wanglab/gogpt-training-data huggingface dataset:
Protein: Rab27 (Small monomeric GTPase) (G5EBS5)
Organism: Caenorhabditis elegans
Subcellular location: Late endosome {ECO:0000256|ARBA:ARBA00004603}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Rabphilin-1
- MAP kinase-activating death domain protein
- Rab proteins geranylgeranyltransferase component A 1
- C2 domain-containing protein
- C2 domain-containing protein
- C2 domain-containing protein
- Rab GDP dissociation inhibitor
- C2 domain-containing protein
- C2 domain-containing protein
- C2 domain-containing protein aex-1
Sequence:
MGDYDYLIKFLALGDSGVGKTSFLHRYTDNTFTGQFISTVGIDFKEKKVVYKSSRGGFGGRGQRVLLQLWDTAGQERFRSLTTAFFRDAMGFILIFDITNEQSFLNIRDWLSQLKVHAYCEQPDIIICGNKADLENRRQVSTARAKQLADQLGLPYFETSACTSTNVEKSVDCLLDLVMQRIQQSVETSSLPLSECRGVSLDGDPSAASSYCANC
Protein: Probable amino-acid acetyltransferase NAGS2, chloroplastic (EC 2.3.1.1) (N-acetylglutamate synthase 2) (B5X4Z4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: N-acetylglutamate synthase involved in arginine biosynthesis.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Arginine biosynthesis bifunctional protein ArgJ
- Probable N-acetyl-gamma-glutamyl-phosphate reductase, chloroplastic
- Argininosuccinate lyase, chloroplastic
- Argininosuccinate synthase, chloroplastic
- Ornithine transcarbamylase, chloroplastic
- Acetylornithine aminotransferase, chloroplastic/mitochondrial
- Ornithine aminotransferase, mitochondrial
- Nitrogen regulatory protein P-II homolog
- Acetylglutamate kinase, chloroplastic
- Glutamate dehydrogenase 2
Sequence:
MERGALVGSSSTSSYYVPYHFRQSKSNFSSFKPKNKLNPTQFRFNCSWFKPVSSITAAKCNMFDYAVTAAGDVEAEHPVDDKQFVRWFREAWPYLWAHRGCTFVVIISGEIIAGSSCDAILKDIAFLHHLGIRFVLVPGTQEQIDQLLAERGREATYVGRYRVTDAASLQAAKEAAGAISVMLEAKLSPGPSICNIRRHGDRSRLHDIGVRVDTGNFFAAKRRGVVDGVDFGATGEVKKIDVDRICERLDGGSVVLLRNLGHSSSGEVLNCNTYEVATACALAIGADKLICIMDGPILDESGHLIHFLTLQEADMLVRKRAQQSDIAANYVKAVGDGSMAYPEPPNNTNGNITSAQNGRAVSFWGNGNHTPIFQNGVGFDNGNGLWPCEQGFAIGGEERLSRLNGYLSELAAAAFVCRGGVKRVHLLDGTISGVLLLELFKRDGMGTMVASDVYEGTRDARVEDLAGIRHIIKPLEESGILVRRTDEELLRALDSFVVVEREGQIIACAALFPFFKDKCGEVAAIAVASDCRGQGQGDKLLDYIEKKASSLGLEKLFLLTTRTADWFVRRGFQECSIEIIPESRRQRINLSRNSKYYMKKLIPDRSGISVMRI
Protein: ABC-type antigen peptide transporter (EC 7.4.2.14) (Q9TZD9)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- ABC-type antigen peptide transporter
- HAlF transporter
- Amino acid transporter
- Nucleolar protein 16
- AP-3 complex subunit beta
- Acyl-CoA synthetase 7
Sequence:
MNSTVASRFSWGLILASIDFLACLLFACLHDGTFKFANFTSQFGDFSFFTSTIDLFLLQFFRFALWMVPAAIHVANKADTLTMWKEPIFCSALLICAASPTKLLLLTEKLKPDEFLTFGDTAFLVWNFISAIILNSSWTRYFSRTPSSYIILEDEDLEVAPKQTFELIFRLLQYCKREWLWHISGFSWLFIYSITRIFVPYYTGQVIATVVATKSYPALSNAVYIMTIISLVSAVAAGFRGGSFEYAYARIQRAIRYDLFHGLVKQDVAFYDAHKTGEVTSRLAADCQTMSDTVALNVNVFLRNCVMLLGSMIFMMKLSWRLSLVTFILVPIIFVASKIFGTYYDLLSERTQDTIAESNDVAEEVLSTMRTVRSFSCENVEADRFYGKLTHTLDVTRTKAIAYIGFLWVSELFQSFIIVSVLWYGGHLVLTQKMKGDLLVSFLLYQMQLGDNLRQMGEVWTGLMQSVGASRKVFEYIDREPQIQHNGEYMPENVVGKIEFRNVHFSYPTRSDQPILKDLSFTVEPGETVALVGPSGSGKSSCISLLENFYVPNAGQVLVDGVPLEEFEHHYIHKKIALVGQEPVLFARSVMENVRYGVEVADTEIIRSCEMANAHGFIMQTTLKYETNVGEKGTQMSGGQKQRIAIARALVREPAILLLDEATSALDTESEHLVQEAIYKNLDGKSVILIAHRLSTVEKADKIVVINKGRVEQIGNHETLLKDTNGTYAKLVQRQMMGDQKPRKRPAVARSGPQPAASINVAGPSQGNAMSLLSTSFSQSASSVTSH
Protein: Arginase (EC 3.5.3.1) (A0A1D8PP00)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Ornithine aminotransferase
- Ornithine decarboxylase
