wanglab/gogpt-training-data huggingface dataset:
Protein: Sex determination protein fruitless (Q8IN81)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probably acts as a transcriptional regulator. Part of the somatic sex determination hierarchy; sex determination genes transformer (tra) and transformer-2 (tra-2) switch fru splicing from the male-specific pattern to the female-specific pattern through activation of the female-specific fru 5'-splice site. Vital for the development of males and females. Controls the development of the male specific abdominal muscle of Lawrence. Plays a role in male courtship behavior and sexual orientation. Enhances male-specific expression of takeout in brain-associated fat body.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein doublesex
- Female-specific protein transformer
- Transformer-2 sex-determining protein
- Protein sex-lethal
Sequence:
MMATSQDYFGNPYALFRGPPTTLRPRESPLGVGHPHGHGHLHSHAHAHGHGHAHSHYAALDLQTPHKRNIETDVRAPPPPLPPPPLPLPPASPRYNTDQGAMDQQFCLRWNNHPTNLTGVLTSLLQREALCDVTLACEGETVKAHQTILSACSPYFETIFLQNQHPHPIIYLKDVRYSEMRSLLDFMYKGEVNVGQSSLPMFLKTAESLQVRGLTDNNNLNYRSDCDKLRDSAASSPTGRGPSNYTGGLGGAGGVADAMRESRDSLRSRCERDLRDELTQRSSSSMSERSSAAAAAAAAAAAVAAAGGNVNAAAVALGLTTPTGGERSPSVGSASAAAAAAAVAAAVAAAANRSASADGCSDRGSERGTLERTDSRDDLLQLDYSNKDNNNSNSSSTGGNNNNNNNNNNNSSSNNNNSSSNRERNNSGERERERERERERDRDRELSTTPVEQLSSSKRRRKNSSSNCDNSLSSSHQDRHYPQDSQANFKSSPVPKTGGSTSESEDAGGRHDSPLSMTTSVHLGGGGGNVGAASALSGLSQSLSIKQELMDAQQQQQHREHHVALPPDYLPSAALKLHAEDMSTLLTQHALQAADARDEHNDAKQLQLDQTDNIDGRVKCFNIKHDRHPDRELDRNHREHDDDPGVIEEVVVDHVREMEAGNEHDPEEMKEAAYHATPPKYRRAVVYAPPHPDEEAASGSGSDIYVDGGYNCEYKCKELNMRAIRCSRQQHMMSHYSPHHPHHRSLIDCPAEAAYSPPVANNQAYLASNGAVQQLDLSTYHGHANHQLHQHPPSATHPSHSQSSPHYPSASGAGAGAGSVSVSIAGSASGSATSAPASVATSAVSPQPSSSSTGSTSSAAAVAAAAAAAANRRDHNIDYSTLFVQLSGTLPTLYRCVSCNKIVSNRWHHANIHRPQSHECPVCGQKFTRRDNMKAHCKIKHADIKDRFFSHYVHM
Protein: Zinc finger protein BRUTUS (Protein EMBRYO DEFECTIVE 2454) (Q8LPQ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential protein. Negatively regulates the response to iron deficiency and thus contributes to iron homeostasis. Exhibits E3 ubiquitin-protein ligase activity in vitro. Plays a role in root growth, rhizosphere acidification, and iron reductase activity in response to iron deprivation. Facilitates 26S proteasome-mediated degradation of PYEL proteins in the absence of iron.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000269|PubMed:24253678, ECO:0000269|PubMed:25452667}.
