wanglab/gogpt-training-data huggingface dataset:
Protein: Anthrax toxin receptor 1 (Tumor endothelial marker 8) (Q9H6X2)
Organism: Homo sapiens (Human)
Function: Plays a role in cell attachment and migration. Interacts with extracellular matrix proteins and with the actin cytoskeleton. Mediates adhesion of cells to type 1 collagen and gelatin, reorganization of the actin cytoskeleton and promotes cell spreading. Plays a role in the angiogenic response of cultured umbilical vein endothelial cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16762926}; Single-pass type I membrane protein {ECO:0000269|PubMed:16762926}. Cell projection, lamellipodium membrane {ECO:0000269|PubMed:16762926}; Single-pass type I membrane protein {ECO:0000269|PubMed:16762926}. Cell projection, filopodium membrane {ECO:0000269|PubMed:16762926}; Single-pass type I membrane protein {ECO:0000269|PubMed:16762926}. Note=At the membrane of lamellipodia and at the tip of actin-enriched filopodia (PubMed:16762926). Colocalizes with actin at the base of lamellipodia (PubMed:16762926). {ECO:0000269|PubMed:16762926}.
Interaction partners:
- Anthrax toxin receptor 2
- Low-density lipoprotein receptor-related protein 6
- von Willebrand factor
- Vascular endothelial growth factor receptor 2
- Furin
Sequence:
MATAERRALGIGFQWLSLATLVLICAGQGGRREDGGPACYGGFDLYFILDKSGSVLHHWNEIYYFVEQLAHKFISPQLRMSFIVFSTRGTTLMKLTEDREQIRQGLEELQKVLPGGDTYMHEGFERASEQIYYENRQGYRTASVIIALTDGELHEDLFFYSEREANRSRDLGAIVYCVGVKDFNETQLARIADSKDHVFPVNDGFQALQGIIHSILKKSCIEILAAEPSTICAGESFQVVVRGNGFRHARNVDRVLCSFKINDSVTLNEKPFSVEDTYLLCPAPILKEVGMKAALQVSMNDGLSFISSSVIITTTHCSDGSILAIALLILFLLLALALLWWFWPLCCTVIIKEVPPPPAEESEEEDDDGLPKKKWPTVDASYYGGRGVGGIKRMEVRWGEKGSTEEGAKLEKAKNARVKMPEQEYEFPEPRNLNNNMRRPSSPRKWYSPIKGKLDALWVLLRKGYDRVSVMRPQPGDTGRCINFTRVKNNQPAKYPLNNAYHTSSPPPAPIYTPPPPAPHCPPPPPSAPTPPIPSPPSTLPPPPQAPPPNRAPPPSRPPPRPSV
Protein: L-arabinose transport system permease protein AraH (P0AE26)
Organism: Escherichia coli (strain K12)
Function: Part of the binding-protein-dependent transport system for L-arabinose. Probably responsible for the translocation of the substrate across the membrane.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996}.
Interaction partners:
- L-arabinose-binding periplasmic protein
- Arabinose import ATP-binding protein AraG
- Ribose import binding protein RbsB
- D-allose-binding periplasmic protein
- Galactose/methyl galactoside import ATP-binding protein MglA
- Galactofuranose-binding protein YtfQ
- Ribose import ATP-binding protein RbsA
- Xylose import ATP-binding protein XylG
- D-allose import ATP-binding protein AlsA
- Uncharacterized ABC transporter ATP-binding protein YphE
Sequence:
MSSVSTSGSGAPKSSFSFGRIWDQYGMLVVFAVLFIACAIFVPNFATFINMKGLGLAISMSGMVACGMLFCLASGDFDLSVASVIACAGVTTAVVINLTESLWIGVAAGLLLGVLCGLVNGFVIAKLKINALITTLATMQIVRGLAYIISDGKAVGIEDESFFALGYANWFGLPAPIWLTVACLIIFGLLLNKTTFGRNTLAIGGNEEAARLAGVPVVRTKIIIFVLSGLVSAIAGIILASRMTSGQPMTSIGYELIVISACVLGGVSLKGGIGKISYVVAGILILGTVENAMNLLNISPFAQYVVRGLILLAAVIFDRYKQKAKRTV
Protein: Protein phosphatase 1 regulatory subunit 12A (Myosin phosphatase-targeting subunit 1) (Myosin phosphatase target subunit 1) (Q9DBR7)
Organism: Mus musculus (Mouse)
Function: Key regulator of protein phosphatase 1C (PPP1C). Mediates binding to myosin. As part of the PPP1C complex, involved in dephosphorylation of PLK1. Capable of inhibiting HIF1AN-dependent suppression of HIF1A activity (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O14974}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:O14974}. Note=Also along actomyosin filaments. {ECO:0000250|UniProtKB:O14974}.
