wanglab/gogpt-training-data huggingface dataset:
Protein: Disintegrin and metalloproteinase domain-containing protein 18 (ADAM 18) (Transmembrane metalloproteinase-like, disintegrin-like, and cysteine-rich protein III) (tMDC III) (Q9Y3Q7)
Organism: Homo sapiens (Human)
Function: Sperm surface membrane protein that may be involved in spermatogenesis and fertilization. This is a non catalytic metalloprotease-like protein (By similarity).
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
Sequence:
MFLLLALLTELGRLQAHEGSEGIFLHVTVPRKIKSNDSEVSERKMIYIITIDGQPYTLHLGKQSFLPQNFLVYTYNETGSLHSVSPYFMMHCHYQGYAAEFPNSFVTLSICSGLRGFLQFENISYGIEPVESSARFEHIIYQMKNNDPNVSILAVNYSHIWQKDQPYKVPLNSQIKNLSKLLPQYLEIYIIVEKALYDYMGSEMMAVTQKIVQVIGLVNTMFTQFKLTVILSSLELWSNENQISTSGDADDILQRFLAWKRDYLILRPHDIAYLLVYRKHPKYVGATFPGTVCNKSYDAGIAMYPDAIGLEGFSVIIAQLLGLNVGLTYDDITQCFCLRATCIMNHEAVSASGRKIFSNCSMHDYRYFVSKFETKCLQKLSNLQPLHQNQPVCGNGILESNEECDCGNKNECQFKKCCDYNTCKLKGSVKCGSGPCCTSKCELSIAGTPCRKSIDPECDFTEYCNGTSSNCVPDTYALNGRLCKLGTAYCYNGQCQTTDNQCAKIFGKGAQGAPFACFKEVNSLHERSENCGFKNSQPLPCERKDVLCGKLACVQPHKNANKSDAQSTVYSYIQDHVCVSIATGSSMRSDGTDNAYVADGTMCGPEMYCVNKTCRKVHLMGYNCNATTKCKGKGICNNFGNCQCFPGHRPPDCKFQFGSPGGSIDDGNFQKSGDFYTEKGYNTHWNNWFILSFCIFLPFFIVFTTVIFKRNEISKSCNRENAEYNRNSSVVSESDDVGH
Protein: Rho guanine nucleotide exchange factor 18 (114 kDa Rho-specific guanine nucleotide exchange factor) (p114-Rho-GEF) (p114RhoGEF) (Septin-associated RhoGEF) (SA-RhoGEF) (Q6ZSZ5)
Organism: Homo sapiens (Human)
Function: Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPases. Its activation induces formation of actin stress fibers. Also acts as a GEF for RAC1, inducing production of reactive oxygen species (ROS). Does not act as a GEF for CDC42. The G protein beta-gamma (Gbetagamma) subunits of heterotrimeric G proteins act as activators, explaining the integrated effects of LPA and other G-protein coupled receptor agonists on actin stress fiber formation, cell shape change and ROS production. Required for EPB41L4B-mediated regulation of the circumferential actomyosin belt in epithelial cells.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15558029}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15558029}. Cell membrane {ECO:0000269|PubMed:29601110}. Apical cell membrane {ECO:0000269|PubMed:22006950}. Note=In unactivated eosinophils, distributed around the cell periphery in the perimembranous region (PubMed:29601110). In activated eosinophils, relocates to the tip of the nucleopod, a membrane structure formed during activation when the nucleus moves to one end of the cell, and is also concentrated in membrane protrusions at the opposite end of the cell (PubMed:29601110). Localizes to the apical cell membrane in epithelial cells (PubMed:22006950). {ECO:0000269|PubMed:22006950, ECO:0000269|PubMed:29601110}.