Interaction partners:
- Transcription factor bHLH47
- Transcription factor bHLH115
- Transcription factor ORG3
- Transcription factor bHLH104
- Transcription factor bHLH101
- Transcription factor ORG2
- Transcription factor ILR3
- Oligopeptide transporter 3
- Transcription factor bHLH100
- AT5g05250/K18I23_5
Sequence:
MATPLPDFETARGGGAVASSSTTVLPSSVSSSSSSSRPLPVANSFSDDAEEISPILIFLFFHKAVCSELEALHRLALEFATGHHVDLRLLRERYRFLRSIYKHHCNAEDEVIFSALDIRVKNVAQTYSLEHKGESNLFDHLFELLNSATETDESYRRELARSTGALQTSVSQHLAKEQKQVFPLLIEKFKYEEQAYIVWRFLCSIPVNMLAVFLPWISSSISVDESKEMQTCLKKIVPGEKLLQQVIFTWLGGKSNTVASCRIEDSMFQCCLDSSSSMLPCKASREQCACEGSKIGKRKYPELTNFGSSDTLHPVDEIKLWHKSINKEMKEIADEARKIQLSGDFSDLSAFDERLQYIAEVCIFHSLAEDKIIFPAVDGEFSFSEEHDEEENQFNEFRCLIENIKSAGASSTSAAEFYTKLCSHADQIMETIQRHFHNEEIQVLPLARKNFSFKRQQELLYQSLCIMPLRLIERVLPWLTASLTEDEAKNFLKNLQAGAPKSDVALVTLFSGWACKGRKAGECLSPNGNGLCPVKTLSNIKEVNLQSCNACASVPCTSRSTKSCCQHQDKRPAKRTAVLSCEKKTTPHSTEVANGCKPSGNGRSCCVPDLGVNNNCLELGSLPAAKAMRSSSLNSAAPALNSSLFIWEMDSNSFGTGHAERPVATIFKFHKAISKDLEFLDVESGKLIDCDGTFIRQFIGRFHLLWGFYKAHSNAEDDILFPALESKETLHNVSHSYTLDHKQEEKLFGDIYSVLTELSILHEKLQSDSMMEDIAQTDTVRTDIDNGDCNKKYNELATKLQGMCKSIKITLDQHIFLEELELWPLFDKHFSIQEQDKIVGRIIGTTGAEVLQSMLPWVTSALSEDEQNRMMDTWKQATKNTMFDEWLNECWKGSPDSSSTETSKPSPQKDNDHQEILDQSGELFKPGWKDIFRMNQNELEAEIRKVYQDSTLDPRRKDYLVQNWRTSRWIAAQQKLPKEAETAVNGDVELGCSPSFRDPEKQIYGCEHYKRNCKLRAACCDQLFTCRFCHDKVSDHSMDRKLVTEMLCMRCLKVQPVGPICTTPSCDGFPMAKHYCSICKLFDDERAVYHCPFCNLCRVGEGLGIDFFHCMTCNCCLGMKLVNHKCLEKSLETNCPICCEFLFTSSEAVRALPCGHYMHSACFQAYTCSHYTCPICGKSLGDMAVYFGMLDALLAAEELPEEYKNRCQDILCNDCERKGTTRFHWLYHKCGSCGSYNTRVIKSETIPPDCSTSS
Protein: Insulin-like growth factor-binding protein 4 (IBP-4) (IGF-binding protein 4) (IGFBP-4) (P22692)
Organism: Homo sapiens (Human)
Function: IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors.
Subcellular location: Secreted.
Interaction partners:
- Insulin-like growth factor 1
- Insulin-like growth factor 2
- Pappalysin-1
- Insulin-like growth factor-binding protein 1
- Low-density lipoprotein receptor-related protein 6
- Frizzled-8
- Pappalysin-2
- Bone marrow proteoglycan
Sequence:
MLPLCLVAALLLAAGPGPSLGDEAIHCPPCSEEKLARCRPPVGCEELVREPGCGCCATCALGLGMPCGVYTPRCGSGLRCYPPRGVEKPLHTLMHGQGVCMELAEIEAIQESLQPSDKDEGDHPNNSFSPCSAHDRRCLQKHFAKIRDRSTSGGKMKVNGAPREDARPVPQGSCQSELHRALERLAASQSRTHEDLYIIPIPNCDRNGNFHPKQCHPALDGQRGKCWCVDRKTGVKLPGGLEPKGELDCHQLADSFRE
Protein: F-box and leucine rich repeat protein 22 (H0YMQ4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MWPLLTMHITQLNRECLLHLFSFLDKDSRKSLARTCSQLHDVFEDPALWSLLHFRSLTELQKDNFLLGPALRSLSICWHSSRVQVCSIEDWLKSAFQRSICSRHESLVNDFLLRVCDRVRGLNDTVAPGT
Protein: Homeobox protein VEGA (Ventral homeobox) (Q9DG33)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MVKNFSVDWLAQSFHDSPVLEVQEPEKKTRPHVPCVVQPRPPTSYDKVYLQPKPKINKAELKTESSKETPAQVTPRNCSSPSFSENSGYSSGYESEAAASECASVEDGHDAEKDGATRRIRTKFTPEQIDKLEKIFNKHKYLDAGERVKTALKLGLSETQIRTWFQNRRMKLKREVQEMRADFLLPQMVLPPVIPVQYQCYDRQRLPFPPHGPLVQQMMMPLHPHHPHPQHHQLMMPRHHYY
Protein: Glutamate receptor subunit (Q24351)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034100}.