Interaction partners:
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Rho-associated protein kinase 1
- Protein phosphatase 1 regulatory subunit 14A
- Rho-associated protein kinase 2
- Myosin regulatory light polypeptide 9
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Myosin regulatory light chain 12B
- cGMP-dependent protein kinase 1
- Myosin light polypeptide 6
Sequence:
MKMADAKQKRNEQLKRWIGSETDLEPPVVKRQKTKVKFDDGAVFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDIAEEEAMEELLQNEVNRQGVDIEAARKEEERVMLRDARQWLNSGHISDVRHAKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTAFDVADEDILGYLEELQKKQTLLHSEKRDKKSPLIESTANMENNQPQKAFKNKETLIIEPEKNASRIESLEHEKADEEEEGKKDESSCSSEEDEEDDSESEAETDKTKPMASVSNAHTSSTQAAPAAVTAPTLSSNQGTPTSPVKKFPISTTKISPKEEERKDESPASWRLGLRKTGSYGALAEISASKEAQKEKDTAGVMRSASSPRLSSSLDNKEKEKDNKGTRLAYVTPTIPRRLASTSDIEEKENRESSSLRTSSSYTRRKWEDDLKKNSSINEGSTYHRSCSFGRRQDDLISCSVPSTTSTPTVTSAAGLQRSLPSSTSTAAKTPPGSSSAGTQSSTSNRLWAEDSTEKEKDSAPTAVTIPVAPTVVNAAAPSTTTLTTTTAGTVSEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRSRSTRTREQENEEKEKEEKEKQDKEKQEEKKESEASREDEYKQKYSRTYDETYTRYRPVSTSSSSAPSSSSLSTLGSTLYASSQLNRPNSLVGITSAYSRGLAKENEREGEKKEEEKEGEDKSQPKSIRERRRPREKRRSTGVSFWTQDSDENEQERQSDTEDGSSKRETQTDSVSRYDSSSTSSSDRYDSLLGRSASYSYLEDRKPYSSRLEKDDSTDFKKLYEQILAENEKLKAQLHDTNMELTDLKLQLEKATQRQERFADRSQLEMEKRERRALERRISEMEEELKMLPDLKADNQRLKDENGALIRVISKLSK
Protein: Cytosolic endo-beta-N-acetylglucosaminidase 2 (ENGase 2) (EC 3.2.1.96) (Endo-beta-N-acetyglucosaminidase 85B) (AtENGase85B) (Q9SRL4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Endoglycosidase that releases N-glycans from glycoproteins by cleaving the beta-1,4-glycosidic bond in the N,N'-diacetylchitobiose core. Involved in the production of high-mannose type N-glycans during plant development and fruit maturation.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:21796445}.
