGPSTTCTEESCANQGVCLQQWDGFTCDCTMTSYGGPVCNDPGTTYIFGKGGALITYTWPPNDRPSTRMDRLAVGFSTHQRSAVLVRVDSASGLGDYLQLHIDQGTVGVIFNVGTDDITIDEPNAIVSDGKYHVVRFTRSGGNATLQVDSWPVNERYPAGNFDNERLAIARQRIPYRLGRVVDEWLLDKGRQLTIFNSQAAIKIGGRDQGRPFQGQVSGLYYNGLKVLALAAESDPNVRTEGHLRLVGEGPSVLLSAETTATTLLADMATTIMETTTTMATTTTRRGRSPTMRDSTTQNTDDLLVASAECPSDDEDLEECEPSTGGELILPIITEDSLDPPPVATRSPFVPPPPTFYPFLTGVGATQDTLPPPAARRPSSGGPCQAERDDSDCEEPVEASGFASGEVFDSSLPPTDDEDFYTTFPLVTDRTTLLSPRKPRPNLRTDGATGAPGVLFAPSAPAPNLPAGKMNHRDPLQPLLENPPLGPGVPTAFEPRRPPPLRPGVTSAPGFPRLPTANPTGPGERGPPGAVEVIRESSSTTGMVVGIVAAAALCILILLYAMYKYRNRDEGSYQVDQSRNYISNSAQSNGAVVKEKAPAAPKTPSKAKKNKDKEYYV
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Neuronal cell surface protein that may be involved in cell recognition and cell adhesion. May mediate intracellular signaling.
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E9Q816
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CP2W1_MOUSE
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Cytochrome P450 2W1 (EC 1.14.14.-)
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MALLLLGVWGILLLLGLWGLLQGCTRSPSLAPRWPPGPRPLPFLGNLHLLGVTQQDRALMELSERYGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGGGIFFSSGARWRAGRQFTVRTLQSLGVQQPSMVGKVLQELACLKGQLDSYGGQPLPLALLGWAPCNITFTLLFGQRFDYQDPVFVSLLSLIDQVMVLLGSPGIQLFNTFPRLGAFLRLHRPVLSKIEEVRTILRTLLETRRPPLPTGGPAQSYVEALLQQGQEDDPEDMFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLPHVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPPGLSPADLDLRPAPAFTMRPPAQTLCVVPRS
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A cytochrome P450 monooxygenase that may play a role in retinoid and phospholipid metabolism. Catalyzes the hydroxylation of saturated carbon hydrogen bonds. Hydroxylates all trans-retinoic acid (atRA) to 4-hydroxyretinoate and may regulate atRA clearance. Other retinoids such as all-trans retinol and all-trans retinal are potential endogenous substrates. Catalyzes both epoxidation of double bonds and hydroxylation of carbon hydrogen bonds of the fatty acyl chain of 1-acylphospholipids/2-lysophospholipids. Can metabolize various lysophospholipids classes including lysophosphatidylcholines (LPCs), lysophosphatidylinositols (LPIs), lysophosphatidylserines (LPSs), lysophosphatidylglycerols (LPGs), lysophosphatidylethanolamines (LPEs) and lysophosphatidic acids (LPAs). Has low or no activity toward 2-acylphospholipids/1-lysophospholipids, diacylphospholipids and free fatty acids. May play a role in tumorigenesis by activating procarcinogens such as aflatoxin B1, polycyclic aromatic hydrocarbon dihydrodiols and aromatic amines. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR NADPH-ferrihemoprotein reductase).
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E9Q876
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ABCAC_MOUSE
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Glucosylceramide transporter ABCA12 (EC 7.6.2.1) (ATP-binding cassette sub-family A member 12)
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MASQFHQLRILVWKNWLGVKRQPLWTLVLILWPVIIFIILAITRTKFPPTAKPTCYLAPRNLPSAGFFPFLQTLLCDTDSKCKDTPYGPRDLLRRKGIDGPLFKESEILKKPSNPKRDSNLSLRSTQVPERSHTSLATVPPRPSYDLEGTGTENFNGSQLLTRILGLEKLLKQNSTPEDIRRELCESYPGYTADYAFSWVTLGKNVFNKFCLSNMTLLESSLQELKYQVSQMSSDPDNQKRVFRGLVQVLSFFSQVQQQREVWQLLSSLPDVFQNGTSLSSLFGVLQKANRVLLVVQKVYPRVQTDEGFSTLQKSVKHLLNTLDSPMQGDNSTHAWSDDDEQTLSPSSLAAQLLILENFEDAILNISSNSPYSPYLACVRNMTDNLAKGSPDNLKLLQSTIHFRKSFLQNGSSEDSFPPFLEILKSKLSQLRNLTELLCESETFSSIKKSCQFSNMSFERLCEDHAFHVQLIEAAELGTDLTTGLLYHDNIISAKLRGLLTGDPSKINLNVDWLLEQALQMNYLENITRLIPTVEAMLHVNTSADASEKPGQLREMFKNIDLLKEDLRAIGMSNTSIDKLLAIPIPDNRAEIISRVFWLHSCDTNVTNPKLEDAMKEFCKLPLPERSHQSYLIGLTLLHYLDIYNFTYKVFFPRKDQKPMERMMELFIKLREILNQLASGTHPLLDKMRSLRQMHLPRSVPLTQAMYRNTRMNSPAGSFSTISQALCSQGITTEYLTAMLPSSQKPKGNHTKDFLTYKLTKEEIASKYGIPLNATPFCFSLYKDIINMPAGPVIWAFLKPMLLGKILYSPYNPTTKAIMEKSNVTLRQLAELREKSQEWMDKSPIFMNSFHLLNQTIPMLQNTLRNPFVQVFVKFSVGLDAVELLKQIDDLDVLRLKLVNNIDIIDQLNTLSSLTVNISSCVLYDRIQASDTVEEMETVAEQLYKSNELFGSVIFKLPSNGSLHRGFDPEKVSLPPIVRYTIRMSLKTAQTTRSIRTKIWAPGPHNSPSHNQIYGRAFIYLQDSIERAIIELQTGRNSQEVAVQVQAVPYPCFMKDNFLTSVSYSLPIVLMVAWVVFIAAFVKKLVYEKDLRLHEYMKMMGVNSCSHFFAWLIESIGFLLVTIAILIVILKFGNILPKTNGFILFLYFSDYSFSVIAMSYLISVFFNNTNIAALIGSLIYVIAFFPFIVLVTVEDELSYVIKVFMSLLSPTAFSYASQYIARYEEQGVGLQWENMYKSPVQDDTTSFGWLCCLILADSFIYFFIAWYVRNVFPGTYGMAAPWYFPILPSYWKERFGCAEVKHEKSNGLMFTNIMMQNTNPSASKTSPDCAFPSNIEPEPKDLQVGVALHGVTKIYGSKTAVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIKTDLNTVRKNMGVCMQHDVLFSYLTTKEHLLLYGSIKVPHWTKTQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVISKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSPFYLKEAFGDGYHLTLTKKKSPNLDTNAICDTVAVTAMIQSHLPEAYLKEDIGGELVYVLPPFSTKVSGAYLSLLRALDKGMGKLNIGCYGISDTTVEEVFLNLTKDSQKSSNMSLEHLTQRKVGNPSANGTSTPDDLSVSSSNFTDRDDKVLTRSEKLEGFGLLLKKIMAILIKRFHHTRRNWKGLIAQVILPIVFVATAMGLGTLRDSSNSYPEIMISPSIYGTSEQTAFYANFDPSTSGLVSALWNFPGIDNVCLNTSDLQCLKKDDLGKWNTSGEAIDNFGVCSCSDNVQECPKFNYHPPHRRTYSSQVIYNLTGKHMENYLITTANHFVQKRYGGWSFGMKLTNDLRFDVTAVPDNRTLAKVWYDPEGYHSLPAYLNSLNNFLLRVNMSEYDAARHGIIMYSHPYPGVQDQEQATISSLIDILVALSILMGYSVTTASFVTYIVREHQTKAKQLQHISGIGVTCYWVTNFIYDMVFYLVPVAFSIGVIAIFKLPAFYSGNNLGAVSLLLLLFGYATFSWMYLLAGLFHETGMAFITYVCVNLFFGINSIVSLSVVYFLSKEKPNDPTLELISETLKRIFLIFPQFCFGYGLIELSQQQAVLDFLKAYGVEYPSETFEMDKLGAMFVALVSQGTMFFLLRLLINEWLIKKLRLFFRKFTSSPIMETVDEDEDVRAERFRVESGAAEFDLVQLHRLTKTYQLIHKKIIAVNNISLGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKSGSLGHVDSHSSLVGYCPQEDALDDLVTVEEHLYFYARVHGIPEKDIKDTVHKLLRRLHLMAYKDRSTSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWRIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGRFQCIGSLQHIKSRFGRGFTVKVHLKNNKVSMETLTKFMQLHFPKTYLKDQHLSMLEYHVPVTAGGVANIFDLLETNKTALNITNFLVSQTTLEEVFINFAKDQKSYENVDTSSQGSTISVDSQEDQLDS
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Transports lipids such as glucosylceramides from the outer to the inner leaflet of lamellar granules (LGs) membrane, whereby the lipids are finally transported to the keratinocyte periphery via the trans-Golgi network and LGs and released to the apical surface of the granular keratinocytes to form lipid lamellae in the stratum corneum of the epidermis, which is essential for skin barrier function. In the meantime, participates in the transport of the lamellar granules-associated proteolytic enzymes, in turn regulates desquamation and keratinocyte differentiation. Furthermore, is essential for the regulation of cellular cholesterol homeostasis by regulating ABCA1-dependent cholesterol efflux from macrophages through interaction with NR1H2 and ABCA1. Plays pleiotropic roles in regulating glucose stimulated insulin secretion from beta cells, regulating the morphology and fusion of insulin granules, lipid raft abundance and the actin cytoskeleton. Also involved in lung surfactant biogenesis.
