wanglab/gogpt-training-data huggingface dataset:
Protein: Gustatory receptor for sugar taste 64a (P83293)
Organism: Drosophila melanogaster (Fruit fly)
Function: One of the few identified sugar gustatory receptors identified so far and which promotes the starvation-induced increase of feeding motivation. Required in combination with Gr64f to detect sucrose, maltose, and glucose.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Gustatory receptor for sugar taste 43a
- Gustatory receptor for bitter taste 66a
- Gustatory and pheromone receptor 33a
- Gustatory receptor for bitter taste 93a
- Gustatory and odorant receptor 63a
- Gustatory and pheromone receptor 32a
- Gustatory receptor for sugar taste 64f
Sequence:
MKGPNLNFRKTPSKDNGVKQVESLARPETPPPKFVEDSNLEFNVLASEKLPNYTNLDLFHRAVFPFMFLAQCVAIMPLVGIRESNPRRVRFAYKSIPMFVTLIFMIATSILFLSMFTHLLKIGITAKNFVGLVFFGCVLSAYVVFIRLAKKWPAVVRIWTRTEIPFTKPPYEIPKRNLSRRVQLAALAIIGLSLGEHALYQVSAILSYTRRIQMCANITTVPSFNNYMQTNYDYVFQLLPYSPIIAVLILLINGACTFVWNYMDLFIMMISKGLSYRFEQITTRIRKLEHEEVCESVFIQIREHYVKMCELLEFVDSAMSSLILLSCVNNLYFVCYQLLNVFNKLRWPINYIYFWYSLLYLIGRTAFVFLTAADINEESKRGLGVLRRVSSRSWCVEVERLIFQMTTQTVALSGKKFYFLTRRLLFGMAGTIVTYELVLLQFDEPNRRKGLQPLCA
Protein: IQ motif and SEC7 domain-containing protein 3 (Potential synaptic guanine nucleotide exchange factor for Arf) (SynArfGEF-Po) (Q76M68)
Organism: Rattus norvegicus (Rat)
Function: Acts as a guanine nucleotide exchange factor (GEF) for ARF1.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9UPP2}. Postsynaptic density {ECO:0000250|UniProtKB:Q3TES0}.
Interaction partners:
- Transmembrane protein 236
Sequence:
MESLLENPVRAVLYLKELTAIVQNQQSLIHTQRQRIDELERRLDELSAENRSLWEHQQLLQAQPPPGLVPPPSAPLPAPAATAPAATAAQEPLQDHGQLIPATPEPPLQHHGQLLAQPQPAPSSRVQTPQSPHQHPVAPGAVADKEKERPSSCCAAAGALLQHASPAALGKGVLSRRPKNETVLHQFCCPATDTEQKPACSDLASQSDGSCAQAGGGMEDSVVAAVAAGRPSAHAPKAQAPELQQEEERPGAVGSPRAGPLRAASPGQQQPALATALCSHTPAASEYELSLDLKNKQIEMLEHKYGGHLVSRRAACTIQTAFRQYQLSKNFEKIRNSLLESRLPRRISLRKVRAPTAESLVAEKALLESCGLLGLPLGRSPSLPPTFAGSLTELEDSFTEQVQSLAKSIDDALSTWSLKTMCSLQESGAYQLHQALHPSAGQPGLETEAAREPDSGPGSGDEAGSLPQGHSGTLMMAFRDVTVQIANQNISVSSSTALSVANCLGAQTAQATAEPAAVQTEQGDAATQEVSEVPASELMDPPVEDSEAAESGAQSAHEPTVAEAVVEEAVATEAEEEEEGAGQAGKGAEAEVGDNSEQLSSSSASTKSAKSGSEVSAAASKEALQAVILSLPRYHCENPASCRSPTLSTDTLRKRLYRIGLNLFNINPDKGIQFLISRGFIPDTPIGVAHFLLQRKGLSRQMIGEFLGNSKKQFNRDVLDCVVDEMDFSNMELDEALRKFQAHIRVQGEAQKVERLIEAFSQRYCMCNPEVVQQFHNPDTIFILAFAIILLNTDMYSPNIKPDRKMMLEDFIRNLRGVDDGADIPRELVVGIYERIQQKELKSNEDHVTYVTKVEKSIVGMKTVLSMPHRRLVCCSRLFEVTDVNKLQKQAAHQREVFLFNDLLVILKLCPKKKSSFTYTFCKAVGLLGMRFHLFENEYYSHGITLATPLSGSEKKQVLHFCALGSDEMQKFVEDLKESIAEVTELEQIRIEWELERQQGTKTLSARSAGAQGDPQSKQGSPTAKREAMAGEKATESSGEVSIHNRLQTFQHSPKLGVERGAPAPSPPTSPPPPLPPDPQPSPLREQPPPLPLPPPTPPGTLVQCQQIVKVIVLDKPCLARMEPLLSQALSCYASSSSDSCGSTPLRGPGSPVKVIHQPPLPPPPPPYNHPHQFCPPGSLLLRRRYSSGSRSLV
Protein: Fumarate reductase (CoM/CoB) subunit A (EC 1.3.4.1) (Thiol:fumarate reductase subunit A) (D9PU00)