Interaction partners:
- Cytosolic endo-beta-N-acetylglucosaminidase 1
- Mitochondrial ATP-independent inner membrane protease subunit 1b
Sequence:
MPKSNDDDVAQSEAVPLLDLVKPSLPISFPIKALQDLKSRSYFDSFHFQFNRSTVPFRRNSDCLPNRPRVLVCHDMKGGYVDDKWVQGCENEAGFAIWHWYLMDIFVYFSHSLVTIPPPCWTNTAHRHGVKVLGTFITEWDEGKATCKEMLATKESAQMYAERLAELATALGFDGWLINIENDIDEEQIPNMKEFVSHLKKVLHLSTPGALVIWYDSVTVRGNLQWQDQLTELNKPFFDLCDGIFMNYTWKESYPNLSAEVAGDRKFDVYMGIDVFGRGSFGGGQWTVNAALDLLKRNNVSAAIFAPGWVYETAQPPNFHTAQNKWWSLVEKSWGIVQTYPQVLPFYSDFNQGFGYHVSLEGRQLSDSPWYNISCQSLQPLLEFNEDNKDIIQVTVDQEGKNVFDFSEQHLNNYYEYDSAREASFNGGGNIVFRGKLKGDAYFTTRLFKPHLQLSSSPITISYSVKSDETSNLGILLSFSSPSLETKSILVAPEDPIRRFDDMSLQCLTTSVQTVSEWTVHEASLVMDGHTLTEISAFCYRPENSTKSAEFVALLGHISVKDHVQNQQNPEILLPASSWVIEAHNVELVPGNSSSKILRVKLEWRQKDLEDSAFTRYNVYAENVKSTDLRPRKVLEKPKSETVLLGIAHVPAYYVAELVVESDVKAVRFMVQACGEDASLGKLDEALNLLVDLEGLSVNHD
Protein: Polysaccharide biosynthesis domain-containing protein (A0A1D8PTY0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MSAQPFSAENADNLEEIEMQFAVKAVQQAETYWSLLEKIPGSKLKLTKHDDDIFNQLLEDFPEFKEPSNVAVIREEDMKSTSGKARWRAFCEKFNEIEDYNFGTLLRLKANEEYSQDGTMFAVRIQFYAIEIARNRYGLNDWISKKE
Protein: SD09011p (Q8MQW2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
IISPTTSRREVGDGELDTEEPTGSGGQRKSSVERSLAPVIRGRKSIKDLKEAKEVKSEEPPAAASESRAASGVTPGQVKEQHVADGNEMESLPITDKKDHKDTKDKGDERETDQEEEKEKSADTEIIADTEKTSEKQKYTEKDKAADKDGGKEKDIDANKDIDKEKEKVKEVLPPVVPIAPVTPTCNRVTRKSHAQEQAINTRVTRNRRQSSTVGANSTASLVAASSSVTEQPPPSRGRRKKPVVVAPPLEPAVKRKRSQDVEADSDANNSTKYSKVEVVKSEEAEAPEEDSSAVPIKQESVDGNEVSSISPTVTPTPTPAPTPAPVPGSRRGRGRPQNRNSSSPATTTRATRLSKAGSPVIVTPVAQEPAPPKRRRVGSSTRKTVSASSLAPSSQGGAGDEDSKDSMASSMDDLLMAAADIKQEKLTPDFDDSLMPEGLPSTSGASSANGHSCTEPLTVDTEINVKPADSKVKPKESPVVAVEESPSQSETQSAKVSAHAGKAPSLSPDMISEGVSAVSVRKFYKKPEFLENNLGIEKYPELGEIVQTVSNNDTETDVEMAVDGEVNQPSTPKSQDKKKEEQEKNQKSGLKAAKKAPAKLEPKAEDISEILTDVPVDISTEAVEIIEEAEEDTCSNSSIKPGELRLDESNDEPELLLEDALIVNGDENETPDQPEEKEDQVEFFHTGEYDDFEHEIMVELAKEGVLDASGNALSQQKVELEHPEDVTLHESKNDIEAEESVERKPLKDPSVADEMEDMNEESYIDIKDQTNQLLVEHLAEEAMEADCGPEDNKENLSTSASSTAADGLDIQLAIKEDDDEEKPLAVIADEQKPGLLLTNDMKVDEKPNGKQESVCDEHVQLVPNLRQEQEIHLQNLGLLTHQAAEHRRKCLLEAQARQAQMQLQQHHHHQHKRQGARGGGSATHVESSGTLKTVIKLNRSSNGGVSGSGGLPTGTVIHGGCGSSSASSTSSSSVGSATRKSSGTLGSGAGAGAGVRRQSLKMTFQKGRARGHGAADRSADQYGAHAEDSYYTIQNENEDSSHSESQGQTDHGFYQMVKKDEKEKILIPEKASSFKFHPGRLCEDQCYYCSGKFGLYDTPCHVGQIKSVERQQKILANEEKLTVDNCLCDACFRHVDRRANVPSYKKRLSASGHLEMGSAAGSALEKQFAGDSGVITESGGEAGSTAAVAVQQRSCGVKDCVEAARHSLRRKCIRKRVKKYQLSLEIPAGSSNVGLCEAHYNTVIQFSGCVLCKRRLGKNHMYNITTQDTIRLEKALSEMGIPVQLGMGTAVCKLCRYFANLLIKPPDSTKAQKAEFVKNYRKRLLKVHNLQDGSHELSEADEEEAPNATETERPTSDGHEDPEMPMVADYDGPTDSNSSSSSTAALDTSKQMSKLQAILQQNVGADAAGAAGTGTVAASPGGSGSGADISNVLRGNPNISMRELFHGEEELGVQFKVPFGCSSSQRTPEGWTRVQTFLQYDEPTRRLWEELQKPYGNQSSFLRHLILLEKYYRNGDLVLAPHASSNATVYTETVRQRLNSFDHGHCGGLNIAGSPSSSGSGKRSGVPQPTGASVLATALTTPLTSHSSSPASISSEQHSSVDPVIPLVDLNDDDEGEDGAGGAGERESTNRQQDVILECLRTASVDKLTKQLSSNAVTIIARPKDKSQLSCNSGSSTSISSSSSAISSPEEVAVTKVTAVAPVQSKDAPPLAPASSGVSNSRSILKTNLLGMNKAVELVPLTTAPHAYKPTGCHKPEKQQKILDVANKQPGSQGEPVPSSALLGLQSKLKPPTHQQQVSGSGAGTSGSQKPSNVAQLLSSPPELISLHRRQTSGAAAGSSSFLQGKRLQLPRSGAGPSGAGTGTGAGAAGSRSAGGPPPPNVVILPDALTPQERHESKSWKPTLIPLEDQHKVPNKSHALYQTADGRRLPALVQVQSGGKPYLISIFDYNRMCILRREKLMRDQLLKSNAKPKPQNQQQQGQTHQQQQNSAASAAAFSNMVKLAQQHTARQQLQQLQQKPQQQQQLPTLQPGGVRLARLPQKLLMPPLTNPQIGSQAPNLQPLLSSTLDNSNNCWLWKNFPDPNQYLLNGNGGGAGSSSSKLPHLTAKPATATSSSGAANKSAGSLFTLKQQQHQQKLIDNAIMSKIPKSLTVIPQQMGGNTGGDMGGSSSSGKD
Protein: Protocadherin 7 isoform 3 (Q2TJI5)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
YCRSKNKNGYEAGKKDHEDFFTPQQHDKSKKPKKDKKNKKSKQPLYSSIVTVEASKPNGQRYDSVNEKLSDSPSMGRYRSVNGGPGSPDLARHYKSSSPLPTVQLHPQSPTAGKKHQAVQDLPPANTFVGAGDNISIGSDHCSEYSCQTSNKYSKQPFRRVTFSVVSQPQDPHQGSLQSCYDSGLEESETPSSKSSSGPRLGALPLPEDNYERTTPDGSVDSRPLPDVALTGKCTRECDEYGHSDSCWMPVRTSPERKKSQPKLSTFMPVDERGSQEKLANGEAAIMGDRNRNLLNKKLTSSYETFSAASFSKNEEANPEDIPLTKTGEYKPSPVNTLTRREVYL
Protein: Protocadherin 9 isoform 1 (Q2TJI0)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
RCRHASRFKAAQRSKQGAEWMSPNQENKQNKKKKRKKRKSPKSSLLNFVTIEESKPDDAVHEPINGTISLPAELEEQGIGRFDWGPAPPTTFKPNSPDLAKHYKSASPQPAFHLKPDTPVSVKKHHVIQELPLDNTFVGGCDTLSKRSSTSSDHFSASECSSQGGFKTKGPLHTRQVNEHFYWSISTAYKCPVNQY
Protein: GRIP1-associated protein 1 (GRASP-1) (HCMV-interacting protein) [Cleaved into: GRASP-1 C-terminal chain (30kDa C-terminus form)] (Q8VD04)
Organism: Mus musculus (Mouse)
Function: Regulates the endosomal recycling back to the neuronal plasma membrane, possibly by connecting early and late recycling endosomal domains and promoting segregation of recycling endosomes from early endosomal membranes. Involved in the localization of recycling endosomes to dendritic spines, thereby playing a role in the maintenance of dendritic spine morphology. Required for the activity-induced AMPA receptor recycling to dendrite membranes and for long-term potentiation and synaptic plasticity (By similarity).
Subcellular location: Early endosome membrane {ECO:0000250|UniProtKB:Q9JHZ4}; Peripheral membrane protein {ECO:0000305}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q9JHZ4}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9JHZ4}. Cell projection, axon {ECO:0000250|UniProtKB:Q9JHZ4}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9JHZ4}. Synapse {ECO:0000250|UniProtKB:Q9JHZ4}. Note=Localizes to recycling endosomal tubules that are emanating from early endosomes. {ECO:0000250|UniProtKB:Q9JHZ4}.