Interaction partners:
Sequence:
MRLCPVVIYAFIIIIGFLEGIIALGGDDRNEITVGAIFYENEKEIELSFDQAFREVNNMKFSELRFVTIKRYMPTNDSFLLQQITCELISNGVAAIFGPSSKAASDIVAQIANATGIPHIEYDLKLEATRQEQLNHQMSINVAPSLSVLSRAYFEIIKSNYEWRTFTLIYETPEGLARLQDLMNIQALNSDYVKLRNLADYADDYRILWKETDETFHEQRIILDCEPKTLKELLKVSIDFKLQGPFRNWFLTHLDTHNSGLRDIYNEDFKANITSVRLKVVDANPFERKKTRLTKVDQILGNQTMLPILIYDAVVLFASSARNVIRAMQPFHPPNRHCGSSSPWMLGAFIVNEMKTISEDDVEPHFKTENMKLDEYGQRIHFNLEIYKPTVNEPMMVWTPDNGIKKRLLNLELESAGTTQDFSEQRKVYTVVTHYEEPYFMMKEDHENFRGREKYEGYAWISLASFPSSWSSITEFMIVNGNGKYNPETKQWDGIIRKLIDHHAQIGVCDLTITQMRRSVVDFTVPFMQLGISILHYKSPPEPKNQFAFLEPFAVEVWIYMIFAQLIMTLAFVFIARLSYREWLPPNPAIQDPDELENIWNVNNSTWLMVGSIMQQGCDILPRGPHMRILTSMWWFFALMMLSTYTANLAFLTSNKWQSSIKSPQDLIEQDKVHFGSMRGGSTSLFFSESNDTDYQRAWNQMKDFNPSAFTSTNKEGVARVRKEKGGYAFLMETTSLTYNIERNCDLTQIGEQIGEKHYGLAVPLGSDYRTNLSVSILQLSERGELQKMKNKWWKNHNVTCDSYHEVDGDELSIIELGGVFLVLAGGVLIGVILGIFEFLWNVQNVAVEERVTPWQAFKAELIFALKFWVRKKPMRISSSSDKSSSRRSSGSRRSSKEKSRSKTVS
Protein: Peroxisomal bifunctional enzyme (PBE) (PBFE) (L-peroxisomal bifunctional enzyme) (L-PBE) (Multifunctional enzyme 1) (MFE1) (Multifunctional protein 1) (MFP-1) [Includes: Enoyl-CoA hydratase/3,2-trans-enoyl-CoA isomerase (EC 4.2.1.17) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)] (Q9DBM2)
Organism: Mus musculus (Mouse)
Function: Peroxisomal trifunctional enzyme possessing 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and delta 3, delta 2-enoyl-CoA isomerase activities. Catalyzes two of the four reactions of the long chain fatty acids peroxisomal beta-oxidation pathway. Can also use branched-chain fatty acids such as 2-methyl-2E-butenoyl-CoA as a substrate, which is hydrated into (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA (By similarity). Optimal isomerase for 2,5 double bonds into 3,5 form isomerization in a range of enoyl-CoA species. Also able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species (By similarity). With HSD17B4, catalyzes the hydration of trans-2-enoyl-CoA and the dehydrogenation of 3-hydroxyacyl-CoA, but with opposite chiral specificity (Probable). Regulates the amount of medium-chain dicarboxylic fatty acids which are essential regulators of all fatty acid oxidation pathways. Also involved in the degradation of long-chain dicarboxylic acids through peroxisomal beta-oxidation (By similarity).
Subcellular location: Peroxisome {ECO:0000305|PubMed:24075987}.