Organism: Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Function: Catalyzes the reduction of fumarate with reduced coenzyme M (CoM-S-H) and coenzyme B (CoB-S-H). In vitro, is able to reduces fumarate with reduced benzyl viologen, oxidize CoM-S-H and CoB-S-H to CoM-S-S-CoB with methylene blue, and reduce CoM-S-S-CoB with reduced benzyl viologen. The enzyme has specificity for the two thiol compounds as the CoB--CoM heterodisulfide reductase. The enzyme is very sensitive to oxygen.
Subcellular location: Cytoplasm {ECO:0000303|PubMed:2499256}.
Interaction partners:
- Fumarate reductase
- Predicted NADH dehydrogenase
- Succinate--CoA ligase subunit beta
- Succinate--CoA ligase subunit alpha
- Fumarate hydratase
- Fumarase related protein
- Predicted fumarate hydratase
- Predicted fumarate hydratase
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
- Indolepyruvate oxidoreductase subunit IorA
Sequence:
MESELYECDVLIIGSGGAGCRAAIEVSEHKLTPIIVSKGLSFKSGCTGMAEGGYNAAFACVDPEDSPDVHFEDTMRGGGFINDPRLVRILVDEAPDRLRDLEEYGALFDRQESGLLDQRPFGGQTYRRTCYHGDRTGHEMITALKEEVIRRDIETIDEVMITSLLVEDGSVLGAMGVSIMNSEPVAFRASSTILASGGAGHIYPVTSNTMQKGGDGFAIAWKAGADLIDMEQVQFHPTGMVYPESRRGVLVTEAVRGEGGILLNSEGERFMGRYDPRGELATRDVVARAIYTEIMEGRGTENGGVYLDVSHLPDEVIEEKLETMLLQFLDVGVDIRSEPMEVAPTAHHFMGGVRIDEWGRTNLKNLFAAGEVSGGVHGANRLGGNALADTQVFGRRAGISAAKNAMSSSRRHVRSLIEEEEQRIKDMVRDGSIRPAEIRDELHEAMWSDVAIVRSRRSLESAMSRISTLMDKLGDLDVPETGGFNSNLLEALELENMLITASLVTRSALIREESRGSHYREDFPETRPEWKRSILLNRKMEPQFIGR
Protein: Probable conserved transmembrane protein (O06422)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable conserved lipoprotein LpqU
- 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
- Uncharacterized protein Rv3630
- Fluoride-specific ion channel FluC 1
- Probable conserved membrane protein
- Possible lipoprotein LpqQ
- Putative non-heme bromoperoxidase BpoC
- Possible conserved transmembrane protein
- GDP-mannose-dependent alpha-mannosyltransferase
- Probable conserved integral membrane protein
Sequence:
MISPKPLLHILIHGLSDELPDTRGRIVLRWLRIAVLIVTGLVTLQSVLLVAGAWRNDIAIQRNMGVAQAEVLSAGPRRSTIEFVTPDRITYRPQLGVLYPSELSTGMRIYVEYNKRDPNLVRVQHRNAGLAIIPAGSIAVVAWLIAAAALVVLAVLDKRLERRENSASATG
Protein: Adenine deaminase (Adenase) (Adenine aminase) (EC 3.5.4.2) (Q72EX7)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Hypoxanthine phosphoribosyltransferase
- Purine nucleoside phosphorylase
Sequence:
MTYRPLLNDLVDMAAGRAPVDLVVRNARIVDVFSQRIVEAPLAIGGGRFLGFFEAEAHATLDAEGRYLLPGLIDGHVHIESSLVSPAQFARLVLARGTTAVIADPHEIANVCGLAGLRYMLDATRDLPLDVRLALPSCVPATPFENAGAVLDAAALATLMDDPRVAGLGEMMNFPGVLAGDADVLDKIALALDRGKTVDGHSPGLAGRDLATYAAARIATDHECTTVDEMHERIALGMYVLLREGSAARDMARLAPGITPGNARRCVFCTDDRQPADILRDGHIDNHLRIAVSHGVDPVTAVTIATLNAAECFGLRDRGAVAPGRVADFVLVDDLTGFAVRKVYAAGRLVARDGAVVVDLPDHADPAVRDTVNIRPLDDTAFRLPLPTGLARVIGLQPHSLLTDALERDVPRDASGCFTPGDGLVKLAVVERHKATGNVGVGIIEGYGLRGGAVATTVAHDSHNIVVAGDNDADMLVAVRELERTGGGITLCAGGRVLASLPLPVAGLMSDRPATEVSATFAQMLSIAHETLHISRDIEPFMTLSFLTLPVIPALKLTDRGLFDVRTFSFTTVGV