- ornithine carbamoyltransferase
- Urea amidolyase
- Arginine biosynthesis bifunctional protein ArgJ
- Argininosuccinate lyase
- chitin deacetylase
- Proline dehydrogenase
- Argininosuccinate synthase
- Protein ARG5,6
Sequence:
MSSIQYKYHPDKKASIITAPFSGGQPKGGVELGPDYILKAGFQKQIESLGWTTDLKEPLEGTDYEKMKTNDKDDFGVKNSKIVSESCQKIHDAVKGSLAEGKLPITIGGDHSIGTATVSASLVHDPSTCVVWVDAHADINTPKTTDSGNLHGCPLSFIMGIDRDSYPPEFSWVPQVLKSNKLVYIGLRDVDDGEKEILRKHNIAAFSMYHVDKYGIGKVVEMALDKVNPNRDCPVHLSYDVDAIDPSFVPATGTRVEGGLSLREGLFIAEEIAQSGLLQSLDIVETNPMLAETEEHVLDTVSAACAIGRCALGQTLL
Protein: Insulin-like growth factor 2 mRNA-binding protein 2 (IGF2 mRNA-binding protein 2) (IMP-2) (Hepatocellular carcinoma autoantigen p62) (IGF-II mRNA-binding protein 2) (VICKZ family member 2) (Q9Y6M1)
Organism: Homo sapiens (Human)
Function: RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation (By similarity). Preferentially binds to N6-methyladenosine (m6A)-containing mRNAs and increases their stability. Binds to the 5'-UTR of the insulin-like growth factor 2 (IGF2) mRNAs. Binding is isoform-specific. Binds to beta-actin/ACTB and MYC transcripts. Increases MYC mRNA stability by binding to the coding region instability determinant (CRD) and binding is enhanced by m6A-modification of the CRD.
Subcellular location: Nucleus. Cytoplasm. Cytoplasm, P-body {ECO:0000269|PubMed:29476152}. Cytoplasm, Stress granule {ECO:0000269|PubMed:29476152}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Localizes at the connecting piece and the tail of the spermatozoa. In response to cellular stress, such as oxidative stress, recruited to stress granules.
Interaction partners:
- High mobility group AT-hook 2
- Insulin-like growth factor 2
- Alpha-ketoglutarate-dependent dioxygenase FTO-)-demethylase FTO)
- Hematopoietically-expressed homeobox protein HHEX
- Threonylcarbamoyladenosine tRNA methylthiotransferase
- ATP-dependent RNA helicase A
- Heterogeneous nuclear ribonucleoproteins C1/C2
- Heterogeneous nuclear ribonucleoproteins A2/B1
- YTH domain-containing family protein 1
- YTH domain-containing protein 1
Sequence:
MMNKLYIGNLSPAVTADDLRQLFGDRKLPLAGQVLLKSGYAFVDYPDQNWAIRAIETLSGKVELHGKIMEVDYSVSKKLRSRKIQIRNIPPHLQWEVLDGLLAQYGTVENVEQVNTDTETAVVNVTYATREEAKIAMEKLSGHQFENYSFKISYIPDEEVSSPSPPQRAQRGDHSSREQGHAPGGTSQARQIDFPLRILVPTQFVGAIIGKEGLTIKNITKQTQSRVDIHRKENSGAAEKPVTIHATPEGTSEACRMILEIMQKEADETKLAEEIPLKILAHNGLVGRLIGKEGRNLKKIEHETGTKITISSLQDLSIYNPERTITVKGTVEACASAEIEIMKKLREAFENDMLAVNQQANLIPGLNLSALGIFSTGLSVLSPPAGPRGAPPAAPYHPFTTHSGYFSSLYPHHQFGPFPHHHSYPEQEIVNLFIPTQAVGAIIGKKGAHIKQLARFAGASIKIAPAEGPDVSERMVIITGPPEAQFKAQGRIFGKLKEENFFNPKEEVKLEAHIRVPSSTAGRVIGKGGKTVNELQNLTSAEVIVPRDQTPDENEEVIVRIIGHFFASQTAQRKIREIVQQVKQQEQKYPQGVASQRSK
Protein: Estradiol 17-beta-dehydrogenase 2 (EC 1.1.1.62) (17-beta-hydroxysteroid dehydrogenase type 2) (17-beta-HSD 2) (Testosterone 17-beta-dehydrogenase) (EC 1.1.1.239) (P51658)
Organism: Mus musculus (Mouse)
Function: Catalyzes the NAD-dependent oxidation of highly active 17beta-hydroxysteroids, such as estradiol (E2), testosterone (T), and dihydrotestosterone (DHT), to their less active forms and thus regulates the biological potency of these steroids. Oxidizes estradiol to estrone, testosterone to androstenedione, and dihydrotestosterone to 5alpha-androstan-3,17-dione. Also has 20-alpha-HSD activity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P37059}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P37059}.