Interaction partners:
- Cingulin
- Cingulin-like protein 1
- Rho-associated protein kinase 2
- Transforming protein RhoA
- Tight junction protein 1
Sequence:
MGDDQEDDFPRRLSESMEDLSLDLGALQGSEYLQDLGLGAPSHSQPGETPDSRPTGEEPGRDSLFSSLAGSQDLSRRRSWERSRSCSESWRRLSLDASAVDEEPCLPRTLASLALNLPGGGLKTWTQGCLSGGGTPAESPGKECDSPKKRGRSRSVPVSFYEIRSPEISPGLEVPTPPVQGLEPPVLECMEKDHVEPDHVLIVQQVLQELRQYHGARQRACMSASPGGAHSNLTWFEFLSESEDGAGKNEKSDKSTSVKRRLSCLRSRVTRQKEKGKSPAHLKDKGQDARERRECVNGHQLLQGTFSGPSSCPLCGKPFLSSASLKEHPRGTLLSDGSPALSRNVGMTVSQKGGPQPTPSPAGPGTQLGPITGEMDEADSAFLKFKQTADDSLSLTSPNTESIFVEDPYTASLRSEIESDGHEFEAESWSLAVDAAYAKKQKREVVKRQDVLYELMQTEVHHVRTLKIMLKVYSRALQEELQFSSKAIGRLFPCADDLLETHSHFLARLKERRQESLEEGSDRNYVIQKIGDLLVQQFSGENGERMKEKYGVFCSGHNEAVSHYKLLLQQNKKFQNLIKKIGNFSIVRRLGVQECILLVTQRITKYPVLVERIIQNTEAGTEDYEDLTQALNLIKDIISQVDAKVSECEKGQRLREIAGKMDLKSSSKLKNGLTFRKEDMLQRQLHLEGMLCWKTTSGRLKDILAILLTDVLLLLQEKDQKYVFASVDSKPPVISLQKLIVREVANEEKAMFLISASLQGPEMYEIYTSSKEDRNAWMAHIQRAVESCPDEEEGPFSLPEEERKVVEARATRLRDFQERLSMKDQLIAQSLLEKQQIYLEMAEMGGLEDLPQPRGLFRGGDPSETLQGELILKSAMSEIEGIQSLICRQLGSANGQAEDGGSSTGPPRRAETFAGYDCTNSPTKNGSFKKKVSSTDPRPRDWRGPPNSPDLKLSDSDIPGSSEESPQVVEAPGTESDPRLPTVLESELVQRIQTLSQLLLNLQAVIAHQDSYVETQRAAIQEREKQFRLQSTRGNLLLEQERQRNFEKQREERAALEKLQSQLRHEQQRWERERQWQHQELERAGARLQEREGEARQLRERLEQERAELERQRQAYQHDLERLREAQRAVERERERLELLRRLKKQNTAPGALPPDTLAEAQPPSHPPSFNGEGLEGPRVSMLPSGVGPEYAERPEVARRDSAPTENRLAKSDVPIQLLSATNQFQRQAAVQQQIPTKLAASTKGGKDKGGKSRGSQRWESSASFDLKQQLLLNKLMGKDESTSRNRRSLSPILPGRHSPAPPPDPGFPAPSPPPADSPSEGFSLKAGGTALLPGPPAPSPLPATPLSAKEDASKEDVIFF
Protein: Uncharacterized protein YaiW (P77562)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Peptide antibiotic transporter SbmA
Sequence:
MSRVNPLSSLSLLAVLVLAGCSSQAPQPLKKGEKAIDVASVVRQKMPASVKDRDAWAKDLATTFESQGLAPTLENVCSVLAVAQQESNYQADPAVPGLSKIAWQEIDRRAERMHIPAFLVHTALKIKSPNGKSYSERLDSVRTEKQLSAIFDDLINMVPMGQTLFGSLNPVRTGGPMQVSIAFAEQHTKGYPWKMDGTVRQEVFSRRGGLWFGTYHLLNYPASYSAPIYRFADFNAGWYASRNAAFQNAVSKASGVKLALDGDLIRYDSKEPGKTELATRKLAAKLGMSDSEIRRQLEKGDSFSFEETALYKKVYQLAETKTGKSLPREMLPGIQLESPKITRNLTTAWFAKRVDERRARCMKQ
Protein: 5-hydroxytryptamine (Serotonin) receptor 2A, isoform B (Q8IPN2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- G protein alpha s subunit subunit alpha)
- Tryptophan 5-hydroxylase 2
- Guanine nucleotide-binding protein G
- Sodium-dependent serotonin transporter
Sequence:
MEMQSYSGRGPSTGTSETATATAAVASASASDTAATFTLRHFNCRLEEADWPGPRQPFIDCEGSHTNSTSYTPSSLPTSKNLIEGPNNTFQCARQAIDEAEHNAFYSCDGESPLSENCTLRLKARLLRWPYEAYEHIRLAINGALSDYASDKLSDSSSCDEGGMVLQCKLGQAHELLLCHLQQLEREPLREVGSAEESFSNDSLLQAFQIELGAERDGLWSFLNLSELMEPDHGFLGIMNVTNTSLDMFLPNLTALNTTSTASTADMATEFAVTKSFLDYSPHGYDFLFLFVVFFIFAGGLGNILVCLAVALDRKLQNVTNYFLFSLAIADLLVSLFVMPMGAIPAFLGYWPLGFTWCNIYVTCDVLACSSSILHMCFISLGRYMGIRNPLGSRHRSTKRLTGIKIAIVWVMAMMVSSSITVLGLVNEKNIMPEPNICVINNRAFFVFGSLVAFYIPMLMMVTTYALTIPLLRKKARFAAEHPESELFRRLGGRFTLRPQHSQQQLQMFSSFSGSNNKFLSMGDGNRNFNTEGEMEEGGAPSRRSGVEPAERPLMQQRTASSRSMGTVSFRNVVNGTSGAAGSGRRTTGTAHSSFRFSGAGIFRHSSSSPASSCHSTSTSRSSSFWRKHGGYPNLMDRLAIHLRLSLVPPSSHPNRRASVRVTISQPQLGYPTNVGGNGGRTVGATEVGAGGNGSSAGRTSNSSLGGTSLMKIATIQGPILNQSQAAGGNHMVQKVKPTALKPEEPQRNKVRPFKFAFNRVATPTLNLRFLNNRSKRNSLSANAVATEQKATKVLGLVFFTFVLCWSPFFILNIIFAACPECQVPEHVVNTCLWLGYVSSTINPIIYTIFNRTFRAAFIRLLKCNCKRSGRPLRYRSVTEGRGALSLCAPSALPLAISFQGAPLMTPSTANATPMSEFRASCRTVTDDEC
Protein: Protein mago nashi homolog 2 (OsMAGO2) (Mago nashi-like protein 2) (P49030)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). The MAGO-Y14 heterodimer inhibits the ATPase activity of EIF4A3, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The MAGO-Y14 heterodimer interacts with the EJC key regulator PYM leading to EJC disassembly in the cytoplasm (By similarity). EJC core heterodimers play essential roles in plant growth and development, and pollen and seed development. The MAGO-Y14 heterodimer selectively binds to the UDT1 (UNDEVELOPED TAPETUM 1) pre-mRNA transcript and regulates the splicing of UDT1, a key regulator in stamen development.
Subcellular location: Nucleus {ECO:0000269|PubMed:24820023}. Cytoplasm {ECO:0000250|UniProtKB:P61326}. Note=Nucleocytoplasmic shuttling protein. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. {ECO:0000250|UniProtKB:P61326}.
Interaction partners:
- RNA-binding protein Y14B
- RNA-binding protein Y14A
- Os04g0440100 protein
- Eukaryotic initiation factor 4A-III homolog A
- Eukaryotic initiation factor 4A-III homolog B
- Expressed protein
- Os06g0256200 protein
- Expressed protein
- DEAD-box ATP-dependent RNA helicase 56
- DEAD-box ATP-dependent RNA helicase 15
Sequence:
MATGGAAGEDVPGGGEFYLRYYVGHKGKFGHEFLEFEFRPDGKLRYANNSNYKNDTMIRKEVFVSPSVLREARRIIQESEIMKEDDNNWPEPDRVGRQELEIVMGNEHISFTTSKIGSLVDVQTSKDPEGLRIFYYLVQDLKCFVFSLINLHFKIKPIQS
Protein: Squamosa promoter-binding-like protein 8 (Q8GXL3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Trans-acting factor that binds specifically to the consensus nucleotide sequence 5'-TNCGTACAA-3'. Binds specifically to the 5'-GTAC-3' core sequence. Involved in development and floral organogenesis. Required for ovule differentiation, pollen production, filament elongation, seed formation and siliques elongation. Also seems to play a role in the formation of trichomes on sepals. May positively modulate gibberellin (GA) signaling in flower.
Subcellular location: Nucleus {ECO:0000269|PubMed:16095614}. Cytoplasm {ECO:0000269|PubMed:16095614}. Note=Mostly located in nucleus.