Interaction partners:
- Trifunctional enzyme subunit beta, mitochondrial
- Peroxisomal acyl-coenzyme A oxidase 1
- 3-ketoacyl-CoA thiolase B, peroxisomal
- 3-ketoacyl-CoA thiolase A, peroxisomal
- 3-ketoacyl-CoA thiolase, mitochondrial
- Peroxisomal acyl-coenzyme A oxidase 3
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
- Long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
Sequence:
MAEYLRLPHSLAMIRLCNPPVNAISPTVITEVRNGLQKASLDHTVRAIVICGANDNFCAGADIHGFKSPTGLTLGSLVDEIQRYQKPVVAAIQGVALGGGLELALGCHYRIANAKARVGFPEVMLGILPGARGTQLLPRVVGVPVALDLITSGRHISTDEALKLGILDVVVKSDPVEEAIKFAQTVIGKPIEPRRILNKPVPSLPNMDSVFAEAIAKVRKQYPGRLAPETCVRSVQASVKHPYEVAIKEEAKLFMYLRGSGQARALQYAFFAEKSANKWSTPSGASWKTASAQPVSSVGVLGLGTMGRGIAISFARVGIPVVAVESDPKQLDTAKKIITSTLEKEASKSGQASAKPNLRFSSSTKELSSVDLVIEAVFEDMNLKKKVFAELSALCKPGAFLCTNTSALDVDDIASSTDRPQLVIGTHFFSPAHIMRLLEVIPSRYSSPTTIATVMSLSKRIGKIGVVVGNCYGFVGNRMLAPYYNQGYFLIEEGSKPEDVDGVLEEFGFRMGPFRVSDLAGLDVGWKVRKGQGLTGPSLPPGTPTRKRGNTRYSPIADMLCEAGRFGQKTGKGWYQYDKPLGRIHKPDPWLSEFLSQYRETHHIKQRSISKEEILERCLYSLINEAFRILEEGMAASPEHIDVIYLHGYGWPRHVGGPMYYAASVGLPTVLEKLQKYYRQNPDIPQLEPSDYLRRLVAQGSPPLKEWQSLAGPHSSKL
Protein: 60S acidic ribosomal protein, putative (Q38EY6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 60S acidic ribosomal protein, putative
- 60S acidic ribosomal protein P2, putative
- 60S acidic ribosomal protein P0
- 60S ribosomal protein L7a
- 60S ribosomal protein L19, putative
- 60S ribosomal protein L35A, putative
- 60S ribosomal protein L35, putative
- 60S ribosomal protein L5, putative
- 60S ribosomal protein L27a
- 60S ribosomal protein L4
Sequence:
MSMKYLAAYALASLAKPAPTADDVKAICKASGVKVEEDSLAFVMEAIDGRSVNTLIAEGVAKMSAVSVAAAPAAGGAAAPAAGGAAAGGAAAPAKKQEVEEEEDDDMGFGLFD
Protein: Translocon-associated protein subunit delta (TRAP-delta) (Signal sequence receptor subunit delta) (SSR-delta) (Q07984)
Organism: Rattus norvegicus (Rat)
Function: TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins.
Subcellular location: Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Interaction partners:
- Translocon-associated protein subunit gamma
- Translocon-associated protein subunit beta
- Translocon-associated protein subunit alpha
- Protein transport protein Sec61 subunit beta
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Myeloid-derived growth factor
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
- Sec61 translocon gamma subunit.
- Protein transport protein Sec61 subunit alpha isoform 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
Sequence:
MAAMASFGALALLLLSGLSCCSAEACLEPQITPSYYTTSDAVISTETVFIVEISLTCKNRVQNMALYADVSGKQFPVTRGQDVGRYQVSWSLEHKSAHAGTYEVRFFDEESYSLLRKAQRNNEDVSIIPPLFTVSVDHRGTWNGPWVSTEVLAAAIGIVIYYLAFSAKSHIQA
Protein: RELT-like protein 2 (Q8BRJ3)
Organism: Mus musculus (Mouse)
Function: Induces activation of MAPK14/p38 cascade, when overexpressed. Induces apoptosis, when overexpressed.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8NC24}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8NC24}.
