wanglab/gogpt-training-data huggingface dataset:
Protein: Teashirt homolog 1 (Serologically defined colon cancer antigen 3 homolog) (Q5DTH5)
Organism: Mus musculus (Mouse)
Function: Probable transcriptional regulator involved in developmental processes. May act as a transcriptional repressor (Potential).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MPRRKQQAPRRSAAYVPEEELKAAEIDEEHAEDGGLSLDIQESEFACNEETEIKEAQSYQNSPVSTATNQDAGYGSPFSEGSDQLAHFKSSSSREEKEESQCPDSVSYPQDSLAQIKAVYANLFSESCWSSLALDLKKSNSATSNNDASQKESSTPTPTPPTSTASTACTTATTAITSCSTSTSHSSTTSNSSSSGYDWHQAALAKTLQQTSSYGLLPEPSLFSTVQLYRQNNKLYGSVFTGASKFRCKDCSAAYDTLVELTVHMNETGHYRDDNRDKDSEKTKRWSKPRKRSLMEMEGKEDAQKVLKCMYCGHSFESLQDLSVHMIKTKHYQKVPLKEPVPAITKLVPSTKKRALQDLASPCSPEPTGVATEVALSESAKDQKTANPYVTPNNRYGYQNGASYTWQFEARKAQILKCMECGSSHDTLQQLTAHMMVTGHFLKVTTSASKKGKQLVLDPVVEEKIQSIPLPPTTHTRLPASSIKKQPDSPAGSVASEEKKEPEKEKEKEKAPPAAGDAERKIKEETEDATEKFEPTALYQYLREEDLDDSPKGGVDILKSLENTVSTAISKAQNGAPSWGGYPSIHAAYQLPGTVKPLQSAVQSVQIQPSYASSVKSLSSTEHNALLHSPGSLTPPPHKSNVSAMEELVEKVTGKVSIKKEERPTEKEKSSPVKAISPVAKENKDLPKTEETGSKPQKKGSDSETGKAKKESTLDAHTPNGTEPLKAKVTNGCGHLGIITDHSPEPSFINPLSALQSIMNTHLGKVSKPVSPSLDPLAMLYKISNSMLDKPVYPTTPAKQADAIDRYYYENSDQPIDLTKSKNKPLVSGVADAVSSPLRESALMDISDMVKNLTGRLTPKSSTPSTVSEKSDADGSSFEEALDELSPVHKRKGRQSNWNPQHLLILQAQFASSLRETAEGKYIMSDLGPQERVHISKFTGLSMTTISHWLANVKYQLRRTGGTKFLKNLDTGHPVFFCNDCASQFRTASTYVSHLETHLGFSLKDLSKLPLSQIQEQQSVVSKALTNKTLGPLGSSEEDLGSTFQCKLCNRTFASKHAVKLHLSKTHGKSPEDHLIYVTELEKQ
Protein: GDP-6-deoxy-D-mannose reductase (EC 1.1.1.281) (Q6T1X6)
Organism: Aneurinibacillus thermoaerophilus
Function: Reductase that catalyzes the conversion of GDP-6-deoxy-D-mannose to GDP-4-dehydro-6-deoxy-D-mannose (GDP-D-rhamnose).
