entry
stringlengths 6
10
| entry_name
stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
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A1Z9P3
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SHRM_DROME
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Protein Shroom
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MKMRNHKENGNGSEMGESTKSLAKMEPENNNKISVVSVSKLLLKDSNGANSRSSNSNASFSSASVAGSVQDDLPHHNSSSSQLGQQHGSSLDQCGLTQAGLEEYNNRSSSYYDQTAFHHQKQPSYAQSEGYHSYVSSSDSTSATPFLDKLRQESDLLSRQSHHWSENDLSSVCSNSVAPSPIPLLARQSHSHSHSHAHSHSNSHGHSHGHAHSASSSSSSNNNSNGSATNNNNNNSSESTSSTETLKWLGSMSDISEASHATGYSAISESVSSSQRIVHSSRVPTPKRHHSESVLYLHNNEEQGDSSPTASNSSQMMISEEANGEESPPSVQPLRIQHRHSPSYPPVHTSMVLHHFQQQQQQQQDYQHPSRHHTNQSTLSTQSSLLELASPTEKPRSLMGQSHSMGDLQQKNPHQNPMLGRSAGQQHKSSISVTISSSEAVVTIAPQPPAGKPSKLQLSLGKSEALSCSTPNMGEQSPTNSIDSYRSNHRLFPVSTYTEPVHSNTSQYVQHPKPQFSSGLHKSAKLPVITPAGATVQPTWHSVAERINDFERSQLGEPPKFAYLEPTKTHRLSNPALKALQKNAVQSYVERQQQQQKEEQQLLRPHSQSYQACHVERKSLPNNLSPIMVGLPTGSNSASTRDCSSPTPPPPPRRSGSLLPNLLRRSSSASDYAEFRELHQAQGQVKGPSIRNISNAEKISFNDCGMPPPPPPPRGRLAVPTRRTSSATEYAPMRDKLLLQQAAALAHQQHHPQQHRHAQPPHVPPERPPKHPNLRVPSPELPPPPQSELDISYTFDEPLPPPPPPEVLQPRPPPSPNRRNCFAGASTRRTTYEAPPPTAIVAAKVPPLVPKKPTSLQHKHLANGGGGSRKRPHHATPQPILENVASPVAPPPPLLPRARSTAHDNVIASNLESNQQKRSNSKASYLPRQSLEKLNNTDPDHGIYKLTLTSNEDLVAHTKPSYGVTGKLPNNLPDVLPLGVKLHQQPKLQPGSPNGDANVTLRYGSNNNLTGNSPTVAPPPYYGGGQRYSTPVLGQGYGKSSKPVTPQQYTRSQSYDVKHTSAVTMPTMSQSHVDLKQAAHDLETTLEEVLPTATPTPTPTPTPTPPRLSPASSHSDCSLSTSSLECTINPIATPIPKPEAHIFRAEVISTTLNTNPLTTPPKPAMNRQESLRENIEKITQLQSVLMSAHLCDASLLGGYTTPLITSPTASFANEPLMTPPLPPSPPPPLEPEEEEEQEENDVHDKQPEIEELQLMQRSELVLMVNPKPSTTDMACQTDELEDRDTDLEAAREEHQTRTTLQPRQRQPIELDYEQMSRELVKLLPPGDKIADILTPKICKPTSQYVSNLYNPDVPLRLAKRDVGTSTLMRMKSITSSAEIRVVSVELQLAEPSEEPTNLIKQKMDELIKHLNQKIVSLKREQQTISEECSANDRLGQDLFAKLAEKVRPSEASKFRTHVDAVGNITSLLLSLSERLAQTESSLETRQQERGALESKRDLLYEQMEEAQRLKSDIERRGVSIAGLLAKNLSADMCADYDYFINMKAKLIADARDLAVRIKGSEEQLSSLSDALVQSDC
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Binds to Rho-kinase Rok and targets it to the apical cell cortex where it mediates apical constriction. During embryogenic axis elongation, required for the localization to adherens junctions and the establishment of planar polarization of both Rho-kinase Rok and myosin regulatory light chain sqh. May be involved in the assembly of microtubule arrays during cell elongation (By similarity).
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A1Z9S1
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BL1S1_DROME
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Biogenesis of lysosome-related organelles complex 1 subunit 1 (BLOC-1 subunit 1)
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MLTSMVKEHHKEQAKRKQEQEVRRKEAIEASNELTQSLVDTLNVGVAQAYLNQKRLDAEAKQLHLGATNFAKQTHQWLQLIDQFSTALKDLGDVENWARSIEGDMHTINQTLELAYKASRATQTSSGAGTSLEASTSASASANPSAT
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Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) involved in pigment granule biogenesis and membrane trafficking in synapses. In response to high synaptic activity at neuromuscular junctions, stabilizes Pldn protein levels and, together with Pldn, plays a role in promoting efficient synaptic vesicle recycling and re-formation through early endosomes.
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A1Z9X0
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APKC_DROME
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Atypical protein kinase C (EC 2.7.11.13)
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MQKMPSQILNDGSSVSLNSASMNMANTPNSITVKTAYNGQIIITTINKNISYEELCYEIRNICRFPLDQPFTIKWVDEENDPCTISTKMELDEAIRLYEMNFDSQLVIHVFPNVPQAPGLSCDGEDRSIYRRGARRWRKLYRVNGHIFQAKRFNRRAFCAYCQDRIWGLGRQGFKCIQCKLLVHKKCHKLVQKHCTDQPEPLVKERAEESSDPIPVPLPPLPYEAMSGGAEACETHDHAHIVAPPPPEDPLEPGTQRQYSLNDFELIRVIGRGSYAKVLMVELRRTRRIYAMKVIKKALVTDDEDIDWVQTEKHVFETASNHPFLVGLHSCFQTPSRLFFVIEFVRGGDLMYHMQRQRRLPEEHARFYAAEISLALNFLHEKGIIYRDLKLDNVLLDHEGHIKLTDYGMCKEGIRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLLYEMLAGRSPFDLAGASENPDQNTEDYLFQVILEKTIRIPRSLSVRAASVLKGFLNKNPADRLGCHRESAFMDIVSHPFFKNMDWELLERKQVTPPFKPRLDSDRDLANFPPEFTGEAVQLTPDDDHVIDNIDQSEFEGFEYVNPLLMSLEDCV
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Serine/threonine protein kinase which is required for apico-basal cell polarity in the germ line as well as in epithelial and neural precursor cells, for epithelial planar cell polarity and for cell proliferation. During oocyte development, required for the posterior translocation of oocyte specification factors and for the posterior establishment of the microtubule organizing center within the presumptive oocyte. Phosphorylates l(2)gl which restricts l(2)gl activity to the oocyte posterior and regulates posterior enrichment of par-1, leading to establishment of correct oocyte polarity. Essential for apical localization of l(2)gl and par-6 in neuroblasts and for exclusion of mira from the apical cortex. Phosphorylates baz which is required for targeting of baz to the postsynaptic region where it is involved in actin organization, and for apical exclusion of baz which is necessary for establishment of the apical/lateral border in epithelial cells. Phosphorylates yrt which prevents its premature apical localization and is necessary for correct epithelial cell polarization. Required for the establishment of mitotic spindle orientation during symmetric division of epithelial cells and for apical exclusion of raps/Pins. Involved in symmetric adherens junction positioning during embryogenesis. Required for polarization of the spermatid cyst which is necessary for sperm differentiation. Required for stimulation of the Toll signaling pathway which activates Dif and dl and plays a role in innate immunity. Plays a role in memory enhancement.
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A1ZA47
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ZASP_DROME
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PDZ and LIM domain protein Zasp (Z band alternatively spliced PDZ-motif protein)
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MAQPQLLQIKLSRFDAQPWGFRLQGGTDFAQPLLVQKVNAGSLSEQAGLQPGDAVVKINDVDVFNLRHKDAQDIVVRSGNNFVITVQRGGSTWRPHVTPTGNVPQPNSPYLQTVTKTSLAHKQQDSQHIGCGYNNAARPFSNGGDGGVKSIVNKQYNTPVGIYSDESIAETLSAQAEVLAGGVLGVNFKKNEKEYQGDRSEVLKFLREEETGQSTPAFGNSHYEHDAPQQLQQPQQQYNQHQQHYHQQQQQQQSSTTRHVSAPVNSPKPPSTGGLPTGQNICTECERLITGVFVRIKDKNLHVECFKCATCGTSLKNQGYYNFNNKLYCDIHAKQAAINNPPTGTEGYVPVPIKPNTKLSASTISSALNSHGYGGHSNGYSNGNSTPAPAPVASSQATATVATVAPSAATAATAAATPQAATATDSPAATASSSDNMSAYVADEPSSIYGQISAESVALAPPPPQPPTAGGGDQPFEYVTLTGNVIRSVQAPGKGACPSYKVNQGYARPFGAAAPKSPVSYPPQQQQQSPRPAPGGQNPYATLPRSNVGQQGGEAVEELQPEFEEEDCYEMDIEVALAASRQSQRGSSFTWPPPQDDSHLAPTAAPLYIPPPETQHVVVSNPVQQVPPLPPGGATARLDPQPVVGTSANGAPQWQSYSAPQLTTASARQLAEQESSSDSYTSTSTTTTTTSEEYQRMYAAQVQAYQMQEQSGSEFDYQVDYASTQDSVQDYPSGRRSAQECVDSLAVPLSTYKLVDMVREVTPSPVTTPTQTPAPAAPTTRRVVFNDEPEIKELPQLPAELETIPEASEAVEDREGLVIEQRCQILESERKFQPTPEIKIEIAPVRQIPPTKIPNPMPKEWINPMIRVLTTAPEVPFHLVECPFPRPCGDDFEAEAAAAEAAKTQEVPEPLPPQVSAAPPATVSVEPSPAPLRESPPRGSRLSQAMVTAPEFELKFAPPADQGIPLPEETEPYMPPPIDTKPYLREDYRPKSPFVSALTTAPDRPFEGHFDKDVPIHMIDLPTPKEHLSMCDALCTAPERGYTPLNPENAMHRVDEEQKQQELKKREFQVLDHEEELGIRPEPPQSVEYYETRRDQPRKSSAFAAMQAFQPSREPLSSNTVSNAGSVADTPRASIVSALKEETDLEYQKYLKAQQRNQKRLDYFHQKEEELSGLQGQQLTQLQRELSNQQQNLLSQQQLQQSKLLQLQQCVQSQELQQQVQHLTQKSQQQPPQANQQQQQQQQQRGTQQQQHSQVTQRTQQQQQQVPQQVTQQQQQEHSLLSQTTLAETQTLQANAQSQSSASYSSKATACSNSSSTVPPANTSTAFAPAPAPAPTSIPVRPSAIAVQSSYCSSQFDVHELIEETAEELEHSEVLFPPPSPLSHLTKQGKAVQSGLHKADSIPKYQRNWTVLPTQSPIRTPEPQELRENVPLAFVDAPKAPVTSDSSTVHRPIAQVAAPTTVVAPSREREKERRPQLSVPIIVEDRSGPVTMAFQPLDELVRPDQALTPTRPYTPSLTNKPAPIVPFYQTEEKLVFEECSATHARNYNELNASPFPDRTRSPAPGPPPNPLNAIRAPRMKEPETKSNILSVSGGPRLQTGSITTGQSYQGQLLAHSEQSSQSASQSYNQQPERITEQRVGNLNIQQREQSSQLQQQAQSQTQSQTRSQVGNTQIERRRKVTEEFERTQSAKTIEIRTGSQSVSQSKAQSQSISQAQTQAQSQSQNQSDTERRSSYGKTGFVASQAKRLSCMEEEISSLTSQSQAISARASALGEGCFPNLRSPTFDSKFPLKPAPAESIVPGYATVPAATKMLTAPPPGFLQQQQQQQQRSAFSGYQATTSSVQQSSFASSSKATTSSLSSSSASASASASVARSSQSLTQASAITTTTNNQATTAYRSSNGSITKPNLASRPSIASITAPGSASAPAPVPSAAPTKATAPFKAPIVPKSVIANAVNAAAPPAPAVFPPDLSDLNLNSNVDNSPGAGGKSAGAFGATSAPKRGRGILNKAAGPGVRIPLCNSCNVQIRGPFITALGRIWCPDHFICVNGNCRRPLQDIGFVEEKGDLYCEYCFEKYLAPTCSKCAGKIKGDCLNAIGKHFHPECFTCGQCGKIFGNRPFFLEDGNAYCEADWNELFTTKCFACGFPVEAGDRWVEALNHNYHSQCFNCTFCKQNLEGQSFYNKGGRPFCKNHAR
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Regulator of cell matrix adhesion having two related functions, one upstream of Actn organizing the Z line and the other downstream of integrins regulating assembly of integrin adhesion sites. Also required for the formation of myotendinous junctions in muscles.
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A1ZA55
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CGLR1_DROME
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Cyclic GMP-AMP synthase-like receptor 1 (cGLR1) (EC 2.7.7.-)
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MAMNLENIVNQATAQYVKIKEHREPYTAHYNALKDKVYSEWKSSAVLGKLLKGSTLCGGYGDKLKVSIPDEFDLLIHLVFPENDKIIVKADASKPGNVILDMTKVMEIIGSQEHNKPVFDRLQKIVNNKKQLLEDKLNSFLESIMTQTLNKMGNQIEVAGRISHLQYKKCGPAHTIFVKGSCKYSVDFVPAIRLSAAQVVLAPEQRIHFGETLYWDAIPKPMKPAKTDNTSFTSSFYEAERRLLYGKQFLKPAIRLMKQNRNVKNKANLKSYHIKTLFLWQVIQQDPSYWSNSPKDIFIEMLGKLADSLALTPKKGKLPFFWDPKLDMFAQLTDSQRTDLYNHFRKCEYTFRKDNGNVNDCTENNVHSSFSKNTTYKL
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Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (3',2'-cGAMP) from ATP and GTP and plays a key role in antiviral innate immunity. Synthesizes 3',2'-cGAMP in a two-step reaction through production of the linear intermediate pppA(2'-5')pG. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 3',2'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the antiviral immune response via activation of the NF-kappa-B transcription factor Rel (Relish). 3',2'-cGAMP is protected from poxin cleavage.
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A1ZAB5
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CLU_DROME
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Protein clueless (Clustered mitochondria protein homolog)
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MALETEAKNSNATATGDATATATKASGKAKENNNTAGGKKNLNPNSNQQNSNQNLVNGNGTAADGPAAKKKGKKNRNKSPTEPTTEAVLSNGHAEKPTVVDAVEDNADTNANVEKPQEGGAPDAEADGDDIDLDALQDIGITVNISSPGADLLCVQLSSMELVQEIHQLLMDREETCHRTCFSLQLDNVTLDNFAELKSINNLEQGSTIKVVEEPYTMREARIHVRHVRDLLKNLDPADAYNGIDCTSLTYLNTITQGDLLDKKRTRPDSVDCTPPEYVTPGVSDPPILPLHPNVKNAKGPQALKVLTTSAWNPPPGPRKLHGDLMYLYVVTMEDKRFHISACSKGFFINQSTDDTFNPKPDNPSHLSHSLIDLLSHISPSFRRAFQTIQKRRTMRHAFERVATPYQVYQWAAPILEHTVDAIRAEDAFSSKLGYEEHIPGQTRDWNEELQTTRELPRKTLPERLLRERAIFKVHGDFVTAATRGAMAVIDGNVLAINPGEDTKMQMFIWNNIFFSMGFDVRDHYKELGGDAAAFVAPRYDLHGVRVYNAVDIEGLYTLGTVVVDYRGYRVTAQSIIPGILEREQEQSVVYGSIDFGKTVLSHPKYLELLRQAGKHLKILPHVVLNERDEPVELCSSVECKGIIGNDGRHYILDLLRTFPPDVNFLKLQDVQLSKELVDMGFPIEHRHKLCCLRQELLEAFIEDRHVNFIRIAAARLQQLTTIKQSEKSEANPVPALEGAEAASKVNGAEKPDDKEKKNEEEEKKERSTSGEARAAAIVNAIREAQSNVATSNEVQAAEVVKRACAAVGSLKEKEFDFRFNPDVFSPGIRHADGEEGTSLAKQKVLVQEAAEFLVLKQIPAFIKEHMSHSSSPIDGQSLTESLHSHGINVRYLGKVIKILSQMPRMDYLHRIAVLELIVRATKHIYYTYMQNTEPLHLSAAISHFLNCLLTNGPVNPAVSSEEAHKKRGNGGKHNKHKSSKGGKGQQQQQTTGNQNGSSSGSSNSSSASDWTLMTPRSLWQQIRKEAKVYWDWELDCDSIETAVSKYGILRISLMRAFCLKVGIQVLLREYNFESKHKPTFGDDDIVNVFPIVKHISPRATDAYNFYTTGQAKIQQGLFKEGYELISGALNLLNNVFGALHQENGSCLRMLARLSYLLGDAQDALAIQQRAVIMSERVNGMDHPSTILEYTHLSLYSFANGHVGMSLKLLYRARYLMVLICGEDHPEVALIDSNISLILHALGEYELSLRFIEHALKLNLKYFGDKDMHVALSYHLMARTQSCMGDFRSALNNEKETYSFYKSQLGENHEKTRDSAECLRLLTQQAVLLQRKMNDIYSSGKLTSDLPPIHITPPSMGSVLDMLNTINGILFVKISRKDIVKVRSEIEKHFKTDSTENEVNDAINSIVAAANNNGEAEDAVSKDIKEQPEAGKQLTNGDKAAATEATSS
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mRNA-binding protein involved in proper cytoplasmic distribution of mitochondria. {ECO:0000255|HAMAP-Rule:MF_03013, ECO:0000269|PubMed:19638420}.
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A1ZAJ2
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KIF1A_DROME
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Kinesin-like protein unc-104 (Protein immaculate connections) (DUnc104)
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MSSVKVAVRVRPFNSREIARESKCIIEMAGATTAITNPKVPPNTSDSVKRFNFDYSYWSHDHHDADFSTQSMVYKDIGEEMLQHSFDGYNVCIFAYGQTGAGKSYTMMGRQEEQQEGIIPMICKDLFTRIQDTETDDLKYSVEVSYMEIYCERVRDLLNPKNKGNLRVREHPLLGPYVEDLSKLAVTDYQDIHDLIDEGNKARTVAATNMNETSSRSHAVFTIFFTQRRHDLMTNLTTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVASKKKNTKKADFIPYRDSALTWLLRENLGGNSKTAMIAAISPADINYDETLSTLRYADRAKQIVCKAVVNEDANAKLIRELKEEIQKLRDLLKAEGIEVQEEDELTKSTVIKSPTKSRNRNGSTTEMAVDQLQASEKLIAELNETWEEKLKRTEEIRVQREAVFAEMGVAVKEDGITVGVFSPKKTPHLVNLNEDPNLSECLLYYIKEGLTRLGTHEANVPQDIQLSGSHILKEHCTFENKNSTVTLLPHKDAIIYVNGRKLVEPEVLKTGSRVILGKNHVFRFTNPEQARELRDKIETENEAENEVEKTDTQQVDWNFAQCELLEKQGIDLKAEMKKRLDNLEEQYKREKLQADQQFEEQRKTYEARIDALQKQVEEQSMTMSMYSSYSPEDFHQEEDVYTNPMYESCWTAREAGLAAWAFRKWRYHQFTSLRDDLWGNAIFLKEANAISVELKKKVQFQFTLLTDTLYSPLPPELASTVAPVHQEDEFGAPPVSKTLVAVEVTDTKNGATHHWSLEKLRQRLELMREMYHNEAEMSPTSPDYNVESLTGGDPFYDRFPWFRMVGRSFIYLSNLLYPVPLVHKVAIVNERGDVRGYLRIAVQPVLDEESIDFNNGVKQSARLVFNEDDAKPKYRALNEKDDVQRYIDNGGLDSKLEELEDVDSGRGIDSNSASECHENSEEPGEHLQVGKEFTFRVTVLQATGIGAEYADIFCQFNFLHRHEEAFSTEPVKNSASGAPLGFYHVQNITVPVTKSFIEYLKTQPIMFKIFGHYQTHPLHKDAKQDFVSRPPPRRMLPPSIPISQPVRSPKFGPLPCAPTSTVLAKHDVLVWFEICELAPNGEYVPSVVEHSDDLPCRGLFLLHQGIQRRIRITIVHEPTTEVKWKDINELVVGRIRNTPESSDEQDEDACVLSLGLFPGEALEVPGDDRSFYRFEAAWDSSLHNSALLNRVSQGGETIYITLSAYLELENCARPAIITKDLSMVIYGRDARTGPRSLKHLFSGQYRNPEANRLTGVYELALRRASEAGSPGVQRRQRRVLDTSSTYVRGEENLHGWRPRGDSLIFDHQWELEKLTRLEEVGRMRHLLLLRERLGMDTNPNPTTKTEKDVCNLAARAATSPVHMVIPQSPQTPVKDPQQIIPEREYNQREQDLMLKCLKLVQGRYTKSEANDTQTQSDVSPSDEGCADMTVSCISSNSMENNKFVIRRRLCSPDRADAPNGWEAPAPATQPALPLRLYVPELEEIRVSPVVARKGLLNVLEHGGSGWKKRWVIVRRPYVFIYRSEKDPVERAVLNLATAHVECSEDQAAMVKIPNTFSVVTKHRGYLLQTLGDKEVHDWLYAINPLLAGQIKSRLARRTLEPASQTASQIQATNAANANSASK
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Required for presynaptic maturation, has a role in axonal transport of dense-core vesicles carrying synaptic vesicle precursors, components required for the morphological transformation of axonal growth cones to mature boutons.
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A1ZAU8
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PTRO_DROME
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Patronin (Short spindle protein 4)
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MDVETQEIRQARQRASVKWLLSKAFNNRVPDNLKEPFYRDHENQERLKPQIIVELGNATLYCQTLANLYSDPNYQSMNHWSIIQTLARKGVPVAESADMPITETVLIQTNPLRINAHMSVIESLMVLYAKEISSGDRVMAAIRRISGNNYQAPTGQSYEQALLGWISHACAALKKRIIKEVDAGLPDDNGSRLQTPDIPPVRDFQDLCDGICLALLISYYCPKVVPWTSVRINYLPAVEDSIHNILLVCNFSQKHLPYTVMHMTPEDVTYMRGSMKLNLVVLLTDLFNLFEIHPAKCVCYPGMDGQVPHSNSFGGGLNRRSTPPNEYQTVQSNNFDGNHAEAFVVHKSRGITTLASMHSQQQQQLHQQQQHQQQYHQQPLQQHPSQSQLQIQQQEPLVPARLRQAKEKTNVESKADERGRRSRRNSSSEDSQLTIENFGGSQDQLNTLGRYERDRERKLSNTSVGSYPVEPAVAVRSSIADARGTLQLGYDTDSGSEKQDRETEKYSMRRQVSVDNVPTVSSHNLSNAGSPLPVARHKQHSSDKDYSSNSGMTPDAYNDSRSTSGYDPESTPVRKSSTSSMPASPAAWQLDVGDDDMRSLENASKLSTIRMKLEEKRRRIEQDKRKIEMALLRHQEKEDLESCPDVMKWETMSNESKRTPDMDPVDLDKYQQSIAIMNMNLQDIQQDIHRLATQQSQMQAQHLQAQQLMQAQQIANMLNQAYNAPVSAYSSRPPSRDPYQQQLHHQQQQPMPMPQPMQYVNEHGQYMSPPQPAHYMPQQAQQPQSIYSDNGAAYNHSNHSPYGGTPQYRSSVVYDDYGQPTNHFYLHESSPQPQAHQHPQRRTWAHSAAAAAYEQQQQIQPSLVDVNAWQTQQHQKQKQTWMNRPPSSAGAPSPGSFMLHQNGGGGGGGGGGGELQHLFQVQASPQHGQRQVSGSNGVQRQQSLTNLRDNRSPKAPQNMGMPMGMPMQQEDMMAPQSICFIGDEEDVDELERNIIESMQSTHISDFVHQQQQQHQHQQQLQQQQRLQGHSGRGSSSEDYDSGEMISNKLNITSGNLTYRIPSPSRPSIQANSFQDPRAMAAASGGEDQPPEKGFYISFDDEQPKRPKPPLRAKRSPKKESPPGSRDSVDNQATLKRESLSHLHNNNNIGFGNDDVNSKPVTRHSIHGLNNSNSVKSPGNATYNKYTDEPPIQLRQLAVSGAMSPTSNERHHLDDVSNQSPQQTQQPMSPTRLQQSSNNAEAAKNKALVIGADSTNLDPESVDEMERRKEKIMLLSLQRRQQQEEAKARKEIEASQKREKEREKEEERARKKEEQMARRAAILEQHRLKKAIEEAEREGKTLDRPDLHVKLQSHSSTSTTPRLRQQRTTRPRPKTIHVDDASVDISEASSISSRGKKGSSSNLTGYGQLSSNSMKRDYYRGSQDSLTVKESPDDYPSTSSTPIGRRGSYKTSREPAGVERGRTLSRISVAKGSTLNFRGRKSNSLMNLCGPKLYKQPAAKSNRGIILNAVEYCVFPGVVNREAKQKVLEKIARSEAKHFLVLFRDAGCQFRALYSYQPETDQVTKLYGTGPSQVEEVMFDKFFKYNSGGKCFSQVHTKHLTVTIDAFTIHNSLWQGKRVQLPSKKDMALVI
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Involved in mitotic spindle assembly. Regulates microtubule (MT) severing. Antagonizes the activity of the kinesin-13 depolymerase Klp10A thereby switching off the depolymerization of the MTs at their pole-associated minus ends, which turns off poleward flux and induces anaphase B spindle elongation. Involved in asymmetric cell division of sensory organ precursor (SOP) cells by playing a role in the asymmetric localization of Sara-expressing endosomes to the pIIa daughter cell but not to the pIIb cell. Klp98A targets Sara-expressing endosomes to the central spindle which is symmetrically arranged in early cell division. During late cytokinesis, central spindle asymmetry is generated by enrichment of Patronin on the pIIb side which protects microtubules from depolymerization by Klp10A while unprotected microtubules on the pIIa side are disassembled by Klp10A, leading to the asymmetric delivery of Sara-expressing endosomes to the pIIa daughter cell.
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A1ZAW0
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DCR2_DROME
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Endoribonuclease Dcr-2 (Protein Dicer-2) (EC 3.1.26.3)
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MEDVEIKPRGYQLRLVDHLTKSNGIVYLPTGSGKTFVAILVLKRFSQDFDKPIESGGKRALFMCNTVELARQQAMAVRRCTNFKVGFYVGEQGVDDWTRGMWSDEIKKNQVLVGTAQVFLDMVTQTYVALSSLSVVIIDECHHGTGHHPFREFMRLFTIANQTKLPRVVGLTGVLIKGNEITNVATKLKELEITYRGNIITVSDTKEMENVMLYATKPTEVMVSFPHQEQVLTVTRLISAEIEKFYVSLDLMNIGVQPIRRSKSLQCLRDPSKKSFVKQLFNDFLYQMKEYGIYAASIAIISLIVEFDIKRRQAETLSVKLMHRTALTLCEKIRHLLVQKLQDMTYDDDDDNVNTEEVIMNFSTPKVQRFLMSLKVSFADKDPKDICCLVFVERRYTCKCIYGLLLNYIQSTPELRNVLTPQFMVGRNNISPDFESVLERKWQKSAIQQFRDGNANLMICSSVLEEGIDVQACNHVFILDPVKTFNMYVQSKGRARTTEAKFVLFTADKEREKTIQQIYQYRKAHNDIAEYLKDRVLEKTEPELYEIKGHFQDDIDPFTNENGAVLLPNNALAILHRYCQTIPTDAFGFVIPWFHVLQEDERDRIFGVSAKGKHVISINMPVNCMLRDTIYSDPMDNVKTAKISAAFKACKVLYSLGELNERFVPKTLKERVASIADVHFEHWNKYGDSVTATVNKADKSKDRTYKTECPLEFYDALPRVGEICYAYEIFLEPQFESCEYTEHMYLNLQTPRNYAILLRNKLPRLAEMPLFSNQGKLHVRVANAPLEVIIQNSEQLELLHQFHGMVFRDILKIWHPFFVLDRRSKENSYLVVPLILGAGEQKCFDWELMTNFRRLPQSHGSNVQQREQQPAPRPEDFEGKIVTQWYANYDKPMLVTKVHRELTPLSYMEKNQQDKTYYEFTMSKYGNRIGDVVHKDKFMIEVRDLTEQLTFYVHNRGKFNAKSKAKMKVILIPELCFNFNFPGDLWLKLIFLPSILNRMYFLLHAEALRKRFNTYLNLHLLPFNGTDYMPRPLEIDYSLKRNVDPLGNVIPTEDIEEPKSLLEPMPTKSIEASVANLEITEFENPWQKYMEPVDLSRNLLSTYPVELDYYYHFSVGNVCEMNEMDFEDKEYWAKNQFHMPTGNIYGNRTPAKTNANVPALMPSKPTVRGKVKPLLILQKTVSKEHITPAEQGEFLAAITASSAADVFDMERLEILGDSFLKLSATLYLASKYSDWNEGTLTEVKSKLVSNRNLLFCLIDADIPKTLNTIQFTPRYTWLPPGISLPHNVLALWRENPEFAKIIGPHNLRDLALGDEESLVKGNCSDINYNRFVEGCRANGQSFYAGADFSSEVNFCVGLVTIPNKVIADTLEALLGVIVKNYGLQHAFKMLEYFKICRADIDKPLTQLLNLELGGKKMRANVNTTEIDGFLINHYYLEKNLGYTFKDRRYLLQALTHPSYPTNRITGSYQELEFIGDAILDFLISAYIFENNTKMNPGALTDLRSALVNNTTLACICVRHRLHFFILAENAKLSEIISKFVNFQESQGHRVTNYVRILLEEADVQPTPLDLDDELDMTELPHANKCISQEAEKGVPPKGEFNMSTNVDVPKALGDVLEALIAAVYLDCRDLQRTWEVIFNLFEPELQEFTRKVPINHIRQLVEHKHAKPVFSSPIVEGETVMVSCQFTCMEKTIKVYGFGSNKDQAKLSAAKHALQQLSKCDA
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Double-stranded RNA (dsRNA) endoribonuclease which cleaves endogenous (endo), exogenous (exo), and viral dsRNAs to produce short interfering RNAs (siRNAs). The generated siRNAs then mediate gene silencing, also called RNA interference (RNAi), by controlling the elimination of endogenous transcripts from mobile and repetitive DNA elements of the genome as well as exogenous RNA of viral origin. Also acts in an RNAi-independent manner to activate translation through cytoplasmic polyadenylation. As well as its role in dsRNA processing, essential in several steps of the siRNA biogenesis pathway, including siRNA loading into the Argonaute2 (Ago2)-containing RNA-induced silencing complex (RISC), length-dependent dicing and guide strand selection for target silencing by the RISC. Cleaves dsRNAs into siRNAs that are predominantly around twenty-one nucleotides in length. Displays a preference for binding and processing blunt termini (BLT), likely non-self dsRNAs, over dsRNAs with 2 nucleotides 3' overhanging (3'ovr) termini, which are typically the structure of endogenous dsRNAs. According to many reports, the cleavage reaction mode of the enzyme changes according to the termini of the dsRNA substrate. BLT dsRNAs undergo an ATP-dependent processive reaction whereby multiple siRNAs of heterogeneous sizes are produced before the enzyme dissociates. In contrast, dsRNAs with 3'ovr termini, which are typically the structure of endogenous dsRNAs, undergo ATP-independent, distributive cleavage whereby the enzyme dissociates after each cleavage to produce siRNAs of around 22 nucleotides. However, according to another report, the mode of cleavage reaction is not affected by the terminal structures of the dsRNAs substrates. This report suggests that the enzyme is able to initiate processive cleavage of both BLT and 3'ovr dsRNA substrates, and only rarely initiates distributive cleavage. During dsRNA processing and Ago2-loading, requires association with dsRNA-binding accessory proteins loqs isoform PD (loqs-PD) and r2d2. Functions with r2d2 to form the RLC which is responsible for Ago2-loading of endo- and exo-siRNAs. Interaction with loqs-PD increases initial binding to dsRNA substrates and promotes processing of a subset of endo- and exo-dsRNAs. In the absence of r2d2, may also form an alternative RLC with loqs-PD to load siRNAs into the RISC. Many reports suggest that loqs-PD and r2d2 function independently with dcr-2 in distinct siRNA pathways, and may compete for binding to the enzyme. However, another report proposes that loqs-PD and r2d2 function with dcr-2 sequentially in the same RNAi pathway, with loqs-PD promoting dcr-2 cleavage of endo- and exo-siRNAs, and r2d2 and dcr-2 forming the RLC which loads both types of siRNAs into Ago2. Function with loqs-PD allows the dicer enzyme to cleave dsRNA templates independently of their termini, and is required for ATP-dependent processing of a subset of siRNAs but is not required for antiviral RNAi. This suggests that the enzyme's intrinsic termini preferences function in viral defense, while function with loqs-PD allows processing of endogenous dsRNAs with diverse termini. However, according to another report the mode of cleavage reaction is not affected by the presence or absence of loqs-PD. Loaded siRNAs serve as a guide to direct the RISC to complementary RNAs to degrade them or prevent their translation. The RLC plays an important role in the ATP-dependent asymmetry sensing of the duplex, and is therefore also responsible for the selection of the strand that ultimately acts as the guide siRNA for the RISC. Thermodynamically asymmetric siRNAs are preoriented in the RLC by the dsRNA-binding r2d2 protein which preferentially bind to the most thermodynamically stable strand prior to loading onto Ago2. Both r2d2 and Dcr-2 also initiate unwinding of the siRNA duplex, at which point the heterodimer is exchanged by Ago2. The strand that was bound by r2d2 is discarded while the one that was bound by Dcr-2 is loaded onto Ago2 and serves as guide to direct the RISC to complementary RNAs to degrade them or prevent their translation. Independently of its role in RNAi, acts with the cytoplasmic poly(A) polymerase wisp to promote cytoplasmic polyadenylation and translational activation of certain messenger RNAs including r2d2 and toll (Tl) transcripts. Consequently it is involved in the post-transcriptional regulation of the Toll immune signaling pathway and promoting resistance to fungal and viral infections. As an RNA-binding protein, likely functions in cytoplasmic polyadenylation by recruiting the poly(A) RNA polymerase wisp to target mRNAs.
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A1ZAY1
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DLISH_DROME
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SH3 domain-containing protein Dlish (Dachs ligand with SH3 domains)
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MAFLCPVRMRRDKKKATNASIERDLPAVGVLGMGRITGSSSIETLVRVGIEKEHGLSPDSKMVVLHDFTPCVDDELEVKRGQLVNILYRENDWVYVIGQDSRQEGFIPFSYCAPCNTQLADLAVKKKLPREQCPEQPIEENIPLLGTDNKLDVLCDETLNPGSANSIENTLLVEPECTPFVKEPSGRCIVLYTFIARDENDLSVERGEFVTVLNREDPDWFWIMRSDGQEGFVPASFIYPADSVRVLQQQKATLNAMETILQQGQQGQQSQQQQQPQLGLGTDDLRYHGTELVMLYDYKAQAPDDLYLSVRRGDWIYADLTNQTVDGWLWAYAPKTRKYGFIPKAYARPPAMTSL
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Required for the apical cell cortex localization, total cellular level and full activity of dachs.
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A1ZBD6
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MCTP_DROME
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Multiple C2 and transmembrane domain-containing protein
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MSRIQYVDQVDQVELDQQQQPGSSSTVSGSTPPLQISPHGSPSLQQSQRLGKHLSKSASELNGHDCHLSESPHISPKRAKSAVAQQLAGVSSGGVASGVGVLQKTHGFFNNLRHRWSRAKSKDRLGRKSPSDFLEESTDYAADYSSEGSSVTHSPRHRSTTIGGSPLAREFRATAKMAQVIQRFGGSMEGRIDEHPENGSAGCSPPELSTQQQLEALQANELRRKREAQLRQFVFFQLRVHLKSGSDLVAMDKNGLSDPYVKFKVGGRLLHKSRTIHRDLNPVWDEVFIVPIEDPFQPIIVKVFDYDWGLQDDFMGSAKLDLTQLELGKAEDIHLQLCDSSGNGGSGLGEILINLTLWPRSQEDKEMHFQRNSKLAESSKRLKSQIWSSVVTILLVKAKDLPLAEDGSKLNDTHFKFRLGNEKYKSKSSWTERWLEQFDLHLFDEDQNLEIALWNRNTLYGKAIIDLSVFQRENTHGIWKPLEDCPGEVHLMLTISGTTALETISDLKAFKEDPREAQLLRERYKFLRCLQNLRDVGHLTVKVFGATGLAAADIGGKSDPFCVLELGNARLQTQTEYKTLTPNWNKIFTFNVKDITQVLEITVFDEDRDHRVEFLGKLVIPLLRIKSGVKRWYTLKDKNLCVRAKGNSPQIQLELTVVWSEIRAVCRALQPKEEKLIQQEAKFKRQLFLRNVNRLKEIIMDILDAARYVQSCFEWESPVRSSIAFVFWIVACVYGDLETVPLVLLLIILKNWLVRLITGTTDAAAHYDYEYDEDDDDDKEKEEKKSIKERLQAIQEVSQTVQNTIGYLASLGESTINTFNFSVPELTWLAVVLLLGAILVLHFVPLRWLLLFWGLMKFSRRLLRPNTIPNNELLDFLSRVPDNEEINQYRELPPSAPTDQTRNNPKKKLKGS
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Calcium sensor which is essential for the stabilization of normal baseline neurotransmitter release and for the induction and long-term maintenance of presynaptic homeostatic plasticity.
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A2A259
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PK2L1_MOUSE
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Polycystin-2-like protein 1 (Polycystin-2L1) (Polycystic kidney disease 2-like 1 protein) (Polycystin-2 homolog)
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MNSMESPKNQELQTLGNRAWDNPAYSDPPSPNRTLRICTVSSVALPETQPKKPEVRCQEKTQRTLVSSCCLHICRSIRGLWGTTLTENTAENRELYVKTTLRELVVYIVFLVDICLLTYGMTSSSAYYYTKVMSELFLHTPSDSGVSFQTISSMSDFWDFAQGPLLDSLYWTKWYNNQSLGRGSHSFIYYENLLLGAPRLRQLRVRNDSCVVHEDFREDILNCYDVYSPDKEDQLPFGPQNGTAWTYHSQNELGGSSHWGRLTSYSGGGYYLDLPGSRQASAEALQGLQEGLWLDRGTRVVFIDFSVYNANINLFCILRLVVEFPATGGTIPSWQIRTVKLIRYVNNWDFFIVGCEVVFCVFIFYYVVEEILEIHLHRLRYLSSVWNILDLVVILLSIVAVGFHIFRTLEVNRLMGKLLQQPDTYADFEFLAFWQTQYNNMNAVNLFFAWIKIFKYISFNKTMTQLSSTLARCAKDILGFAIMFFIVFFAYAQLGYLLFGTQVENFSTFVKCIFTQFRIILGDFDYNAIDNANRILGPVYFVTYVFFVFFVLLNMFLAIINDTYSEVKEELAGQKDQLQLSDFLKQSYNKTLLRLRLRKERVSDVQKVLKGGEPEIQFEDFTSTLRELGHEEHEITAAFTRFDQDGDHILDEEEQEQMRQGLEEERVTLNAEIENLGRSVGHSPPGELGAEAARGQSWVSGEEFDMLTRRVLQLQCVLEGVVSQIDAVGSKLKMLERKGELAPSPGMGEPAVWENLYNPS
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Pore-forming subunit of a heteromeric, non-selective cation channel that is permeable to Ca(2+). Pore-forming subunit of a calcium-permeant ion channel formed by PKD1L2 and PKD1L1 in primary cilia, where it controls cilium calcium concentration, but does not affect cytoplasmic calcium concentration. The channel formed by PKD1L2 and PKD1L1 in primary cilia regulates sonic hedgehog/SHH signaling and GLI2 transcription. Pore-forming subunit of a channel formed by PKD1L2 and PKD1L3 that contributes to sour taste perception in gustatory cells. The heteromeric channel formed by PKD1L2 and PKD1L3 is activated by low pH, but opens only when the extracellular pH rises again. May play a role in the perception of carbonation taste. May play a role in the sensory perception of water, via a mechanism that activates the channel in response to dilution of salivary bicarbonate and changes in salivary pH.
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A2A288
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ZC12D_HUMAN
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Probable ribonuclease ZC3H12D (EC 3.1.-.-) (MCP-induced protein 4) (Transformed follicular lymphoma) (Zinc finger CCCH domain-containing protein 12D) (p34)
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MEHPSKMEFFQKLGYDREDVLRVLGKLGEGALVNDVLQELIRTGSRPGALEHPAAPRLVPRGSCGVPDSAQRGPGTALEEDFRTLASSLRPIVIDGSNVAMSHGNKETFSCRGIKLAVDWFRDRGHTYIKVFVPSWRKDPPRADTPIREQHVLAELERQAVLVYTPSRKVHGKRLVCYDDRYIVKVAYEQDGVIVSNDNYRDLQSENPEWKWFIEQRLLMFSFVNDRFMPPDDPLGRHGPSLSNFLSRKPKPPEPSWQHCPYGKKCTYGIKCKFYHPERPHHAQLAVADELRAKTGARPGAGAEEQRPPRAPGGSAGARAAPREPFAHSLPPARGSPDLAALRGSFSRLAFSDDLGPLGPPLPVPACSLTPRLGGPDWVSAGGRVPGPLSLPSPESQFSPGDLPPPPGLQLQPRGEHRPRDLHGDLLSPRRPPDDPWARPPRSDRFPGRSVWAEPAWGDGATGGLSVYATEDDEGDARARARIALYSVFPRDQVDRVMAAFPELSDLARLILLVQRCQSAGAPLGKP
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May regulate cell growth likely by suppressing RB1 phosphorylation. May function as RNase and regulate the levels of target RNA species (Potential). In association with ZC3H12A enhances the degradation of interleukin IL-6 mRNA level in activated macrophages. Serve as a tumor suppressor in certain leukemia cells. Overexpression inhibits the G1 to S phase progression through suppression of RB1 phosphorylation.
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A2A2Y4
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FRMD3_HUMAN
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FERM domain-containing protein 3 (Band 4.1-like protein 4O) (Ovary type protein 4.1) (4.1O)
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MFASCHCVPRGRRTMKMIHFRSSSVKSLSQEMRCTIRLLDDSEISCHIQRETKGQFLIDHICNYYSLLEKDYFGIRYVDPEKQRHWLEPNKSIFKQMKTHPPYTMCFRVKFYPHEPLKIKEELTRYLLYLQIKRDIFHGRLLCSFSDAAYLGACIVQAELGDYDPDEHPENYISEFEIFPKQSQKLERKIVEIHKNELRGQSPPVAEFNLLLKAHTLETYGVDPHPCKDSTGTTTFLGFTAAGFVVFQGNKRIHLIKWPDVCKLKFEGKTFYVIGTQKEKKAMLAFHTSTPAACKHLWKCGVENQAFYKYAKSSQIKTVSSSKIFFKGSRFRYSGKVAKEVVEASSKIQREPPEVHRANITQSRSSHSLNKQLIINMEPLQPLLPSPSEQEEELPLGEGVPLPKEENISAPLISSSPVKAAREYEDPPSEEEDKIKEEPLTISELVYNPSASLLPTPVDDDEIDMLFDCPSRLELEREDTDSFEDLEADENAFLIAEEEELKEARRALSWSYDILTGHIRVNPLVKSFSRLLVVGLGLLLFVFPLLLLLLESGIDLSFLCEIRQTPEFEQFHYEYYCPLKEWVAGKVHLILYMLGCS
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Putative tumor suppressor gene that may be implicated in the origin and progression of lung cancer.
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A2A432
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CUL4B_MOUSE
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Cullin-4B (CUL-4B)
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MSRSTRSKERRENDTDSEDNSSETSNQERRRCRQGPPRPPYPPLLPPVFPPPTPPPQVRRTRGLQDLGAMKSVCPGTSGFSSPNPSAASAAAQEVRSATDGNTSTTPPTSAKKRKLNSSSSSSNSSNEREDFDSTSSSSTPPQPRDSASPSTSSFCLGVPVATSSHVPIQKKLRFEDTLEFVGIDTKMAEESSSSSSSSSPTAATSQQQQQQQLKTKSILISSVASVHHANGLAKSSTAVSSFANSKPGSAKKLVIKNFKDKPKLPENYTDETWQKLKEAVEAIQNSTSIKYNLEELYQAVENLCSHKISANLYKQLRQICEDHIKAQIHQFREDSLDSVLFLKKIDRCWQNHCRQMIMIRSIFLFLDRTYVLQNSMLPSIWDMGLELFRAHIISDQKVQTKTIDGILLLIERERNGEAIDRSLLRSLLSMLSDLQIYQDSFEQQFLQETNRLYAAEGQKLMQEREVPEYLHHVNKRLEEEADRLITYLDQTTQKSLIASVEKQLLGEHLTAILQKGLNSLLDENRIQDLSLLYQLFSRVRGGVQVLLQQWIEYIKAFGSTIVINPEKDKTMVQELLDFKDKVDHIIDTCFLKNEKFINAMKEAFETFINKRPNKPAELIAKYVDSKLRAGNKEATDEELEKMLDKIMIIFRFIYGKDVFEAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDMELSKDIMIQFKQYMQNQNVPGNIELTVNILTMGYWPTYVPMEVHLPPEMVKLQEIFKTFYLGKHSGRKLQWQSTLGHCVLKAEFKEGKKELQVSLFQTMVLLMFNEGEEFSLEEIKHATGIEDGELRRTLQSLACGKARVLAKNPKGKDIEDGDKFICNDDFKHKLFRIKINQIQMKETVEEQASTTERVFQDRQYQIDAAIVRIMKMRKTLSHNLLVSEVYNQLKFPVKPADLKKRIESLIDRDYMERDKENPNQYNYIA
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Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit. CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in response to radiation-induced DNA damage (By similarity). Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication (By similarity). A number of DCX complexes (containing either TRPC4AP or DCAF12 as substrate-recognition component) are part of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (By similarity). The DCX(AMBRA1) complex is a master regulator of the transition from G1 to S cell phase by mediating ubiquitination of phosphorylated cyclin-D (CCND1, CCND2 and CCND3) (By similarity). The DCX(AMBRA1) complex also acts as a regulator of Cul5-RING (CRL5) E3 ubiquitin-protein ligase complexes by mediating ubiquitination and degradation of Elongin-C (ELOC) component of CRL5 complexes (By similarity). Required for ubiquitination of cyclin E (CCNE1 or CCNE2), and consequently, normal G1 cell cycle progression (By similarity). Component of the DCX(WDR77) complex, which mediates ubiquitination and degradation of Irgm1 in intestinal cells. Regulates the mammalian target-of-rapamycin (mTOR) pathway involved in control of cell growth, size and metabolism (By similarity). Specific CUL4B regulation of the mTORC1-mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8 (By similarity). With CUL4A, contributes to ribosome biogenesis (By similarity).
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A2A5K6
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ZN335_MOUSE
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Zinc finger protein 335 (NRC-interacting factor 1) (NIF-1)
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MEENEVESSSDAAPRPGQPEEPSESGLGVCTSEAVSADSSDAATVPGLTEADDSGVGQSSDGGNHSVEEVSESISTDPLPHGCLPDSSSVSRGPVAEMPGGPPALVHSSVLPDPSMLVSDCTASSSDLGSAIDKIIESTIGPDLIQSCITVTSGEEGGAETTQYLILQGPDDGAPMASSMSTSTLANSLAAIEALADGPTSTSACLEPPEEPQGDPSSVAQQPPAPVTEELDLQSLEAMMEVVVVQQFKCKMCQYRSSTKATLLRHMRERHFRPALAAAAAATGKRGRVRKWGTSTKTTEEDRPEEEEEDDDIVDAGAIDDLEEDSDYNPAEDEPRGRQLRLQRPTPSTPRPRRRPGRPRKLPRLETSDLHDGVGQPLVSSQSTQSPPELQDLEAPSSSGLRALGKVGRGLVESGVSQSDAENAAPSCQDEADAPPRRRGRPSRRFLGKKYRKYYYKSPKPLLRPYLCRICGSRFLSHEDLRFHVNSHEAGDPQLFRCLQCSYRSRRWSSLKEHMFNHVGSKPYKCDECSYTSVYRKDVIRHAAVHSQDRKKRPDPTPKLSSFPCPVCGRVYPMQKRLTQHMKTHSTEKPHMCDKCGKSFKKRYTFKMHLLTHIQAVANRRFKCEFCEFVCEDKKALLNHQLSHVSDKPFKCSFCPYRTFREDFLLSHVAVKHTGAKPFACEYCHFSTRHKKNLRLHVRCRHANSFEEWGRRHPEEPPSRRRPFFSLQQIEELKQQHSTAPGPPLSSPGPEAPQEPAPFQSPETPPLLCPDALGGTTIIYQQGAEESTAVATQTALDLLLNMSAQRELGATALQVAVVKSEGIEAELTSTGGQPSPEDTTPRVVTLHMAESGSSVAAESQLGPSDLQQIALPSGPFGGASYSVITAPPVEGRTSASGPPYREEPPGEAAQAVVVSDTLKEAGTHYIMAADGTQLHHIELTADGSISFPSPDTLAPGTKWPLLQCGGPPRDGSEVLSPTKTHHMGGSQGSSTPPPAASHTLGLVVPQSPPSAAASSTKKFSCKVCSEAFPSRAEMESHKRAHAGPAAFKCPDCPFSARQWPEVRAHMAQHSSLRPHQCNQCSFASKNKKDLRRHMLTHTNEKPFSCHVCGQRFNRNGHLKFHIQRLHSIDGRKTGTSTARAPAQTIILNSEEETLATLHTAFQSSHGVLGTERLQQALSQEHIIVAQEQTVTNQEEATYIQEITADGQTVQHLVTSDNQVQYIISQDGVQHLLPQEYVVVPDGHHIQVQEGQITHIQYEQGTPFLQESQIQYVPVSPSQQLVTQAQLEAAAHSAVTAVADAAMAQAQGLFGTEEAVPEQIHQLQHQGIEYDVITLSDD
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Component or associated component of some histone methyltransferase complexes may regulate transcription through recruitment of those complexes on gene promoters (By similarity). Enhances ligand-dependent transcriptional activation by nuclear hormone receptors (By similarity). Plays an important role in neural progenitor cell proliferation and self-renewal through the regulation of specific genes involved brain development, including REST. Also controls the expression of genes involved in somatic development and regulates, for instance, lymphoblast proliferation (By similarity).
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A2A5N8
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LMBL1_MOUSE
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Lethal(3)malignant brain tumor-like protein 1 (H-l(3)mbt) (H-l(3)mbt protein) (L(3)mbt-like) (L(3)mbt protein homolog)
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MEGHTDMEILRTVKGSSTGEVNVHLVARDSAGPHPQLPTTAFIIPTNAATLGLPSTALDVPYPREPVHVGALERVAGSEPVTATILPQLSTGTGTNSTVRLLDWTGVSAPLPGSGMRFRINEYAPLNMIGVERPRSPEQRHEGGMARRDAGIQHPDVHQDRQDITSLEPPVDASSCKCQACGPQQSSGLDVGSSGDRCSQPFQKRSVIVENSGCTIASELLKPMKKRKHKEYQSPSEESEPEAVKQGEGKDAEREPTPSTPENEEWSRSQLVSSEKKDGWSWESYLEEQKAVTAPVSLFQDSQAVTHNKNGFKLGMKLEGIDPQHPSMYFILTVAEVCGYRLRLHFDGYSECHDFWVNANSPDIHPAGWFEKTGHKLQLPKGYKEEEFSWSQYLRSTKAQAAPKHLFVSQSHSTPPVGFQVGMKLEAVDRMNPSLVCVASVTDVVDSRFLVHFDDWGDTYDYWCDPSSPYIHPVGWCQKQGKPLTPPQDYPDPDSFCWEKYLEETGTSAVPNWAFKVRPPHSFLVNMKLEAVDRRNPALIRVASVEDVEDHRIKLHFDGWSHNYDFWIDADHPDIHPAGWCSKTGHPLEPPLRPRESSSVSPGGCPPLSHRSPPHTKTSKYNFHHRKCPTPGCDGSGHVTGKFTAHHCLSGCPLAEKNQSRLKAELSDSETAARKKNPSNLSPRKKPRHQGRIGRPPKYRKIPEEDLQALPPSVVHQSLFMSTLPTHADRPLSVCWEQHCKLLPGVAGISASTVSKWTIEEVFGFVQTLTGSEDQARLFKDEMIDGEAFLLLTQADIVKIMSVKLGPALKIYNAILMFKNTDDAFK
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Polycomb group (PcG) protein that specifically recognizes and binds mono- and dimethyllysine residues on target proteins, therey acting as a 'reader' of a network of post-translational modifications. PcG proteins maintain the transcriptionally repressive state of genes: acts as a chromatin compaction factor by recognizing and binding mono- and dimethylated histone H1b/H1-4 at 'Lys-26' (H1bK26me1 and H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condense chromatin and repress transcription. Recognizes and binds p53/TP53 monomethylated at 'Lys-382', leading to repress p53/TP53-target genes. Also recognizes and binds RB1/RB monomethylated at 'Lys-860'. Participates in the ETV6-mediated repression. Probably plays a role in cell proliferation. Overexpression induces multinucleated cells, suggesting that it is required to accomplish normal mitosis (By similarity).