Interaction partners:
- Dehydrogenase/reductase SDR family member 11
- 17-beta-hydroxysteroid dehydrogenase type 1
- 3-oxo-5-alpha-steroid 4-dehydrogenase 1
- Steroid 17-alpha-hydroxylase/17,20 lyase
- 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7
- Aromatase
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2
- 3-oxo-5-alpha-steroid 4-dehydrogenase 2
- Sulfotransferase 1E1
Sequence:
MSPFASESAWLCLAAAAVLGGTLLCGCRSGRQLRSQAVCLAGLWGGACLLSLSLLCTLFLLSVACFLLLYMSSSDQDLLPVDQKAVLVTGADSGFGHGLAKHLDKLGFTVFAGVLDKEGPGAEELRKHCSERLSVLQMDVTKPEQIKDAHSKVTEKIQDKGLWAVVNNAGVFHLPIDGELIPMSIYRKCMAVNFFGTVEVTKAFLPLLRKSKGRLVNVSSMGGTVPLQMTSAYAATKAALTMFSTIIRQELDKWGVKVVTIKPGGFKTNITGSQDIWDKMEKEILDHFSKDIQENYGQDYVHTQKLIIPTLKERSNPDITPVLRDIQHAISARNPSSFYYPGRMAYLWVCLAAYCPTSLLDYVIKKGFYPQPTPRALRTVH
Protein: E3 ubiquitin-protein ligase Arkadia isoform X4 (Ring finger protein 111 (EC 6.3.2.-)) (N0A274)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus, PML body {ECO:0000256|ARBA:ARBA00004322}.
Interaction partners:
Sequence:
MKSEISADARQKQEPLKGPLANPEPMETAKSFPAEMEVIGKAGSDFTSPLCAETRHRPSRDAGGRRDCERGLSGRKKRKSQQPGPSYCSLKEAPMSEATLTPPRHRPMLLETRSEDERNPESSLSDCASSPSSSLRFGDSDTLSSDEDGMPMTVRQQLKAHGAASTGSTGSSTGTAVGIRPLLARTRASRSHKWARLEPDSNHVKRPCLGSRRPLHRKRFVKGGAGGVTQRTPKQKERLLLQRKKREVIARKKYALLHSTSSSSEEMTSDDSSPSSTEAEHELYVDVNSSSSQASTAAVASGVLDEDVVVIEATPAPAVPASEEINVTSTDSEVEIVTVGDAFRPRSVGGHGRMHWGPSCSQSRAQEGRGRHRLSTVIQPLRQSAGEVVDLTVDEDDLSVVPTTSDSTHPQPVSSSSSSSSRNACTSASPQEGPGPSSSCSAAAPDSTLAAQSHGGVPRSGTTNTTATEDESRRSLLGENGGVAMPRLPSCCPQHSPCSGPSSGHLSMGHTHSGCMQSGATQQSGPPQPGSQHSHTHSHHFHHHHHTAPVPSSLAYQESSCPLERPTAMPAPCGGVSNQYHDQTLPVDLSSSAVRSSGSSSTGFHGTSAFDPCCPGSASRPPVYVSQAAPGPSQQTVADSFSPTIVAQPQPQPPQLSSCRHYMHPTYGSLSRPLHHQSSSSCPHSHSNAPPPQQPPPQGDYVIPHPVLPFHTPLPTHAPGHTVPTAPPPSLPSHHLPGSSAPLPQHLPPEHQALQHHLPVLGPNSVQRLHHHDLLQRMEVQRRRMMQHPTRAHERPPPHPHRMHPNYGHGHHIHVPQTMSSLPRQSDQRTTWELGIEAGVTVAPYPSGHLHPHLPHYHPPPRLHHFPIQLMHTGSMPEVTYPHIRYISSRMTFGRTYEDLLHLEERLGTVNRGASQGTIERCTYPHKYKKRKLHGKQEEEEGAEEDTEEKCTICLSILEEGEDVRRLPCMHLFHQLCVDQWLLTNKKCPICRVDIEAQLSSES