Protein: Low molecular weight phosphotyrosine protein phosphatase (EC 3.1.3.48) (Low molecular weight cytosolic acid phosphatase) (EC 3.1.3.2) (PTPase) (Small tyrosine phosphatase) (P41893)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May contribute to dephosphorylation of 'Tyr-15' of cdc2.
Subcellular location: Cytoplasm.
Interaction partners:
- Probable FAD synthase
- Probable acid phosphatase SPBC4.06
- Alkaline phosphatase
- Riboflavin kinase
- Putative hydroxymethylpyrimidine/phosphomethylpyrimidine kinase C18B5.05c
- Putative hydroxymethylpyrimidine/phosphomethylpyrimidine kinase 1
- Putative hydroxymethylpyrimidine/phosphomethylpyrimidine kinase 2
- Riboflavin synthase
- Probable thiamine biosynthetic bifunctional enzyme
- Acid phosphatase
Sequence:
MTKNIQVLFVCLGNICRSPMAEAVFRNEVEKAGLEARFDTIDSCGTGAWHVGNRPDPRTLEVLKKNGIHTKHLARKLSTSDFKNFDYIFAMDSSNLRNINRVKPQGSRAKVMLFGEYASPGVSKIVDDPYYGGSDGFGDCYIQLVDFSQNFLKSIA
Protein: Caveolin-3 (P51638)
Organism: Rattus norvegicus (Rat)
Function: May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. May also regulate voltage-gated potassium channels. Plays a role in the sarcolemma repair mechanism of both skeletal muscle and cardiomyocytes that permits rapid resealing of membranes disrupted by mechanical stress. Mediates the recruitment of CAVIN2 and CAVIN3 proteins to the caveolae.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:24567387, ECO:0000269|PubMed:26497963}; Peripheral membrane protein {ECO:0000250}. Membrane, caveola {ECO:0000250|UniProtKB:P51637}; Peripheral membrane protein {ECO:0000250}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P51637}. Note=Potential hairpin-like structure in the membrane. Membrane protein of caveolae (By similarity). {ECO:0000250}.
Interaction partners:
- Caveolin-2
- Dysferlin
- Proto-oncogene tyrosine-protein kinase Src
- Dystrophin
- Caveolin-1
- Tripartite motif-containing protein 72
- Calmodulin-1
- Calmodulin-like protein 3
- Calmodulin-like protein 4
- Tyrosine-protein kinase Fyn
Sequence:
MMTEEHTDLEARIIKDIHCKEIDLVNRDPKNINEDIVKVDFEDVIAEPEGTYSFDGVWRVSYTTFTVSKYWCYRLLSTLLGVPLALLWGFLFACISFCHIWAVVPCIKSYLIEIQCISHIYSLCIRTFCNPLFAALGQVCSNIKVVLRREG
Protein: Tripartite motif-containing protein 2 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRIM2) (RING-type E3 ubiquitin transferase TRIM2) (D3ZQG6)
Organism: Rattus norvegicus (Rat)
Function: UBE2D1-dependent E3 ubiquitin-protein ligase that mediates the ubiquitination of NEFL and of phosphorylated BCL2L11. Plays a neuroprotective function. May play a role in neuronal rapid ischemic tolerance. Plays a role in antiviral immunity and limits New World arenavirus infection independently of its ubiquitin ligase activity.