Interaction partners:
- Glutamate receptor-interacting protein 1
- Ras-related protein Rab-4B
- Syntaxin-12
- Vacuolar fusion protein CCZ1 homolog
- Ras-related protein Rab-4A
- Vacuolar protein sorting-associated protein 41 homolog
Sequence:
MAQALSEEEFQRMQTQLLELRTNNYQLSDELRKNGVELSSLRQKVAYLDKEFSKAQKALSKSKKAQEVEVLLSENEMLQAKLHSQEEDFRLQNSTLMAEFSKLCSQLEQLELENRQLKEGVPGAAGAHVDGELLRLQAENTALQKNMAALQERYGKEAVRPSAVGEGQGDPPGDVLPTPLAPMPLAEVELKWEMEREEKKLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKELLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEAEESLQQQQQEQEETLKLCREEHAAELKGKDEELQNVREQLQQAQEERDGHVKTISNLKQEVKDTVDGQRILEKKGSAVLKDLKRQLHLERKRADKLQERLQEILTNSKSRTGLEELVLSEMNSPSRTQTGDSSSVSSFSYREILKEKESSAIPARSLSSSPQAQPPRPAELSDEEVAELFQRLAETQQEKWMLEEKVKHLEVSSASMAEDLCRKSAIIETYVMDSRIDVSVAAGHTDRSGLGSVLRDLVKPGDENLREMNKKLQNMLEEQLTKNMHLHKDMEVLSQEIVRLSKECVGSPDPDLEPGEAN
Protein: Ankyrin repeat, SAM and basic leucine zipper domain-containing protein 1 (Germ cell-specific ankyrin, SAM and basic leucine zipper domain-containing protein) (Q8VD46)
Organism: Mus musculus (Mouse)
Function: Plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Its association with pi-bodies suggests a participation in the primary piRNAs metabolic process. Required prior to the pachytene stage to facilitate the production of multiple types of piRNAs, including those associated with repeats involved in regulation of retrotransposons. May act by mediating protein-protein interactions during germ cell maturation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12040005, ECO:0000269|PubMed:19730684}. Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. Specifically localizes to pi-bodies, a subset of the nuage which contains primary piRNAs.
Interaction partners:
- Piwi-like protein 2
- RNA helicase Mov10l1
- Tudor domain-containing protein 1
- ATP-dependent RNA helicase DDX4
- Putative ATP-dependent RNA helicase TDRD12
- Inactive peptidyl-prolyl cis-trans isomerase FKBP6
- Mitochondrial cardiolipin hydrolase
- ATP-dependent RNA helicase TDRD9
- Small RNA 2'-O-methyltransferase
- Tudor and KH domain-containing protein
Sequence:
MAAGTLRGLAVAGGGESSDSEDDGWDIGYLDRSSQKLKRSLPVEEKNETFKKALTTGDISLVKELLDSGINVDSSFRYGWTPLMYAASVANAELVRFLLDRGANASFDKDKLTILISACSARGSEEQVLKCVELLLSRNADPNTACRRLMTPIMYAARDGHTQVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVILKLLELGANKMLQTKDGRTPSEIAKRNKHLEIFNFLSLTLNPLEGKLQQLTKEETICKLLATDSDKEKDHIFSPYTAFGDLEIFLHGLGLEHMTDSLKEKDITLRHLLTMKKDELTKNGIASKDQQKILAALKELEVEEINFGKLPEVTKLEISGDEFLNFLLKLNKQCGHLITAVQNIITELPVNSHKIVLEWASPRNFTSVCEELVSNVEDLNEEVCRLKELIQKMQNERENDPTHIPLVEEVSTWKTRILKRSAVTVCGFGLLLFIGKLTLQRK
Protein: Anoctamin-2 (Transmembrane protein 16B) (Q9NQ90)
Organism: Homo sapiens (Human)