Interaction partners:
- Protein NBR1 homolog
- E3 ubiquitin-protein ligase PRT1
- Protein SPOROCYTELESS
- MADS-box protein AGL42
- MADS-box protein SOC1
Sequence:
MLDYEWDNPSSIVLSGDERNPDSDPTRSSFSFFDPISHYNNDHRHITISPPLLSSFSNQQQQHHLTLYGQTNSNNQFLHHHHHHHSLYGSTTTTTPYGASDPIYHPHSSAPPASLFSYDQTGPGSGSGSSYNFLIPKTEVDFTSNRIGLNLGGRTYFSAADDDFVSRLYRRSRPGESGMANSLSTPRCQAEGCNADLSHAKHYHRRHKVCEFHSKASTVVAAGLSQRFCQQCSRFHLLSEFDNGKRSCRKRLADHNRRRRKCHQSASATQDTGTGKTTPKSPNDSGVKASSSPSSNAPPTISLECFRQRQFQTTASSSTSASSSSNSMFFSSG
Protein: Transcription coactivator (F4I701)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MKTTQLFKGANVFMSRNLVPPEVFDTLLDAFKLNGAEIFLCCDPSRSGPSDFHVIASPDHEKFKDLKAKGCNLIGPQCALFCAKEGRPLPQRGFTCCLAMDGLKVLASGFLVDEKVKIKELVTSMGGVLLSRASSDVNFVIVKNVLAAKYKWALNKKPIVTLNWLHRCWNEHRVVPQEPYKIPPFSGLTICVTRIPADERKGMEKVISEYGGSYSAELTKSCTHLIADAAEGDKYKVARKWGHIQIVTRKWFQQSIDKKVCLNEESYPVLGSIPLTRGVRDLGVHNGLEKFPSAATASAADSYVSCAQSRDSDIEASASQNVFPTSMNPSTDVKEPGGGPTARPQEQNIDGCTARDSESEDNDLYLSDCRIFLLGFEASEMRKLAKLVRRGGGSRYMLLNERMTHIVVGTPSESEKREARSVAASGVIQVVIPSWLEDCDREKKEIPVHNIYTANHLILPRDSACLTKGSFARMSSMEQTKNTHDQTMVYDSSSRSINVSNGPATLLGKNKEAMQEFGRKDEIHTGRKIVSPTQKETLISLVTCESKEQRSIQCEFSGQNDQERKSSVFKGETFCFSHSFPEDRRPQIVEWVNQGGGEVVNDPLINNAHFTIECHGGFQSTETTQTIYVSSHWVRNCLKVGCLLAVSSHILYSPLPCQTPLPGFESLCICSSQHNEKNVELLRNLSVVLGADFVERLTRKVTHLICNFAKGDKYVRASKWGIISVTPDWLYECVRQNQVVCTDNFHPRELTTQDREAGSQFHTQFVPMASRDSMSLPVSHSEDREKIQSFAGKSGCGKGEVYNRLGEIGKEQTFPSKKAKLLRDGQESDVFPVRELPSNCDRPSHSGDGIVTGYDVASGREVPDVADTIEDLLEQTSKIQDQKSPGRILEKTHFSTSEQYNTGNHSVTGLSRHWINRVHKNDDMGSPPGDATTDTYGNFSETQTESQVVGYEEDLSGRQMLIDRVRTRSSLT
Protein: Elongator complex protein 2 (ELP2) (SHINC-2) (STAT3-interacting protein 1) (StIP1) (Q6IA86)
Organism: Homo sapiens (Human)
Function: Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine). The elongator complex catalyzes the formation of carboxymethyluridine in the wobble base at position 34 in tRNAs.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11714725, ECO:0000269|PubMed:11818576}. Nucleus {ECO:0000269|PubMed:11714725, ECO:0000269|PubMed:11818576}.