Interaction partners:
- Polyubiquitin-C
Sequence:
MASEGASIPSPVVRQIDKQFLICSICLERYKNPKVLPCLHTFCERCLQNYIPAHSLTLSCPVCRQTSILPEKGVAALQNNFFITNLMDVLQRTPGSNGEDPSILQTVTAVAAGKPLSCPNHDGNVMEFYCQSCETAMCRECTEGEHAEHPTVPLKDVVEQHKASLQVQLDAVNKRLPEIDSALQFISEIIHQLTNQKASIVDDIHSTFDELQKTLNVRKSVLLMELEVNYGLKHKVLQSQLDTLLQGQESIKSCSNFTAQALNHGTETEVLLVKKQMSEKLNELADQDFPLHPRENDQLDFIVETEGLKKSIHNLGTILTTNAVASETVATGEGLRQTIIGQPMSVTITTKDKDGELCKTGNAYLTAELSTPDGSVADGEILDNKNGTYEFLYTVQKEGDFTLSLRLYDQHIRGSPFKLKVIRSADVSPTTEGVKRRVKSPGSGHVKQKAVKRPASMYSTGKRKENPIEDDLIFRVGTKGRNKGEFTNLQGVAASTSGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIADYDNKWVSIFSNDGKFKTKIGSGKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFAGPHFAAVNSSNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSYINTSADPLYGPQGLALTSDGHVVVADSGNHCFKVYRYLQ
Protein: PML-like coiled-coil domain-containing protein (Q8BSJ6)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
YASDQEVLDMHSFLRKALCSLRQEEPQNQKVQLLTRGFEEFKLCLQDFISCITQRINAAVASPEAASNQPEAASTHPVTTSTPEDLEQPKEVQSVQAQALELSKTQPVAMVKTVPGAHPVPVYAFSMQGPTYREEASQTVGSMKRKCSHEDCSRKIIKMESTEENEDRLATSSPEQSWPSTFKATSPPHLDGTSNPESTVPEKKILLPNNNHVTSDTGETEERVVVISSSEDSDTENLSSHELDDSSSESSSLQLEGPNSLKALDESLAEPHLEDRTLVFFDLKIDNETQKISQLAAVNRESKFRVLIQPEAFSVYSKAVSLEAGLRHFLSFLTTMHRPILACSRLWGPGLPIFFQTLSDINKLWEFQDTISGFLAVLPLIRERIPGASSFKLGNLAKTYLARNMSERSALASVLAMRDLCCLLEISPGLPLAQHIYSFSSLQCFASLQPLIQASVLPQSEARLLALHNVSFVELLNAYRTNRQEGLKKYVHYLSLQTTPLSSSASTQVAQFLQALSTHMEGLLEGHAPAGAEGKAESKGCLA
Protein: Malolactic enzyme (MLE) (EC 4.1.1.101) (F9UMS6)
Organism: Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) (Lactobacillus plantarum)
Function: Involved in the malolactic fermentation (MLF) of wine, which results in a natural decrease in acidity and favorable changes in wine flavors. Catalyzes the decarboxylation of L-malate to L-lactate.