Function: Calcium-activated chloride channel (CaCC) which may play a role in olfactory signal transduction. Odorant molecules bind to odor-sensing receptors (OSRs), leading to an increase in calcium entry that activates CaCC current which amplifies the depolarization of the OSR cells, ANO2 seems to be the underlying chloride channel involved in this process. May mediate light perception amplification in retina.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20056604}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Calcium-activated chloride channel regulator 4
- Calcium-activated chloride channel regulator 2
- Calcium-activated chloride channel regulator 1
- Cyclic nucleotide-gated channel alpha-2
- Cyclic nucleotide-gated channel alpha-4
Sequence:
MATPGPRDIPLLPGSPRRLSPQAGSRGGQGPKHGQQCLKMPGPRAPGLQGGSNRDPGQPCGGESTRSSSVINNYLDANEPVSLEARLSRMHFHDSQRKVDYVLAYHYRKRGVHLAQGFPGHSLAIVSNGETGKEPHAGGPGDIELGPLDALEEERKEQREEFEHNLMEAGLELEKDLENKSQGSIFVRIHAPWQVLAREAEFLKIKVPTKKEMYEIKAGGSIAKKFSAALQKLSSHLQPRVPEHSNNKMKNLSYPFSREKMYLYNIQEKDTFFDNATRSRIVHEILKRTACSRANNTMGINSLIANNIYEAAYPLHDGEYDSPEDDMNDRKLLYQEWARYGVFYKFQPIDLIRKYFGEKIGLYFAWLGLYTSFLIPSSVIGVIVFLYGCATIEEDIPSREMCDQQNAFTMCPLCDKSCDYWNLSSACGTAQASHLFDNPATVFFSIFMALWATMFLENWKRLQMRLGYFWDLTGIEEEEERAQEHSRPEYETKVREKMLKESNQSAVQKLETNTTECGDEDDEDKLTWKDRFPGYLMNFASILFMIALTFSIVFGVIVYRITTAAALSLNKATRSNVRVTVTATAVIINLVVILILDEIYGAVAKWLTKIEVPKTEQTFEERLILKAFLLKFVNAYSPIFYVAFFKGRFVGRPGSYVYVFDGYRMEECAPGGCLMELCIQLSIIMLGKQLIQNNIFEIGVPKLKKLFRKLKDETEAGETDSAHSKHPEQWDLDYSLEPYTGLTPEYMEMIIQFGFVTLFVASFPLAPVFALLNNVIEVRLDAKKFVTELRRPDAVRTKDIGIWFDILSGIGKFSVISNAFVIAITSDFIPRLVYQYSYSHNGTLHGFVNHTLSFFNVSQLKEGTQPENSQFDQEVQFCRFKDYREPPWAPNPYEFSKQYWFILSARLAFVIIFQNLVMFLSVLVDWMIPDIPTDISDQIKKEKSLLVDFFLKEEHEKLKLMDEPALRSPGGGDRSRSRAASSAPSGQSQLGSMMSSGSQHTNV
Protein: E3 ubiquitin-protein ligase itt1 (EC 2.3.2.31) (RING finger protein itt1) (RING-type E3 ubiquitin transferase itt1) (Q9US46)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- tRNA-dihydrouridine
- Eukaryotic peptide chain release factor GTP-binding subunit
- Putative acyl carrier protein, mitochondrial
- E3 ubiquitin-protein ligase dbl4
- Eukaryotic peptide chain release factor subunit 1
Sequence:
MLEVEVESDNKHLVADELIALQSIYPEIHLDGNNYGRLNIPVNTESDYFLSFKSPDESTLTDTIVVRHFPDLVMEFFLPEAYPFNSPPTFFLKSSWLPLKQKRVLTSSLIKLWNEIHDCVLFDAIEHVRSIATIAFHLPTEMVFPGGFDDLKKEILAFDKNAKLLEFQIRKFQCNVCFDEFNGTDCFQLTRCGHVSCQSCLRDYYTMCIQEGMFSQIKCIDLDCGKDAPVLTLKELESIVGVQLTNRYKELEEKRRYENDSNIIFCPRSFCQGPSKRDPGQKLAICQKCDFAFCSFCQATWHGDLSPCKLEGDSKKLVEMYLNYQENEPEKALELEKRYGKRIIDRLVEQVKNDEEAEKWVLLNGQRCPTCDRVVERIDGCCHMNCLCGTHFCFLCGAYLMEQNPYKHFNDPVSSCYGMLFASAAEKQRFSENWT
Protein: OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 4 (OTU domain-containing protein 4) (EC 3.4.19.12) (Deubiquitinating enzyme OTU4) (Q8LBZ4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Hydrolase that can remove conjugated ubiquitin from proteins in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Cysteine protease with a preference for 'Lys-63' over 'Lys-48'-linked over 'Met-1' ubiquitin (UB) tetramers (e.g. Ub3 and Ub4) as substrates. Cleaves also RUB-GST fusion.