Interaction partners:
Sequence:
MRALITGVAGFVGKYLANHLTEQNVEVFGTSRNNEAKLPNVEMISLDIMDSQRVKKVISDIKPDYIFHLAAKSSVKDSWLNKKGTFSTNVFGTLHVLDAVRDSNLDCRILTIGSSEEYGMILPEESPVSEENQLRPMSPYGVSKASVGMLARQYVKAYGMDIIHTRTFNHIGPGQSLGFVTQDFAKQIVDIEMEKQEPIIKVGNLEAVRDFTDVRDIVQAYWLLSQYGKTGDVYNVCSGIGTRIQDVLDLLLAMANVKIDTELNPLQLRPSEVPTLIGSNKRLKDSTGWKPRIPLEKSLFEILQSYRQA
Protein: LD29542p (Rabenosyn-5) (Q9VLS5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Vacuolar protein sorting-associated protein 45
- Ras-related protein Rab5
- small monomeric GTPase
- AT21416p
- HL02043p
- Rabaptin-5-associated exchange factor for Rab5
- LD23667p
- LD47384p
- Uncharacterized protein, isoform C
- Ras-related protein Rab7
Sequence:
MSGNPFDSDEDQSSASGEILEGFLCPICRADLKSIDVLTDHFARQHAEEEDALKSFKDIFTKAKKKILNPFEDEKGASVSSPAGSSSSAAGKNPNGNGDRNGPSNARSRLNVFNYMARQQPGAECSHFEYFQSIRNPRLERYASETNKLIIRLHRLLKDLPADSVQRRQHEQQTVAWLDGSSVKLCPSCAKSFHIARRQHHCRLCGGIMCNDCSKFLPLEDAMQLASLSTTRSEPLQQLHQHENAIRLCEHCLWLLDTRKDMHESRTCRPLLVQVYEQIRQLQKEVTPDLDMYLKIINSLNEGDTIFTLADAGALRGKIGQVAEAMDMRSKRILAIFCEPGSREEALKKAIRLGCIQAIKERMLSLPPLPEESHIRQMQERRRMETEQRILTEQRMAMEAYERNNMAANQSNVGVPGPESGSFAQGSDLQSLNNWSAPQAASKSSLDDPLIEQINIIKGYIKQARQDMNFEVVETLELNLRELQREVYERQRQSQGSTAASPTEA
Protein: Eomesodermin homolog (T-box brain protein 2) (T-brain-2) (TBR-2) (O95936)
Organism: Homo sapiens (Human)
Function: Functions as a transcriptional activator playing a crucial role during development. Functions in trophoblast differentiation and later in gastrulation, regulating both mesoderm delamination and endoderm specification. Plays a role in brain development being required for the specification and the proliferation of the intermediate progenitor cells and their progeny in the cerebral cortex. Also involved in the differentiation of CD8+ T-cells during immune response regulating the expression of lytic effector genes.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- T-cell surface glycoprotein CD8 alpha chain
- T-box transcription factor T
- Mothers against decapentaplegic homolog 2
- Granzyme K
- Homeobox protein MIXL1
- Catenin beta-1
- Forkhead box protein H1
- Mothers against decapentaplegic homolog 3
- Killer cell lectin-like receptor subfamily G member 1
- Transcription factor 7
Sequence:
MQLGEQLLVSSVNLPGAHFYPLESARGGSGGSAGHLPSAAPSPQKLDLDKASKKFSGSLSCEAVSGEPAAASAGAPAAMLSDTDAGDAFASAAAVAKPGPPDGRKGSPCGEEELPSAAAAAAAAAAAAAATARYSMDSLSSERYYLQSPGPQGSELAAPCSLFPYQAAAGAPHGPVYPAPNGARYPYGSMLPPGGFPAAVCPPGRAQFGPGAGAGSGAGGSSGGGGGPGTYQYSQGAPLYGPYPGAAAAGSCGGLGGLGVPGSGFRAHVYLCNRPLWLKFHRHQTEMIITKQGRRMFPFLSFNINGLNPTAHYNVFVEVVLADPNHWRFQGGKWVTCGKADNNMQGNKMYVHPESPNTGSHWMRQEISFGKLKLTNNKGANNNNTQMIVLQSLHKYQPRLHIVEVTEDGVEDLNEPSKTQTFTFSETQFIAVTAYQNTDITQLKIDHNPFAKGFRDNYDSSHQIVPGGRYGVQSFFPEPFVNTLPQARYYNGERTVPQTNGLLSPQQSEEVANPPQRWLVTPVQQPGTNKLDISSYESEYTSSTLLPYGIKSLPLQTSHALGYYPDPTFPAMAGWGGRGSYQRKMAAGLPWTSRTSPTVFSEDQLSKEKVKEEIGSSWIETPPSIKSLDSNDSGVYTSACKRRRLSPSNSSNENSPSIKCEDINAEEYSKDTSKGMGGYYAFYTTP
Protein: Junctophilin-1 (Q22667)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Endomembrane system {ECO:0000256|ARBA:ARBA00004184}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004184}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004163}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004163}.