Interaction partners:
- Elongator complex protein 3
- Elongator complex protein 5
- Elongator complex protein 1
- Elongator complex protein 4
- Elongator complex protein 6
- RNA polymerase-associated protein RTF1 homolog
- RNA polymerase-associated protein LEO1
- Parafibromin
- Little elongation complex subunit 2
- RNA polymerase-associated protein CTR9 homolog
Sequence:
MVAPVLETSHVFCCPNRVRGVLNWSSGPRGLLAFGTSCSVVLYDPLKRVVVTNLNGHTARVNCIQWICKQDGSPSTELVSGGSDNQVIHWEIEDNQLLKAVHLQGHEGPVYAVHAVYQRRTSDPALCTLIVSAAADSAVRLWSKKGPEVMCLQTLNFGNGFALALCLSFLPNTDVPILACGNDDCRIHIFAQQNDQFQKVLSLCGHEDWIRGVEWAAFGRDLFLASCSQDCLIRIWKLYIKSTSLETQDDDNIRLKENTFTIENESVKIAFAVTLETVLAGHENWVNAVHWQPVFYKDGVLQQPVRLLSASMDKTMILWAPDEESGVWLEQVRVGEVGGNTLGFYDCQFNEDGSMIIAHAFHGALHLWKQNTVNPREWTPEIVISGHFDGVQDLVWDPEGEFIITVGTDQTTRLFAPWKRKDQSQVTWHEIARPQIHGYDLKCLAMINRFQFVSGADEKVLRVFSAPRNFVENFCAITGQSLNHVLCNQDSDLPEGATVPALGLSNKAVFQGDIASQPSDEEELLTSTGFEYQQVAFQPSILTEPPTEDHLLQNTLWPEVQKLYGHGYEIFCVTCNSSKTLLASACKAAKKEHAAIILWNTTSWKQVQNLVFHSLTVTQMAFSPNEKFLLAVSRDRTWSLWKKQDTISPEFEPVFSLFAFTNKITSVHSRIIWSCDWSPDSKYFFTGSRDKKVVVWGECDSTDDCIEHNIGPCSSVLDVGGAVTAVSVCPVLHPSQRYVVAVGLECGKICLYTWKKTDQVPEINDWTHCVETSQSQSHTLAIRKLCWKNCSGKTEQKEAEGAEWLHFASCGEDHTVKIHRVNKCAL
Protein: Queuine tRNA-ribosyltransferase catalytic subunit 1 (EC 2.4.2.64) (Guanine insertion enzyme) (tRNA-guanine transglycosylase) (Q9JMA2)
Organism: Mus musculus (Mouse)
Function: Catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming queuine, allowing a nucleophilic attack on the C1' of the ribose to form the product (By similarity).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:19414587}. Mitochondrion outer membrane {ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:19414587}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000305|PubMed:19414587}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:19414587}. Nucleus {ECO:0000269|PubMed:19414587}. Note=Weakly associates with mitochondria, possibly via QTRT2. {ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:19414587}.
Interaction partners:
- Queuine tRNA-ribosyltransferase accessory subunit 2
- Thymidylate synthase
- tRNA
Sequence:
MAAVGSPGSLESAPRIMRLVAECSRSGARAGELRLPHGTVATPVFMPVGTQATMKGITTEQLDSLGCRICLGNTYHLGLRPGPELIRKAQGLHGFMNWPHNLLTDSGGFQMVSLFSLSEVTEEGVHFRSPYDGEETLLSPERSVEIQNALGSDIIMQLDHVVSSTVTGPLVEEAMHRSVRWLDRCIAAHKHPDKQNLFAIIQGGLNADLRTTCLKEMTKRDVPGFAIGGLSGGESKAQFWKMVALSTSMLPKDKPRYLMGVGYATDLVVCVALGCDMFDCVYPTRTARFGSALVPTGNLQLKKKQYAKDFSPINPECPCPTCQTHSRAFLHALLHSDNTTALHHLTVHNIAYQLQLLSAVRSSILEQRFPDFVRNFMRTMYGDHSLCPAWAVEALASVGIMLT
Protein: Fimbrial subunit CupA1 (Q9I1Y7)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Chaperone CupA5
- Usher CupA3
- Chaperone CupA2
- Usher CupB3
- Chaperone CupB4
- Chaperone CupB2
- Usher CupC3
- Chaperone CupC2
- Fimbrial subunit CupA4
- Probable pili assembly chaperone
Sequence:
MTRTSNPCAVVLAFAAIAASGTAMAANTITFSGEVTDQTCQVAVNGFTDPTVILDSVPVSALDGAVGRSAGETAFTLQLTDCVAPTADEHFTTLFQATNPSAAGNLVNTAASGATGVALQLLDSVGGNPVDLAGGAAVPAGDIVLANGATSTSYDYAVQYVSEAATVTPGPVLGVVTYTLRYE
Protein: Oleosin L (A0A060L4I9)
Organism: Pinus massoniana (Chinese red pine)
Subcellular location: Lipid droplet {ECO:0000269|PubMed:24954070}. Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Surface of oil bodies. Oleosins exist at a monolayer lipid/water interface. {ECO:0000305}.