Interaction partners:
- L-lactate dehydrogenase 1
- Fumarate hydratase class II
- Malate transport protein
- L-2-hydroxyisocaproate dehydrogenase
- L-2-hydroxyisocaproate dehydrogenase
- L-lactate dehydrogenase 2
- L-2-hydroxyisocaproate dehydrogenase
- Malic enzyme, NAD-dependent
- Lactate racemase
- L
Sequence:
MTKTASEILNNPFLNKGTAFTKEERQALGLTGTLPSKVQTIDEQATQAYAQFKSKPSRLEQRIFLMNLFNENRTLFFHLMDEHVVEFMPIVYDPVVADSIEQYNELFLDPQNAAFVSVDAPEDIEATLKNAADGRDIRLVVVTDAEGILGMGDWGVNGVDIAIGKLMVYTAAAGIDPSQVLPVSIDAGTNNQKLLDDPLYLGNRHKCVSGEQYYDVIDKFVAAEQQLFPDSLLHFEDFGRDNAQVILDKYKDQIATFNDDIQGTGMVVLAGILGALNISKESIKDQKILSFGAGTAGMGIANQILDELMQAGLTEEEAKQHFYAVDKQGLLFDDTEGLTPAQKAFTRKRSEFSNADELTNLEAVVKAVHPTVMIGTSTQPGTFTESIIKEMAAHTERPIIFPLSNPTKLAEAKAEDLIKWTDGRALVATGIPADDVEYKGVTYQIGQGNNALMYPGLGFGLIASTAKVLNAETLSAACHALGGIVDTSKPGAAVLPPVAKITEFSQKLAEVVAQSVIDQKLNKEPIADAKQAVADMKWVPEYRAISK
Protein: Phosphoprotein (Protein P) (P03422)
Organism: Measles virus (strain Edmonston) (MeV) (Subacute sclerose panencephalitis virus)
Function: Essential component of the RNA polymerase and the nascent chain assembly complex. Also required during RNA synthesis.
Interaction partners:
Sequence:
MAEEQARHVKNGLECIRALKAEPIGSLAIEEAMAAWSEISDNPGQERATCREEKAGSSGLSKPCLSAIGSTEGGAPRIRGQGPGESDDDAETLGIPPRNLQASSTGLQCYYVYDHSGEAVKGIQDADSIMVQSGLDGDSTLSGGDNESENSDVDIGEPDTEGYAITDRGSAPISMGFRASDVETAEGGEIHELLRLQSRGNNFPKLGKTLNVPPPPDPGRASTSGTPIKKGTERRLASFGTEIASLLTGGATQCARKSPSEPSGPGAPAGNVPECVSNAALIQEWTPESGTTISPRSQNNEEGGDYYDDELFSDVQDIKTALAKIHEDNQKIISKLESLLLLKGEVESIKKQINRQNISISTLEGHLSSIMIAIPGLGKDPNDPTADVEINPDLKPIIGRDSGRALAEVLKKPVASRQLQGMTNGRTSSRGQLLKEFQLKPIGKKMSSAVGFVPDTGPASRSVIRSIIKSSRLEEDRKRYLMTLLDDIKGANDLAKFHQMLMKIIMK
Protein: PDGF- and VEGF-receptor related, isoform J (EC 2.7.10.1) (E1JHB7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
- LD28763p
- PDGF- and VEGF-related factor 2
- FI06402p
- Pi3K21B, isoform B
- Epidermal growth factor receptor
- DShc protein
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma
- Growth factor receptor-bound protein 2
- phosphatidylinositol 3-kinase
Sequence:
MAMLPRLILLPLLLILRISWSDAVPLQQFSPDPDDSIENCGGENGAPLMTPCKSAIILDAQTSTTLKCEDDEPMSWWTSQSQYVHVKSFDNTEDPARPFGTSLHLIEVTADYVAAYYCVKTSKFSQIAKEEQSDEAMIELVNQGYASSIYVYVNDPDTKLVDSHNVVTARQYTDVVIPCKPAMPDTEVLLETSNGEMHSSKSVGRYDPQRGFTIEIRSIVDGGDYYCRPNPPFPHNEEEMTSIEVRFIATGLDIPRTQTTNMVYTYAPGVTDGDDEVLTVTNQSTGNLALIRGGDGTLSRERARRSPARLAPMNASPSPRPGQDGKPLPKPVIRSSVEHHVFTDTNFTLDCEQSAYVESVYGMEWFTPSRDENRIFASQSRTDPKTRNSTHQTGRSTLTVLNAQPSDTGLYKCVTTDNSNQNVQRATYRIKVLKQNESYLNVGEPSGHYNVQEYANRTIQMTANFEGFPTPSFSWFKPDGTEVRQSENNFKILSTELSTMLQVLNAQLQDSGTYVLRGSNSFGVVQREYNVSVMDAPALKMSDAYVQVGSVARLECTVRSYPPAIVTFFFRPCSLEPQWPTCSVLNQNFSLPSEQEKYQFQTRPRPGKLSVERIYEVSFLPTEPGILTCIAQNIIDGKERRTLTKAHVLLGNISENMTIYGFDKDHKIAKEDNVNFTCEALAYHFDGNLKWFINGEDLKESDSVHIETSHTKYSYKSTVHITTISDRDRGTYECRAYHNDKDAVYSSREIDLYVHDPSAPQWTNGGQEGHSKIKRKLSQTLELECASTAVPVAIVRWFKDDKEVTESKLRHIIEKESKLLITHLYPGDEGVYKCVVENRLDRIERSFTVVISDLPGISMAWVWFGVILFLILIGLCVFLAVRYQKEHKRHLALKAAGLANFEEGAVGHINPDLTLDEQAELLPYNREFEFPRENLKLGKQLGAGAFGVVLKGEAKGIRREEPTTTVAVKMVKATADNEVVRALVSELKIMVHLGQHLNVVNLLGAVTKNIAKRELMVIVEYCRFGNIQNFLLRNRKCFINQINPDTDHIDPSIMTQRMSDNYELHRDTNGGGLKYANVGFPIHSYINEPHNNNTQPPTHRRNSDNDPRSGTRAGRTGSGTATYSYDRQMDTCATVMTTVPEDDQIMSNNSVQPAWRSNYKTDSTEAMTVTTVDLISWAFQVARGMDYLSSKKVLHGDLAARNILLCEDNVVKICDFGLARSMYRGDNYKKSENGKLPIKWLALESLSDHVFSTYSDVWSYGIVLWEMFSLAKVPYPGIDPNQELFNKLNDGYRMEKPKFANQELYEIMLECWRKNPESRPLFAELEKRFANMLGEDVASHYLDLNNPYMQSNIEYMKKQSTDYLALMGSPDELAPAAPRYVNGHIVPDIRIEELPDDYMEMSRDSDPDACTAIFSPTRLEGESSDFPDFSSETTFNFPGARQSPTLSNNLNSGSSKPLRKKNGMPTVDVADQAPEEIPMLHRSSTGSDGSPEQGRRFNQALKQQYVTPTPSPRHHVETKLNGEPSENYVNMKPPRKNIPGKTTTGGGGAAAGASTEAFSNPSYQPLSTVNEKEQRRY
Protein: Sodium channel regulatory subunit beta-3 (Q8BHK2)
Organism: Mus musculus (Mouse)
Function: Modulates channel gating kinetics. Causes unique persistent sodium currents. Inactivates the sodium channel opening more slowly than the subunit beta-1. Its association with NFASC may target the sodium channels to the nodes of Ranvier of developing axons and retain these channels at the nodes in mature myelinated axons (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9NY72}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9NY72}.
Interaction partners:
- Sodium channel regulatory subunit beta-2
- Sodium channel regulatory subunit beta-4
- Sodium channel protein type 5 subunit alpha
- Sodium channel protein type 4 subunit alpha
- Sodium channel protein type 3 subunit alpha
- Sodium channel protein type 2 subunit alpha
- Sodium channel protein type 9 subunit alpha
- Sodium channel protein type 8 subunit alpha
- Sodium channel protein type 1 subunit alpha
- Sodium channel protein type 10 subunit alpha
Sequence:
MPAFNRLLPLASLVLIYWVRVCFPVCVEVPSETEAVQGNSMKLRCISCMKREEVEATTVVEWFYRPEGGKDFLIYEYRNGHQEVESPFQGRLQWNGSKDLQDVSITVLNVTLNDSGLYTCNVSREFEFEAHRPFVKTTRLIPLRVTEEAGEDFTSVVSEIMMYILLVFLTLWLFIEMIYCYRKVSKAEEAAQENASDYLAIPSENKENSVVPVEE
Protein: Translation initiation factor eIF2B subunit gamma (eIF2B GDP-GTP exchange factor subunit gamma) (Q9NR50)
Organism: Homo sapiens (Human)
Function: Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P56288}.