Interaction partners:
- Importin N-terminal domain-containing protein
- Stromal interaction molecule 1
- MHD domain-containing protein
- AP-1 complex subunit mu-1-I
- Voltage-dependent L-type calcium channel subunit alpha
- Phosphatidylinositol-3,5-bisphosphate 3-phosphatase mtm-1
- Voltage-dependent calcium channel type A subunit alpha-1
- Calsequestrin
Sequence:
MNGGRFDFDDGGTYVGGWEEGKAHGHGVCTGPQAKGEYAGAWHYGFEVSGVYTWPSGNTYQGQWQNGKRHGLGIEQRGRWLYKGEWTQGYKGRYGVRQSANSQARYQGTWSAGFHDGYGTEIYVDSGSYQGQWLRGMRHGYGIRKSTTYEKAAKFRSKSQTHASLTSLRSGRVEEENAAEEHRHKEGLSGRGGFVLRANSSAPQRRRRSLSERSLAVKRTLLSGLRIKKQHSTGDIHQRVASMTGSLRSSGSTMSCTSEDSLHHHGLQQPEEEAVEESSIETYMGEWKNDMRSGFGVCERSDGLKYQGEWANNAKCGYGVTTFKDGTKEEGRYKNNILIASSRRKGVIFMRASKFREKLEQALGAASRAASIAQQKADIAASRTSTARERSEQASFIARQANDDSEVARIHAKQFDPSFKQPGTRRLLKDNNGGESFGTDLSDAISYSRHLSQTHSKQHSFEQTLSVDMAEDMTPPSKAYHNHVMPNSNTNHVNFMPQYGYSDPNSQLQTPINSQDLLQPHIPNIDPSIPSVSIVQDDEKPLILQPQTNISQPGPSNLSTQAPNVMSSRFSLSDDHYDQYVMAGGAQQQQKLRRNRPSLMRQADVNESCAASGLNRRSTLASARDRNGDVNHPGAIGATHAAKLTAATSDGDNMGSLPNLAELETQGVRLRREEAARLAGQRRQEVLRENEEAALLRANPLRHFLQPAFRAWLVRWRIPILLAIANISLLMLFYHLLTYEKKKKSSS
Protein: MADS-box transcription factor ANR1 (Protein AGAMOUS-LIKE 44) (Protein ARABIDOPSIS NITRATE REGULATED 1) (Q9SI38)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor. Required for root plasticity in response to nitrate, NO(3)(-). Promotes lateral root growth in a NRT1.1-dependent manner.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein NRT1/ PTR FAMILY 6.3
- Protein NLP7
- LOB domain-containing protein 37
- Protein NLP6
- High-affinity nitrate transporter 2.1
- CBL-interacting serine/threonine-protein kinase 8
- Transcription factor TCP20
- Transcription factor TGA1
- Nitrate regulatory gene2 protein
- Protein AUXIN SIGNALING F-BOX 3
Sequence:
MGRGKIVIRRIDNSTSRQVTFSKRRSGLLKKAKELSILCDAEVGVIIFSSTGKLYDYASNSSMKTIIERYNRVKEEQHQLLNHASEIKFWQREVASLQQQLQYLQECHRKLVGEELSGMNANDLQNLEDQLVTSLKGVRLKKDQLMTNEIRELNRKGQIIQKENHELQNIVDIMRKENIKLQKKVHGRTNAIEGNSSVDPISNGTTTYAPPQLQLIQLQPAPREKSIRLGLQLS
Protein: NmrA-like family domain-containing protein 1 (Q9HBL8)
Organism: Homo sapiens (Human)
Function: Redox sensor protein. Undergoes restructuring and subcellular redistribution in response to changes in intracellular NADPH/NADP(+) levels. At low NADPH concentrations the protein is found mainly as a monomer, and binds argininosuccinate synthase (ASS1), the enzyme involved in nitric oxide synthesis. Association with ASS1 impairs its activity and reduces the production of nitric oxide, which subsecuently prevents apoptosis. Under normal NADPH concentrations, the protein is found as a dimer and hides the binding site for ASS1. The homodimer binds one molecule of NADPH. Has higher affinity for NADPH than for NADP(+). Binding to NADPH is necessary to form a stable dimer.
Subcellular location: Cytoplasm. Cytoplasm, perinuclear region. Nucleus. Note=Under normal redox growth conditions localizes in the cytoplasm and perinuclear region. Nuclear localization is promoted by increased intracellular nitric oxide and reduced NADPH/NADP(+) ratios.