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A2A5R2
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BIG2_MOUSE
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Brefeldin A-inhibited guanine nucleotide-exchange protein 2 (Brefeldin A-inhibited GEP 2) (ADP-ribosylation factor guanine nucleotide-exchange factor 2)
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MQESQTKSMFVSRALEKILADKEVKRPQHSQLRRACQVALDEIKAELEKQRLGAAAPPKANFIEADKYFLPFELACQSKSPRVVSTSLDCLQKLIAYGHITGNAPDSGAPGKRLIDRIVETICNCFQGPQTDEGVQLQIIKALLTAVTSPHIEIHEGTILQTVRTCYNIYLASKNLINQTTAKATLTQMLNVIFTRMENQVLQEARELEKPMQSKPQSPVIQATAGSPKFSRLKQSQAQSKPTTPEKAELPNGDHAQSGLGKVSLENGEAPRERGSPVSGRAEPSRGTDSGAQEVVKDILEDVVTSAVKEAAEKHGLPEPDRALGALECQECAVPPGVDENSQTNGIADDRQSLSSADNLEPDVQGHQVAARFSHILQKDAFLVFRSLCKLSMKPLGEGPPDPKSHELRSKVVSLQLLLSVLQNAGPVFRSHEMFVTAIKQYLCVALSKNGVSSVPDVFELSLAIFLTLLSNFKMHLKMQIEVFFKEIFLNILETSTSSFEHRWMVIQTLTRICADAQCVVDIYVNYDCDLNAANIFERLVNDLSKIAQGRSGHELGMTPLQELSLRKKGLECLVSILKCMVEWSKDLYVNPNHQATLGQERLPDQEMGDGKGLDMARRCSVTSVESTVSSGTQTAIQDDPEQFEVIKQQKEIIEHGIELFNKKPKRGIQFLQEQGMLGAAVEDIAQFLHQEERLDSTQVGEFLGDSTRFNKEVMYAYVDQLDFCEKEFVSALRTFLEGFRLPGEAQKIDRLMEKFAARYIECNQGQTLFASADTAYVLAYSIIMLTTDLHSPQVKNKMTKEQYIKMNRGINDSKDLPEEYLSSIYDEIEGKKIAMKETKEHTIATKSTKQSVASEKQRRLLYNVEMEQMAKTAKALMEAVSHAKAPFTSATHLDHVRPMFKLVWTPLLAAYSIGLQNCDDTEVASLCLEGIRCAVRIACIFGMQLERDAYVQALARFSLLTASSSITEMKQKNIDTIKTLITVAHTDGNYLGNSWHEILKCISQLELAQLIGTGVKTRYLSGSGREREGSLKGHSLAGEEFMGLGLGNLVSGGVDKRQMASFQESVGETSSQSVVVAVDRIFTGSTRLDGNAIVDFVRWLCAVSMDELASPHHPRMFSLQKIVEISYYNMNRIRLQWSRIWHVIGDHFNKVGCNPNEDVAIFAVDSLRQLSMKFLEKGELANFRFQKDFLRPFEHIMKKNRSPTIRDMVIRCIAQMVSSQAANIRSGWKNIFAVFHQAASDHDGNIVELAFQTTGHIVSTIFQHHFPAAIDSFQDAVKCLSEFACNAAFPDTSMEAIRLIRFCGKYVSERPRVLQEYTSDDMNVAPGDRVWVRGWFPILFELSCIINRCKLDVRTRGLTVMFEIMKSYGHTFAKHWWQDLFRIVFRIFDNMKLPEQQSEKSEWMTTTCNHALYAICDVFTQFYEALHEVLLSDVFAQLQWCVKQDNEQLARSGTNCLENLVISNGEKFSPAVWDETCNCMLDIFKTTIPHVLLTWRPAGMEEEVSDRHLDVDLDRQSLSSIDRNASERGQSQLSNPTDDSWKGAPYAHQKLLASLLIKCVVQLELIQTIDNIVFYPATSKKEDAEHMVAAQQDTLDAEIHIETENQGMYKFMSSQHLFKLLDCLQESHSFSKAFNSNYEQRTVLWRAGFKGKSKPNLLKQETSSLACCLRILFRMYVDENRRDSWDEIQQRLLRVCSEALAYFITVNSESHREAWTSLLLLLLTKTLKISDEKFKAHASMYYPYLCEIMQFDLIPELRAVLRKFFLRIGLVYKIWIPEEPSQVPAALSSTW
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Promotes guanine-nucleotide exchange on ARF1 and ARF3 and to a lower extent on ARF5 and ARF6. Promotes the activation of ARF1/ARF5/ARF6 through replacement of GDP with GTP. Involved in the regulation of Golgi vesicular transport. Required for the integrity of the endosomal compartment. Involved in trafficking from the trans-Golgi network (TGN) to endosomes and is required for membrane association of the AP-1 complex and GGA1. Seems to be involved in recycling of the transferrin receptor from recycling endosomes to the plasma membrane. Probably is involved in the exit of GABA(A) receptors from the endoplasmic reticulum. Involved in constitutive release of tumor necrosis factor receptor 1 via exosome-like vesicles the function seems to involve PKA and specifically PRKAR2B. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways (By similarity).
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A2A5Z6
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SMUF2_MOUSE
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E3 ubiquitin-protein ligase SMURF2 (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase SMURF2) (SMAD ubiquitination regulatory factor 2) (SMAD-specific E3 ubiquitin-protein ligase 2)
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MSNPGGRRNGPVKLRLTVLCAKNLVKKDFFRLPDPFAKVVVDGSGQCHSTDTVKNTLDPKWNQHYDLYIGKSDSVTISVWNHKKIHKKQGAGFLGCVRLLSNAINRLKDTGYQRLDLCKLGPNDNDTVRGQIVVSLQSRDRIGTGGQVVDCSRLFDNDLPDGWEERRTASGRIQYLNHITRTTQWERPTRPASEYSSPGRPLSCFVDENTPITGTNGATCGHSSDPRLAERRVRSQRHRNYMSRTHLHTPPDLPEGYEQRTTQQGQVYFLHTQTGVSTWHDPRVPRDLSNINCEELGPLPPGWEIRNTATGRVYFVDHNNRTTQFTDPRLSANLHLVLNRQNQLKDQQQQQVVPLCPDDTECLTVPRYKRDLVQKLKILRQELSQQQPQAGHCRIEVSREEIFEESYRQVMKMRPKDLWKRLMIKFRGEEGLDYGGVAREWLYLLSHEMLNPYYGLFQYSRDDIYTLQINPDSAVNPEHLSYFHFVGRIMGMAVFHGHYIDGGFTLPFYKQLLGKSITLDDMELVDPDLHNSLVWILENDITGVLDHTFCVEHNAYGEIIQHELKPNGKSIPVTEENKKEYVRLYVNWRFLRGIEAQFLALQKGFNEVIPQHLLKTFDEKELELIICGLGKIDVSDWKVNTRLKHCTPDSNVVKWFWKAVEFFDEERRARLLQFVTGSSRVPLQGFKALQGAAGPRLFTIHQIDACTNNLPKAHTCFNRIDIPPYESYEKLYEKLLTAIEETCGFAVE
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E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Interacts with SMAD7 to trigger SMAD7-mediated transforming growth factor beta/TGF-beta receptor ubiquitin-dependent degradation, thereby down-regulating TGF-beta signaling. In addition, interaction with SMAD7 activates autocatalytic degradation, which is prevented by interaction with AIMP1. Also forms a stable complex with TGF-beta receptor-mediated phosphorylated SMAD1, SMAD2 and SMAD3, and targets SMAD1 and SMAD2 for ubiquitination and proteasome-mediated degradation. SMAD2 may recruit substrates, such as SNON, for ubiquitin-dependent degradation. Negatively regulates TGFB1-induced epithelial-mesenchymal transition and myofibroblast differentiation.
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A2A6C4
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SPP2C_MOUSE
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Signal peptide peptidase-like 2C (SPP-like 2C) (SPPL2c) (EC 3.4.23.-) (Intramembrane protease 5) (IMP-5)
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MACLGSLHPLGSLLLLFLLLLLSPEARGEYGLVRVVSKNWSKDYCVLYSSDYVNLPRDLHHAPLLSLHDGTKTPWCPDEDSFHQAQDSSPRQRPLHQTTTMVTRGNCSFYAKGWLAQDQGAQGLLIVSRARNQQCSDTISKPQDPSKPWPALTIPVAVLRYTDMLDIVSHTYGDTDVRVAMFAPLEPVTDYNMAIIFILAVGTVAAGGYWAGLMEANKLQRRQAQRGGGLGGHNQQQTVAAERSQRAWEDDDFEDAPMDFTPAMTGAVVTMSCSIMILLYFFYDCFVYVMIGIFSLGASTGLYSCLAPILCHLPLWRYQWVLPGQRVSVTWPLLLLAGLCAMVTVLWVIHRNEDHWAWLLQDTLGVAYCLFVLRRVRLPTFKNCTLFLLALLAFDVFFVFITPLFTKTGESIMVEVASGPADSSSHERLPMVLKVPRLSFSALTLCNQPFSILGFGDIVVPGFLVAYCHRFDMQVQSRQVYYMACTVAYAVGLLVTFVAMILMQMGQPALLYLVSSTLLTSLAVATCRQEFTLFWTGQGRAKIPAEPVAQPCIASAVGSKMKLEDAKDSRTTNRFEQAVDGESGDLESSTGDDMAEMVTLSEDEATSPEGHSESSEGWSDTNLDPNELPSGSPMALEAMLIPLIQPIPHPSELGHIRTQSRVHDSSLPWMGLHKRKGLKVKKSMSAQAPL
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Sperm-specific intramembrane-cleaving aspartic protease (I-CLiP) that cleaves distinct tail-anchored proteins and SNARE proteins. In elongated spermatids, modulates intracellular Ca(2+) homeostasis by controlling PLN abundance through proteolytic cleavage. During spermatogenesis, processes SNARE proteins and impacts vesicular trafficking which supports compartmental reorganization in maturating spermatids and may play a role in formation of the acrosome. In round spermatids, acts as a scaffold protein supporting FREY1 in IZUMO1 recruitment at the endoplasmic reticulum membrane and coordination of IZUMO1 complex assembly. Stabilizes FREY1 at the endoplasmic reticulum membrane through interaction. May recruit IZUMO1 interaction partners.
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A2A6M5
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CACO2_MOUSE
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Calcium-binding and coiled-coil domain-containing protein 2 (Nuclear domain 10 protein NDP52) (Nuclear domain 10 protein 52)
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MDQCPIPTLLEHGNFSQVLFNNVEKFYAPRGDIMCYYTLTEKFIPRRKDWIGIFKVGWKTTQEYYTFMWAPLPKDQNKDSATQQEIQFKAYYLPKDVERYQFCYVDEDGLVRGTSVPFQFCPDPDEDIMVVINKEKVEEMEQLSEELYQQNQELKDKYADLHEQLQRKQVALEATQRVNKTLEHKVEEKASWEKEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEEEKASWEKEKASWEEEKASWEKEKAPWEVEKAPWKEVKAYWWNDLHR
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Xenophagy-specific receptor required for autophagy-mediated intracellular bacteria degradation (By similarity). Acts as an effector protein of galectin-sensed membrane damage that restricts the proliferation of infecting pathogens upon entry into the cytosol by targeting LGALS8-associated bacteria for autophagy (By similarity). Initially orchestrates bacteria targeting to autophagosomes and subsequently ensures pathogen degradation by regulating pathogen-containing autophagosome maturation (By similarity). Bacteria targeting to autophagosomes relies on its interaction with MAP1LC3A, MAP1LC3B and/or GABARAPL2, whereas regulation of pathogen-containing autophagosome maturation requires the interaction with MAP3LC3C (By similarity). May play a role in ruffle formation and actin cytoskeleton organization and seems to negatively regulate constitutive secretion (By similarity).
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A2A6Q5
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CDC27_MOUSE
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Cell division cycle protein 27 homolog
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MTVLQEPVQAAIWQALNHYAYRDAVFLAERLYAEVHSEEALFLLATCYYRSGKAYKAYRLLKGHSCTTPQCKYLLAKCCVDLSKLAEGEQILSGGVFNKQKSHDDLVTEFGDSACFTLSLLGHVYCKTDRLAKGSECYQKSLSLNPFLWSPFESLCEIGEKPDPDQTFKLTSLQNFSSCLPNTCTTLVSNHSLSHRQPETVLTETPQDTIELNRLNLESSNSKYSLNTDSSVSYIDSTVISPDNVPLGPGTAILSKQVQNKPKTGRSLLGGPTALSPLTPSFGILPLETPSPGDGSYLQNYTNTPSVIDVAPTGAPTKKSVARMGQTGTKSVFSQSGNSREVTPVLVAQTQSSGPQTSTTPQVLSPTITSPPNALPRRSSRLFTSDSSTTKENSKKLKMKFPPKIPNRKTKSKTNKGGLTQPSINDSLEITKLDSSIISEGKITTVTPQIQAFNLQKAAAEGLMSLLREMGKGYLALCSYNCKEAINILSHLPSHHYSTGWVLCQIGRAYFELSEYMQAERIFSEVRRIESFRVEGMEIYSTTLWHLQKDVALSVLSKDLTDMDKNSPEAWCAAGNCFSLQREHDIAIKFFQRAIQVDPNYAYAYTLLGHEFVLTEELDKALACFRNAIRVNPRHYNAWYGLGMIYYKQEKFSLAEMHFQKALDINPQSSVLLCHIGVVQHALKKSEKALDTLNKAIVIDPKNPLCKFHRASVLFANEKYKSALQELEELKQIVPKESLVYFLIGKVYKKLGQTHLALMNFSWAMDLDPKGANNQIKEAIDKRYLPDDEEPITQEEQIMGTDESQESSMTDADDTQLHAAESDEF
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Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity).
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A2A7Q9
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RN19B_MOUSE
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E3 ubiquitin-protein ligase RNF19B (EC 2.3.2.31) (IBR domain-containing protein 3) (Natural killer lytic-associated molecule) (RING finger protein 19B)
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MGSEKDSESPRSTSLHAAAPDPKCRSGGRRRRLTFHSVFSASARGRRARTKPQAEPPPPAAPPPPPPPAPAPVEAQAPPVEALPSEPAAEAEAEAVAAGPEEDEAAEGGGAEEVECPLCLVRLPPERAPRLLSCPHRSCRDCLRHYLRLEISESRVPISCPECSERLNPHDIRLLLADPPLMHKYEEFMLRRYLASDPDCRWCPAPDCGYAVIAYGCASCPKLTCEREGCQTEFCYHCKQIWHPNQTCDMARQQRAQTLRVRTKHTSGLSYGQESGPADDIKPCPRCSAYIIKMNDGSCNHMTCAVCGCEFCWLCMKEISDLHYLSPSGCTFWGKKPWSRKKKILWQLGTLIGAPVGISLIAGIAIPAMVIGIPVYVGRKIHSRYEGRKTSKHKRNLAITGGVTLSVIASPVIAAVSVGIGVPIMLAYVYGVVPISLCRGGGCGVSTANGKGVKIEFDEDDGPITVADAWRALKNPSIGESSIEGLTSVLSTSGSPTDGLSVMQGPYSETASFAALSGGTLSGGILSSGKGKYSRLEVQADVQKEIFPKDTASLGAISDSASTRAMAGSIISSYNPQDRECNNMEIQVDIEAKPSHYQLVSGSSTEDSLHVHAQVAEKEEEGNGAGGGSGGSEDDPPYKHQSCEQKDCLASKAWDISLAQPESIRSDLESSDTQSDDVPDITSDECGSPRSHAAACPSTPQVHGAPSPSAHKNLAAPAEGQTVLKSEEYEVE
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E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as UCKL1. Involved in the cytolytic activity of natural killer cells and cytotoxic T-cells. Protects against staurosporin-induced cell death (By similarity).
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A2A825
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CPLN2_MOUSE
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Ciliogenesis and planar polarity effector 2 (REM2- and Rab-like small GTPase 1)
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MARPPMHGSVIVPDWHETVEGKEYLACILRKNRRREFGLLERPVLPPSVVIDTASYKIFVSGKSGVGKTALVAKLAGLEVPIVHHETTGIQTTVVFWPAKLKASDCVVMFRFEFWDCGESALKKFDHMLPACKENADAFLFLFSFTDRASFEDLPGQLTRVAGEAPGLVKIVIGSKFDQYMHTDVPARDLTAFRQAWELPLFRVKSVPGRRLADGRTLDGRAGLADTAHVLNGLAEQLWHQDQVAAGLLPSSPESAPG
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Potential effector of the planar cell polarity signaling pathway. Plays a role in targeted membrane trafficking most probably at the level of vesicle fusion with membranes. Involved in cilium biogenesis by regulating the transport of cargo proteins to the basal body and to the apical tips of cilia. More generally involved in exocytosis in secretory cells (By similarity).
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A2A863
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ITB4_MOUSE
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Integrin beta-4 (CD antigen CD104)
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MAGPCCSPWVKLLLLAAMLSASLPGDLANRCKKAQVKSCTECIRVDKSCAYCTDELFKERRCNTQAELLAAGCRGESILVMESSLEITENTQIDTSLHRSQVSPQGLQVRLRPGEERSFVFQVFEPLESPVDLYILMDFSNSMSDDLDNLKQMGQNLAKILRQLTSDYTIGFGKFVDKVSVPQTDMRPEKLKEPWPNSDPPFSFKNVISLTENVEEFWNKLQGERISGNLDAPEGGFDAILQTAVCTRDIGWRADSTHLLVFSTESAFHYEADGANVLAGIMNRNDEKCHLDASGAYTQYKTQDYPSVPTLVRLLAKHNIIPIFAVTNYSYSYYEKLHKYFPVSSLGVLQEDSSNIVELLEEAFYRIRSNLDIRALDSPRGLRTEVTSDTLQKTETGSFHIKRGEVGTYNVHLRAVEDIDGTHVCQLAKEDQGGNIHLKPSFSDGLRMDASVICDVCPCELQKEVRSARCHFRGDFMCGHCVCNEGWSGKTCNCSTGSLSDTQPCLREGEDKPCSGHGECQCGRCVCYGEGRYEGHFCEYDNFQCPRTSGFLCNDRGRCSMGECVCEPGWTGRSCDCPLSNATCIDSNGGICNGRGYCECGRCHCNQQSLYTDTTCEINYSAIRLGLCEDLRSCVQCQAWGTGEKKGRACDDCPFKVKMVDELKKAEEVVEYCSFRDEDDDCTYSYNVEGDGSPGPNSTVLVHKKKDCPPGSFWWLIPLLIFLLLLLALLLLLCWKYCACCKACLGLLPCCNRGHMVGFKEDHYMLRENLMASDHLDTPMLRSGNLKGRDTVRWKITNNVQRPGFATHAASTSPTELVPYGLSLRLGRLCTENLMKPGTRECDQLRQEVEENLNEVYRQVSGAHKLQQTKFRQQPNTGKKQDHTIVDTVLLAPRSAKQMLLKLTEKQVEQGSFHELKVAPGYYTVTAEQDARGMVEFQEGVELVDVRVPLFIRPEDDDEKQLLVEAIDVPVGTATLGRRLVNITIIKEQASGVVSFEQPEYSVSRGDQVARIPVIRHILDNGKSQVSYSTQDNTAHGHRDYVPVEGELLFHPGETWKELQVKLLELQEVDSLLRGRQVRRFQVQLSNPKFGARLGQPSTTTVILGEHDETDRSLINQTLSSPPPPHGDLGAPQNPNAKAAGSRKIHFNWLPPPGKPMGYRVKYWIQGDSESEAHLLDSKVPSVELTNLYPYCDYEMKVCAYGAQGEGPYSSLVSCRTHQEVPSEPGRLAFNVVSSTVTQLSWAEPAETNGEITAYEVCYGLVNEDNRPIGPMKKVLVDNPKNRMLLIENLRESQPYRYTVKARNGAGWGPEREAIINLATQPKRPMSIPIIPDIPIVDAQGGEDYENFLMYSDDVLRSPASSQRPSVSDDTGCGWKFEPLLGEELDLRRVTWRLPPELIPRLSASSGRSDEDGSVAGGVEGEGSGWIRGATPRPPGEHLVNGRMDFAYPGSANSLHRMTAANVAYGTHLSPHLSHRVLSTSSTLTRDYHSLTRTEHSHSGTLPRDYSTLTSLSSQDSRGAVGVPDTPTRLVFSALGPTSLKVSWQEPQCDRMLLGYSVEYQLLNGGEMHRLNIPNPGQTSVVVEDLLPNHSYVFRVRAQSQEGWGREREGVITIESQVHPQSPLCPLPGSAFTLSTPSAPGPLVFTALSPDSLQLSWERPRRPNGDILGYLVTCEMAQGGAPARTFRVDGDNPESRLTVPGLSENVPYKFKVQARTTEGFGPEREGIITIESQVGGPFPQLGSHSGLFQNPVQSEFSSVTSTHSTTTEPFLMDGLTLGTQRLEAGGSLTRHVTQEFVTRTLTASGSLSTHMDQQFFQT
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Integrin alpha-6/beta-4 is a receptor for laminin. It plays a critical structural role in the hemidesmosome of epithelial cells. Is required for the regulation of keratinocyte polarity and motility. ITGA6:ITGB4 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling. ITGA6:ITGB4 binds to IGF1 and this binding is essential for IGF1 signaling. ITGA6:ITGB4 binds to IGF2 and this binding is essential for IGF2 signaling.
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A2A884
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ZEP3_MOUSE
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Transcription factor HIVEP3 (Human immunodeficiency virus type I enhancer-binding protein 3 homolog) (KB-binding and recognition component) (Kappa-B and V(D)J recombination signal sequences-binding protein) (Kappa-binding protein 1) (KBP-1) (Recombinant component) (Schnurri-3) (Zinc finger protein ZAS3)
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MDPDQSIKGTKKADGSPRKRLTKGEAIQTSVSSSAPYPGSGTTAPSESATQELLATQPFSGPSQEKTGQQQKPARRPSIEASVHISQLPQHPLTPAFMSPGKPEHLLEGSTWQLVDPMRPGPSGSFVAPGLHPQSQLLPSHASILPPEELPGIPKVFVPRPSQVSLKPAEEAHKKERKPQKPGKYICQYCSRPCAKPSVLQKHIRSHTGERPYPCGPCGFSFKTKSNLYKHRKSHAHRIKAGLASGSSSEMYPPGLEMERIPGEEFEEPTEGESTDSEEETGAASGPSTDVLPKPKHPLLSSSLYSSGSHGSSQERCSLSQSSTGPSLEDPAPFAEASSEHPLSHKPEDTHTIKQKLALRLSERKKLIEEQTFLSPGSKGSTESGYFSRSESAEQQVSPPNTNAKSYAEIIFGKCGRIGQRTSMLASTSTQPLLPLSSEDKPSLVPLSVPRTQVIEHITKLITINEAVVDTSEIDSVKPRRSSLTRRSSVESPKSSLYRDSLSSHGEKTKQEQSLLSLQHPPSSTHPVPLLRSHSMPSAACTISTHHHTFRGSYSFDDHVADPEVPSRNTPVFTSHPRMLKRQPAIELPLGGEYSSEEPGPSSKDPTSKPSDEPEPKESDLTKKTKKGFKTKGANYECTICGARYKKRDNYEAHKKYYCSELQITKAHSVGAHEVEKTQAEPEPWSQMMHYKLGATLELTPLRKRRKEKSLGDEEEPPAFGSPGPSETAHNRPLGSTKSPAEASKSAPSLEGPTSFQPRTPKPGAGSEPGKERRTMSKEISVIQHTSSFEKSDPPEQPSGLEEDKPPAQFSSPPPAPHGRSAHSLQPRLVRQPNIQVPEILVTEEPDRPDTEPEPPPKEPEKTEEFQWPQRSQTLAQLPAEKLPPKKKRLRLAEMAQSSGESSFESSVPLSRSPSQESSISLSGSSRSASFDREDHGKAEAPGPFSDTRSKTLGSHMLTVPSHHPHAREMRRSASEQSPNVPHSSHMTETRSKSFDYGSLSPTGPSLAVPAAPPPPAAPPERRKCFLVRQASLNRPPEAELEAVPKGKQESSEEPAASKPSTKSSVPQISVGTTQGGPSGGKSQMQDRPPLGSSPPYTEALQVFQPLGTQLPPPASLFSLQQLLPQEQEQSSEFFPTQAMAGLLSSPYSMPPLPPSLFQAPPLPLQPTVLHPSQLHLPQLLPHAADIPFQQPPSFLPMPCPAPSTLSGYFLPLQSQFALQLPGEIESHLPPVKTSLPPLATGPPGPSSSTEYSSDIQLPPVTPQATSPAPTSAPPLALPACPDAMVSLVVPVRIQTHMPSYGSAMYTTLSQILVTQSPGSPASTALTKYEEPSSKSMTVCEADVYEAEPGPSSISKEQNRGYQTPYLRVPERKGTSLSSEGILSLEGCSSTASGSKRVLSPAGSLELTMETQQQKRVKEEEASKADEKLELVSTCSVVLTSTEDRKKTEKPHVGGQGRSRREAETLSSLSSDVSDPKELSPLSHSTLSHGTAPGSEALKEYAQPSSKAHRRGLPPMSVKKEDPKEQTDLPPLAPPSSLPLSDTSPKPAKLQEGTDSKKVLQFPSLHTTTNVSWCYLNYIKPNHIQHADRRSSVYAGWCISLYNPNLPGVSTKAALSLLRSKQKVSKETYTMATAPHPEAGRLVPSNSRKPRMTEVHLPSLVSPESQKDPARVEKEEKQGKAEEGTPTSKRGEPARVKIFEGGYKSNEEYIYVRGRGRGRYVCEECGIRCKKPSMLKKHIRTHTDVRPYVCKHCHFAFKTKGNLTKHMKSKAHSKKCQETGVLEELEAEEGTSDDLHQDSEGQEGAEAVEEHQFSDLEDSDSDSDLDEDEEEEEEEEESQDELSGPCSEAAPPCLPPTLQENSSPVEGPQAPDSTSDEVPQGSSISEATHLTASSCSTPSRGTQGLPRLGLAPLEKDMSSAPSPKATSPRRPWSPSKEAGSRPSLTRKHSLTKNDSSPQQCSPAREAQASVTSTPGPQMGPGRDLGPHLCGSPRLELSCLTPYPIGREAPAGLERATDTGTPRYSPTRRWSLGQAESPPQTVLPGKWALAGPCSPSADKSGLGLGPVPRALLQPVPLPHTLLSRSPETCTSAWRKTESRSPSAGPAPLFPRPFSAPHDFHGHLPSRSEENLFSHLPLHSQLLSRAPCPLIPIGGIQMVQARPGAQPTVLPGPCAAWVSGFSGGGSDLTGAREAQERSRWSPTESPSASVSPVAKVSKFTLSSELEEERTGRGPGRPPDWEPHRAEAPPGPMGTHSPCSPQLPQGHQVAPSWRGLLGSPHTLANLKASSFPPLDRSSSMDCLAETSTYSPPRSRNLSGEPRTRQGSPELLGRGELRTPLFLPKGSGPPSI
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Plays a role of transcription factor binds to recognition signal sequences (Rss heptamer) for somatic recombination of immunoglobulin and T-cell receptor gene segments Binds also to the kappa-B motif of gene such as S100A4, involved in cell progression and differentiation. Kappa-B motif is a gene regulatory element found in promoters and enhancers of genes involved in immunity, inflammation, and growth and that responds to viral antigens, mitogens, and cytokines. Involvement of HIVEP3 in cell growth is strengthened by the fact that its down-regulation promotes cell cycle progression with ultimate formation of multinucleated giant cells. Strongly inhibits TNF-alpha-induced NF-kappa-B activation Interferes with nuclear factor NF-kappa-B by several mechanisms: as transcription factor, by competing for Kappa-B motif and by repressing transcription in the nucleus through a non transcriptional process, by inhibiting nuclear translocation of RELA by association with TRAF2, an adapter molecule in the tumor necrosis factor signaling, which blocks the formation of IKK complex. Interaction with TRAF proteins inhibits both NF-Kappa-B-mediated and c-Jun N-terminal kinase/JNK-mediated responses that include apoptosis and pro-inflammatory cytokine gene expression. Positively regulates the expression of IL2 in T-cell. Essential regulator of adult bone formation.
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A2A891
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CMTA1_MOUSE
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Calmodulin-binding transcription activator 1
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MWRAEGKWLPKTSRKSVSQSVFCGTSTYCVLNTVPPIEDDHGNSNSSHVKIFLPKKLLECLPKCSSLPKERHRWNTNEEIAAYLITFEKHEEWLTTSPKTRPQNGSMILYNRKKVKYRKDGYCWKKRKDGKTTREDHMKLKVQGVECLYGCYVHSSIIPTFHRRCYWLLQNPDIVLVHYLNVPAIEDCGKPCGPILCSINTDKKEWAKWTKEELIGQLKPMFHGIKWTCSNGNSSSGFSVEQLVQQILDSHQTKPQPRTHNCLCTGSLGAGSSVHHKCNSAKHRIISPKVEPRAGGYGGHSEVQHNDVSEGKHEPSHGRSTSREKRNGKVAKPALLHQNSTEVSSTNQVEVPDTTQSSPVSISSGLNSDPDMVDSPVVTGVSSMAVASVMGGLSQSATVFMSEVTNEAVYTMSPTAGPNHHLLSPDASQGLVLAVSSDGHKFAFPTTGSSDSLSMLPANVSEELVLSTTLDGGRKIPETAMNFDPDCFLNNPKQGQTYGGGGLKAEMVSTNIRHSPPAERSFGFTSVLTKEIKTEDTSFEQQMAKEAAYSSSAAAAASSSLTLTAAGSSLLPSGGGLSPSTTLEQMDFSAIDSNKDYASSFSQTGHSPHIHQTPSPSFFLQDASKPLPLEQNTHSSLSESGAAFVMPTVKTEASSQTSSCSGHVETRIESTSSLHLMQFQANFQAMAAEGEVTMETSQAAEGNEVLLKSGELQACGSEHYLQPETNGVIRSAGGVPLLPSNVVQGLYPVAQPSLGNSSNMELSLDHFDISFSNQFSDLINDFISVEGGSGTIYGHQLVSGDSAALSQSEDGARAPFTQAEMCIPCCSPQQGSLQLSSAEGGPSTMAYMHVAEVVSAASAQGALGMLQQSGRVFMVTDYSPEWSYPEGGVKVLITGPWQEASNNYSCLFDQISVPASLIQPGVLRCYCPAHDTGLVTLQVAFNNQIISNSVVFEYKARALPTLPSSQHDWLSLDDNQFRMSILERLEQMERRMAEMTGSQQHKQASGGGGSGSGSGSGAGGGQAQCASGAGTLGSCFESRVVVVCEKMMSRACWAKSKHLIHSKTFRGMTLLHLAAAQGYATLIQTLIKWRTKHADSIDLELEVDPLNVDHFSCTPLMWACALGHLEAAVVLYKWDRRAISIPDSLGRLPLGIARSRGHVKLAECLEHLQRDEQAQLGQASRIHCAPSEEPTTDSWMAQWQREAMSPPEIPKGVTVIASTNPELRRPRSEPSNYYSTEGHKDYPAPKKHKLNPESFQARQEKLLCTALSLEQPNIRKQSPRSKQPSPETISPSEGVREYSREAAPPTPETAASQASASQPVVKWSAKDLYIGVSTVQVTGNPKGTSVVKDAAPSQVRPREPMSVLMLANREVVNTEMGAYRDRTEHEDCPQPMDDIQVNMMTLAEHIIEATPDRIKQENFVPMESSALERTDPATISSTMSWLASYLADADRLPSAAHIRSAYTEPLTPSSNASLSPAGSPVSEVAFEKPSLPSAADWSEFLSASTSEKVESELAQLTLSDHEQRELYEAARLVQTAFRKYKGRPLREQQEVAAAVIQRCYRKYKQLTWIALKYALYKKMTQAAILIQSKFRSYYEQKRFQQSRRAAVLIQNFYRSYKKCGRRRPARRTAVIVQQKLRSSLLTKKQDQAARKIMRFLRRCRHSPLVDHRLYKRSERIEKGQGT
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Transcriptional activator.
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A2A8L1
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CHD5_MOUSE
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Chromodomain-helicase-DNA-binding protein 5 (CHD-5) (EC 3.6.4.12) (ATP-dependent helicase CHD5)
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MRGPLGTEEELPRLFAEEMENEEEMSEEEDGGLEGFEDFFPAEPVSLPKKKPKKLKESKSSKGKRKKKEGSNDEMSDNEEDLEEKSESEGSDYSPTKKKKKKLKEKKEKKEKKEKRKKRGEDEDDNDDGGLKEPKSSGQLMAEWGLDDVDYLFSEDDYHTLTNYKAFSQFLRPLIAKKNPKIPMSKMMTVLGAKWREFSANNPFKGSSAAAAAAAVAAAVETVTIAPPLAISPQQVPQTLPIRKAKTKEGKGPGVRKKNKGAKDSKKKGRGKRVAGLKFRFGGISKRKKGSSSEEDEREDSDLDNASIHSSSVRSECSAALGKKNKRRRKKKRIDDGDGYETDHQDYCEVCQQGGEIILCDTCPRAYHLVCLDPELEKAPEGKWSCPHCEKEGIQWEPKDDDEEEEEGGCEEEEDDHMEFCRVCKDGGELLCCDACPSSYHLHCLNPPLPEIPNGEWLCPRCTCPPLKGKVQRILHWRWTEPPAPFVVGLPGPEVEPGMPPPRPLEGIPEREFFVKWAGLSYWHCSWVKELQLELYHTVMYRNYQRKNDMDEPPPFDYGSGDEDGKSEKRKNKDPLYAKMEERFYRYGIKPEWMMVHRILNHSFDKKGDIHYLIKWKDLPYDQCTWEIDEIDIPYYDNLKQAYWGHRELMLGEDARLPKRLVKKGKKLKDDKQEKPPDTPIVDPTVKFDKQPWYIDATGGTLHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVTYTGDKESRSVIRENEFSFEDNAIRGGKKVFRMKKEVQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRRLKADVFKNMPAKTELIVRVELSQMQKKYYKFILTRNFEALNSKGGGNQVSLLNIMMDLKKCCNHPYLFPVAAVEAPVLPNGSYDGSSLVKSSGKLMLLQKMLKKLRDEGHRVLIFSQMTKMLDLLEDFLEYEGYKYERIDGGITGGLRQEAIDRFNAPGAQQFCFLLSTRAGGLGINLATADTVIIYDSDWNPHNDIQAFSRAHRIGQNKKVMIYRFVTRASVEERITQVAKRKMMLTHLVVRPGLGSKSGSMTKQELDDILKFGTEELFKDDVEGMMSQGQRPTTPIPDIQSTKGGSLTAGAKKKHGSTPPGDNKDVEDSSVIHYDDAAISKLLDRNQDATDDTELQNMNEYLSSFKVAQYVVREEDGVEEVEREVIKQEENVDPDYWEKLLRHHYEQQQEDLARNLGKGKRIRKQVNYNDASQEDQEWQDELSDNQSEYSIGSEDEDEDFEERPEGQSGRRQSRRQLKSDRDKPLPPLLARVGGNIEVLGFNARQRKAFLNAIMRWGMPPQDAFNSHWLVRDLRGKSEKEFRAYVSLFMRHLCEPGADGAETFADGVPREGLSRQHVLTRIGVMSLVRKKVQEFEHVNGKYSTPDLVPEGAEGKKPGEVISSDPNTPVPASPAQLPPAPLGLTDKMEAQLGYTDEKESGMQKPKKSLEIQTLPTALDRVEGEDKHQSSDSKDRAREERTEEVEKAQGSPEQPLKEEVLPDKEPIPDKPELSLGHSGDFRPDDPKTEEKEPGETQQNGDREEDEEGKKEDKNGKFKFMFNIADGGFTELHTLWQNEERAAVSSGKIYEIWHRRHDYWLLAGIVTHGYARWQDIQNDPRYMILNEPFKSEIHKGNYLEMKNKFLARRFKLLEQALVIEEQLRRAAYLNMTQDPNHPAMALNARLAEVECLAESHQHLSKESLAGNKPANAVLHKVLNQLEELLSDMKADVTRLPSMLSRIPPVAARLQMSERSILSRLTNRAGDPTIQQTSSRRRDFPLFQRSFPAEPSHLPNPRGREKLQPF
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Chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. May specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3. Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin. Plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. Regulates the expression of genes involved in cell proliferation and differentiation. Downstream activated genes may include CDKN2A that positively regulates the p53/TP53 pathway, which in turn, prevents cell proliferation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa.
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A2A8L5
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PTPRF_MOUSE
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Receptor-type tyrosine-protein phosphatase F (EC 3.1.3.48) (Leukocyte common antigen related) (LAR)
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MAPEPAPGRRMVPLVPALVMLGLMAGAHGDSKPVFVKVPEDQTGLSGGVASFVCQATGEPKPRITWMKKGKKVSSQRFEVIEFDDGAGSVLRIQPLRVQRDEAIYECTATNSLGEINTSAKLSVLEEDQLPSGFPTIDMGPQLKVVEKGRTATMLCAAGGNPDPEISWFKDFLPVDPAASNGRIKQLRSGALQIESSEESDQGKYECVATNSAGTRYSAPANLYVRVRRVAPRFSIPPSSQEVMPGGSVNLTCVAVGAPMPYVKWMMGAEELTKEDEMPVGRNVLELSNVMRSANYTCVAISSLGMIEATAQVTVKALPKPPIDLVVTETTATSVTLTWDSGNTEPVSFYGIQYRAAGTDGPFQEVDGVASTRYSIGGLSPFSEYAFRVLAVNSIGRGPPSEAVRARTGEQAPSSPPRRVQARMLSASTMLVQWEPPEEPNGLVRGYRVYYTPDSRRPLSAWHKHNTDAGLLTTVGSLLPGITYSLRVLAFTAVGDGPPSPTIQVKTQQGVPAQPADFQANAESDTRIQLSWLLPPQERIVKYELVYWAAEDEGQQHKVTFDPTSSYTLEDLKPDTLYHFQLAARSDLGVGVFTPTVEARTAQSTPSAPPQKVTCVSTGSTTVRVSWVPPPADSRNGIITQYSVAYEAVDGEDRKRHVVDGISREHSSWDLLGLEKWTEYRVWVRAHTDVGPGPESSPVLVRTDEDVPSGPPRKVEVEPLNSTAVHVSWKLPVPNKQHGQIRGYQVTYVRLENGEPRGQPIIQDVMLAEAQETTISGLTPETTYSITVAAYTTKGDGARSKPKVVTTTGAVPGRPTMMVSTTAMHTALLQWHPPKELPGELLGYRLQYRRADEARPNTIDFGKDDQHFTVTGLHKGATYVFRLAAKNRAGPGEEFEKEITTPEDVPSGFPQNLRVTGLTTSTTELTWDPPVLAERNGHITNYTVVYRDINSQLELQNVTNDTHLTLLGLKPDTTYDIKVRAHTSKGAGPLSPSIQSRTMPVEQVFAKNFRVAAAMKTSVLLSWEVPDSYKSAVPFKILYNGQSVEVDGHSMRKLIADLQPNTEYSFVLMNRGSSAGGLQHLVSIRTAPDLLPQKPLPASAFIEDGRFSLSMPQVQDPSLVRWFYIVVVPIDRVGGNLLAPRWNTPEELELDELLEAIEQGEEKQRRRRRQAERLKPYVAAQVDVLPDTFTLGDKKSYRGFYNRPLSPDLSYQCFVLASLKEPMDQKRYASSPYSDEIVVQVTPAQQQEEPEMLWVTGPVLAVILIILIVIAILLFKRKRTHSPSSKDEQSIGLKDSLLAHSSDPVEMRRLNYQTPGMRDHPPIPITDLADNIERLKANDGLKFSQEYESIDPGQQFTWENSNSEVNKPKNRYANVIAYDHSRVLLTSIDGVPGSDYINANYIDGYRKQNAYIATQGPLPETMGDFWRMVWEQRTATVVMMTRLEEKSRVKCDQYWPVRGTETYGLIQVTLVDTVELATYTMRTFALHKSGSSEKRELRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPLDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYVFIHEALLEAAMCGHTEVLARNLYAHIQKLGQVPPGESVTAMELEFKLLANSKAHTSRFVSANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFLDGYRQQKAYIATQGPLAESTEDFWRMLWEHNSTIIVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYLGSFDHYAT
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Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase) and dephosphorylates EPHA2 regulating its activity (By similarity).
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A2A8U2
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TM201_MOUSE
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Transmembrane protein 201 (Spindle-associated membrane protein 1)
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MEGVSALLASCPTAGLAGGLGVTACAAAGVVLYRIARRVKPTHTMVNCWFCNHDTLVPYGNRNCWDCPHCEQYNGFQENGDYNKPIPAQYMEHLNHVVSSVPSPRDPAQPQQWVSSQVLLCRRCSHHQTTKIKQLAAFTPREEGRYDEEIEVYRHHLEQMYKLCRPCQAAVEYYIKHQNRQLRALLLSHQFRRREADQAHGQSFSSSAVKAPFQVILLRALAFLACAFLLFTTLYGPSEPFTPGAALPPALPPGGNSSAASDNTTSQAEGWQQLLGLLPEHATEKLHEAWAFGQSHQTSIVAVGLLTCLLAMLLAGRIRLRRIDAFSTCLWALLLGLHLAEHYLQAASPGWLDTLKFSTTSLCCLVGFTAAVATRKSTGPRRFRPRRYFSGDSASLFPSSPSLAVPYPSVTSSPASLFIPTPPGFLPLTKQQLFRSPRRVSPSSLPGRLSRALSLGTIPPLTRTDSGYLFSGSRPPSRVSPAGEVSLSDYFSLLSSSFPASPLPSPAPSVASSVASSSGSLRHRRPLISPARLNLKGQKLLLFSSPGEAPNTPSSSEEFSPPNGSLFIESPQLPQRNHTRDTKHTMEMRSMLARDSARSSHSIKKEDESSQSSTCVVDTTTKGCSEETTPWKARVSPSLVRGLLAVSLAVNALFTSAYLYQSLR
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Involved in nuclear movement during fibroblast polarization and migration. May recruit Ran GTPase to the nuclear periphery (By similarity). [Isoform 2]: May define a distinct membrane domain in the vicinity of the mitotic spindle. Involved in the organization of the nuclear envelope implicating EMD, SUN1 and A-type lamina.
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A2A935
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PRD16_MOUSE
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Histone-lysine N-methyltransferase PRDM16 (EC 2.1.1.367) (PR domain zinc finger protein 16) (PR domain-containing protein 16) (Transcription factor MEL1) (MDS1/EVI1-like gene 1)
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MRSKARARKLAKSDGDVVNNMYEPDPDLLAGQSAEEETEDGILSPIPMGPPSPFPTSEDFTPKEGSPYEAPVYIPEDIPIPPDFELRESSIPGAGLGIWAKRKMEIGERFGPYVVTPRAALKEADFGWEMLTDTEVSSQESCIKKQISEDLGSEKFCVDANQAGSGSWLKYIRVACSCDDQNLAMCQINEQIYYKVIKDIEPGEELLVHVKEGAYSLGVMAPSLDEDPTFRCDECDELFQCRLDLRRHKKYACSSAGAQLYEGLGEELKPEGLGVGSDGQAHECKDCERMFPNKYSLEQHMIVHTEEREYKCDQCPKAFNWKSNLIRHQMSHDSGKRFECENCVKVFTDPSNLQRHIRSQHVGARAHACPDCGKTFATSSGLKQHKHIHSTVKPFICEVCHKSYTQFSNLCRHKRMHADCRTQIKCKDCGQMFSTTSSLNKHRRFCEGKNHYTPGSIFTPGLPLTPSPMMDKTKPSPTLNHGGLGFSEYFPSRPHPGSLPFSAAPPAFPALTPGFPGIFPPSLYPRPPLLPPTPLLKSPLNHAQDAKLPSPLGNPALPLVSAVSNSSQGATAATGSEEKFDGRLEDAYAEKVKNRSPDMSDGSDFEDINTTTGTDLDTTTGTGSDLDSDLDSDRDKGKDKGKPVESKPEFGGASVPPGAMNSVAEVPAFYSQHSFFPPPEEQLLTASGAAGDSIKAIASIAEKYFGPGFMSMQEKKLGSLPYHSVFPFQFLPNFPHSLYPFTDRALAHNLLVKAEPKSPRDALKVGGPSAECPFDLTTKPKEAKPALLAPKVPLIPSSGEEQPLDLSIGSRARASQNGGGREPRKNHVYGERKPGVSEGLPKVCPAQLPQQPSLHYAKPSPFFMDPIYRVEKRKVADPVGVLKEKYLRPSPLLFHPQMSAIETMTEKLESFAAMKADSGSSLQPLPHHPFNFRSPPPTLSDPILRKGKERYTCRYCGKIFPRSANLTRHLRTHTGEQPYRCKYCDRSFSISSNLQRHVRNIHNKEKPFKCHLCNRCFGQQTNLDRHLKKHEHEGAPVSQHSGVLTNHLGTSASSPTSESDNHALLDEKEDSYFSEIRNFIANSEMNQASTRMDKRPEIQDLDSNPPCPGSASAKPEDVEEEEEEELEEEDDDSLAGKSQEDTVSPTPEPQGVYEDEEDEEPPSLTMGFDHTRRCVEERGGGLLALEPTPTFGKGLDLRRAAEEAFEVKDVLNSTLDSEVLKQTLYRQAKNQAYAMMLSLSEDTPLHAPSQSSLDAWLNITGPSSESGAFNPINHL
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Binds DNA and functions as a transcriptional regulator. Displays histone methyltransferase activity and monomethylates 'Lys-9' of histone H3 (H3K9me1) in vitro. Probably catalyzes the monomethylation of free histone H3 in the cytoplasm which is then transported to the nucleus and incorporated into nucleosomes where SUV39H methyltransferases use it as a substrate to catalyze histone H3 'Lys-9' trimethylation. Likely to be one of the primary histone methyltransferases along with MECOM/PRDM3 that direct cytoplasmic H3K9me1 methylation. Functions in the differentiation of brown adipose tissue (BAT) which is specialized in dissipating chemical energy in the form of heat in response to cold or excess feeding while white adipose tissue (WAT) is specialized in the storage of excess energy and the control of systemic metabolism. Together with CEBPB, regulates the differentiation of myoblastic precursors into brown adipose cells. Functions as a repressor of TGF-beta signaling.
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A2A974
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CP4CB_MOUSE
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Cytochrome P450 4A12B (EC 1.14.14.1)
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MSASALSSIRFPGSISEYLQVASVLSLLLLLFKTAQLYLHRQWLLSSTQQFPSPPSHWLFGHKILKDQDLQDILTRIKNFPSACPQWLWGSKVRIQVYDPDYMKLILGRSDPKAHGSYRFLAPWIGRGLLLLDGQTWFQHRRMLTPAFHYDILKPYTEIMADSVHVMLDKWEQIVGQDSTLEIFQHITLMTLDTIMKCAFSHEGSVQLDRKYKSYIQAVEDLNNLFFLRVRNIFHQNDIIYRVSSNGCLANSACQLAHDHTDQVIKSRRSQLQDEEELEKLKKKRRLDFLDILLFARMENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGASITWNDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFPDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSRHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLPDPTRVPIPIPRIVLKSKNGIHLHLKKLQ
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A cytochrome P450 monooxygenase involved in the metabolism of fatty acids and their oxygenated derivatives (oxylipins). 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). Catalyzes predominantly the oxidation of the terminal carbon (omega-oxidation) of saturated and unsaturated fatty acids. May act as a major omega-hydroxylase for dodecanoic (lauric) acid in kidney. Participates in omega-hydroxylation of (5Z,8Z,11Z,14Z)-eicosatetraenoic acid (arachidonate) to 20-hydroxyeicosatetraenoic acid (20-HETE), a signaling molecule acting both as vasoconstrictive and natriuretic with overall effect on arterial blood pressure. Acts as an omega-hydroxylase and epoxidase toward (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoc acid (EPA). Catalyzes the epoxidation of the last double bond of EPA with no preferred stereoselectivity, producing both (R,S) and (S,R) stereoisomers. Can also catalyze the omega-1 and omega-2 oxidation of fatty acids with lower efficiency.
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A2A9A2
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DMTA2_MOUSE
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Doublesex- and mab-3-related transcription factor A2 (Doublesex- and mab-3-related transcription factor 5)
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MELRSELPSVPGAATAAATATGPPVASVASVAAAAAAAASLPVSVAGGLLRAPPLLLRAAEKYPRTPKCARCRNHGVVSALKGHKRYCRWKDCLCAKCTLIAERQRVMAAQVALRRQQAQEENEARELQLLYGTAEGLALAAANGIIPPRPAYEVFGSVCATDGGGPGAGAPAGSAGGAGGAEAKLQKFDLFPKTLLQAGRPDSPQPPPGKPLSPDGADSGPRTSSPEVRPGSGSENGDGESFSGSPLARASKEAGGSCPGSAGAGGGGEEDSPGSSSPLGSESGSEADKEEAEAAPTPGLGGGPGPRQRTPLDILTRVFPGHRRGVLELVLQGCGGDVVQAIEQVLNHHRGGLAAGLGPAAPLEKAAVSAAVEDAWPGRVEAAAAGGAGLPAPLQTGPTAPPHHRPLLAGAMTPGALGSLSSRSAFSPLQPNASHFGADAGAYPLGAPLGLSPLRLAYSAAAAHSRGLAFMAPYSTAGLVPTLGFRPPMDYAFSDLMRDRSAAAAAAVHKEPGYGGGLYGPMVNGTPEKQ
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May be involved in sexual development.
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A2A9C3
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SZT2_MOUSE
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KICSTOR complex protein SZT2 (Seizure threshold 2 protein) (Transcript increased in glutamate resistance) (TIGR)
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MASERPEPEVEEAGQVFLLMKKDYRISRNVRLAWFLNHLHQTVQATPQELLLQSEQELEVLSVLPPGWQPDEPVVPRPFLLVPSTRVTFLAWQYRFVIELDLSPSTGIVDDSTGEILFDEVFHALSRCLGGLLRPFRVPGSCINFQPEIYVTIQAYSSIIGLQSHQVLVQGCLLDPSQREAFLQQVYEQLCLFEDKVATMLQQQYEPQGQAEDQSPESGESLGRKVGVSMVTADLGLVSMIRQGILALQLLPSNSSAGIIVITDGVTSVPDVAVCETLLNQLRSGTVACSFVQVGGVYSYDCSFGHVPNVELMKFIAMATFGSYLSTCPETEPGNLGLTVYHRAFLLYSFLRSGEALNPEYYCGSQHRLFNEHLVSASSNPALALRRKKHTEKEVPADLVSTVSVRLREGYSVREVTLAKGGSQLEVKLVLLWKHNMRIEYVAVAPWPLEPEGPRGTRVEVTMEGGYDILHDVSCALRQPIRSLYRTHVIRRFWNTLQSINQTDQMLAHLQSFSSVPEHFTLPDSTKSGVPLFYIPPGSSTPVLSLQHSGSDSSHAQFAAYWKPVLSMDANSWQRWLHMHRLVLILEHDTPLPKHLHTPGSNGRYSTIQCRISHSSLTSLLRDWSSFVLVEGYSYVKLLSSAPDQPPSSFYMVRIISKTPCMVLRLGFPIGTPAQARHKIVSGLKEEILRLRFPHRVQSKEPTPKVKRKGLGGVGGSSPSKSPPTLGPQQALSDRPCLVVLHKPLDKLLIRYEKLPLDYRAPFLLTLEPPGPLPLVSGRSASSSLASLSRYLYHRRWLWSVPSGLAPTLPLSATAQLLSVLTEVRLSEGFHFACSGEGIINMVLELPVQNEPLGQAAAEEKHTCVVQYILFPPHSTSTKDSFSTDDDNDVEVEALEGDSELNLVTEVWVEPQYGRVGPGPENWKHLQDLTYSEIPQALHPRDAACIGSLLTFEYLIQLCQSKEWGPLPPEPRLSDGLDQRGDTCVHEIPFHFDLLGLLPQCQQLQMFFLLLSREPEGVPLAEGPCPTNDMVLCLLHSCLGQELSDREIPLTPADQAAFLNEVLRRSLRDPGPEGPPVGGHAVAKDRAGNSTQASGDSTLPSQSVVIPGVLRSSISAQPPQWHCYARLLGPQHVFLTFLPATFSDVQHLTAYGLESSFQEETKPKLGDWSGAPSLKDPGATGTKATESQVPTLSVTLASDSAQDSGEPSTPSCQDLAANSGRQAPQTEGADGPRTRCPVYIYSCSLEALREQMVGLQPPQAPRDLIFRAQDLDHPSSSSAWMEPRCKEAATHCALLQEHAQRCFVRGLFRSLQQAQSVTCQDLLTAVDACEELLQEIDITSFLLALCGHTWGLPHAPPSPGPLSPGPFSSSIEEGPEPRERAILVSESSIETEDLSEPEFQSSRVSGNLDPGPEISLTDVCQLRGEAHDALHSLIQEKFLEISRLHFRTVPSNPHYFFYCPPSSRREDEGPRDTVDRKISDLEFSEAELVGEEGDTSACCVVTESDPELEVEYRESREPDLGPAGLDSASLSDADTVNPDEDSFSILGGDSPTGPDSLMHDLPPLFLHLTCSVRLRGQHSSVPVCSLPTCLGQVLSSLEGPPIGGRVPLRDLSITLDVFVLTLPLEVELPPASDPQHHRSTSESSASFPRSPGQPSSLRSDDGLGPPLPPPEEERHPGLSSLAMPHRLAIESTMNEIRWLLEDEMVGALRRGGIPQSPALHRAAAHIHSSSGRPTCLRQAPPLSFVFGPERSLTQFKEEFRRLHLPGHVLLEDPDSGFFFVAAGQQPGVLHGEPPSAAWAWHNHEDRAEDAEGEVLTASPQVPGSLEDSEGTPLISLPSLSQGGSQPGPSRGLSLMSSQGSVDSDHLGYDGGSSGSDSEGPGETLGEKALFTLRTPPGPAPPQPSLPVLPGPSLPDFWLIVRILQDRVEVYAHARSLSREDGGPGAECRHLQQFLVRRVGEICREVNQRLLLQDLHDSHVCNSLLVAESEEDLWRSETPFHSRQRAVLPSDDFAADESCAPRGYLAATMQFVPGHFSCDVVWGTVIRVHSRLKMGPSMGVSRAIQALRSVLNAFSVVNRKNMFVYQERATKAVYYLRLLETSCSDRPWEGDTLPPSLALSRSQEPISSEDSVAPRSPLDMASSRSSDAVRPVGQVDRHIQLLVHGVGQAGPEITDELVRVLRRRLDEATLDIITVMLVRNCKLTPADVEFIQPPGSLPSEVLHLVLPPSCRPCLPALAWYLRQNLLTFLHSPKYTDSNSRNHFQHPLPAQGGLPDLDIYLYNKPGGQGTGGKGVACITLAFVEEGGTPISLASWPPSSPGPPDPLREEEFEQLTQVIRCPNTLDSCSAQDGSPRLRLDVWEKGNISIVQLEEKLRAAARQALADAIMELRLLPASLCTEDIPPGSLKSGPLDTKSPACRANTFPCTPVSGEPVTPPSKAGRRSFWDMLSKTEAGDLGSPKTTDDIVLDRPEDTRGRRRHKTENVRTPGGSERAPGPDSGAQRQRRRTTQLEEGEVGTLHPVFARVIQRWMGFMVQIGCASVSRSSTHMVSRFLLPSILSEFTTLVISMAGDTSVRVFEQHLGSEPDVFSPCSPGQLGPAPRPAAQRHLLLLGRNFAQWRRPTQQAAKAVQRFESGGDGSPGRSAPRQRLLLLEVTDKKLQLLTYNWAPDLGAALGRALIRLVQWQNARAHLISCLLSQKLGLFHHCGQLDFPMRDGKEPNPFLLPTMEVETLIRNASPPLSREQGRLSGSSRGGGPLSLDTFPFDEALRDITAARPSSTGGPAPRPPDPVTYHGQQFLEIKMTERKELERQMKMENLFVTWQQRSAPASMPISAGELETLKQSSRLVHYCATALLFDPAAWLHGPPETCAPSEGQRRPCPESGSGSREVPTSCESLDVPPPGAREEPWLKELSLAFLQQYVQYLQSIGFVLVPLRPPSPARSTSRLRAMAILGTEGRGSFSCPKAKAEGSPKSTSTPVTTYHLQRALPGGIILMELTFQGCYFCVKQFALECSRIPMGQAVNSQLSLLFTEECDKVRDLMHVHSFSYDFHLRLVHQHVLGAHLALRHGYHLTTFLQHFLAHHPDGPHFGRNHIYQGTLELPTPLIAAHQLYNYVADHASSYHMKPLRMARPGGPEHNEYALVSAWHSSGSYLDSEGLRHQDDFDVSLLVCHSAAPFEEQGEAERHVLRLQFFVVLTSQRELFPRLTADMRRFRKPSRLPLEPETPGSLVGSPREASGMMLAPGPAPLFPPLAAEVGMARARLAQLVRLAGGHCRRDTLWKRLFLLEPPGPDRLRLGGRLALAELEELLEAVHAKSIADIDPQLDCFLSMTVSWYQSLIKVLLSRFPQSCRHFQSPDLGTQYLVVLNQKFTDCFVLVFLDSHLGKTSLTVVFREPFPVQPQDSESPPAQLVSTYHHLESVINTACFTLWTRLL
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As part of the KICSTOR complex functions in the amino acid-sensing branch of the TORC1 signaling pathway. Recruits, in an amino acid-independent manner, the GATOR1 complex to the lysosomal membranes and allows its interaction with GATOR2 and the RAG GTPases. Functions upstream of the RAG GTPases and is required to negatively regulate mTORC1 signaling in absence of amino acids (By similarity). In absence of the KICSTOR complex mTORC1 is constitutively localized to the lysosome and activated. The KICSTOR complex is also probably involved in the regulation of mTORC1 by glucose. May play a role in the cellular response to oxidative stress.