Interaction partners:
- Eukaryotic translation initiation factor 2 subunit 2
- Eukaryotic translation initiation factor 2 subunit 1
- Translation initiation factor eIF2B subunit alpha
- Eukaryotic translation initiation factor 2 subunit 3
- Translation initiation factor eIF2B subunit beta
- Translation initiation factor eIF2B subunit delta
- Translation initiation factor eIF2B subunit epsilon
- Guanine nucleotide exchange factor MSS4
- dTDP-D-glucose 4,6-dehydratase
- CUB domain-containing protein 2
Sequence:
MEFQAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTRDVQKALCAEFKMKMKPDIVCIPDDADMGTADSLRYIYPKLKTDVLVLSCDLITDVALHEVVDLFRAYDASLAMLMRKGQDSIEPVPGQKGKKKAVEQRDFIGVDSTGKRLLFMANEADLDEELVIKGSILQKHPRIRFHTGLVDAHLYCLKKYIVDFLMENGSITSIRSELIPYLVRKQFSSASSQQGQEEKEEDLKKKELKSLDIYSFIKEANTLNLAPYDACWNACRGDRWEDLSRSQVRCYVHIMKEGLCSRVSTLGLYMEANRQVPKLLSALCPEEPPVHSSAQIVSKHLVGVDSLIGPETQIGEKSSIKRSVIGSSCLIKDRVTITNCLLMNSVTVEEGSNIQGSVICNNAVIEKGADIKDCLIGSGQRIEAKAKRVNEVIVGNDQLMEI
Protein: Epoxide hydrolase 2 (E5RFH6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTLRAAVFDLDGVLALPAVFGVLGRTEEALALPRGLLNDAFQKGGPEGATTRLMKGEITLSQPRVRLHFVELGSGPAVCLCHGFPESWYSWRYQIPALAQAGYRVLAMDMKGYGESSAPPEIEEYCMEVLCKEMVTFLDKLGLSQAVFIGHDWGGMLVWYMALFYPERVRAVASLNTPFIPANPNMSPLESIKANPVFDYQLYFQEPGVAEAELEQNLSRTFKSLFRASDESVLSMHKVCEAGGLFVNSPEEPSLSRMVTEEEIQFYVQQFKKSGFRGPLNWYRNMERNWKWACKSLGRKILIPALMVTAEKDFVLVPQMSQHMEDWIPHLKRGHIEDCGHWTQMDKPTEVNQILIKWLDSDARNPPVVSKM
Protein: GTP-binding protein Rhes (Ras homolog enriched in striatum) (SE6C) (P63033)
Organism: Rattus norvegicus (Rat)
Function: GTPase signaling protein that binds to and hydrolyzes GTP. Regulates signaling pathways involving G-proteins-coupled receptor and heterotrimeric proteins such as GNB1, GNB2 and GNB3. May be involved in selected striatal competencies, mainly locomotor activity and motor coordination.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14724584, ECO:0000269|PubMed:19498170}; Lipid-anchor {ECO:0000269|PubMed:14724584, ECO:0000269|PubMed:19498170}. Note=Found in granular structures throughout the cytosol.
Interaction partners:
- Huntingtin
- Beclin-1
Sequence:
MMKTLSSGNCTLNVPAKNSYRMVVLGASRVGKSSIVSRFLNGRFEDQYTPTIEDFHRKVYNIHGDMYQLDILDTSGNHPFPAMRRLSILTGDVFILVFSLDSRESFDEVKRLQKQILEVKSCLKNKTKEAAELPMVICGNKNDHSELCRQVPAMEAELLVSGDENCAYFEVSAKKNTNVNEMFYVLFSMAKLPHEMSPALHHKISVQYGDAFHPRPFCMRRTKVAGAYGMVSPFARRPSVNSDLKYIKAKVLREGQARERDKCSIQ
Protein: F-box/WD repeat-containing protein 1A (E3RSIkappaB) (Epididymis tissue protein Li 2a) (F-box and WD repeats protein beta-TrCP) (pIkappaBalpha-E3 receptor subunit) (Q9Y297)
Organism: Homo sapiens (Human)
Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes and binds to phosphorylated target proteins. SCF(BTRC) mediates the ubiquitination of CTNNB1 and participates in Wnt signaling. SCF(BTRC) mediates the ubiquitination of phosphorylated NFKB1, ATF4, CDC25A, DLG1, FBXO5, PER1, SMAD3, SMAD4, SNAI1 and probably NFKB2. SCF(BTRC) mediates the ubiquitination of NFKBIA, NFKBIB and NFKBIE; the degradation frees the associated NFKB1 to translocate into the nucleus and to activate transcription. Ubiquitination of NFKBIA occurs at 'Lys-21' and 'Lys-22'. SCF(BTRC) mediates the ubiquitination of CEP68; this is required for centriole separation during mitosis. SCF(BTRC) mediates the ubiquitination and subsequent degradation of nuclear NFE2L1 (By similarity). Has an essential role in the control of the clock-dependent transcription via degradation of phosphorylated PER1 and PER2. May be involved in ubiquitination and subsequent proteasomal degradation through a DBB1-CUL4 E3 ubiquitin-protein ligase. Required for activation of NFKB-mediated transcription by IL1B, MAP3K14, MAP3K1, IKBKB and TNF. Required for proteolytic processing of GLI3. Mediates ubiquitination of REST, thereby leading to its proteasomal degradation. SCF(BTRC) mediates the ubiquitination and subsequent proteasomal degradation of KLF4; thereby negatively regulating cell pluripotency maintenance and embryogenesis (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q3ULA2}. Nucleus {ECO:0000250|UniProtKB:Q3ULA2}.