Interaction partners:
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- NADH dehydrogenase flavoprotein 1, mitochondrial
- Argininosuccinate synthase
- NADH dehydrogenase 1 alpha subcomplex subunit 8
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 12
- Ubiquitin carboxyl-terminal hydrolase 7
Sequence:
MVDKKLVVVFGGTGAQGGSVARTLLEDGTFKVRVVTRNPRKKAAKELRLQGAEVVQGDQDDQVIMELALNGAYATFIVTNYWESCSQEQEVKQGKLLADLARRLGLHYVVYSGLENIKKLTAGRLAAAHFDGKGEVEEYFRDIGVPMTSVRLPCYFENLLSHFLPQKAPDGKSYLLSLPTGDVPMDGMSVSDLGPVVLSLLKMPEKYVGQNIGLSTCRHTAEEYAALLTKHTRKVVHDAKMTPEDYEKLGFPGARDLANMFRFYALRPDRDIELTLRLNPKALTLDQWLEQHKGDFNLL
Protein: Protein ISD11 (Iron-sulfur protein biogenesis, desulfurase-interacting protein 11) (Q6Q560)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for mitochondrial iron-sulfur proteins biosynthesis.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16341090, ECO:0000269|PubMed:16823961}.
Interaction partners:
- Frataxin homolog, mitochondrial
- Cysteine desulfurase, mitochondrial
- Iron sulfur cluster assembly protein 1, mitochondrial
- Acyl carrier protein, mitochondrial
- Iron sulfur cluster assembly protein 2, mitochondrial
- Adrenodoxin homolog, mitochondrial
- GTP-binding protein YPT1
- Probable NADPH:adrenodoxin oxidoreductase, mitochondrial
- Iron-sulfur cluster assembly factor IBA57, mitochondrial
- NifU-like protein
Sequence:
MPGFTAPTRRQVLSLYKEFIKNANQFNNYNFREYFLSKTRTTFRKNMNQQDPKVLMNLFKEAKNDLGVLKRQSVISQMYTFDRLVVEPLQGRKH
Protein: CASP8 and FADD-like apoptosis regulator, isoform CRA_b (FLIP short form) (Q99MZ5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MALSTVSAEVIHQVEESLDEDEKEMMLFLCRDVTENLAPPNVRDLLDCLSERGQLSFAALAELLYRVRRFDLLKRILKTDKAAVEDHLCRSPHLVSDYRVLLMEIGENLNQSDVSSLIFLTKDYTGRGKVAKDKSFLDLVIELEKLNLIGSDQLNLLEKCLKSIHRIDLKTKIQKYTQSSQEARSNMNALQASLPKLSIKEHLYNSRVSLEPVCGISA
Protein: L-gulonate 3-dehydrogenase (EC 1.1.1.45) (L-gulonate 3-dehydrogenase) (Q9VXI1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- EG:BACR7A4.14 protein
- HL08109p)
- Probable enoyl-CoA hydratase, mitochondrial
- LD24679p
- Beta hydroxy acid dehydrogenase 2
- Acetyl-CoA acetyltransferase 1, isoform A)
- acetyl-CoA C-acyltransferase
- Uncharacterized protein, isoform A
- Acetyl-CoA acetyltransferase 2
- RH57257p)
Sequence:
MSAKNEKVGIVGSGLIGRSWSMLFASVGYQVVLYDILPEQVSTALTATQKELQDLEAKGLLRGKLTAAQQFACISGTNDLKELVKGAIFVQECIPERLDLKKALYKQLDAVVGPNTILSSSTSTFLPSLFSADLKNKANVLVSHPVNPPYYVPLVEIVPAPWTKPEWVKKTRALMEEIGQKPVTLSREIEGFALNRIQYAILNETWRLVEAGILNVKDIDSVMSNGLGPRYAFLGPLETAHLNAEGMANYFERYSNTIYAVSETMGPTPKMEGPVAVEVAKQLGEMVPLDQLAQRRNYRDNCLTQLSILKNKLNQ
Protein: Oxidoreductase vrtI (EC 1.14.-.-) (Viridicatumtoxin synthesis protein I) (D7PHZ1)
Organism: Penicillium aethiopicum
Function: Oxidoreductase; part of the gene cluster that mediates the biosynthesis of viridicatumtoxin, a tetracycline-like fungal meroterpenoid with a unique, fused spirobicyclic ring system. The first step of the pathway is the production of the malonamoyl-CoA starter unit for the polyketide synthase vrtA. The aldolase vrtJ may be involved in the synthesis of the malonamate substrate for malonamoyl-CoA synthetase vrtB. The polyketide synthase vrtA then may utilize the malonamoyl-CoA starter unit, followed by sequential condensation of eight malonyl-CoA units to form the polyketide backbone. The cyclization of the last ring could be mediated by the lactamase-like protein vrtG. The proposed post-PKS tailoring steps are an hydroxylation at C5 catalyzed the cytochrome P450 monooxygenase vrtE, a hydroxylation at C12a catalyzed by VrtH and/or VrtI, and an O-methylation by the O-methyltransferase vrtF. VrtC is then proposed to catalyze the transfer of a geranyl group synthesized by vrtD to the aromatic C ring of the tetracyclic polyketide intermediate of viridicatumtoxin to yield previridicatumtoxin. Finally, the cytochrome P450 monooxygenase vrtK catalyzes the spirocyclization of the geranyl moiety of previridicatumtoxin to afford viridicatumtoxin.