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E9Q8I9
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FRY_MOUSE
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Protein furry homolog
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MASQQDSGFFEISIKYLLKSWSNASPVGNGYIKPPVPPASGTHREKGPPAMLPINVDPDSKPGEYVLKSLFVNFTTQAERKIRIIMAEPLEKPLTKSLQRGEDPQFDQVISSMSSLSEYCLPSILRTLFDWYKRQNGIEDESHEYRPRTSNKSKSDEQQRDYLMERRDLAIDFIFSLVLIEVLKQIPLHPVIDSLIHDIINLAFKHFKYKEGYLGPNTGNMHIVADLYAEVIGVLAQAKFPAVKKKFMAELKELRHKEQSPYVVQSIISLIMGMKFFRIKMYPVEDFEASLQFMQECAHYFLEVKDKDIKHALAGLFVEILVPVAAAVKNEVNVPCLRNFVESLYDTTLELSSRKKHSLALYPLVTCLLCVSQKQLFLNRWHVFLNNCLSNLKNKDPKMARVALESLYRLLWVYMIRIKCESNTATQSRLITITTTLFPKGSRGVVPRDMPLNIFVKIIQFIAQERLDFAMKEIIFDFLCVGKPAKAFSLNPERMNIGLRAFLVIADSLQQKDGEPPMPVTGAVLPSGNTLRVKKTYLSKTLTEEEAKMIGMSLYYSQVRKAVGNILRHLDKEVGRCMMLTNVQMLNKEPEDMITGERKPKIDLFRTCVAAIPRLLPDGMSKLELIDLLARLSIHMDDELRHIAQNSLQGLLVDFSDWREDVLFGFTNFLLREVNDMHHTLLDSSLKLLLQLLTQWKLVIQTQGRAYEQANKIRNSELIPNGSSHRMQSERGPHCSVLHAVEGFALVLLCSFQVATRKLSVLILKEIRALFLALGQPEDDDRPMIDVMDQLSSSILESFIHVAVSDSATLPPTHNVDLQWLVEWNAVLVNSHYDVKSPSHVWIFAQSVKDPWVLCLFSFLRQENLPKHCPTALSYAWPYAFTRLQSVMPLVDPNSPVNAKKTSTASSGDNYVTLWRNYLILCFGVAKPSIMSPGHLRASTPEIMATTPDGTVSYDNKAIGTPSVGVLLKQLVPLMRLESIEITESLVLGFGRTNSLVFRELVEELHPLMKEALERRPENKKRRERRDLLRLQLLRIFELLADAGVISDSTNGALERDTLALGALFLEYVDLTRMLLEAENDKEVEILKDIRAHFSAMVANLIQCVPVHHRRFLFPQQSLRHHLFILFSQWAGPFSIMFTPLDRYSDRNHQITRYQYCALKAMSAVLCCGPVFDNVGLSPDGYLYKWLDNILACQDLRVHQLGCEVVMLLLELNPDQINLFNWAIDRCYTGSYQLASGCFKAIATVCGNRNYPFDIVTLLNLVLFKASDTNREIYEVSMQLMQILEAKLFVHSKKVAEQRPGSILYGTHGPLPPLYSVSLALLSCELARMYPELTLPLFSEVSQRFPTTHPNGRQIMLTYLLPWLHNIELVDSRLLLPGSSPSSPEDEVKDREGEVTASHGLKGNGWGSPEATSLVLNNLMYMTAKYGDEVPGAEMENAWNALANNEKWSNNLRVTLQFLISLCGVSSDTILLPYIKKVATYLCRNNTIQTMEELLFELQQTEPVNPIVQHCDNPPFYRFTASSKASAAASGTTSSSNTVVAGQDSFPDPEESKILKESDDRFSNVIRAHTRLESRYSNSSGGSYDEDKNDPISPYTGWLLSITEAKQPQPLPMPCSGGCWAPLVDYLPETITPRGPLHRCNIAVIFMTEMVVDHSVREDWALHLPLLLHAVFLGLDHYRPEVFEHSKKLLLHLLIALSCNSNFHAIASVLLQTREMGEAKTLTMQPAYQPEYLYTGGFDFLREDQSSPVPDSGLNSSSTSSSISLGGSSGNLPQMTQEVEDVEAATETDEKASKLIEFLTTRAFGPLWCHEDITPKNQNSKSAEQLSNFLRHVVSVFKDSRSGFHLEQHLSEVALQTALASSSRHYAGRSFQIFRALKQPLSAHALSDLLSRLVEVIGEHGDEIQGYVMEALLTLEAAVDNLSDCLKNSDLFTVLSRSSSPDLSSSSKLTASRKSTGQLNVNPGTPGSGGGGGGSGNTTTAERSRHQRSFSVPKKFGVVDRSSDPPRSATLDRIQACTQQGLSSKTRSNSSLKESLTDPSHVSHPTNLLATIFWVTVALMESDFEFEYLMALRLLNRLLAHMPLEKAENREKLEKLQAQLKWADFPGLQQLLLKGFTSLTTTDLTLQLFSLLTSVSKVPMVDSSQAIGFPLNVLCLLPQLIQHFENPNQFCKDIAERIAQVCLEEKNPKLSNLAHVMTLYKTHSYTRDCATWVNVVCRYLHEAYADITLNMVTYLAELLEKGLPSMQQPLLQVIYSLLSYMDLSVVPVKQFNMEVLKTIEKYVQSIHWREALNILKLVVSRSASLVLPSYQHSDLSKIELHRVWTSASKELPGKTLDFHFDISETPIIGRRYDELQNSSGRDGKPRAMAVTRSASSTSSGSNSNVLVPVSWKRPQYSQKRTKEKLVHVLSLCGQEVGLSKNPSVIFSSCGDLDLPEHQTSLVSSEDGPREQENMDDTNSEQQFRVFRDFDFLDVELEDGEGESMDNFNWGVRRRSLDSLDKCDMQILEERQLSRSTPSLNKMSHEDSDESSEEDLTASQILEHSDLIMNLSPSEEANPMELLTSACDSAPADPHSFNTRMANFEASLPDINNLQISEGSKAEAVPEEEDTTVHEDDLSSSINELPAAFECSDSFSLDMTEAEEKGNRGLDQYTLASFGEGDRGVSPPPSPFFSAILAAFQPAACDDAEEAWRSHINQLMCDSDGSCAVYTFHVFSSLFKNIQKRFCFLTCDAASYLGDNLRGIGSKFVSSSQMLTSCSECPTLFVDAETLLSCGLLDKLKFSVLELQEYLDTYNNRKEATLSWLANCKATFAGGSRDGVITCQPGDSEEKQLELCQRLYKLHFQLLLLYQSYCKLIGQVHEVSSVPELLNMSRELSDLKRNLKEATAAIATDPLYIEGAWSEPTFTSTEAAIQSMLECLKNNELGKALRQIKECRSLWPNDIFGSSSDDEVQTLLNIYFRHQTLGQTGTYALVGSNHSLTEICTKLMELNMEIRDMIRRAQNYRVLTAFLPDSSVSGTSL
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Plays a crucial role in the structural integrity of mitotic centrosomes and in the maintenance of spindle bipolarity by promoting PLK1 activity at the spindle poles in early mitosis. May function as a scaffold promoting the interaction between AURKA and PLK1, thereby enhancing AURKA-mediated PLK1 phosphorylation.