Subcellular location: Cytoplasm {ECO:0000305}. Note=Prediction of a peroxisomal location. {ECO:0000269|PubMed:15333753}.
Interaction partners:
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 9
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 11
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 10
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 2
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 7
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 6
- Putative OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 8
- At2g28120/F24D13.9
- Solute carrier family 35 protein
- Arginine-glutamic acid dipeptide repeat protein
Sequence:
MMICYSPITTCSRNAISIKRHLGSRLYGVVAHGSSKFSCYSLLSGLSRRHYTGFRVSVSNRPSSWHDKGLFGSVLINRPTVAPKEKLEVSFLSPEANMKCSKIESNMRNLYCYSRFAYTGVIVSLLVCYSSTSQSAYADSSRDKDANNVHHHSSDGKFHNGKRVYTDYSIIGIPGDGRCLFRSVAHGFCLRSGKLAPGEKMQRELADELRTRVADEFIQRRQETEWFVEGDFDTYVRQIRDPHVWGGEPELFMASHVLQMPITVYMKDDKAGGLISIAEYGQEYGKDDPIRVLYHGFGHYDALLLHESKASIPKSKL
Protein: Receptor-like protein kinase HERK 1 (EC 2.7.11.-) (Protein HERCULES RECEPTOR KINASE 1) (Q9LX66)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Receptor-like protein kinase required for cell elongation during vegetative growth, mostly in a brassinosteroid-(BR-) independent manner.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19383785, ECO:0000305|PubMed:17644812}; Single-pass type I membrane protein {ECO:0000269|PubMed:19383785, ECO:0000305|PubMed:17644812}.
Interaction partners:
- GPI-anchored protein LORELEI
- Cyclase-associated protein 1
- Protein WVD2-like 2
- Protein RALF-like 1
- GPI-anchored protein LLG1
- Rapid alkalinization factor 23
- Ferritin-4, chloroplastic
- GPI-anchored protein LLG2
- AT3g61540/F2A19_140
- GPI-anchored protein LLG3
Sequence:
MGIEKFETFILISTISILLCICHGFTPVDNYLINCGSPTNGTLMGRIFLSDKLSSKLLTSSKEILASVGGNSGSDIYHTARVFTEVSSYKFSVTRGRHWVRLYFNPFDYQNFKMGSAKFAVSSQSHVLLSDFTVTSSKVVKEYSLNVTTNDLVLTFTPSSGSFAFVNAIEVISIPDTLITGSPRFVGNPAQFPDMSMQGLETIHRVNMGGPLVASNNDTLTRTWVPDSEFLLEKNLAKSMSKFSTVNFVPGYATEDSAPRTVYGSCTEMNSADNPNSIFNVTWEFDVDPGFQYYFRFHFCDIVSLSLNQLYFNLYVDSMVAATDIDLSTLVDNTLAGAYSMDFVTQTPKGSNKVRVSIGPSTVHTDYPNAIVNGLEIMKMNNSKGQLSTGTFVPGSSSSSKSNLGLIVGSAIGSLLAVVFLGSCFVLYKKRKRGQDGHSKTWMPFSINGTSMGSKYSNGTTLTSITTNANYRIPFAAVKDATNNFDESRNIGVGGFGKVYKGELNDGTKVAVKRGNPKSQQGLAEFRTEIEMLSQFRHRHLVSLIGYCDENNEMILIYEYMENGTVKSHLYGSGLPSLTWKQRLEICIGAARGLHYLHTGDSKPVIHRDVKSANILLDENFMAKVADFGLSKTGPELDQTHVSTAVKGSFGYLDPEYFRRQQLTDKSDVYSFGVVLFEVLCARPVIDPTLPREMVNLAEWAMKWQKKGQLDQIIDQSLRGNIRPDSLRKFAETGEKCLADYGVDRPSMGDVLWNLEYALQLQEAVIDGEPEDNSTNMIGELPPQINNFSQGDTSVNVPGTAGRFEESSIDDLSGVSMSKVFSQLVKSEGR