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A2A9F4
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KDF1_MOUSE
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Keratinocyte differentiation factor 1
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MPRPGQPRPSSGPPRLGPWERPSELCLETNDERSQPPPGRRTRRPDPKDPGHHGPESITFISGSAEPANEPPTCCLLWRPWGWDWCRAAFCFRRCRDCLQRCGACVRGCSPCLSAGDPIEGSAEAAWAKEHNGVPPSPDRAPPSRRDGQRLKTSMGSSFSYPDVKLKGIPVYPYRHATSPVPDVDSCCKEPLAEPPPTRHSLPSTFTNSPRGSEEYYSFHESDLDLPEMGSGSMSSREIDVLIFKKLTELFSVHQIDELAKCTSDTVFLEKTSKISDLISSITQDYHLDEQDAEGRLVRGIIRISTRKSRSRPQTSEGRSARSTAPAAAPDSGHETMLGSGLSQDELTVQISQETTADAIARKLRPYGAPGYPASQDSSFQGTDTDSSGAPLLQVYC
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Plays a role in the regulation of the epidermis formation during early development. Required both as an inhibitor of basal cell proliferation and a promoter of differentiation of basal progenitor cell progeny.
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A2AA28
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MET23_MOUSE
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Histone-arginine methyltransferase METTL23 (EC 2.1.1.319) (Methyltransferase-like protein 23)
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MDSVRPRAPWAPPPDPASLDSPTCEPGLMAGTQLFRFREEPVPGGNRAVLEVRVPQVLHVQYGMYVWPCAVVLAQYLWFHRRSLPGKAVLEVGAGVSLPGILAAKCGAKVILSDSSEFPHCLDICRQSCQMNNLPQVEVVGLTWGHISKDILSLPPQDIILGSDVFFEPEDFESILATVYFLMQKNPKVQFWSTYQVRSADWSLEGLLYKWDMKCVHIPLESFDADKEDIAESTLPGRHTVEMLIISFAKDSF
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Histone methyltransferase that dimethylates histone H3 at 'Arg-17', forming asymmetric dimethylarginine (H3R17me2a), leading to activate transcription via chromatin remodeling. Maternal factor involved in epigenetic chromatin reprogramming of the paternal genome in the zygote: mediates H3R17me2a, promoting histone H3.3 incorporation in the male pronucleus, leading to TET3 recruitment and subsequent DNA demethylation.
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A2AAE1
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BLTP1_MOUSE
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Bridge-like lipid transfer protein family member 1 (Fragile site-associated protein homolog)
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MDQRKNDSIVPSITQLEDFLTEHNSNVVWLLVATILSCGWIIYLTYYNSRNVGLILTLVLNRLYKHGYIHIGSFSFSVLSGKVMVREIYYITEDMSIRIQDGFIIFRWWKMYNPKQKQHDPKAETRLYITVNDFEFHVYNRSDLYGRLQELFGLEPTIIPPKKDDDKTRENGRTRTQSKIERVKVKTESQDPTSSWRSLIPVIKVNVSTGRLAFGNHYQPQTLCINFDDAFLTYTTKPPSSHLDQFMHIVKGKLENVRVMLVPSPRYVGLQNDEPPRLMGEGFVVLQSNDVDLYYYMDEPGLVPEETEESTEGDISSEDCKLQDLPPCWGLDIVCGKGTDFNYGPWADRQRDCLWKFFFPPDYQVLKVSEIAQPGRPRQILAFELRMNIITDATIDLLFTKNRETNAVHVNVGAGSYLEINIPMTVDENGYTPAIKGQLLHVDATTSMQYRTLLEAEMLAFHINASYPRIWNMPQTWQCELEVYKATYHFIFAQKNFFTDLIQDWSSDNAPDIFSFVPYTWNFKIMFHQFEMIWAANQHNWIDCSTKQQENVYLAACGETLNIDFSLPFTDFVPATCNTRFSLRGEDVDLHLFLPDCHPSKYSLFMLVKNCHPNKMVPETGIPAECQSGQKTVKPKWRNVTQEKAGWVECWTVPSVMLTIDYTWHPIYPQKADEQLKQSLSEMEETMLSVLRPAQKTSERVVSSPSMSPRPPVDPSELPPDKLHVEMELSPDSQITLYGPLLNAFLCIKENYFGEDDMYMDFEEVISSPVLSLSTSSSSGWTAVGMDNDKRENESSAKSIHPLALRPWDITVLVNLYKVHGRLPVHGTTDGPECPTAFLERLCFEMKKGFRETMLQLVLSPLNVFVSDNYQQRPPVDEVLREGHINLSGLQLRAHAMFSAEGLPLGSDSLEYAWLIDVQAGSLTAKVTAPQLACLLEWGQTFVFHVVCREYELERPKSVIVCQHGIDRRFCESKLSCIPGPCPTSDDLKYTMTRLAIDGSDIYIVEHGCATNIKMGAVRIANCNLHNQSVGEGISAAIQDFQVRQYIEQLNNCRIGLQPAVLRRAYWLEAGSANLGLITVDIALAADHHSKHEAQRHFLETHDARTKRLWFLWPDDTLKNKRCRNKCGCLGGCRFFGGTVTGLDFFKLEELTPSSSSAFSSTSAESDMYYGQSLLQPGEWIITKEIPKTVDGNVNSMKRKEWENKSVGIEGERKTQHLSLQVPLRSHSSSSSSEENSSSSAAQPLLAGEKESPSSAADDHSVQKDLLHSARRDDGQASVPTEISGTSPVSPNTQDKSVGQSPLRSPLKRQASVCSTRLGSTKSLTAAFYGDKQPVTVGVQFSSDVSRSDENVLDSPKQRRSFGSFPYTPSADSNSFHQYRSMDSSMSMADSEAYFSAAEEFEPISSDEGPGTYPGRKKKKKQMQQIDYSRGSIYHSVEGPLAVHGEGITDPRTLPFKTHPSQASFVSALGGEDEVIEHVYIVEGEKRGESEQVTSQQPVMSCYHTYLTQFQVINWSVKHPTNKRTSKSSLHRPLDLDTPTSEESSSSFEQLCVPTFKVIKQGLTANSLLDRGMQLSGSTSNTPYTPLDKKIVDTTDDETLTEEWTLDQPVAQTKTTAIVEVKGTVDVVLTPLVAEALDRYIEAMVHRVSTRHPAAIVDDLHTKVLREAVQNSKTTFSENLSPKQDIRGTKTEHPMIGTTNQGQIQTNVTTKQDNVTIKGLQANVSIPKVNLCLLQASVEESPATVPSRSVTHVSLVALCFDRIATQVRMNRGVVEETANNVDAGKTSNFDRYVHASKMQPQSSGSLRSNAGAEKGKEIAAKLNIHRVHGQLRGLDTTDIGTCAITAIPFEKSKVLFTLEELDEFTFVDETDQQAIPDVTRIGPSQEKWGWIMFECGLENLTIKGGRQSGAVLYNSFGIMGKNSVTERGGVLTSNNSSDSPTGSGYNTDVSDDNLPCDRTSPSSDINGNSVSDEQDEGVESDDLKKDLPLMPPPPDSCSMKLTIKEIWFSFAAPTNVRSPAHAFSRQLNLLSTATPAVGAWLVPIDQLKSSLNKLETEGTLRICAVMGCIMTEALENKSVHFPLRSKYNRLTKVARFLQENPSCLLCNILHHYLHQANYSIIDDATMSDGLPALVTLKKGLVALARQWMKFIVVTPAFKGVSLHRPAQPLKPPATVDQEHEEGLGLDNGGGLQSDTSADGAEFEFDAATVSEHTMLLEGTANRPPPGSSGPVTGAEIMRKLSKTHTHSDSALKIKGIHPYHSLSYTSGDTATDSPVHVGRAGMPVKESPRKESLLSYLTGSFPSLHNLLEGTPQRSSAAVKSSSLTRTGNTVATDMLSEHPLLSEPSSVSFYNWMSNAVGNRGSVVQESPVTKSGHNSLPTGVAPNLPTIPSASDFNTVLSSDQNTLDGTHSQHSTSQDDVAGVEEANQGFPAVQLADAQVVFKPLLSHTGIQSQDTMPLCYRMYFGEHLSFSGTLDCLRADIVDSDTAKDRKGKRARRQGHVNLPPLEFKPALMLETFSISAVVMEKSVCTPQNSTSALSFHDLNKRYYNTFHCNFTISCQSISQHVDMALVRLIHQFSTMIDDIKATQTDIKLSRYTAGSASPTPTFKTRKHRDFRSSDFSRSSRGSLNGGNRVNNAKNKRANNENNKKESRNKNSLGRSERRTSKVSRKGSKDVVDHMTIHMDDSDSITVSEQSEPSAECWQNMYKLLNFYSLISDPTGILEKSSETFGPAGVRSPTEPTCRVVFENEQDNNSLTKTQRKRSLVTSEPQHVTLIVFGIGMVNRTHLEADIGGLTMESELKRIHGSFTLKEKMKDVLHQKMTETCATAHIGGVNIVLLEGITPNIQLEDFPTSPTSTAKQEFLTVVKCSIAKSQALYSAQRGLKTNNAAVFKVGAISINIPQHPATLHSMMVRSSHQLSKQISDLIRQPSTAPQPMKEDIATPLPSEKTPTSVNQTPIETNEFPQLPEGLEKKPIVLKFSAMLDGIAIGAALLPSLKAEYKMGRMRSHGMTGAQTRFTFELPNHRLRFTSKVSATDMSTIPPSASLNLPPVTMSGKYIMEEHDSYSDQVWSIDELPSKQGYYLQGNYLRCVAEVGSFEHNLTTDLLNHLVFVQKVFMKEVNEVIQKVSGGEQPIPLWNEHDGTTDGDKPKILLYSLNLQFKGIQVTATTPSMRAVRFETGLIELELSNRLQTKASPGSSSYLKLFGKCQVDLNLALGQIVKHQVYEEAGSDFHQVAYFKTRIGLRNALREEISGSSDREAVLITLNRPIVYAQPVAFDRAVLFWLNYKAAYDNWNEQRMALHKDIHMATKEVVDMLPGIQQTSAQAFGTLFLQLTVNDLGICLPITNTAQSNHTGDLDTGSALVLTIESTLITACSSESLVSKGHFKNFCIRFADGFETSWDDWKPEIRGDLVMNACVVPDGTYEVCSRTTGQAAAESSSAGTWTLNVLWKMCGIDVHMDPNIGKRLNALGNTLTTLTGEEDIDDIADLNSVNIADLSDEDEVDTMSPTIHTEAVDYRRQGTSSSQPGELRGRKIMKRLVDIRELNEQAKVIDDLKKLGASEGTINQEIQRYQQLESVAVNDIRRDVRKKLRRSSMRAASLKDKWGLGYKPSYSRSKSISASGRPPLKRMERASSRIGETDELPEIRVDAASPGPRVTFNIQDTFPEETELDLLSVTIEGPSHYSSNSEGSCSVFSSPKTTGGFSPSVPFQSEDGRRDDSLSSTSEDSEKDEKDEDRERERFYIYRKPSHTSRKKATGFAAVHQLLTERWPTTPVNRSLSGTATERNIDFELDIRVEIDSGKCVLHPTTLLQEHDDISLRRSYDRSSRSLDQDSPSKKKKFQTNYASTTHLMTGKKVPSSLQTKPSDLETTVFYIPGVDVKLHYNSKTLKTESPNASRGSSLPRTLSKESKLYGMKDSAASPSPSPLPCTVQSKTNTLLPPQPPPIPSAKGKGSGGVKTAKLYAWVALQSLPEEMVISPCLLDFLEKALETIPITPIERNYTAVSSQDEDMGHFDIPDPMEESTTSLVSSSTSAYSSFPVDVVVYVRVQPSQIKFSCLPVSRVECMLKLPSLDLVFSSNRGELETLGTTYPAETVSPGSNAPQTGAKTSASKAGMPGSSGLGSPLGRSRHSSSQSDLTGSSSSSSGLSFTACMSDFSLYVFHPYGAGKQKSTVSGLTSGSGGLGNVDEEPTSVTGRKDSLSINLEFVKVSLSRIRRSGGASFFESQSVSKSTSKMDTTLINISAVCDIGSASFKYDMRRLSEILAFPRAWYRRSIARRLFLGDQTVNLPTSGPGTPDSIEGVSQHLSPESSRKAYCRTWDQPSQSASFTHMPQSPNVFNEHMTNNTMSPGTAAQSLKSPASIRSRSVSDSSVPRRDSISKTSTPVNKSNKAASQQGTPWETLVVFAINLKQLNVQMNMSNVMGNTTWTTSGLKSQGRLSVGSNRDREISMSVGLGRSQLDSKGGVVGGTIDVNALEMVAHISEHPNQQPNHKIQITMGSTESRVDYMGSSILMGIFSNADLKLQDEWKVNLYNALDSSMTDKSEIFVHGDLKWDIFQVMISRSTTPDLIKIGMKLQEFFTQQFDTSKRALSTWGPVPYLPPKTMTNNLEKNSQEQLLDAAHHRHWPGVLKVVSGCHISLFQVPLPEDGMQFGGSMSLHGNHMTLACFHGPNFRSKSWALFHLEEPNIAFWTEAQKIWEDGSSDHSTYIVQTLDFHLGHNTMVTKPCGALESPMATITKITRRRHENPPHGVASVKEWFNYVTATRNEELNLLRNVDANNTENSTTVKNSSLLSGFRGGSSYNHETETIFALPRMQLEFKSIHVQEPQEPSLQDASLKPKVECSVVTEFTDHICVTMDAELIMFLHDLVSAYLKEKEKAIFPPRILSTRPGQKCPLIIHDDSSSDRDREDSITYTTVDWRDFMCNTWHLEPTLRLISWTGRKIDPVGVDYILQKLGFHHARTTIPKWLQRGVMDPLDKVLSVLIKKLGTALQDEKEKKGKDKEEH
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Tube-forming lipid transport protein which provides phosphatidylethanolamine for glycosylphosphatidylinositol (GPI) anchor synthesis in the endoplasmic reticulum. Plays a role in endosomal trafficking and endosome recycling. Also involved in the actin cytoskeleton and cilia structural dynamics. Acts as regulator of phagocytosis.
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A2AAJ9
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OBSCN_MOUSE
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Obscurin (EC 2.7.11.1) (Obscurin-RhoGEF) (Obscurin-myosin light chain kinase) (Obscurin-MLCK)
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MDHSFSGAPRFLTRPKAFVVSVGKDATLSCQIVGNPTPHVSWEKDRQPVEAGARFRLAQDGDVYRLTILDLALGDSGQYVCRARNAIGEAFAAVGLRVDSEGTCAEQAPHFLLRPTSIRVREGADATFRCRVGGSPQPAVSWSKDGRRLGPPDAPHVRVEEHGESSALRIRSARPRDGGTYEVRAENPLGSASAAAALVVDSDAEVAGPPGTSTATLLAHLQQRREAMRAEGIPPSPPGAGTRTCTVTEGKHARLSCFVTGEPKPETVWKKDGQLVTEGRRHVVYEDEQENFVLKILFCKQSDRGLYTCTASNLVGQTYSSVLVVVREPTVPFKKRLQDLEVREKESATFQCEVAQPATEAAWFKEETRLWASAKYDIEEEGTERRLTVRNVSADDDAVYICETTEGSRTVAELSVQGNLTRKLPRKTAVRTGDTAIFWVELAVPEGPVRWLRNQEEMVAGGRVAITAEGTCHTLTIFQCTLEDMGEVAFVSGGCRTTTQFCVSAPRRPPLYPPADPVVKAKTESSVTLSWSAPPHGDRPVTIDGYVLEKRKLGAYAWSRCHEAGWLATTEFTITGVAEEGDFQFRVSAINHFGQGPYLEFPGTMHLVPMLAVKTPLKAVEAVEGGEVTFSVDLTVASSGEWFLDGEALKASSIYVIRCDRTRHMLTIREVPARLHGAQLKFVANGIETSIQMVVRAALGLPSSKLPAAAAREVLAQLHEEAQLLAELSDQAAAVTWLKDGRELSLGPKYEMQVSAGRRALLVRDVAQDDAGLYECVSRGSRTAYQLLVQDITDGYRDWGPAGPQKHMCKCAGAKIARYLGSSCYRFLQYDKGVWHWLEAALDTRQGKGTSSCSLHEKPKLVFAKGQQAHSEVKAEAGNSATLSCEVTQAQTEVTWFKDGKKLSSSSKVRMEASGCSRRLVVQQAGKADAGEYSCEAGGQKLSFRLDVAEPKLVFAKGQQAHSEVKAEAGASATLSCEVAQAQTEVTWFKDGKKLSSSSKVRMEASGCSRRLVVQQAGKADAGEYSCEAGGQKLSFRLDVAEPKMVFAKEQQARSEVKAEAGASATLSCEVAQAQTEVTWFKDGKKLSSSSKVRMEASGCSRRLVVQQAGKADAGEYSCEAGGQKLSFRLDVTEPKLVFAKEQQARSEVKAEVGNSATLSCEVAQAQTEVTWFKDGKKLSSSSKVRMEASGCSRRLVVQQAGKADAGEYSCEAGGQKLSFRLDVAEPKLVFAKEQQARSEVKAEAGNSATLSCEVAQAQTEVTWFKDGKKLSSSSKVRMEASGCSRRLVVQQAGKADAGEYSCEAGGQKLSFHLDVTEPKLVFAKEQQAHSEVKAEAGASATLSCEVAQAQTEVTWFKDGKKLSSSSKVRMEASGCSRRLVVQQAGKADAGEYSCEAEGQKLSFRLDVAEPKLVFAKEQQARSEVKAEAGASATLSCEVAQAQTEVTWFKDGKKLSSSSKVRVEASGCSRRLVVQQAGKADAGEYSCEAGGQKLSFRLDVAEPKLVFAKEQQANSEVKAEAGASATLSCEVAQAQTEVTWFKDGKKLSSSSKVRVEASGCSRRLVVQQAGKADAGEYSCEAGGQKLSFRLDVAEPKLAFAKEQQAHSEVKAEAGASATLSCEVAQAQTEVTWFKDGKKLSSSSKVRVEASGCSRRLVVQQAGKADAGEYSCEAGGQKLSFRLDVAEPKLAFAKEQQAHSEVKAEAGASATLSCEVAQAQTEVTWFKDGKKLSSSSKVRVEASGCSRRLVVQQAGKADAGEYSCEAGGQKLSFRLDVAEPKLAFAKEQQAHSEVKAEAGASATLSCEVAQAQTEVTWFKDGKKLSSSSKVRVEASGCSRRLVVQQAGKADAGEYSCEAGGQKLFFRLDVAEPKLMFAKEQQAHSEVKAEAGASATLSCEVAQAQTEVTWFKDGKKLSSSSKVRVEASGCSRRLVVQQAGKADAGEYSCEAGGQKLSFRLDVAEPKLVFAKEQQAHSEVKAEAGASATLSCEVAQAQTEVTWFKDGKKLSSSSKVRVEASGCSRRLVVQQVGKADAGEYSCEARGQKLSFRLDVADTRLMFAKEQQARTEVKAEAGNSATLSCEVAQAQTEVTWFKDGKKLSSSSKVRVEASGCSRRLVVQQAGKADAGEYSCEAGGQKLSFRLDVAEAESQIPERPSRREPLVVKEHETIILTATIAAPSVAAVTWLKDGVEIRRSKRHEATSLGDTHTLTVRGAQVLDSAIYSCRVGKEGQDFPVQVEEVAAKFSKPLEPVEGELGGTVMLVCELSPEQAEVVWRCGNTQLRPGKRFQMTSEGPRRTLTVSGLREDDAEEYVCESRDDRTSARLTVKVPRVVKFTSGLSAMVAEEGQEATFQCVVSPSDAGVTWYKDGMQLQPSEKFVMVESGASRSLTILGLTLEDAGQVTVEAEGASSSAALRVREAPVLFKKKLEPQTVEERTSVTLEVELTRPWPEVKWTRNAAVLTPSENVEIRAEGARHCLVLRSVGFADRGFFGCETPDDKTQAKLNVEMRQVRLVRGLQEVEAKEQGTASMDVELSHAEVEGSWTRDGLRLQPGPKCHLAVQGPVHILTLSALQPQDSGLVAFRAEGVHTSARLIVTELPVSFTRVLQDVVATQKEKVTLECELSRPVDVRWLKDGVELRAGKAIGIVAQGTCRSLVIYRCETGDQGVYVCDALDAQTSASLRVQGRTYTLIFRRVLAEDAGEVKFVAENAESRAHLRVKELPVTLLRPLRDKIAMEKHRGVLECQVSRASAQVRWFKGGVELQSGPKYEVVSDGLYRKLVINDVQPEDEDTYTCDAGNVKTSAQFFVEEQSITIVRGLKDMTVMEPAPAWFECETSIPSVRPPKWLLGKTVLQAGGNVGLEQDGTVHRLTLHKTCSTMTGPVHFTIGKSRSSAQLVVSDIPVVLTRPLEPKAGRELQSVVLSCDFRPAPKAVQWYKDDTPLSPSEKFKMALEGQMAELRILRLTPADAGVYRCQAGSAQSSAEVTVEAREVTVIQPLQDAEAMEEGRVCFSCELSHKDEDIEWSLNGTPLYNDSFHEISHEGCLHTLVLKSVRQADTGTVCATSPKVSVSARLVVKGKPVVFLKALDDVSAEERGTLTLQCEVSDPEARVVWRKDGVELGPSDKYDFLHKAGARGLTVHDLSHEDAGLYTCQVGSKETQSKVSVHDLHVGITKRLKTVEVLEGESCSFECVLSHESPSDPAVWTVGGKTVGGSGHFHAVRQGRKYTLTVKDAALSDAGEVVFSVLGLTSKASLIIRERPVDITKPLEDQRTTLGEDVMLSCELSRAGTSVRWLKDGKAIRKSQKYDLLSEGTRAVLVVRKASLKDSGEYTCETEASKSTAKLCVEEKANRFTEELADLQVEEKGRAVFTCKTEHPASVVTWRKGLLELRASGKHVPSQEGLTLKLTINALERTDSDTYTCDIGQARTQARLLVHGQKVRVIEDLEDTAVQEGSSAKFCCRIAPADYGPVHWFLDKTPLHSNELNEITVQPGGYHVLTLRQLALKDSGTVYFEAGDQRTSAALRVTEKPSIFSRPLTDVTVTEGEDLTLVCETTTVDSSVRWTKDGKTLRPSARCQLSHEGCQAQLLITATTPQDGGRYKCEIGGASSSSIVRVHALPVRFRESLKDVEVPEGKAATLRCVLSSVAAPVEWRHGDDVLKSSNKYSLRQEGAVLELVIRDLQPQDSGQYSCSFGDQTTSATLTVKTSSAQFVGKLRNKEATEGTTVTLRCELTKEAPVEWKKGTETLRNGDKYSLKQDGAVCELQICSLLVADAGEYSCVCGQEKTSATLTVKALLVHFVRRLRSKEATEGDTTTLQCELSKAAPVEWRKGTETLRDGDRYSLKQDGAVCELQIRSLTIADAGEYLCTCGQEKTSATLTVRALPAKFKDSLKNEEATEGTTATLSCELSKAAPVTWKKGPKTLQSGDKYVLRQDGAVCGLQIHGLTMADAGEYSCVCGQEKTSATLTVRGLPAKFIEDLRSQEATEGATAILRCELSKAAPVEWRKGSETLKDGDRYTLRQDGAVCELQIRGLAVVDTGTYSSLPTKFTEGLRNEEATEGTMATLRCQMSKAAPVEWRKGSETLRDGDRYSLRQDGAMCELQIRGLTIEDSGEYTCVCGQEKTSATLSVKALPSRFIEDLRSQEATEGTMATLRCQMSKTAPVEWKKGSETLRDGGRYSLRQDGPVCELQICDLAVEDAGEYSCVCGQEKTSATLSIKALPPRFIEDLRSQEATEGTMATLRCQMSKAAPVEWRKGSETLGDGGRYSLRQNGAVCELQIHDLAVEDTGEYSCVCGQEKTSATLNVKALPPRFIEDLRSQEATEGTMATLRCQMSKAAPVEWRKGSETLRDGGRYSLRQDGAVCELQIHDLDVEDAGQYSCVCGQEKTSAVLTVDALPPKFTEGLKKEEATEGTMVTLRCQMSKEATVEWRKGAKTLSDGGRYSLRQDGAMCELQICGLAVEDAGEYSCVCGQEKTSATLSVKALPPRFIEDLRSQEATEGTMATLRCQMSKAAPVEWRKGSETLRDGDRYSLRQDGAVCELQIRDLAVEDAGEYLCVCGQEKTSATLSVKALPPRFIEDLRSQEATEGTMATLRCQMSKAAPVEWRKGSKTLRDGDRYSLRQDGAMCELQICDLAVEDTGDYSCVCGQEKTSATLSVKALPPRFIEDLRSQEAREGTVATLRCRMSKAAPVEWRKGSETLKDGDRYSLRQEGNLCELQIRDLAVEDTEEYSCVCGQEKTSATLSVKALPAKFIEDLRSQEAPESSTVTLRCKLSKKASVVWKKGSETLRNGARYSLRQDGAVCELEIRDLTVEDTGEYSCTCGQERTSATLSIMAPQVVFQQPLQNLQAEEGSMASLRCELSVPNAAMVWSKGGLELQGDTRREARQQGCVAELLLRDLRREDAGEYSCTCGSQTTSATLMVTAAPVRFLRELQAQDVDEGATARLRCELSREAVSVEWRKGSLQLFPCAKYQMVQEGTTAELLVHGVEQEDAGEYTCDAGHTQSIARLSVRAPKPKFKTDLQSTEQEAGGTARLCCQLSEAEPGTPVQWLKEGVELHVGSKYEMRRQGAVCELLIHGLEAKDTGEYACLVGGQKTLASLRVKEPEVTIVRGLVDMEVQADEDVEFTCKVSQAGATDVQWHLQGLPLQSNEVTEVAVLADGCTHVLQLKGVTLEDAGTVSFHVGGLSSSAQLTVRVPEVTVLEPLKDVQLSEGQDAHFRCRLSRASGQEARWALGGVPLQCNEMNDITVEQGTLYLLTLHKVTLEDAGTITLQVGSCSSEAQLKVTAKNTVLRGLENVDALEGGEALFECQLSQPEVAAHTWLLDDEPVHTSEKVEVVYFENGLRHLLLLKNLKPQDSCRVTFLAGDVVTSAFLTVRGWRLEVLEPPHDASVKAGMQVRFTCILSEAVPVGEATWYINGAAIQPDDTDWTVTTDGSHHALTLSNAQPQHAGEVTFAARDAVASARLSVLALPDPPEDAEVVGRSDHSVTLSWVAPMSDGGGGLCGYRVEMKEASTGQWQLCHDLVPGPECVVDDLVPGKTYRFRVAAVGPAGAGEPVHLPQMVKIAPAPAPAPAPAPAPAPETRQAVVGEDICLELEVAADGGEVVWHKGTERIQPGGHFEVLSRGQRQMLVIKGFRTEDQGEYRCGPIQGLPSSGAATFNVVMTSGSGDEVPAQPSLPPEAAQEGDLHLLWEALARKRRMSREPTLDSISELPEEDSRVQHLRQEAEETAPDLSEGYSTADELARTGEADLSHTSSDDESRAGTPSLVTYLKKAGGPGISPLASKHEAQVTTSVKPQKQQEPVVPTCPPPGDLSAADLMDPSLDKAAVKIQAAFKGYKVRKEMKQQEGPVFSRTFGDTEAQVGDVLRLECVLATKTDMRACWLKDGIELTDGRHYHIDQLKDGTCSLLVTGLAPTDSGRYTCQVSTKSGRVSHSACVVVSGTESEAESSSGGELDDAFRRAARRLHRLFRTKSPAELSEEELFLSADEGPGEPEEPADWQTYREDENFVCIRFESLAEARQAVTCFRNMFATMGIGVEISLGEQGPRGVEMRIGKVAPTVTPAVPLAKTPGLQTSDAAPVFLTELQNQDVQDGYPMSFDCVVTGQPVPSVRWFKDGKLLEEDDHYMINEDQQGGHQLIITAVVPADMGVYRCLAENSMGVSSTKAELRVELTSTDYDTAADATETSSYFSAQGYLSSREQEGTESDEGQLPQVLEELKDLQVAPGTRLAKFQLKVKGYPAPKLYWFKDGQPLTTSDHIRMTDKKTLHTLEIVSVTREDSGQYAAYISNAVGAAYSSARLLVRGPSEPEEKPASDVHERLVPPRILEKFTPKKVKRGSSITFSVKVEGHPAPSVHWLKEEAEKGVLWIGPDTPGYTMASSSKQHSLVLLDVGRQHQGTYTCIATNPAGQALCSASLHISGLAKEEEQERVKEALISSFLQGTSQAVSAQMSESAGFADLVGQSKGESLVAEEAHSHLSLAEVGTEEFLQKLTSQITEMVSAKISQAKLQVPGGDSDEETKTPSASPRHGRSRPSSSVQESSSESEDGDSRGEIFDIYVVTADYLPLGAEQDAIILREGQYVEVLDSAHPLRWLVRTKPTKSSPSRQGWVSPAYLDKRLKLSPEWGPTEAPEFPGEAVSEDEYRTRLSSVIQELLSSEQAFVGELQFLESHHMKHLERSPRVPAAVASQKTVIFRNVQDISHFHSSFLKELQGCGTDDDVAMCFIKNQEAFEKYLEFLVGRVQAESVVVSTPVQEFYKKYAEETLSAKDPTQPPPPPLQHYLEQPVERVQKYQALLKELIRNKARNRQNCALLEQAYAVVSALPQRAENKLHVSLMENYPGTLEALGEPIRQGHFIVWEGAPGARMPWKGHNRHVFLFRNYLVICKPRRDSRTDTFSYVFRNMMKLSSIDLNDQVEGDDRAFEVWHEREDSVRKYLLQARTVIIKNSWVKEICGIQQRLAQPVWRPPEFEEELADCTAELGETVKLACRVTGTPKPIVSWYKDGKPVEVDPHHILIEDPDGSCTLILDNLTGIDSGQYMCFAASAAGNASTLGKILVQVPPRFVNKVRATPFVEGEDAQITCTVEGAPYPQIRWYKDGTLLAPGNRYRMLNEPRSGVLVLVIQAASKEDLGHYECELVNRLGSTRGGGELYMQSPALRARDQHHREQIVAAVEDTSVEGSAHSAQDGADQQAASVLWRLLGSEALGPSPGDLPNTRQSEPPAFEEAASQIPGAASGTPEVSQPGTHKGLEQETTSSGSQGWTVPIRVEGTAWPGAGTGQLLLDVHSQVIMETTQRTYVCQAPDTGVTRAPSMQVTIEDVQVQVGDMAQFDAVIEGHPPPIVTWYKGSTQLTSSARLSQRQDGTTYSLVLTDVAPHDAGVYTCVANNAGGQVLCKAELLVHGGDKLDAENQVYRRKLHSFYDVQEEIGRGVFGFVKRVQHKGNKMFCAAKFIPLRSKTRAQAYQERDILATLGHPLVTGLLDQFETRKTLILILELCSSEELLDRLFKKGVVTEAEVKVYIQQLVEGLHYLHSHGILHLDIKPPNILMVHPAREDIKICDFGFAQKITPSEPQYSKYGSPEFVSPEIIEQNPVSEGSDIWAMGVISYLSLTCSSPFAGESDRATLLNVLEGRVSWSSPTAAHLSEDAKDFIKATLQRTPRARPSTSQCLAHPWFLKSMPAEEAHFINTKQLKFLLARSRWQRSLMSYKSILVMRSIPELLQGPPDSPSLGVARHLRGEASGASSSSSSSDNELAPFARAKSLPPSPVTHSPLLHPRGFLRPSASLPEETEASMPTADAAVPASPQSAGPPASPGCVPRHSVISSLFYQQAGEGAERGNKTSGAKRHPARRRHLLKGGYIARALPGLREPLMEYSLLEEEAAREEQASLMTKTPSFETALRLPSSSVREVPGRSHSLDNPPVTTGPSPEACKEQLLFPPSTGLTHETTAKDRGHKEGFLQESVPFPPMSGDSRPGKQEGSSQDSCRGKPASSCHSELGSGSQEGCGPPSSQSLGSLPPQSLKKELSTSCGPLFSEQPQAAPFPTQVSPLLGSEKEPQDGSLSEGPVPVPSSSPGSASQVDASLDTEGLSEAGDTCDFTPPPQRPQEQATTRKFSLESRGGYAGVAGYGTFAFGGDAGGMLGQGPLWARMAWAVSQSSEEQDEAATESPQPLESLGPIAEASGVPLRTSPSLTPWEEVEQVSLVQIRDLSGDAEAADTISLDISEVDPAYLNLSDLYDIKYLPFEFMIFRRVPKPIEQPESPGSETEAGQGLADFLEEAAWPWPGELGLRAGLEITEEPEEPGDLEALLGEAAVGRKRKWSPSRGLFQFPGRCLSGEEPVELGLRQRVKASMAHISRILKGRPEGPEREGPPRKKAGLASFRLSGLKGRDQELSDEAVVLGQSVTLACQVLAQPTAQATWSKDGVLLESSGHLLISSTLKNFQLLTILVVKEEDLGTYTCCVSNPLGTAVTTGVLRKAERPSSSPRPEVGELYKDAVLLVWKPVESCGPVTYIVQCCIEGGSWTTLASDISDCCYLTGKLSRGGMYIFRTACVSKAGMGPYSSPSEQVLLGGPNHLASEEESSRGRPAQLLPSTKTFAFQMQIRRGRFSVVRQCREKASGRALAAKIVPYQPEDKTAVLREYEALKRLHHPHLAQLHAAYLSPRHLVLILELCSGPELLPSLAERESYSESDVKDYLWQMLSATQYLHAQHILHLDLRSENMMVTEYNLLKVIDLGNAQSLDQEKVPAPENFKDYLETMAPELLEGQGAVPQTDIWAIGVTAFIMLSGEYPESSEGTRDLQKGLRKGLIRLSRCYAGLSGGAVAFLQSSLCAQPWGRPCASTCLQCGWLTEEGPTGSRPTPVTFPTVRLRAFVREREKRRALLYKKHNLAQVR
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Structural component of striated muscles which plays a role in myofibrillogenesis. Probably involved in the assembly of myosin into sarcomeric A bands in striated muscle (By similarity). Has serine/threonine protein kinase activity and phosphorylates N-cadherin CDH2 and sodium/potassium-transporting ATPase subunit ATP1B1. Binds (via the PH domain) strongly to phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) and phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), and to a lesser extent to phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-phosphate (PtdIns(4)P), phosphatidylinositol 5-phosphate (PtdIns(5)P) and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) (By similarity). Isoform 2 and isoform 3: bind phosphatidylinositol bisphosphates (PIP2s) via their PH domains and negatively regulate the PI3K/AKT/mTOR signaling pathway, thus contributing to the regulation of cardiomyocyte size and adhesion.
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A2AAY5
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SPD2B_MOUSE
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SH3 and PX domain-containing protein 2B (Factor for adipocyte differentiation 49) (Tyrosine kinase substrate with four SH3 domains)
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MPPRRSIVEVKVLDVQKRRVPNKHYVYIIRVTWSSGATEAIYRRYSKFFDLQMQMLDKFPMEGGQKDPKQRIIPFLPGKILFRRSHIRDVAVKRLIPIDEYCKALIQLPPYISQCDEVLQFFETRPEDLNPPKEEHIGKKKSGNDPTSVDPMVLEQYVVVADYQKQESSEISLSVGQVVDIIEKNESGWWFVSTAEEQGWVPATCLEGQDGVQDEFSLQPEEEEKYTVIYPYTARDQDEMNLERGAVVEVVQKNLEGWWKIRYQGKEGWAPASYLKKNSGEPLPPKLGPSSPAHSGALDLDGVSRHQNAMGREKELLNNQRDGRFEGRLVPDGDVKQRSPKMRQRPPPRRDMTIPRGLNLPKPPIPPQVEEEYYTIAEFQTTIPDGISFQAGLKVEVIEKSLSGWWYIQMEDKEGWAPATFIDKYKKTSSASRPNFLAPLPHEMTQLRLGDAAATENNTGPEAVGPSRPLPEAPHGAVDSGMLWSKDWKGGKEAPRKASSDLSASTGYEEISDPTQEEKPSLPPRKESIIKSEEELLERERQKMEPLRGSSPKPPGMILPMIPAKHAPLARDSRKPEPKLDKSKFPLRNDMGLECGHKVLAKEVKKPNLRPISRSKAELSEEKVDPTSQNLFMKSRPQVRPKPTPSPKTEPAQSEDHVDIYNLRSKLRPAKSQEKALLDGESHHAAGSHDTALSRSFLPGEGPGHGQDRSGRQDGLSPKETPCRAPPRPAKTTDPGPKNVPVPVQEATLQQRPVVPPRRPPPPKKTSSSPLSCRPLPEVRGAQREESRVAPAAGRALLVPPKAKPFLSNSSVGQDDMRGKGGLGPRVTGKVGETREKAASFLNADGPKDSLYVAVANFEGDEDTSSFQEGTVFEVREKNSSGWWFCQVLSGAPSWEGWIPSNYLRKKP
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Adapter protein involved in invadopodia and podosome formation and extracellular matrix degradation. Binds matrix metalloproteinases (ADAMs), NADPH oxidases (NOXs) and phosphoinositides. Acts as an organizer protein that allows NOX1- or NOX3-dependent reactive oxygen species (ROS) generation and ROS localization. Plays a role in mitotic clonal expansion during the immediate early stage of adipocyte differentiation.
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A2ABV5
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MED14_MOUSE
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Mediator of RNA polymerase II transcription subunit 14 (Cofactor required for Sp1 transcriptional activation subunit 2) (CRSP complex subunit 2) (Mediator complex subunit 14) (Thyroid hormone receptor-associated protein complex 170 kDa component) (Trap170)
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MAPVQLDNHQLIPPGGGGGSSGGGGSSSGSASAPAPPPPAAAVAAAAAAAASPGYRLSTLIEFLLHRAYSELMVLTDLLPRKSDVERKIEIVQFASRTRQLFVRLLALVKWANDAGKVEKCAMISSFLDQQAILFVDTADRLASLARDALVHARLPSFAIPYAIDVLTTGSYPRLPTCIRDKIIPPDPITKIEKQATLHQLNQILRHRLVTTDLPPQLANLTVANGRVKFRVEGEFEATLTVMGDDPEVPWRLLKLEILVEDKETGDGRALVHSMQIDFIHQLVQSRLFADEKPLQDMYNCLHCFCLSLQLEVLHSQTLMLIRERWGDLVQVERYHAGKSLSLSVWNQQVLGRKTGTASVHKVTIKIDENDVSKPLQIFHDPPLPASDSKLVERAMKIDHLSIEKLLIDSVHARAHQRLQELKAILRSFNANESSSIETALPALIVPILEPCGNSECLHIFVDLHSGMFQLMLYGLDPATLEDMEKSLNDDMKRIIPWIQQLKFWLGQQRCKQSIKHLPTITTETLQLANYSTHPIGSLSKNKLFIKLTRLPQYYIVVEMLEVPNKPTQLSYNYYFMSVSTADREDSPVMALLLQQFKDNIQDLMSYTKTGKQTRTGTKHKLSDDPCPIDSKKAKRSGEMCAFNKVLAHFVAMCDTNMPFVGLRLELSNLEIPHQGVQVEGDGFNHAIRLLKIPPCKGISEETQKALDRSLLDCTFRLQGRNNRTWVAELVFANCPLNGTSTREQGPSRHVYLTYENLLSEPVGGRKVVEMFLNDWSSIARLYECVLEFARSLPEIPAHLNIFSEVRVYNYRKLILCYGTTKGSSISIQWNSIHQKFHIALGTVGPNSGCSNCHNTILHQLQEMFNKTPNVVQLLQVLFDTQAPLNAINKLPTVPMLGLTQRTNTAYQCFSILPQSSTHIRLAFRNMYCIDIYCRSRGVVAIRDGAYSLFDNSKLVEGFYPAPGLKTFLNMFVDSNQDARRRSVNEDDNPPSPIGGDMMDSLISQLQPPQQQPFPKQPGTSGAYPLTSPPTSYHSTVNQSPSMMHTQSPGNLHAASSPSGALRAPSPASFVPTPPPSSHGISIGPGASFASPHGTLDPSSPYTMVSPSGRAGNWPGSPQVSGPSPATRLPGMSPANPSLHSPVPDVSHSPRAGTSSQTMPTNMPPPRKLPQRSWAASIPTILTHSALNILLLPSPTPGLVPGLAGSYLCSPLERFLGSVIMRRHLQRIIQQETLQLINSNEPGVIMFKTDALKCRVALSPKTNQTLQLKVTPENAGQWKPDELQVLEKFFETRVAGPPFKANTLIAFTKLLGAPTHILRDCVHIMKLELFPDQATQLKWNVQFCLTIPPSAPPIAPPGTPAVVLKSKMLFFLQLTQKTSVPPQEPVSIIVPIIYDMASGTTQQADIPRQQNSSVAAPMMVSNILKRFAEMNPPRQGECTIFAAVRDLMANLTLPPGGRP
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Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity).
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A2AC93
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DNAI2_MOUSE
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Dynein axonemal intermediate chain 2 (Axonemal dynein intermediate chain 2)
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MEIVYVYLKKRSEFGKQCNFSDRQAELNIDILPNPELAALYVERNPVDTGIQCSASMSEHEANTERFEMESCGVNHVEGGWPKDVNPQELEQTIRFRKKVEKDENYINAVMQLGSIMEHCIKQNNAIDIYEEYFDDEEAVEVTEEAPSAKTINVFRDPQEIKRTATHLSWHPDGNRKLAVAYSCLKFQRAPMSMNYDSYIWDLENPNRPEIALKPLSPLVTLEYNPKDSHVLLGGCYNGQIACWDTRKGSLVAELSTIEFSHRDPVYGTIWLQSKTGTECFSASTDGQVMWWDIRKISEPIEVVIMDISRKEQLENALGAISLEFESTLPTKFMVGTEQGIVISCNRKAKTQAEKIVCTFYGHHGPIYALQRNPFYPKNFLTVGDWTARIWSEDSRESSIMWTKYHMAYLSDGAWSPVRPAVFFTTKMDGTLDIWDLVFKQCDPALSLKVCDDPLFCLRVQDNGCLIACGSELGTTTLLEVSSSLSTLQRNEKNIASSIFERETRREKILEARHREMRLKEKGKVEGKEDDQKEEEAALDLDELVGKAEEEFFEVIFSELKRKEAEALKKKPKPRKKSSVKVEAEEEVEENVGEEEEAGGIIGIDAVEDMSEEAGEEQEDVPT
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Part of the dynein complex of respiratory cilia.
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A2AD83
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FRMD7_MOUSE
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FERM domain-containing protein 7
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MLHLKVQFLDDSQKIFVVDQKSSGKALFNLSCGHLNLAEKEYFGLEFCSHSGNNVWLELLKPITKQVKNPKEVVFKFMVKFFPVDPGHLREELTRYLFTLQIKKDLALGRLPCSDNCTALMVSHILQSELGDFHEETVRKHLVQTQYLPSQASLESKIMQFHQQHIGRSPAESDILLLDIARKLDMYGIRPQPASDGEGMQIHLAVAHMGVLVLRGNTKINTFNWAKIRKLSFKRKHFLIKLHANILVLCKDTLEFTMASRDACKAFWKTCVEYHAFFRLSEEPKSKPKTLLCSKGSSFRYSGRTQRQLLEYGKKGRLKSLPFERKQYPSQYHERQCRSSPDILSDVSKQVEDLRLTYGSSYYRNVNGVHASESMLDSRRRNSAVEVTFAAELEHSKPEAEATSLHPSQSSSSFTFIYADPVFNTDPEPIEFFEERSPLSSFQTTSKFADSHTSKASPARQLTYTDVPYIPCTSQKVDIMPPQVFFYVDKPPQVPRRSLIMAEENMRPDSYVDHSAIKPAKRSPRNMRIKSLQQDLQELQEAMARTSGRSNINVEPEEEDPHLDDAFAYNLQEQTPKRSQSQSDMKTIRFPFGSEFRPLGPCPALTRKTDLFACTFAEQEFPTVLIDQSSAERYVASESSDSESEIIKPDYYFLYGKGTKSPRARIRLSSGSLQLEEEDETISFATPGAEDRTLLKPCNYFLA
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Plays a role in neurite development, may be through the activation of the GTPase RAC1. Plays a role in the control of eye movement and gaze stability.
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A2AF47
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DOC11_MOUSE
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Dedicator of cytokinesis protein 11 (Activated Cdc42-associated guanine nucleotide exchange factor) (ACG) (Zizimin-2)
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MAEVRKFTKRLSKPGTAAELRQSVSEAVRGSVVLEKAKLVEPLDYENVITQRKTQIYSDPLRDLLMFPMEDISISVIGRQRRTVQSTVPEDAEKRAQSLFVKECIKTYSTDWHVVNYKYEDFSGDFRMLPCKSLRPEKIPNHVFEIDEDCEKDEDSSSLCSQKGGVIKQGWLHKANVNSTITVTMKVFKRRYFYLTQLPDGSYILNSYKDEKNSKESKGCIYLDACIDVVQCPKMRRHAFELKMLDKYSHYLAAETEQEMEEWLIMLKKIIQINTDSLVQEKKDTVEAIQEEETSSQGKAENIMASLERSMHPELMKYGRETEQLNKLSRGDGRQNLFSFDSEVQRLDFSGIEPDVKPFEEKCNKRFMVNCHDLTFNILGHIGDNAKGPPTNVEPFFINLALFDVKNNCKISADFHVDLNPPSVREMLWGTSTQLSNDGNAKGFSPESLIHGIAESQLCYIKQGIFSVTNPHPEIFLVVRIEKVLQGNITHCAEPYIKNSDPIKTAQKVHRTAKQVCSRLGQYRMPFAWAARPIFKDVQGSLDLDGRFSPLYKQDSSKLSNEDILKLLSEYKKPEKTKLQIIPGQLSITVECVPVDLPNCITSSYVPLKPFEKNCQNITVEVEEFVPEMTKYCYPFTIYKNHLYVYPLQLKYDSQKSFAKARNIAVCVEFRDSDESDASALKCIYGKPAGSVFTTNAYAVVSHHNQNPEFYDEIKIELPIHLHQKHHLLFTFYHVSCEINTKGTTKKQDTVETPVGFAWVPLLKDGRVITLEQQLPVSANLPPGYLNVNDAESRRQSNADIKWVDGAKPLLKIKTHLESTIYTQDLHVHKFFHHCQLIQSGSKEVPGELIKYLKCLHAMEIQVMIQFLPVILMQLFRVLTNMTHEDDVPINCTMVLLHIVSKCHEEGLESYLRSFIKYSFRPEKPSTLQAQLIHETLATTMIAILKQSADFLAINKLLKYSWFFFEIIAKSMATYLLEENKIKLPRGQRFPEAYHHVLHSLLLAIIPHVTIRYAEIPDESRNGNYSLASFLKRCLTLMDRGFVFNLINDYISGFSPKDPKVLAEYKFEFLQTICNHEHYIPLNLPMAFAKPKLQRVQDSNLEYSLSDEYCKHHFLVGLLLRETSIALQDNYEIRYTAISVIKNLLIKHAFDTRYQHKNQQAKIAQLYLPFVGLLLENIQRLAGRDTLYSCAAMPSSASRDEFPCGFVSPTNRGSLASDKDTAYGSFQNGHGIKREDSRGSLIPEGATGFPDPGSTSENTRQSSSRSSVSQYNRLDQYEIRNLLMCYLYIVKMISEDTLLTYWNKVSPQELINILVLLEVCLFHFRYMGKRNIARVHDAWLSKHFGIDRKSQTMPALRNRSGVMQARLQHLSSLESSFTLNHSSATTEADIFHQALLEGNTATEVSLTVLDTISFFTQCFKNQLLNNDGHNPLMKKVFDIHLAFLKNGQSEVSLKHVFASLRSFISKFPSAFFKGRVNMCAAFCYEVLKCCTSKISSTRNEASALLYLLMRNNFEYTKRKTFLRTHLQIIIAVSQLIADVALSGGSRFQESLFIINNFANSDRPMKATAFPTEVKDLTKRIRTVLMATAQMKEHEKDPEMLIDLQYSLAKSYASTPELRKTWLDSMAKIHIKNGDFSEAAMCYVHVAALVAEFLHRKKLFPSGCSAFKKITPNIDEEGAMKEDAGMMDVHYSEEVLLELLEQCVDGLWKAERYEVISEISKLIIPIYEKRREFEKLTQVYRTLHGAYTKILEVMHTKKRLLGTFFRVAFYGQSFFEEEDGKEYIYKEPKLTGLSEISLRLVKLYGEKFGTENVKIIQDSDKVNAKELDPKFAHIQVTYVKPYFDDKELTERKTEFERNHNINRFVFEAPYTLSGKKQGCIEEQCKRRTILTTSNSFPYVKKRIPINCEQQVNLKPIDVATDEIKDKTAELHKLCSSVDVDMIQLQLKLQGCVSVQVNAGPLAYARAFLNESQANKYPPKKVNELKDMFRKFIQACSIALELNERLIKEDQIEYHEGLKSNFRDMVKELSDIIHEQILQEDTMHSPWMNNTLHVFCAISGTSSNRGYGSPRYAEV
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Guanine nucleotide-exchange factor (GEF) that activates CDC42 by exchanging bound GDP for free GTP. Required for marginal zone (MZ) B-cell development, is associated with early bone marrow B-cell development, MZ B-cell formation, MZ B-cell number and marginal metallophilic macrophages morphology. Facilitates filopodia formation through the activation of CDC42.
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A2AFS3
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ELAP1_MOUSE
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Endosome/lysosome-associated apoptosis and autophagy regulator 1
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MAEPGHNPHPSARDGGKTERRTPRLLWLLLWAGTTFQVTLGTGPELHACKESEYHFEYTACDSTGSRWRVAVPHSPGLCTSLPDPVKGTECSFSCNAGEFLDMKDQSCKPCAEGRYSLGTGIRFDEWDELPHGFASLSANLEVDDSISESTENCTSSKWVPRGDYIASNTDECTATLMYAVNLKQSGTVNFEYYYPDSSIIFEFFVQNDQCQPSADDSRWMKTTEKGWVELNRGNNVLYWRTTAFSVWSKVSKPVLVRNIAITGVAYTSECFPCKPGTYAAKQGSPFCKLCPANYYSNKGETSCHPCDADKYSEKGSSTCKVRPACTDKDYFYTHTACDAQGETQLMYKWAIPKICGEDLEGAVKLPASGVKTRCPPCNPGFFKTDNSTCEPCPYGSYSNGSDCTHCPAGTEPAVGFEYKWWNTLPSNMETTVLSGINFEYKGLTGWEVAGDHIYTAVGASDNDFMILTLVVPGFRPPQSVVADTENKEVARITFVFETICSVNCELYFMVGMNSRTNTPVETWKGTKGKQSYTYTIEENATVSFTWAFQRTTLHETGRKYTNDVAKIYSINVTNVMGGVASYCRPCALEASDLGSSCTSCPAGHYINRDSGTCHLCPSNTILKAHQPYGAQACVPCGPGTKNNKIHSLCYNDCTFSRNTPSRIFNYNFSALAGTVSLAGVPSFTSKGLKYFHHFTLSLCGNQGKKMAVCTDNVTDLRIPDGEAGFSKSVTAYVCQVVIIPSEVMGYKAGVSSQPVSLADRLVGVSTDMTLEGIVSPVELFHPETSGIPDIVFFFRSNDVTQSCSSGRSTTIRLRCNPMKAAPGTLRLPSMCSDGTCDGCNFHFLWESVAACPLCSASDYHTFVSSCVAGIQKTTYMWREPKLCSGGISLPEQRVTICKTIDFWLKVGISAGTCTAILLTVLTCYFWKKNQKLEYKYSKLVMNATLKDCDLPAADSCAIMEGEDVEDDFIFTSKKSLFGKIKSFTSKRTPDGFDSVPLKTSSGGPDMDM
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May protect cells from cell death by inducing cytosolic vacuolization and up-regulating the autophagy pathway. May play a role in apoptosis and cell proliferation through its interaction with HSPA5.
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A2AG06
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MEIOC_MOUSE
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Meiosis-specific coiled-coil domain-containing protein MEIOC (Meiosis-specific with coiled-coil domain protein)
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MEVSGGDTCRPRHPQGLREGPEPKVAAAAAAFRGSANRCWNLSVDTSNRLSDVFNSMMLTGSAPFYDCYKSQNEDNVDLRQTCTPLSSSTEYASSIDSSLFYAPWSTYGDDIKQPPSSQISVKNRIQTERNDYGSETDLYGLVSNILEEQDKSQPYFAEGTCSSNLKSVWPMNTSRFVDHHDLLTEPKRPVDTSISQQAFYSGESVSAVEKQYLHNSSLTPQQKIDELYHGYTGLDLEEQWLYLSRSDHSNCYNSQANDTVKATFQEYPFVKNCFTPQTGLSDIMKESGIDTYAYGREKICTKGLETPLQHKRAEIFLSQFNRYNENADYCRYPEYAHPNKAKLNKCSNFSVQDGKKLANGTPETPTVEADAYTKLFQVKPANQKKMEETIPDQQNFAFPKTTPHLTEKQFAKEAAFTADFGLKSEYGLKPHTACPTNNDFANVSEKQQFAKPDPLNSEYFKSVNLFSNSATSSGGISLNRPTWMNVQTKNNLPIPYRNQGNLMKLNSHLSAASKGSNHSSDFPQLSSTNLTSNSNLFQKYCQENPSAFSSFDFSYNGAERIQSVNHMEGLTKTGEDNLFESVTEKKIKQPNGFCDSYSASQYGIIENVNKHNFQAKPQSGHYDPEDIPKHFDGLPQNTYQDLLESQGHFNSHRQGSGDNNINSRVNRTQASCFSNNYMMGDLRHNQGFQQLGSNGFPLRSTHPFGHSVVPLLDSYDLFSYDDLSHLYPYFNDMMYGDNSFSGFVPTFGFQRPIKTRSGPASELHIRLEECYEQWRALEKERKKTELALAKNYPGKKVSSTNNTPIPRLTSNPSRVDRLIVDELREQARVVTLLGKMERLRSSPLHANISTALDRHLESIHIVQSRRKDEIVNASNRQRQGVPRCQDDRDVFALATAIKEMCVATRKARTTLWCALQMTLPKTASTAGQADMEKAFQDLVNCEEKVHESINSSNPMNQRGETSKH
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Is required for meiosis completion in both male and female germ cells. Confers stability to numerous meiotic mRNAs in gonads allowing proper initiation and progression into meiosis prophase I. The function may involve YTHDC2 and is independent of induction by retinoic acid (RA). Maintains an extended meiotic prophase I by properly promoting the transition from a mitotic to a meiotic cell cycle program by binding transcripts through its interaction with YTHDC2 that regulate the mitotic cell cycle.