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E9Q8Q8
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SACA6_MOUSE
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Sperm acrosome membrane-associated protein 6
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MTSQRSLSSPQTRRPSVMGLISLVGSIVLLFLLIFRASTWACLFCFTTYEERLRVCQLFVGREETKINLCRNELEGAFEDLKDMKINYDERSYLHDEFTQMTVSLQEKAARRREPFWLAFKDAAAKLKRTIEHLKKAPACIPPCGLQEVARLFHCSGCFSKLCDLPLDCPVQDMLVNRGDQALFSCIVAFELPESEITYSWKFVGGVRTKDVTYFRDMPGAHGYLARIRPVQPKHGGTFSCVILHDQRPLARLYFYLNVTGPPPPEDTELQVTFREVMNRTPAEPEMIQPWSPSLGELLTNPQALTLGNLFLLAATAALGSASVTLLVWLFFRWYLSGN
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Sperm protein required for fusion of sperm with the egg membrane during fertilization.
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E9Q8T2
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PRD15_MOUSE
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PR domain zinc finger protein 15 (EC 2.1.1.-) (PR domain-containing protein 15)
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MCPPTIWEKGGQVGARWSLRAPEVSAMAEDGSEEIMFIWCEDCSQYHDSECPELGPVVMVKDSFVLSRARSSLPSNLEIRRLDDGAEGVFAVTQLVKRTQFGPFESRRVAKWEKESAFPLKVFQKDGHPVCFDTSNEDDCNWMMLVRPALEPGHQNLTAYQHGSDVYFTTSKDIPAGTELRVWYAAFYAKKMDKPMLKQACSSVQAAGTPEPSVSVEPERGQWVCKVCSNTFLELQLLNEHLLGHLEQAKSLPAGGQQHEAASEKEPDAPRMEPPTAAESKSIQSVMVTKEPKKKPRRGRKPKASKVEQPLVIIKDKEPSEHVAEIITEIPPDEPVSATPDERIMELVLGKLAAPTNEASSVPKFPHHPSSTIALKRGLVLSSRHGVRRKLVRQLGEHKRIHQCGTCSKVFQNSSNLSRHVRSHGECAHGDKLFKCEECSKLFSRKESLKQHVSYKHSRNEVDGEYRYRCGSCGKTFRMESALEFHNCRTDDKTFQCEMCFRFFSTNSNLSKHKKKHGDKKFACEVCSKMFYRKDVMLDHQRRHLDGVRRVKREDLEASGESLVRYKKEPSGCPVCGKVFSCRSNMNKHLLTHGDKKYTCEICGRKFFRVDVLRDHIHVHFKDIALMDDHQREEFIGKIGISSEENDDNSDESADSEPHKYSCKRCQLTFGRGKEYLKHIMEVHKEKGHGCSICHRRFALKATYHAHMVIHRENLPDPNVQKYIHPCEICGRIFNSIGNLERHKLIHTGVKSHACEQCGKSFARKDMLKEHMRVHDNIREYLCAECGKGMKTKHALRHHMKLHKGIKEYECKECHRKFAQKVNMLKHYKRHTGIKDFMCELCGKTFSERNTMETHKLIHTVGKQWTCSVCDKKYVTEYMLQKHVQLTHDKVEAQSCQLCGTKVSTRASMSRHMRRKHPEVLAVRIDDLDHLPETTTIDASSIGIVQPALGLEQEELAEGKHGKAAKRSHKRKQKPEEEAGAPVPEDTTFSEYPEKEPEFTGSVGDETNSAVQSIQQVVVTLGDPNVTAPSSSVGLTNITVTPITTAAGTQFTNLQPVAVGHLTNPDRQLQLDNSILTVTFDTVSGSAMLHNRQNDVQIHPQPEATNPQSVAHFINLTTLVNSITPLGNQLSEQHPLTWRAVPQTDVLQPPQAPAAPQQAVQPQVQNEQQQMYSY
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Sequence-specific DNA-binding transcriptional regulator. Plays a role as a molecular node in a transcriptional network regulating embryonic development and cell fate decision. Stimulates the expression of upstream key transcriptional activators and repressors of the Wnt/beta-catenin and MAPK/ERK pathways, respectively, that are essential for naive pluripotency and self-renewal maintenance of embryonic stem cells (ESCs). Specifically promotes SPRY1 and RSPO1 transcription activation through recognition and direct binding of a specific DNA sequence in their promoter regions. Also plays a role in induced pluripotent stem cells (iPSCs) reprogramming. Involved in early embryo development.