Interaction partners:
Sequence:
MSEPQPDLEPPQHGLYMLFLLVLVFFLMGLVGFMICHVLKKKGYRCRTSRGSEPDDAQLQPPEDDDVNEDTVERIVRCIIQNEANAEALKEMLGDSEGEGTVQLSSVDATSSLQDGAPSHHHTVHLGSAAPCIHCSRSKRPPLVRQGRSKEGKSRPRPGETTVFSVGRFRVTHIEKRYGLHEHRDGSPTDRSWGSGGGQEPGGSQAAGGGQPRTGTAAIERLLPEPPPSQAAATHSVQNGRLQDASLVPCTLEGTPGTSAELNLGPRGRDPSPGLSSQEANGQPTKLDTSGQQESLPPEAGGM
Protein: Putative acyl-CoA binding protein (Q4QHU9)
Organism: Leishmania major
Interaction partners:
Sequence:
MMRGEAADGATVLSEFTVLRKPSNDNKYWHTAVHQGEPVTFRVLDDSGIDPVDGAGYVMARVQAMQKHMQEARVDVAAEHAYRAVLVEVSLLDDPIAVPEETQRDMNCAVDLWCPLHVALMTSNKAAAQALLQFHVEHAVTAMTYIASTPSAIGNAGAVDALDSPPVAPALDDDAPDAPGDDHTASVPPVAASPILECHVHRELGGAVVLLGHFDGRVRLSSAAVRKSRLPTPVRGGSPHAAPVSSSPGGIESALAGGCHCSTGIAVGEDALVQNQCKHNDALLREEDALFEDKGEEYCLRNILVAMRPLLQSVVLEIKRRAQCTTTTAPLSLQHHHHTHKASLACATPVVPESAIDFVHDYCSSLSMLPQHPPLLIDGDTVFDVCNHGDLALLANVIDVFEGCFAPILRGQTLLTDRCAGGRGVGFAAPTGAAFPHNFSLSSPPSLSGTGQSSSPSFLSLGGDASAHSMAGTSHKGSVGRHVHALPPAPFWWSCPPQNVHRLAFVAVWIGCREAIDENSGSGRRRAVSMSNKNRVTMVAIRQLQESRVAAQKLDSTIWSGHLITIMKLLSRECSLEDYVDFVEEGGYFAFTSPRGFSGLFLSVLVSGVMAAALVPEPAMLRVLRCKVETLLADVPGRPSPLRTYVMGRPSTHAERFRELWLDAGCHGIANPDGGNGQNDAGDTETGGFNPVGGIQSAERRPMKFRSRIELLYYAVIEQVVAAAEEAWRMHEADDGDSSEAAGDSAAPSSSSSPWPSGATKAEALTALQGWLLMWANFLTSLRDWTPHRGSFSCSTASSQMPQQERPQHSLNSGAEGQLTVGGMSPPLTATTAPHHEHTASSEDLFSDDANETADMVQRVSHALVERLETGREPLPALRRALFPNGANDVETGAPAAGASAHVDKDLPVSSIDQEFASAQHAFAATAGRESDEVKLKFYGLFKQATVGDVNTDRPGIFDYAGKAKWDAWSKLKGISLLDAKRMYVSQYKMMMELRKSRK
Protein: Tip attachment protein J (Central tail fiber) (Host specificity protein J) (gpJ protein) (P03749)
Organism: Escherichia phage lambda (Bacteriophage lambda)
Function: Attaches the virion to the host receptor LamB, inducing viral DNA ejection. During tail assembly, initiates distal tail tip assembly by interacting with gpI, gpL and gpK. During virus entry to host cell, binds strongly to host LamB in an irreversible attachment. The binding induces structural changes in the tail leading to viral DNA injection through LamB trimeric pore.
Subcellular location: Virion {ECO:0000305}. Host cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MGKGSSKGHTPREAKDNLKSTQLLSVIDAISEGPIEGPVDGLKSVLLNSTPVLDTEGNTNISGVTVVFRAGEQEQTPPEGFESSGSETVLGTEVKYDTPITRTITSANIDRLRFTFGVQALVETTSKGDRNPSEVRLLVQIQRNGGWVTEKDITIKGKTTSQYLASVVMGNLPPRPFNIRMRRMTPDSTTDQLQNKTLWSSYTEIIDVKQCYPNTALVGVQVDSEQFGSQQVSRNYHLRGRILQVPSNYNPQTRQYSGIWDGTFKPAYSNNMAWCLWDMLTHPRYGMGKRLGAADVDKWALYVIGQYCDQSVPDGFGGTEPRITCNAYLTTQRKAWDVLSDFCSAMRCMPVWNGQTLTFVQDRPSDKTWTYNRSNVVMPDDGAPFRYSFSALKDRHNAVEVNWIDPNNGWETATELVEDTQAIARYGRNVTKMDAFGCTSRGQAHRAGLWLIKTELLETQTVDFSVGAEGLRHVPGDVIEICDDDYAGISTGGRVLAVNSQTRTLTLDREITLPSSGTALISLVDGSGNPVSVEVQSVTDGVKVKVSRVPDGVAEYSVWELKLPTLRQRLFRCVSIRENDDGTYAITAVQHVPEKEAIVDNGAHFDGEQSGTVNGVTPPAVQHLTAEVTADSGEYQVLARWDTPKVVKGVSFLLRLTVTADDGSERLVSTARTTETTYRFTQLALGNYRLTVRAVNAWGQQGDPASVSFRIAAPAAPSRIELTPGYFQITATPHLAVYDPTVQFEFWFSEKQIADIRQVETSTRYLGTALYWIAASINIKPGHDYYFYIRSVNTVGKSAFVEAVGRASDDAEGYLDFFKGKITESHLGKELLEKVELTEDNASRLEEFSKEWKDASDKWNAMWAVKIEQTKDGKHYVAGIGLSMEDTEEGKLSQFLVAANRIAFIDPANGNETPMFVAQGNQIFMNDVFLKRLTAPTITSGGNPPAFSLTPDGKLTAKNADISGSVNANSGTLSNVTIAENCTINGTLRAEKIVGDIVKAASAAFPRQRESSVDWPSGTRTVTVTDDHPFDRQIVVLPLTFRGSKRTVSGRTTYSMCYLKVLMNGAVIYDGAANEAVQVFSRIVDMPAGRGNVILTFTLTSTRHSADIPPYTFASDVQVMVIKKQALGISVV
Protein: Signal transducer and activator of transcription 6 (O70429)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
TLNLKFMAEVGTSRGLLPEHFLFLAQKIFNDNSLSIEAFQHRCVSWSQFNKEILLGRGFTFWQWFDGVLDLTKRCLRSYWSDRLIIGFISKQYVTSLLLNEPDGTFLLRFSDSEIGGITIAHVIRGQDGSSQIENIQPFSA
Protein: Arrestin domain-containing protein 4 (A0A0B4J1F4)
Organism: Mus musculus (Mouse)
Function: Functions as an adapter recruiting ubiquitin-protein ligases to their specific substrates. Plays a role in endocytosis of activated G protein-coupled receptors (GPCRs) (By similarity). Through an ubiquitination-dependent mechanism also plays a role in the incorporation of SLC11A2 into extracellular vesicles. May play a role in glucose uptake (By similarity).
Subcellular location: Early endosome {ECO:0000269|PubMed:19605364}. Cell membrane {ECO:0000269|PubMed:19605364, ECO:0000269|PubMed:27462458}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle {ECO:0000269|PubMed:19605364}. Note=Also found in extracellular vesicles different from exosomes. {ECO:0000269|PubMed:27462458}.
Interaction partners:
- E3 ubiquitin-protein ligase NEDD4
Sequence:
MGGEAGADGPRGRVKSLGLVFEDESKGCYSSGETVAGHVLLEAAEPVALRGLRLEAQGRATSAWGPSAGARVCIGGGSPAASSEVEYLNLRLSLLEAPAGEGVTLLQPGKHEFPFRFQLPSEPLATSFTGKYGSIQYCVRAVLERPQVPDQSVRRELQVVSHVDVNTPPLLTPMLKTQEKMVGCWLFTSGPVSLSVKIERKGYCNGEAIPIYAEIENCSSRLVVPKAAIFQTQTYLASGKTKTVRHMVANVRGNHIGSGSTDTWNGKMLKIPPVTPSILDCCIIRVDYSLAVYIHIPGAKRLMLELPLVIGTIPYSGFGRRNSSVASQFSMDMCWLALALPEQPEAPPNYADVVSEEEFSRHVPPYPQPSDCDGEACYSMFACIQEFRFQPPPLYSEVDPHPGDAQETQPVSFIL
Protein: Complement C1s subcomponent (EC 3.4.21.42) (C1 esterase) (Complement component 1 subcomponent s) [Cleaved into: Complement C1s subcomponent heavy chain; Complement C1s subcomponent light chain] (P09871)
Organism: Homo sapiens (Human)
Function: C1s B chain is a serine protease that combines with C1q and C1r to form C1, the first component of the classical pathway of the complement system. C1r activates C1s so that it can, in turn, activate C2 and C4.