Interaction partners:
Sequence:
MGARSKEARHRWFSRLPPDASSSFLPCKRPKSVAFVLWIRPSCFLRESLPAELSGLPGLPLPPQAPTNTMNCGLPEAALSVIDWGRLKSGDVNEGARLLSACDDQGFFYLDLSSEPSFLHDHKSVLHFMDQYFHQGLADKMKDDRQSDTHGYEPVATSTGALNTLPDYYESLKASRDELHGDGRNLAPAVCDRQDLFLRFSDMMHQMVIAILQELDCQLGFGGDRASFQDFHRKDAESLTTLSMFRYPKQETLDLGVGHNKHTDIGTLTFLLCDQWGLQVLSKDPAGWRFVAPREGHAVINVGDTLRFLSGNRFRSAVHRVIPTQRLQHEDRYSIAYFLRAANDTQFTDSAGRQVSAKQWHDEKFDVFRETHEEQEKMPILTGGMERLENLPGIWCGVRLTDGICHRLGAEDC
Protein: Protein couch potato (Q01617)
Organism: Drosophila melanogaster (Fruit fly)
Function: May play a role in the development or function of the peripheral nervous system by regulating the processing of nervous system-specific transcripts.
Subcellular location: Nucleus {ECO:0000269|PubMed:1427076}.
Interaction partners:
Sequence:
MLGSHHQLLIAATAAAAAAAAAEPQLQLQHLLPAAPTTPAVISNPINSIGPINQISSSSHPSNNNQQAVFEKAITISSIAIKRRPTLPQTPASAPQVLSPSPKRQCAAAVSVLPVTVPVPVPVSVPLPVSVPVPVSVKGHPISHTHQIAHTHQISHSHPISHPHHHQLSFAHPTQFAAAVAAHHQQQQQQQAQQQQQAVQQQQQQAVQQQQVAYAVAASPQLQQQQQQQQHRLAQFNQAAAAALLNQHLQQQHQAQQQQHQAQQQSLAHYGGYQLHRYAPQQQQQHILLSSGSSSSKHNSNNNSNTSAGAASAAVPIATSVAAVPTTGGSLPDSPAHESHSHESNSATASAPTTPSPAGSVTSAAPTATATAAAAGSAAATAAATGTPATSAVSDSNNNLNSSSSSNSNSNAIMENQMALAPLGLSQSMDSVNTASNEEEVRTLFVSGLPMDAKPRELYLLFRAYEGYEGSLLKVTSKNGKTASPVGFVTFHTRAGAEAAKQDLQGVRFDPDMPQTIRLEFAKSNTKVSKPKPQPNTATTASHPALMHPLTGHLGGPFFPGGPELWHHPLAYSAAAAAELPGAAALQHATLVHPALHPQVPVRSYL
Protein: CCA tRNA nucleotidyltransferase 1, mitochondrial (EC 2.7.7.72) (Mitochondrial tRNA nucleotidyl transferase, CCA-adding) (mt CCA-adding enzyme) (mt tRNA CCA-diphosphorylase) (mt tRNA CCA-pyrophosphorylase) (mt tRNA adenylyltransferase) (Q96Q11)
Organism: Homo sapiens (Human)
Function: Adds and repairs the conserved 3'-CCA sequence necessary for the attachment of amino acids to the 3' terminus of tRNA molecules, using CTP and ATP as substrates.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11256614, ECO:0000269|PubMed:27317422, ECO:0000305|PubMed:11504732}. Cytoplasm {ECO:0000269|PubMed:27317422, ECO:0000305|PubMed:11504732}. Nucleus {ECO:0000269|PubMed:27317422}.