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E9Q8T7
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DYH1_MOUSE
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Dynein axonemal heavy chain 1 (Axonemal beta dynein heavy chain 1) (Ciliary dynein heavy chain 1) (mDHC7)
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MEECNKEGPSSSSQGPGYCPVKVPESHDLEKILQESNYHPERNPLNPDPKTPPLPLTDLRQPRKSPLTGTDKKYPLMKQRGFYSDILSPGTLDKLGNVCCGPYMSQNLIRQADLDKFTPKVDSFVIPEDFQERVEQQIIGATTRLLTQTDFPLQSYEPKVQVPFQVLPGQCPRKIEIERRKQQYLRLDIEQLLTSEGIDSNKLMPRHPDLQHPQTIEQGRDPLFPIYLPLKVFDNEEFDCRTPTEWLNMGLEPGSQNRKPVPGKALLPTDDDLGHEDPKNQELDYRWCEVGVLDYDEEKKLYLVQKTDKRGLVRDEMGMPILNGGITPAGRPPLLATQYWVPRIQLLFCAEDPRVFTQRVVQANALRKYTEALLMYNLYVDCMPTEGRRVINEQSLSKIKQWALSTPRMRKGQSVLEHLSCLAREVNLDYERSMNKINFDQIVSSNPETFSYVTLPEKEEEKVPNQGLVSVPEYPFREQKEDFTFVSLLTRPEVITALSKVRAECNKVTSMSLFHSSLSKYSRLEEFEQIQSQTFSQVQMFLKDSWISTLKVAMRGSLRDMSKGWYNLYETNWEVYLMSKLRKLMELIKYMLQDTLRFLVQDSLGSFTQFIGDACCSVLECVDDMDWGEDLVNSPYKPRKNPLFIVDLVLDNSGVHYSTPLEHFEMILLNLFDKGILATHAVPQLEKLVMEDIFISGDPLLESVGLHEPLVEELRANITNAMHKAMMPLQAYAKEYRKYLELNNNDISTFLKTYQTQCPSAEEVREVVITHLKEKEILDNSLPSSIIIGPFYINVDNVKQSLSKKRKALATSMLDILAKNLHKEVDSICEEFRSISRKIYEKPNSIEELAELRDWMKGIPEKLVFLEERIVKVMSDYEVMDEFFYNLTTDDFNDKWAANNWPSKILGQIDMVRQQHVEDEEKFRKIQLMDQNNFQEKLEGLQLVVAGFSIHVEIARAHEIANEVRRVKKQLKDCQQLAMLYNNRERIFGLPITNYDKLSRMVKEFQPYLDLWTTASDWLRWSESWMNDPLSAIDAEQLEKNVIESFKTMHKCVKQFKDIPACQEVALDIRTRIEEFKPYIPLIQGLRNPGMRNRHWEVLSNEININVRPKANLTFARCLEMNLQDHIESISKVAEVAGKEYAIEQALDKMEKEWSSILFNVLPYKETDTYILKSPDEASQLLDDHIVMTQSMSFSPYKKPFEQRINSWETKLKLTQEVLEEWLNCQRAWLYLEPIFSSEDITRQLPVESKRYQTMERIWRKIMKNAYENREVINVCSDQRLLDSLRDCNKLLDLVQKGLSEYLETKRTAFPRFYFLSDDELLEILSQTKDPTAVQPHLRKCFENIARLLFQEDLEITHMYSAEGEEVKLSFSIYPSSNVEDWLLEVERSMKASVHDIIEMAIKAYPTMLRTEWVLNWPGQVTIAGCQTYWTMEVAEALEAGNISSKLFPQLSKQLSDLVALVRGKLSRMQRMVLSALIVIEVHAKDVVSKLIDENVVSVHDFEWISQLRYYWTKDDLYIRAVNAEFIYGYEYLGNSGRLVITPLTDRCYLTLTGALHLKFGGAPAGPAGTGKTETTKDLGKALAIQTVVFNCSDQLDFMAMGKFFKGLASAGAWACFDEFNRIDIEVLSVVAQQITTIQKAQQQRVERFMFEGVEIPLVPSCAVFITMNPGYAGRTELPDNLKALFRPVAMMVPDYAMIAEISLYSFGFNEANVLAKKITTTFKLSSEQLSSQDHYDFGMRAVKTVISAAGNLKRENPTMNEELICLRAIRDVNVPKFLQEDLKLFSGIVSDLFPTIKEEETDYGILDQAIRRSCEKNNLKDVEGFLIKCIQLYETTVVRHGLMLVGPTGSGKSNCYRVLAAAMTLLKGKPSISGGVYEAVNYYVLNPKSITMGQLYGEFDLLTHEWTDGIFSSLIRAGAIASDTNKKWYMFDGPVDAVWIENMNTVLDDNKKLCLSSGEIIKLTEAMTMMFEVQDLAVASPATVSRCGMVYLEPSILGLMPFVECWLKRLPAIIKPYEEQFKSLFTKYLENSINFVRNTVKEVIASTNSNLTMSLLKLLDCFFRPFLPREGLKKIPSEKLSHIPELIEPWFIFSLVWSVGATGDHTSRISFSQWLRLKMRLEQVKLGFPEDGLVYDYRLDDAGISSTEDDDEEEDENKQVSWVKWMDYSAPFTMMPDTNYCNIIVPTMDTVQMSYLLGMLLTNHKPVLCIGPTGTGKTLTVSNKLLKYLPLEYISHFLTFSARTSANQTQDLIDSKLDKRRKGVFGPPLGRNFIFFIDDLNMPALETYGAQPPIELLRQWMDHGGWYDRKVIGAFKNLVDINFVCAMGPPGGGRNAITPRLTRHFNYLSFIEMDEVSKKRIFSIILECWMDGLLGEKSYREPVPGAPNIDDLTEPLVDATINVYGIITSQLLPTPAKSHYTFNLRDLSKVFQGMLMAEPSKVEDKVQLLRLWYHENCRVFRDRLVNEEDRSWFDELLEAQMEEFGVAFNKVCPFQPILYGDFMSPGSDVKSYELITSESKMMQVIEEYMEDYNQINTAKLRLVLFVDAMSHICRISRTLRQALGNALLLGVGGSGRSSLTRLASHMAEYECFQIELSKNYGMSEWREDVKKVLLKAGLQNLPITFLFSDTQIKNESFLEDINNVLNSGDIPNIYSADEQDQIINTMRPYIQEQGLQPTKANLMAAYTGRVRSNIHMVLCMSPIGEVFRARLRQFPSLVNCCTIDWFNEWPAEALKSVATTFLSEIPELECSEEVIQGLIQVCVFIHQSVASKCVEYLAELARHNYVTPKSYLELLNIFSILIGQKKMELKTAKNRMKSGLDKLLRTSEDVAKMQEELEIMRPLLEEAAKDTMLTMEQIKVDTAIAEETRKSVQAEEIKANEKANKAQAIADDAQKDLDEALPALDAALASLRNLNKNDVTEVRAMQRPPPGVKLVIEAVCIMKGIKPKKVPGEKPGSKVDDYWEPGKGLLQDPGRFLESLFKFDKDNIGEAVIKAIQPYIDNEEFQPAAIAKVSKACTSICQWVRAMHKYHFVAKAVEPKRQALREAQDDLEVTQRILEEAKHHLHEVEDGIATMQAKYRECVAKKEELEMKCEQCEQRLGRADKLINGLADEKVRWQETVENLENMLDNIFGDVLVAAGFVAYLGPFTGQYRTTLYEYWVNQLTVHHVPHTSKPTLITTLGNPVKIRSWQIAGLPNDTLSVENGVINQFSQRWTHFIDPQGQANKWIKNMERESGLDVFKLSDRDFLRSMENAIRFGKPCLLENVGEELDPALEPVLLKQTYKQQGNIVLKLGDTVIPYHEDFRMYITTKLPNPHYSPEISTKLTLINFTLSPSGLEDQLLGQVVAEERPDLEEAKNQLIVSNAKMRQELKDIEDQILYRLSSSEGNPVDDMELIKVLEASKMKAAEIQAKVRIAEQTEKDIDLTRMEYIPVAVRTQILFFCVSDLANVDPMYQYSLEWFLNIFLSGIANSERADNLKKRIVNINRYLTFSLYSNVCRSLFEKHKLMFAFLLCVRIMMNEGKINQAEWRYLLSGGSIQTMFENPAPQWLSDRAWRDILALSNLPTFATFSNDFVMYLSEFQAIFDSAEPHRELLPGIWNAYLDEFQKLLILRCLRGDKVTNAMQDFVATHLEPRFIEPQTANLSAVFKESNSTTPLIFVLSPGTDPAADLYKFAEEMKFSKKFSAISLGQGQGPRAEAMMRNSIERGKWVFFQNCHLAPSWMPALERLIEHINPDKVHRDFRLWLTSLPSNKFPVSILQNGSKMTIEPPRGVKANLLKSYNSLSDDFLHSCQKVVEFKSLLLSLCLFHGNALERRKFGPLGFNIPYEFTDGDLRICISQLKMFLDEYEDIPYKVLKYTAGEINYGGRVTDDWDRRCVMNILEDFYNPAVLSSEHSYSNSGIYHQIPPTYDLNGYLSYIKSLPLNDMPEIFGLHDNANITFAQNETFALFNAILQLQPKSSSMGGQSREELVEDVAENILLQVPGPIELQEVTKKFPVLYEESMNTVLVQEVIRYNKLLEVITQTLSDMLKAIKGLVVMSLELELMSISLYNNTVPELWKSKAYPSLKPLASWIMDLLLRLDFMHSWINDGIPPVFWISGFFFPQAFLTGTLQNFARKFVISIDTITFDFKVLPEASSEIKERPQTGCYIHGLFLEGARWDSMNFQLAESRPKELYTEMAVIWLLPEANRKVQNQDFYLCPIYKTLTRAGTLSTTGHSTNYVIAVEIPSNQPQRHWIKRGVALICALDY
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Force generating protein of cilia required for sperm flagellum motility. Produces force towards the minus ends of microtubules. Dynein has ATPase activity the force-producing power stroke is thought to occur on release of ADP (By similarity). Required in spermatozoa for the formation of the inner dynein arms and biogenesis of the axoneme (By similarity).