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A2AGH6
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MED12_MOUSE
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Mediator of RNA polymerase II transcription subunit 12 (Mediator complex subunit 12) (OPA-containing protein) (Thyroid hormone receptor-associated protein complex 230 kDa component) (Trap230) (Trinucleotide repeat-containing gene 11 protein)
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MAAFGILSYEHRPLKRLRLGPPDVYPQDPKQKEDELTALNVKQGFNNQPAVSGDEHGSAKNVNFNPAKISSNFSSIIAEKLRCNTLSDTGRRKSLMNQKDNFWLVTARSQSAINTWFTDLAGTKPLTHLAKKVPIFSKKEEVFGYLAKYTVPVMRAAWLIKMTCAYYAAMSETKVKKKNTADPFTEWTQIITKYLWEQLQKMAEYYRPGPAGSGGCGSTIGPLPHDVEMAIRQWDYNEKLALFMFQDGMLDRHEFLTWVLECFEKIRPGEDELLKLLLPLLLRYSGEFVQSAYLSRRLAYFCTRRLALQLDGVSSHSSHVIAAQSTSSLPTTPAPQPPTSSTPSTPFSDLLMCPQHRPLVFGLSCILQTILLCCPSALVWHYSLTDSRIKTGSPLDHLPIAPSNLPMPEGNSAFTQQVRAKLREIEQQIKERGQAVEVRWSFDKCQEATAGFTIGRVLHTLEVLDSHSFERSDFSNSLDSLCNRIFGLGPSKDGHEISSDDDAVVSLLCEWAVSCKRSGRHRAMVVAKLLEKRQAEIEAERCGESEAADEKGSVASGSLSAPSAPIFQDVLLQFLDTQAPMLTDPRSESERVEFFNLVLLFCELIRHDVFSHNMYTCTLISRGDLAFGAPGPRPPSPFDDPTDDPERKEAEGSSSSKLEDPGLSESMDIDPSSSVLFEDMEKPDFSLFSPTMPCEGKGSPSPEKPDVEKEVKPPAKEKIEGTLGILYDQPRHVQYATHFPIPQEESCSHECNQRLVVLFGVGKQRDDARHAIKKITKDILKVLNRKGTAETDQLAPIVPLNPGDLTFLGGEDGQKRRRNRPEAFPTAEDIFAKFQHLSHYDQHQVTAQVSRNVLEQITSFALGMSYHLPLVQHVQFIFDLMEYSLSISGLIDFAIQLLNELSVVEAELLLKSSDLVGSYTTSLCLCIVAVLRHYHACLILNQDQMAQVFEGLCGVVKHGMNRSDGSSAERCILAYLYDLYTSCSHLKSKFGELFSDFCSKVKNTIYCNVEPSESNMRWAPEFMIDTLENPAAHTFTYTGLGKSLSENPANRYSFVCNALMHVCVGHHDPDRVNDIAILCAELTGYCKSLSAEWLGVLKALCCSSNNGTCGFNDLLCNVDVSDLSFHDSLATFVAILIARQCLLLEDLIRCAAIPSLLNAACSEQDSEPGARLTCRILLHLFKTPQLNPCQSDGNKPTVGIRSSCDRHLLAASQNRIVDGAVFAVLKAVFVLGDAELKGSGFTVPGGTEELPEEEGGGGSSGRRQGGRNISVETASLDVYAKYVLRSICQQEWVGERCLKSLCEDSNDLQDPVLSSAQAQRLMQLICYPHRLLDNEDGENPQRQRIKRILKNLDQWTMRQSSLELQLMIKQTPNTEMNSLLENIAKATIEVFQQSAETGSSSGSTASNMPSSSKTKPVLSSLERSGVWLVAPLIAKLPTSVQGHVLKAAGEELEKGQHLGSSSRKERDRQKQKSMSLLSQQPFLSLVLTCLKGQDEQREGLLASLHSQVHQIVINWRENQYLDDCKPKQLMHEALKLRLNLVGGMFDTVQRSTQQTTEWAQLLLEIIISGTVDMQSNNELFTTVLDMLSVLINGTLAADMSSISQGSMEENKRAYMNLVKKLQKDLGERQSDSLEKVHQLLPLPKQNRDVITCEPQGSLIDTKGNKIAGFDSIFKKEGLQVSTKQKISPWELFEGLKPSTAPLSWAWFGTVRVDRRVARGEEQQRLLLYHTHLRPRPRAYYLEPLPLPPEDEEPPAPALLEPEKKAPEPPKTDKPGAAPPSTEERKKKSTKGKKRSQPATKNEDYGMGPGRSGPYGVTVPPDLLHHANPGSISHLSYRQSSMGLYTQNQPLPAGGPRVDPYRPVRLPMQKLPTRPTYPGVLPTTMSTVMGLEPSSYKTSVYRQQQPTVPQGQRLRQQLQAKIQSQGMLGQSSVHQMTPSSSYGLQTSQGYTSYVSHVGLQQHTGPAGTMVPPSYSSQPYQSTHPSTNPTLVDPTRHLQQRPSGYVHQQAPTYGHGLTSTQRFSHQTLQQTPMMGTMTPLSAQGVQAGVRSTSILPEQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQYHIRQQQQQQQMLRQQQQQQQQQQQQQQQQQQQQQQQQQQQPHQQQQQAAPPQPQPQSQPQFQRQGLQQTQQQQQTAALVRQLQQQLSNTQPQPSTNIFGRY
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Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. This subunit may specifically regulate transcription of targets of the Wnt signaling pathway and SHH signaling pathway (By similarity).
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A2AGL3
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RYR3_MOUSE
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Ryanodine receptor 3 (RYR-3) (RyR3) (Brain ryanodine receptor-calcium release channel) (Brain-type ryanodine receptor) (Type 3 ryanodine receptor)
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MAEAGEGGEDEIQFLRTEDEVVLQCIANIHKEQRKFCLAAEGLGNRLCFLEPTSEAKYIPPDLCVCNFVLEQSLSVRALQEMLANTVENGGEGAAQGGGHRTLLYGHAILLRHSFSGMYLTCLTTSRSQTDKLAFDVGLREHATGEACWWTIHPASKQRSEGEKVRIGDDLILVSVSSERYLHLSISNGSIQVDASFMQTLWNVHPTCSGSSIEEGYLLGGHVVRLFHGHDECLTIPSTDQNDSQHRRVFYEAGGAGTRARSLWRVEPLRISWSGSNIRWGQAFRLRHLTTGHYLALTEDQGLLLQDRGKSDTKSTAFSFRASKEIKEKLDSSHKRDMEGMGVPEIKYGDSVCFVQHVASGLWVTYKAQDAKTSRLGPLKRKVILHQEGHMDDGLTLQRCQQEESQAARIIRNTTALFSQFVSGNNRTTAPVALPTEEVLQTLQDLIAYFQPPEDEMQHEDKQNKLRSLKNRQNLFKEEGMLALVLNCIDRLNIYNSVAHFAGIVREESGMAWKEILNLLYKLLAALIRGNRNNCAQFSNNLDWLISKLDRLESSSGILEVLHCILIESPEALNLIAEGHIKSIISLLDKHGRNHKVLDVLCSLCLCNGVAVRANQNLICDNLLPRRNLLLQTRLINDVTSIRPNIFLGVAEGSPQYKKWYFELIIDQVEPFLTAEPTHLRVGWASSSGYAPYPGGGEGWGGNGVGDDLYSYGFDGLHLWSGRIPRAVASINQHLLKSDDVVSCCLDLGVPSISFRINGQPVQGMFENFNTDGLFFPVMSFSAGVKVRFLMGGRHGEFKFLPPSGYAPCYEALLPKEKMRLEPVKEYKRDADGVRDLLGTTQFLSQASFIPCPIDTSQVVLPLHLEKIRDRLAENIHELWGMNKIELGWTYGKVRDDNKRQHPCLVEFSKLPETEKNYNLQMSTETLKTLLALGCHIAHVNPAAEEDLKKVKLPKNYMMSNGYKPAPLDLSDVKLLPPQEILVDKLAENAHNVWAKDRIKQGWTYGIQQDLKNKRNPRLVPYALLDERTKKSNRDSLREAVRTFVGYGYNIEPSDQELADPTVEKVSIDKIRFFRVERSYAVKSGKWYFEFEVVTGGDMRVGWARPGCRPDIELGADDQAFVFEGSRGQRWHQGSGYFGRTWQPGDVVGCMINLDDASMVFTLNGELLITNKGSELAFADYEIENGFVPICSLGLSQIGRMNLGTDASTFKFYTMCGLQEGFEPFAVNMNRDVAVWFSKRLPTFVNVPKDHPHIEVVRIDGTMDSPPCLKVTHKTFGTQNSNANMIYCRLSMPVECHSSFSHSPCLDSEAFQKRKQMQEILSHTTTQCYYAIRIFAGQDPSCVWVGWVTPDYHLYSEKFDLNKNCTVTVTLGDERGRVHESVKRSNCYMVWGGDIVASSQRSSRSNVDLEIGCLLDLAMGMLSFSANGKELGTCYQVEPNTKVFPAVFLQPTSTSLFQFELGKLKNAMPLSAAIFKSEEKNPTPQCPPRLDVQTIQPVLWSRMPSSFLKVETERVSERHGWVVQCLEPLQMMALHIPEENRCVDILELCEQEDLMQFHYHTLRLYSAVCALGNSRVASALCSHVDLSQLFYAIDNKYLPGLLRSGFYDLLISIHLANAKERKLMMKNEYIIPITSATRNIRLYPDESKRHGLPGVGLRTCLKPGFRFSTPCFVVTSEDHQKQSPEIPLQILKTKALSMLTEAVHCSGAHIRDPVGGSVEFQFVPVLKLIGTLLVMGVFDDDDVRQILLLIDPSVFGEHSGETEEGVEKEVTHAEEKAVEAGEKACKEAPVKGLLQTRLPESVKLQMCELLSYLCDCELQHRVEAIVAFGDIYVSKLQANQKFRYNELMQALNMSAALTARKTREFRSPPQEQINMLLNFHLGENCPCPEEIREELYDFHEDLLVHCGVPLEEEEEEEEDTSWTGKLCALVYKIKGPPKPEKEQPTEEEKPYPTTLKELVSQTMIRWAQENQIQDAELVRMMFNLLRRQYDSIGELLQALRKTYTISQASVNDTINLLAALGQIRSLLSVRMGREEELLMINGLGDIMNNKVFYQHPNLMRVLGMHETVMEVMVNVLGTEKSQIAFPKMVASCCRFLCYFCRISRQNQKAMFEHLSYLLENSSVGLASPSMRGSTPLDVAASSVMDNNELALGLEEPDLEKVVTYLAGCGLQSCPMLLARGYPDVGWNPIEGERYLSFLRFAVFVNSESVEENASVVVKLLIRRPECFGPALRGEGGNGLLAAMQGAIKISENPALDLPSQGYKTEVTQDDGEEEEIVHMGNAIMSFYSALIDLLGRCAPEMHLIQTGKGEAIRIRSILRSLVPTEDLVGIISIPLKLPSLNKDGSVSEPDMAANFCPDHKAPMVLFLDRVYGIKDQTFLLHLLEVGFLPDLRASASLDTVSLSTTEAALALNRYLCSAVLPLLTRCAPLFSGTEHCTSLIDSTLQTIYRLSKGRSLTKAQRDTIEECLLAICNHLRPSMLQQLLRRLVFDVPQLSEYCKMPLKLLTNHYEQCWKYYCLPSGWGSYGLAVEEELHLTEKLFWGIFDSLSHKKYDLDLFRMALPCLSAIAGALPPDYLDTRITATLEKQVSVDADGNFDPKPINTMNFSLPEKLEYIVTKYAEHSHDKWACDKSHSGWKYGISLDENVKTHPLIRPFKTLTEKEKEIYRWPARESLKTMLAVGWTVERTKEGEALVQQRENEKLRCVSQTNQGNSYSPAPLDLSNVVLSRELQGMVEVVAENYHNIWAKKKKLELESKGGGSHPLLVPYDTLTAKEKFRDREKAQDLFKFLQVNGILVSRGMKDLELDASSMEKRFAYKFLKKILKYVDAAQEFIAHLEAIVSSGKTEKSPHDQEIKFFAKVLLPLVDQYFTNHRLYFLSSPLKPLSSSGYASHKEKEMVASLFCKLAALVRHRISLFGSDSTTMVSCLHILAQTLDTRTVMKSGSELVKAGLRAFFENAAEDLEKTSENLKLGKFTHSRTQIKGVSQNINYTTVALLPILTSIFEHIAQHQFGVDLLLSDVQVSCYHILCSLYSLGTGKNIYVERQRPALGECLASLAAAIPVAFLEPSLNRHNPLSVFNTKTPRERSILGMPDKVEDMCPDIPQLEGLMKEINDLAESGARYTEMPHVIEVILPMLCNYLSYWWERGPENLPPSTGPCCTKVTSEHLSLILGNILKIINNNLGIDEASWMKRIAVYAQPIISKARPDLLRSHFIPTLEKLKKKAVKTVQEEEQLKTDGKGDTQEAELLILDEFAVLCRDLYAFYPMLIRYVDNNRSNWLKSPDPDSDQLFRMVAEVFILWCKSHNFKREEQNFVIQNEINNLAFLTGDSKSKMSKSGGQDQERKKTKRRGDLYSIQTSLIVAALKKMLPIGLNMCTPGDQELISLAKSRYSCRDTDEEVKEHLRNNLHLQEKSDDPAVKWQLNLYKDVLRNDEPSNPEKTVERVQSISAALFHLEQVEQPLRSKKAVWHKLLSKQRKRAVVACFRMAPLYNLPRHRSINLFLHGYQRFWIETEAHFFEEKLVQDLAKSPRVEDEEEEETERQPDPLHQIILHFSRNALTERSKLEDDPLYTSYSSMMAKSCQSGEDEEEEEDKEKTFEEKEMEKQKTLYQQARLHERGAAEMVLQMISASKGEMSPMVVETLKLGIAILNGGNAGVQQKMLDYLKEKKDAGFFQSLSGLMQSCSVLDLNAFERQNKAEGLGMVTEEGTLIVRERGEKVLQNDEFTQDLFRFLQLLCEGHNSDFQNFLRTQMGNTTTVNIIISTVDYLLRLQESISDFYWYYSGKDIIDESGQHNFSKALAVTKQIFNSLTEYIQGPCIGNQQSLAHSRLWDAVVGFLHVFANMQMKLSQDSSQIELLKELLDLLQDMVVMLLSLLEGNVVNGTIGKQMVDTLVESSTNVEMILKFFDMFLKLKDLTSSDTFKEYDPDGKGIISRKEFQKAMEGLKQYTQSEIDFLLSCTEADENDMFNYVDFVERFHEPAKDIGFNVAVLLTNLSEHMPNDSRLKSLLDPAESVLNYFEPYLGRIEIMGGAKKIERVYFEISESSRTQWEKPQVKESKRQFIFDVVNEGGEQEKMELFVNFCEDTIFEMQLASQISESDSTDRPEEEEEEDEDSAYSIETEGEEEEKSFESASAFTMACVSVKRNVTKFLKRATLKNLRKQYRNVKKMSAKELVKVFFSFFWMLFVGLFQLLFTIFGGIFQILWNTVFGGGLVEGAKNIRVTKILGDMPDPTQFGIHDDVIETDRAEVTEPGVTTELVHFVKGEAGDTDIMSDLFGIHSKKEGGLKQGPEVGLGDLSEIIGKDEPPTLESTVRKKRKAQAAEMKAVHEAEGKAESEKADMEDREKEDKIKEEGQTDYLWADVTVKKTRRRGQKAEKPEAFMANFFKGLEIYQTKLLHYLARNFYNLRFLALFVAFAINFILLFYKVTEEPLEEETEDVANLWNSFNDDDEEEAMVFFVLQESTGYMAPTLRALAIVHTIISLVCVVGYYCLKVPLVVFKREKEIARKLEFDGLYITEQPSEDDIKGQWDRLVINTPSFPNNYWDKFVKRKVINKYGDLYGAERIAELLGLDKNALDFSPVEEAKAEAASLVSWLSSIDMKYHIWKLGVVFTDNSFLYLAWYTTMSVLGHYNNFFFAAHLLDIAMGFKTLRTILSSVTHNGKQLVLTVGLLAVVVYLYTVVAFNFFRKFYNKSEDDDEPDMKCDDMMTCYLFHMYVGVRAGGGIGDEIEDPAGDPYEMYRIVFDITFFFFVIVILLAIIQGLIIDAFGELRDQQEQVREDMETKCFICGIGNDYFDTTPHGFETHTLQEHNLANYLFFLMYLINKDETEHTGQESYVWKMYQERCWDFFPAGDCFRKQYEDQLG
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Calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm in muscle and thereby plays a role in triggering muscle contraction. May regulate Ca(2+) release by other calcium channels. Calcium channel that mediates Ca(2+)-induced Ca(2+) release from the endoplasmic reticulum in non-muscle cells. Plays a role in cellular calcium signaling. Contributes to cellular calcium ion homeostasis. Isoform 2 lacks a predicted transmembrane segment and does not form functional calcium channels by itself however, it can form tetramers with isoforms that contain the full complement of transmembrane segments and modulate their activity.
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A2AGT5
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CKAP5_MOUSE
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Cytoskeleton-associated protein 5
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MGDDSEWLKLPVDQKCEHKLWKARLSGYEEALKIFQKIKDEKSPEWSKYLGLIKKFVTDSNAVVQLKGLEAALVYVENAHVAGKTTGEVVSGVVSKVFNQPKAKAKELGIEICLMYVEIEKGESVQEELLKGLDNKNPKIIVACIETLRKALSEFGSKIISLKPIIKVLPKLFESRDKAVRDEAKLFAIEIYRWNRDAVKHTLQNINSVQLKELEEEWVKLPTGAPKPSRFLRSQQELEAKLEQQQSAGGDAEGGGDDGDEVPQVDAYELLDAVEILSKLPKDFYDKIEAKKWQERKEALEAVEVLVKNPKLEAGDYADLVKALKKVVGKDTNVMLVALAAKCLTGLAVGLRKKFGQYAGHVVPTILEKFKEKKPQVVQALQEAIDAIFLTTTLQNISEDVLAVMDNKNPTIKQQTSLFIARSFRHCTSSTLPKSLLKPFCAALLKHINDSAPEVRDAAFEALGTALKVVGEKSVNPFLADVDKLKLDRIKECSEKVELVHGKKSGLATEKKESKPLPGRAAASGAAGDKDTKDVSGPKPGPLKKTPTAKAGGPSKKGKTTAPGGSASAGTKNKKGLETKEIVEPELSIEVCEEKASAVLPPTCIQLLDSSNWKERLACMEEFQKAVELMERTEMPCQALVKMLAKKPGWKETNFQVMQMKLHIVALIAQKGNFSKTSAQIVLDGLVDKIGDVKCGNNAKEAMTAIAEACMLPWTAEQVMSMAFSQKNPKNQSETLNWLSNAIKEFGFSELNVKAFISNVKTALAATNPAVRTSAITLLGVMYLYVGPSLRMIFEDEKPALLSQIDAEFQKMQGQSPPAPTRGIAKHSTSATDEGEDGEEPGEGGNDVVDLLPRIEISDKITSELVSKIGDKNWKIRKEGLDEVAGIINEAKFIQPNIGELPTALKGRLNDSNKILVQQTLNILQQLAVAMGANIRQHVKNLGIPVITVLGDSKNNVRAAALATVNAWAEQTGMKEWLEGEDLSEELKKENPFLRQELLGWLAEKLPTLRSTPTDLILCVPHLYSCLKDRNGDVRKKAQDALPFFMMHLGYEKMAKATGKLKPTSKDQVLAMLEKAKANMPSKPAAPAKAMSKPMGGSAPAKTQPIPAPVEDSVSSTIEAKPDLKKAKAPGVSSKAKSVQGKKVPSKTTLKEDDDKSGPIFIVVPNGKEQRMRDEKGLKVLKWNFTTPRDEYIEQLKTQMSTCVAKWLQDEMFHSDFQHHNKALAVMVDHLESEKDGVISCLDLILKWLTLRFFDTNTSVLMKALEYLKLLFTLLSEEEYHLTENEASSFIPYLILKVGEPKDVIRKDVRAILNRMCLVYPASKMFPFIMEGTKSKNSKQRAECLEELGCLIESYGMNVCQPTPGKALKEIAIHIGDRDNAVRNAALNTIVTVYNVHGDQVFKLIGNLSEKDMSMLEERIKRSAKRPSAAPVKQAEEKPQRTQNINSNANMLRKGPAEDMSSKLNQARSLSGHPEAAQMVRREFQLDLDEIENDNGTVRCEMPELVQHKLDDIFEPVLIPEPKIRAVSPHFDDMHSNTASTINFIISQVASGDINTSIQALTQIDEVLRQEDKAEAMSGHIDQFLIATFMQLRLIYSTHMADEKLDKDEIIKLYSCIIGNMISLFQIESLAREASTGVLKDLMHGLITLMLDSRIEDLEEGQQVIRSVNLLVVKVLEKSDQTNILSALLVLLQDSLLATASSPKFSELVMKCLWRMVRLLPDTINSINLDRILLDIHIFMKVFPKEKLKQCKSEFPIRTLKTLLHTLCKLKGPKILDHLTMIDNKNESELEAHLCRMMKHSMDQTGSKSDKETEKGASRIDEKSSKAKVNDFLAEIFKKIGSKENTKEGLAELYEYKKKYSDTDIEPFLKNSSQFFQSYVERGLRVIEMERESKGRIPTSTGISPQMEVTCVPTPTSTVSSLGNTNGEEVGPSVYLERLKILRQRCGLDNTKQDDRPPLTSLLSKPAIPPVASSTDMLHSKLSQLRESREQHQHSDLDSNQTHSAGTMTSSSSTTNIDDLKKRLERIKSSRK
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Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. Acts as processive microtubule polymerase. Promotes cytoplasmic microtubule nucleation and elongation. Plays a major role in organizing spindle poles. In spindle formation protects kinetochore microtubules from depolymerization by KIF2C and has an essential role in centrosomal microtubule assembly independently of KIF2C activity. Contributes to centrosome integrity. Acts as component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge. The TACC3/ch-TOG/clathrin complex is required for the maintenance of kinetochore fiber tension. Enhances the strength of NDC80 complex-mediated kinetochore-tip microtubule attachments.
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A2AH22
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AMRA1_MOUSE
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Activating molecule in BECN1-regulated autophagy protein 1
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MKVVPEKNAVRILWGRERGTRAMGAQRLLQELVEDKTRWMKWEGKRVELPDSPRSTFLLAFSPDRTLLASTHVNHNIYITEVKTGKCVHSLIGHRRTPWCVTFHPTISGLIASGCLDGEVRIWDLHGGSESWFTDSNNAIASLAFHPTAQLLLIATANEIHFWDWSRREPFAVVKTASEMERVRLVRFDPLGHYLLTAIVNPSNQQGDDEPEIPIDGTELSHYRQRALLQSQPVRRTPLLHNFLHMLSSRSSGIQVGEQSTVQDSATPSPPPPPPQPSTERPRTSAYIRLRQRVSYPTTVECCQHPGILCLCSRCAGTRVPSLLPHQDSVPPASARATTPSFSFVQTEPFHPPEQASSTQQDQGLLNRPSAFSTVQSSTAGNTLRNLSLGPTRRSLGGPLSSHPSRYHRELAPGLTGSEWTRTVLTLNSRSEVESMPPPRTSASSVSLLSVLRQQEGGSQASVYTSATEGRGFPSSGLATESDGGNGSSQNNSGSIRHELQCDLRRFFLEYDRLQELDQSLSGETPQTQQAQEMLNNNIESERPGPSHLPTPHSSENNSNLSRGHLNRCRACHNLLTFNNDTLRWERTTPNYSSGEASSSWHVSTTFEGMPPSGNQLPPLERTEGQMPSSSRLELSSSASSQEERTVGVAFNQETGHWERIYTQSSRSGTVSQEALHQDMPEESSEEDSLRRRLLESSLISLSRYDGAGSREHPIYPDPARLSPAAYYAQRMIQYLSRRDSIRQRSMRYQQNRLRSSTSSSSSDNQGPSVEGTDLEFEDFEDNGDRSRHRAPRNARMSAPSLGRFVPRRFLLPEYLPYAGIFHERGQPGLATHSSVNRVLAGAVIGDGQSAVASNIANTTYRLQWWDFTKFDLPEISNASVNVLVQNCKIYNDASCDISADGQLLAAFIPSSQRGFPDEGILAVYSLAPHNLGEMLYTKRFGPNAISVSLSPMGRYVMVGLASRRILLHPSTEHMVAQVFRLQQAHGGETSMRRVFNVLYPMPADQRRHVSINSARWLPEPGLGLAYGTNKGDLVICRPEALNSGIEYYWDQLSETVFTVHSSSRSSERPGTSRATWRTDRDMGLMNAIGLQPRNPTTSVTSQGTQTLALQLQNAETQTEREEEEPGAASSGPGEGEGSEYGGSGEDALSRIQRLMAEGGMTAVVQREQSTTMASMGGFGNNIIVSHRIHRSSQTGTESGAARTSSPQPSTSRGLPSEPGQLAERALSPRTASWDQPSTSGRELPQPALSSSSPVPIPVPLASNEGPTMHCNVTNNSHLPEGDGSNRGEAAGPSGEPQNR
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Substrate-recognition component of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex involved in cell cycle control and autophagy. The DCX(AMBRA1) complex specifically mediates the polyubiquitination of target proteins such as BECN1, CCND1, CCND2, CCND3, ELOC and ULK1. Acts as an upstream master regulator of the transition from G1 to S cell phase: AMBRA1 specifically recognizes and binds phosphorylated cyclin-D (CCND1, CCND2 and CCND3), leading to cyclin-D ubiquitination by the DCX(AMBRA1) complex and subsequent degradation. By controlling the transition from G1 to S phase and cyclin-D degradation, AMBRA1 acts as a tumor suppressor that promotes genomic integrity during DNA replication and counteracts developmental abnormalities and tumor growth. AMBRA1 also regulates the cell cycle by promoting MYC dephosphorylation and degradation independently of the DCX(AMBRA1) complex: acts via interaction with the catalytic subunit of protein phosphatase 2A (PPP2CA), which enhances interaction between PPP2CA and MYC, leading to MYC dephosphorylation and degradation. Acts as a regulator of Cul5-RING (CRL5) E3 ubiquitin-protein ligase complexes by mediating ubiquitination and degradation of Elongin-C (ELOC) component of CRL5 complexes (By similarity). Acts as a key regulator of autophagy by modulating the BECN1-PIK3C3 complex: controls protein turnover during neuronal development, and regulates normal cell survival and proliferation. In normal conditions, AMBRA1 is tethered to the cytoskeleton via interaction with dyneins DYNLL1 and DYNLL2 (By similarity). Upon autophagy induction, AMBRA1 is released from the cytoskeletal docking site to induce autophagosome nucleation by mediating ubiquitination of proteins involved in autophagy (By similarity). The DCX(AMBRA1) complex mediates 'Lys-63'-linked ubiquitination of BECN1, increasing the association between BECN1 and PIK3C3 to promote PIK3C3 activity. In collaboration with TRAF6, AMBRA1 mediates 'Lys-63'-linked ubiquitination of ULK1 following autophagy induction, promoting ULK1 stability and kinase activity (By similarity). Also activates ULK1 via interaction with TRIM32: TRIM32 stimulates ULK1 through unanchored 'Lys-63'-linked polyubiquitin chains (By similarity). Also acts as an activator of mitophagy via interaction with PRKN and LC3 proteins (MAP1LC3A, MAP1LC3B or MAP1LC3C) possibly by bringing damaged mitochondria onto autophagosomes. Also activates mitophagy by acting as a cofactor for HUWE1 acts by promoting HUWE1-mediated ubiquitination of MFN2 (By similarity). AMBRA1 is also involved in regulatory T-cells (Treg) differentiation by promoting FOXO3 dephosphorylation independently of the DCX(AMBRA1) complex: acts via interaction with PPP2CA, which enhances interaction between PPP2CA and FOXO3, leading to FOXO3 dephosphorylation and stabilization. May act as a regulator of intracellular trafficking, regulating the localization of active PTK2/FAK and SRC. Also involved in transcription regulation by acting as a scaffold for protein complexes at chromatin.
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A2AHL1
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ANO3_MOUSE
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Anoctamin-3 (Transmembrane protein 16C)
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MVHHSGSIQSFKQQKGMNISKSEITTEASLKPSRRSLPCLAQSYAHSKSLSQSASLFQSTESESQAPTSVTFLSADKPEHVTSEESRKDSTLKCSFADLSDFCLALGKDKDYLDESEHANYDRSRLLNDFVTKDKPASKTKLSKNDMSYIASSGLLFKDGKKRIDYILVYRKTNIQYDKRNTFEKNLRAEGLMLEKEPAIANPDIMFIKIHIPWDTLCKYAERLNIRVPFRKKCYYTDQKNKSKSRVQNYFKRIKKWMSQNPMVLDKSAFPELEESDCYTGPFSRARIHHFIINNKDTFFSNATRSRIVYHMLERTKYENGISKVGIRKLITNGSYIAAFPPHEGAYKSSLPIKTHGPQNNRHLLYERWARWGMWYKHQPLDLIRMYFGEKIGLYFAWLGWYTGMLIPAAVVGLCVFFYGLVTMNESQVSQEICKATEVFMCPLCDKNCSLQRLNDSCIYAKVTYLFDNGGTVFFAIFMAIWATVFLEFWKRRRSILTYTWDLIEWEEEEETLRPQFEAKYYRMEVINPITGKPEPHQPSSDKVTRLLVSVSGIFFMISLVITAVFAVVVYRLVVMEQFASFKWNFVKQHWQFATSGAAVCINFIIIMLLNLAYEKIAYLLTNLEYPRTESEWENSFALKMFLFQFVNLNSSIFYIAFFLGRFVGHPGKYNKLFERWRLEECHPSGCLIDLCLQMGVIMFLKQIWNNFMELGYPLIQNWWSRHKIKRGIQDASIPQWENDWNLQPMNIHGLMDEYLEMVLQFGFTTIFVAAFPLAPLLALLNNIIEIRLDAYKFVTQWRRPLPARATDIGIWLGILEGIGILAVITNAFVIAITSDYIPRFVYEYKYGPCANHVKQNENCLKGYVNNSLSFFDLSELGMGKSGYCRYRDYRGPPWSSKPYEFTLQYWHILAARLAFIIVFEHLVFGIKSFIAYLIPDIPKGLRERIRREKYLVQEMMYEAELEHLQQQRRKSGQPIHHEWP
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Has calcium-dependent phospholipid scramblase activity scrambles phosphatidylcholine and galactosylceramide. Does not exhibit calcium-activated chloride channel (CaCC) activity. Seems to act as potassium channel regulator and may inhibit pain signaling can facilitate KCNT1/Slack channel activity by promoting its full single-channel conductance at very low sodium concentrations and by increasing its sodium sensitivity.
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A2AI05
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NDOR1_MOUSE
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NADPH-dependent diflavin oxidoreductase 1 (EC 1.18.1.-) (NADPH-dependent FMN and FAD-containing oxidoreductase)
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MQVPQLLVLFGSQTGTAQDEAERLGREARRRRLGCRVQALDSYSVANLIREPLVIFVCATTGQGDPPDNMKNFWRFIFRKSLPSSSLCQMDFAVLGLGDSSYAKFNFVAKKLHRRLLQLGGSALLPPCLGDDQHELGPDAAIDPWVGDLWEKIMVMYPVPLDIPEIPHGVPLPSKFIFQFLQEVPSIGAEELNIASSAPQTPPSELQPFLAPVITNQRVTGPQHFQDVRLIEFDITDSNISFAAGDVVFILPSNSEAHTQQFCQVLCLDPNQFFTLKPREPGVPDPPGLPQPCTVWNLVSQYLDIASVPRRSFFELLACLSQHALEREKLLELSSARGQEELWEYCSRPRRTILEVLCDFPHTAGAIPPDYLLDLIPRIRPRAFSIASSLLAHPRRLQILVAVVKYQTRLKEPRHGLCSSWLASLNPGQAGPVRVPLWVRPGSLVFPKTPDTPIIMVGAGTGVAPFRAAIQERVAHGQTGNFLFFGCRQRDQDFYWQTEWQKLEQKGWLTLVTAFSREQEQKVYVQHRLRELGPLVWELLDGQGAYFYLAGNAKYLPTDVSEALMSIFQEEGRLSTADASAYLARLQQTLRFQTETWA
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NADPH-dependent reductase which is a central component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Transfers electrons from NADPH via its FAD and FMN prosthetic groups to the [2Fe-2S] cluster of CIAPIN1, another key component of the CIA machinery. In turn, this reduced cluster provides electrons for assembly of cytosolic iron-sulfur cluster proteins. It can also reduce the [2Fe-2S] cluster of CISD1 and activate this protein implicated in Fe/S cluster repair (By similarity). In vitro can fully activate methionine synthase/MTR in the presence of soluble cytochrome b5/CYB5A (By similarity).
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A2AIR5
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NMD3A_MOUSE
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Glutamate receptor ionotropic, NMDA 3A (GluN3A) (N-methyl-D-aspartate receptor) (N-methyl-D-aspartate receptor subtype 3A) (NMDAR3A) (NR3A) (NMDAR-L)
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MRRLSLWWLLSRVCLLLPPPCALVLAGVPSSSSHPQPCQILKRIGHAVRVGAVHLQPWTTAPRAASRAQDGGRAGAQRDEPESGTWRPPAPSQGARWLGSALHGRGPPGSRKLGEGAGTETLWPRDALLFAVENLNRVEGLLPYNLSLEVVMAIEAGLGDLPLMPFSSPSSPWSSDPFSFLQSVCHTVVVQGVSALLAFPQSQGEMMELDLVSSVLHIPVLSIVRHEFPRESQNPLHLQLSLENSLSSDADVTVSILTMNNWYNFSLLLCQEDWNITDFLLLTENNSKFHLESIINITANLSSTKDLLSFLQVQLENIRNSTPTMVMFGCDMGSIRQIFEMSTQFGLSPPDLHWVLGDSQNVEELRTEGLPLGLIAHGKTTQSVFEYYVQDAMELVARAVATATMIQPELALLPSTMNCMDVKTTNLTSGQYLSRFLANTTFRGLSGSIKVKGSTIVSSENNFFIWNLQYDPMGKPMWTRLGSWQGGRIVMDSGIWPEQAQRHKTHFHHPNKLHLRVVTLIEHPFVFTREVDDEGLCPAGQLCLDPMTNDSSILDSLFSSLHSSNDTVPIKFKKCCYGYCIDLLEQLAEDMNFDFDLYIVGDGKYGAWKNGHWTGLVGDLLSGTANMAVTSFSINTARSQVIDFTSPFFSTSLGILVRTRDTAAPIGAFMWPLHWTMWLGIFVALHITAIFLTLYEWKSPFGMTPKGRNRNKVFSFSSALNVCYALLFGRTAAIKPPKCWTGRFLMNLWAIFCMFCLSTYTANLAAVMVGEKIYEELSGIHDPKLHHPSQGFRFGTVRESSAEDYVRQSFPEMHEYMRRYNVPATPDGVQYLKNDPEKLDAFIMDKALLDYEVSIDADCKLLTVGKPFAIEGYGIGLPPNSPLTSNISELISQYKSHGFMDVLHDKWYKVVPCGKRSFAVTETLQMGIKHFSGLFVLLCIGFGLSILTTIGEHIVYRLLLPRIKNKSKLQYWLHTSQRFHRALNTSFVEEKQPCSKTKRVEKSRWRRWTCKTEGDSELSLFPRSNMGPQQLMVWNTSNLSHDNQRKYIFNDEEGQNQLGTQTHQDIPLPPRRRELPASLTTNGKADSLNVARNSVMQELSELEKQIQVIRQELQLAVSRKTELEEYQRTNRTCES
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NMDA receptor subtype of glutamate-gated ion channels with reduced single-channel conductance, low calcium permeability and low voltage-dependent sensitivity to magnesium. Mediated by glycine. During the development of neural circuits, plays a role in the synaptic refinement period, restricting spine maturation and growth (By similarity). By competing with GIT1 interaction with ARHGEF7/beta-PIX, may reduce GIT1/ARHGEF7-regulated local activation of RAC1, hence affecting signaling and limiting the maturation and growth of inactive synapses. May also play a role in PPP2CB-NMDAR mediated signaling mechanism (By similarity).
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A2AIV2
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VIR_MOUSE
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Protein virilizer homolog
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MAVDSSMELLFLDTFKHPSAEQSSHIDVVRFPCVVYINEVRVIPPGVRAHSGLPDNRAYGETSPHTFQLDLFFNNVSKPSAPVFDRLGSLEYDENTSIIFRPNSKVNTDGLVLRGWYNCLTLAIYGSVDRVISHDRDSPPPPPPPPPPPQPQPTLKRNLKHADGEKEDQFNGSPPRPQPRGPRTPPGPPPPDDDEDDPMSLPVSGDKEEDVPHREDYFEPISPDRNSVPQEGQYSDEGEVEEEPQEEGEDDEDDVDVEEEEDEDEDDCHTVDSIPDDEEEDEEEEGEEDEEGEGDDGYEQISSDEDGIADLERETFKYPNFDVEYTPEDLASVPPMTYDPYDRELAPLLYFSCPYKTTFEIEISRMKDQGPDKENSGAVEASVKLTELLDLYQEDRGAKWVTALEEIPSLIIKGLSYLQLKNTEQDSLGQLVDWTMQALNLQVAFRQPIALNVRQLKAGTKLVTSLAECGAPGVTELLQAGVINVLFDLLFADHVSSSLKLNAFKALDSVISMTEGMEAFLRSTQNEKSGYQRLLELILLDQTVRVVTAGSAILQKCHFYEILSEIKRLGDHIAEKTSAVPNHSEPDQDTDAVLERANPDYENEVEASMDMDLLESSIISEGEIEKLTNLLEEVFHVMETAPHTMTQPPVKSFPTIARITGPPERDDPYPVLFRYLHSHHFLELVTLLLSIPITSAHQGVLQATKDVLKFLAQSQKGLLFFMSEYEATNLLIRALCHLYDQDEEEGLQSDGADDAFALWLQDSTQTLQCITELFSHFQRCTASEETDHSDLLGTLHNLYLITFNPVGRSAVGHVFSLDKNLQSLITLMEYYSKEALGDSKSKKSVAYNYACVLTLVVAQSSSGVQMLEQHAASLLKLCKADENNAKLQELGKWLEPLKNLRFEINCIPNLIEYVKQNIDNLMTAEGVGLTTALRVLCNVACPPPPVEGQQKDLKWNLAVIQLFSAEGMDTFIRVLQKLNSILTQPWRLHVNMGTTLHRVTTISMARCTLTLLKTMLTELLRGGSFEFKDMRVPSALVTLHMLLCSIPLSGRLDSDEQKIQNDIIDILLTFTQGVNEKLTISEETLANNTWSLMLKEVLSSILKVPEGFFSGLILLSELLPLPLPMQTTQVIEPHDISVALNTRKLWSMHLHVQAKLLQEIVRSFSGTTCQPIQHMLRRICVQLCDLASPTALLIMRTVLDLIVEDLQSTSEDKEKQYTSQTTRLLALLDALASHKACKLAILHLINGTIKGDERYAEIFQDLLALVRSPGDSVTRQQCVEYVTSILQSLCDQDIALILPSPSEGPASELEQLSNSLPSKELMTAICDCLLATLANSESSYNCLLTCVRTMMFLAEHDYGLFHLKSSLRKNSSALHSLLKRVVSTFSKDTGELASASLDFMRQILNADAMGCCGDDSGLMEVEGAHPPRTMSLNAAELKQLLQSKEESPESLFLELEKLVLEHSKDDDSLESLLDNVIGLKQMLESSGEPLPLSDQDVEPVLSAPESLQNLFNNRTAYVLADVMDDQLKSMWFTPFQAEEIDTDLDLVKVDLIELSEKCCSDFDLHSELERSFLSEPSSPGRSKTTKGFKLGKHKHETFITSSGKSEYIEPAKRAHVVPPPRGRGRGGFGQGIRPHDIFRQRKQNTSRPPSMHVDDFVAAESKEVVPQDGIPPPKRPLKVSQKISSRGGFSGNRGGRGAFHSQNRFFTPPASKGNYSRREGTRGSSWSAQNTPRGNYNESRGGQSNFNRGPLPPLRPLSSTGYRPSPRDRASRGRGGLGPSWASTNSGSGGSRGKFVSGGSGRGRHVRSFTR
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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 in the 3'-UTR near the stop codon: recruits the catalytic core components METTL3 and METTL14, thereby guiding m6A methylation at specific sites. Required for mRNA polyadenylation via its role in selective m6A methylation: m6A methylation of mRNAs in the 3'-UTR near the stop codon correlating with alternative polyadenylation (APA).
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A2AIV8
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CARD9_MOUSE
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Caspase recruitment domain-containing protein 9
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MSDYENDDECWSTLESFRVKLISVIDPSRITPYLRQCKVLNPDDEEQVLSDPNLVIRKRKVGVLLDILQRTGHKGYVAFLESLELYYPQLYRKVTGKEPARVFSMIIDASGESGLTQLLMTEVMKLQKKVQDLTALLSSKDDFIKELRVKDSLLRKHQERVQRLKEECELSSAELKRCKDENYELAMCLAHLSEEKGAALMRNRDLQLEVDRLRHSLMKAEDDCKVERKHTLKLRHAMEQRPSQELLWELQQEKDLLQARVQELQVSVQEGKLDRNSPYIQVLEEDWRQALQEHQKQVSTIFSLRKDLRQAETLRARCTEEKEMFELQCLALRKDAKMYKDRIEAILLQMEEVSIERDQAMASREELHAQCTQSFQDKDKLRKLVRELGEKADELQLQLFQTESRLLAAEGRLKQQQLDMLILSSDLEDSSPRNSQELSLPQDLEEDAQLSDKGVLADRESPEQPFMALNKEHLSLTHGMGPSSSEPPEKERRRLKESFENYRRKRALRKMQNSWRQGEGDRGNTTGSDNTDTEGS
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Adapter protein that plays a key role in innate immune response against fungi by forming signaling complexes downstream of C-type lectin receptors. CARD9-mediated signals are essential for antifungal immunity against a subset of fungi from the phylum Ascomycota. Transduces signals in myeloid cells downstream of C-type lectin receptors CLEC7A (dectin-1), CLEC6A (dectin-2) and CLEC4E (Mincle), which detect pathogen-associated molecular pattern metabolites (PAMPs), such as fungal carbohydrates, and trigger CARD9 activation. Upon activation, CARD9 homooligomerizes to form a nucleating helical template that recruits BCL10 via CARD-CARD interaction, thereby promoting polymerization of BCL10 and subsequent recruitment of MALT1: this leads to activation of NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways which stimulate expression of genes encoding pro-inflammatory cytokines and chemokines. CARD9 signaling in antigen-presenting cells links innate sensing of fungi to the activation of adaptive immunity and provides a cytokine milieu that induces the development and subsequent of interleukin 17-producing T helper (Th17) cells. Also involved in activation of myeloid cells via classical ITAM-associated receptors and TLR: required for TLR-mediated activation of MAPK, while it is not required for TLR-induced activation of NF-kappa-B. CARD9 can also be engaged independently of BCL10: forms a complex with RASGRF1 downstream of C-type lectin receptors, which recruits and activates HRAS, leading to ERK activation and the production of cytokines. Acts as an important regulator of the intestinal commensal fungi (mycobiota) component of the gut microbiota. Plays an essential role in antifungal immunity against dissemination of gut fungi: acts by promoting induction of antifungal IgG antibodies response in CX3CR1(+) macrophages to confer protection against disseminated C.albicans or C.auris infection. Also mediates immunity against other pathogens, such as certain bacteria, viruses and parasites CARD9 signaling is however redundant with other innate immune responses. In response to L.monocytogenes infection, required for the production of inflammatory cytokines activated by intracellular peptidoglycan: acts by connecting NOD2 recognition of peptidoglycan to downstream activation of MAP kinases (MAPK) without activating NF-kappa-B.
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A2AIW0
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ENTR1_MOUSE
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Endosome-associated-trafficking regulator 1 (Serologically defined colon cancer antigen 3)
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MSGYARRQGAPPLSRTRSLVVPDAPAFYERRSCLPQLDCERPHGGDLHPHLFGFRPTFMCYVPSPVLASVGDTGFGYGKGKCTNQGPSGAPETRFGGDKLEDLEEANPFSFKEFLKTKNLSLSKEDTTTSRIYPKEASRHPLGLEHSSPASQLMGYGLESQQPFFEDPTRASNLEEDEDDGWNITYLPSAVDQTHSSRDTQDSPPCDTYLSFFSNSSELACPESLPPWTLSDTDSRISPASPAGSPNADFAAHEESLGDRHLRTLQISYEALKDENSKLRRKLNEVQSFSETQTEMVRTLERKLEAKMIKEESDFHDLESVVQQVEQNLELMTKRAVKAENHVLKLKQEINLLQAQLSNLRRENEALRSGQGASLSVVKQNTDVALQNLHLVMNSAHASIKQLVSGADTLNLVAEILKSIDRISEVKDEVDS
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May be involved in modulation of TNF response. May be involved in presentation of TNFRSF1A on the cell surface. Involved in the endosome-to-plasma membrane trafficking and recycling of SNX27-retromer-dependent cargo proteins, such as GLUT1. Involved in the regulation of cytokinesis the function may involve PTPN13 and GIT1 (By similarity). Endosome-associated protein that plays a role in membrane receptor sorting, cytokinesis and ciliogenesis. Involved in the endosome-to-plasma membrane trafficking and recycling of SNX27-retromer-dependent cargo proteins, such as GLUT1. Involved in the regulation of cytokinesis the function may involve PTPN13 and GIT1. Plays a role in the formation of cilia. Involved in cargo protein localization, such as PKD2, at primary cilia (By similarity). Involved in the presentation of the tumor necrosis factor (TNF) receptor TNFRSF1A on the cell surface, and hence in the modulation of the TNF-induced apoptosis.
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A2AJ15
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MA1B1_MOUSE
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Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase (EC 3.2.1.113) (ER alpha-1,2-mannosidase) (ER mannosidase 1) (ERMan1) (Man9GlcNAc2-specific-processing alpha-mannosidase) (Mannosidase alpha class 1B member 1)
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MYPPPAPPPAPHRDFISVTLSLGESYDNSKSRRRRSCWRKWKQLSRLQRNVILFVLGFLILCGFLYSLHTADQWKALSGRPAEVEKMKQEVLPVLPAPQKESAEQEGFADILSQKRQRHFRRGPPHLQIRPPNTVSKDGMQDDAKEREAALGKAQQEENTQRTVISWRGAVIEPEQATELPYKRAEASIKPLVLASKIWKEPAPPNERQKGVIEAFLHAWKGYQKFAWGHDELKPVSKTFSEWFGLGLTLIDALDTMWILGLKQEFKQARKWVSENLDFQKNVDVNLFESTIRILGGLLSTYHLSGDSLFLTKAEDFGKRLMPAFTTPSKIPYSDVNIGTGFAHSPQWTSDSTVAEVTSIQLEFRELSRLTGIKKFQEAVEEVTKHIHSLSGKKDGLVPMFINTNSGLFTHPGVFTLGARADSYYEYLLKQWIQGGKKETQLLEDYVKAIEGIKAHLLRQSQPRKLTFVGELAHGRFSAKMDHLVCFLPGTLALGVHHGLPADHMDLARALMETCYQMNQQMETGLSPEIAHFNMYPRADHKDVEVKPADRHNLLRPETVESLFYLYRVTRDRKYQDWGWEILQSFNKYTRVPSGGYSSINNVQNSHKPEPRDKMESFFVGETLKYLYLLFSDDLELLSLDSCVFNTEAHPLPIWAPA
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Involved in glycoprotein quality control targeting of misfolded glycoproteins for degradation. It primarily trims a single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2), but at high enzyme concentrations, as found in the ER quality control compartment (ERQC), it further trims the carbohydrates to Man(5-6)GlcNAc(2) (By similarity).
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A2AJ77
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PRD12_MOUSE
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PR domain zinc finger protein 12 (EC 2.1.1.-) (PR domain-containing protein 12)
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MMGSVLPAEALVLKTGLKAPGLALAEVITSDILHSFLYGRWRNVLGEQLLEDKSHHASPKTAFTAEVLAQSFSGEVQKLSSLVLPVEVIIAQSSIPGEGLGIFSKTWIKAGTEMGPFTGRVIAPEHVDICKNNNLMWEVFNEDGTVRYFIDASQEDHRSWMTYIKCARNEQEQNLEVVQIGTSIFYKAIEMIPPDQELLVWYGNSHNTFLGIPGVPGLEEEQKKNKHEDFHPADSATGTAGRMRCVICHRGFNSRSNLRSHMRIHTLDKPFVCRFCNRRFSQSSTLRNHVRLHTGERPYKCQVCQSAYSQLAGLRAHQKSARHRPPSTALQAHSPALPAPHAHAPALAAAAAAAAAAHHLPAMVL
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Involved in the positive regulation of histone H3-K9 dimethylation.
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A2AJ88
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PLPL7_MOUSE
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Patatin-like phospholipase domain-containing protein 7 (EC 3.1.1.-) (EC 3.1.1.5) (Neuropathy target esterase-related esterase) (NRE) (NTE-related esterase)
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MQNEEDACLEAGYCLGTTLSSWRLHFMEEQSQSTMLMGIGIGALLTLAFVGITFFFVYRRVRRLRRAEPTPQYRFRKRDKVMFYGRKIMRKVTTLPHTLVGNTSAPRQRVRKRTKVLSLAKRILRFKKEYPTLQPKEPPPSLLEADLTEFDVKNSHLPSEVLYMLKNVRVLGHFEKPLFLELCKHMVFVQLQEGEHVFQPGEPDISIYVVQDGRLEVCIQDADGTEVVVKEVLPGDSVHSLLSILDVITGHTAPYKTVSARAAVSSTVLWLPAAAFQGVFEKYPETLVRVVQIIMVRLQRVTFLALHNYLGLTTELFNPESQAIPLLSVASVAGRAKRQMSYGPEEQLERSLRPSEFSSSDHGSSCVTVSGPLLKRSCSVPLPSNHGEVDELRQSQGSGSNTSAFQESHEGATSDLGMAYNRARILPHSDEQLGNSLASKSKKSVVAETPSAIFHYSENFRDETGACGKTDAIFRAATKDLLTLMKLDDPSLLDGRVAFLHVPAGTLVSKQGDQDVNILFVVSGMLHVYQQKIDSLEDTCLFLTHPGEMVGQLAVLTGEPLMFTIRANRDCSFLSISKAHFYEIMRKRPDVVLGVAHTVVKRMSSFVRQIDFALDWMEVEAGRAIYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLVGVVETLTHQARATTVHAVRDSELAKLPAGALTSIKRRYPQVVTRLIHLLGEKILGSLQQGSATGHQLGFNTASSKWDLGNPPGNLSTVAALPASEDVPLTAFALELQHALSAIGPVLLLTSDNIKQRLGSAALDSIHEYRLSSWLGQQEDIHRIVLYQADGTLTPWTQRCIRQADCILIVGLGEQEPAVGELEQMLESTAVRAQKQLILLHKEDGPVPSRTVEWLNMRSWCSGHLHLCCPRRVFSKRSLPKLVEMYTRVFQRPPDRHSDFSRLARMLTGNAIALVLGGGGARGCAQVGILRALAECGVPVDIIGGTSIGAFMGALFAEERSYSQTRIRAKQWAEGMTSMMKTILDLTYPITSMFSGTGFNSSISNIFKDRQIEDLWLPYFAITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLCDPKDGHLLMDGGYINNLPADVARSMGAKVVIAIDVGSRDETDLTNYGDALSGWWLLWKRWNPLATKVKVLNMAEIQTRLAYVCCVRQLEMVKNSDYCEYLRPPIDSYRTLDFGKFDEICEVGYQHGRTVFDIWVRSGVLEKMLQDQQGTSKRKDCGVFTCPNSSFTDLAEIVSRIEPAKVAAVDDESDYQTEYEEELPAIPKETYADFQSTGIELDSDSEYEPSMLQGPPSLTSPEQSQDSFPWLPNQDDQGPRLEHPS
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Lysophospholipase which preferentially deacylates unsaturated lysophosphatidylcholine (C18:1), generating glycerophosphocholine. Can also deacylate, to a lesser extent, lysophosphatidylethanolamine (C18:1), lysophosphatidyl-L-serine (C18:1) and lysophosphatidic acid (C16:0).
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A2AJB7
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LCN5_MOUSE
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Epididymal-specific lipocalin-5 (Epididymal retinoic acid-binding protein) (E-RABP) (mE-RABP) (Epididymal secretory protein 10) (MEP 10) [Cleaved into: Epididymal-specific lipocalin-5, major form; Epididymal-specific lipocalin-5, minor form]
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MCSVARHMESIMLFTLLGLCVGLAAGTEAAVVKDFDVNKFLGFWYEIALASKMGAYGLAHKEEKMGAMVVELKENLLALTTTYYNEGHCVLEKVAATQVDGSAKYKVTRISGEKEVVVVATDYMTYTVIDITSLVAGAVHRAMKLYSRSLDNNGEALNNFQKIALKHGFSETDIHILKHDLTCVNALQSGQI
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Associates with spermatozoa in the epididymal fluid but does not bind tightly to them. Binds both all-trans and 13-cis retinoic acid. May act as a retinoid carrier protein which is required for epididymal function and/or sperm maturation.