Interaction partners:
- Gamma-crystallin D
- Polyribonucleotide nucleotidyltransferase 1, mitochondrial
- Beta-crystallin B2
- Proline-rich protein 9
- N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase
- Gamma-crystallin B
- Zinc phosphodiesterase ELAC protein 2
- Beta-crystallin B3
- Transcription factor Maf
- tRNA dimethylallyltransferase
Sequence:
MLRCLYHWHRPVLNRRWSRLCLPKQYLFTMKLQSPEFQSLFTEGLKSLTELFVKENHELRIAGGAVRDLLNGVKPQDIDFATTATPTQMKEMFQSAGIRMINNRGEKHGTITARLHEENFEITTLRIDVTTDGRHAEVEFTTDWQKDAERRDLTINSMFLGFDGTLFDYFNGYEDLKNKKVRFVGHAKQRIQEDYLRILRYFRFYGRIVDKPGDHDPETLEAIAENAKGLAGISGERIWVELKKILVGNHVNHLIHLIYDLDVAPYIGLPANASLEEFDKVSKNVDGFSPKPVTLLASLFKVQDDVTKLDLRLKIAKEEKNLGLFIVKNRKDLIKATDSSDPLKPYQDFIIDSREPDATTRVCELLKYQGEHCLLKEMQQWSIPPFPVSGHDIRKVGISSGKEIGALLQQLREQWKKSGYQMEKDELLSYIKKT
Protein: Paraflagellar rod component (Q38A18)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEKTQPFNDLICQVARVGVTNVQWCGEKMNDSQLDTLISAMELSPVRIENINLSKNEITSAGASLLCTYIKKNSNIKEVYLNENLIDDAGAREFISIFNNQVHPTIFDVSGNQCSSAVVNNLALLAKQDQHSKEIHQSLLAGEAEELDISGMNINKIDPRLLTFFILDTHALRSLIVSGCAAGDAGATLIGDLLKNSAVSHVDLSDNDISDAGVSQFIERADLLHHPTITSISFSKNIRISNYGMQQMSKTLFNTNDVITSFDVSDTSVTSSVRSTIAHECELNKEPSCLKRAVAAIRTNDPSCTSVNLQWERLTQTAARFVAPVLKLNTIMLELNLGNTSAGDKGAELLAAALQQNKTLRILGLANNNITSRGAKVLFQRLHQQGVLEELNLANNRIDDEAETSILNTLQLNPTIKVLNLVNNLLSGDCMSEIDELILLNQAPKTVQTIVSDIENRPASVTKVALSGKTGEEYCNDTSVRILCNALVLNKVVTTVDLSKNVVGDIGVTYLCEMLMTNSTIVELNLESNSITDRGAQRLAHALRTNASLQHLNLSNNSITDVGAGDFVDTLRFNYALTSILFEKTTVTSDLRTKIAEAADMNKEPRGFKDVMYMLRDGSIKTPKLDLARKNCPRPITDESVNTLCVQLRGISVVRELILSGNSVGTEGCKSIGKLLAHEGSGICHIDLSLNPVDDEGLGELAKGLLSKNCVLQILNLRGTEVTSTGIINLTNTVKANATLREVIVPERVSADVFCRMNQELMVNAQPKSLKPLLTSINENEVIPLLVFKDPVLPFTDAACHLLCAAIVNNEHITSVDMSNNKLTSDSVPFIAEALSSCPKITSVNLSHNEIDETGGYELVKCLAENDYVTTLSLEGNPIPEEVIFKLNELLHLNRGSIDLKKILLKHRKGRLADKTINLNSKGKQYKLNDEDVRLLCEVMVECGSIRAVDLGMNMITDVGCEMIADALLQAPRIEAIYLDYNPIGEIGGEALYNVLKVNHQIHTLLLEGTNVPEEIWEEILSLLRVNETANHERIDMRAIRLEEVNDETQFRSTDYAISQEQKVGIDAFKAYESSVRALVKE
Protein: Protein XRP2 (Q966I6)
Organism: Caenorhabditis elegans
Interaction partners:
- ADP-ribosylation factor-like protein 3
- Protein unc-119
- ADP-ribosylation factor-like protein 13B
- Nephrocystin-1-like protein
- NePHronoPhthisis
- Cytoplasmic dynein 2 light intermediate chain 1
- Cyclin-dependent kinase-like 1
- MecKel-Gruber Syndrome
- B9 domain-containing protein 2
- Transmembrane protein 107
Sequence:
MSCCFSKKLFGRRSKREDRYKVSEDAVPKPEEGGEPPKYSWDRREKVNAEDFTIANIHNTTLKKESKDGGPLQMENCTDSTILYLYQTSQVIIDDCRHCTIVLGPAAGSVFVRDCANCTIFTSCQQLRTRDCTSIRISILCPTEPIVENSSDIHFFHLAMRYPELKDQMHAVGLRPFTNRIASVHDFTPAGVNGKGNFRVTPEVVQISDGQEEILRAKGVILKPSPADFIPRFTDTTDPDPTFLYVLGKSEPVDELGDRAIELLHAIYKSGMQVMGTCDLETSTVDSKLVPFAGQAERMILFQLKGNLANLECDVEFDVMSENDLVPLRNLLIHLEGKKNG
Protein: Vasoactive intestinal peptide receptor 1b (F1R383)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Vasoactive intestinal peptide b.