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E9Q912
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GDS1_MOUSE
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Rap1 GTPase-GDP dissociation stimulator 1
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MDNLSDTLKKLKITAADRTEGSLEGCLDCLLQALAQNNAETSEKIQGSGILQLFANLLTPQASCTAKVADIIAEVAKNEFMRIPCVDAGLISPLVQLLNSKDQEVLLQTGRALGNICYDSHEGRSAVDQAGGAQIVIDHLRSLCGRTDPASEKLMTVFCGMLMNYSNENDSLQAQLISMGVIPTLVKLLGIHCHNAALTEMCLVAFGNLAELESSKEQFASTNIAEELVKLFKKQIEHDKREMIFEVLAPLAENDAIKLQLVEAGLVECLLEIVQQKVDSNKEDDVAELKTASDLMVLLLLGDESMQKLFEGGKGSVFQRVLSWIPSNNHQLQLAGALAIANFARNDGNCIHMVDNGIVEKLMDLLDRHVEDGNVTVQHAALSALRNLAIPVVNKAKMLSAGVTETVLKFLKSEMPPVQFKLLGTLRMLIDAQAEAAEQLGKNAKLVERLVEWCEAKDHAGVMGESNRLLSALIRHSKSKDVIKTIVQSGGIKHLVTMATSEHVIMQNEALVALALIAALELGPAEKDLASAQLVQILHRLLADERSAPEIKYNSMVLICALMGSESLYKEVQDLAFLDVVSKLRSHENKSVAQQASLTEQRLTVES
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Acts as a GEF (guanine nucleotide exchange factor) for the Rho family of small GTP-binding proteins (G proteins) that stimulates the dissociation of GDP to enable subsequent binding of GTP. Additionally, appears to chaperone the processing and/or trafficking of small GTPases containing a C-terminal polybasic region independently of GEF activity. Targets include RAP1A/RAP1B, RHOA, RHOB, RHOC, RAC1 and KRAS. Regulates mitochondrial dynamics by controlling RHOT function to promote mitochondrial fission during high calcium conditions. Able to promote the Ca(2+) release from the endoplasmic reticulum via both inositol trisphosphate (Ins3P) and ryanodine sensitive receptors leading to a enhanced mitochondrial Ca(2+) uptake. [Isoform 1]: Acts as a GEF (guanine nucleotide exchange factor) for unprenylated RHOA. Chaperones the entry and passage of small GTPases through the prenylation pathway. Recognizes the last amino acid in the GTPase C-terminal CAAX motif with a preference for 'Leu' over 'Met', indicating involvement in the geranylgeranylation pathway. May also recognize prenylated GTPases.
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E9Q956
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MCMD2_MOUSE
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Minichromosome maintenance domain-containing protein 2 (MCM domain-containing protein 2)
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METLQMKEAALVYLDRSGGLQKFIDDCKSYNDSKQSYAVYRFSILIDPCDVVELDADLGNHILHHPLKAARVFQSVCFVAVKTLSLIGQLQTETQINIVLKLTHLPALPSYTLDLCEFPLNYASQRFYMMQGIVIAMTTITKYTQGARFLCSDGVCPLSKGFQYVRVHVPGATESATVRNDFLCSLCSSSLQEDRKFRVLGDKQIVEIITTKMFHAFQGDSKNQPFRFQSLGIFLRDELVNKMKIGNEYKIIGIPVCVKTSQTALCVEANNITPHTAKVPLGISDNFRRLLSLTSSSCWKFTAMLANVFASQIVAPGTYNLLKLCLLMSLVQTRDCNREREDCLDILVITSDTLLVDRLLNFSMNLVSRGIRHPVCTEVFPTVSRNKYGTGAVSIQAGSALLAKGGICFIGDLTSHKKDKLEQLQSALESRSVTVFIPGKKFGDDFDQQMTFPIQCSFWSFVDMDSSSRRNVQKTSTLIGQMDCSLIPANLAEAFGLLINCSEASPCHPLLPTVQHTLKKAVEPEGLLYLASKQFTTEDFEKLLAFAKSLNMEFSLEAERMIHGYYLASRRIRTDSIHGSKLSASALKYLVSLSEAHARLSLRTTVLREDALIAALLLEISLTLRYGATPFCVAPNALFPFELYNEEYLEQRDLYLTQCQQQLQQFIATCGPGTTVFSSDE
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Plays an important role in meiotic recombination and associated DNA double-strand break repair.
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E9Q9A9
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OAS2_MOUSE
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2'-5'-oligoadenylate synthase 2 ((2-5')oligo(A) synthase 2) (2-5A synthase 2) (EC 2.7.7.84) (2',5'-oligoadenylate synthetase-like 11)
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MGNWLTGNWSSDRSSGYSSGWSPGGSSGVPSGPVHKLEKSIQANLTPNENCLKQIAVSSVPSQKLEGYIQENLKPNRESLKQIDQAVDAIWDLLRSQIPVKEVAKGGSYGRETALRGCSDGTLVLFMDCFQQFQDQIKYQDAYLDVIELWLKIHEKKSVKHEHALVVQVSVPGQRILLQLLPVFNPLRSNENPSSCVYVDLKKSMDQVRASPGEFSDCFTTLQQRFFKKYPQRLKDLILLVKHWYEQCQEKWKTPPPQPLLYALELLTVYAWEQGCQAEDFDMAQGVRTVLRLIQRPTELCVYWTVNYNFEDETVRNILLHQLRSQRPVILDPTDPTNNVGKDDGFWELLTEEAMAWLYSPSLNTESPAPYWDVLPMPLFVTPSHLLNKFIKDFLQPNKLFLKQIKEAVDIICSFLKNVCFLNSDTKVLKTVKGGSTAKGTALKRGSDADIVVFLSSLESYDSLKTNRSQFVQEIQKQLEEFVQAQEWEVTFEISKWKAPRVLSFTLKSKTLNESVEFDVLPAYDALGQLRSDFTLRPEAYKDLIELCASQDIKEGEFSICFTELQRNFIQTRPTKLKSLLRLIKHWYKQYERKMKPKASLPPKYALELLTVYAWEQGSGTDDFDIAEGFRTVLDLVIKYRQLCIFWTVNYNFEEEYMRKFLLTQIQKKRPVILDPADPTGDVGGGDRWCWHLLAEEAKEWLSSPCFQVEQKGLVQPWKVPVMQTPGSCGGQIYPTVGGVTK
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Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. Activated by detection of double stranded RNA (dsRNA): polymerizes higher oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNASEL) leading to its dimerization and subsequent activation. Activation of RNASEL leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNASEL-dependent pathway or an alternative antiviral pathway independent of RNASEL. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation. May act as a negative regulator of lactation, stopping lactation in virally infected mammary gland lobules, thereby preventing transmission of viruses to neonates. Non-infected lobules would not be affected, allowing efficient pup feeding during infection.