Protein: CREB1 protein (cAMP responsive element binding protein 1) (cDNA, FLJ96224, Homo sapiens cAMP responsive element binding protein 1 (CREB1),transcript variant A, mRNA) (Q53X93)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTMESGAENQQSGDAAVTEAENQQMTVQAQPQIATLAQVSMPAAHATSSAPTVTLVQLPNGQTVQVHGVIQAAQPSVIQSPQVQTVQISTIAESEDSQESVDSVTDSQKRREILSRRPSYRKILNDLSSDAPGVPRIEEEKSEEETSAPAITTVTVPTPIYQTSSGQYIAITQGGAIQLANNGTDGVQGLQTLTMTNAAATQPGTTILQYAQTTDGQQILVPSNQVVVQAASGDVQTYQIRTAPTSTIAPGVVMASSPALPTQPAEEAARKREVRLMKNREAARECRRKKKEYVKCLENRVAVLENQNKTLIEELKALKDLYCHKSD
Protein: Probable methyltransferase PMT26 (EC 2.1.1.-) (Q8L7V3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- RING-type E3 ubiquitin transferase
- Transmembrane 9 superfamily member 9
- Protein CANDIDATE G-PROTEIN COUPLED RECEPTOR 7
- PRA1 family protein B2
- Vacuolar-sorting receptor 6
- V-type proton ATPase subunit G1
- Syntaxin-61
- Vacuolar-sorting receptor 3
Sequence:
MAQPRYTRIDNRRPSSNYCSTVTVVVFVALCLVGIWMMTSSSVGPAQNVDEVSLDNKDGIKKQMTPPAEEGNGQKFEDAPVETPNEDKKGDGDASLPKEDESSSKQDNQEEKKEEKTKEEFTPSSETKSETEGGEDQKDDSKSENGGGGDLDEKKDLKDNSDEENPDTNEKQTKPETEDNELGEDGENQKQFESDNGEKKSIDDDKKSSDDDKENKTGNEDTETKTEKENTETNVDVQVEQEGQSKNETSGDLSPPGAQLELLNETTAQNGSFSTQATESKNEKEAQKGSGDKLDYKWALCNTTAGPDYIPCLDNVQAIRSLPSTKHYEHRERHCPDSPPTCLVPLPDGYKRPIEWPKSREKIWYTNVPHTKLAEYKGHQNWVKVTGEYLTFPGGGTQFKHGALHYIDFIQESVPAIAWGKRSRVVLDVGCGVASFGGFLFDRDVITMSLAPKDEHEAQVQFALERGIPAISAVMGTTRLPFPGRVFDIVHCARCRVPWHIEGGKLLLELNRVLRPGGFFVWSATPVYQKKTEDVEIWKAMSELIKKMCWELVSINKDTINGVGVATYRKPTSNECYKNRSEPVPPICADSDDPNASWKVPLQACMHTAPEDKTQRGSQWPEQWPARLEKAPFWLSSSQTGVYGKAAPEDFSADYEHWKRVVTKSYLNGLGINWASVRNVMDMRAVYGGFAAALRDLKVWVMNVVPIDSPDTLAIIYERGLFGIYHDWCESFSTYPRSYDLLHADHLFSKLKQRCNLTAVIAEVDRVLRPEGKLIVRDDAETIQQVEGMVKAMKWEVRMTYSKEKEGLLSVQKSIWRPSEVETLTYAIG
Protein: Neural cell adhesion molecule 2 (F1M8G9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MSLLLSFYLLGLLVSSGQALLQVTISLSKVELSVGESKFFTCTAIGEPESIDWYNPQGEKIISTQRVMLQKEGVRSRLTIYNANIEDAGIYRCQATDAKGQTQEATVVLEIYQKLTFREVLSPQEFKQGEDAEVVCRVSSSPAPAVSWLYHNEEVTTIPDNRFAVLANNNLQILNINKSDEGIYRCEGRVEARGEIDFRDIIVIVNVPPAIVMPQKSFNATAERGEEMTLTCKASGSPDPAISWFRNGKLIEENEKYILKGSNTELTVRNIINKDGGSYVCKATNKAGEDQKQAFLQVFVQPHILQLKNETTSENGHVTLICEAEGEPVPEITWKRAIDGVTFSEGDKSPDGRIEVKGQHGRSSLHIRDVKLSDSGRYDCEAASRIGGHQRSMHLDIEYAPKFVSNQTMYYSWEGNPINISCDVKANPPASIHWRREKLVLPAKNTTHLKTHSVGRKMILEIAPTSDNDFGRYNCTATNRIGTRFQEYILELADVPSSPRGVKIIELSQTTAKISFNKPESHGGVPIHHYQVDVKEVTSETWKIVRSHGVQTTVVLSSLEPNTTYEVRVAAVNGKGQGDYSKIEIFQTLPVREPSPPSIHGQPSSGKSFKISITKQDDGGAPILEYIVKYRSKDKEDQWLEKKVQGNKDHIILEHLQWTMGYEVQITAANRLGYSEPTVYEFSMPPKPNIIKDTLFNGLGLGAIIGLGVAALLLILVVTDVSCFFIRQCGLLMCITRRMCGKKSGSSGKSKELEEGKAAYLKDGSKEPIVEMRTEDERITNHEDGSPVNEPNETTPLTEPEKLPLKEENGKEVLNAETIEIKVSNDIIQSKEDDIKA
Protein: Zye (Q9VPG1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- FI17806p1
- Cuticular protein 47Ec
- Peroxidase
Sequence:
MVNVGHIFVWALLLVTTRGTDLSDDEALNDVLGELEFDDSSPRLTRDTSLSAKHIEKIDVKCDQGSGMMVEVEFSEDFEGVIYSQGYFSDPKCNYVKGDRSGRSFTFTVPYDGCGSKPSCSVCASIENILIIQDDRDIQNSFDIARKISCSRGDEREKTVYFKPFVVDMLEVISVDTPSGPVECWMEIGTGTPPNVKPIQGTLTLGTDITFTINVKHSEQAWDINILQCYASDDMDFEARTTKRLQLSDKRGCSIKEKIFGEWRKFEAGSSLTSTYYNTLKAFRFPDRSQVYLKCDIELCNGACKRDYTCGSLRSLTCPEGSTDPQCLQDHLISPKPRCYPGSNEPGCPRPTSPPPTTIRIPIASTFTPRPRCYPGSNDPSCNETPQTTSLPSCPLGSTDPRCRVAPPATKKPRCFSGSRDPECQPATYLPPTTRRSSTKPRCYPGSTDPDCQPATRAPITTVKPGCYPGSDDPECQPATYVPQTTRRPSITTKRPRCYPGSTDPECQPRTRPTITTSQPRCSQGSTDPECQPATYLPPTTRRTPIPTTRVPLTTSKPNCYPGSTDTRCPQAPGPRCYPGSPDPSCQPPTRITQKPPTSPQPKCYPGSSDPECLNCYPGSPDPRCPKVPTTKKAGCYEGSDDPRCQPATYLPPSTRRPPTIAPRPRCYLGSTDPSCPQQTQPTTRTPITTIKPRCFPGSNDPECQPATTRRPLTTSKPNCYPGSTDRRCPQEPVTTSRPRCYPGSSDPECQPATLVPPTTVRTTITTSRQRCYPGSSDPSCQPPTTRKPITTPKPNCYPGSTDSRCPQTPRTTQQPRCYPGSTDPDCQPATYLPPTTARTTITTAKPRCYPGSSDPYCQPPTTKKPNCYPGSTDSRCPQKPPITPKPKCYPGSTDLECLNCYPGSPDPRCPKVPTTKKAGCFDGSDDPKCQPATYLPPSTKRTPTIAPKPRCYPGSKDPGCPQITTRAPTSTSRPRCYPGSTDPECHPTTSSPAITRIPVTTRIPLTTAKPRCYPGSQEPGCQPATRPPITTSKPRCYPGSLDPECQPSTYLPPTPVRTTVPTIPTTRIPVTTSKPNCYPGSTDRRCPKEPVTTPKPRCYPGSPNPECQKATYSPPTTRTPVTTSKPNCYPGSTDSRCPQKPPTTLKPKCSPGSSDPECLNCYPGSPDPRCPKVPTTKKSGCFDGSQDPRCQPATYLPPSSRRPPTTAPKPRCHPGSTDPSCPQPTQPITTRLPITTQKARCYPGSTAPECQPATTPTPTSTRPITTITTSKPNCYPGSTDRRCPQIPVTTTKPRCYPGSTDPQCQPATYLPPTTVTTVRPRCYPGSNDPGCQPPQTTKTPITTSKPVCYLGSTDSRCRQNPSTTQKPKCSVGSTDPECQPATYLPPTTVSPTIPTTKPRCYPGSTDTSCQPKTYSPPTSRPLITTSKPRCYPGSPDPECQPATYLPPTTRRTTIPVTKPRCYPGSSDPECQPETYSPPTTRPPVTTSKPNCYPGSTDSRCPQKPPTTLQPKCYPGSSDPECLNCYPGSPDPRCPKIPTTKKAGCFEGSDDPRCQPATYLPPSSRRPPTIAPKPRCYPGSTDPSCPQPTQPTTTRTPLTTSRPRCYPGSTDRECQPATYSPPTSRSQITTLKPRCYPGSKDPECQPATYAPPTTRTPVTTSKPNCYPGSTDKRCPQEIVTTQKPRCYPGSPDPECQPATYLPPTTSRTTIPPTRPRCYPGSSDPSCQPTTNLPPTTRTPVTTRKPNCYPGSTDSRCPQTPQTTIRPKCYPGSTDPDCQPTTNLPPSTPRPTVPTTQPRCYPGSSDPYCQSPTTRAPLTTPKPNCYPGSTDSRCPQKPPTTLAPKCFPGSSDPECLNCYPGSPDPRCPKVPTTRKAGCSDGSDDPRCQPATYLPPSTTRAPKPNCYTGSTDPRCPQPTQATTLRTPVTTTRCYPGSPDPDCQPATRAPVTTLRPKCYSGSNDPECLPSTYSPPTTRIPVTTSSPNCYPGSRDTRCPQAPVTTQRPRCYPGSKDPECQPATYLPPTTARTTIPTVRPRCYPGSNDPDCQPSTYTPPVTKTPITTPKPRCYPGSSDPSCQPATYLPPTTASRCYPGSSDPKCQPATYAPPSTRAPLTTSRPNCYPGSTDRRCPQTPPTTPRPRCYPGSSDPECLPGTTSRPPIAGTTPVYCYPGSIDPRCPDSGYRGTSRIPATYLPPLSDPGYDRTIRNAKTLFFNEINQLAFTDNNVFELDDDEVESSRVKRELKLDEDDLLSKRIIKRESNQEHNSEQEVISLTLGVRTGISVK
Protein: Vesicle trafficking 1 (Q5TGM0)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endosome membrane {ECO:0000256|ARBA:ARBA00004481}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004481}.
Interaction partners:
Sequence:
MTSETLWWLITLKKQLGDNEAITQEIVGCAHLENYALKMFLYADNEDRAGRFHKNMIKSFYTASLLIDVITVFGELTDENVKHRKYARWKATYIHNCLKNGETPQAGPVGIEEDNDIEENEDAGAASLPTQPTQPSSSSTYDPSNMPSGNYTGIQIPPGAHAPANTPAEVPHSTGVASNTIQPTPQTIPAIDPALFNTISQGDVRLTPEDFARAQKYCKYAGSALQYEDVSTAVQNLQKALKLLTTGRE
Protein: UMP-CMP kinase 2, mitochondrial (EC 2.7.4.14) (Nucleoside-diphosphate kinase) (EC 2.7.4.6) (Q5EBM0)
Organism: Homo sapiens (Human)
Function: May participate in dUTP and dCTP synthesis in mitochondria. Is able to phosphorylate dUMP, dCMP, CMP, UMP and monophosphates of the pyrimidine nucleoside analogs ddC, dFdC, araC, BVDU and FdUrd with ATP as phosphate donor. Efficacy is highest for dUMP followed by dCMP; CMP and UMP are poor substrates. May be involved in mtDNA depletion caused by long term treatment with ddC or other pyrimidine analogs. Also displays broad nucleoside diphosphate kinase activity.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:17999954, ECO:0000269|PubMed:34142025, ECO:0000269|PubMed:36443312, ECO:0000269|PubMed:37075076}. Note=Mitochondrial localization is required for its antiviral function. {ECO:0000269|PubMed:37075076}.