- VIP peptides
- Adcyap1a protein
- Adcyap1b protein
- Somatoliberin
- Glucagon b
Sequence:
MDASKVVLLASAFGFVFSPVAAVQMCDVVNEIELARARCENKTAGNVTSGCKGMWDIIACWPSAKIGEHVVIPCPNYFRHFSDQHEGNLSKTCTADGWTEMDSLEIAVNCGYNLNGTVDDDSFFRSVKIGYTIGHSVSLISLTTAIAILCIFRKLHCTRNYIHMHLFVSFILKAIAVFVKDAVLYDVVQESDNCSTGSVGCKAVIVFFQYCIMASFFWLLVEGLYIHALLAVSFFSERKYFWCYILIGWGGPTVFIMAWSFAKAYFNDVGCWDIIENSDPFWWIIKTPILASILMNFILFICIIRILRQKINCPDIGRNESNQYSRLAKSTLLLIPLFGINFIIFAFIPENIKTELRLVFDLILGSFQGFVVAVLYCFLNGEVQGEIKRKWRRWHLERFLGPDTKYQHPSMGSNGNNFSTQISMLTRCSPKTRRASTCQDETSITV
Protein: Tubulin--tyrosine ligase (TTL) (EC 6.3.2.25) (Q8NG68)
Organism: Homo sapiens (Human)
Function: Catalyzes the post-translational addition of a tyrosine to the C-terminal end of detyrosinated alpha-tubulin.
Interaction partners:
- Tubulin alpha-1A chain
- Tubulin alpha-1B chain
- Tubulin beta-2A chain
- Tubulin beta-2B chain
- Stathmin-4
- Enhancer of mRNA-decapping protein 3
- CAP-Gly domain-containing linker protein 1
- Small vasohibin-binding protein
Sequence:
MYTFVVRDENSSVYAEVSRLLLATGHWKRLRRDNPRFNLMLGERNRLPFGRLGHEPGLVQLVNYYRGADKLCRKASLVKLIKTSPELAESCTWFPESYVIYPTNLKTPVAPAQNGIQPPISNSRTDEREFFLASYNRKKEDGEGNVWIAKSSAGAKGEGILISSEASELLDFIDNQGQVHVIQKYLEHPLLLEPGHRKFDIRSWVLVDHQYNIYLYREGVLRTASEPYHVDNFQDKTCHLTNHCIQKEYSKNYGKYEEGNEMFFKEFNQYLTSALNITLESSILLQIKHIIRNCLLSVEPAISTKHLPYQSFQLFGFDFMVDEELKVWLIEVNGAPACAQKLYAELCQGIVDIAISSVFPPPDVEQPQTQPAAFIKL
Protein: Serine/threonine-protein phosphatase 2A regulatory subunit psrA (Protein PPP2R5A/B56 homolog) (Protein phosphatase 2A regulatory B subunit) (Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit) (protein phosphatase 2A B56 regulatory subunit homolog) (Q54VB6)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Involved in developmental cell fate decision.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:18673380}.