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E9Q9D5
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RBL2A_MOUSE
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Rab-like protein 2A
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MAGDRNRHCELEQEKYDTHENVKIICLGDSAVGKSKLMERFLMDGFQPQQLSTYALTLYKHTATVDGKTILVDFWDTAGQERFQSMHASYYHKAHACIMVFDVQRKITYKNLGTWYAELREFRPEIPCILVANKIDADIQMTQKNFSFAKKFSLPLYFVSAADGTNVVKLFNDAIRLAVAYKESSQDFMDEVLQELENFKLEQKEEDTSGQEQSDTTKSPSPS
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Plays an essential role in male fertility, sperm intra-flagellar transport, and tail assembly. Binds, in a GTP-regulated manner, to a specific set of effector proteins including key proteins involved in cilia development and function and delivers them into the growing sperm tail.
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E9Q9F6
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CTSRD_MOUSE
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Cation channel sperm-associated auxiliary subunit delta (CatSper-delta) (CatSperdelta) (Transmembrane protein 146)
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MLVLMLAAAVATMVRAHTLCRVHTVRTGKVFKSNIQLQGDPLFYAFPNTFVLKNVCKADISVYLGQKVFLTIDNFESSLLPLTVPKSLAVGVPSITSAHFVSGSLVLFVISGKGYSYDYYENTWRKLEGISEPVSHISGDVCCFKGSFCLELSNNLFAYLRGGQIPGTNIYFSDNGGFSFQLMNTDKLSHLTGTLGGIFHLHSMSQVGVLMVENNLGTFHYMEYPLNHSMGIAFSYKNLLEVIMKPYQRGFMVLWNQKSILVSSNSGQIVEHVRLIDQKIFTDLDVEHANINIYSVASNAYELAFLVAEDHLYYGSQSYMGTYVIKLPHQPLWSTHTSIYFEDIGILQVLTPVADPHFAAYDFDKCTVNVQSSLMDEKLALQPCNVELLESTMINTMFTIDMNSKLKLSALMIPRKGENPTPLVMVSNPHALGFKANLNEFGNTFDGNSKYKLDIELKQQHHWGNSDFNFTASIKRHAISSVTVDIADKTLSCVDLKPLSTLISVGCDMTKKIVVQNKISACTMGILNPVQLQKNYTYTIEKEAYDPINHNGEAQDDLIVFYEYKDLGCPRLVYYDKPWKPVVELWKNGIVEEIMNAEYVISEINGLVTYSYSLTAATANCRSQPQNWSTFESDIENEEPFLWNRENYVSCHEDNKDNPLLWPNVEYQVLGGQTNNKIIFGQRNGIYTFHLSVVDPYYSYCNLNTIFSVYVHGALPVTKFQPLLTILLMVTTTLLTAWLAYAIPKQLRSEKGQRLLGFCYQILQLCLGVCFCTWLRGKLRQWLRPRRVKDQNRGKVRVAQKHPET
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Auxiliary component of the CatSper complex, a complex involved in sperm cell hyperactivation. Sperm cell hyperactivation is needed for sperm motility which is essential late in the preparation of sperm for fertilization. Required for CATSPER1 stability before intraflagellar transport and/or incorporation of the CatSper complex channel into the flagellar membrane.
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E9Q9K5
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TRDN_MOUSE
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Triadin
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MTEITAEGNASTTTTVIDNKNGCIPKSPGKVLKRSVTEDIVTTFSSPAAWLLVIALIITWSAVAIVMFDLVDYKNFSASSIAKIGSDPLKLVNDAVEETTDWIYGFFSLLSDIISSEGDEDDEDADEDIDKGEIEEPPLKRKEIHQEKAEKEEKPEKKIQTKASHREREKGKEKLKGEKPEKTATHKEKLEKKERPETKMMAKEDKKIKTKEKTEEKAKKEMKVGKQEKVKPTAAKAKETPKTPPKARKKDDKEMPAVHEQKDQYAFCRYMIDMFVHGDLKPGQSPVMPPPSLTPSKPALSTTALEEKEKEEKKKMEKKDTSDTKKKEKEVKKKSEETTIDGKGKEPGKPPETKQMTAKLTTQAAARKDEKKEESKKMRKPTEEQPKGKKQEKKEKHIEPAKTPKKEHPGPSEKLKKAKAEQAKEEIAAASTKKALHGKKEEKAKTVEQEVKKEKSGKSSSDLKDKEVKKEKSGKSSSDLKDKEPQLKNEEKSKPQVKKEAKLASSDKGQTRKQNITRPEQVIPHVKPEKAEHQEKGHPSIKKDKPKPSSKGAPEVPDSGKKKIEKSEKESKVPTREENLQVYNVTKAEKPGKIPKDSKEAPASKKDKEDSKEAPTSKKDKEDSKDVPHSKKDKEVTDDVSSPKKQTRPISFFQCVYLNGYNGYGFQFPVTPVQQPGENPGKTNSPGQKQQEQ
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Contributes to the regulation of lumenal Ca2+ release via the sarcoplasmic reticulum calcium release channels RYR1 and RYR2, a key step in triggering skeletal and heart muscle contraction. Required for normal organization of the triad junction, where T-tubules and the sarcoplasmic reticulum terminal cisternae are in close contact. Required for normal skeletal muscle strength. Plays a role in excitation-contraction coupling in the heart and in regulating the rate of heart beats.
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E9Q9M8
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PWP2B_MOUSE
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PWWP domain-containing protein 2B
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MEPRAGCRLPVRVEQVVNGALVVTVSCGERSFAGILLDCTKKSGLFGLSPSTLLPLADNSSAVSCHGQAPEEGTGEVMQLETGPLHPHHKDPEKDQPPKTAVSEPPPPLIPPVPAGNLPPFPPYFEGAPFPHPLWLRNTYQQWVPQPPPRTIKRTRRRLSRNRDPGRLILSTIRLRPRQVLCEKCKSTVSPQEASPSPLNTPKPRRRLGSGPDSEHRKPEEPEDSAVIATAAPRRSKREKREEDRVAGERVPRSPVIKISYSTPQGKGEVVKIPSRVHGSVEPFCPQQSLQNGSQDSEVSRDVEPRGGGDRPPSGSSASIPKLKLTRPVPPISDLPPPKIRLKPHRLGDGEHEPLYRAELVEELNGCPRGPLVSSPALFADGSSHGLEDLSSGSSGEDDDLKRFPQGKHGRDGLAFLVDCPGRRTDCTSESVCSTDSLDELKSSGSEVTSPDTGDLSSGDSASVPSSSADTRQTVPPLTVRLHTQSVSRCVTEDGRTVAVGDIVWGKIHGFPWWPARVLDISLGQKEDGEPSWQEAKVSWFGSPTTSFLSISKLSPFSEFFKLRFNRKKKGMYRKAITEAANATQHVAPEIRELLTQFEM
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Chromatin-binding protein that acts as an adapter between distinct nucleosome components (H3K36me3 or H2A.Z) and chromatin-modifying complexes, contributing to the regulation of the levels of histone acetylation at actively transcribed genes. Competes with CHD4 and MBD3 for interaction with MTA1 to form a NuRD subcomplex, preventing the formation of full NuRD complex (containing CHD4 and MBD3), leading to recruitment of HDACs to gene promoters resulting in turn in the deacetylation of nearby H3K27 and H2A.Z (By similarity). Plays a role in facilitating transcriptional elongation through regulation of histone acetylation. Negatively regulates brown adipocyte thermogenesis by interacting with and stabilizing HDAC1 at the UCP1 gene promoter, thereby promoting histone deacetylation at the promoter leading to the repression of UCP1 expression.