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A2AJK6
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CHD7_MOUSE
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Chromodomain-helicase-DNA-binding protein 7 (CHD-7) (EC 3.6.4.12) (ATP-dependent helicase CHD7)
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MADPGMMSLFGEDGSLFSEGLEGLGECGYPENPVNPMGQQMPIDQGFPSLQPSLHHPSPNQNQTKLTHFDHYSQYEQKMHLMDQPNRMMGSAPGNGLASPHSQYHTPPVPQVPHGGGGGGQMGVYPGIQNERHGQSFVDGGSMWGPRAVQVPDQIRAPYQQQQPQPAPSGPPAQGHPQHMQQMGSYLARGDFSMQQHGQPQQRMGQFSQGQEGLSQGSPFIATSGPGHLSHMPQQSPSMAPSLRHPVQQQFHHHPAALHGESVAHSPRFSPNPPQQGAVRPQTLNFSSRNQTVPSPTVNNSGQYSRYPYSNLNQGLVNSTGMNQNLGLTNSTPMNQSVPRYPNAVGFPSNSGQGLVHQQPIHSSGSLNQMNTQTMHPSQPQGTYASPPPMSPMKAMSNPAGTPPPQVRPGSAGMPMEVGSYPNMPHPQPSHQPPGAMGIGQRNMGPRNMQQPRSFMGMSSAPRELTGHMRPNGCPGVGLADPQAIQERLIPGQQHPGQQPSFQQLPTCPPLQPHPGLHQSSPPHPHHQPWAQLHPSPQNTPQKVPVHQHSPSEPFLEKPVPDMTQVSAQNAQLVKSDDYLPSIEQQPQQKKKKKKNNHIAAGDSSKGFGKDDFPGGVENQELRRNSLDVSQEEKKKKKRPKVKKDPKESKEPKEKKEPKTPKAPKIPKEPKEKKAKTVTPKPKSSKKSSNKKPDSEASALKKKVNKGKTEGSENSDLDKTPPPSPAPEEDEDPGVQKRRSSRQVKRKRYTEDLEFKISDEEADDADAAGRDSPSNTSQSEQQESVDAEGPVVEKIMSSRLVKKQKESGEEVEVEEFYVKYKNFSYLHCQWASVEDLEKDKRIQQKIKRFKSKQGQSKFLSEIEDDLFNPDYVEVDRIMDFARSTDDRGEPVIHYLVKWCSLPYEDSTWELKQDIDQTKIEEFEKLMSREPETERVERPPADDWKKSESSREYKNNNKLREYQLEGVNWLLFNWYNMRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTELNVVVYHGSQASRRTIQLYEMYFKDPQGRVIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKTEEQVQKLQAILKPMMLRRLKEDVEKNLAPKEETIIEVELTNIQKKYYRAILEKNFTFLSKGGGQANVPNLLNTMMELRKCCNHPYLINGAEEKILEEFKETHNAESPDFQLQAMIQAAGKLVLIDKLLPKLKAGGHRVLIFSQMVRCLDILEDYLIQRRYPYERIDGRVRGNLRQAAIDRFSKPDSDRFVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKSVKIYRLITRNSYEREMFDKASLKLGLDKAVLQSMSGRENATNGVQQLSKKEIEDLLRKGAYGALMDEEDEGSKFCEEDIDQILLRRTHTITIESEGKGSTFAKASFVASGNRTDISLDDPNFWQKWAKKAELDIDALNGRNNLVIDTPRVRKQTRLYSAVKEDELMEFSDLESDSEEKPCAKPRRPQDKSQGYARSECFRVEKNLLVYGWGRWTDILSHGRYKRQLTEQDVETICRAILVYCLNHYRGDENIKSFIWDLITPTADGQTRALLNHSGLSAPVPRGRKGKKVKAQSTQPVVHDAHWLASCNPDALFQEDSYKKHLKHHCNKVLLRVRMLYYLRQEVIGDQAEKILEGADSSEADVWIPEPFHAEVPTDWWDREADKSLLIGVFKHGYEKYNSMRADPALCFLERVGMPDAKAIAAEQRGTDMLADGGDGGEFDREDEDPEYKPTRAPFKDEIDEFANSPAEDKEESMEVHSSGKHSESNAELGQLYWPNTSTLTTRLRRLITAYQRSYKRQQMRQEALMKTDRRRRRPREEVRALEAEREAIISEKRQKWTRREEADFYRVVSTFGVIFDPVKQQFDWNQFRAFARLDKKSDESLGKYFSCFVAMCRRVCRMPAKPEDEPPDLASLIEPITEERASRTLYRIELLRKIREQVLHHPQLSDRLKLCQPSLDLPEWWECGRHDRDLLVGAAKHGVSRTDYHILNDPELSFLDAHKSFAQNRGASTVPPLNTLAMGFGQTPPVISSAHVHEEKAMEQAEGKAEECEHSPAKERSDGKEEEEEAGGAKDGKQECEVEASSVKGELKGVEGSADPGSKSVSEKGSEEDEEEKLEDDDKSEESSQPEAGAVSRGKTFDEESNASLSTARDETRDGFYMEDGDASVAQLLHERTFAFSFWPKDRVMINRLDNICEAVLKGKWPVNRRQMFDFQGLVPGYPPSAVDSPLQKRSFAELSMVSQASISASEDITTSPQLSKDDALNLSVPRQRRRRRRKVEIEAERAAKRRNLMEMVAQLRESQVVSENGQEKVVDLSKASREATSSTSNFSSLTSKFILPNVSTPVSDAFKSQMELLQAGLSRTPTRHMLNGSLVDGEPPMKRRRGRRKNVEGLDLLFMSHKRTPLSAEDAEVTKAFEEDIETPPIRNIPSPGQLDPDTRIPVINLEDGTRLVGEDAPKNKDLVDWLKLHPTYTVDMPSYVPKNTDVLFSSFQKPKQKRHRCRNPNKLDINTLTGEERVPVVNKRNGKKMGGAMAPPMKDLPRWLEENPEFAVAPDWTDIVKQSGFVPESMFDRLLTGPVVRGEGASRRGRRPKSEIARAAAAAAAVASTSGINPLLVNSLFAGMDLTSLQNLQNLQSLQLAGLMGFPPGLATAATAGGDAKSPAAVLPLMLPGMAGLPNVFGLGGLLNNPLSAATGNTTTASSQGEPEDGTSKAEEKGNDNEDENRDSEKSTDTVSAADSANGSVGAATAPAALPSNPLAFNPFLLSTMAPGLFYPSMFLPPGLGGLTLPGFPALAGLQNAVGTSEEKAADKAEGGPCKDGETLEGSDAEENLDKTVESSILEDEVAQGEELDSLEGGDEIENTGNDE
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Probable transcription regulator. Maybe involved in the in 45S precursor rRNA production (By similarity).
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A2AJN7
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S4A11_MOUSE
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Solute carrier family 4 member 11 (Sodium borate cotransporter 1) (NaBC1)
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MSQNEHCQDSGEYFSAGTQGYFKNNMEDNLEVREDSLGDEVFDTVNSSIVSGESIRFFVNVNLEVQPSKSDLEAATGGCVLLHTSRKYLKLKNFEEEVRAHRDLDGFLAQASIILNETATSLDDVLRTMLNRFALDPNHAEPDCDLDLLMAKLFTDAGAPMESKVHLLSDTIQGVTATVRGVQYEQSWLCIICTMKTLQKRHVCISRLVRPQNWGENSCEVRFVILVLAPPKMKSTKTAMEVARTFATMFSDITFRQKLLKTRTEEEFKEALVHQRQLLTMMMPRAAGHSMSSLHTHRHPQPPKCKDFFPFGKGIWMDIMRRFPVYPMDFTDGIIGKSKSVGKYVTTTLFLYFACLLPTIAFGSLNDENTNGAIDVQKTIAGQSIGGLLYALFSGQPLVILLTTAPLAIYTQVIRVICDDYNLDFNAFYAWTGLWNSFFLALYAFLNLSLLMNLFKRSTEEIIALFISITFVLDAVKGMVKIFGKYYYGHHYHTKRTSSLVSLLGIGRSPNSSLHTALNASLLASPVEMATTSSPGSTHSGQATAVLSLLIMLGTLWLGYTLYQFKKSPYLHPCVRETLSDCALPIAVLSFSLIGSYGFQEIEMSKFRYNPSESLFEVAQIHSLSFKAIGSAMGLGFLLSLLFFIEQNLVAALVNAPENRLVKGTAYHWDLLLLAIINTGLSLFGLPWIHAAYPHSPLHVRALALVEERVENGHIYETIVDVKETRLTALGASVLVGLSLLLLPFPLQWIPKPVLYGLFLYIALTSLDGNQLFSRVALLLKEQTSYPPTHYIRRVPQRKIHYFTGLQILQLLLLCAFGMSSLPYMKMVFPLIMIAMIPIRYNLLPRIIEAKYLDVMDAEHRP
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Multifunctional transporter with an impact in cell morphology and differentiation. In the presence of borate B(OH)4(-), acts as a voltage-dependent electrogenic Na(+)-coupled B(OH)4(-) cotransporter controlling boron homeostasis (By similarity). At early stages of stem cell differentiation, participates in synergy with ITGA5-ITGB1 and ITGAV-ITGB3 integrins and BMPR1A to promote cell adhesion and contractility that drives differentiation toward osteogenic commitment while inhibiting adipogenesis. In the absence of B(OH)4(-), acts as a Na(+)-coupled OH(-) or H(+) permeable channel with implications in cellular redox balance. Regulates the oxidative stress response in corneal endothelium by enhancing antioxidant defenses and protecting cells from reactive oxygen species. In response to hypo-osmotic challenge, also acts as water permeable channel at the basolateral cell membrane of corneal endothelial cells and facilitates transendothelial fluid reabsorption in the aqueous humor. In the presence of ammonia, acts as an electrogenic NH3/H(+) cotransporter and may play a role in ammonia transport and reabsorption in renal Henle's loop epithelium (By similarity).
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A2AJX4
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MALR1_MOUSE
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MAM and LDL-receptor class A domain-containing protein 1
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MFLPKAAVSAFSMHGSLCFLWTVCLSISPLSQQGVQAFQCSNGVSLPSDYVCDFTDHCGDNSEEQQCWSYGRCNFEDRLCSMTEDQTLQPGWTRRSGIISNSPPFWDHNGNISAHFLALVSRVDSISSNLRSRIFLPTNDQQVCQITFYNFSSNQNGKLIAGLQTLCGDPIEHLWQKTEILQSRWERNVITVQSSQQFQVIFQAQMLATHGQEEVIAIDDISFSSGCLPADVCQTCGFDLDTCGLATEASAGRTSWMCTKVREIPSLDSVPWQDQRGHDEGSFVWMRAGHASVSRLVESSAYLNSSVCHCMDGNCRLQFNYTMENSILRVRLYNDKEEKKTWTFNTSTYSTWMKADVLIPEDLKAFKVVLEGTVLSQKSFIGIDQLLVYNFGQTHSQKLCSVNEYTPASRQCLTHSSVCDSGMDHSNGIDEDSEACASLLTWDFESGFCGWEPFPTEDSHWEVVRGLSNGEHLFLEAGHTVSRNQGSFIYFGPQKSTAVARLGSPILTKSLTTFTPCQVRFWYHLSEHSSLSVFTRTSVDGSLLKQSEVTQFSDSQWSQAKVDLHAKAEESTLPFQLVLEATILSSNATVAVDDISISHECEISYKSLRSTSIQNKVADCDFEANSCGWFEASGGDHFDWVWSSQSNLSADLEQQAPPRDHTHGTAQGHFMFILKTSNSLFQTAKLQSPTFSQTGPGCTMSFWFYNYGLSVGAAELQLHLENSRDTTALWRVLYNQGNQWSEATVQLGRLTQPFYLSLEKVSLAVYSGVSAVDDIHFENCALPPPVESCDEPDHFWCRQTKACIGRHQLCDLVDDCGDYTDETGCAPGLQCNFENGICNWEQSTKDDFNWTRYQGPTSTMNTGPMKDHTLGTAKGHYLYIETSGPQGFQDKAVLLSPILNATEAKVCTFRLYYHMFGKHIYRLAIYQRIWSNTKGQLLWQIFGDQGNRWIRKDLSITSRKPFQILIMASVGDGFTGDIAIDDLSFMDCTLYPDNLPMDIPSPPETSVPVTLPPNNCTDDQFVCRSNGHCVGNIQKCDFRYDCIDKSDESSCVLEVCTFEERKLCKWYQPIPANSLHDSNTFRWGLGNGISIHHGEENHRPSVDHTKNTTDGWYLYADSSNGKFGDLADIVTPVISLMGPRCTLVFWTYMNGATVGSLQVLIKMGNTISKVWAQSGQQGPQWKKAEVFLGIHSHVEIVFRAKRGVSYIGDVAVDDVSFQNCSPLLSTNRKCTTDEFMCANKHCIEKDKLCDFVNDCADNSDETTFICGTSSGRCDFEFDLCTWEQDQDEDIDWNLKASNIPATSTEPAVDHTLGNSSGHYIILKSFFPQQPVKTGRISSPVISKRSKDCKIIFNYHMYGSGIAALLLLQVTVTNHTRVLLNLTKEQGNFWQRKELSLSSDEDFRVKFEGRVGEGIRGNIALDDIVLTKSCLPSHHSTREEPAFPLPTGFCPRGYEECQNGRCYSPEQRCNFVDDCGDNSDENECGGSCTFEKGWCGWKNSLAENSDWVLGIGSYKSQRPPKDHTLGNEHGHFMYLEATPVGLHGDKAHFKSATWQESSAACTMSFWYFISAKATGSIQILIKTDKGLWEVWQQSKPDPGNHWRRATILLGKLRNFEVIFQGIRTRDLGGGAAIDDIEFNNCTTVGETTDICSEETDFLCQDKKCIASHLVCDYKPDCSDTSDEAHCGYYTSTAGSCNFETTSGDWTVECGLTQDPEDDLDWSIGSIIPTEGLSRDSDHTPGSGRHFLYVNTSLAEEGSTARIITSHFFPASLGICTVRFWFYMVDPHIVGILKVYLIEKSGLNILMWSMMRNKNTGWTYAHVPLSSNSPFKVAFEADLGGKEDIFIALDDITFTPTCASGGPALPQPPLCEEGQFACIYALQCVSASEKCDGQEDCIDGSDEMNCSLGPSPQPCSDTEFQCFESQCIPSLLLCDGVADCQFNEDESSCVNQSCPSGALACNSSGLCIPAHQRCDGTAHCKDIQVDESSCSECPIHYCRNGGTCVIENIGPTCRCVQGWTGNRCHIRSNLSTEGSVHTQNYIWTLLGIGLGFLLTHIAVAILCSLGIRRRPMRKSEGVGNHSFINPVYRNCINQEKTQSSIYSFPNPFYGAASGSLETVSHHLKS
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Enhances production and/or transport of FGF15 and thus has a role in regulation of bile acid synthesis.
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A2AKK5
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ACNT1_MOUSE
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Acyl-coenzyme A amino acid N-acyltransferase 1 (EC 2.3.1.-)
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MMIKLIATPSNALVDEPVSIRATGLPPSQIVTIKATVKDENDNVFQSQAFYKTNEAGEVDLEKTPALGGDYVGVHPMGLFFSLKPKKAFHRLMKKDVMNSPFCICLDLYDSVNWLETVRIPSKASQRVQRWFVGPGVKREQIQEGRVRGALFLPPGKGPFPGIIDLFGVIGGLVEFRASLLASHGFAVLALAYFAYKDLPEKLQEVDLEYFEEAANFLLSHPKIQQPGIGVISTSKGAEIGLAMACYLKQVIATVCINGATTTTAVPLRYQDLVVTPIQQALERMEVHVSGAVCFRHTTQYLQNKNILPVEKAQGKILFIVGENDELLDSKLHAQRAMDRLRRHGRSSGRMLAYPGAGHLIEPPYSPLCFASWQPVLGRPMCFGGDLMAHAAAQEHSWREIQKFFRKHLLQSGSKL
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Acyltransferase which efficiently conjugates very long-chain and long-chain fatty acids to taurine. Shows no conjugation activity in the presence of glycine.
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A2AKQ0
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S35D1_MOUSE
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Nucleotide sugar transporter SLC35D1 (Solute carrier family 35 member D1) (UDP-galactose transporter-related protein 7) (UGTrel7) (UDP-glucuronic acid/UDP-N-acetylgalactosamine transporter) (UDP-GlcA/UDP-GalNAc transporter)
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MAEVHRRQHAPVKGEAPAKSSTHRDEEELGMAPAETLTVFLKLLAAGFYGVSSFLIVVVNKSVLTNYRFPSSLCVGLGQMVATVAVLWVGKTLRVVKFPDFDRNVPRKTFPLPLLYFGNQITGLFSTKKLNLPMFTVLRRFSILFTMFAEGALLKKTFSWGIKMTVFAMIIGAFVAASSDLAFDLEGYVFILINDVLTAANGAYVKQKLDSKELGKYGLLYYNALFMILPTLAIAYFTGDAQKAMEFEGWADTLFLLQFTLSCVMGFILMYATVLCTQYNSALTTTIVGCIKNILITYIGMVFGGDYIFTWTNFIGLNISIAGSLVYSYITFTEEQLSKQSEASNKLDTKGKGAV
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Antiporter that transports nucleotide sugars across the endoplasmic reticulum (ER) membrane in exchange for either their cognate nucleoside monophosphate or another nucleotide sugar (By similarity). Transports various UDP-sugars including UDP-N-acetyl-alpha-D-glucosamine (UDP-GlcNAc), UDP-N-acetyl-alpha-D-galactosamine (UDP-GalNAc) and UDP-alpha-D-glucuronate (UDP-GlcA), which are used by ER glucosyltransferases as sugar donors for the synthesis of sugar chains of glycoproteins, glycolipids and oligosaccharides (By similarity). May couple UDP-GlcNAc or UDP-GalNAc efflux to UDP-GlcA influx into the ER lumen that in turn stimulates glucuronidation and subsequent excretion of endobiotics and xenobiotics (By similarity). Plays a role in chondroitin sulfate biosynthesis, which is important for formation of cartilage extracellular matrix and normal skeletal development.
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A2AKX3
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SETX_MOUSE
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Probable helicase senataxin (EC 3.6.4.-) (Amyotrophic lateral sclerosis 4 protein homolog) (SEN1 homolog)
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MSTCCWCTPGGSSTIDVLKRYASSTGSSEFQTADEDLCYCLECVAEYHRARDEVPFLHEVLWELETLRLVSHFEKSMKAEAEDDDDLYIVDNNGEEQLFDCSGQDFENKLRVPLFEILKYPYLLLHERVNELCVEALCRMEQNNCSFQVFDKYPGIYLFLVHPNEMVRRWAILTARNLGKVDRDDYYDLQEVLTCLFKVIELGLLESPDIYTSSVLEKGKLILLPAHMYDTTNYKNYWLGICMLLTILEEQAMDSLLLGSDKQNDFMQSILHTMEKQSDDDSMDPFWPALHCFMVILDRLGSKVWGQLIDPIEAFQTIINNESYNREIQNIRNSSIRTKLEPEPHFDDMVTCSQIVYNFNPEKTKKDSGWRSAICPDYCPNMYEEMETLANVLQSDIGQDMRVHNSTFLWFIPFVQSLMDLKDLGVAYIVEVIHHLYSEVKDVLNQTDAVCDKVTEFFILILISVIELHRNKKCLHLLWVSSQQWVEAVVKCAKLPTTAFVRSCEKSPGSTSRGAAIMSSLALHSVQSNSVQLACVQLIRGLLKEGYQLGQQTLCKRFWDKLNLFLRGNLSLGWQLTGQETHELQMCLKQIIRNIKFKMPQYSTFGDSTSTFKTPPSFKEESDKIDRKHKKNIYCLENCSPVSSKEPMKADTHRVLMKVNTTEEENFKQHYIDLNEEEQEPLPAELCLKQKSEALFSESAQEQVKISAEKSGKESSSYAPSNSTSRNGPEWGCDRGVIMSAHSLTDSSSDFMEQVSTSNEDVSLKDGSVGKTSKPSFKLQKDEICAKLSHVIKKQIRKSTLVDNIIDLEENTAISDLENCSGTDGGALKEDSIGHNVPSDPVLDDKHEEQKSQNSSLFKKEIKSEELDNSSSDDEDKLQIQEGRADDDLVSFTEVTDTLVKAPCEGHVKMVVESRDKEMRESTALTSNLVEGQVPHDSSKPLVAGRQIDLCNITLISQTTVIQFPSGLSKQNSFQLQKGDKRCLTANQNSAATCRGQVIVISDSDEEEDEDEDERSSSEENIKQSKACIGKDCSEHRSLAVNASVEKQLVKEEERYPVEFEDSESQVFEFESSSEVFSVWQDHKIDSKNSLQGEQKSYVTHVADSTNNNLGCGDSVSEEVVRNKAEGVKEHAGPHSSVSAEEFCKTGVKKPKRKRYDKVTAEDPQRPSSSVGTDQLPDRRDLTESDLKSADMGMATPSSSVERDSTILQKSTKSRTHSKPVRKVPASKATKKTHSDTRRGQSKSSCYISCRTSPAIVPPKKLRQCPEPTSTVEKLGLKKAPRKAFELSQRSLECIVQLRDHGKTVGVVDAPKKAKLISPQTLSIKNNKKLLTSQDLQFQRLMRSRSHKKRDFDYKNTDTVRVSRIVQGSDVLEADSDEPDDHRVSEPLAISNEKQLAKCMLSKTEVAEASSDPWVTGITCLVNQCESRVLSGGVPTDVVMVSASEDPVDGGAVTVQVGEVASVKAAEPASSSDTDDDDNLFLTQHDPQDMDLCSQLENKTIIVAHKKDTVQREDSLSRPQLESLSITKCKYKDCVETTKNQGEYCPRHSEAKAADDGLFRKPGLPLSVARPLRPTTTKIFSSSSASRTANLSKSLESTTLQQSALKNKSSGAQPNLKVTPPSSMGSQKPVAEVKSLCNIFHFQTPSSSSKQSCKLTFSENRPTSAASPVNILLPSQSIFDTFIKEVLKWKYQMFLNFDKCGAPTSLCQSISRPVPVRFQDCAEYFNVFLPLIILNAFETVAQEWLSSPNKENFYQLQLRKFPADYKKYWEFLIYLNESELAKQLHPKENDLVFLAPEKSYMDRHGMQDCSHYYCGYVHKFRRTSVMRSGKAECSLCIQTQDTLPASVKNLTRCIVISSLVTTQRKLKAMSLLSSRNQLARAVLNPNPMDFCTKDLLTTTSERIVAYLKDFNEDQKKAIETAYAMVKHSPSVAKICLIHGPPGTGKSKTIVGLLYRLLTENQRKGHSDENFNAKIKQNRVLVCAPSNAAVDELMKKIILEFKEKCKDKKNPLGNCGDINLVRLGPEKSINTEVLKFSLDSQVNHRMKKDLPSHIQEMLRRKEILDAQLDELSRQRALCRGGREMQRQELDEHIAIVSKERQELASKIKEVQGRPQRAQNTIILESHVICCTLSTSGGLLLESAFRGQGGVPFSCVIVDEAGQSCEVETLSPLIHRCNKLILVGDPKQLPPTVISMKAQEYGYDQSMMARFCKLLEENVEQNMIGRLPVLQLTIQYRMHPDICLFPSNYVYNKNLKTNRLTESIRCSSEWPFQPYLVFDVGDGSERRDNDSYINVQEIKLVMEIIKLIKEKRKDISFRNIGIITHYKAQKTMIQKDLEKEFDKKGPAEVDTVDAFQGRQKDCIIVTCVRASAVQGSIGFLASLQRLNVTITRAKYSLFILGHLRTLMENQHWYELIQDAQKRGAIIKTSDPNYRHDAMKILKLKPVLQRSLTHPPATAPEAPRPQGGLPSNRLDSGLATTSFAASLYHTPSDTVTSKGPERPLLQDRLRDPRLLRRLDAEAKGTFLKDPQPVSPQLPGVVHLLGEPGFPVVFQDLGFVVPPSTAIVAPLGSHRSPMQAEPPPAHPAAAASTSKRKYSDPDAGLSHKREPRAFSGEQGRHGSVTHHVLRSTDWDRRRLDDSSAKRRQFL
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Probable RNA/DNA helicase involved in diverse aspects of RNA metabolism and genomic integrity. Plays a role in transcription regulation by its ability to modulate RNA Polymerase II (Pol II) binding to chromatin and through its interaction with proteins involved in transcription. Contributes to the mRNA splicing efficiency and splice site selection. Required for the resolution of R-loop RNA-DNA hybrid formation at G-rich pause sites located downstream of the poly(A) site, allowing XRN2 recruitment and XRN2-mediated degradation of the downstream cleaved RNA and hence efficient RNA polymerase II (RNAp II) transcription termination (By similarity). Required for the 3' transcriptional termination of PER1 and CRY2, thus playing an important role in the circadian rhythm regulation. Involved in DNA double-strand breaks damage response generated by oxidative stress. In association with RRP45, targets the RNA exosome complex to sites of transcription-induced DNA damage (By similarity). Plays a role in the development and maturation of germ cells: essential for male meiosis, acting at the interface of transcription and meiotic recombination, and in the process of gene silencing during meiotic sex chromosome inactivation (MSCI). Plays a role in neurite outgrowth in hippocampal cells through FGF8-activated signaling pathways. Inhibits retinoic acid-induced apoptosis. May be involved in telomeric stability through the regulation of telomere repeat-containing RNA (TERRA) transcription (By similarity).
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A2AL36
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CNTRL_MOUSE
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Centriolin (Centrosomal protein 1) (Centrosomal protein of 110 kDa) (Cep110)
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MKKGSERRLSKAKMPLSSHFPGPSSLRSSMRSRSLSPLIGSETQPLHPGGQWPAQAELTDESTVPLEPQQRKGAESYVGVRYITEALIKKLTKQDNLALVKSLNLSLSKDGGKKFRYIENLEKCVKLEVLNLSYNLIVKIEKVDKLLRLRELNLSYNKISKIEGLENMCNLQKLNLAGNEIEHIPVWFAKKLKSLRVLNLKGNKISSLQDVSKLKPLQDLTSLVLIDNPVVALPHYLQFIIFHLRSLESLEGQPVTTQDRQEAFERFSLEEIERLEKDLEKKTVETEELKNKQTKFLEEIKNQDKLNKSLKEEAMLQKQSCEELESDLSTKKELLKQKTVELTRACQKQYELEQELAFYKIDAKFEPLNYYPSEYAEIDKYPDESPYIGKSRYKRNMFATETYIVSDAQAVQIRKMVPEGGQLRHEHTPPRVQAPPDLQLEDTEKKISAAQTRLSELHHEIETAEQKVLRATQEFKQLEEAIQQKKISEAEKDLLLKQLSGRLQHLNRLRQEALDLEIQMEKQRKEIAEKHEEINTVQLATDSLDPKDPKHSHMKAQKRGKEQQLDIMNRQYTQLESRLDEILCRIAKETEEIKDLEQQLTDGQIAANEALKKDLEGVISGLQEYLGTIKGQATQAQNECRKLQDEKETLLQRLTEVQQEKEELELIAMDAENMRKELAELESALQEQHEVNASLQQAQGDLSAYETELETQLKLKDAETSQLKQELEKLLRRTQLEQSVLQTELEKERESLRDALGKAQSSEEKQQENNELRTQLKQLQDDNSLLKKQLKEFQNHLNHVVDGLIHPEEVAARVDELRKRLKLGAGEMRIHSPSDVLGKSLADLQKQFSEILARSQWEKEEAQVRERKLHEEMALQQEKLANGQEEFRQACERALEARIKFDKRQHNARIQQLENEIHYLQENLKSMEKIQGLTDLQLQEADEEKERILAQLQELEKKKKREDARSQEQFLGLDEELKSLKKAVAASDKLAAAELTIAKDQLKSLHGTVVRINQERAEELQEAERFSREAMQAAKDLSRAEAEIELLQHLLREREGQFRDEMENADLGAKGANSQLLEIEALNEAMAKQRAEITRLRDVLNLTGAGTKGGIENVLEEIAELRHAVSAQNEYISSMADPFRRQGWWYFMPPAPSSKVSSHSSQATKDSGLGLKYTASTPLRKPQPGQQEEKDSSGPLPASGYWVYSPIRSTLHKSFSKREDADSGGDSQEESGLDDQEEPPFVPPPGYIMYTVLPDGSPVPQGVALYAPSPPLPNSSHPLTPGTVVYGPPPAGAPIIYGPPPANFAVPLVPAGVQHCNIPEHHNLENEVSRLEDIMQHLKSKQREERRQKASTQHSEEEVDGLHRDIDDLLQEKKELELEVEELHRTIERHQQRKDFIDGHVENLMTELEIEKSLKHHEDIVDEIECLEKTLLKRRSELREADRLLAEAENELACTKEKTKSAVEKFTDAKRNLLQTESDAEALEKRAQETALNLVKAEQQLRLLQADAEDLEQHKIKQEEILKEINKVVAAKDADFQCLNEKKEKLTEELQSLQRDIKAAQHSEDHHLQVLRESETLLQAKRAELETLKSQVTSQQQELAVLDSELGHRREELLLLQDSLAQAKADLQEALTLGETEVAEKCSHIREVKSLLEELSFQKGELNVHISEKKTQLALIQQEMEKEEKNLQVVLQQLSRHKTELKNVADILQLETSELQGLKLQHDQKVVELEKAQVDVLEEKLELENLQQATQQQRRELERQRQLLERDRRETERVRAESQALQSCVECLSKEKEDLQGQCESWEKKSSHAQRVLAATEESNKMEQSNLGKLELSVRKLRQELEQLSQDKLALHSEVAEVQQQLQGKQEAINSLQEELDSTQDHLDLAKQDLIHTTKCQNELLNEQTQLQEDISKWMARLESCQKETETKEQQVQQLQDEIRESKLRLDQQEMMFQKLQKEREREEQKFEAGKVTLEQQQRQLEKELTDQKSRLKQLLTDVSAAEGRLGTLQEEERRIEGLERMLSQAKQQLSEREQQLMAKSGELLALQKEADDMRADFSLLRNQFLTERKKAEKQVAGLKEALKIQRSQLEKNLLEQKQENSCMQKEMATIELVAQDNHERARRLMKELSQMQQEYLELKKQVANQKDLERRQMEVSDAMRTLKSEVKDEIRTSLRNLNQFLPELPADLASILERNENLRELESLKENFPFTTKERIFEEKSNFPQVHIMDEHWRGEALRQRLRRHEDQLKAQLRHCMSKQAEVLIKGKQQTEGTLHSLRRQVDALGELVTSTSTDSASSPSLPSLVEDSQHGHSQSSFQVLQVPLEEPNSYRH
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Involved in cell cycle progression and cytokinesis. During the late steps of cytokinesis, anchors exocyst and SNARE complexes at the midbody, thereby allowing secretory vesicle-mediated abscission (By similarity).
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A2ALS5
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RPGP1_MOUSE
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Rap1 GTPase-activating protein 1 (Rap1GAP) (Rap1GAP1) (ARPP-90)
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MIEKMQGSRMDEQRCSFPPPLKTEEDYIPYPSVHEVLGREGPFPLILLPQFGGYWIEGTNHEISSLPETEPLQSPTTKVKLECNPTARIYRKHFLGKEHFNYYSLDTALGHLVFSLKYDVIGDQEHLRLLLRTKCRTHHDVIPISCLTEFPNVVQMAKLVCEDVNVDRFYPVLYPKASRLIVTFDEHVISNNFKFGVIYQKLGQTSEEELFSTNEESPAFVEFLEFLGQKVKLQDFKGFRGGLDVTHGQTGTESVYCNFRNKEIMFHVSTKLPYTEGDAQQLQRKRHIGNDIVAVVFQDENTPFVPDMIASNFLHAYVVVQAEGGGPDGPLYKVSVTARDDVPFFGPPLPDPAVFRKGPEFQEFLLTKLINAEYACYKAEKFAKLEERTRAALLETLYEELHIHSQSMMGLGGDDDKMENGSGGGGFFESFKRVIRSRSQSMDAMGLSNKKPNTVSTSHSGSFTPNNPDLAKAAGISLIVPGKSPTRKKSGPFGSRRSSAIGIENIQEVQEKRESPPAGQKTPDSGHVSQEPKSENSSTQSSPEMPTTKNRVESAAQRTEVLQGFSRSSSSASSFTSVVEETEGVDGDDTGLESVSSSGTPHKRDSFLYSTWLDDSVSTTSGGSSPGLTRSPHPDVGKSGDPACPEIKIQLETSEQHTPQMGC
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GTPase activator for the nuclear Ras-related regulatory protein RAP-1A (KREV-1), converting it to the putatively inactive GDP-bound state.
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A2ALU4
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SHRM2_MOUSE
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Protein Shroom2 (Protein Apxl)
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MEGAEPRARPERLAEAEAPATDGVRLVEVQLSGGAPWGFTLKGGREHGEPLVITKIEEGSKAAAVDKLLAGDEIVAINDVSLSGFRQEAICLVKGSHKTLKLVVKRKSDPSWRPHSWHATKYFDVHPEPAASLFLNTSGSPSWKSQHQASSSSHDLSGSWEHTSLQRTSDHFSSMGSIDSLDHSSQLYPSGHLSSAKSNSSIDHLGGHSKRDSAYGSFSTCSSTPDHTLPKADASSTENILYKVGLWEASRPGSSRQSQSTGDPQGLQDRPSCFIPRVPGNSSKSPRPEDNVEPKIATHGRSNFGPVWYVPDKKKAPSPPPLGLPLRSDSFSVAARGHEKARGPPFSDLASMQHFITLPHVQPRGDHRMETTDRQWKLTHLSSGKEIGNVGYQSEGHLDCRWLCSDDRAGRPSGPPGRLQFSDVHFLKSYHGSQHQQQCSDESPRAPSSPRELLHITPGGGLQEPPEPSQDDNPTQVRWPGSAHQKLDDRGRSHYFPGSLRQPVQGSAQVVIPRGDYWHSDTTPVDLEYPLLRPVGQRTYLQQHEETPASHEKEGYHQLNAGIEGCCSGIQEPPRASRTVRTGLQCPSNDFKLVDGESGRISRQRTPMLHSLTQDGTWRPGNSKDCGNDKPPLFDAQVGKPTRRSDRFATTLRNEIQMRRAKLQKSKSTVTLAGDSEAEDCAGDWRADVGAVPEGSFPSTYKEHLKEAQTRVLKATSFQRRDLDPTPADQYSGPSEHRTFDHSASSSLSSFPGEPDSAPRFCETGLAKAPSSGVGVPHVLRIGGRKRFTAEQKLKSYSEPEKINEVGLSGDHRPHPTVRTPEDTVGTFADRWKFFEETSKSLLQKAGHRQVHCGLPREKAERPQTGHHECESTEPWFQKRSLATSCGEILSDRKVEKASEKLNPPRRLGTFAEYQASWKEQKKPLEARSSGRYHSADDILDAGLDQQQRPQYIHERSRSSPSTDHYSQEVPVEPNRQAEDSGDHKEAILCTLQAEEGCSAPSAQPQDSQHVNEDTTFPQPETQLSSKCQHLQTSAMETSRSPSPQFAPQKLTDKPPLLIHEDNSARIERVMDNNTTVKMVPIKIVHSESQPEKESRQSLACPAELPPLPSGLERDQIKTLSTSEQCYSRFCVYTRQEVEAPHRARPPEPRPPSTPAPPVRDSCSSPPSLNYGKAKEKTMDDLKSEELAREIVGKDKSLADILDPSVKIKTTMDLMEGIFPKDEYLLEEAQQRRKLLPKVPLPRVTEDKKQDPGMPGVVSLATNSTYYSTSAPKAELLIKMKDLQEPEEYSAGDLDHDLSVKKQELIDSISRKLQVLREARESLLEDIQANNALGDEVEAIVKDVCKPNEFDKFRMFIGDLDKVVNLLLSLSGRLARVENALNNLDDNPSPGDRQSLLEKQRVLTQQHEDAKELKENLDRRERIVFDILATYLSEENLADYEHFVKMKSALIIEQRELEDKIHLGEEQLKCLFDSLQPERSK
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May be involved in endothelial cell morphology changes during cell spreading. In the retinal pigment epithelium, may regulate the biogenesis of melanosomes and promote their association with the apical cell surface by inducing gamma-tubulin redistribution.
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A2ALV5
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SHOC1_MOUSE
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Protein shortage in chiasmata 1 ortholog (EC 3.6.-.-) (Protein ZIP2 homolog) (MZip2)
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MALNGRTMFPAFKYYAIDYLQEDIIKERLYRDALLLQIPSCLNQDKNIIDDKYRTPWTRAIPVQEMEDNSVLEQWRTRFCVEGVPEKKTVTGVMINGTFEEIVPSSNPNSPPGIENDKLFPSKDYVDDFIPVKCSLYYPGVKAEHQGLLIDEEMIFMNKAMDNHLPTVNGLLSRLKLYLVKDPFLDFKEELSGKDNFTEYFSVQECSEPFVRDFHMAEETFCKKKLPSVFPSGFKSLISTNPKQEILILPPSKLKKPLNSIPKIMDSVDESECFKGDITSKHEFDTEDIKCNSTENLTFASLCEPECSEPGDLEMPPTHLILPRQHSAVSSLHMGFQTFPFSATCKINLLSAGESANKYCMLWQLGGCRNSWVSFLLTVPRFQEPSSQYSLADMRNIFSVKGDSLVINPAKAKGWRQARLHPIMAETLAHLKAYLCHNGLSSQETKLEIFLPTKVFQLESWLELKSRPLPIVPISEKSTDVHQLHPQKRPIPSSEKEVPHLCLSGESISVKKSKVEANPKNDQEPEARIMQKPENSCVGLGCSSQVPSAESASSSQIQASYDKKQDDLDLLSEFIILRSKHQTFPSEADVDVKSHDHDQNNEFQDKEKYSLTLQEESLVASNSKAPEERCEERTDGVIEIPASDTQCQAYCLLEATANPILKELVCLCTYPAANWKFATVNFDQTRFFLKEQEKKINDATHPDKNDDRKMTFRHAALLHLLITIRDVLLTCNLDTALGYLSNAKDIYKSVLDSRLDNIWRQLKILQFIKEKRPKSNYKIQELQCQILSRLQNQQQMKVLIIIRMDSDGEKHLLIKTLKKIEGLTMTVLRSNDRKKILETTSILKGTNACVVVHNHSIGADFPWSSFSLVVEYNHVGHSCWAEHCQLLDIPFLAFKVAVPDTALQRDALLDGFGGFLLKIPIPYVFFASEGLLNTPEILRLLESNYNITLVERCCCGSLKLFGSTECYVVVTVDEHTAIVVQDLEELHHEKASDNIIMRLMALSFQYSCCWIILYSKETLNSQYHLTEETLRHLAQVYAALVSSGLKSEELDVKLIIAPGVEETALIIRQIADHNLMTSTRDPHEWLDKSWVEVSPSKEEMSLLDFPCINPLVAQLMLHRAPSLHWLLIATPAELQELLPQVPGKVLKHFCSITSLFKISSPSMTKSSQISSLQEDMNQTDLFISQSSAPIIQEQEEYYPYEDSEGTSSSPVELRATPCMLPSAAPHSQRGCWEDPSCGPDPVQNNPSLMNAESKKVTWPSVPSWSDSESDVFSLARTQVSCEPIMTLTDSQRRGTNGFVNCPEAKGPRNMQVSTPVFLPENSQSHLHWDFKKNSCRKQIYSFNPSCGTEQTTYNKWYSWKDDFSSNQPECLWDEMEDVTYRNANAGTRETFWRELPAVPSWDSPCASDSNANQRGFKGLDFCQRAGNYLGQRSLPVSSSNWGDYKTPTDLMYSQVPQPKKRRLMYEKVPGRVDGQTRLKFL
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ATPase required during meiosis for the formation of crossover recombination intermediates. Binds DNA: preferentially binds to single-stranded DNA and DNA branched structures (By similarity). Does not show nuclease activity in vitro, but shows ATPase activity, which is stimulated by the presence of single-stranded DNA (By similarity). Plays a key role in homologous recombination and crossing-over in meiotic prophase I in male and female germ cells. Required for proper synaptonemal complex assembly and homologous chromosome pairing. Required for recruitment of TEX11 and MSH4 to recombination intermediates.
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A2AM29
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AF9_MOUSE
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Protein AF-9 (Myeloid/lymphoid or mixed-lineage leukemia translocated to chromosome 3 protein homolog)
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MASSCAVQVKLELGHRAQVRKKPTVEGFTHDWMVFVRGPEHSNIQHFVEKVVFHLHESFPRPKRVCKDPPYKVEESGYAGFILPIEVYFKNKEEPKKVRFDYDLFLHLEGHPPVNHLRCEKLTFNNPTEDFRRKLLKAGGDPNRSIHTSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSTSFSKPHKLMKEHKEKPSKDSREHKSAFKEPSRDHNKSSKDSSKKPKENKPLKEEKIVPKMAFKEPKPMSKEPKADSNLLTVTSGQQDKKAPSKRPPASDSEELSAKKRKKSSSEALFKSFSSAPPLILTCSADKKQIKDKSHVKMGKVKIESETSEKKKSMLPPFDDIVDPNDSDVEENMSSKSDSEQPSPASSSSSSSSSFTPSQTRQQGPLRSIMKDLHSDDNEEESDEAEDNDNDSEMERPVNRGGSRSRRVSLSDGSDSESSSASSPLHHEPPPPLLKTNNNQILEVKSPIKQSKSDKQIKNGECDKAYLDELVELHRRLMTLRERHILQQIVNLIEETGHFHITNTTFDFDLCSLDKTTVRKLQSYLETSGTS
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Chromatin reader component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. Specifically recognizes and binds acylated histone H3, with a preference for histone H3 that is crotonylated. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. Recognizes and binds histone H3 crotonylated at 'Lys-9' (H3K9cr), and with slightly lower affinity histone H3 crotonylated at 'Lys-18' (H3K18cr). Also recognizes and binds histone H3 acetylated and butyrylated at 'Lys-9' (H3K9ac and H3K9bu, respectively), but with lower affinity than crotonylated histone H3. In the SEC complex, MLLT3 is required to recruit the complex to crotonylated histones. Recruitment of the SEC complex to crotonylated histones promotes recruitment of DOT1L on active chromatin to deposit histone H3 'Lys-79' methylation (H3K79me). Plays a key role in hematopoietic stem cell (HSC) maintenance by preserving, rather than confering, HSC stemness. Acts by binding to the transcription start site of active genes in HSCs and sustaining level of H3K79me2, probably by recruiting DOT1L.
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A2AMM0
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CAVN4_MOUSE
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Caveolae-associated protein 4 (Muscle-related coiled-coil protein) (Muscle-restricted coiled-coil protein)
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MEHNGSASNAGKIHQNRLSSVTEDEDQDAALTIVTVLDRVASVVDSVQASQKRIEERHREMGNAIKSVQIDLLKLSQSHSNTGYVVNKLFEKTRKVSAHIKDVKARVEKQQVRVTKVETKQEEIMKKNKFRVVIFQEDIPCPASLSVVKDRSLPENQEEAEEVFDPPIELSSDEEYYVEESRSARLRKSGKEHIDHIKKAFSRENMQKTRQTLDKKVSGIRTRIVTPERRERLRQSGERLRQSGERLRQSGERFKKSISSAAPSKEAFKIRSLRKAKDPKAEGQEVDRGMGVDIISGSLALGPIHEFHSDEFSETEKEVTKGGYSPQEGGDPPTPEPLKVTFKPQVRVEDDESLLLELKQSS
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Modulates the morphology of formed caveolae in cardiomyocytes, but is not required for caveolar formation. Facilitates the recruitment of MAPK1/3 to caveolae within cardiomyocytes and regulates alpha-1 adrenergic receptor-induced hypertrophic responses in cardiomyocytes through MAPK1/3 activation. Contributes to proper membrane localization and stabilization of caveolin-3 (CAV3) in cardiomyocytes. Induces RHOA activation and activates NPPA transcription and myofibrillar organization through the Rho/ROCK signaling pathway.
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A2AMT1
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BFSP1_MOUSE
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Filensin (Beaded filament structural protein 1) (Lens fiber cell beaded-filament structural protein CP 95) (CP95) [Cleaved into: Filensin C-terminal fragment; Filensin N-terminal fragment]
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MYRRSYVFQARQERYERAQPAGPAAQPGGTAPGLAALQALGERVAVQVQRARALQQRHAGLRRQLDAFQRLGEQPGPEDALARHVEANLQRARDLTAEHARLERQEAEAQRALDEFRSKYENECECQLVLKEMLERLNKEADEALLRNLHLQLEAQFLQADISVAKDRYKKNLLEIQTYITVLQQIVQTAPQVSLVTGMRESGLLMQEKLFTEREVAALQNQLEEGREAVTHLQAQKAELQAQTTALEQAIKHAHECYDEELQLYNEQIENLRKEIEEAERSLERSSYDCRQLAVAQQTLRNELDRYHRIIEIEGSRLSSVFIETPISLITPSHGAPLSLGSSVKDLARAVQDITAAKPRQKALPKSLPKRKEIIAQDKVEETLEDAPLKPPQEPKALQVERKAEGGSQPGAGGGHGVSPTQEGGPEDVPDGGQISKAFGKLCKVVKERVSGHKEPEPEPPTDLFTKGRHVLVTGESSFVDPEFYSSSIPARGGVVISIEEDSMHHDGHVEPSPGQPMPPVENGQGVPQGREGDHSNHQQGTDKNGLRAKEPKDLEEKDDDGKKEAEGSRRPCPVIIPGPDEPSTSHSQTSGSNQGGPVGPASKSSSLLAKGPSKALSIKKVEVVESIEKISTESIQTYEETSVIVETLIGKSKGNKKLGEKSLPDTRA
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Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA. Involved in altering the calcium regulation of MIP water permeability (By similarity).
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A2AN08
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UBR4_MOUSE
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E3 ubiquitin-protein ligase UBR4 (EC 2.3.2.27) (N-recognin-4) (RING-type E3 ubiquitin transferase UBR4) (Zinc finger UBR1-type protein 1) (p600)
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MATSGGEEAAAAAPAPGAPATGQDTTPGWEVAVRPLLSASYSAFEMKELPQLVASVIESESEILHHEKQYEPFYSSFVALSTHYITTVCSLIPRNQLQSVAAACKVLIEFSLLRLENPDEACAVSQKHLILLIKGLCTGCSRLDRTEIITFTAMMKSAKLPQTVKTLSDVEDQKELASPVSPELRQKEVQMNFLNQLTSVFNPRTVPSPPISPQALVEGENDEQSSPDQVSAAKTKSVFIAQNVASLQELGGSEKLLRVCLNLPYFLRYINRFQDAVVANSFFIMPATVADATAVRNGFHSLVIDVTMALDTLSLPVLEPLNPSRLQDVTVLSLSCLYAGVSVATCMAILHVGSAQQVRTGSTSSKEDDYESDAATIVQKCLEIYDMIGQAISSSRRAGGEHFQNFQLLGAWCLLNSLFLILNLSPTALADKGKEKDPLAALRVRDILSRTKEGVGSPKLGPGKGHQGFGVLSVILANHAIKLLASLFQDLQVEALHKGWETDGPPAVLSIMAQSTSTQRIQRLIDSVPLTNLLLTLLSTSYRKACVLQRQRKGSMSSDASASTDSNTYYEDDFSSTEEDSSQDDDSEPILGQWFEETISPSKEKAAPPPPPPPPPLESSPRVKSPNKQASGEKGNILASRKDPELFSGLASNILNFITTSMLNSRNSFIRSYLSASLSEHHMATLASIIKEVDKDGLKGSSDEDFAAALYHFNHSLVTSDLQSPNLQNTLLQQLGVAPFSEGPWPLYIHPQGLSVLSRLLLIWQHKAGAQGDPDVPECLKVWDRFLTTMKQNALQGVVPSETEDLNVEHLQLLLLIFHSFSEKGRRAILTMLVQSIQELSVNMEVQMRTAPLILARLLLIFDYLLHQYSKAPVYLFEQVQHNLLSPPFGWASGSQDSSSRRANTPLYHGFKEVEENWSKHFSSDAAPQPRFYCVLSTEASEEDLNRLDSEACEVLFSKPVKYDELYSSLTTLLAAGSQLDTTRRKEKKNVTALEACALQYYFLILWRILGILPPSKTYMNQLAMNSPEMSECDILHTLRWSSRLRISSYVSWIKDHLIKQGMKPEHAGSLIELAASKCSSVKYDVEIVEEYFARQISSFCSIDCTAVLQLHEIPSLQSIYTLDAAVSKVQVSLDEHFSKMAAETDPHKSSEITKNLLPATLQLIDTYASFTRAYLLQNLNEEGSTEKPSQEKLHGFAAVLAIGSSRCKANTLGPTLVQNLPSSVQSVCESWNNINTNEFPNIGSWRNAFANDTIPSESYISAVQAAHLGTLCGQSLPLAASLKHTLLSLVRLTGDLIVWSDEMNPAQVIRTLLPLLLESSTESAAEISSNSLERILGPAESDEFLARVYEKLITGCYNILANHADPNSGLDESILEECLQYLEKQLESSQARKAMEEFFSDGGELVQIMMATANEDLSAKFCNRVLKFFTKLFQLTEKSPNPSLLHLCGSLAQLACVEPVRLQAWLTRMTTSPPKDSDQLEVIQENRQLLQLLTTYIVRENSQVGEGVCAVLLGTLTPMATDMLANGDGTGFPELMVVMATLASAGQGAGHLQLHNAAVDWLGRCKKYLSQKNVVEKLNANVMHGKHVMVLECTCHIMSYLADVTNALSQSNGQGPSHLSVDGEERAIEVDSDWVEELAVEEEDSQAEDSDEDSLCNKLCTFTITQKEFMNQHWYHCHTCKMVDGVGVCTVCAKVCHKDHEISYAKYGSFFCDCGAKEDGSCLALVKRTPSSGMSSTMKESAFQSEPRVSESLVRHASTSPADKAKVTISDGKVTDEEKPKKSSLCRTVEGCREELQNQANFSFAPLVLDMLSFLMDAIQTNFQQASAVGSSSRAQQALSELHTVDKGVEMTDQLMVPTLGSQEGAFENVRMNYSGDQGQTIRQLISAHVLRRVAMCVLSSPHGRRQHLAVSHEKGKITVLQLSALLKQADSSKRKLTLTRLASAPVPFTVLSLTGNPCKEDYLAVCGLKDCHVLTFSSSGSVSDHLVLHPQLATGNFIIKAVWLPGSQTELAIVTADFVKIYDLSIDALSPTFYFLLPSSKIRDVTFLFNEEGKNIIVIMSSAGYMYTQLMEEASSAQQGPFYVTNVLEINHEDLKDSNSQVAGGGVSVYYSHVLQMLFFSYSQGRSFAATVSRSTLEVLQLFPINIKSSNGGSKTSPALCQWSEVMNHPGLVCCVQQTTGVPLVVMVKPGTFLIQEIKTLPAKAKIQDMVAIRHTACNEQQRTTMILLCEDGSLRIYMANVENTSYWLQPSLQPSSVISIMKPVRKRKTATITARTSSQVTFPIDFFEHNQQLTDVEFGGNDLLQVYNAQQIKHRLNSTGMYVANTKPGGFTIEISNNSSTMVMTGMRIQIGTQAIERAPSYIEIFGRTMQLNLSRSRWFDFPFTREEALQADRKLSLFIGASVDPAGVTMIDAVKIYGKTKEQFGWPDEPPEDFPSASVSNICPPNLNQSNGTGESDSAAPATTSGTVLERLVVSSLEALESCFAVGPIIEKERNKHAAQELATLLLSLPAPASVQQQSKSLLASLHSSRSAYHSHKDQALLSKAVQCLNTSSKEGKDLDPEVFQRLVITARSIAVTRPNNLVHFTESKLPQMETEGADEGKEPQKQEGDGCSFITQLVNHFWKLHASKPKNAFLAPACLPGLTHIEATVNALVDIIHGYCTCELDCINTASKIYMQMLLCPDPAVSFSCKQALIRVLRPRNKRRHVTLPSSPRSNTPMGDKDDDDDDDADEKMQSSGIPDGGHIRQESQEQSEVDHGDFEMVSESMVLETAENVNNGNPSPLEALLAGAEGFPPMLDIPPDADDETMVELAIALSLQQDQQGSSSSALGLQSLGLSGQAPSSSSLDAGTLSDTTASAPASDDEGSTAATDGSTLRTSPADHGGSVGSESGGSAVDSVAGEHSVSGRSSAYGDATAEGHPAGPGSVSSSTGAISTATGHQEGDGSEGEGEGEAEGDVHTSNRLHMVRLMLLERLLQTLPQLRNVGGVRAIPYMQVILMLTTDLDGEDEKDKGALDNLLAQLIAELGMDKKDVSKKNERSALNEVHLVVMRLLSVFMSRTKSGSKSSICESSSLISSATAAALLSSGAVDYCLHVLKSLLEYWKSQQSDEEPVAASQLLKPHTTSSPPDMSPFFLRQYVKGHAADVFEAYTQLLTEMVLRLPYQIKKIADTSSRIPPPVFDHSWFYFLSEYLMIQQTPFVRRQVRKLLLFICGSKEKYRQLRDLHTLDSHVRGIKKLLEEQGIFLRASVVTASSGSALQYDTLISLMEHLKACAEIAAQRTINWQKFCIKDDSVLYFLLQVSFLVDEGVSPVLLQLLSCALCGSKVLAALAASTGSSSVASSSAPPAASSGQATTQSKSSTKKSKKEEKEKEKEGESSGSQEDQLCTALVNQLNRFADKETLIQFLRCFLLESNSSSVRWQAHCLTLHIYRNSNKAQQELLLDLMWSIWPELPAYGRKAAQFVDLLGYFSLKTAQTEKKLKEYSQKAVEILRTQNHILTNHPNSNIYNTLSGLVEFDGYYLESDPCLVCNNPEVPFCYIKLSSIKVDTRYTTTQQVVKLIGSHTISKVTVKIGDLKRTKMVRTINLYYNNRTVQAIVELKNKPARWHKAKKVQLTPGQTEVKIDLPLPIVASNLMIEFADFYENYQASTETLQCPRCSASVPANPGVCGNCGENVYQCHKCRSINYDEKDPFLCNACGFCKYARFDFMLYAKPCCAVDPIENEEDRKKAVSNINTLLDKADRVYHQLMGHRPQLENLLCKVNEAAPEKPQEDSGTAGGISSTSASVNRYILQLAQEYCGDCKNSFDELSKIIQKVFASRKELLEYDLQQREAATKSSRTSVQPTFTASQYRALSVLGCGHTSSTKCYGCASAVTEHCITLLRALATNPALRHILVSQGLIRELFDYNLRRGAAAIREEVRQLMCLLTRDNPEATQQMNDLIIGKVSTALKGHWANPDLASSLQYEMLLLTDSISKEDSCWELRLRCALSLFLMAVNIKTPVVVENITLMCLRILQKLIKPPAPTSKKNKDVPVEALTTVKPYCNEIHAQAQLWLKRDPKASYEAWKKCLPIRGVDGNGKSPSKSELHRLYLTEKYVWRWKQFLSRRGKRTTPLDLKLGHNNWLRQVLFTPATQAARQAACTIVEALATVPSRKQQVLDLLTSYLDELSVAGECAAEYLALYQKLIASCHWKVYLAARGVLPYVGNLITKEIARLLALEEATLSTDLQQGYALKSLTGLLSSFVEVESIKRHFKSRLVGTVLNGYLCLRKLVLQRTKLIDETQDMLLEMLEDMTTGTESETKAFMAVCIETAKRYNLDDYRTPVFIFERLCSIIYPEENEVTEFFVTLEKDPQQEDFLQGRMPGNPYSSNEPGIGPLMRDIKNKICQDCDLVALLEDDSGMELLVNNKIISLDLPVAEVYKKVWCATNEGEPMRIVYRMRGLLGDATEEFIESLDSTTDEEEDEEEVYRMAGVMAQCGGLQCMLNRLAGVKDFKQGRHLLTVLLKLFSYCVKVKVNRQQLVKLETNTLNVMLGTLNLALVAEQESKDSGGAAVAEQVLSIMEIILDESNAEPLSEDKGNLLLTGDKDQLVMLLDQINSTFVRSNPSVLQGLLRIIPYLSFGEVEKMQILVERFKPYCSFEKYDEDHSGDDKVFLDCFCKIAAGIKNNSNGHQLKDLILQKGITQNALDYMKKHIPSAKNLDADIWKKFLSRPALPFILRLLRGLAMQHPATQVLIGTDSITSLHKLEQVSSDEGIGTLAENLLEALREHPDVNKKIDAARRETRAEKKRMAMAMRQKALGTLGMTTNEKGQVVTKTALLKQMEELIEEPGLTCCICREGYKFQPTKVLGIYTFTKRVALEEMENKPRKQQGYSTVSHFNIVHYDCHLAAVRLARGREEWESAALQNANTKCNGLLPVWGPHVPESAFATCLARHNTYLQECTGQREPTYQLNIHDIKLLFLRFAMEQSFSADTGGGGRESNIHLIPYIIHTVLYVLNTTRATSREEKNLQGFLEQPKEKWTESAFDVDGPHYFTILALHVLPPEQWKAIRVEILRRLLVASHARAVAPGGATRLTDKAVKDYSAYRSSLLFWALVDLIYNMFKKVPTSNTEGGWSCSLAEYIRHNDMPIYEAADKALKTFQEEFMPVETFSEFLDAAGLLSEITDPESFLKDLLNSVP
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E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. Together with clathrin, forms meshwork structures involved in membrane morphogenesis and cytoskeletal organization. Regulates integrin-mediated signaling. May play a role in activation of FAK in response to cell-matrix interactions. Mediates ubiquitination of ACLY, leading to its subsequent degradation.