Interaction partners:
Sequence:
MEAAQQKNESVMDYAPDWTQISVLFFVVMGGGVLASLSALALAGTVVLMLILTPVFLLLSPVILPVGAVIALAAAAFMAAVTIGIAGAAALIWVYRYARGQPTVGSEKIDRARVRLFEAAEKLKAQLQYKLFNENSKANFD
Protein: Contig An01c0020, genomic contig (A2Q7D0)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEEAFSPVDSLAGSPTPELPLLTVSPADTSLDDSSVQAGETKAEEKKPVKKRKSWGQELPVPKTNLPPRKRAKTEDEKEQRRIERVLRNRAAAQTSRERKRLEMEKLENEKIQMEQQNQFLLQRLSQMEAENNRLNQQVAQLSAEVRGSRGNTPKPGSPVSASPTLTPTLFKQERDEIPLERIPFPTPSITDYSPTLRPSTLAESSDVTQHPAVSVAGLEGEGSALSLFDVGSNPEPHAADDLAAPLSDDDFHRLFNVDSPVGSDSSVLEDGFAFDVLDGGDLSAFPFDSMVDFDPESVGFEGIEPPHGLPDETSRQTSSVQPSLGASTSRCDGQGIAAGC
Protein: Protein Wnt-8 (XWnt-8) (P28026)
Organism: Xenopus laevis (African clawed frog)
Function: Ligand for members of the frizzled family of seven transmembrane receptors. Plays a role in ventral mesodermal patterning during embryogenesis. Mimics Nieuwkoop center activity. Causes dorsal mesodermal differentiation of animal cap ectoderm when coexpressed with noggin and nuclear, sequence-specific DNA-binding protein xBra. None of these molecules causes dorsal mesoderm formation when expressed alone.
Subcellular location: Secreted, extracellular space, extracellular matrix.
Interaction partners:
Sequence:
MQNTTLFILATLLIFCPFFTASAWSVNNFLMTGPKAYLTYSASVAVGAQNGIEECKYQFAWERWNCPESTLQLATHNGLRSATRETSFVHAISSAGVMYTLTRNCSMGDFDNCGCDDSRNGRIGGRGWVWGGCSDNAEFGERISKLFVDGLETGQDARALMNLHNNEAGRLAVKETMKRTCKCHGISGSCSIQTCWLQLAEFRDIGNHLKIKHDQALKLEMDKRKMRSGNSADNRGAIADAFSSVAGSELIFLEDSPDYCLKNISLGLQGTEGRECLQSGKNLSQWERRSCKRLCTDCGLRVEEKKTEIISSCNCKFHWCCTVKCEQCKQVVIKHFCARRERDSNMLNTKRKNRGHRR
Protein: Sorting nexin 9 (A0A8I6GJY7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004180}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004180}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004180}.
Interaction partners:
Sequence:
MGFRVISLPVCLHRLMQQAVDESGSDVLRLAGKADFSSSYKMLQSGSTASQEARVMYDFAAEPGNNELTVNEGEIITITNPNVGGGWLEGKNSKGEQGLVPTDYVEILPNDGKDPFSCGNSVADQAFLDSLSASTAQANSSSANSNNQVGGGSDPWSAWNAPRSGNWDSSDAWGTRTDGAGAQRNSSANNWDTGFGHPQAYQGPATGDDDEWDEDWDDPKSSSPYFKDSEPAEAGGIQRGNSRAGASSMKLPLNKFPGFAKPGMEQYLLAKQLAKPKEKIPIIVGDYGPMWVYPTSTFDCVVADPRKGSKMYGLKSYIEYQLTPTNTNRSVNHRYKHFDWLYERLLVKFGSAIPIPSLPDKQVTGRFEEEFIKMRMERLQAWMTRMCRHPVVSESEVFQQFLNFRDEKEWKTGKRKAEKDELVGVMIFSTMEPEAPDLDLIEIEQKCDAVGKFTKAMDDGVKELLTVGQEHWKRCTGPLPKEYQKIGKALQSLAAVFSSSGYQGETDLNNAITEAGKTYEEIASLVAEQPKKDLHFLMECNHEYKGFLGCFPDIIGAHKGAIEKVKESDKLVATSKITPQDKQTMVKRVGTMSYALQAEMNHFHSNRIYDYNSVIRLYLEQQVQFYETIAEKLRQALGRFPVM
Protein: Verprolin (P37370)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in cytoskeletal organization and cellular growth. May exert its effects on the cytoskeleton directly, or indirectly via proline-binding proteins (e.g. profilin) or proteins possessing SH3 domains.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305|PubMed:14562095}.