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E9Q9R9
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DLG5_MOUSE
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Disks large homolog 5
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MEPQRRELLAQCQQSLAQAMTEVEAVLGLLEAAGALSPGERRQLDEEAGGAKAELLLQLLLAKEQDHFQDLRAALEKTQPHLLPILYLNGVVGPPQSTEGAGSTYSVLSIMPSDSESSSSLSSVGTTGKAPSPPPLLTEQQANDTVENLSIQLRLMTRERNELRKRLAFATHGATFDKRPYHRLNPDYERLKIQCVRAMSDLQSLQNQHTNALKRCEEVAKETDFYHTLHSRLLSDQTQLKDDVDMLRRENGKLRRERNLLQQSWEDMKRLREEDQKEIGDLRAQQQQVLKHNGSSEILNKLYDTAMDKLEVVKKDYDALRKRYSEKVAMHNSDLSRLEQLGEENQRLQKQTEMLTQQRDTAIQLQHQCALSLRRFETIHHELSKATAQNKDLQWEMELLQSELTELRSKQVKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEALQEADVAKCRRDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMECQLEKEARFRQLMAHSSHDSAIDTDSMEWETEVVEFERETEDIDLKALGFDMAEGVNEPCFPGDCGIFVTKVDKGSIADGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRRRKSLGGKVVTPLHINLSGQKDSGISLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLKVFPQSSSWSGQNIFENIKDSDRMLSCRAHGPEVQAHNKRNLLQHNNSTQTDIFYTDRLEDRKELGHSGGSSSFLHKPFSGSSSPVSPQACPSTSERSLNSFRSDTSAERGYGLVDMRSQRPLLSFETEVGPCGAVEVPLDKIDPEGSNSGGTWPKAVLGSTSGPEKLSVYKKPKQRKSIFDPNTFKRPQTPPKIDYLLPGPGLTHSPQPSKRVGSLTPPKPPRRSDSIKFQHRLETSSESEATLVGSSPSTSPPSAPPPSMDPSEPTHASPPRKARVRIASSYHSEGDGDTSYLPAKKPCDEDLTSQKVDELGQKRRRPKSAPSFRPKISPVVIPAQCLEEQECVPAIGELSPEGQEWSPYSPGHASRHGNPLLYPNRPSVGTVPRSMTPGTTVGSILRNPIYTVRSHRVLPCGSPPVPRDAGSQSLSPSVQHQGRLSLDLSHRACSDYSEMRASQGSNSLPSSARLGSSSNLQFKAERIKIPLTPRYPRSVMGSDRGSLSHSECSTPPRSPLNIDTLSSCSQPQTTASTLPRIAVNPSSHGERRKDRPFVEEPRHVKVQKGSEPLGISIVSGEKGGVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILAQYNPHIHQLNSHSRSSSHLDPAATPHSTLQGSSAGTPEHPSVIDPLMEQDEGPGTPPAKQSASSTRSVGDTTKKTPDPRIVFIKKSQLDLGVHLCGGNLHGVFVAEVEDDSPAKGPDGLVPGDLILEYGSLDMRSRTVEDVYVEMLKPKDSLRLKVQYRHEEFTRVKGLPGDSFYIRALYDRLAEVEPELSFKKDDILYVDDTLPQGVFGSWMAWQLDENAQKIQRGQIPSKYVMDQEFSRRLSMSEVKDDNTAKTLSAAARRSFFRRKHKHKRSGSKDGKDLLALDTFSNDSIPLFEDSVSLAYQRVQKVDCTSLRPVLLLGPLLDVVKEMLVNEAPGKFCRCPLEVMKASQQAIERGVKDCLFVDYKRRSGHFDVTTVASIKEITEKNRHCLLDIAPHAIERLHHMHIYPIVIFIRYKSAKHIKEQRDPVYLRDKVTQRHSKEQFETAQKIDQEYSRYFTGVVQGGALSSICTQILAMVSQEQSKVLWIPACPP
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Acts as a regulator of the Hippo signaling pathway. Negatively regulates the Hippo signaling pathway by mediating the interaction of MARK3 with STK3/4, bringing them together to promote MARK3-dependent hyperphosphorylation and inactivation of STK3 kinase activity toward LATS1. Positively regulates the Hippo signaling by mediating the interaction of SCRIB with STK4/MST1 and LATS1 which is important for the activation of the Hippo signaling pathway. Involved in regulating cell proliferation, maintenance of epithelial polarity, epithelial-mesenchymal transition (EMT), cell migration and invasion (By similarity). Plays an important role in dendritic spine formation and synaptogenesis in cortical neurons regulates synaptogenesis by enhancing the cell surface localization of N-cadherin. Acts as a positive regulator of hedgehog (Hh) signaling pathway. Plays a critical role in the early point of the SMO activity cycle by interacting with SMO at the ciliary base to induce the accumulation of KIF7 and GLI2 at the ciliary tip for GLI2 activation.
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E9Q9U0
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U17PB_MOUSE
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Ubiquitin carboxyl-terminal hydrolase 17-like protein B (USP17-B) (EC 3.4.19.12) (Deubiquitinating enzyme 1A)
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MVVALSFPEADPAMSPPSAPELHQDEAQVVEELAANGKHSLSWESPQGPGCGLQNTGNSCYLNAALQCLTHTPPLADYMLSQEHSQTCCSPEGCKMCAMEAHVTQSLLHTHSGDVMKPSQNLTSAFHKRKQEDAHEFLMFTLETMHESCLQVHRQSEPTSEDSSPIHDIFGGWWRSQIKCHHCQGTSYSYDPFLDIPLDISSVQSVKQALQDTEKAEELCGENSYYCGRCRQKKPASKTLKLYSAPKVLMLVLKRFSGSMGKKLDRKVSYPEFLDLKPYLSQPTGGPLPYALYAVLVHEGATCHSGHYFCCVKAGHGKWYKMDDTKVTSCDVTSVLNENAYVLFYVQQNDLKKGSINMPEGRIHEVLDAKYQLKKSGEKKHNKSPCTEDAGEPCENREKRSSKETSLGEGKVLQEQDHQKAGQKQENTKLTPQEQNHEKGGQNLRNTEGELDRLSGAIVVYQPICTAN
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Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes.
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E9Q9W4
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S27A6_MOUSE
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Long-chain fatty acid transport protein 6 (FATP-6) (Fatty acid transport protein 6) (Arachidonate--CoA ligase) (EC 6.2.1.15) (Fatty-acid-coenzyme A ligase, very long-chain 2) (Long-chain-fatty-acid--CoA ligase) (EC 6.2.1.3) (Solute carrier family 27 member 6) (Very long-chain acyl-CoA synthetase homolog 1) (VLACS2) (VLCSH1) (mVLCS-H1) (EC 6.2.1.-)
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MLLSWLTGLGAGLLSLHFLQKLLFPYFWDDFWYLLKVVRYGIQMEMYKLRGELVTVLDKFLSHTRKQPRKAFIIYEGDVYTYEDVDKRSNRIAHALLNHSSLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFDSLLHCINTCEPTAVVVGGDLLGSIEEILPSLPKHVRVWGMKDSVPEGIDSLQEKLSLASDEPVPPSHHVTSSLKSTCLYIFTSGTTGLPKAAVISQLQVLKGSVGLWAFGCTADDIIYITLPLYHSSGSLLGIGGCVELGATCVLKKKFSASQFWNDCKKYNVTVFQYIGELCRYLCKQPQREGEKDHRVRLAVGNGLSSDVWRQFLDRFGNIKMCELYGATEGNIVFMNHTGKIGSVGRANFFYSLFFSFELIKYDFQKDEPWRNGQGWCSCVRKGEPGLLISRVNKKNPFFGYAGSDTHTKSKLLFDVFRKGDVYFNTGDLMFQDQENFVYFWDRLGDTFRWKGENVATTEVADVLGRLDFIQEANVYGVRVPGYEGKAGMTSVILKPNKSLDLEKMYNQVVTSLPAYACPLFLRIQDKMETTGTFKLKKLQLVEEGFDPLKISDPLYFMDNLKKSYVPLTEEIYNQIMSEEVKL
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Mediates the import of long-chain fatty acids (LCFA) into the cell by facilitating their transport at the plasma membrane (By similarity). Also functions as an acyl-CoA ligase catalyzing the ATP-dependent formation of fatty acyl-CoA using LCFA and very-long-chain fatty acids (VLCFA) as substrates. Plays a pivotal role in regulating available LCFA substrates from exogenous sources in tissues undergoing high levels of beta-oxidation such as the heart (By similarity).