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A2ANU3
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SYNG1_MOUSE
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Synapse differentiation-inducing gene protein 1 (SynDIG1) (Dispanin subfamily C member 2) (DSPC2) (Transmembrane protein 90B)
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MDGIIEQKSVLVHSKISDAGKRNGLINTRNFMAESRDGLVSVYPAPQYQSHRLVASAAPGSLEGGRSEPVQQLLDPNTLQQSVESHYRPNIILYSDGVLRSWGDGVATDCCETTFIEDRSPTKDSLEYPDGKFIDLSGDDIKIHTLSYDVEEEEELQELESDYSSDTESEDNFLMMPPRDHLGLSVFSMLCCFWPLGIAAFYLSHETNKAVAKGDFHQASTSSRRALFLAVLSITIGTGIYVGVAVALIAYLSKNNHL
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May regulate AMPA receptor content at nascent synapses, and have a role in postsynaptic development and maturation.
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A2AP18
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PLCH2_MOUSE
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1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase eta-2 (EC 3.1.4.11) (Phosphoinositide phospholipase C-eta-2) (Phosphoinositide phospholipase C-like 4) (PLC-L4) (Phospholipase C-like protein 4) (Phospholipase C-eta-2) (PLC-eta2)
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MGGLAWGPSRAAGSSWVNASGTWEQPLRGFSGLQGGRRRGRGEKGIPEEPLCQLTPQLGLSLRVPFGLGDYGLDMPGPQPSAASQTTGAVACLAEVLLWVGGSVVVSPRWQLSLVVERCMSAMQEGTQMVKLRGSSKGLVRFYYLDEHRSCLRWRPSRKNEKAKISIDSIQEVSEGRQSEIFQRYPDSSFDPNCCFSIYHGSHRESLDLVSPSSEEARTWVTGLRYLMAGISDEDSLARRQRTRDQWLKQTFDEADKNGDGSLSISEVLQLLHKLNVNLPRQRVKQMFREADTDDHQGTLGFEEFCAFYKMMSTRRDLYLLMLTYSNHKDHLDASDLQRFLEVEQKMNGVTLESCQNIIEQFEPCLENKSKGMLGIDGFTNYTRSPAGDIFNPEHNRVHQDMTQPLSHYFITSSHNTYLVGDQLMSQSRVDMYAWVLQAGCRCVEVDCWDGPDGEPIVHHGYTLTSKILFKDVIETINKYAFIKNEYPVILSIENHCSVVQQKKMAQYLTDILGDKLDLSSVSSEDATMLPSPQMLKGKILVKGKKLPANISEDAEEGEVSDEDSADEMEDDCKLLNGDASTNRKRVENIAKKKLDSLIKESKIRDCEDPNDFSVSTLSPSGKLGRKAEAKKGQSKVEEDVEAGEDSGVSRQNSRLFMSSFSKRKKKGSKIKKVASVEEGDETLDSPGSQSRGTARQKKTMKLSRALSDLVKYTKSVGTHDVEIEVVSSWQVSSFSETKAHQILQQKPTQYLRFNQHQLSRIYPSSYRVDSSNYNPQPFWNAGCQMVALNYQSEGRMLQLNRAKFSANGDCGYVLKPQCMCQGVFNPNSEDPLPGQLKKQLALRIISGQQLPKPRDSVLGDRGEIIDPFVEVEVIGLPVDCSKEQTRVVDDNGFNPMWEETLVFTVHMPEIALVRFLVWDHDPIGRDFIGQRTLAFSSIMPGYRHVYLEGMEEASIFVHVAVSDISGKVKQTLGLKGLFLRGTKPGSLDSHAAGQPLPRPSVSQRLLRRTASAPTKSQKPSRKGFPELALGTQDAGSEGAADDVAPSSPNPALEAPTQERSGSSSPRDTRLFPLQRPISPLCSLEPIAEEPALGPGLPLQAAAPTGPSQEGSQCPVGLGAKVTSSQQTSLGAFGTLQLRIGGGRENEEPPLRPHNGGISSGPREGTSGRQTDSKSRSRVPGHLPVVRRAKSEGQVLSELSPTPAVYSDATGTDRLWQRLEPGSHRDSVSSSSSMSSNDTVIDLSLPSLGLCRSRESIPGVSLGRLTSRPCLASAARPDLPPVTKSKSNPNLRVAGGLPTAPDELQPRPLAPRLTGHHPRPPWHHLTLVGLRDCPVSAKSKSLGDLTADDFAPSFQGSTSSLSCGLGSLGVAHQVLEPGIRRDALTEQLRWLTGFQQAGDITSPTSLGPAGDGSVGGPSFLRRSSSRSQSRVRAIASRARQAQERQQRLRGQDSRGPPEEERGTPEGACSVGHEGCVDVPMPAKGAPEQVCGAADGQLLLRL
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The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. This phospholipase activity is very sensitive to calcium. May be important for formation and maintenance of the neuronal network in the postnatal brain.
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A2APB8
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TPX2_MOUSE
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Targeting protein for Xklp2
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MSQVPTTYSFDAPTDFINFSSLDAEEDTENIDSWFDEKANLENKFLRQRGIGEPFQGKNSLRKAKLQQGFVTPLKAVDNTYHKETEKENLQKQSIPSNDCSSLDAKRAVSGNTPVQPQRRSIRLSAQKDLEQKEKNHVASVEMKAKRCVAPATDCPPQKRMKVSHKKKLEEEEEGSAPATSRKNERETLEKAKGKHTVPGVPPAREKVLKSTEEQEIEKRLRMQQEVVELRRKNEEFKKLALAGPGQPVKKSTSQVTKTVDFHFLTDERIKQHPKNQEEYKEVNFMSELRKHSSTPARGTRGCTIIKPFNLSKGKKRTFDEAASTYVPIAQQVEAFHKRTPNRYHLRNKKDESLLPSKSVNKIARDPQTPILQTKYRTRAVTCKSTAEQEAEELEKLQQYKFKARELDPRIFESGPILPKRAPVKPPTQPVGFDLEIEKRIHERESKKKTEDEQFEFHSRPCPTKILEDVVGVPEKKVIPATVPKSPVFALKNRIRVPIKDEEEEKPVVIKAQPVPHYGVPYKPHIAEARNVEVCPFSFDTRDKERQLQKEKKIKEMQKGEVPKFKALPVPHFDTINLPEKKVKNVTQAEPFSLETDKRGAYKAEMWKHQLEEEQKQQKDAACFKARPNTVIFQEPFVPKKEKKSLAENPSGSLVQEPFQLATERRAKERQELEKKMAEVEAWKLQQLEEVRQQEEEQQKEELARLRKELVHKANPIRKYAAVEVKSSELPLTVPVSPKFSTRFQ
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Spindle assembly factor required for normal assembly of mitotic spindles. Required for normal assembly of microtubules during apoptosis. Required for chromatin and/or kinetochore dependent microtubule nucleation. Mediates AURKA localization to spindle microtubules. Activates AURKA by promoting its autophosphorylation at 'Thr-288' and protects this residue against dephosphorylation. TPX2 is inactivated upon binding to importin-alpha. At the onset of mitosis, GOLGA2 interacts with importin-alpha, liberating TPX2 from importin-alpha, allowing TPX2 to activates AURKA kinase and stimulates local microtubule nucleation.
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A2APC3
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TTLL9_MOUSE
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Probable tubulin polyglutamylase TTLL9 (EC 6.3.2.-) (Tubulin--tyrosine ligase-like protein 9)
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MSRQKNQNSKGHGVSKGKEREQRTLIRFKTTLMNTLMDVLRHRPGWVEVKDEGEWDFYWCDVSWLRENFDHTYMDEHVRISHFRNHYELTRKNYMVKNLKRFRKYLERESGKTEAAKCDFFPKTFEMPCEYHLFVEEFRKNPGITWIMKPVARSQGKGIFLFRRLKDIMDWRKGTSGKKPTGVETQPARANMNPSGSHDTRSSDDQKDDLPVENYVAQRYVENPYLIGGRKFDLRVYVLVMSYIPLRAWLYRDGFARFSNTRFTLNSIDDHYVHLTNVAVQKTSPDYHLKKGCKWMLQRFRQYLASKHGPKAVETLFSDMDNIFIKSLQSVQKVIISDKHCFELYGYDILIDQDLKPWLLEVNASPSLTASSQEDYELKTCLLEDTLHVVDMEARLTGKEKRVGGFDLMWNDGPVSREDGPSDLSGMGNFVTNTHLGCVNDRKEQLRQLFRSLQAQRKAPS
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Probable tubulin polyglutamylase that generates side chains of glutamate on the gamma-carboxyl group of specific glutamate residues within the C-terminal tail of target proteins. Similar to TTLL1, may acquire enzymatic activity only in complex with other proteins as it is most likely lacking domains important for autonomous activity (Probable). Mediates tubulin polyglutamylation which induces establishment of microtubule heterogeneity in sperm flagella, thereby playing a role in normal motile flagella axoneme structure and sperm flagella beating pattern.
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A2APF3
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CTCFL_MOUSE
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Transcriptional repressor CTCFL (Brother of the regulator of imprinted sites) (CCCTC-binding factor) (CTCF paralog) (CTCF-like protein)
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MAAAEVPVPSGYFTQIKEQKLKPGDLEEEKEEDGVQRVEAQEGVVKEVEAENSCLLLEARAPVESDRRILTLQTVHLESQDVHLQGLGWLSVPHSEELSGTVPEAEGILQLPSVLWLDPEPQLSLQHCVTVSIPEELYPPEELQRIHFHLLRENVLMAEENPELTPDLDESTALKKPEEDEKDQLPPQGETDKREERLLLLEMKPKEGKDDEIVLTISHLSLEEQQDPPAANQTSVPGAKAAKPKRRRQTKGKPQSFQCDTCPFTSSKLSTFNRHIKIHSNERPHLCHLCLKAFRTVTLLRNHVNTHTGTRPHKCRDCDMAFVTSGELVRHRRYKHTYEKPFKCSLCKYASVEASKMKRHIRSHTGERPFQCCQCAYASRDSYKLKRHMRTHSGEKPYECPTCHVRFTQSGTMKIHIAQKHGENVPKYECPHCATIIARKSDLRVHLRNLHSQSPEEMKCRYCPAGFHERYALIQHQRTHKNEKKFKCKQCDYACKQERCLKAHMRMHTGEKPFSCLACNKHFRQKQLLTVHLRKYHDPNFVPNLHLCLKCDKRFSRWSNLQRHRKKCDPEHETLAPNKDRRPVTRTQASEGEAGHKEGEPQCPGEQALGHQGEAAGSQSPDHGLTCEIIFNMMDK
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Testis-specific DNA binding protein responsible for insulator function, nuclear architecture and transcriptional control, which probably acts by recruiting epigenetic chromatin modifiers. Plays a key role in gene imprinting in male germline, by participating in the establishment of differential methylation at the IGF2/H19 imprinted control region (ICR). Directly binds the unmethylated H19 ICR and recruits the PRMT7 methyltransferase, leading to methylate histone H4 'Arg-3' to form H4R3sme2. This probably leads to recruit de novo DNA methyltransferases at these sites. Seems to act as tumor suppressor. In association with DNMT1 and DNMT3B, involved in activation of BAG1 gene expression by binding to its promoter. Required for dimethylation of H3 lysine 4 (H3K4me2) of MYC and BRCA1 promoters.
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A2APX8
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SCN1A_MOUSE
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Sodium channel protein type 1 subunit alpha (Sodium channel protein brain I subunit alpha) (Sodium channel protein type I subunit alpha) (Voltage-gated sodium channel subunit alpha Nav1.1)
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MEQTVLVPPGPDSFNFFTRESLAAIERRIAEEKAKNPKPDKKDDDENGPKPNSDLEAGKNLPFIYGDIPPEMVSEPLEDLDPYYINKKTFIVLNKGKAIFRFSATSALYILTPFNPLRKIAIKILVHSLFSMLIMCTILTNCVFMTMSNPPDWTKNVEYTFTGIYTFESLIKIIARGFCLEDFTFLRDPWNWLDFTVITFAYVTEFVDLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCVQWPPTNASLEEHSIEKNITMDYNGTLVNETVFEFDWKSYIQDSRYHYFLEGVLDALLCGNSSDAGQCPEGYMCVKAGRNPNYGYTSFDTFSWAFLSLFRLMTQDFWENLYQLTLRAAGKTYMIFFVLVIFLGSFYLINLILAVVAMAYEEQNQATLEEAEQKEAEFQQMLEQLKKQQEAAQQAAATTASEHSREPSAAGRLSDSSSEASKLSSKSAKERRNRRKKRKQKEQSGGEEKDDDEFHKSESEDSIRRKGFRFSIEGNRLTYEKRYSSPHQSLLSIRGSLFSPRRNSRTSLFSFRGRAKDVGSENDFADDEHSTFEDNESRRDSLFVPRRHGERRNSNLSQTSRSSRMLAVFPANGKMHSTVDCNGVVSLVGGPSVPTSPVGQLLPEVIIDKPATDDNGTTTETEMRKRRSSSFHVSMDFLEDPSQRQRAMSIASILTNTVEELEESRQKCPPCWYKFSNIFLIWDCSPYWLKVKHIVNLVVMDPFVDLAITICIVLNTLFMAMEHYPMTEHFNHVLTVGNLVFTGIFTAEMFLKIIAMDPYYYFQEGWNIFDGFIVTLSLVELGLANVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKDCVCKIATDCKLPRWHMNDFFHSFLIVFRVLCGEWIETMWDCMEVAGQAMCLTVFMMVMVIGNLVVLNLFLALLLSSFSADNLAATDDDNEMNNLQIAVDRMHKGIAYVKRKIYEFIQQSFVKKQKILDEIKPLDDLNNRKDNCISNHTTEIGKDLDCLKDVNGTTSGIGTGSSVEKYIIDESDYMSFINNPSLTVTVPIAVGESDFENLNTEDFSSESDLEESKEKLNESSSSSEGSTVDIGAPAEEQPVIEPEETLEPEACFTEGCVQRFKCCQISVEEGRGKQWWNLRRTCFRIVEHNWFETFIVFMILLSSGALAFEDIYIDQRKTIKTMLEYADKVFTYIFILEMLLKWVAYGYQTYFTNAWCWLDFLIVDVSLVSLTANALGYSELGAIKSLRTLRALRPLRALSRFEGMRVVVNALLGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYHCVNTTTGDIFEISEVNNHSDCLKLIERNETARWKNVKVNFDNVGFGYLSLLQVATFKGWMDIMYAAVDSRNVELQPKYEESLYMYLYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPGNKFQGMVFDFVTRQVFDISIMILICLNMVTMMVETDDQSDYVTSILSRINLVFIVLFTGECVLKLISLRHYYFTIGWNIFDFVVVILSIVGMFLAELIEKYFVSPTLFRVIRLARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYAIFGMSNFAYVKREVGIDDMFNFETFGNSMICLFQITTSAGWDGLLAPILNSKPPDCDPNKVNPGSSVKGDCGNPSVGIFFFVSYIIISFLVVVNMYIAVILENFSVATEESAEPLSEDDFEMFYEVWEKFDPDATQFMEFEKLSQFAAALEPPLNLPQPNKLQLIAMDLPMVSGDRIHCLDILFAFTKRVLGESGEMDALRIQMEERFMASNPSKVSYQPITTTLKRKQEEVSAVIIQRAYRRHLLKRTVKQASFTYNKNKLKGGANLLVKEDMLIDRINENSITEKTDLTMSTAACPPSYDRVTKPIVEKHEQEGKDEKAKGK
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Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. Plays a key role in brain, probably by regulating the moment when neurotransmitters are released in neurons. Involved in sensory perception of mechanical pain: activation in somatosensory neurons induces pain without neurogenic inflammation and produces hypersensitivity to mechanical, but not thermal stimuli.
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A2AQ07
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TBB1_MOUSE
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Tubulin beta-1 chain
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MREIVHIQIGQCGNQIGAKFWEVIGEEHGIDCAGSYCGTSALQLERISVYYNEAYGKKYVPRAVLVDLEPGTMDSIRSSRLGVLFQPDSFVHGNSGAGNNWAKGHYTEGAELIENVMDVVRRESESCDCLQGFQIVHSLGGGTGSGMGTLLMNKIREEYPDRILNSFSVMPSPKVSDTVVEPYNAVLSIHQLIENTDACFCIDNEALYDICFRTLRLTTPTYGDLNHLVSLTMSGITTSLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTAQGSQQYRALSVAELTQQMFDARNIMAACDPRRGRYLTVACIFRGKMSTKEVDQQLLSIQTRNSNCFVEWIPNNVKVAVCDIPPRGLNMAATFLGNNTAIQELFTRVSEHFSAMFRRRAFVHWYTSEGMDISEFGEAESDIHDLVSEYQQFQDVRAGLEDSEEDVEEAEVEAEDKDH
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Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
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A2AQ19
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RTF1_MOUSE
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RNA polymerase-associated protein RTF1 homolog
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MRGRLCVGRAAAVAAAVAAAAVAVPLAGGQEGSQGGVRRGSRGTTMVKKRKGRVVIDSDTEDSGSDENLDQELLSLAKRKRSDSEEKEPPVSQPAASSDSETSDSDDEWTFGSNKNKKKGKTRKVEKKGAMKKQANKAASSGSSDRDSSAESSAPEEGEVSDSESSSSSSSSDSDSSSEDEEFHDGYGEDLMGDEEDRARLEQMTEKEREQELFNRIEKREVLKRRFEIKKKLKTAKKKEKKEKKKKQEEEQEKKKLTQIQESQVTSHNKERRSKRDEKLDKKSQAMEELKAEREKRKNRTAELLAKKQPLKTSEVYSDDEEEEDDDKSSEKSDRSSRTSSSDEEEEKEEIPPKSQPVSLPEELNRVRLSRHKLERWCHMPFFAKTVTGCFVRIGIGNHNSKPVYRVAEITGVVETAKVYQLGGTRTNKGLQLRHGNDQRVFRLEFVSNQEFTESEFMKWKEAMFSAGMQLPTLDEINKKELSIKEALNYKFNDQDIEEIVKEKERFRKAPPNYAMKKTQLLKEKAMAEDLGDQDKAKQIQDQLNELEERAEALDRQRTKNISAISYINQRNREWNIVESEKALVAESHNMRNQQMDPFTRRQCKPTIVSNSRDPAVQAAILAQLNAKYGSGVLPDAPKEMSKGQGKDKDLNSKTASDLSEDLFKVHDFDVKIDLQVPSSESKALAITSKAPPAKDGAPRRSLNLEDYKKRRGLI
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Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both independently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1) UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. Binds single-stranded DNA (By similarity). Required for maximal induction of heat-shock genes. Required for the trimethylation of histone H3 'Lys-4' (H3K4me3) on genes involved in stem cell pluripotency this function is synergistic with CXXC1 indicative for an involvement of a SET1 complex. {ECO:0000250, ECO:0000269|PubMed:19345177}.
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A2AQ25
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SKT_MOUSE
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Sickle tail protein (Enhancer trap locus 4)
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MEESEGQKCEPNLPPSGDSRQMPQQGRSNLHVTSQEDAACRRPRERLSNGNARAQVSKPARNIPRRHTLGGPRSSKEILGMQPSEMDRKREAFLEHLKQKYPHHATAIMGHQERLRDQTKSPKLSHSPQPPNLGDPVEHLSETSGDSLEAMSEGEVPSPFARGSRTRASLPVVRSANQTKERSLGVLYLQYGDETKQLRMPNEVTSTDTIRALFVSAFPQQLTMKMLESPSVAIYIKDDSRNVYYELNDVRNIQDRSLLKVYNKDPSHAFNHMTKAVNGDMRMQREIVYARGDGLVAPRPGSVAHPPHVIPNSPPSTPVPHSLPPSPSRIPYGGSRPMAIPGNATIPRDRLSSLPVSRSISPSPSAILERRDVKPDEDMSSKNLVMFRNEGFYADPYLYHEGRMSIASSHGGHPLDVPDHVIAYHRTAIRSASAYCSPSLQAEMHMEQSLYRQKSRKYPDSHLPTLGSKTPPASPHRVGDLRMIDLHPHLNTHGPPHTLQPDRASPSRQSFKKEPGTLVYIEKPRNTSGLSSLVDLGPPLVEKQGFAYSTTTIPKDRETRERMQAMEKQIASLTGLVQSALFKGPITSSSKEASSEKMVKATANRNQADGAGTAHVSAGKVLGSVEFSLPPSQPLPAGTSPIHTSLLDMRRNVAELRLQLQQMRQLQLQNQEILRAMMKKAELEISNKVKETMKRLEDPVQRQRTLVEQERQKYLHEEERIVKKLCELEDFVEDLKKDSSSTGRVVTLKDVEDGAFLLRQVGEAVATLKGEFPTLQNKMRAVLRIEVEAVRFLKEEPHKLDSLLKRVRSMTDVLTMLRRHVTDGLLKGTDASQAAQYVAMEKATAAEVLKHQEETAHAPGQPLHCSTGSPGDVKSEVVPLSTMTVHHVQSSPVVMQPSQHSSALMNPAQNLPGGTRPHTASPPAITQEVTSAQSAPGPQSPQTPVNGSSMQSLFIEEIHSVSAKNRAVSIEKAEKKWEEKRQNLEHYNGKEFEKLLEEAQANIMKSIPNLEMPPASSPVSKGDAAGDKLELSEDSPNSEQELDKIGGKSPPPPPPPPRRSYLPGSGLTTTRSGDVVYTGRSMSKVSSEDPGPTPQTRATKCPPEEPASAWAPSPPPVPAPSSKEEEEEEEEGDKIMAELQAFQKCSFMDVNPNSHAEQSRANSHLKDTRAGATAPPKEKKNLEFYHEDVRKSDVECENGPQVESQKVTAGALRPSGPPKWERVMVDSISDTSRTSECRADTFTEENATPNKSLFRDSRNYSQKNVPKVSFSSSGLNSLEGEINKGPNVSGLQCAIPDLENQKLNFGKTKEIGQQGQENADKSHIPLPTRSAEFSIHDVKTQDQDVPVTGYGQVVLRSKVGRHANMNMNEDGESTPSSPSEEHTATDNIAFMITKTAVQVLSSGEVHDIVSQKGQDVQTVNIDGRKETASQHEGTEGEEPVVCLDKKPVIIIFDEPMDIRSAYKRLSTIFEECDEELERMLTEEKIEEEEEDENEDSGVRTSSQMSCEQVDSRSDRMGQKAETQSQPHVLSAELLTPGVQGVRKAEQRKLSSADSPDSGNKCGMVDDQFESPKKKFKFKFPKKQLAALTQAIRTGTKTGKKTLQVVVYEEEEEDGTLKQHKEAKRFEITRSQPEDALKTMARRQEQLSPEGTLPASRTDEIRKSTYRTLDSLEQTIKQLENTISEMSPRALVDTSCSSNRDCGASLPHMAQEVSPRSLLVLDEVPPAPEPPTSISPASRKGSSTTPQTSRMPVPMTSKNRPGSLDKASKQSKLQDPRQYRQANGSAKKAGGDCKPTSPSLPASKIPALSPSSGKSSSLPSASGDSSNLPNAPATKPSIASTPLSPQAGRSAHSASLIPSVSNGSLKFQSPPHAGKGHHHLSFALQTQNGRAAPTTSSSSSPPSPASPTSLNQGARGIRTIHTPSLASYKAQNGSSSKATPSTAKETS
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Required for normal development of intervertebral disks.
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A2AR95
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LRAD3_MOUSE
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Low-density lipoprotein receptor class A domain-containing protein 3
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MWLLGPLCLLLSSTAESQLLPGNNFTNECNIPGNFMCSNGRCIPGAWQCDGLPDCFDKSDEKECPKAKSKCGPTFFPCASGIHCIIGRFRCNGFEDCPDGSDEENCTANPLLCSTARYHCRNGLCIDKSFICDGQNNCQDNSDEESCESSLEPGSGQVFVTSENQLVYYPSITYAIIGSSVIFVLVVALLALVLHHQRKRNNLMTLPVHRLQHPVLLSRLVVLDHPHHCNVTYNVNNGVQYVATQAEQNASEVGSPPSYSEALLDQRPAWYDLPPPPYSSDTESLNQADLPPYRSRSGSAYSASSQAASSLLSVEASSHNPEQPGSPEGSAEPRDSVPSQGTEEV
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May influence APP processing, resulting in a decrease in sAPP-alpha production and increased amyloidogenic P3 peptide production. May regulate ITCH and NEDD4 E3 ligase activity and degradation (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q86YD5, ECO:0000269|PubMed:21795536}.
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A2ARA8
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ITA8_MOUSE
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Integrin alpha-8 [Cleaved into: Integrin alpha-8 heavy chain; Integrin alpha-8 light chain]
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MSAGTHCGPPGNRAPPFARLCCVSAALGMLWSPACLAFNLDVDKLTVYSGPEGSYFGYSLDFYIPDARTASVLVGAPKANTSQPDIVEGGAVYYCPWPSERSAQCKQIPFDTTNNRKIRVNGTKEPIEFKSNQWFGATVRAHKGKVVACAPLYHWRTLKPNPAKDPVGTCYVAIQNFSAYAEHSPCRNSNADPEGQGYCQAGFSLDFYKNGDLIVGGPGSFYWQGQVITVSIADIIANYSFKDILRKLAAEKQTDVAPASYDDSYLGYSVAAGEFTGDSQQELVAGIPRGAQNFGYVSIINSTDMTFIQNFTGEQMASYFGYTVVVSDVNNDGMDDILVGAPLFMEREFESNPREVGQVYLYLQASALLFQDPQVLTGTETFGRFGSSVAHLGDLNQDGYNDIAIGVPFAGKDQRGKVLIYNGNPRGLHSKPSQVLQGIWGSQTIPSGFGFSLRGDADIDKNDYPDLLVGAFGKGKVAVYRARPVVTVDAQLLLHPMIINLENKTCQIPEFPTPVACFSVRVCASIAGQSISNTIALLAEVQLDFLKQKGAIKRTLFLHNHQSHFTFPFVMKQQKSLHCQDFMVYLRDETEFRDKLSPINISLNYSLDDSTFKDSLEVKPILNHYRDNVVTEQAHILVDCGEDNLCVPDLKLSARPDKHQIIIGDENHLMLIINARNEGEGAYEAELFVIIPEEADYVGIERNNKGLRPLSCEYKMENVTRMVVCDLGNPMVTGTNFSLGLRFAVPRLEKTNMSINFDLQIRSSNKDNPDSNFERVQINITAIAQVEIRGVSHPPQIVLPIHNWEPEKKPHKEEEVGPLVEHIYELHNIGPSTISDSILDVGWPFSARDEFLLYIFHLQTLGPLQCQTNPEINPQDIKPAASPEDTPELSAFLRNATIPHLVRKRDVPVVQLHRQSPARILNCTNIDCLQISCAVGRLGGGESAVLKVRSRLWAHTFLKRKNDHYALASLVSFEVKKMPYKEQPAKLPAGSTAVKTSVIWATPNVSFSIPLWVIILAILLGLLVLAILTLALWKCGFFDRARPPQDEMTDREQLTSDKTPEA
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Integrin alpha-8/beta-1 functions in the genesis of kidney and probably of other organs by regulating the recruitment of mesenchymal cells into epithelial structures. It recognizes the sequence R-G-D in a wide array of ligands including TNC, FN1, SPP1 TGFB1, TGFB3 and VTN. NPNT is probably its functional ligand in kidney genesis. Neuronal receptor for TNC it mediates cell-cell interactions and regulates neurite outgrowth of sensory and motor neurons.
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A2ARI4
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LGR4_MOUSE
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Leucine-rich repeat-containing G-protein coupled receptor 4 (G-protein coupled receptor 48)
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MPGPLRLLCFFALGLLGSAGPSGAAPPLCAAPCSCDGDRRVDCSGKGLTAVPEGLSAFTQALDISMNNITQLPEDAFKNFPFLEELQLAGNDLSFIHPKALSGLKELKVLTLQNNQLKTVPSEAIRGLSALQSLRLDANHITSVPEDSFEGLVQLRHLWLDDNILTEVPVRPLSNLPTLQALTLALNNISSIPDFAFTNLSSLVVLHLHNNKIKSLSQHCFDGLDNLETLDLNYNNLDEFPQAIKALPSLKELGFHSNSISVIPDGAFAGNPLLRTIHLYDNPLSFVGNSAFHNLSDLHSLVIRGASLVQWFPNLAGTVHLESLTLTGTKISSIPDDLCQNQKMLRTLDLSYNDIRDLPSFNGCRALEEISLQRNQISLIKETTFQGLTSLRILDLSRNLIREIHSGAFAKLGTITNLDVSFNELTSFPTEGLNGLNQLKLVGNFQLKDALAARDFANLRSLSVPYAYQCCAFWGCDSYANLNTEDNSPQDHSVTKEKGATDAANATSTAESEEHSQIIIHCTPSTGAFKPCEYLLGSWMIRLTVWFIFLVALLFNLLVILTVFASCSSLPASKLFIGLISVSNLLMGIYTGILTFLDAVSWGRFAEFGIWWETGSGCKVAGSLAVFSSESAVFLLTLAAVERSVFAKDVMKNGKSSHLRQFQVAALVALLGAAIAGCFPLFHGGQYSASPLCLPFPTGETPSLGFTVTLVLLNSLAFLLMAIIYTKLYCNLEKEDPSENSQSSMIKHVAWLIFTNCIFFCPVAFFSFAPLITAISISPEIMKSVTLIFFPLPACLNPVLYVFFNPKFKDDWKLLKRRVTRKHGSVSVSISSQGGCGEQDFYYDCGMYSHLQGNLTVCDCCESFLLTKPVSCKHLIKSHSCPVLTVASCQRPEAYWSDCGTQSAHSDYADEEDSFVSDSSDQVQACGRACFYQSRGFPLVRYAYNLPRVRD
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Receptor for R-spondins that potentiates the canonical Wnt signaling pathway and is involved in the formation of various organs. Upon binding to R-spondins (RSPO1, RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. In contrast to classical G-protein coupled receptors, does not activate heterotrimeric G-proteins to transduce the signal. Its function as activator of the Wnt signaling pathway is required for the development of various organs, including liver, kidney, intestine, bone, reproductive tract and eye. May also act as a receptor for norrin (NDP), such results however require additional confirmation in vivo. Required during spermatogenesis to activate the Wnt signaling pathway in peritubular myoid cells. Required for the maintenance of intestinal stem cells and Paneth cell differentiation in postnatal intestinal crypts. Acts as a regulator of bone formation and remodeling. Involved in kidney development required for maintaining the ureteric bud in an undifferentiated state. Involved in the development of the anterior segment of the eye. Required during erythropoiesis. Also acts as a negative regulator of innate immunity by inhibiting TLR2/TLR4 associated pattern-recognition and pro-inflammatory cytokine production. Plays an important role in regulating the circadian rhythms of plasma lipids, partially through regulating the rhythmic expression of MTTP. Required for proper development of GnRH neurons (gonadotropin-releasing hormone expressing neurons) that control the release of reproductive hormones from the pituitary gland.
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A2ARP1
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VIP1_MOUSE
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Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1 (EC 2.7.4.24) (Diphosphoinositol pentakisphosphate kinase 1) (Histidine acid phosphatase domain-containing protein 2A) (InsP6 and PP-IP5 kinase 1) (VIP1 homolog)
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MWSLTANEDESTTAHFFLGAGDEGLGTCGIGMRTEESDSELLEDEEDEVPPEPQIIVGICAMTKKSKSKPMTQILERLCRFDYLTVVILGEDVILNEPVENWPSCHCLISFHSKGFPLDKAVAYSKLRNPFLINDLAMQYYIQDRREVYRILQEEGIDLPRYAVLNRDPACPEECSLIEGEDQVEVNGAVFPKPFVEKPVSAEDHNVYIYYPSSAGGGSQRLFRKIGSRSSVYSPESSVRKTGSYIYEEFMPTDGTDVKVYTVGPDYAHAEARKSPALDGKVERDSEGKEVRYPVMLTAMEKLVARKVCVAFKQTVCGFDLLRANGHSFVCDVNGFSFVKNSMKYYDDCAKILGNTIMRELAPQFQIPWSIPTEAEDIPIVPTTSGTMMELRCVIAIIRHGDRTPKQKMKMEVTHPRFFALFEKHGGYKTGKLKLKRPEQLQEVLDITRLLLAELEKEPEAEIEEKTGKLEQLKSVLEMYGHFSGINRKVQLTYYPHGVKASNEGQDLQREPLAPSLLLVLKWGGELTPDGRVQAEELGRAFRCMYPGGQGDYAGFPGCGLLRLHSTFRHDLKIYASDEGRVQMTAAAFAKGLLALEGELTPILVQMVKSANMNGLLDSDSDSLSSCQHRVKARLHHILQQDAPFGPEDYDQLAPTGSTSLLNSMSVIQNPVKVCDQVFALIENLTHQIRERMQDPSSVDLQLYHSETLELMLQRWSKLERDFRQKSGRYDISKIPDIYDCVKYDVQHNGSLGLQGTAELLRLSKALADVVIPQEYGISREEKVEIAVGFCLPLLRKILLDLQRTHEDESVNKLHPLYSRGVLSPGRHVRTRLYFTSESHVHSLLSVFRYGGLLDETQDAQWQRALAYLSAISELNYMTQIVIMLYEDNTRDPLSEERFHVELHFSPGVKGVEEGSAPAGCGFRPASSENEEMKTDPGSIENLCPGKASDEPDRALQTSPQPVEGTGLPRRSPLIRNRKAGSMEVLSETSSSRPGGYRLFSSSRPPTEMKQSGLGSQCTGLFSTTVLGGSSSAPNLQDYARTHGKKLPPASLKHRDELLFVPAVKRFSVSFAKHPTNGFEGCSMVPTIYPLETLHNALSLRQVSEFLTKVCQRHTDAHAQASAALFDSMHNHQASDSPFSPPRTLHSPPLQLRHRSEKPPWYSSGPSSTVSSAGPSSPTTVDGNSHFGFSDQSSVNIHMTEEKQGFGLLQETPGDGTRELHIERQQELVEPAQSPQELPVEICPSGSQGVTKVSQTCQEVPDIVQPCHNIHEEIGQPQQEVPDISQLLLKDHDTTTNTCHLCQASQLSQKVCEEICQLCQDNHEESNQLCQEVSVKLGRMVHGFPVNVDSTAQETLMEIGRPTQEIPEDPYQEFSVKVGVLAQKAPAISELSQDIPEADKPSQELSEETELQAQEVSEEIDQESEVVDELPPEAIS
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Bifunctional inositol kinase that acts in concert with the IP6K kinases IP6K1, IP6K2 and IP6K3 to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also respectively called InsP7 and InsP8, regulate a variety of cellular processes, including apoptosis, vesicle trafficking, cytoskeletal dynamics, exocytosis, insulin signaling and neutrophil activation. Phosphorylates inositol hexakisphosphate (InsP6) at position 1 to produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4. Alternatively, phosphorylates PP-InsP5 at position 1, produced by IP6Ks from InsP6, to produce (PP)2-InsP4. Activated when cells are exposed to hyperosmotic stress.
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A2ARP9
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CTSR2_MOUSE
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Cation channel sperm-associated protein 2 (CatSper2)
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MAQEQGHFQLLRADAIRSKLIDTFSLIEHLQGLSQAVPRHTLREILDPSYQQKLMSGDQEQLVRFSIKPRRMGHITHSRRLLSRLRVRCSRMPPLSLWAGWVLDSSVFSKFIISLIFLNTFVLMVEIELMESTNTALWPVKLALEVADWFILLSFIVEILLMWLASFSLFWKDAWNVFDFFVTLLSLLPELVVLLGVPAHSVWLQLLRVCRVLRSLKLFARFRQIKVILLALVRALKSMTFLLMLLLIFFYIFAVTGVYFFREYSRSTIEGLEYNMFFSDLLNSLVTVFILFTLDHWYAVLQDIWKVPESSRVFSSIYVILWLLLGSIIFRNIIVAMMVTNFQNIRSELSEEMSHLEVQYKADMFKQQIIQRRQHSESLRGTSLGKVSEDIIETSDASDDDDDDDDDDDDDDDDDDDKSDATESDNEESDSENSESENSESEKIDPEKDYAKKSYPEKSHPEKSYPEKSHPEKSYPEKSHPKKSYDEQAEAEKVKEESKEKAYPVSHSISSHGSTAADTAFLENLDWETLVHENLPGLMDMDQDDRIVWPRDSLFRYFELLEKLQYNLEERKKLQEFAVQALMSFEDK
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Voltage-gated calcium channel that plays a central role in sperm cell hyperactivation. Controls calcium entry to mediate the hyperactivated motility, a step needed for sperm motility which is essential late in the preparation of sperm for fertilization. Activated by intracellular alkalinization.
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A2ARV4
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LRP2_MOUSE
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Low-density lipoprotein receptor-related protein 2 (LRP-2) (Glycoprotein 330) (gp330) (Megalin)
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MERGAAAAAWMLLLAIAACLAPVSGQECGSGNFRCDNGYCIPASWRCDGTRDCLDDTDEIGCPPRSCGSGFFLCPAEGTCIPSSWVCDQDKDCSDGADEQQNCPGTTCSSQQLTCSNGQCVPIEYRCDHVSDCPDGSDERNCYYPTCDQLTCANGACYNTSQKCDHKVDCRDSSDEANCTTLCSQKEFQCGSGECILRAYVCDHDNDCEDNSDEHNCNYDTCGGHQFTCSNGQCINQNWVCDGDDDCQDSGDEDGCESNQRHHTCYPREWACPGSGRCISMDKVCDGVPDCPEGEDENNATSGRYCGTGLCSILNCEYQCHQTPYGGECFCPPGHIINSNDSRTCIDFDDCQIWGICDQKCESRQGRHQCLCEEGYILERGQHCKSNDSFSAASIIFSNGRDLLVGDLHGRNFRILAESKNRGIVMGVDFHYQKHRVFWTDPMQAKVFSTDINGLNTQEILNVSIDAPENLAVDWINNKLYLVETRVNRIDVVNLEGNQRVTLITENLGHPRGIALDPTVGYLFFSDWGSLSGQPKVERAFMDGSNRKDLVTTKLGWPAGITLDLVSKRVYWVDSRYDYIETVTYDGIQRKTVARGGSLVPHPFGISLFEEHVFFTDWTKMAVMKANKFTDTNPQVYHQSSLTPFGVTVYHALRQPNATNPCGNNNGGCAQICVLSHRTDNGGLGYRCKCEFGFELDADEHHCVAVKNFLLFSSQTAVRGIPFTLSTQEDVMVPVTGSPSFFVGIDFDAQHSTIFYSDLSKNIIYQQKIDGTGKEVITANRLQNVECLSFDWISRNLYWTDGGSKSVTVMKLADKSRRQIISNLNNPRSIVVHPAAGYMFLSDWFRPAKIMRAWSDGSHLMPIVNTSLGWPNGLAIDWSTSRLYWVDAFFDKIEHSNLDGLDRKRLGHVDQMTHPFGLTVFKDNVFLTDWRLGAIIRVRKSDGGDMTVVRRGISSIMHVKAYDADLQTGTNYCSQTTHPNGDCSHFCFPVPNFQRVCGCPYGMKLQRDQMTCEGDPAREPPTQQCGSSSFPCNNGKCVPSIFRCDGVDDCHDNSDEHQCGALNNTCSSSAFTCVHGGQCIPGQWRCDKQNDCLDGSDEQNCPTRSPSSTCPPTSFTCDNHMCIPKEWVCDTDNDCSDGSDEKNCQASGTCHPTQFRCPDHRCISPLYVCDGDKDCVDGSDEAGCVLNCTSSQFKCADGSSCINSRYRCDGVYDCKDNSDEAGCPTRPPGMCHPDEFQCQGDGTCIPNTWECDGHPDCIQGSDEHNGCVPKTCSPSHFLCDNGNCIYNSWVCDGDNDCRDMSDEKDCPTQPFHCPSSQWQCPGYSICVNLSALCDGVFDCPNGTDESPLCNQDSCLHFNGGCTHRCIQGPFGATCVCPIGYQLANDTKTCEDVNECDIPGFCSQHCVNMRGSFRCACDPEYTLESDGRTCKVTASENLLLVVASRDKIIMDNITAHTHNIYSLVQDVSFVVALDFDSVTGRVFWSDLLEGKTWSAFQNGTDKRVVHDSGLSLTEMIAVDWIGRNIYWTDYTLETIEVSKIDGSHRTVLISKNVTKPRGLALDPRMGDNVMFWSDWGHHPRIERASMDGTMRTVIVQEKIYWPCGLSIDYPNRLIYFMDAYLDYIEFCDYDGQNRRQVIASDLVLHHPHALTLFEDSVFWTDRGTHQVMQANKWHGRNQSVVMYSVPQPLGIIAIHPSRQPSSPNPCASATCSHLCLLSAQEPRHYSCACPSGWNLSDDSVNCVRGDQPFLISVRENVIFGISLDPEVKSNDAMVPISGIQHGYDVEFDDSEQFIYWVENPGEIHRVKTDGSNRTAFAPLSLLGSSLGLALDWVSRNIYYTTPASRSIEVLTLRGDTRYGKTLITNDGTPLGVGFPVGIAVDPARGKLYWSDHGTDSGVPAKIASANMDGTSLKILFTGNMEHLEVVTLDIQEQKLYWAVTSRGVIERGNVDGTERMILVHHLAHPWGLVVHGSFLYYSDEQYEVIERVDKSSGSNKVVFRDNIPYLRGLRVYHHRNAADSSNGCSNNPNACQQICLPVPGGMFSCACASGFKLSPDGRSCSPYNSFIVVSMLPAVRGFSLELSDHSEAMVPVAGQGRNVLHADVDVANGFIYWCDFSSSVRSSNGIRRIKPNGSNFTNIVTYGIGANGIRGVAVDWVAGNLYFTNAFVYETLIEVIRINTTYRRVLLKVSVDMPRHIVVDPKHRYLFWADYGQKPKIERSFLDCTNRTVLVSEGIVTPRGLAVDHDTGYIYWVDDSLDIIARIHRDGGESQVVRYGSRYPTPYGITVFGESIIWVDRNLRKVFQASKQPGNTDPPTVIRDSINLLRDVTIFDEHVQPLSPAELNNNPCLQSNGGCSHFCFALPELPTPKCGCAFGTLEDDGKNCATSREDFLIYSLNNSLRSLHFDPQDHNLPFQAISVEGMAIALDYDRRNNRIFFTQKLNPIRGQISYVNLYSGASSPTILLSNIGVTDGIAFDWINRRIYYSDFSNQTINSMAEDGSNRAVIARVSKPRAIVLDPCRGYMYWTDWGTNAKIERATLGGNFRVPIVNTSLVWPNGLTLDLETDLLYWADASLQKIERSTLTGSNREVVISTAFHSFGLTVYGQYIYWTDFYTKKIYRANKYDGSDLIAMTTRLPTQPSGISTVVKTQQQQCSNPCDQFNGGCSHICAPGPNGAECQCPHEGSWYLANDNKYCVVDTGARCNQFQFTCLNGRCISQDWKCDNDNDCGDGSDELPTVCAFHTCRSTAFTCANGRCVPYHYRCDFYNDCGDNSDEAGCLFRSCNSTTEFTCSNGRCIPLSYVCNGINNCHDNDTSDEKNCPPITCQPDFAKCQTTNICVPRAFLCDGDNDCGDGSDENPIYCASHTCRSNEFQCVSPHRCIPSYWFCDGEADCVDSSDEPDTCGHSLNSCSANQFHCDNGRCISSSWVCDGDNDCGDMSDEDQRHHCELQNCSSTEFTCINSRPPNRRCIPQHWVCDGDADCADALDELQNCTMRACSTGEFSCANGRCIRQSFRCDRRNDCGDYSDERGCSYPPCRDDQFTCQNGQCITKLYVCDEDNDCGDGSDEQEHLCHTPEPTCPPHQFRCDNGHCIEMGTVCNHVDDCSDNSDEKGCGINECQDSSISHCDHNCTDTITSFYCSCLPGYKLMSDKRTCVDIDECKETPQLCSQKCENVIGSYICKCAPGYIREPDGKSCRQNSNIEPYLVFSNRYYIRNLTIDGTSYSLILQGLGNVVALDFDRVEERLYWIDAEKQIIERMFLNKTNQETIISHRLRRAESLAVDWVSRKLYWLDAILDCLFVSDLEGRQRKMLAQHCVDANNTFCFENPRGIVLHPQRGYVYWADWGDHAYIARIGMDGTNKTVIISTKIEWPNAITIDYTNDLLYWADAHLGYIEFSDLEGHHRHTVYDGTLPHPFALTIFEDTVFWTDWNTRTVEKGNKYDGSGRVVLVNTTHKPFDIHVLHPYRQPIMSNPCATNNGGCSHLCLIKAGGRGFTCECPDDFQTVQLRDRTLCMPMCSSTQFLCGNNEKCIPIWWKCDGQKDCSDGSDESDLCPHRFCRLGQFQCRDGNCTSPQALCNARQDCADGSDEDRVLCEHHRCEANEWQCANKRCIPEYWQCDSVDDCLDNSDEDPSHCASRTCRPGQFKCNNGRCIPQSWKCDVDNDCGDYSDEPIHECMTAAYNCDNHTEFSCKTNYRCIPQWAVCNGFDDCRDNSDEQGCESVPCHPSGDFRCGNHHCIPLRWKCDGIDDCGDNSDEESCVPRECTESEFRCADQQCIPSRWVCDQENDCGDNSDERDCEMKTCHPEHFQCTSGHCVPKALACDGRADCLDASDESACPTRFPNGTYCPAAMFECKNHVCIQSFWICDGENDCVDGSDEEIHLCFNVPCESPQRFRCDNSRCIYGHQLCNGVDDCGDGSDEKEEHCRKPTHKPCTDTEYKCSNGNCVSQHYVCDNVDDCGDLSDETGCNLGENRTCAEKICEQNCTQLSNGGFICSCRPGFKPSTLDKNSCQDINECEEFGICPQSCRNSKGSYECFCVDGFKSMSTHYGERCAADGSPPLLLLPENVRIRKYNISSEKFSEYLEEEEHIQAIDYDWDPEGIGLSVVYYTVLSQGSQFGAIKRAYLPDFESGSNNPVREVDLGLKYLMQPDGLAVDWVGRHIYWSDAKSQRIEVATLDGRYRKWLITTQLDQPAAIAVNPKLGLMFWTDQGKQPKIESAWMNGEHRSVLASANLGWPNGLSIDYLNGDRIYWSDSKEDVIESIKYDGTDRRLIINDAMKPFSLDIFEDQLYWVAKEKGEVWRQNKFGKGNKEKLLVVNPWLTQVRIFHQLRYNQSVSNPCKQVCSHLCLLRPGGYSCACPQGSDFVTGSTVECDAASELPITMPSPCRCMHGGSCYFDENDLPKCKCSSGYSGEYCEIGLSRGIPPGTTMALLLTFAMVIIVGALVLVGFFHYRKTGSLLPSLPKLPSLSSLAKPSENGNGVTFRSGADVNMDIGVSPFGPETIIDRSMAMNEQFVMEVGKQPVIFENPMYAAKDSTSKVGLAVQGPSVSSQVTVPENVENQNYGRSIDPSEIVPEPKPASPGADETQGTKWNIFKRKPKQTTNFENPIYAEMDTEQKEAVAVAPPPSPSLPAKASKRSSTPGYTATEDTFKDTANLVKEDSDV
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Multiligand endocytic receptor. Acts together with CUBN to mediate endocytosis of high-density lipoproteins. Mediates receptor-mediated uptake of polybasic drugs such as aprotinin, aminoglycosides and polymyxin B (By similarity). In the kidney, mediates the tubular uptake and clearance of leptin. Also mediates transport of leptin across the blood-brain barrier through endocytosis at the choroid plexus epithelium (By similarity). Endocytosis of leptin in neuronal cells is required for hypothalamic leptin signaling and leptin-mediated regulation of feeding and body weight. Mediates endocytosis and subsequent lysosomal degradation of CST3 in kidney proximal tubule cells. Mediates renal uptake of 25-hydroxyvitamin D3 in complex with the vitamin D3 transporter GC/DBP. Mediates renal uptake of metallothionein-bound heavy metals (By similarity). Together with CUBN, mediates renal reabsorption of myoglobin (By similarity). Mediates renal uptake and subsequent lysosomal degradation of APOM (By similarity). Plays a role in kidney selenium homeostasis by mediating renal endocytosis of selenoprotein SEPP1. Mediates renal uptake of the antiapoptotic protein BIRC5/survivin which may be important for functional integrity of the kidney. Mediates renal uptake of matrix metalloproteinase MMP2 in complex with metalloproteinase inhibitor TIMP1. Mediates endocytosis of Sonic hedgehog protein N-product (ShhN), the active product of SHH (By similarity). Also mediates ShhN transcytosis (By similarity). In the embryonic neuroepithelium, mediates endocytic uptake and degradation of BMP4, is required for correct SHH localization in the ventral neural tube and plays a role in patterning of the ventral telencephalon. Required at the onset of neurulation to sequester SHH on the apical surface of neuroepithelial cells of the rostral diencephalon ventral midline and to control PTCH1-dependent uptake and intracellular trafficking of SHH. During neurulation, required in neuroepithelial cells for uptake of folate bound to the folate receptor FOLR1 which is necessary for neural tube closure. In the adult brain, negatively regulates BMP signaling in the subependymal zone which enables neurogenesis to proceed. In astrocytes, mediates endocytosis of ALB which is required for the synthesis of the neurotrophic factor oleic acid (By similarity). Involved in neurite branching. During optic nerve development, required for SHH-mediated migration and proliferation of oligodendrocyte precursor cells. Mediates endocytic uptake and clearance of SHH in the retinal margin which protects retinal progenitor cells from mitogenic stimuli and keeps them quiescent. Plays a role in reproductive organ development by mediating uptake in reproductive tissues of androgen and estrogen bound to the sex hormone binding protein SHBG. Mediates endocytosis of angiotensin-2 (By similarity). Also mediates endocytosis of angiotensin 1-7 (By similarity). Binds to the complex composed of beta-amyloid protein 40 and CLU/APOJ and mediates its endocytosis and lysosomal degradation (By similarity). Required for embryonic heart development. Required for normal hearing, possibly through interaction with estrogen in the inner ear.
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A2AS55
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ANR16_MOUSE
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Ankyrin repeat domain-containing protein 16
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MALPGDPRRLCRLVQEGRLRDLQEELAVARGCRGPAGDTLLHCAARHGRQDILAYLVEAWSMDIEATNRDYKRPLHEAASMGHRDCVRYLLGRGAVVDSLKKADWTPLMMACTRKNLDVIQDLVEHGANPLLKNKDGWNSFHIASREGHPVILRYLLTVCPDAWKTESNIRRTPLHTAAMHGCLEAVQVLLERCHYEPDCRDNCGVTPFMDAIQCGHVSIAKLLLEQHKACSSAADSMGAQALHRAAVTGQDEAIRFLVCGLGIDVDVRAKSSQLTALHYAAKEGQTNTVQTLLSLGADINSTDERNRSVLHLACAGQHVACTRLLLQSGLKDSEDLTGTLAQQLTRSVDILQDFDHDVKS
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Required to prevent the misactivation of serine (Ser) with tRNA(Ala) by promoting the hydrolysis of Ser-mischarged tRNA(Ala), thereby playing a role in translational fidelity. Binds directly to the catalytic domain of AARS/AlaRS and captures Ser that is misactivated by AARS/AlaRS, preventing the charging of Ser adenylates to tRNA(Ala) and precluding Ser misincorporation in nascent peptides.
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A2AS89
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GDAH_MOUSE
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Guanidino acid hydrolase, mitochondrial (EC 3.5.3.-) (Arginase, mitochondrial) (EC 3.5.3.1) (Guanidinobutyrase, mitochondrial) (EC 3.5.3.7) (Guanidinopropionase, mitochondrial) (EC 3.5.3.17)
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MLRLLRSSWARGLGSGVATWRPSAGLFRPGCPGIRQASGASDTPHHQSPSSESPVQPVGVGVCSMMRLPLQSSPEGLDAAFIGVPLDTGTSNRPGARFGPCRIREESLMLGAVNPSTGALPFQSLRVADLGNVNVNLYNLQDSCLLIREAYQNVLAAGCIPLTLGGDQTITYPILQAVAKEHGPVGLVHVGAHTNTTDKPREEKVYHRTPFRRSVDEGLLDSKRVVQIGIRGSSRTLDPYRYSRSQGFRVVLAEDCWMKSLVPLMAEVRQQMGGKPLYISFAIDALDPAYAPGTGTPEIAGLTPSQALEIIRGCQGLNVVGCDLVEVSPPYDLSGNTALLAANLLFEMLCALPKVTTV
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Hydrolyzes linear guanidino acids to form urea and the corresponding amines. Displays specificity for substrates having a negatively charged head group and short chains including taurocyamine, guanidino propanoic and butanoic acids. May protect cells by detoxifying potentially harmful amounts of guanidino acids. Metabolizes L-arginine with low efficiency.
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A2ASI5
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SCN3A_MOUSE
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Sodium channel protein type 3 subunit alpha (Sodium channel protein brain III subunit alpha) (Sodium channel protein type III subunit alpha) (Voltage-gated sodium channel subtype III) (Voltage-gated sodium channel subunit alpha Nav1.3)
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MAQALLVPPGPESFRLFTRESLAAIEKRAAEEKAKKPKKEQDIDDENKPKPNSDLEAGKNLPFIYGDIPPEMVSEPLEDLDPYYVSKKTFVVLNKGKAIFRFSATSALYILTPLNPVRKIAIKILVHSLFSMLIMCTILTNCVFMTLSNPPDWTKNVEYTFTGIYTFESLIKILARGFCLEDFTFLRDPWNWLDFSVIVMAYVTEFVDLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCLQWPPSDSAFEINTTSYFNGTMDSNGTFVNVTMSTFNWKDYIADDSHFYVLDGQKDPLLCGNGSDAGQCPEGYICVKAGRNPNYGYTSFDTFSWAFLSLFRLMTQDYWENLYQLTLRAAGKTYMIFFVLVIFLGSFYLVNLILAVVAMAYEEQNQATLEEAEQKEAEFQQMLEQLKKQQEEAQAVAAASAASRDFSGIGGLGELLESSSEASKLSSKSAKEWRNRRKKRRQREHLEGNHRPEGDRFPKSESEDSVKRRSFLFSLDGNPLSGDKKLCSPHQSLLSIRGSLFSPRRNSKTSIFSFRGRAKDVGSENDFADDEHSTFEDSESRRDSLFVPHRPGERRNSNGTTTETEVRKRRLSSYQISMEMLEDSSGRQRAMSIASILTNTMEELEESRQKCPPCWYRFANVFLIWDCCDSWLKVKHLVNLIVMDPFVDLAITICIVLNTLFMAMEHYPMTEQFSSVLTVGNLVFTGIFTAEMVLKIIAMDPYYYFQEGWNIFDGIIVSLSLMELGLANVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKINEDCKLPRWHMNDFFHSFLIVFRVLCGEWIETMWDCMEVAGQTMCLIVFMLVMVIGNLVVLNLFLALLLSSFSSDNLAATDDDNEMNNLQIAVGRMQKGIDYVKNKIRECFRKAFFRKPKVIEIHEGNKIDSCMSNNTGVVEISKELNYLKDGNGTTSGVGTGSSVEKYVIDENDYMSFINNPSLTVTVPIAVGESDFENLNTEEFSSESELEESKEKLNATSSSEGSTVDVAPPREGEQAEIEPEEDLKPEACFTEGCIKKFPFCQVSTEEGKGKIWWNLRKTCYSIVEHNWFETFIVFMILLSSGALAFEDIYIEQRKTIKTMLEYADKVFTYIFILEMLLKWVAYGFQTYFTNAWCWLDFLIVDVSLVSLVANALGYSELGAIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYHCVNMTTGSMFDMSEVNNFSDCQALGKQARWKNVKVNFDNVGAGYLALLQVATFKGWMDIMYAAVDSRDVKLQPVYEENLYMYLYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPANKFQGMVFDFVTRQVFDISIMILICLNMVTMMVETDDQSKYMTLVLSRINLVFIVLFTGEFLLKLISLRYYYFTIGWNIFDFVVVILSIVGMFLAELIEKYFVSPTLFRVIRLARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYAIFGMSNFAYVKKEAGIDDMFNFETFGNSMICLFQITTSAGWDGLLAPILNSAPPDCDPDAIHPGSSVKGDCGNPSVGIFFFVSYIIISFLVVVNMYIAVILENFSVATEESAEPLSEDDFEMFYEVWEKFDPDATQFIEFCKLSDFAAALDPPLLIAKPNKVQLIAMDLPMVSGDRIHCLDILFAFTKRVLGESGEMDALRIQMEDRFMASNPSKVSYEPITTTLKRKQEEVSAAIIQRNYRCYLLKQRLKNISNTYDKETIKGRIVLPIKGDMVIDKLNGNSTPEKTDGSSSTTSPPSYDSVTKPDKEKFEKDKPEKESKGKEV
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Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. May contribute to the regulation of serotonin/5-hydroxytryptamine release by enterochromaffin cells. In pancreatic endocrine cells, required for both glucagon and glucose-induced insulin secretion.