Interaction partners:
- Plasma protease C1 inhibitor
- Complement C1r subcomponent
- Complement C1q subcomponent subunit B
- Complement C4-B
- Complement C4-A
- Complement C1q subcomponent subunit C
- Complement C1q subcomponent subunit A
- Complement C2
- Immunoglobulin heavy variable 4-38-2
- Complement C3
Sequence:
MWCIVLFSLLAWVYAEPTMYGEILSPNYPQAYPSEVEKSWDIEVPEGYGIHLYFTHLDIELSENCAYDSVQIISGDTEEGRLCGQRSSNNPHSPIVEEFQVPYNKLQVIFKSDFSNEERFTGFAAYYVATDINECTDFVDVPCSHFCNNFIGGYFCSCPPEYFLHDDMKNCGVNCSGDVFTALIGEIASPNYPKPYPENSRCEYQIRLEKGFQVVVTLRREDFDVEAADSAGNCLDSLVFVAGDRQFGPYCGHGFPGPLNIETKSNALDIIFQTDLTGQKKGWKLRYHGDPMPCPKEDTPNSVWEPAKAKYVFRDVVQITCLDGFEVVEGRVGATSFYSTCQSNGKWSNSKLKCQPVDCGIPESIENGKVEDPESTLFGSVIRYTCEEPYYYMENGGGGEYHCAGNGSWVNEVLGPELPKCVPVCGVPREPFEEKQRIIGGSDADIKNFPWQVFFDNPWAGGALINEYWVLTAAHVVEGNREPTMYVGSTSVQTSRLAKSKMLTPEHVFIHPGWKLLEVPEGRTNFDNDIALVRLKDPVKMGPTVSPICLPGTSSDYNLMDGDLGLISGWGRTEKRDRAVRLKAARLPVAPLRKCKEVKVEKPTADAEAYVFTPNMICAGGEKGMDSCKGDSGGAFAVQDPNDKTKFYAAGLVSWGPQCGTYGLYTRVKNYVDWIMKTMQENSTPRED
Protein: Guanine nucleotide-binding protein alpha-2 subunit (GP2-alpha) (Q04665)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. This protein may be involved in the determination of the cAMP level according to nutritional conditions, most probably as a regulator of adenylyl cyclase.
Subcellular location: Cell membrane {ECO:0000305|PubMed:20139237}; Peripheral membrane protein {ECO:0000305|PubMed:20139237}; Cytoplasmic side {ECO:0000305|PubMed:20139237}.
Interaction partners:
- Guanine nucleotide-binding protein subunit beta
- Adenylate cyclase
- Guanine nucleotide-binding protein subunit gamma
- Glucose receptor protein git3
- Regulator of G-protein signaling 1
- Guanine nucleotide-binding protein negative regulator 1
- cAMP-dependent protein kinase catalytic subunit
- 3',5'-cyclic-nucleotide phosphodiesterase
- cAMP-dependent protein kinase regulatory subunit
- Mitogen-activated protein kinase sty1
Sequence:
MTIFNGLSESGESKKLNSKIEKQIENASKKDKKIYKVLLLGASDSGKSTISKQIKILNKNGFSQEEIMTFIPVIRRNLLESAKTLVKIIVQKGINLDPLGTHNCEIIEKFNPTPGELINANIGQAITSLWSANSVRSCTYGNDSVLIDSAPYFFSRADEICSRHYVPTIDDILRSRNSTLGISEISFTLDHLQIRMFDVGGQRTERRKWIYCFENVNSIIFCVSLNDYDKKLYERAAPERNRLVESISLFDSIINSQWFMHSSIILFLNKFDLFRKKLEHVPFQDYFPQYEGKNSVKSITRYILWLFVNPSINRAKHNIYPHITTAVDTSNIKVVFSAVKETILQHSLKEAGMF
Protein: F-box only protein 46 (F-box only protein 34-like) (Q6PJ61)
Organism: Homo sapiens (Human)
Function: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex.
Interaction partners:
- S-phase kinase-associated protein 1
- Cullin-1
Sequence:
MDRGSLLPFQLWCPRPFGTYSQNQPRPPSAALKPSACPEPGGGAEPDHGPAHSENTPPALATEVPASQPAPLLSAAAAGDEGRVLLDTWYVIKPGNTKEKVAFFVAHQCGGGSRASSMKVKGHWGSDSSKAKRRRRCLDPTKAPPDPGGREGPPAAEEGPASAGEDVDLLSVAEMVALVEQRAALALQSYPRPTTPAPVVFVSAEQGGPAKGVGSERRSGGGDCSRVAEAVAHFEAQRDSPPTKGLRKEERPGPGPGEVRIAFRISNGREPRAPDSGLPSGGGGRPGCAYPGSPGPGARAKDKITCDLYQLISPSRDALPSNVEFLLARADEASEGDSPAPARPEDTPPAPPPPPARDCGASGFHVDVVVTGVVDECIFFGKDGTKNVKEETVCLTVSPEEPPPPGQLFFLQNRGPDGPPEPPPADSPATAPGPDDAEGTADTSLCRLYRHVSHDFLEIRFKIQRLLEPRQYMLLLPEHVLVKIFSFLPTRALAALKCTCHHFKGIIEAFGVRATDSRWSRDPLYRDDPCKQCRKRYEKGDVSLCRWHPKPYHHDLPYGRSYWMCCRRADRETPGCRLGLHDNNWVLPCNGPGGGRAGREEGR