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E9Q9W7
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PDZD7_MOUSE
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PDZ domain-containing protein 7
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MARGFTVGFDPLGLGELSSGSLSSVSSRGHLGSDSGSTATRYLLRKQQRLLNGPSRGIRASSPMGRVILINSPIEANSDESDIIHAVRVEKSPSGRLGFSVRGGSEHGLGIFVSKVEEGSSAERAGLCVGDKITEVNGLSLESTTMGSAVRLLTSSSCLHMMVRRMGRVPGIKFSKEKTTWVDVVNRRLVVEKCSSTPSDRSSEDGVRRIVHLYTTSDDFCLGFNIRGGKEFGLGIYVSKVDHGGLAEENGIKVGDQVLAANGVRFDDISHSQAVEVLKGQTHIMLTIKETGRYPAYKEMVSEYCWLDRLSNGVLQQLSPASESSSSVSSYASSAPCSSGSLPSDRMDVCLGPEEPTSHGPGWGRADTAMQTEPDLDSRVETWCSVRPTVILRDTAIRSDGPSSTRHLDSALSESPKTALLLALSRPRTPITRSQSHLTLWEEKKQRKKEKSGSSGEKGALQRSKTLMNLFFKGGRQGRPAGDGHREAWTLDSRSPTKVRPRLDLEKAGSVGPVQKFVTWRLRRDRERGRALLSARSGSPSGQAPTVNEQVQAWESRRPLIQDLARRLLTDDEVLAVTRHCSRYVHEGGVEDLVRPLLAILDRPTKLLLLRDIRSVVAPTDLGRFDSMVMPVELEAFEALKSRAVGPSALRPTRQDTPPKRHLITPVPDSRGGFYLLPVNSSEDEDGEIREKLGVLKVSLGASAPHHKGIPPLQDVPVDAFSLRRGACAPPPQPPPVAPRPPRPNWLLTEPLSREDTQQNQSQTPAQSCSRSRSRSRSRSHSRGQGKSPGRRRSPSPAPIATAATANGRYHRPRKARPLLPRLLDGQVAKVGARQGPLENGRIAEEAVGNVSTGALRTITLSKMKQSLGISISGGIESKVQPMVKIEKIFPGGAAFLCGDLQAGFELVAVDGESLEQVTHQRAVDTIRRAYRNKAREPMELVVRVPGPGLLPLASDLRVVKDQSLAPDCPSALGPVDDARILTQLPPPEARQLQQSLSSALKVPQSIPKLSPILKDPHDPS
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In cochlear developing hair cells, essential in organizing the USH2 complex at stereocilia ankle links. Blocks inhibition of adenylate cyclase activity mediated by ADGRV1.
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E9QA28
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CEA16_MOUSE
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Carcinoembryonic antigen-related cell adhesion molecule 16
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MKMPLTWYSWFLLSAWILNTGAEISITPEPAQPAEGDNVTLVVHGLSGELLAYNWYAGPTLSLTFLVASYIVSTGDETPGPAHTGREAVRPDGSLDIHGALPGHTGTYILQTLNRQFQTEVGYGHMQVYEILAPPTVMANDTALVERRDTLRLVCSSPSPAEVRWFFNGDALPVAVRLGMSPDGRMLTRHGVRREEAGAYQCEVWNPVSVSRSEPLNLTVYFGPERVAILQDSTTRTGCTIKVDFNMSLTLWCVARSCPEPEYVWAFNGKALKNGQDHLNISSMTAAHEGTYTCIAKNSKTLLSGSASVVVKLSAAAVAMMIVPVPTKPTEGQDVTLTVQGYPKDLLVYAWYRGPASEPNRLLSQLPSGNWIAGPAHTGREVGFANCSLLVQKLNLTDAGRYTLKTVTLQGKTDTLEVELQVAPLE
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Required for proper hearing, plays a role in maintaining the integrity of the tectorial membrane.
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E9QA62
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LMOD3_MOUSE
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Leiomodin-3
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MSGHSRNSEQEDTLSEELDEDELLANLSPEELKELQSEMEVMAPDPHLPVGMIQKDQTDKAPTGNFNHKSLVDYMYLQKASRRMLEDERVPVSFVQSEKNTQNQREVGDKGIKNMPQFLKEKLNSEILAKKRESNGSNNVQEAEDDDEDEEEEEEDDEDEEEEEEDEEDDEGEEDEDGEQANREKNDAKEQIHNNPGTYQQLATKTAHEQKDTSETKEKGEKKIAKLDPKKLALDTSFLKVSARPSGNQTDLDGSLRRVRQNDPDMKELNLNNIENIPKEMLLDFVNAMKKNKHIKTFSLANVGADESVAFALANMLRENRSVTTLNIESNFITGKGIVAIMRCLQFNETLTELRFHNQRHMLGHHAEMEISRLLKANTTLLKMGYHFELPGPRMVVTNLLTRNQDKRRQKRQEEQQQQQLKEQRKLIAMLENGLGLPPGMWERLGGPMPDPRMQEFFQPASGRPLDAQEVPFGSRKEMIKNPPQPPQCKTDPDSFRVVKLKRIQRKSRMPEAREAQEKTNLKDVIKTLKPVPRNRPPPLVEITPRDQLLNDIRHSNVAYLKPVQLPKELE
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Essential for the organization of sarcomeric actin thin filaments in skeletal muscle. Increases the rate of actin polymerization (By similarity).
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E9QAG8
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ZN431_MOUSE
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Zinc finger protein 431 (Zinc finger protein 932)
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MVDALTYDDVYVNFTQEEWALLNPSQKSLYKDVMLETYRNLNAVGYNWEDSNIEEHCESSRRHGRHERNHTGEKPYEGIQYGEAFVHHSSLQMRKIIHTGEKRYKCNQCDKAYSRHSILQIHKRTHSGEKPYECNQCGKAFTQHSHLKIHMVTHTGEKPYKCDQCGKAFAFHSTLQVHKRTHTGEKPYECNQCSKAFAHHCHLRVHKRIHTGEKPYKCDQCGKAFVGQNDLKRHERVHTGEKPYKCNECGKAFVCNASLRTHKTTHTGVKPYECKQCTKSFASHGQLQKHERIHTGEKPYKCDQCGKAFASHDKFQKHERIHIGEKPYKCKQCTKSFASHDKLQKHERIHTGEKPYECKQCTKSFASHNKLQKHERIHTGEKPYKCDQCNKAFVYESYLQVHKKTHTGEKPYKCNECGKAFARHSHLKVHKITHTGEKPYKCNQCGKALAYHSTLQVHQRTHTGEKPYECEQCGKAFANQSYFQVHKRIHTGEKPYKCDQCGKAFVGSSDLKRHERVHTGRETLQM
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Sequence-specific DNA binding transcriptional repressor. Represses target gene transcription by recruiting HDAC1 and HDAC2 histone deacetylases. Acts as a specific transcriptional repressor for PTCH1 during embryonic development. Required for osteoblast differentiation and sonic hedgehog/SHH signaling response. Binds to the consensus site 5'-GCGCCC-3' in the promoter of PTCH1.
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