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A2ASQ1
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AGRIN_MOUSE
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Agrin [Cleaved into: Agrin N-terminal 110 kDa subunit; Agrin C-terminal 110 kDa subunit; Agrin C-terminal 90 kDa fragment (C90); Agrin C-terminal 22 kDa fragment (C22)]
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MPPLPLEHRPRQQPGASVLVRYFMIPCNICLILLATSTLGFAVLLFLSNYKPGIHFTAAPSMPPDVCRGMLCGFGAVCEPSVEDPGRASCVCKKNVCPAMVAPVCGSDASTYSNECELQRAQCNQQRRIRLLRQGPCGSRDPCANVTCSFGSTCVPSADGQTASCLCPTTCFGAPDGTVCGSDGVDYPSECQLLRHACANQEHIFKKFDGPCDPCQGSMSDLNHICRVNPRTRHPEMLLRPENCPAQHTPICGDDGVTYENDCVMSRIGAARGLLLQKVRSGQCQTRDQCPETCQFNSVCLSRRGRPHCSCDRVTCDGAYRPVCAQDGHTYDNDCWRQQAECRQQQTIPPKHQGPCDQTPSPCRGAQCAFGATCTVKNGKAVCECQRVCSGGYDPVCGSDGVTYGSVCELESMACTLGREIRVARRGPCDRCGQCRFGSLCEVETGRCVCPSECVESAQPVCGSDGHTYASECELHVHACTHQISLYVASAGHCQTCGETVCTFGAVCSAGQCVCPRCEHPPPGPVCGSDGVTYLSACELREAACQQQVQIEEARAGPCEPAECGSGGSGSGEDNACEQELCRQHGGVWDEDSEDGPCVCDFSCQSVLKSPVCGSDGVTYSTECHLKKARCEARQELYVAAQGACRGPTLAPLLPMASPHCAQTPYGCCQDNVTAAQGVGLAGCPSTCHCNPHGSYSGTCDPVTGQCSCRPGVGGLRCDRCEPGFWNFRGIVTDGHSGCTPCSCDPRGAVRDDCEQMTGLCSCRPGVAGPKCGQCPDGQALGHLGCEADPTTPVTCVEMHCEFGASCVEEAGFAQCVCPTLTCPEANSTKVCGSDGVTYGNECQLKTIACRQRLDISIQSLGPCRESVAPGVSPTSASMTTPRHILSRTLASPHSSLPLSPSTTAHDWPTPLPTSPQTVVGTPRSTAATPSDVASLATAIFRESGSTNGSGDEELSGDEEASGGGSGGLEPPVGSVVVTHGPPIERASCYNSPLGCCSDGKTPSLDSEGSNCPATKAFQGVLELEGVEGQELFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFWSIRLRELGPGKLVRAIVDVHFDPTTAFQAPDVGQALLQQIQVSRPWALAVRRPLREHVRFLDFDWFPTFFTGAATGTTAAVATARATTVSRLSASSVTPRVYPSYTSRPVGRTTAPLTTRRPPTTTASIDRPRTPGPQRPPKSCDSQPCLHGGTCQDLDSGKGFSCSCTAGRAGTVCEKVQLPSVPAFKGHSFLAFPTLRAYHTLRLALEFRALETEGLLLYNGNARGKDFLALALLDGHVQFRFDTGSGPAVLTSLVPVEPGRWHRLELSRHWRQGTLSVDGEAPVVGESPSGTDGLNLDTKLYVGGLPEEQVATVLDRTSVGIGLKGCIRMLDINNQQLELSDWQRAVVQSSGVGECGDHPCSPNPCHGGALCQALEAGVFLCQCPPGRFGPTCADEKNPCQPNPCHGSAPCHVLSRGGAKCACPLGRSGSFCETVLENAGSRPFLADFNGFSYLELKGLHTFERDLGEKMALEMVFLARGPSGLLLYNGQKTDGKGDFVSLALHNRHLEFRYDLGKGAAIIRSKEPIALGTWVRVFLERNGRKGALQVGDGPRVLGESPKSRKVPHTMLNLKEPLYVGGAPDFSKLARGAAVASGFDGAIQLVSLRGHQLLTQEHVLRAVDVAPFAGHPCTQAVDNPCLNGGSCIPREATYECLCPGGFSGLHCEKGIVEKSVGDLETLAFDGRTYIEYLNAVTESELTNEIPAPETLDSRALFSEKALQSNHFELSLRTEATQGLVLWIGKVGERADYMALAIVDGHLQLSYDLGSQPVVLRSTVKVNTNRWLRVRAHREHREGSLQVGNEAPVTGSSPLGATQLDTDGALWLGGLQKLPVGQALPKAYGTGFVGCLRDVVVGHRQLHLLEDAVTKPELRPCPTL
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[Isoform 1]: Heparan sulfate basal lamina glycoprotein that plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ) and directs key events in postsynaptic differentiation. This neuron-specific (z+) isoform is a component of the AGRN-LRP4 receptor complex that induces the phosphorylation and activation of MUSK. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane. Calcium ions are required for maximal AChR clustering. AGRN function in neurons is highly regulated by alternative splicing, glycan binding and proteolytic processing. Modulates calcium ion homeostasis in neurons, specifically by inducing an increase in cytoplasmic calcium ions. Functions differentially in the central nervous system (CNS) by inhibiting the alpha(3)-subtype of Na+/K+-ATPase and evoking depolarization at CNS synapses. This transmembrane agrin (TM-agrin) isoform, the predominate form in neurons of the brain, induces dendritic filopodia and synapse formation in mature hippocampal neurons in large part due to the attached glycosaminoglycan chains and the action of Rho-family GTPases. Isoform 2 and isoform 3: these isoforms lacking the 'z' insert (z0) are muscle-specific, have no AChR clustering ability and may be involved in nervous system endothelial cell differentiation. [Agrin N-terminal 110 kDa subunit]: Involved in regulation of neurite outgrowth probably due to the presence of the glycosaminoglcan (GAG) side chains of heparan and chondroitin sulfate attached to the Ser/Thr- and Gly/Ser-rich regions. Also involved in modulation of growth factor signaling (By similarity). {ECO:0000250, ECO:0000269|PubMed:10402191, ECO:0000269|PubMed:11018052, ECO:0000269|PubMed:12796478, ECO:0000269|PubMed:17611272, ECO:0000269|PubMed:19303856, ECO:0000269|PubMed:21885656, ECO:0000269|PubMed:8653787}. [Agrin C-terminal 22 kDa fragment]: This released fragment is important for agrin signaling and to exert a maximal dendritic filopodia-inducing effect. All 'z' splice variants (z+) of this fragment also show an increase in the number of filopodia.
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A2ASS6
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TITIN_MOUSE
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Titin (EC 2.7.11.1) (Connectin)
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MTTQAPMFTQPLQSVVVLEGSTATFEAHVSGSPVPEVSWFRDGQVISTSTLPGVQISFSDGRARLMIPAVTKANSGRYSLRATNGSGQATSTAELLVTAETAPPNFSQRLQSMTVRQGSQVRLQVRVTGIPTPVVKFYRDGAEIQSSLDFQISQEGDLYSLLIAEAYPEDSGTYSVNATNSVGRATSTAELVVQGEEVVPAKKTKTIVSTAQISETRQTRIEKKIEAHFDARSIATVEMVIDGATGQLPHKTPPRIPPKPKSRSPTPPSIAAKAQLARQQSPSPIRHSPSPVRHVRAPTPSPVRSVSPAGRISTSPIRSVKSPLLIRKTQTTTMATGPEVPPPWKQEGYVASSTEAEMRETTMTSSTQIRREERWEGRYGVQEQVTISGAAAAAASASVSSSFTAGAITTGTKEVKQETDKSAAVATVVAAVDMARVREPAISAVEQTAQRTTTTAVHIQPAQEQARKEAEKTAVTKVVVAADKAKEQELKSRTREVMVTTQEQTHISHEQIRKETEKAFVPKVVISATKAKEQETRITGEITTKQEQKRITQETIRQETEEIAASMVVVATAKSTKLEAAVGVQEETAIQQDQMHLTHEQMMKETRKTVVPKVIVATPKIKEQDLVSRSREAITTKRDQVQITQEKKRKEVETTALSTIAVATAKAKEQETVLRSREAMATRQEHIQVTHGQVGVGKKAEAVATVVAAVDQARVREPREPTHVEESHSQQTTLEYGYKEHISTTKVPEQPRRPASEPHVVPQAVKPAVIQAPSETHIKTTDQMGMHISSQVKKTTDISTERLVHVDKRPRTASPHFTVSKISVPKTEHGYEASIAGSAIATLQKELSATSSTQKITKSVKAPTVKPGETRVRAEPTPSPQFPFADMPPPDTYKSQAGIEVKKEVGVSISGSTVREEHFEVLRGREAKVTETARVPAPAEVPVTPPTLVSGLKNVTVIEGESVTLECHISGYPSPKVTWYREDYQIESSIDFQITFQGGIARLMIREAFAEDSGRFTCSAVNEAGTVSTSCYLAVQVSEEFDKETTLTEKFATEEKRFVESRDVVMTDTSITEEQAGPGEPAAPFFISKPVVQKLVEGGSVVFECQIGGNPKPHVYWKKSGVPLTTGYRYKVSYNKQTGECRLVISMTFADDAGEYTIVIRNKHGETSASASLLEEADYEALVKTQQEMLYQTQMSTFIQEPKVGEIAPGFAYSEYEKEYEKEQALIRKKMAKDTVMVRTFVEDQEFHISSFEERLIKEIEYRIIKTTLEELLEEDGEEKMAVDISESEAIESGFDIRIKNYRILEGMGVTFHCKMSGYPLPKIAWYKDGKRIRHGERYQMDFLQDGRASLRIPVVLPEDEGIYTAFASNIKGNAICSGKLYVEPAAPFSAPTYMPTPEAVSRIRSVSPRSLSRSPIRMSPAMSPARMSPARMSPARMSPARMSPGRRLEETDESQLERLYKPVFVLKPASFKCLEGQTARFDLKVVGRPMPETFWFHNGQQIVNDYTHKVVIKEDGTQSLIIVPASPSDSGEWTVVAQNRAGKSTISVTLTVEAVEHQIKPAFVEKLKNVNIKEGSRLEMKVRATGNPNPDIVWLKNSDIIVPHKYPRIRIEGTRGEAALKIDSIISQDSAWYTATAINKAGRDTTRCKVNVEVEFAEPEPERKLIIPRGTYRAKEIAAPELEPLHLRYGQEQWEEGDLYDKEKQQKPFFKKKLTSLRLKRFGPAHFECRLTPIGDPTMVVEWLHDGKPLEAANRLRMINEFGYCSLDYGAAYSRDSGVITCRATNKYGTDHTSATLIVKDEKSLVEESQLPDGKKGLQRIEELERMAHEGALTGVTTDQKEKQKPDIVLFPEPVRVLEGETARFRCRVTGYPQPKVNWYLNGQLIRKSKRFRVRYDGIHYLDIVDCKSYDTGEVKVTAENPEGVTEHKVKLEIQQREDFRSVLRRAPEPKPEFHVHEPGKLQFEVQKVDRPVDTSETKEVVKLKRAERITHEKVSEESEELRSKFKRRTEEGYYEAITAVELKSRKKDESYEELLKKTKDELLHWTKELTEEEKKALAEEGKITIPTFKPERIELSPSMEAPKIFERIQSQTVGQGSDAHFRVRVVGKPDPECEWYKNGVKIERSDRIYWYWPEDNVCELVIRDVTAEDSASIMVKAINIAGETSSHAFLLVQAKQLITFTQELQDVVAKEKDTMATFECETSEPFIKVKWYKDGIEVHAGDKYRMHSDRKVHFLSVLTIDTSDAEDYSCVLVEDENIKTTAKLIVEGAVVEFVKELQDIEVPESYSGELECIISPENIEGKWYHNDVELKSNGKYSITSRRGRQNLTVKDVTKEDQGEYSFVVDGKKTTCKLKMKPRPIAILQGLSDQKVCEGDIVQLEVKVSLENVEGVWMKDGQEVQHSDRVHIVIDKQSHMLLIEDMTKEDAGNYSFTIPALGLSTSGNVSVYSVDVITPLKDVNVIEGTKAVLECKVSVPDVTSVKWYLNDEQIKPDDRVQSIVKGTKQRLVINRTHASDEGPYKLMVGRVETSCNLSVEKIKIIRGLRDLTCTETQNVVFEVELSHSGIDVVWNFKGKEIKPSSKYKIEAHGKIYKLTVLNMMKDDEGEYAFYAGENTTSGKLTVAGGAISTPLTDQTVAESQEAVFECEVANPESEGEWLKDGKHLALSNNFRGESDGHKRRLVIAAAKLDDAGEYTYKVATSKTSAKLKVEAVKIKKTLRNLTVTETQDAVFSVELTHPDVKGVQWIKNGVVLDSNDKYEISVKGTLYSLKIKNCAMADESVYGFKLGRLGASARLHVETVKIIKKPKDVTALENATVTFEVSVSHDTVPVKWFHKNVEIKPSDKHRLVSERKVHKLMLQSISPSDAGEYTAMVGQLECKAKLFVETLHITKTMKSIEVPETKAASFECEVSHFNVPSMWLKNGVEIEMSEKFKIVVQGKLHQLIIMNTSTEDSAEYTFVCGNDQVSATLTVTPIMITSMLKDINAEEKDTITFEVTVNYEGISYKWLKNGVEIKSTDRCQMRTKKLTHSLNIRNVHFGDAADYTFVAGKATSTATLYVEARHIEFRKHIKDIKVLEKKRAMFECEVSEPDITVQWMKDGQELQIADRIKIQKEKYVHRLLIPSTRMSDAGKYTVVAGGNMSTANLFVEGRDVRIRSIKKEVQVIEKQRAVVEFEVNEDDVDAHWYKDGIEINFQVQERHQYVVERRIHRMFISETRHSDAGEYTFVAGRNRSSVTLYVNAPEPPQVLQELQPVTVQSGKPARFCAVISGRPQPKISWYKEEQLLSTGFKCKFLHDGQEYTLLLIEAFPEDAAVYTCEAKNDYGVATTSASLSVEVPEVVSPDQEMPVYPPAIVTPLQDTVTSEGRPARFQCQVSGTDLKVSWYCKDKKIKPSRFFRMTQFEDTYQLEIAEAYPEDEGTYAFVANNAVGQVSSTATLRLEAPESILHERIGQQIEMEMKEIASLLSAEEDFQTYSSDLRLPNANETLELLSEPPARSTQFDSRQEGAAPVFIREISDVEISVEDVAKLSVTVTGCPKPKIQWFFNGMLLTPSADYKFVFDGDTHSLIILFTRFQDEGEYTCLASNEYGKAVCSAHLRISPRGERSTEMESGEKKALEKPKGPCPPYFFKELKPVHCGPGIPAVFEYSVHGEPAPTVLWFKEDMPLYTSVCYTIIHSPDGSGTFIVNDPQRGDSGLYLCKAQNLWGESTCAAELLVLPEDTDVPDASCKEESTLGVPGDFLETSARGPLVQGVDSRQEITAFAEGTISKAALIAEETLQLSYERSVDDSEVGTGVTIGAQKLPPVVLSTPQGTGELPSIDGAVHTQPGRGPPPTLNLQAVQAQTTLPKEATLQFEEPEGVFPGASSAAQVSPVTIKPLITLTAEPKGNYPQSSTAAPDHALLSSVAAETLQLGEKKIPEVDKAQRALLLSQSLAEGCVESLEVPDVAVSNMRSEPQVPFQHTCTEGKILMASADTLKSTGQDVALRTEEGKSLSFPLALEEKQVLLKEEQSEVVAVPTSQTSKSEKEPEAIKGVKEVREQELLSKETLFPSMPEEQRLHLKTQVRRALQAAVAREQANLFSEWLRNIDKVEVTAVNFTQEPKRILCTYLITSVSSLTEELTVTIEDIDPQMANLETGLKDALCSIVCEERNILMAEDPRIHEEDKIDVQGGRDHLSDAQKVETVIEAEADSKYLVSKEEVSWSKVESQLKDGDTNEVPQAETLKLAEESGTQKTSTEMSQEEAEGTLADLCPAVLKHLVDTISEEGDTVHLTSSISNAKEVHWYFKGNLVPSDGKFKCLKEQNAYTLVIEAVKTEDEGEYVCEASNDSGKAKTSAKLTVGERAAPVIKRRIEPLEVALGHLAKFTCEIQGAPNVRFQWFKAGREIYESDKCSIRSSNYVSSLEILRTQVVDCGEYTCKASNEYGSVSCTATLTVTEAYPPTFLSRPKALTTFVGKAAKFLCTVSGTPVIEIIWQKDGAALSPSPDCRVTDADNKHSLELSNLTVQDRGIYSCKASNKFGADICQAELTIIDKPHFIKELEAVQSAINKKIHLECQVDEDRKVTITWSKDGQKLPAGKDYKIYFEDKIASLEIPLAKLKDSGTYTCTASNEAGSSSSSAAVAVREPPSFVKKVDPSYLMLPGESARLHCKLKGSPVIQVTWFKNNKELSESNTVRMSFVNSEAILDITDVKVDDSGTYSCEATNDVGSDSCSTEVVIKEPPSFIKTLEPADIVRGANALLQCEIAGTGPFEVNWFKDKKQIRSSKKYRLFTQKTFVYLEISSFNSADVGDYECVVANEVGKCGCVATHLLKEPPTFVKKVDDFTALAGQTVTLQAAVRGSEPISVMWMKGQEVIKEDGKIKMSFSNGVAVLTIPDVQISLGGKYTCLAENEAGSQTSVGELIVKEPAKIIERAELIQVTAGDPATLEYTVSGTPELKPKWYKDGRPLVASKKYRISFKNNIAQLKFYSAELHDSGQYTFEISNEVGSSSCETTFTVLDRDIAPLFTKPLRNVDSVVGGACRLDCKIAGSLPMRVSWFKDGKELTASDRYQIAFVEGTASLEISRVDMNDAGNFTCRATNSVGSKDSSGALIVQEPPSFVTKPGSRDVLPGSAVCLKSAFQGSAPLTIKWFKGDKELVSGGSCYITKETSESSLELYAVKTSDSGTYTCKVSNVAGSVECSADLFVKEPATFIEKLEPSQLLKKGDGTQLACKVTGTPPIKITWFANDRELRESSKHKMSFAESTAVLRLTDVAIEDSGEYMCEAQNEAGSDHCTGIVIVKESPYFTKEFKSIEVLKEYDVMLLAEVAGTPPFEITWFKDNTTLRSGRKYKTFLQDQLVSLQVLKFVAADAGEYQCRVTNEVGSSTCSARVTLREPPSFIKKIEATSSLRGGTAAFQATLKGSLPITVTWLKDNDEITEDDNIRMTFENNVASLYLSGIEVKHDGKYVCQAKNDAGIQRCSALLSVKEPATIMEEAVSIDVTQGDPATLQVKFSGTKEISAKWFKDGQELTLGPKYKISVTDTVSILKIISTEKKDSGEYTFEVQNDVGRSSCKASINVLDLIIPPSFTKKLRKMDSIKGSFIDLECIVAGSHPISIQWFKDDQEISASDKHKFSFHDNTAFLEISQLEGTDSGTYTCSATNKAGHSQCSGHLTVKEPPYFVEKPQSQDVNPGTRVQLKALVGGTAPMTIKWFKDNKELHPGAARSVWKDDTSTILELFSAKAADSGTYICQLSNDVGTTSSKATIFVKEPPQFIKKPSPVLVLRNGQSTTFECQVTGTPEIRVSWYLDGNEITDLRKYGISFVDGLATFQISNARVENSGTYVCEARNDAGTASCSIELKVKEPPIFIRELEPVEVVKDSDVELECEVMGTTPFEVTWLKNNKEIRSGKKYTMSEKMSVFYLHITKCDPSDVGEYQCIIANEGGSCACSARVALKEPPSFIKKIENVTTVLKSSATFQSTVAGSPPISITWLKDDQILEENDNVHISFEDSVATLQVRSVDNGHSGRYTCQAKNESGIERCYAFLLVQEPAQIIEKAKSVDVTEKDPVTLECVVAGTPELKVKWLKDGKQIVPSRYFSMSFENNVASFRIQSVMKQDSGQYTFKVENDFGSSSCDAYLRVLDQDIPPSFTKKLTKMDKVLGSSIHMECKVSGSLPISAQWFKDGKEISTSAKYRLVCHENTVSLEVSNLELEDTANYTCKVSNVAGDNACSGILTVKEPPSFLVKPERQQAIPDSTVEFKAVLKGTPPFKIKWLKDDVELVSGPKCFIGLEGSTSFLNLYSVDSSKTGQYTCQVTNDVGSDSCTTMLLVTEPPKFVKKLEASKIIKAGDSARLECKITGSPEIQVVWYRNEHELTASDKYQMTFIDSVAVIQMNSLGTEDSGDFICEAQNPAGSTSCSTKVIVKEPPVFSSFPPIVETLKNTEVSLECELSGTPPFEVVWYKDKRQLRSSKKYKVASKNFHASIHILNVESTDIGEYHCKAQNEVGSDACVCAVKLKEPPKFISKLNSLTVVAGEPAELQASIEGAQPISVQWLKEKEEVIRESENIRISFVNNVATLQFAKVEPANAGKYICQVKNDGGVRENMATLTVLEPAVIIEKAGSMTVTVGETCALECKVAGTPELSVEWYKDGKLLTSSQKHKFSFYNKISSLKILSVEKEDAGTYTFQVQNNVGKSSCTAVVDVSDRMVPPSFTRRLKDTGGVLGTSCILECKVAGSSPISIAWFHEKTKIVSGAKYQTTFSDNVCTLQLNSLDSSDMGSYTCVAANVAGSDECRALLTVQEPPSFVKEPEPLEVLPGKNITFTSVIRGTPPFKVGWFRGARELVKGNRCNIYFEDTVAELELFNIDISQSGEYTCVVSNNAGQASCTTRLFVKEPATFVKKLSDHSVEPGKSIILEGTYTGTLPISVTWKKDGVSITPSERCNIVTTEKTCILEILSSTKGDAGHYSCEIENEAGRDACDALVSTLEPPYFVTELEPLEASVGDSVSLQCQVAGTPEITVSWFKGDTKLRSTPEYRTYFTNNVATLVFNKVSINDSGEYTCMAENSIGTAASKTIFRIQERQLPPSFARQLKDIEQTVGLPVTLTCRLNGSAPIQVCWYRDGVLLRDDENLQMSFVDNVATLKILQTDLSHSGQYSCSASNPLGTASSTARLTAREPKKSPFFDIKPVSIDVIAGESADFECHVTGAQPMRVTWSKDNKEIRPGGNYTITCVGNTPHLRILKVGKGDSGQYTCQATNDVGKDMCSAQLSVKEPPKFIKKLDASKVAKQGESIQLECKISGSPEIKVVWFRNDSELHESWKYNMSFVNSVALLTINEASAEDTGDYICEAHNGVGDASCSTALKVKAPPVFTQKPPPVGALKGSDVILQCEISGTPPFEVVWVKDRKQVRSSKKFKITSKNFDTSLHIFNLEAPDIGEYHCKATNEVGSDTCACTVKFKEPPRFVKKLSDASTLIGDPVELQAVVEGFQPISVVWLKDKGEVIRESENVRISFVDNIATLQLGSPEASQSGKYVCQIKNDAGMRECSAVLTVLEPATIVEKPEPMTVTTGNPFTLECVVAGTPELSAKWFKDGRELSSGSRHHITFVRNLASLKIPSAEMNDKGLYTFEVENRVGKSSCTVSVHVSDRVVPPSFVRRLKDTSATLGASVVLECRVSGSAPISVGWFLDGNEIISSPKCQSSFADNVCTLTLSSLEPSDTGAYTCVAANVAGQDESSAVLTVQEPPSFEQTPDSVEVLPGMSLTFTSVIRGTPPFKVKWFKGSRELVSGEACTISLEDFVTELELLEVEPGQSGDYSCLVTNDAGSASCTTHLFVKEPATFVKRLADTSVETGSPIVLEATYSGTPPISVSWMKNEYPLSQSPNCGITTTEKSSILEILESTIEDYAQYACLIENEAGQDICEALVSVLEPPYFIEPLEHVEAAIGEPITLQCKVDGTPEIRISWYKEHTKLRSAPAYKMQFKNNVASLVINKVDHSDVGEYTCKAENSVGAVASSAVLVIKERKLPPSFARKLKDVHETLGFPVAFECRINGSEPLQVSWYKDGELLKDDANLQMSFVHHVATLQILQTDQSHVGQYNCSASNPLGTASSSAKLILSEHEVPPFFDLKPVSVDLALGESGSFKCHVTGTAPIKITWAKDNREIRPGGNYKMTLVENTATLTVLKVAKGDAGQYTCYASNVAGKDSCSAQLGVQEPPRFIKKLDQSRIVKQDEYTRYECKIGGSPEIKVLWYKDEVEIQESSKFRMSFEDSVAILEMHSLSVEDSGDYTCEARNAAGSASSSTSLKVKEPPVFRKKPFPVETLKGADVHLECELQGTPPFQVSWHKDKRELRSGKKYKIMSENLLTSIHILNVDTADIGEYQCKATNDVGSDTCVGSVTMKAPPQFVKKLTDISTIIGKEVQLQTTIEGAEPISVAWFKDKGEIVRESDNIWISYSENIATLQFSRAEPANAGKYTCQIKNDAGMQECYATLSVLEPAAIVEKPESIKVTTGDTCTLECTVSGTPELSTKWFKDGKELTSDNKYKISFFNKVSGLKIINVVPGDSGVYSFEVQNPVGKDSCKVSIQVSDRIIPPSFTRKLKETNGLSGSSVVMECKVYGSPPISVLWFHDGNEISSGRKYQTTLTDNTCALTVNMLEEADAGDYTCIATNVAGSDECSAPLTVREPPSFVQKPDPMDVLTGSNVTFTSIVKGSPPFTVSWFKGSTELVPGARCNVSLQDSVGELELFDVDTSQSGEYTCIVSNEAGRASCTTRLFVKAPAIFVKRLNDYSIEKGKPLILEGTFSGTPPISVTWKKNGINVIASQRCNITTTEKSAILEILSSTVEDSGQYNCYIENASGKDSCSAQILILEPPYFVKQLEPVKVTVGDSASLQCQLAGTPEIGVSWYKGDTKLRPTATCKMHFKNNVATLVFTQVDSSDSGEYICRAENSVGEVSSSTFLTVQEQKLPPSFSRQLRDVQETVGLPVVFECAVSGSEPISVSWYKDGKPLKDSPNIQTSFLDNIATLNIFKTDRSLSGQYSCTATNPIGSASSGAKLILTEGKNPPFFDIPLAPMDAVVGESADLECHVTGTQPIKVTWAKDNREIRSGGNYQISYLENSAHLTIVKVDKGDSGQYTCYAVNEVGKDSCTAQLNIKERLIPPSFTKKLSETVEETEGNSFKLEGRVAGSQPITVAWYKNNVEIHPTSNCEIMFKNNALLLQVKRASMADAGLYTCKATNDAGSALCTSSIVIKEPKKPPVFDQHLAPVTASEGDSVQLSCHVQGSEPIRIQWLKAGREVKPSDRCSFSFASGTAMLELKETAKADSGDYVCKASNVAGSDTSKCKVTIKEKPAAAPAAKKAAVDGKLFFVSEPQSIRVVEKTTATFIAKVGGDPIPNVKWTKGKWRQLNQGGRILIHQKGDEAKLEIRDTTKTDSGLYRCVAFNKHGEIESNVNLQVDERKKQEKIEGDLRAMLKKTPALKKGSGEEEEIDIMELLKNVDPKEYEKYARMYGITDFRGLLQAFELLKQSQEEETHRLEIEELEKSERDEKEFEELVAFIQQRLTQTEPVTLIKDIENQTVLKDNDAIFEIDIKINYPEIKLSWYKGTEKLEPSNKYEISIDGDRHTLRVKNCQPKDQGNYRLVCGPHIASAKLTVIEPAWERHLQDVTLKEGQTCTMTCQFSVPNVKSEWFRNGRVLKPQGRVKTEVEHKVHKLTIADVRAEDQGQYTCKHEDLETSAELRIEAEPIQFTKRIQNIVVSEHQSATFECEVSFDDAIVTWYKGPTELTESQKYNFRNDGRCHYMTIHNVTPDDEGVYSVIARLEPRGEARSTAELYLTTKEIKLEMKPPDIPDSRVPIPTMPIRAVPPEEIPPAVAPSIPLLLPLPEEKKPPAKRIEVTKKGVKKDTKKVVTKPKEEAPPPPVAKKPPPPTPMIPAKASEIIDVSSKAEEVKITTITRKKEVHKEKEAVYEREEAVYEKKVHIEPWEEPYEELETEPYTEPYEEPYYEEPDEDYEEIKVEAKKQVHEEWEEDFEEGQEYYEREEGYDEGEEEWEEIYHEREIIQVQKEVHEELHEKKIPAKVPEKKVPPPKVVKKPVVEKVEKTTRRMEEEKVQVIKVPEVSKKIVPQKPSRTPVQEEIIEVKVPAVHTKKMVISEEKMFFASHTEEEVSVSVPEVQKKTVTEEKIHVAVSKKIEPPPKVPEPPKKPVPEEVVPVPIPKKVEPPAAKVPEAPKKPVPEEKKPVPIPKKKEPAAPPQVPEAPKKPAPEEKIPVPVTKKKEAPPAKVPEVQKKVVTEEKIAIITQREESPPPAVPEIPKKKVPEEKRPVPRKEEVPPPKVPVPPKKAVPEAVVPAPIPKKAPPRAEVSKKTVVEEKRFAAEEKLSVAVPQRVELMRHEEEEWTYSEEEERVSVSVYREEERDEEEAEITEYEVLEEPEEYVVEEKMHFISKKVEVEPAKVPEKKIIPKPKVPAKIEEPPPTKVPEPPKKIVPEKKVPAPAPKKVPPAKAPEESKRPVPEKRAPAEEVGIEEPPPTKVAERHMKITQEEKVLVAVTKKEAPPRARVPEEPKKVAPEERFPKLKPRREEEPPAKVTEVRKRAVKEEKVSIEVPKREPRPTKEVTVTEEKKWSYTREEETVSEHREEEYEDYEDYEEYKEFEEYEPTEEYDQYDEYAEREVEHYEEHEEYVTEPKKPVPVKPAQEPVPAKPKAPPPKVLKKAVPEEKAPLPIQKKLKPLPPKAPEEPKKVVEEKIQISITKREKQQVTEPVAKVPMKPKRVVPEAKIPAPTKEVAVPVRVPGVPKKRELEEVVVFKEEVEAHEEYIVEEEEEYVHEEEYVHKEEYVHEEEYVHKEEYIHEEEEHLHEEEETIAEEEVVPVAPVKVPVVPKKPVPEEKKPVPVPKKKEAPPAKVPEIPKKPEEKVPVPIPKKEKAPPAKVPEVPKKPVPEEKPPVPVPKKVEPPPAKVPEVPKKPVPEKKVPAPTPKKVEAPPAKVPEVPKKPIPEEKKPTALLKKMEAPPPKAPKKREVVPVPVALPREEEEEEVPFEEVPEEEILPEEEVPSEEEAPPEEVPPEEEEVLPEEEEVLPEEEEVLPEEEEVQPEEEALPEIKPKVPKPAPVPKKTVPEKKVPVPVPKKVEPPPPPKVPEIKKKVPEKKVVVPKKEEAPPTKVPEVSKKVEERRIIPPKEEEVPPAEVYEEAEEPTPEEIPEEPPSIEEEEIVEEEEEEEEVLPPRAPEVVKKAVPEAPTPVPKKAEAPPAKVPKKIPEEKVPVPVQKKEAPPAKVPEKKKIPEKKVPVPKKEAVPPAKGKAVFEEKISVAYQQEELVQERIELELVEAKVEEAFEEEEFHEVQEYFEEEEFHEVEEFIRVEERRFQEEHKVEEVHRVIEFLEAEEVEVYEKPKIPPKKGPEVSEKVIPPKKPPTKVIPRKEPPAKVPEVTKKTVVEEKIRAPEEPKVPAPKAPEVPKKITPEEKVREAVPKKPEVPPPKVPEVPKKIIQEEKLPVVLPEDTEIYMYEASEETVIEEEHVTLPQKARLKVAKVPAPPQTVVTEEKTYVTIRKTRETLALKESETTREAFPELKSYKAVPEIPEPPSPEDLEIIEDVLPEKRPPASKRRKTQLPTAPEAPREMPPEMNTFEEISVEPEMLPTQVLDTYQEATVEKKTLRISRKKPELPSDEEVPEAPREVVAKKKVLPPQVPEVVPVKVPGAPKEVVSERKSLEEPPKKPAVRPVTVPEEPKEVIPEKKVSLVPPKKPAAPPVTVPEAPEEVFSEDEETLAPPQEPEAPPAKVPEAPKEVVPEKKVSVVPPKKPEAPPAKVPEAPKEAAPEKKVPVAPKKKPEAPPVKVPEAPKKVVPEKKLPVAAPKKPEAPAAEVPEVPKTAVPQKKIPEAIPPKPESPPLEVPEVPPKEVTPEKKVPAAPPTKPEIPPPKVPEAPQAAVVEEKTPEALPKKAEAAPVPVPQVQETVPEKTRPVGPPKKPEATTVPVPKVQKTIPEKTRPEAPPKRPEARTVPETVPEKTRPMAPPKKPEATTLPVPEVQETVPEKTRPVGPPKKPEATTVPVPEVQETIPEKTRPPKKPEATPVPVPEVQETVPEKTRPVGPPKKPEATTVSVPEVQETIPEKTRPAAPPKKPEATAVPETIPEKTRPEAPPKRPEATTVPVPEADQAVVPEKKVPRVPPKKVEAPPITVPEEPKEVIPEKKVSLVPPKKPAAPPVTVPEAPEEVFSEDEETLAPPQEPEAPPAKVPEAPKEVVPEKKVSVVPPKKPEAPPAKVPEAPKEAAPEKKVPVAPKKKPEAPPVKVPEAPKKVVPEKKLPVAAPKKPEAPAAEVPEVPKAAVPQKKIPEAIPPKPESPPPEVYEEPEEEIVPEEPPEEAVEEPVPAPPPKVTEPPKKPVPEKKAPPAVVKKPEPPPAKVPEVPKEAPPEKKVPPKKPEAPPAKVPEVPKEVVTEKKVAVPKKPEVPPAKVPEVPKKPVIEEKPAIPVVEKVASPPAEVYEEPEEVTAEEEEPAPAVEEEEYEAPPPPAPVPEEPKKVVPEKKFPVIKKPEAPPPKVPEVPKKAVPVKKVPVVKKPEPPEAEVPEVPKKLVPVKKEPVPVTKKTEVLPEKVPEAPKKITPEKKESVPVPEEPEAPPASVEETPEETIYEEKATITIGRKETPPVEEREIEKFIQPEEPELEPEPEEIPVQEPEPEKKVIEKPKLKPRPPARPPSPPKEDVKEKMFQLKAVSKKKVPEKPEVVEKVEPAPLKVPTAEKKVRKLLPEPKPQPKEEVVLKSVLRKKPEEEEPKVEPKKVEKAKKPEEPQPPPKAVEVEAPPEPTPKERKVPEPAKVPEIKPAIPLPGPEPKPKPEPEVKTMKAPPIEPAPTPIAAPVTAPVVGKKAEAKPKDEAAKPKGPIKGVAKKTPSPIEAERKKLRPGSGGEKPPDEAPFTYQLKAVPLKFVKEIKDIVLTEAESVGSSAIFECLVSPSTAITTWMKDGSNIRESPKHRFIADGKDRKLHIIDVQLSDAGEYTCVLRLGNKEKTSTAKLIVEELPVRFVKTLEEEVTVVKGQPLYLSCELNKERDVVWRKDGKIVVEKPGRIVPGVIGLMRALTINDADDTDAGTYTVTVENANNLECSSCVKVVEIIREWLVKPIRDQHVKPKGTAVFTCDIAKDTPNIKWFKGYDEIPLEPNDKTEILKEGNHLFLKVKNAMPEDIDEYAVEIEGKRYPAKLTLGEREVELLKPIEDVTIYEKESASFDAEISEEDIPGEWKLKGELLRPSPTCEIKAEGGKRFLTLHKVKLDQAGEVLYQACNAITTAILTVKEIELDFAVPLKDVTVPEKRQARFECVLTREANVIWSKGPDIIKASDKFDIIADGKKHILVINDSQFDDEGVYTAEVEGKKTSAQLFVTGIRLKFISPLEDQTVKEGQTATFVCELSHEKMHVVWFKNDVKLHTTRTVLMSSEGKTYKLEIRETTLDDISQIKAQVKNLSSTANLKVLEADPYFTVKLHDKTGVEKDEIILKCEVSKDVPVKWFKDGEEIVPSPKHSVKTDGLRRILKIKKAELKDKGEYVCDCGTDTTKANVTVEARLIKVEKPLYGVEVFVGETARFEIELSEPDVHGQWKLKGEPLTASPDCEIIEDGKKHVLVLYNCQLDMTGEISFQAANAKSAANLKVKELPLIFITPLSDVKVFEKDEAKFECEVSREPKTFRWLKGTQEITGDDRFELIKDGTRHSLVIKSAAFEDEAKYMFEAEDKRTSGKLIIEGIRLKFLTPLKDVTAKERENAVFTVELSHDNIPVSWFKNDQRLHTSKRVSMHDEGKTHSITFKDLSIDDTSQIRVEAMGISSEAKLTVLEGDPYFTGKLQDYTGVEKDEVILQCEISKADAPVKWFKDGKEIKPSKNVVIKADGKKRMLILKKALKSDIGQYTCDCGTDQTSGKLDIEDREIKLVRPLYSVEVMETETARFETEISEDDIHANWKLKGEALLQTPECEIKEEGKIHVLILHNCRLDQTGGVDFQAANVKSSAHLRVKPRVIGLLRPLKDVTVTAGETATFDCELSYEDIPVEWYLKGKKLEPNDKVVTRSEGRVHTLTLRDVKLEDAGEVQLTAKDFKTQANLFVKEPPVEFTKPLEDQTVEEEATAVLECEVSRENAKVKWFKNGTEILKSKKYEIVADGRVRKLIIHGCTPEDIKTYTCDAKDFKTSCNLNVVPPHVEFLRPLTDLQVKEKETARFECEISKENEKVQWFKDGAEIKKGKKYDIISKGAVRILVINKCLLNDEAEYSCEVRTARTSGMLTVLEEEAVFTKNLANLEVSEGDTIKLVCEVSKPGAEVIWYKGDEEIIETGRFEILTDGRKRILIIQNAQLEDAGSYNCRLPSSRTDSKVKVHELAAEFISKPQNLEILEGEKAEFVCTISKESFEVQWKRDDQTLESGDKYDIIADGKKRVLVVKDATLQDMGTYVVMVGAARAAAHLTVIEKLRIIVPLKDTKVKEQQEVVFNCEVNTEGAKAKWFRNEEAIFDSSKYIILQKDLVYTLRIRDARLDDQANFNVSLTNHRGENVKSAANLIVEEEDLRIVEPLKDIETMEKKSVTFWCKVNRLNVTLKWTKNGEEVAFDNRISYRIDKYKHSLIIKDCGFPDEGEYVVTAGQDKSVAELLIIEAPTEFVEHLEDQTVTEFDDAVFSCQLSREKANVKWYRNGREIKEGKKYKFEKDGSIHRLIIKDCRLEDECEYACGVEDRKSRARLFVEEIPVEIIRPPQDILEAPGADVIFLAELNKDKVEVQWLRNNMIVVQGDKHQMMSEGKIHRLQICDIKPRDQGEYRFIAKDKEARAKLELAAAPKIKTADQDLVVDAGQPLTMVVPYDAYPKAEAEWFKENEPLSTKTVDTTAEQTSFRISEAKKDDKGRYKIVLQNKHGKAEGFINLQVIDVPGPVRNLEVTETFDGEVSLAWEEPLTDGGSKIIGYVVERRDIKRKTWVLVTDRADSCEFTVTGLQKGGVEYLFRVSARNRVGTGEPVETDSPVEARSKYDVPGPPLNVTITDVNRFGVSLTWEPPEYDGGAEITNYVIELRDKTSIRWDTAMTVRAEDLSATVTDVVEGQEYSFRVRAQNRIGVGKPSAATPFVKVADPIERPSPPVNLNASEQTQSSVQLTWEPPLKDGGSPILGYIIERREEGKDNWIRCNMKPVPELTYKVTGLQKGNKYLYRVSAENAAGVSDPSEILGPLTADDAFVEPTMDLSAFKDGLEVIVPNPIKILVPSTGYPRPKATWTFGDQVLEEGDRVKMKTISAYAELVISPSERTDKGIYTLTLENPVKSISGEINVNVIAPPSAPKELKFSDITKDSVHLTWEPPDDDGGSPLTGYVVEKRDMSRKTWTKVMDFVTDLEFTVPDLVQGKEYLFKVCARNKCGPGEPAYTDEPVNMSAPATVPDPPENVKWRDRTANSIFLTWDPPKNDGGSRIKGYIVEKCPRGSDKWVACGEPVPDTKMEVTGLEEGKWYAYRVKALNRQGASKPSKPTEEIQAVDTQEAPEIFLDVKLLAGITVKAGTKIELPATVTGKPEPKITWTKADTLLKPDQRITIENVPKKSTVTITDSKRSDTGTYIIEAVNVCGRATAVVEVNVLDKPGPPAAFDITDVTNESCLLTWNPPRDDGGSKITNYVVERKATDSDVWHKLSSTVKDTNFKATKLTPNKEYIFRVAAENMYGVGEPVQAAPIIAKYQFDPPGPPTRLEPSDITKDAVTLTWCEPDDDGGSPITGYWVERLDPDTDKWVRCNKMPVKDTTYRVKGLTNKKKYRFRVLAENLAGPGKPSRSTEPILIKDPIDPPWPPGKPTVKDIGKTSLVLNWTKPEHDGGAKIESYVIEMLKTGTDEWVRVAEGVPTTEHLLTGLMEGQEYSFRVRAVNKAGESEPSEPSDPVLCREKLYPPSPPRWLEVINITKNTADLKWTVPEKDGGSPITNYIVEKRDVRRKGWQTVDTTVKDTKCTVTPLTEGSLYVFRVAAENAIGQSDYTEIGDSVLAKDTFTTPGPPYALTVVDVTKRHVDLKWEPPKNDGGRPIQRYIIEKKEKLGTRWVKAGKTSGPDCNFRVTDVIEGTEVQFQVRAENEAGVGHPSEPTEILSIEDPTSPPSPPLDLHVTDAGRKHIAIAWKPPEKNGGSPIIGYHVEMCPVGTEKWMRVNSRPIKDLKFKVEEGIVPDKEYVLRVRAVNAVGVSEPSEISENVVAKDPDCKPTIDLETHDIVVIEGEKLNIPVPFRAVPVPTVSWHKDGKEVKASDRLTMKNDHISAHLEVPKSVHADAGVYTITLENKLGSATASINVKVIGLPGPCKDIKASDITKSSCKLTWEPPEFDGGSPILHYVLERREAGRRTYIPVMSGENKLSWTVKDLIPNGEYFFRVKAVNKIGGGEYIELKNPVIAQDPKQPPDPPVDVEVHNPTAKAMTITWKPPLYDGGSKIMGYIIEKITKGEDRWKRCNEHLVPVLTYTAKGLEEGKEYQFRVRAENAAGIGEPSRATPPTKAVDPIDAPKVILRTSLEVKRGDEIALDATISGSPYPTITWIKDENVIVPEEIKKRAAPPVRRKKGEAEEEEPFSLPLTERLSINNSKQGESQLRIRDSLRPDHGQYMIKVENDHGVAKAPCSVSVLDTPGPPINFVFEDIRKDSVLCKWEPPLDDGGSEIINYTLEKKDKTKPDSDWIVITSTLRNCKYSVTKLIEGKEYLFRVRAENRFGPGPPCVSKPLLAKDPFEPPDAPDKPIVEDVTSNSMLVKWNEPKDNGSPILGYWLEKREVNSTHWSRVNKTLLSSLKTKVDGLLEGLTYVFRVCAENAAGPGKFSPPSDPKTARDPISPPGPPVPRVADTSSTTIELEWEPPAFNGGGEIMGYFVDKQLVGTNEWSRCTEKMIKVRQFTVKEIREGADYKLRVSAVNAAGEGPPGETEPVTVAEPQEPPTVELDVSVKGGIQIMAGKTLRIPAEVTGRPVPTKVWTIEEGELDKERVIIENVGTKSELIIKNALRKDHGRYVITATNSCGSKFAAVRVEVFDVPGPVLDLKPVVTNRKMCLLNWSDPADDGGSDITGFIIERKDAKMHTWRQPIETERSKCDITGLIEGQEYKFRVIAKNKFGCGPPVEIGPILAVDPLGPPTSPERLTYTERTKSTITLDWKEPRSDGGSPIQGYIIEKRRHDKPDFERVNKRLCPTTSFLVENLDEHQMYEFRVKAVNDVGESEPSLPLNVVIQDDEVPPTIKLRLAVRGDTIKVKAGEPVNIPADVTGLPMPKIEWSKNEKVIDKPTDTLNITKEEVSRSEAKTELSIPKAAREDKGTYTITASNRLGSVFRNVHVEVYDRPSPPRNLAVTDIKAESCYLTWDAPLDNGGSEITHYIIDKRDASRKKSEWEEVTNTAVERRYGIWKLIPNGQYEFRVRAVNKYGISDECKSDKVVIQDPYRLPGPPGKPKVLERTKGSMLVSWTPPLDNGGSPITGYWLEKREEGGTYWSRVSRAPITKVGLKGVEFNVPRLIEGVKYQFRAMAINAAGIGPPSEPSDPAVAGDPIYPPGPPSCPEVKDKTKSSISLAWKPPAKDGGSPIKGYIVEMQEEGTTDWKPVNEPDKLLTACECVVPNLKELRKYRFRVKAVNEAGESEPSDTTGEIPATDIQEVPEVFIDIGAQDCLVCKAGSQVKIPAVIKGRPTPKSSWEFDGKAKKAMKDGVHDIPEDAQLETAENSSVIIIPECTRAHSGKYSITAKNKAGQKTANCRVKVMDAPGPPKDLKVSDITRGSCRLSWKMPDDDGGDRIKGYVIEKKTIDGKAWTKVNPNCGSTTFVVPDLISEQQYFFRVRAENRFGIGPPAETIQRTTARDPIYPPDPPIKLKIGLITKNTVHLSWKPPKNDGGSPVTHYIVECLAWDPTGKKKEAWRQCNRRDVEELEFTVEDLIEGGEYEFRVKAVNEAGVSKPSATVGPVIVKDQTCPPAIELKEFMEVEEGTDVNIVAKIKGVPFPTLTWFKAPPKKPDSKEPVVYDTHVNKQVVDDTCTLVIPQSRRSDTGLYSITAVNNLGTASKEMRLNVLGRPGPPVGPIKFESISADQMTLSWLPPKDDGGSKITNYVIEKREANRKTWVRVSSEPKECMYTIPKLLEGHEYVFRIMAQNKYGIGEPLDSEPETARNLFSVPGAPDKPTVSSVTRNSMTVNWEEPEYDGGSPVTGYWLEMKDTTSKRWKRVNRDPIKAMTLGVSYKVTGLIEGSDYQFRVYAINAAGVGPASLPSDPVTARDPVAPPGPPFPKVTDWTKSSVDLEWSPPLKDGGSKITGYIVEYKEEGKEEWEKGKDKEVRGTKLVVTGLKEGAFYKFRVRAVNVAGVGEPGEVTDVIEMKDRIVSPDLQLDASVRDRIVVHAGGVIRIIAYVSGKPPPTVTWSMNERALPQEAAIETTAISSSMVIKNCQRSHQGVYSLLAKNEGGERKKTIIVDVLDVPGPVGIPFLSDNLTNDSCKLTWFSPEDDGGSPITNYVIQKREADRRAWTPVTYTVTRQNATVQGLIQGKSYFFRIAAENSIGMGPFVETPNALVIRDPITVPERPEDLEVKEVTKNTVSLTWNPPKYDGGSEIINYVLESRLIGTEKFHKVTNDNLLSRKYTVKGLKEGDTYEYRVSAVNIVGQGKPSFCTKPITCKDELAPPTLDLDFRDKLTVRVGESFALTGRYSGKPKPKIDWFKDEADVLEDDRTHIKTTPTTLALEKTKAKRSDSGKYCVVVENSTGSRKGFCQVNVVDRPGPPVGPVIFDEVTKEYMVISWKPPLDDGGSEITNYIIEKKELGKDIWMPVTSASAKTTCKVPKLLEGKDYIFRIHAENLYGISDPLVSDSMKAKDRFRVPDAPEQPVVTEVTKDSALVTWNKPNDGGKPITNYILEKRETMSKRWVRVTKEPIHPYTKYRVPDLLEGCQYEFRVSAENEIGIGDPSPPSKPVFARDPIAKPSPPINPEAIDTTCNSVELTWQPPRHDGGSKILGYIVEYQKVGDEEWRRANHTPESCPETKYKVTGLRDGQSYKFRVLAVNEAGESDPAHVPEPVLVKDRLEPPELILDANMAREQHIRVGDTLRLSAIIKGVPFPKVTWKKEDREAPTKAQIDVTPVGSKLEIRNAAHEDGGIYSLTVENPAGTKTVSVKVLVLDKPGPPRDLEVSEIRKDSCYLTWKEPLDDGGSVVTNYVVERKDVATAQWSPLSTTSKKKSHMAKHLTEGNQYLFRVAAENQYGRGPFVETPKPIKALDPLHPPGPPKDLHHVDVDKTEVSLVWNKPDRDGGSPITGYLVEYQEEGDKDWIKFKTVKNLDCVVTGLQQGKTYRFRVKAENIIGLGLPDTTIPIECQEKLVPPSVELDVKLIEGLVVKAGTTVRFPAIIRGVPVPTAKWTTDGTEIKTDDHYTVETDSFSSVLTIKNCLRKDTGEYQLTVSNAAGTKTVAVHLTVLDVPGPPTGPINILDVTPEYMTISWQPPKDDGGSPVINYIVEKQDTRKGTWGVVSAGSSKLKLKVPHLQKGCEYVFRVKAENKMGVGPPLDSIPTVAKHKFSPPSPPGKPVVTDITENAATVSWTLPKSDGGSPITGYYVERREITGKWVRVNKTPIADLKFRVTGLYEGNTYEFRVFAENLAGLSNPSPSSDPIKACRPIKPPGPPINPKLKDKSKESADLVWTKPLSDGGSPILGYVVEYQKPGTAQWDRINKDELIRQCAFRVPGLIEGNEYRFRIRAANIVGEGEPRELAESVIAKDILHPPEVELDVTCRDVITVRVGQTIRILARVKGRPEPDITWSKEGKVLVKDKRVDLIHDLPRVELQIKEAVRADHGKYIISAKNSSGHAQGSAIVNVLDRPGPCQNLKVSNVTKENCTISWENPLDNGGSEITNFIVEYRKPNQKGWSIVASDVTKRLVKANLLANNEYYFRVCAENKVGVGPTIETKTPILAINPIDRPGEPENLHIADKGKTFVYLKWRRPDYDGGSPNLSYHVERRLKGSADWERVHKGSIKETHYMVDKCVENQIYEFRVQTKNEGGESDWVRTEEVVVKEDLQKPVLDLKLSGVLTVKAGDTIRLEAGVRGKPFPEVAWTKDKDATDLTRSPRVKIDTSAESSKFSLTKAKRSDGGKYVITATNPAGSFVAYATVNVLDKPGPVRNLKITDVSSDRCTIRWDPPEDDGGCEIQNYILEKCESKRMVWSTYSANVLTPSATVTRLIEGNEYIFRVRAENKIGTGPPTESKPVIAKTKYDRPGRPDPPEVTKVSKEEMTVVWNAPEYDGGKSITGYYLEKKEKHAVRWVPVNKSAIPERRLKVQNLLPGHEYQFRVKAENEVGIGEPSLPSRPVVAKDPIEPPGPPTNFKVVDTTKSSITLAWGKPVYDGGAPIIGYVVEMRPKIADASPDEGWKRCNAAAQLIRMEFTVTSLDENQEYEFRVCAQNQVGIGRPAELKEAIKPKEILEPPEIDLDASMRKLVVVRAGCPIRLFAIVRGRPAPKVTWRKVGIDNVVRKGQVDLVDTMAFLVIPNSTRDDSGKYSLTLVNPAGEKAVFVNVKVLDTPGPVADLKVSDVTKTSCHVSWAPPENDGGSQVTHYIVEKREAERKTWSTVTPEVKKTSFNVTNLVPGNEYFFRVTAVNEYGPGVPTDIPKPVLASDPLSEPDPPRKLEVTEMTKNSATLAWLPPLRDGGAKIDGYIISYREEDQPADRWTEYSVVKDLSLIVTGLKEGKKYKFRVAARNAVGVSMPREAEGVYEAKEQLLPPKILMPEQITIKAGKKLRVEAHVYGKPNPICKWKKGDDEVVTSSHLAIHKADGSSVLIIKDVTRKDSGYYSLTAENSSGSDTQKIKVTVMDAPGPPQPPFDISEIDADACSLSWHIPLEDGGSNITNYIVEKCDVSRGDWVTALASVTKTSCRVGKLIPGQEYIFRVRAENRFGISEPLTSPKMLAKFPFDVPSEPKNARVTKVNKDCIFVAWDRPDSDGGSPITGYLIERKERNSLLWVKANDTIVRSTEYPCAGLVEGLEYSFRIYALNKAGSSPPSKPTEYVTARMPVDPPGKPEVVDVTKNSASLIWARPKHDGGSRIIGYFVEACKLPGDKWVRCNTTPHQIPQEEYTATGLEENAQYQFRAIAKTAVNISQPSEPSDPVTILAENVPPRIELSVEMKSLLTVKAGTNVCLDATVFGKPMPTVSWKKDTTPIKQAEGIKMAMKRNLCTLELFSVNRKDSGDYTITAENSSGSKSATIKLKVLDKPGPPASVKINKMYADRAMLSWEPPLEDGGSEITNYIIDKRETSRPNWAQVSATVPITSCTVEKLIEGHEYQFRICAENKYGVGDPILTEPAIAKNPYDPPGRCDPPVISNITKDHMTVSWKAPADDGGSPITGYLVEKRETQAVNWTKVNRKPVIERTLKATGLQEGTEYEFRVTAINKAGPGKPSDASKAVYAQDPLYPPGPPAFPKVYDTTRSSVSLSWGKPAYDGGSPIIGYLVEVKRADSDHWVRCNLPEKLQKTRFEVTGLMENTEYQFRVYAVNKIGYSDPSDVPDKHCPKDILIPPEGELDAELRKTLILRAGVTMRLYVPVKGRPPPKITWSKPNVNLRERIGLDIKSTDFDTFLRCENVNKYDAGKYILTLENSCGKKEYTIVVKVLDTPGPPVNVTVKEVSKDSAYVTWDPPIIDGGSPIINYVVEKRDAERKSWSTVTTECSKTSFRVSNLEEGKSYFFRVFAENEYGIGDPGETRDAVKASETPGPVVDLKALAITKSSCTIGWKKPRSDGGSRITGYVVDFLTEENKWQRVMKSLSLQYSTKDLKEGKEYTFRVSAENENGEGTPSEIVVVAKDDVVAPDLDLKDLPDLCYLAKENSNFRLKIPIKGKPAPSVSWKKGEDPLATDTRVSVESTAVNTTLVVYDCQKSDAGKYTITLKNVAGTKEGTLSIKVVGKPGIPTGPIKFDEVTAEAMTLKWGPPKDDGGSEITNYVLEKRDSVNNKWVTCASAVQKTTFRVTRLHEGIEYTFRVSAENKYGVGEGLKSEPIVAKHPFDVPDAPPPPNIVDVRHDSVSLTWTDPKKTGGSPITGYHIEFKERNSLLWKRANKTPIRMKDFKVTGLTEGLEYEFRVMAINLAGVGKPSLPSEPVVALDPIDPPGKPEVISVTRNSVTLIWTEPKYDGGHKLTGYIVEKRDLPSKSWMKANHVNVPDCAFTVTDLVEGGKYEFRIRAKNTAGAISAPSESTGTIICKDEYEAPTIVLDPTIKDGLTVKAGDSIVLSAISILGKPLPKSSWSRAGKDIRPSDIAQITSTPTSSMLTVKYATRKDAGEYTITATNPFGTKEEHVKVSVLDVPGPPGPIEISNVSAEKATLTWTPPLEDGGSPIKAYVLEKRETSRLLWTVVSEDIQACRHVVTKLIQGNEYLFRVSAVNHYGKGEPVQSEPVKMVDRFGPPGPPGKPEISNVTKNTATVSWKRPTDDGGSEITGYHVERREKKGLRWVRATKTPVSDLRCKVTGLQEGNTYEFRVSAENRAGIGPPSDASNPVLMKDVAYPPGPPSNAHVTDTTKKSASLAWGKPHYDGGLEITGYVVEHQKVGDDAWIKDTTGTALRITQFVVPDLQTKEKYNFRISAINDAGVGEPAVIPNVEIVEKEVAPDFELDAELRRTLVVRAGLSIRIFVPIKGRPAPEVTWTKDNINLKHRANIENTESFTLLIIPECNRYDTGKFVMTIENPAGKKSGFVNVRVLDTPGPVLNLRPTDITKDSVTLHWDLPLIDGGSRITNYIVEKREATRKSYSTVTTKCHKCTYKVTGLTEGCEYFFRVMAENEYGVGEPTETTEPVRASEAPLPPDSLNIMDITKNTVSLAWPKPRHDGGSKITGYVIEAQRKGSDQWTHISTVKGLECVVRNLTEGEEYTFQVMAVNSAGRSAPRESRPVIVKEQTMLPELDLRGIYQKLVIARAGDNIKVEIPVLGRPKPTVTWKKGDQILKQTQRVNVENTATSTILNINECVRSDSGPYPLTAKNTVGEVGDVITIQVHDIPGPPTGPIKFDEVSSDFVTFSWEPPENDGGVPISNYVVEMRQTDSTTWVELATTVIRTTYKATRLTTGVEYQFRVRAQNRYGVGPGITSASVVANYPFKVPGPPGTPQVTAVTKDSMTISWHEPLSDGGSPILGYHIERKERNGILWQTVSKALVPGNIFKSTGLTDGIAYEFRVIAENMAGKSKPSKPSEPMFALDPIDPPGKPVPLNITRHTVALKWAKPEYTGGFKITSYVVEKRDLPNGRWLKANFSNILENEFTVSGLTEDAAYEFRVIAKNAAGAISPPSEPSDAITCRDDLEAPRIMVDVRFKDTITLKAGEAFKLEADVSGRPPPTMEWTKDGKELEGTGKLEIKIADFSTHLINKDSSRTDSGAYILTATNPGGFAKHIFNVKVLDRPGPPEGPLAVSDVTSEKCVLSWLPPLDDGGAKIDHYIVQKRETSRLAWTNVATEVQVTKLKVTKLLKGNEYIFRVMAVNKYGVGEPLESEPVLAVDPYGPPDPPKNPEVTTITKDSMVVCWGHPDSDGGSEIINYIVERRDKAGQRWVKCNKKALTDLRFKVSGLTEGHEYEFRIMAENAAGISAPSATSPFYKACDTVFKPGPPGNPRVLDTSRSSISIAWNKPIYDGGSEITGYMVEIALPEEDEWQVVTPPAGLKATSYTITSLIENQEYKIRIYAMNSEGLGEPALVPGTPKAEERMLPPEIELDADLRKVVTIRACCTLRLFVPIKGRPAPEVKWAREHGESLDKASIESTSSYTLLVVGNVNRFDSGKYILTVENSSGSKSAFVNVRVLDTPGPPQNLKIKEVTKTSVTLTWEPPLLDGGSKIKNYIVEKRESTRKAYSTVATNCHKTSWKVDQLQEGCSYYFRVLAENEYGIGLPAETAESVKASERPLPPGKITLTDVTRNSVSLSWEKPEHDGGSRILGYIVEMQSKGSDRWATCATVKVTEATITGLIQGEEYSFRVSAQNEKGISDPRQLSVPVIAKDLVIPPAFKLLFNTFTVLAGEDLKIDVPFIGRPPPAVTWHKDDIPLKQTTRVNAESTENNSLLTIKEACREDVGHYTVKLTNSAGEATETLNVIVLDKPGPPTGPVKMDEVTADSVTLSWEPPKYDGGSSINNYIVEKRDTSTTAWQIVSATVARTTIKACRLKTGCEYQFRIAAENRYGKSTYLNSEPVVAQYPFKVPGPPGTPFVTLASKDSMEVQWHEPVSDGGSKVIGYHLERKERNSILWVKLNKTPIPQTKFKTTGLEEGIEYEFRVSAENIVGIGKPSKPSECYAAHDPCDPPGRPEAIIVTRNSVTLQWKKPTYDGGSKITGYIVEKKELPDGRWMKASFTNIIDTQFEVTGLLEDHRYEFRVIARNAAGVFSEPSESTGAITARDEVEPPRISMDPKYRDTVVVQAGESFKIDADIYGKPIPTTQWVKGDQELSSTARLEIKSTDFATSLSVKDAVRVDSGNYILKAKNVAGEKSVTINVKVLDRPGPPEGPVAISGVTAEKCTLAWKPPLQDGGSDITNYIVERRETSRLVWTLVDANVQTLSCKVLKLLEGNEYIFRIMAVNKYGVGEPLESESLIAKNPFVVPDAPKAPEVTAVTKDSMIVVWERPASDGGSEILGYVLEKRDKEGIRWTRCHKRLIGELRLRVTGLLENHNYEFRVSAENAAGLSEPSPPSAYQKACDPIYKPGPPNNPKVMDVTRSSVFLSWTKPIYDGGCEIQGYIVEKCDVSVGEWTMCTPPTGINKTNLEVEKLLEKHEYNFRICAINKAGVGEHADVPGPVMVEEKLEAPDIDLDLELRKVINIRAGGSLRLFVPIKGRPTPEVKWGKVDGDIRDAAIIDVTSSFTSLVLDNVNRYDSGKYTLTLENSSGTKSAFVTVRVLDTPSPPVNLKVTEITKDSVSITWEPPLLDGGSKIKNYIVEKREATRKSYAAVVTNCHKNSWKIDQLQEGCSYYFRVTAENEYGIGLPARTADPIKVAEVPQPPGKITVDDVTRNSVSLSWTKPEHDGGSKIIQYIVEMQAKNTDKWSECARVKSLDAVITNLTQGEEYLFRVIAVNEKGRSDPRSLAVPIIAKDLVIEPDVRPAFSSYSVQVGQDLKIEVPISGRPKPSISWTKDGMPLKQTTRINVTDSLDLTTLSIKETHKDDGGQYGITVSNVVGQKTAAIEIITLDKPDPPKGPVKFDEISAESITLSWNPPLYTGGCQITNYIVQKRDTTTTVWDVVSATVARTTLKVTKLKTGTEYQFRIFAENRYGQSFALESEPVVAQYPYKEPGPPGTPFVTAISKESMVVQWHEPINNGGSPVIGYHLERKERNSILWTKVNKTIIHDTQFKALNLEEGIEYEFRVYAENIVGVGKASKNSECYVARDPCDPPGTPEAIIVKRNEITLQWTKPVYDGGSMITGYIVEKRDLPEGRWMKASFTNVIETQFTVSGLTEDQRYEFRVIAKNAAGAISKPSDSTGPITAKDEVELPRISMDPKFRDTIVVNAGETFRLEADVHGKPLPTIEWLRGDKEIEESARCEIKNTDFKALLIVKDAIRIDGGQYILRASNVAGSKSFPVNVKVLDRPGPPEGPVQVTGVTAEKCTLAWSPPLQDGGSDISHYVVEKRETSRLAWTVVASEVVTNSLKVTKLLEGNKYIFRIMAVNKYGVGEPLESAPVLMKNPFVLPGPPKSLEVTNIAKDSMTVCWNRPDSDGGSEIIGYIVEKRDRSGIRWIKCNKRRITDLRLRVTGLTEDHEYEFRVSAENAAGVGEPSPATVYYKACDPVFKPGPPTNAHVVDTTKNSITLAWSKPIYDGGSEILGYVVEICKADEEEWQIVTPQTGLRVTRFEIAKLIEHQEYKIRVCALNKVGLGEAASVPGTVKPEDKLEAPELDLDSELRKGIVVRAGGSARIHIPFKGRPTPEITWSKEEGEFTDKVQIEKGINFTQLSIDNCDRNDAGKYILKLENSSGSKSAFVTVKVLDTPGPPQNLAVKEVRKDSVLLVWEPPIIDGGAKVKNYVIDKRESTRKAYANVSSKCNKTSFRVENLTEGAIYYFRVMAENEFGVGVPTETSDAVKASEPPSPPGKVTLTDVSQTSASLMWEKPEHDGGSRILGYVVEMQPKGTEKWSVVAESKVCNAVVSGLSSGQEYQFRVKAYNEKGKSDPRVLGIPVIAKDLTIQPSFKLPFNTYSVQAGEDLKIEIPVIGRPRPKISWVKDGEPLKQTTRVNVEETATSTILHIKESSKDDFGKYSVTATNSAGTATENLSVIVLEKPGPPVGPVKFDEVSADFVVISWEPPAYTGGCQISNYIVEKRDTTTTNWQMVSATVARTTIKISKLKTGTEYQFRIFAENRYGKSTPLDSKPVVVQYPFKEPGPPGTPFVTSISKDQMLVQWHEPVNDGGSKVTGYHLEQKEKNSILWVKLNKIPIQDTKFKTTGLDEGLEYEFRVSAENIVGIGKPSKVSECYVARDPCDPPGRPEAIVITRNSVTLKWKKPVYDGGSKITGYIVEKKDLPDGRWMKASFTNVVETEFTVTGLVEDQRYEFRVIARNAADNFSEPSESSGAITARDEIDAPNASLDPKYRDVIIVHAGETFVLEADIRGKPIPDIIWSKDGNELEETAARMEIKSTLQKTTLIVKDCIRTDGGQYTLKLSNVGGTKTIPITVKVLDRPGPPEGPLKVTGVTAEKCYLAWNPPLQDGGASISHYIIEKRETSRLSWTQVSNEVQALNYKVTKLLPGNEYIFRVMAVNKYGIGEALESEPVIACNPYKRPGPPSTPEASAITKDSMVLTWTRPVDDGGAEIEGYILEKRDKEGIRWTKCNKKTLTDLRFRVTGLTEGHSYEFRVAAENAAGVGEPSEPSVFYRACDALYPPGPPSNPKVTDTSRSSVSLAWNKPIYDGGAPVRGYVIELKKAAADEWTTCTPPSGLQGKQFTVTKLKENTEYNFRICAFNTEGVGEPATIPGSVVAQERMEAPEIELDADLRKVVTLRASATLRLFVTIKGRPEPEVKWEKAEGILTERAQIEVTSSYTMLVIDNVTRFDSGRYNLTLENNSGSKTAFVNVRVLDSPSAPVNLTIREVKKDSVTLSWEPPLIDGGAKITNYIVEKRETTRKAYATITNNCTKNTFKIENLQEGCSYYFRVLASNEYGIGLPAETAEPVKVSEPPLPPGRVTLVDVTRNTATIKWEKPESDGGSKITGYVVEMQTKGSEKWSACTQVKTLETTISGLTAGEEYVFRVAAVNEKGRSDPRQLGVPVIAKDIEIKPSVELPFNTFNVKANDQLKIDIPFKGRPQATVAWKKDGQVLRETTRVNVASSKTVTTLSIKEASREDVGTYELCVSNTAGSITVPITVIVLDRPGPPGPIRIDEVSCDNVSISWNPPEYDGGCQISNYIVEKRETTSTTWQVVSQAVARTSIKIVRLTTGSEYQFRVCAENRYGKSSYSESSAVVAEYPFSPPGPPGTPKVVHATKSTMVVSWQVPVNDGGSQVIGYHLEYKERSSILWSKANKVLIADTQMKVSGLDEGLMYEYRVYAENIAGIGKCSKACEPVPARDPCDPPGQPEVTNITRKSVSLKWSKPRYDGGAKITGYIVERRELPDGRWLKCNFTNVQETYFEVTELTEDQRYEFRVFARNAADSVSEPSESTGPITVKDDVEAPRIMMDVKFRDVIIVKAGEVLKINADIAGRPLPVISWAKDGVEIEERAKTEIVSTDYTTTLTVKDCVRRDTGQYVLTLKNVAGTRTMAVNCKVLDKPGPPAGPLEINGLTAEKCSLSWGRPQEDGGADIDYYIVEKRETSRLAWTICEAELRTTSCKVTKLLKGNEYIFRVTGVNKYGVGEPLESMAVKALDPFTTPSPPTSLEITSVTKDSMTLCWSRPETDGGSDISGYIIERREKNSLRWMRVNKKPVYDLRVKSTGLREGCEYEYRVFAENAAGLSLPSETSPLVRAEDPVFLPSPPSKPKIVDSGKTTITIGWVKPLFDGGAPITGYTVEYKKSEETDWKVAIQSFRGTEYTMSGLTTGDEYVFRVRSLNKMGASDPSDSSDPQVAKEREEEPVFDVDSEMRKTLIVKAGSSFTMTVPFRGRPIPNVSWSKPDTDLRTRAYIDSTDSRTLLTIENANRNDSGKYTLTIQNVLSAASMTFVVKVLDSPGPPANITVREVTKETAMLSWDVPENDGGAPVKNYHIEKREASKKAWVSVTNNCNRLSYKVTNLQEGAIYYFRVSGENEFGVGVPAETKEGVKITEKPSPPEKLGVTSVSKDSVSLSWLKPEHDGGSRIIHYVVEALEKGQKTWVKCAVVKTTHHVVSGLRESHEYFFRVFAENQAGLSDPRELLLPVLIKDQLEPPEIDMKNFPSHTVYVRAGSNLKVDIPISGKPLPKVTLSRDGVPLKATMRFNTEITAENLTINLKESVTTDAGRYEITAANSSGTTKTFINIIVLDRPGPPTGPVAISDITEESVTLKWEPPKYDGGSHVTNYIVLKRETSTAVWSEVSATVARTMIKVMKLTTGEEYQFRIKAENRFGISDHIDSVCVVVKLPYTTPGPPSTPWVSNVTRESITVGWHEPVSNGGSAVTGYHLEMKDRNSILWQKANKMIIRTTHFKVTTISAGLIYEFRVYAENAAGIGKPSHPSEPVLAIDACEPPRNVRITDISKNSVNLSWQQPAFDGGSKITGYIVERRDLPDGRWTKASFTNVIETQFTVSGLTQNSQYEFRVFARNAVGSVSNPSEVVGPITCIDSYGGPVIDLPLEYTEVVKYRAGTSVKLRAGISGKPEPTIEWYKDDKELQTNALVCVENSTDLASILIKDANRLNSGSYELKLRNAMGSASATIRVQILDKPGPPGGPIEFKTVTAEKITLLWRPPADDGGAKITHYIVEKRETSRVVWSMVAENLEECIVTTTKIIKGNEYVFRVRAVNKYGIGEPLESEPVVAKNAFVTPGPPSIPEVTKITKNSMTVVWDRPTVDGGSEINGYFLERRDKKSLAWLKVLKETIRDTRQKVTGLTENSDYQYRVCAVNAAGVGPFSEPSDFYKAADPIDPPGPPAKIRIADSTKSSITLGWSKPVYDGGSDVTGYVVEMKQGDEEEWTIVSTRGEVRTTEYVVSNLKPGVNYYFQVSAVNCAGQGEPITMTEPAQAKDVLEEPEIDLDVALRTSVIAKAGEDVQLLIPFKGRPPPTVTWRKDEKNLGSDTRYSIQNTDSSSLLVIPQVTRNDTGKYILTIENGVGQPKSSTVSVKVLDTPAACQKLQVKHVSLGTVTLLWDPPLIDGGSPIINYVIEKRDATKRTWSVVSHKCSGTSFKVTDLSEKTPFFFRVLAENEIGIGEPCETTEPVKAAEVPAPIRDLSMKDSTKTSVVLSWTKPDFDGGSIITDYLVERKGKGEQAWSHAGISKTCEIEIGQLKEQSVLEFRVSARNEKGQSDPVTIGPLTVKELVITPEVDLSEIPGAQISVRIGHNVHLELPYKGKPKPSISWLKDGLPLKESEYVRFSKTENKITLSIKNSKKEHGGKYTVILDNAVCRNSFPITIITLGPPSKPKGPIRFDEIKADSAIMSWDIPEDDGGGEITCYSIEKREASQTNWKMVCSSVARTTFKVSNLVKDSEYQFRVRAENRYGVSEPLASNIIVAKHQFRIPGPPGKPVIYNVTSDGMSLTWDAPVYDGGSEVTGFHVEKKERNSILWQRVNTSPISGREYRATGLIEGLDYQFRVYAENSAGLSSPSDPSKFTLAVSPVDPPGTPDYIDVTRETITLKWNPPLRDGGSKIVAYSIEKRQGSDRWVRCNFTDVSECQYTVTGLSPGDRYEFRIIARNAVGTISPPSQSSGLIMTRDENVPPTVEFGPEYFDGLVIKSGDSLRIKALVQGRPVPRVTWFKDGVEIERRMNMEITDVLGSTSLFVRDATRDHRGVYTVEAKNVSGSTKAEVTVKVQDTPGKVVGPIRFTNITGEKMTLWWEAPLNDGCAPVTHYIIEKRETSRLAWALIEDNCEALSYTAIKLITGNEYQFRISAVNKFGVGRPLESDPVVAQIQYTIPDAPGVPEPSNVTGNSITLTWTRPESDGGSEIQHYILERREKKSTRWVKVISKRPISETRFKVTGLVEGNEYEFHVMAENAAGIGPASGISRLIKCREPVNPPSAPSVVKVTDTSKTTVSLEWARPVFDGGMEIIGYIIEMCKADLGDWHKVNTEPCVKTRYTVTDLQAGEEYKFRVSAVNGAGKGDSCEVTGTIKAVDRLSAPELDIDANFKQTHIVRAGVSIRLFIAYQGRPTPTAVWSKPDSNLSIRADIHTTDSFSTLTVENCNRNDAGKYTLTVENNSGKKSITFTVKVLDSPGPPGPITFKDVTRGSATLMWDAPLLDGGARIHHYVIEKREASRRSWQVVSEKCTRQILKVSELTEGVPYYFRVSAENEYGVGEPYEMPEPIVATEQPAPPRRLDVVDTSKSSAVLAWLKPDHDGGSRITSYLLEMRQKGSDFWVEAGHTKQLTFTVERLVENTEYEFRVKAKNDAGYSEPREAFSSVIIKEPQIEPTADLTGITNQLITCKAGSTFTIDVPISGRPAPKVTWKLEEMRLKETDRMSIATTKDRTTLTVKDSMRGDSGRYFLTLENTAGVKTFTITVVVIGRPGPVTGPIEVSSVSAESCVLSWTEPKDDGGTEITNYIVEKRESGTTAWQLINSSVKRTQIKVTHLTKYKEYCFRVSSENRFGVSKPLESVPIVAEHPFVPPSAPTRPEVYYVSANAMSIRWEEPYHDGGSKIVGYWVEKKERNTILWVKENKVPCLECNYKVTGLVEGLEYQFRTYALNAAGVSKASEASRPIMAQNPVDPPGRPEVTDVTRSTVSLIWSAPVYDGGSKVVGYIIERKPVSEVGDGRWLKCNYTIVSDNFFTVTALSEGDTYEFRVLAKNAAGVISKGSESTGPVTCRDEYAPPKAELDARLQGDLVTIRAGSDLVLDAAVGGKPEPKIIWTKGDKELDLCEKISLQYTGKRATAVIKYCDRSDSGKYTLTVKNASGTKSVSVMVKVLDSPGPCGKLTVSRVTEEKCTLAWSLPQEDGGAEITHYIVERRETSRLNWVIVEGECLTASYVVTRLIKNNEYTFRVRAVNKYGLGVPVESEPIVARNSFTIPSQPGIPEEVGAGKEHIIIQWTKPESDGGNEISNYLVDKREKKSLRWTRVNKDYVVYDTRLKVTSLMEGCDYQFRVTAVNAAGNSEPSEASNFISCREPSYTPGPPSAPRVVDTTKRSISLAWTKPMYDGGTDIIGYVLEMQEKDTDQWCRVHTNATIRNNEFTVPDLKMGQKYSFRVAAVNAKGMSDYSETTAEIEPVERLEIPDLELADDLKKTVIVRAGASLRLMVSVSGRPSPVITWSKKGIDLANRAIIDNTESYSLLIVDKVNRYDAGKYTIEAENQSGKKSATVLVKVYDTPGPCPSVSVKEVSRDSVTITWEIPTIDGGAPVNNYIIEKREAAMRAFKTVTTKCSKTLYRISGLVEGTMYYFRVLPENIYGIGEPCETSDAVLVSEVPLVPTKLEVVDVTKSTVTLAWEKPLYDGGSRLTGYVLEACKAGTERWMKVVTLKPTVLEHTVISLNEGEQYLFRVRAQNEKGVSEPREIVTPVTVQDLRVLPTIDLSTMPQKTIHVPAGRPIELVIPITGRPPPTASWFFAGSKLRESERVTVETHTKVTKLTIRETTIRDTGEYTLELKNVTGTTSETIKVIILDKPGPPTGPIKIDEIDATSVTISWEPPELDGGAPLSGYVVEQRDAHRPGWLPVSESVTRPTFKFTRLTEGNEYVFRVAATNRFGIGSYLQSEVIECRSSISIPGPPETLQIFDVSRDGMTLTWYPPEDDGGSQVTGYIVERKEVRADRWVRVNKVPVTMTRYRSTGLIEGLEYEHRVTAINARGTGKPSRPSKPTVAMDPIAPPGKPQNPRVTDTTRTSVSLAWSVPEDEGGSKVTGYLIEMQKVDQREWTKCNTTPTKIREYTLTHLPQGAEYRFRVLACNAGGPGEPAEVPGTVKVTEMLEYPDYELDERYQEGVFVRQGGVIRLTIPIKGKPFPVCKWTKEGQDISKRAMIATSETHTELVIKEADRNDSGTYDLVLENKCGKKTVYIKVKVIGSPNTPEGPLEYDDIQARSVRVSWRPPADDGGADILGYILERREVPKAAWYTIDSRVRGTSLVVKGLKENVEYHFRVSAENQFGISKPLKSEEPVIPKTPLNPPEPPSNPPEVLDVTKSSVSLSWSRPKDDGGSRVTGYYIERKETSTDKWVRHNKTQITTTMYTVTGLVPDAEYQFRIIAQNDVGLSETSPASEPVVCKDPFDKPSQPGELEILSISKDSVTLQWEKPECDGGKEILGYWVEYRQSGDSAWKKSNKERIKDRQFTIGGLLEATEYEFRVFAENETGLSRPRRTAMSVKTKLTSGEAPGVRKEMADVTTKLGEAAQLSCQIVGRPLPDIKWYRFGKELIQSRKYKMSSDGRTHTLTVMTDEQEDEGVYTCVATNEVGEVESSSKLLLQAAPQFHPGYPLKEKYYGAVGSTLRLHVMYIGRPVPAMTWFHGQKLLQNSEKITIENTEHYTHLVMKNVQRKTHAGKYKVQLSNAFGTVDATLDVEIQDKPDKPTGPIVIEALLKNSVVISWKPPADDGGSWITNYVVEKCEAKEGAEWQLVSSAISVTTCRIVNLTENAGYYFRVSAQNTFGISEPLEVASIVIIKSPFEKPGVPGKPTITAVTKDSCVVAWKPPASDGGAKIRNYYLERREKKQNKWIAVTTEEIRETVFSVQNLIEGLEYEFRVKCENLGGESEWSEISEPVTPKSDVPIQAPHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEIIADGLKYRIQEFKGGYHQLIIASVTDDDATVYQVRATNQGGSVSGTASLEVEVPAKIHLPKTLEGMGAVHALRGEVVSIKIPFSGKPDPVITWQKGQDLIDNNGHYQVIVTRSFTSLVFSNGVERKDAGFYVVCAKNRFGIDQKTVELDVADVPDPPRGVKVSDVSRDSVNLTWTEPASDGGSKVTNYIVEKCATTAERWLRVGQARETRYTVINLFGKTSYQFRVIAENKFGLSKPSEPSEPTVTKEDKTRAMNYDDEVDETREVTTTKASHSKTKELYEKYMIAEDLGRGEFGIVHRCVETSSKRTFMAKFVKVKGTDQVLVKKEISILNIARHRNILYLHESFESMEELVMIFEFISGLDIFERINTSAFELNEREIVSYVRQVCEALEFLHSQNIGHFDIRPENIIYQTRKNSTIKIIEFGQARQLKPGDNFRLLFTAPEYYAPEVHQHDVVSTATDMWSLGTLVYVLLSGINPFLAETNQQMIENIMNAEYTFDEEAFKEISLEAMDFVDRLLVKERKSRMTASEALQHPWLKQRIDRVSTKVIRTLKHRRYYHTLIKKDLNMVVSAARISCGGAIRSQRGVSVAKVKVASIEIGPVSGQIMHAIGEEGGYVKYVCKIENYDQSTQVTWYFGVRQLENSEKYEITYEDGVATMYVKDITKFDDGTYRCKVVNDYGEDSSYAELFVKGVREVYDYYCRRTKKVKRRTDAMRLLERPPEFTLPLYNKTAYVGENVRFGVTITVHPEPRVTWYKSGQKIKPGDDEKKYTFESDKGLYQLTINSVTTDDDAEYTVVARNKHGEDSCKAKLTVTLHPPPTETTLRPMFKRLLANAECHEGQSVCFEIRVSGIPAPTLKWEKDGQPLSLGPHIEIVHEGLDYYALHIRDTLPEDTGYYRVTATNTAGSTSCQAHLQVERLRYVKQEFQSKEERERHVQKQIDKTLRMAEILSGTETVPLTPVAQEALREAAILYKPAVSTKTVKGEYRLQTEEKKEERKLRMPYEVPEPRRFKQATVEEDQRIKQFVPMSDMKWYKKIRDQYEMPGKLDRVVQKRPKRIRLSRWEQFYVMPLPRITDQYRPKWRIPKLTQDDLEMVRPARRRTPSPDYDLYYYRRRRRSLGDMSDEELLLPIDDYLAMKRTEEERLRLEEELELGFSASPPSRSPPRFELSSLRYSSPPAHVKVEDRRRDFRYSTYHVPTKEETSTSYAELRERHAQASYRQPKLRQRIMAEKEEEELLRPVTTTQRLSEYKSELDYMSKEEKSKKKSKRQRQVTEITEIEEEYEISRRAQRESSSSVSRLLRRRRSLSPTYIELMRPVSELIRSHPRPAEEYEDDAERRSPTPERTRPRSPSPVSSERSLSRFERSARFDIFSRYESMKAALKTQKTSERKYEVLSQQPFTLDHAPRITLRMRSHRVPCGQNTRFILNVQSKPTAEVKWYHNGVELQESSKIHYTNTSGVLTLEILDCQTEDGGTYRAVCTNYKGEASDYATLDVTGGAYTTYASQRRDEEVPKSVFPELTKTEAYAVSSFKRTSELEAASSVREVKSQMTETRESLSTYEHYASAEMKSATSEEKSLEEKATVRKIKTTLAARILTKPRSITVHEGESARFSCDTDGEPVPTVTWLREGQVVSTSARHQVTTTKYKSTFEISSVQASDEGNYSVVVENSDGKQEAQFTLTVQKARVIEKAVTSPPRVKSPEPRVKSPETVKSPKRVKSPEPVTSHPKAVSPTETKPTEKGQHLPVSAPPKITQSLKAEASKDIAKLTCAVESSALCAKEVAWYKDGKKLKENGHFQFHYSADGTYELKIHNLSESDCGEYVCEVSGEGGTSKTSFQFTGQSFKSIHEQVSSISETTKSVQKTAESPEAKKQEPIAPESISSKPVIVTGLRDTTVSSDSVAKFTIKVTGEPQPTITWTKDGKAIAQGSKYKLSSNKEEFILEILKTETSDGGLYACTVTNSAGSVSSSCKLTIKAVKDTEAQKVSTQKTSEVTSQKKASAQEEISQKALTSEEIKMSEVKSHETLAIKEEASKVLIAEEVKRSAAASLEKSIVHEEVTKTSQASEEVKTHAEIKTLSTQMNITKGQRATLKANIAGATDVKWVLNGTELPNSEEYRYGVSGSDQTLTIKQASHREEGILSCIGKTSQGVVKCQFDLTLSEELSDAPSFITQPRSQNINEGQNVLFSCEVSGEPSPEIEWFKNNLPISISSNISVSRSRNVYTLEIRNAAVSDSGKYTIKAKNFHGQCSATASLTVLPLVEEPPREVVLKTSSDVSLHGSVSSQSVQMSASKQEASFSSFSSSSASSMTEMKFASMSAQSMSSMQESFVEMSSSSFMGKSSMTQLESSTSRMLKAGGRGIPPKIEALPSDISIDEGKVLTVACAFTGEPTPEITWSCGGRKIQNQEQQGRFHIENTDDLTTLIIMDVQKQDGGLYTLSLGNEFGSDSATVNINIRSM
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Key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The size and extensibility of the cross-links are the main determinants of sarcomere extensibility properties of muscle. In non-muscle cells, seems to play a role in chromosome condensation and chromosome segregation during mitosis. Might link the lamina network to chromatin or nuclear actin, or both during interphase.
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A2ASZ8
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SCMC2_MOUSE
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Mitochondrial adenyl nucleotide antiporter SLC25A25 (Short calcium-binding mitochondrial carrier protein 2) (SCaMC-2) (Solute carrier family 25 member 25)
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MLCLCLYVPIAGAAQTEFQYFESKGLPAELKSIFKLSVFIPSQEFSTYRQWKQKIVQAGDKDLDGQLDFEEFVHYLQDHEKKLRLVFKSLDKKNDGRIDAQEIMQSLRDLGVKISEQQAEKILKSMDKNGTMTIDWNEWRDYHLLHPVENIPEIILYWKHSTIFDVGENLTVPDEFTVEERQTGMWWRHLVAGGGAGAVSRTCTAPLDRLKVLMQVHASRSNNMCIVGGFTQMIREGGAKSLWRGNGINVLKIAPESAIKFMAYEQMKRLVGSDQETLRIHERLVAGSLAGAIAQSSIYPMEVLKTRMALRKTGQYSGMLDCARRILAKEGVAAFYKGYIPNMLGIIPYAGIDLAVYETLKNTWLQRYAVNSADPGVFVLLACGTISSTCGQLASYPLALVRTRMQAQASIEGAPEVTMSSLFKQILRTEGAFGLYRGLAPNFMKVIPAVSISYVVYENLKITLGVQSR
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Electroneutral antiporter that most probably mediates the transport of adenyl nucleotides through the inner mitochondrial membrane. Originally identified as an ATP-magnesium/inorganic phosphate antiporter, it could have a broader specificity for adenyl nucleotides. By regulating the mitochondrial matrix adenyl nucleotide pool could adapt to changing cellular energetic demands and indirectly regulate adenyl nucleotide-dependent metabolic pathways.
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A2AT37
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RENT2_MOUSE
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Regulator of nonsense transcripts 2 (Up-frameshift suppressor 2 homolog) (Upf2)
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MPAERKKSASMEEKESLLNNKEKDCSERRPVSSKEKPRDDLKVTAKKEVSKVPEDKKKRLEEDKRKKEDKERKKKEEEKVKAEEELKKKEEEEKKKQEEEERKKQEEQAKRQQEEAAAQLKEKEESLQLHQEAWERHQLRKELRSKNQNAPDNRPEENFFSRLDSSLKKNTAFVKKLKTITEQQRDSLSHDFNGLNLSKYIAEAVASIVEAKLKLSDVNCAAHLCSLFHQRYSDFAPSLLQVWKKHFEARKEEKTPNITKLRTDLRFIAELTIVGIFTDKEGLSLIYEQLKSIINADRESHTHVSVVISFCRHCGDDIAGLVPRKVKSAAEKFNLSFPPSEIISPEKQQPFQNLLKEYFTSLTKHLKRDHRELQNTERQNRRILHSKGELSEDRHKQYEEFAMSYQKLLANSQSLADLLDENMPDLPQDKPTPEEHGPGIDIFTPGKPGEYDLEGGIWEDEDARNFYENLIDLKAFVPAILFKDNEKSQNKDSNKDDSKEAKEPKDNKEASSPDDLELELENLEINDDTLELEGADEAEDLTKKLLDEQEQEDEEASTGSHLKLIVDAFLQQLPNCVNRDLIDKAAMDFCMNMNTKANRKKLVRALFIVPRQRLDLLPFYARLVATLHPCMSDVAEDLCSMLRGDFRFHVRKKDQINIETKNKTVRFIGELTKFKMFTKNDTLHCLKMLLSDFSHHHIEMACTLLETCGRFLFRSPESHLRTSVLLEQMMRKKQAMHLDARYVTMVENAYYYCNPPPAEKTVRKKRPPLQEYVRKLLYKDLSKVTTEKVLRQMRKLPWQDQEVKDYVICCMINIWNVKYNSIHCVANLLAGLVLYQEDVGIHVVDGVLEDIRLGMEVNQPKFNQRRISSAKFLGELYNYRMVESAVIFRTLYSFTSFGVNPDGSPSSLDPPEHLFRIRLVCTILDTCGQYFDRGSSKRKLDCFLVYFQRYVWWKKSLEVWTKDHPFPIDIDYMISDTLELLRPKIKLCNSLEESIRQVQDLEREFLIKLGLVNDKESKDSMTEGENLEEDEEEEEGGAETEEQSGNESEVNEPEEEEGSEEEEEGEEEEEENTDYLTDSNKENETDEENAEVMIKGGGLKHVPCVEDEDFIQALDKMMLENLQQRSGESVKVHQLDVAIPLHLKSQLRKGPPLGGGEGETESADTMPFVMLTRKGNKQQFKILNVPMSSQLAANHWNQQQAEQEERMRMKKLTLDINERQEQEDYQEMLQSLAQRPAPANTNRERRPRYQHPKGAPNADLIFKTGGRRR
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Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by associating with the nuclear exon junction complex (EJC). Recruited by UPF3B associated with the EJC core at the cytoplasmic side of the nuclear envelope and the subsequent formation of an UPF1-UPF2-UPF3 surveillance complex (including UPF1 bound to release factors at the stalled ribosome) is believed to activate NMD. In cooperation with UPF3B stimulates both ATPase and RNA helicase activities of UPF1. Binds spliced mRNA.
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A2AU37
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RD21L_MOUSE
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Double-strand-break repair protein rad21-like protein 1
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MFYTHVLMSKRGPLAKIWLAAHWEKKLTKAHVFECNLEITIQKIISPKVKIALRTSGHLLLGVVRIYNRKAKYLLADCSEAFLKMKMTFRPGLVDLPKENFEAAYNTITLPEEFHDFEIYNINEIDISEPLAQNQSRPEEITLREEYSNDLLFQAGSFGDEPEILRRHSFFDDNILMNSSGLVVEHSSGSFAEEKSLFFDNGDGFGDEGAAGEMIDNLLQDESTFLEEAYLNKEVSLPPELPSSIMVEPGNSDDQCIPEDEEINEITLLSNEDEGFTLDPIDDLDIADRRRRKKRRLLVDPVKEISSKAMHRQLASFMDTLMVLDLAPPTQRLMMWKKRGGVDMLLSTATQDLINDELKMLFTKCFLSSDYKLAKLTLKESVRKEVGNQQIAEPSVMGEPNSHSELDQPQDWKDVTDESVGSFQENVNMNVNSEQDILGMISPAVEGLSSMNGSLAQENCPAELESSGSKQNTEAEKWNQRLFQTLNVLREFNKMGMQSFSLKKLCRNSDRKQAAAKFYTLLILKKHRAIELSQSVPYADIIATVGPMFYKM
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Meiosis-specific component of some cohesin complex required during the initial steps of prophase I in male meiosis. Probably required during early meiosis in males for separation of sister chromatids and homologous chromosomes. Replaces RAD21 in premeiotic S phase (during early stages of prophase I), while RAD21 reappears in later stages of prophase I. Involved in synaptonemal complex assembly, synapsis initiation and crossover recombination between homologous chromosomes during prophase I. Not required for meiosis in females in young mice, while it is required later as mice age.
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A2AUC9
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KLH41_MOUSE
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Kelch-like protein 41 (Kelch repeat and BTB domain-containing protein 10)
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MDSQRELAEELRLYQSTLLQDGLKDLLEEKKFIDCTLKAGDKSFPCHRLILSACSPYFREYFLSEIEEEKKKEVALDNVDPAILDLIIKYLYSASIDLNDGNVQDIFALSSRFQIPSVFTVCVSYLQKRLAPGNCLAILRLGLLLDCPRLAISAREFVSDRFVQICKEEDFMQLSPQELISVISNDSLNVEKEEVVFEAVMKWVRTDKENRAKNLSEVFDCIRFRLMAEKYFKDHVEKDDIIKSNPEVQKKIKVLKDAFAGKLPEPSKNAEKAGAGEVNGDVGDEDLLPGYLNDIPRHGMFVKDLILLVNDTAAVAYDPMENECYLTALAEQIPRNHSSLVTQQNQVYVVGGLYVDEENKDQPLQSYFFQLDNVTSEWVGLPPLPSARCLFGLGEVDDKIYVVAGKDLQTEASLDSVLCYDPVAAKWSEVKNLPIKVYGHNVISHNGMIYCLGGKTDDKKCTNRVFIYNPKKGDWKDLAPMKTPRSMFGVAIHKGKIVIAGGVTEDGLSASVEAFDLKTNKWEVMTEFPQERSSISLVSLAGALYAIGGFAMIQLESKEFAPTEVNDIWKYEDDKKEWAGMLKEIRYASGASCLATRLNLFKLSKL
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Involved in skeletal muscle development and differentiation. Regulates proliferation and differentiation of myoblasts and plays a role in myofibril assembly by promoting lateral fusion of adjacent thin fibrils into mature, wide myofibrils. Required for pseudopod elongation in transformed cells.
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A2AUM9
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CE152_MOUSE
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Centrosomal protein of 152 kDa (Cep152)
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MSLEFGSVALQTQNEDEEFDKEDFEREKELQQLLTDLPHDMLDDELSSPERHDSDCSMDGRAAEPHPSEHLERKWIERDILPKPHSMNCGNGWEENRSKTEDQHLGYHPGEGGDEGGSGYSPPGKREQADLYRLPEDFRPYTGGSKQAASVITFSDPQRDNFQQFGLSRGPSCGALEPYKAVYKPYRNSSVQKNSSPAQEVAASDMFEGLQQQFLGANETDSAENIHIIQLQVLNKAKERQLDSLVEKLKDSERQVRYLSHQLLIVQDEKDGLALSLRESQQLFQNGKEREMQLEAQIAALEAQVEAFRVSEEKLTKKLRTTEITLESLKQQLVELHHSESLQRAREHHESIVASLTQKHEEQVSSLQKNLDATITALQEQESICTRLKDHVQQLERNQEAVRLEKTELINRLTRSLEDSQKQCAHLLQSGSVQEVAQLQLQLQQAQKAHVLSESMNKALQEELTELKDEISLYESAAELGVLPGDSEGDLSIELTESCVDLGIKKVNWKQSKANRVTQQESPDEDPSKDELILKLKTQVQRLLTSNSVKRHLVSQLQSDLRECRETMEAFQQSKDGDSGMETKTDTSEKTTKQLWLESSEAINREDILQLKNEVQVLQKQNQELKEAEEKLRSTNQDLCNQMRQMVQEFDHDKQEAVARCERTYQQHHEAMKAQIRESLLAKHAVEKQHLLEVYEGTQSQLRSDLDKMNKEMAAVQECYLEVCREKDGLESTLRKTMEKAQEQKRQLLEAREEYVRKLKLELEEKYQETLKTERQSWLQEQAAGATQQAEKESRQKLIQQLEKEWQSKLDDSLAAWRKTTSDRGSQTEQVACPAAVSKAEAAAVLAEEQARQVQQEKELATKEALRKPEVELELKYCEIIAQKVETAVQNARSRWIQELPMLAEYKALLRAQQQEWAKQQELAVAHRLSLALSEAKEKWKSELENMKPNVMSVKELEEKVHSLQKELELKDEEVPVIVRAEVAKARTEWNKEKQEEIHKIQEQNEEDYRQFLEDHRNKINEVLAAAKEDFVKQKAELLLQKETEFQACLDQSRKEWTLQEAQQTQVEIRQYEEDTLTVLAYLLKDTQLEYGGDSQDKQLLEAMSACSSKWISVQYFEKVKACIQKALHDMLSLLTDSVASEQEKRKVVKSSADTVSWTSSEGDSAVPVPLPDSTSVRCAQSSAWLKAEAETDKKICEIKGLRCGHCFQELEKEKQECQDLRRKLEKCRRHLQHLERTHRAAVEKLGEENSRVVEELIEENHDMKNKLEALRALCRTPPRSLSAGAAESAGPSCSRQALEELRGQYIKAVRKIKRDMLRYIQESKERAAEMVKAEVLRERQETARKMRNYYLSCLQQILQDNGKEEGAEKKIMSAASKLATMAELLGTIAESDCRVRCAQAGRSVALPLASEMLTGTERSERSGVNHNIPHYVESKPNSGKTLPRSVCEQLPGRKAAPRSQRRLEESKHREMRPMASTALPSDCRCGDASCRHSGVLAKDVAPEFVPCQGEGGFDLHEKRDALGAGSEPLLYSAAHSFLGGAEKNSSPRCISESRHTTLRSPSEMPRLKALMCGSPTETDSIASEKSQGVGSQDSPVKDGVGPSSSPAWPSDSTLPCGSPAVLFLGDGSQRTQEMLGDSVQWKQFSATSCHPDAQKSNMVCRSSHTLDLPKETLHSQQGKMGATLGHPSPQSTDMLKTDFKRLSGTGPSSLCQKPLIKLTAPMPSQQDSGFDSPLE
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Necessary for centrosome duplication the function seems also to involve CEP63, CDK5RAP2 and WDR62 through a stepwise assembled complex at the centrosome that recruits CDK2 required for centriole duplication (By similarity). Acts as a molecular scaffold facilitating the interaction of PLK4 and CENPJ, 2 molecules involved in centriole formation (By similarity). Proposed to snatch PLK4 away from PLK4:CEP92 complexes in early G1 daughter centriole and to reposition PLK4 at the outer boundary of a newly forming CEP152 ring structure (By similarity). Also plays a key role in deuterosome-mediated centriole amplification in multiciliated that can generate more than 100 centrioles. Overexpression of cep152 can drive amplification of centrioles.
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A2AUU0
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METL8_MOUSE
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tRNA N(3)-methylcytidine methyltransferase METTL8, mitochondrial (EC 2.1.1.-) (Methyltransferase-like protein 8) (Tension-induced/inhibited protein) (mRNA N(3)-methylcytidine methyltransferase METTL8) (EC 2.1.1.-)
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MNVIWRSCICRLRQGKVPHRCQSGVHPVAPLGSRILTDPAKVFEHNMWDHMQWSKEEEDAARKKVEENSATRVAPEEQVKFESDANKYWDIFYQTHKNKFFKNRNWLLREFPEILPVNQNTKEKVGESSWDQVGSSISRTQGTETHCQESFVSPEPGSRGRSAPDPDLEEYSKGPGKTEPFPGSNATFRILEVGCGAGNSVFPILNTLQNIPGSFLYCCDFASEAVELVKSHESYSEAQCSAFIHDVCDDGLAYPFPDGILDVVLLVFVLSSIHPDRALFI
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Mitochondrial S-adenosyl-L-methionine-dependent methyltransferase that mediates N(3)-methylcytidine modification of residue 32 of the tRNA anticodon loop of mitochondrial tRNA(Ser)(UCN) and tRNA(Thr) (By similarity). N(3)-methylcytidine methylation modification regulates mitochondrial translation efficiency and is required for activity of the respiratory chain (By similarity). N(3)-methylcytidine methylation of mitochondrial tRNA(Ser)(UCN) requires the formation of N(6)-dimethylallyladenosine(37) (i6A37) by TRIT1 as prerequisite (By similarity). May also mediate N(3)-methylcytidine modification of mRNAs. The existence of N(3)-methylcytidine modification on mRNAs is however unclear, and additional evidences are required to confirm the role of the N(3)-methylcytidine-specific mRNA methyltransferase activity of METTL8 in vivo (By similarity).
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A2AVA0
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SVEP1_MOUSE
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Sushi, von Willebrand factor type A, EGF and pentraxin domain-containing protein 1 (Polydom)
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MWSRLAFCCWALALVSGWTNFQPVAPSLNFSFRLFPEASPGALGRLAVPPASSEEEAAGSKVERLGRAFRSRVRRLRELSGSLELVFLVDESSSVGQTNFLNELKFVRKLLSDFPVVSTATRVAIVTFSSKNNVVARVDYISTSRAHQHKCALLSREIPAITYRGGGTYTKGAFQQAAQILRHSRENSTKVIFLITDGYSNGGDPRPIAASLRDFGVEIFTFGIWQGNIRELNDMASTPKEEHCYLLHSFEEFEALARRALHEDLPSGSFIQEDMARCSYLCEAGKDCCDRMASCKCGTHTGQFECICEKGYYGKGLQHECTACPSGTYKPEASPGGISTCIPCPDVSHTSPPGSTSPEDCVCREGYQRSGQTCEVVHCPALKPPENGFFIQNTCKNHFNAACGVRCRPGFDLVGSSIHLCQPNGLWSGTESFCRVRTCPHLRQPKHGHISCSTAEMSYNTLCLVTCNEGYRLEGSTRLTCQGNAQWDGPEPRCVERHCATFQKPKGVIISPPSCGKQPARPGMTCQLSCRQGYILSGVREVRCATSGKWSAKVQTAVCKDVEAPQISCPNDIEAKTGEQQDSANVTWQVPTAKDNSGEKVSVHVHPAFTPPYLFPIGDVAITYTATDSSGNQASCTFYIKVIDVEPPVIDWCRSPPPIQVVEKEHPASWDEPQFSDNSGAELVITSSHTQGDMFPHGETVVWYTATDPSGNNRTCDIHIVIKGSPCEVPFTPVNGDFICAQDSAGVNCSLSCKEGYDFTEGSTEKYYCAFEDGIWRPPYSTEWPDCAIKRFANHGFKSFEMLYKTTRCDDMDLFKKFSAAFETTLGNMVPSFCNDADDIDCRLEDLTKKYCIEYNYNYENGFAIGPGGWGAGNRLDYSYDHFLDVVQETPTDVGKARSSRIKRTVPLSDPKIQLIFNITASVPLPEERNDTLELENQQRLIKTLETITNRLKSTLNKEPMYSFQLASETVVADSNSLETEKAFLFCRPGSVLRGRMCVNCPLGTSYSLEHSTCESCLMGSYQDEEGQLECKLCPPRTHTEYLHSRSVSECKAQCKQGTYSSSGLETCESCPLGTYQPEFGSRSCLLCPETTTTVKRGAVDISACGVPCPVGEFSRSGLTPCYPCPRDYYQPNAGKSFCLACPFYGTTTITGATSITDCSSFSSTFSAAEESIVPLVAPGHSQNKYEVSSQVFHECFLNPCHNSGTCQQLGRGYVCLCPPGYTGLKCETDIDECSSLPCLNGGICRDQVGGFTCECSLGYSGQICEENINECISSPCLNKGTCTDGLASYRCTCVKGYMGVHCETDVNECQSSPCLNNAVCKDQVGGFSCKCPPGFLGTRCEKNVDECLSQPCQNGATCKDGANSFRCQCPAGFTGTHCELNINECQSNPCRNQATCVDELNSYSCKCQPGFSGHRCETEQPSGFNLDFEVSGIYGYVLLDGVLPTLHAITCAFWMKSSDVINYGTPISYALEDDKDNTFLLTDYNGWVLYVNGKEKITNCPSVNDGIWHHIAITWTSTGGAWRVYIDGELSDGGTGLSIGKAIPGGGALVLGQEQDKKGEGFNPAESFVGSISQLNLWDYVLSPQQVKLLASSCPEELSRGNVLAWPDFLSGITGKVKVDSSSMFCSDCPSLEGSVPHLRPASGNRKPGSKVSLFCDPGFQMVGNPVQYCLNQGQWTQPLPHCERIRCGLPPALENGFYSAEDFHAGSTVTYQCTSGYYLLGDSRMFCTDNGSWNGISPSCLDVDECAVGSDCSEHASCLNTNGSYVCSCNPPYTGDGKNCAEPVKCKAPENPENGHSSGEIYTVGTAVTFSCDEGHELVGVSTITCLETGEWDRLRPSCEAISCGVPPVPENGGVDGSAFTYGSKVVYRCDKGYTLSGDEESACLASGSWSHSSPVCELVKCSQPEDINNGKYILSGLTYLSIASYSCENGYSLQGPSLLECTASGSWDRAPPSCQLVSCGEPPIVKDAVITGSNFTFGNTVAYTCKEGYTLAGPDTIVCQANGKWNSSNHQCLAVSCDEPPNVDHASPETAHRLFGDTAFYYCADGYSLADNSQLICNAQGNWVPPAGQAVPRCIAHFCEKPPSVSYSILESVSKAKFAAGSVVSFKCMEGFVLNTSAKIECLRGGEWSPSPLSVQCIPVRCGEPPSIANGYPSGTNYSFGAVVAYSCHKGFYIKGEKKSTCEATGQWSKPTPTCHPVSCNEPPKVENGFLEHTTGRTFESEARFQCNPGYKAAGSPVFVCQANRHWHSDAPLSCTPLNCGKPPPIQNGFLKGESFEVGSKVQFVCNEGYELVGDNSWTCQKSGKWSKKPSPKCVPTKCAEPPLLENQLVLKELASEVGVMTISCKEGHALQGPSVLKCLPSGQWNGSFPICKMVLCPSPPLIPFGVPASSGALHFGSTVKYLCVDGFFLRGSPTILCQADSTWSSPLPECVPVECPQPEEILNGIIHVQGLAYLSTTLYTCKPGFELVGNATTLCGENGQWLGGKPMCKPIECPEPKEILNGQFSSVSFQYGQTITYFCDRGFRLEGPKSLTCLETGDWDMDPPSCDAIHCSDPQPIENGFVEGADYRYGAMIIYSCFPGFQVLGHAMQTCEESGWSSSSPTCVPIDCGLPPHIDFGDCTKVRDGQGHFDQEDDMMEVPYLAHPQHLEATAKALENTKESPASHASHFLYGTMVSYSCEPGYELLGIPVLICQEDGTWNGTAPSCISIECDLPVAPENGFLHFTQTTMGSAAQYSCKPGHILEGSHLRLCLQNKQWSGTVPRCEAISCSKPNPLWNGSIKGDDYSYLGVLYYECDSGYILNGSKKRTCQENRDWDGHEPMCIPVDCGSPPVPTNGRVKGEEYTFQKEITYSCREGFILEGARSRICLTNGSWSGATPSCMPVRCPAPPQVPNGVADGLDYGFKKEVAFHCLEGYVLQGAPRLTCQSNGTWDAEVPVCKPATCGPPADLPQGFPNGFSFYHGGHIQYQCFTGYKLHGNPSRRCLPNGSWSGSSPSCLPCRCSTPIIQQGTINATDLGCGKTVQIECFKGFKLLGLSEITCDANGQWSDVPLCEHAQCGPLPTIPNAIVLEGSLSEDNVVTYSCRPGYTMQGSSDLICTEKAIWSQPYPTCEPLSCGPPPTVANAVATGEAHTYESKVKLRCLEGYVMDSDTDTFTCQQDGHWVPERITCSPKKCPVPSNMTRIRFHGDDFQVNRQVSVSCAEGFTHEGVNWSTCQPDGTWEPPFSDESCIPVVCGHPESPAHGSVVGNKHSFGSTIVYQCDPGYKLEGNRERICQENRQWSGEVAVCRENRCETPAEFPNGKAVLENTTSGPSLLFSCHRGYTLEGSPEAHCTANGTWNHLTPLCKPNPCPVPFVIPENAVLSEKEFYVDQNVSIKCREGFLLKGNGVITCSPDETWTHTNARCEKISCGPPSHVENAIARGVYYQYGDMITYSCYSGYMLEGSLRSVCLENGTWTPSPVCRAVCRFPCQNGGVCQRPNACSCPDGWMGRLCEEPICILPCLNGGRCVAPYQCDCPTGWTGSRCHTATCQSPCLNGGKCIRPNRCHCLSAWTGHDCSRKRRAGL
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May play a role in the cell attachment process.
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