Protein: Ubiquitin carboxyl-terminal hydrolase (EC 3.4.19.12) (D4A4F6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Transcription initiation factor TFIID subunit 10
- Transcriptional adapter 3
- Transcription initiation factor TFIID subunit 9B
- Transcription and mRNA export factor ENY2
- Transcriptional adapter
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ataxin 7
Sequence:
MECPHLSSSVCIAPDSAKFPNGSPSSWCCSVCRSNKSPWVCLTCSSVHCGSYRCDDFVVNDTKLGLVQKVREHLQNLENSAFTADRHRKRKLLENSSLNSKLLKVNGSTAAICATGLRNLGNTCFMNAILQSLSNIEQFCCYFKELPAVELRNGKTAGRRTYHTRSQGDSNVSLVEEFRKTLCALWQGSQTAFSPESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHLELQGGFNGVSRSAILQENSTLSANNKCCINGASTVVTTIFGGILQNEVNCLICGTESRKFDPFLDLSLDIPSQFRSKRSKNQENGPVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKKFWIQKLPKALCLHLKRFHWTAYLRNKVDTYVQFPLRGLDMKCYLLEPENSGPDSCLYDLAAVVVHHGSGVGSGHYTAYAVHEGRWFHFNDSTVTVTDEETVGKAKAYILFYVERQARAGADKL
Protein: RH56938p (Q8SWY9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MCNRLRLADIVVRPMQRLTKYSLLLAAIKKHMSDVEEIEAIDVMMHSVENFVGSVNNHLTMRQENERLKGVMVRIESYDVVDTNNEVLDKMIKQNSQMFDLCAPMRGCPAYHVRHLFMEGDHKFKDNLGKSDVHCFLLTDLLLVCKTIAKRGLGALKVIRQPYLTDQLIVQLAPNNTLNCVYLNEFQVATTAFTLQCTEVKNWYDALWRAKTIYQRLKRGGGGGGSGSGTVGGGDSFRFGGSATSGGTADSLGVRKSPMNSSICSHVSSANNSHSGSVEWNDSRNISVDFEKTNSVSSDEGSSIMTGNHGVNLKGKQQLISGLHKTKMGIIGQMGSKSANTLSVQPMNHLGQSLPNLNMHHSHTVPLRRGMAFSTSTKNPPLRKTRNITSQNSINWHQIPATPTPPSPRSQYQSPGVVCMQKSLPLLLPTNTDEGQGPTQPPPPLQKQLSHQAPLPTTIHNQSSTETDV
Protein: Bone morphogenetic protein receptor type-1A (BMP type-1A receptor) (BMPR-1A) (EC 2.7.11.30) (Activin receptor-like kinase 3) (ALK-3) (Serine/threonine-protein kinase receptor R5) (SKR5) (CD antigen CD292) (P36894)
Organism: Homo sapiens (Human)
Function: On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for BMP2, BMP4, GDF5 and GDF6. Positively regulates chondrocyte differentiation through GDF5 interaction. Mediates induction of adipogenesis by GDF6.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19726563}; Single-pass type I membrane protein {ECO:0000255}. Cell surface {ECO:0000250|UniProtKB:P36895}.
Interaction partners:
- Activin receptor type-1
- Bone morphogenetic protein 6
- Bone morphogenetic protein 7
- Bone morphogenetic protein receptor type-2
- Bone morphogenetic protein 4
- Bone morphogenetic protein 2
- Growth/differentiation factor 5
- Activin receptor type-2A
- Bone morphogenetic protein receptor type-1B
- Activin receptor type-2B
Sequence:
MPQLYIYIRLLGAYLFIISRVQGQNLDSMLHGTGMKSDSDQKKSENGVTLAPEDTLPFLKCYCSGHCPDDAINNTCITNGHCFAIIEEDDQGETTLASGCMKYEGSDFQCKDSPKAQLRRTIECCRTNLCNQYLQPTLPPVVIGPFFDGSIRWLVLLISMAVCIIAMIIFSSCFCYKHYCKSISSRRRYNRDLEQDEAFIPVGESLKDLIDQSQSSGSGSGLPLLVQRTIAKQIQMVRQVGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSLYDFLKCATLDTRALLKLAYSAACGLCHLHTEIYGTQGKPAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEVDVPLNTRVGTKRYMAPEVLDESLNKNHFQPYIMADIYSFGLIIWEMARRCITGGIVEEYQLPYYNMVPSDPSYEDMREVVCVKRLRPIVSNRWNSDECLRAVLKLMSECWAHNPASRLTALRIKKTLAKMVESQDVKI