Protein: Protein tweety homolog 3 (hTTY3) (Volume-regulated anion channel subunit TTYH3) (Q9C0H2)
Organism: Homo sapiens (Human)
Function: Probable large-conductance Ca(2+)-activated chloride channel. May play a role in Ca(2+) signal transduction.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15010458, ECO:0000269|PubMed:34385445}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MAGVSYAAPWWVSLLHRLPHFDLSWEATSSQFRPEDTDYQQALLLLGAAALACLALDLLFLLFYSFWLCCRRRKSEEHLDADCCCTAWCVIIATLVCSAGIAVGFYGNGETSDGIHRATYSLRHANRTVAGVQDRVWDTAVGLNHTAEPSLQTLERQLAGRPEPLRAVQRLQGLLETLLGYTAAIPFWRNTAVSLEVLAEQVDLYDWYRWLGYLGLLLLDVIICLLVLVGLIRSSKGILVGVCLLGVLALVISWGALGLELAVSVGSSDFCVDPDAYVTKMVEEYSVLSGDILQYYLACSPRAANPFQQKLSGSHKALVEMQDVVAELLRTVPWEQPATKDPLLRVQEVLNGTEVNLQHLTALVDCRSLHLDYVQALTGFCYDGVEGLIYLALFSFVTALMFSSIVCSVPHTWQQKRGPDEDGEEEAAPGPRQAHDSLYRVHMPSLYSCGSSYGSETSIPAAAHTVSNAPVTEYMSQNANFQNPRCENTPLIGRESPPPSYTSSMRAKYLATSQPRPDSSGSH
Protein: Surface protein (RevA1) (H7C7N3)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Interaction partners:
Sequence:
MRNKNIFKLFFAAMLFVMACKAYVEEKKEIDSLMEDVLALVNDSSGGKFKDYKDKINELKENLKDIGNAELKEKLLNLQNSFQDKLAAKLAALKAAKNTIENITDKDQDISKRKIWSEAKLVGVTVPLLGSNTSGNGDKMSKNAVEQIDKVIKFLEEGTN
Protein: Nuclear receptor coactivator 5 (NCoA-5) (Coactivator independent of AF-2) (CIA) (Q9HCD5)
Organism: Homo sapiens (Human)
Function: Nuclear receptor coregulator that can have both coactivator and corepressor functions. Interacts with nuclear receptors for steroids (ESR1 and ESR2) independently of the steroid binding domain (AF-2) of the ESR receptors, and with the orphan nuclear receptor NR1D2. Involved in the coactivation of nuclear steroid receptors (ER) as well as the corepression of MYC in response to 17-beta-estradiol (E2).
Subcellular location: Nucleus.
Interaction partners:
- Estrogen receptor beta
- E3 SUMO-protein ligase RanBP2
- Nuclear pore complex protein Nup205
- Nuclear pore complex protein Nup93
- Nuclear pore complex protein Nup155
- Nucleoporin p54
- Nuclear pore complex protein Nup214
- Protein SEC13 homolog
- Nuclear pore complex protein Nup107
- mRNA export factor RAE1
Sequence:
MNTAPSRPSPTRRDPYGFGDSRDSRRDRSPIRGSPRREPRDGRNGRDARDSRDIRDPRDLRDHRHSRDLRDHRDSRSVRDVRDVRDLRDFRDLRDSRDFRDQRDPMYDRYRDMRDSRDPMYRREGSYDRYLRMDDYCRRKDDSYFDRYRDSFDGRGPPGPESQSRAKERLKREERRREELYRQYFEEIQRRFDAERPVDCSVIVVNKQTKDYAESVGRKVRDLGMVVDLIFLNTEVSLSQALEDVSRGGSPFAIVITQQHQIHRSCTVNIMFGTPQEHRNMPQADAMVLVARNYERYKNECREKEREEIARQAAKMADEAILQERERGGPEEGVRGGHPPAIQSLINLLADNRYLTAEETDKIINYLRERKERLMRSSTDSLPGPISRQPLGATSGASLKTQPSSQPLQSGQVLPSATPTPSAPPTSQQELQAKILSLFNSGTVTANSSSASPSVAAGNTPNQNFSTAANSQPQQRSQASGNQPPSILGQGGSAQNMGPRPGAPSQGLFGQPSSRLAPASNMTSQRPVSSTGINFDNPSVQKALDTLIQSGPALSHLVSQTTAQMGQPQAPMGSYQRHY