Interaction partners:
- S-phase kinase-associated protein 1
- Catenin beta-1
- NF-kappa-B inhibitor alpha
- E3 ubiquitin-protein ligase RBX1
- Cullin-1
- Axin-1
- Glycogen synthase kinase-3 beta
- S-phase kinase-associated protein 2
- Adenomatous polyposis coli protein
- F-box/WD repeat-containing protein 11
Sequence:
MDPAEAVLQEKALKFMCSMPRSLWLGCSSLADSMPSLRCLYNPGTGALTAFQNSSEREDCNNGEPPRKIIPEKNSLRQTYNSCARLCLNQETVCLASTAMKTENCVAKTKLANGTSSMIVPKQRKLSASYEKEKELCVKYFEQWSESDQVEFVEHLISQMCHYQHGHINSYLKPMLQRDFITALPARGLDHIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKLIERMVRTDSLWRGLAERRGWGQYLFKNKPPDGNAPPNSFYRALYPKIIQDIETIESNWRCGRHSLQRIHCRSETSKGVYCLQYDDQKIVSGLRDNTIKIWDKNTLECKRILTGHTGSVLCLQYDERVIITGSSDSTVRVWDVNTGEMLNTLIHHCEAVLHLRFNNGMMVTCSKDRSIAVWDMASPTDITLRRVLVGHRAAVNVVDFDDKYIVSASGDRTIKVWNTSTCEFVRTLNGHKRGIACLQYRDRLVVSGSSDNTIRLWDIECGACLRVLEGHEELVRCIRFDNKRIVSGAYDGKIKVWDLVAALDPRAPAGTLCLRTLVEHSGRVFRLQFDEFQIVSSSHDDTILIWDFLNDPAAQAEPPRSPSRTYTYISR
Protein: Frizzled homolog 2 (Frizzled-2) (Q90YL7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MQASGSVCVFLALLLPCCFVASGQHQGDNGIAVPDHGFCQPITIPLCTDIAYNQTIMPNLVGHYNQEDAGLEVHQFYPLVKVQCSPELKFFLCSMYAPVCTVLEKAIPPCRSICERAKQGCEVLMNKFGFQWPEALRCEHFPVLGDGHICVGQNDSMATVSPVHMPIPGTPSVQLYSTPDKPFRCPSTLKVPAYLSYKFLGEPDCGAPCESSRTHRAYMFFTDQEIEFARIWILIWSSLCCASTLFTVTTYIVDMQRFKYPERPIIFLSGCYTMVSIAYIAGYFLGDKVVCNESFFPDSYKTIVQGTKKEGCTILFMMLYFFSMASSIWWVILSLTWFLAAGMKWGHEAIEANSQYFHLAAWAVPAVKTISILAMGQIDGDVLSGVCFVGLNNSDALRGFILAPLFLYLFIGTSFLLAGFVSLFRIRTIMKHDGTKTEKLERLMVRIGVFSVLYTVPATIVIACFFYEQAFRQQWEKSWISMNCKSLAIPCPMQPAPHMTPDFTVFMIKYLMTLIVGITSGFWIWSGKTLHSWQKFYVRLTSAGQGETTV