Interaction partners:
- Proline-rich protein LAS17
- Myosin-3
- Myosin-5
- Protein BZZ1
- Actin
- Reduced viability upon starvation protein 167
- Actin cytoskeleton-regulatory complex protein SLA1
- Protein SLA2
- Myosin tail region-interacting protein MTI1
- Actin-related protein 2
Sequence:
MAGAPAPPPPPPPPALGGSAPKPAKSVMQGRDALLGDIRKGMKLKKAETNDRSAPIVGGGVVSSASGSSGTVSSKGPSMSAPPIPGMGAPQLGDILAGGIPKLKHINNNASTKPSPSASAPPIPGAVPSVAAPPIPNAPLSPAPAVPSIPSSSAPPIPDIPSSAAPPIPIVPSSPAPPLPLSGASAPKVPQNRPHMPSVRPAHRSHQRKSSNISLPSVSAPPLPSASLPTHVSNPPQAPPPPPTPTIGLDSKNIKPTDNAVSPPSSEVPAGGLPFLAEINARRSERGAVEGVSSTKIQTENHKSPSQPPLPSSAPPIPTSHAPPLPPTAPPPPSLPNVTSAPKKATSAPAPPPPPLPAAMSSASTNSVKATPVPPTLAPPLPNTTSVPPNKASSMPAPPPPPPPPPGAFSTSSALSASSIPLAPLPPPPPPSVATSVPSAPPPPPTLTTNKPSASSKQSKISSSSSSSAVTPGGPLPFLAEIQKKRDDRFVVGGDTGYTTQDKQEDVIGSSKDDNVRPSPISPSINPPKQSSQNGMSFLDEIESKLHKQTSSNAFNAPPPHTDAMAPPLPPSAPPPPITSLPTPTASGDDHTNDKSETVLGMKKAKAPALPGHVPPPPVPPVLSDDSKNNVPAASLLHDVLPSSNLEKPPSPPVAAAPPLPTFSAPSLPQQSVSTSIPSPPPVAPTLSVRTETESISKNPTKSPPPPPSPSTMDTGTSNSPSKNLKQRLFSTGGSTLQHKHNTHTNQPDVDVGRYTIGGSNSIVGAKSGNERIVIDDSRFKWTNVSQMPKPRPFQNKTKLYPSGKGSSVPLDLTLFT
Protein: Breast cancer anti-estrogen resistance protein 3 (Novel SH2-containing protein 2) (SH2 domain-containing protein 3B) (O75815)
Organism: Homo sapiens (Human)
Function: Acts as an adapter protein downstream of several growth factor receptors to promote cell proliferation, migration, and redistribution of actin fibers. Specifically involved in INS/insulin signaling pathway by mediating MAPK1/ERK2-MAPK3/ERK1 activation and DNA synthesis. Promotes insulin-mediated membrane ruffling (By similarity). In response to vasoconstrictor peptide EDN1, involved in the activation of RAP1 downstream of PTK2B via interaction with phosphorylated BCAR1. Inhibits cell migration and invasion via regulation of TGFB-mediated matrix digestion, actin filament rearrangement, and inhibition of invadopodia activity (By similarity). May inhibit TGFB-SMAD signaling, via facilitating BCAR1 and SMAD2 and/or SMAD3 interaction (By similarity). Regulates EGF-induced DNA synthesis. Required for the maintenance of ocular lens morphology and structural integrity, potentially via regulation of focal adhesion complex signaling (By similarity). Acts upstream of PTPRA to regulate the localization of BCAR1 and PTPRA to focal adhesions, via regulation of SRC-mediated phosphorylation of PTPRA (By similarity). Positively regulates integrin-induced tyrosine phosphorylation of BCAR1 (By similarity). Acts as a guanine nucleotide exchange factor (GEF) for small GTPases RALA, RAP1A and RRAS (By similarity). However, in a contrasting study, lacks GEF activity towards RAP1.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9QZK2}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q9QZK2}. Note=Localization to focal adhesions depends on interaction with PTPRA. {ECO:0000250|UniProtKB:Q9QZK2}.