Interaction partners:
- Nucleoside diphosphate kinase, mitochondrial
- S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
- 5'
- Deoxycytidine kinase
- Deoxycytidylate deaminase
- Ribonucleoside-diphosphate reductase large subunit
- Adenylate kinase 9
- Uridine 5'-monophosphate synthase
- UMP-CMP kinase
- Nucleoside diphosphate kinase 3
Sequence:
MAFARRLLRGPLSGPLLGRRGVCAGAMAPPRRFVLELPDCTLAHFALGADAPGDADAPDPRLAALLGPPERSYSLCVPVTPDAGCGARVRAARLHQRLLHQLRRGPFQRCQLLRLLCYCPGGQAGGAQQGFLLRDPLDDPDTRQALLELLGACQEAPRPHLGEFEADPRGQLWQRLWEVQDGRRLQVGCAQVVPVPEPPLHPVVPDLPSSVVFPDREAARAVLEECTSFIPEARAVLDLVDQCPKQIQKGKFQVVAIEGLDATGKTTVTQSVADSLKAVLLKSPPSCIGQWRKIFDDEPTIIRRAFYSLGNYIVASEIAKESAKSPVIVDRYWHSTATYAIATEVSGGLQHLPPAHHPVYQWPEDLLKPDLILLLTVSPEERLQRLQGRGMEKTREEAELEANSVFRQKVEMSYQRMENPGCHVVDASPSREKVLQTVLSLIQNSFSEP
Protein: General transcription and DNA repair factor IIH subunit SSL1 (TFIIH subunit SSL1) (RNA polymerase II transcription factor B subunit SSL1) (TFB subunit SSL1) (Suppressor of stem-loop protein 1) (Q04673)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- General transcription and DNA repair factor IIH subunit TFB4
- Cyclin CCL1
- RNA polymerase II transcription factor B subunit 3
- General transcription and DNA repair factor IIH helicase subunit XPD/RAD3
- General transcription and DNA repair factor IIH subunit TFB1
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB/SSL2
- Transcription initiation factor IIE subunit alpha
- Transcription initiation factor IIE subunit beta
- Serine/threonine-protein kinase KIN28
- General transcription and DNA repair factor IIH subunit TFB2
Sequence:
MAPVVISESEEDEDRVAITRRTKRQVHFDGEGDDRVDQQQQQHSSSHRDRDKHVQRKKKKRLSNRNLQGSNGGYAWEDEIKRSWDLVKVDDEGDMASLVASIVEARKKRTAKKNITPYQRGIIRSLILTLDCSEAMLEKDLRPNRHAMIIQYAIDFVHEFFDQNPISQMGIIIMRNGLAQLVSQVSGNPQDHIDALKSIRKQEPKGNPSLQNALEMARGLLLPVPAHCTREVLIVFGSLSTTDPGDIHQTIDSLVSEKIRVKVLGLSAQVAICKELCKATNYGDESFYKILLDETHLKELFNEAVTPLPVNKINKGFTLVKMGFPTRIFEDTPTFCSCHSKLVYGGYFCPNCHSKVCSLPTVCPCCDLMLILSTHLARSYHHLMPLKTFAEVPTTEKFRSEDCFSCQSRFPILKNHKNGKLLTSSRYRCEDCKQEFCVDCDVFIHEILHNCPGCESKPVIT
Protein: Estrogen receptor beta (ER-beta) (Nuclear receptor subfamily 3 group A member 2) (Q9IAK1)
Organism: Ictalurus punctatus (Channel catfish) (Silurus punctatus)
Function: Binds estrogens with an affinity similar to that of ER-alpha, and activates expression of reporter genes containing estrogen response elements (ERE) in an estrogen-dependent manner.
Subcellular location: Nucleus.
Interaction partners:
- Progesterone receptor
- Transcription factor Sp1
- histone acetyltransferase
- histone acetyltransferase
- Mediator of RNA polymerase II transcription subunit 1
- Nuclear receptor-interacting protein 1
- Nuclear receptor-interacting protein 1
- histone acetyltransferase
- histone acetyltransferase
- RING-type E3 ubiquitin transferase BRCA1
Sequence:
MSSSLSPTLQTVNGMDQDEPLPLFPSHYPTALGVDRGTVCIPSPYADNGHAEMSFCGPSAPENPAIAPPLSPSLFWSSHNPHAMPALPLHCPPALPYSEPHIHTAWVDTKPHTSGRHSSFLSRPKLFGKRPEDGDGDEALDDDDPSSSSSGAVVKRDMHFCVVCHDYASGYHYGVWSCEGCKAFFKRSIQGHNDYICPATNQCTIDKNRRKSCQACRLRKCYEMGMMKCGARRERCGYRASRRTAPMRDGSARPVGVRGQSQRLPHTPLHVSLSIPVSRASAESGFSGLSPEQLVYCILEAEPPQIYLKQQMKKPYTESTVMMSLTQLADKELVLMISWAKKIPGFVELSLAHQVQLLECCWLEVLMLGLMWRSIDHPGKLIFSLDLKLNRDEGNCVEGIMEIFDMLLAGSSRFRELKLQKEEYVCLKALILLNSSMYMTSSACEKDLESRTKLLRLLDAVTDALVWAISRTGLSTQQQSARLAHLLMLLSHIRHLSNKGMEHLSSMKRKNVVLLYDLLLEMLDANMAQSRHVSTSVCTDPVTPATSPNTPLPPQLHSPVAHHVTQVNESQCSQE
Protein: Rifin (C6KT17)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKLHYANILLFSLPLNILVASSSSNVNDQSNYVNITHHKPNIKSAKIQTTRLLCECDLYTSIYNNDTEMKNVMEIFNKQTEQRFEEYNERMNKNRQKCKEQCNKDIQKIILKDKIEKELKQNLDALHADITTKDIPTYVFEKSLSGKLEKTCLKCTYGLGSNVPLLGLINGVGIYATAQSAAMKVFISETIDGLKGIGGMSNLFGDKIADLVTPSFYGKPMHLVTTILSAKEKLCACPGMQKQILCHGLESVTEQSLPRRIATTASDAYYSAGEKFVELTNSGAIFSNPIVISTIVLLCIALMLLIIYLILRYRRKSRMKKKFQYIKLLKE
Protein: Alpha-actinin A (Actin-binding protein A) (F-actin cross-linking protein) (P05095)
Organism: Dictyostelium discoideum (Social amoeba)
Function: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. Increases the actin-stimulated ATPase activity of myosin. Involved in vegetative cell growth, phagocytosis, motility and development, probably through stabilization of the actin network in the cortical cytoskeleton.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:7820857}. Cytoplasm, cell cortex {ECO:0000269|PubMed:7820857}. Contractile vacuole {ECO:0000269|PubMed:7820857}. Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:7820857}. Note=Expressed diffusely throughout the cytoplasm. Accumulates in the cell cortex, contractile vesicle and phagosome.
Interaction partners:
- Actin domain-containing protein
Sequence:
MSEEPTPVSGNDKQLLNKAWEITQKKTFTAWCNSHLRKLGSSIEQIDTDFTDGIKLAQLLEVISNDPVFKVNKTPKLRIHNIQNVGLCLKHIESHGVKLVGIGAEELVDKNLKMTLGMIWTIILRFAIQDISIEELSAKEALLLWCQRKTEGYDRVKVGNFHTSFQDGLAFCALIHKHRPDLINFDSLNKDDKAGNLQLAFDIAEKELDIPKMLDVSDMLDVVRPDERSVMTYVAQYYHHFSASRKAETAGKQVGKVLDTFMLLEQTKSDYLKRANELVQWINDKQASLESRDFGDSIESVQSFMNAHKEYKKTEKPPKGQEVSELEAIYNSLQTKLRLIKREPFVAPAGLTPNEIDSTWSALEKAEQEHAEALRIELKRQKKIAVLLQKYNRILKKLENWATTKSVYLGSNETGDSITAVQAKLKNLEAFDGECQSLEGQSNSDLLSILAQLTELNYNGVPELTERKDTFFAQQWTGVKSSAETYKNTLLAELERLQKIEDSLVEFAKRAAQLNVWIEAADDHVFDPINVDSVQGVQEIQEKFDAFLHDQSQQFAELEALAALTQQLRELGRSENDYSVISYDELSAKWNNLLAGIEERKVQLANELTTQTNNDVLCQSFSVKANEISDYVRVTLDAISQNTSSDPQEQLNNIRAIITAHAEKKPELDELYTIASQLEEAQVVDNKHTQHSLESIKLKWDKLNTLAKKNEQVVEGEILAKQLTGVTAEELSEFKACFSHFDKDNDNKLNRLEFSSCLKSIGDELTEEQLNQVISKIDTDGNGTISFEEFIDYMVSSRKGTDSVESTKAAFKVMAEDKDFITEAQIRAAISDSKQIDYLLASMPAVEGGFDYNSFAEKLYQ
Protein: Parvalbumin alpha (P02625)
Organism: Rattus norvegicus (Rat)
Function: In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions.
Interaction partners:
- Calretinin
- Calbindin
- Glutamate decarboxylase 1
- Somatostatin
- 45 kDa calcium-binding protein
- Pro-neuropeptide Y
- Cholecystokinin
- Glutamate decarboxylase 2
- Neurotrophic factor BDNF precursor form
- Tyrosine 3-monooxygenase
Sequence:
MSMTDLLSAEDIKKAIGAFTAADSFDHKKFFQMVGLKKKSADDVKKVFHILDKDKSGFIEEDELGSILKGFSSDARDLSAKETKTLMAAGDKDGDGKIGVEEFSTLVAES