Interaction partners:
- Breast cancer anti-estrogen resistance protein 1
- Enhancer of filamentation 1
Sequence:
MAAGKFASLPRNMPVNHQFPLASSMDLLSSRSPLAEHRPDAYQDVSIHGTLPRKKKGPPPIRSCDDFSHMGTLPHSKSPRQNSPVTQDGIQESPWQDRHGETFTFRDPHLLDPTVEYVKFSKERHIMDRTPEKLKKELEEELLLSSEDLRSHAWYHGRIPRQVSENLVQRDGDFLVRDSLSSPGNFVLTCQWKNLAQHFKINRTVLRLSEAYSRVQYQFEMESFDSIPGLVRCYVGNRRPISQQSGAIIFQPINRTVPLRCLEEHYGTSPGQAREGSLTKGRPDVAKRLSLTMGGVQAREQNLPRGNLLRNKEKSGSQPACLDHMQDRRALSLKAHQSESYLPIGCKLPPQSSGVDTSPCPNSPVFRTGSEPALSPAVVRRVSSDARAGEALRGSDSQLCPKPPPKPCKVPFLKVPSSPSAWLNSEANYCELNPAFATGCGRGAKLPSCAQGSHTELLTAKQNEAPGPRNSGVNYLILDDDDRERPWEPAAAQMEKGQWDKGEFVTPLLETVSSFRPNEFESKFLPPENKPLETAMLKRAKELFTNNDPKVIAQHVLSMDCRVARILGVSEEMRRNMGVSSGLELITLPHGHQLRLDIIERHNTMAIGIAVDILGCTGTLEDRAATLSKIIQVAVELKDSMGDLYSFSALMKALEMPQITRLEKTWTALRHQYTQTAILYEKQLKPFSKLLHEGRESTCVPPNNVSVPLLMPLVTLMERQAVTFEGTDMWEKNDQSCEIMLNHLATARFMAEAADSYRMNAERILAGFQPDEEMNEICKTEFQMRLLWGSKGAQVNQTERYEKFNQILTALSRKLEPPPVKQAEL
Protein: Serine/threonine-protein kinase Nek6 (EC 2.7.11.34) (Never in mitosis A-related kinase 6) (NimA-related protein kinase 6) (Q9ES70)
Organism: Mus musculus (Mouse)
Function: Protein kinase which plays an important role in mitotic cell cycle progression. Required for chromosome segregation at metaphase-anaphase transition, robust mitotic spindle formation and cytokinesis. Phosphorylates ATF4, CIR1, PTN, RAD26L, RBBP6, RPS7, TRIP4, RPS6KB1 and histones H1 and H3. Phosphorylates KIF11 to promote mitotic spindle formation. Involved in G2/M phase cell cycle arrest induced by DNA damage. Inhibition of activity results in apoptosis. May contribute to tumorigenesis by suppressing p53/TP53-induced cancer cell senescence (By similarity). Phosphorylates STAT3. Phosphorylates EML4 at 'Ser-144', promoting its dissociation from microtubules during mitosis which is required for efficient chromosome congression (By similarity).
Subcellular location: Cytoplasm. Nucleus. Nucleus speckle {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Note=Co- localizes with APBB1 at the nuclear speckles. Colocalizes with PIN1 in the nucleus. Colocalizes with ATF4, CIR1, ARHGAP33, ANKRA2, CDC42, NEK9, RAD26L, RBBP6, RPS7, TRIP4, RELB and PHF1 in the centrosome. Localizes to spindle microtubules in metaphase and anaphase and to the midbody during cytokinesis (By similarity). {ECO:0000250}.
Interaction partners:
Sequence:
MAGQPSHMPHGGSPNHLCHALGPAPPPDPQRLPNTLSFRCSLADFQIEKKIGRGQFSEVYKATCLLDRKTVALKKVQIFEMMDAKARQDCVKEIGLLKQLNHPNIIKYLDSFIEDNELNIVLELADAGDLSQMIKYFKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGIVKLGDLGLGRFFSSETTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLFSLCQKIEQCDYPPLPGEHYSEKLRELVSMCIYPDPDHRPDIVYVHQVARQMHVWTSST