Interaction partners:
- Serine/threonine-protein phosphatase 2A catalytic subunit A
- Protein phosphatase 2A scaffold subunit
- Serine/threonine-protein phosphatase 2A regulatory subunit phr2AB
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B
- EF-hand domain-containing protein
- Probable inactive serine/threonine-protein kinase bub1
- Probable protein phosphatase methylesterase 1
- Serine/threonine-protein phosphatase 4 catalytic subunit
- Protein phosphatase 4 regulatory subunit 1
- Uncharacterized protein
Sequence:
MKNDHINYQQNLSQSPILNSNKNQTQQNQQQQQQQQQQNPQQQQQFQHQQVPQLSPQQIPFSEPLKNNLTLQHQQQQQQHQQLAGGQHGSLLRKSYSSRFHEKPQGELTKIANFQDVSPEERPSLFLLKLKQCCYVYDFSDNTYMVSKGVKQEALLQCVNFLSTNDQPLHESIYKMVFEMVAVNLFRPLPPRINPYGVMYDPEEDEPILEAAWPHIQVVYEVLLRFIDSPTFNTHIAKNYVDDRFVLQMLDLFDSEDPRERDYLKTTLHRIYGKFLGLRGFIRTAIRNLFCTFVYESHQHNGISEILEVLGSIINGFLVPLKDEHKQFLIKVLIPLHKPKSYSVYCSHLGYCMSQFIEKEPSLAEPIFKSILRLWPCGNSQKEVLFLSEMEDLLGLVSDEQFAKFRNQFFRQMTKCFQSEHFQVAERALYLFSNENIVLLIASKNNFTLALETFYKPLHENSISHWNRSIRNLSISSLKLFMEIDMDLFNKISEKYKESKKKQQQIQQREKFKQNAPETQKSKQINQNNNNNNNNINNNNNNNNNNNGSTETKADKPSMIRRKSLLPVDPSTIAALSSHRSLEDIMSTNSNSGNDDDDENNHTNHDSEIENEVKEDFRVPVNNRYTFT
Protein: Candida glabrata strain CBS138 chromosome M complete sequence (Q6FJ02)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Large ribosomal subunit protein uL23
- RP41
- 40S ribosomal protein S8
- Small ribosomal subunit protein eS21
- Candida glabrata strain CBS138 chromosome A complete sequence
- L21
- 60S acidic ribosomal protein P0
- Large ribosomal subunit protein eL32
- Small ribosomal subunit protein uS5
- Candida glabrata strain CBS138 chromosome M complete sequence
Sequence:
MSSTTVRNSNWRLVEVGRVVLVKKGQSAGKLAAIVEIIDQKQVLIDGPETGVPRQSINLGQVVLTPLTFTLPRGARTSIVSKKWAAAQVTESWKASSWAKKIAQRERRSALSDFERFQVMVLKKQKRYTVKKALAKA
Protein: Protein wntless homolog B (XWntless) (Integral membrane protein GPR177-B) (Q5FWK6)
Organism: Xenopus laevis (African clawed frog)
Function: Required for a subset of Wnt-dependent developmental processes, in particular, eye and pronephros development. Regulates the secretion of wnt4, which is required for eye development.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MAGAIIENMSTKKLCMVGVALLLLQVLAFLVGGLIAPKPTTYVNPVAMKCIDVRKSHRSSKWLMPWGTEPCKSIQSFDEAANRLIEANDIVFAAHIPNSQFEMSPWFQFMLVVLQLDIAFKLNNYIEDHSMVTLDVAVAYRDDLKEEWKELARSVEQRKLNCILPVDKTVANEGRHYDCDVIPLMELGSVSHKYYLFNIRLPVNERQKMNIGIGEIRDMHVVSIFQNGGFTMVWFAMKTFLTPCIIIIMIWYWRRITMMTRSPVLLEKVIFALGISMTFINIPVEWFSIGYDWTWMLLFGDIRQGIFYAMLLSFWIIFCGEHMMDQAERNRISIYWKQVGPIAFGSCCLFIFDMCERGVQLKNPFYSIWTTDVGAEIAMAFIIVAGICACLYFLFLCFMVYQVFRNISGKRSNLPAMSKARRLHYEGLIFRFKFLMIITLACAALTVVFFITTQITEGNWKLGDLSIELNSAFFTGIYGMWNLYVFALMFLYAPSHKHYGDGQSNDGAGMSSGEELQLTTTITHIDGPTELYRLAGKEAQE
Protein: ATP synthase epsilon chain (ATP synthase F1 sector epsilon subunit) (F-ATPase epsilon subunit) (P26533)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Subcellular location: Cellular thylakoid membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- ATP synthase subunit a
- ATP synthase subunit c
- ATP synthase subunit b'
- ATP synthase subunit alpha
- ATP synthase subunit beta
- ATP synthase subunit b
- Hydrogenase subunit
- ATP synthase gamma chain
- ATP synthase subunit delta
- NAD
Sequence:
MTLTVRVITPDKVVWDEEVQELILPSTTGQLGILSNHAPLLTALEIGVMRVRPGKDWQNIAVMGGFAEVENNEVKVLVNGAELGTTIDAESARQAYTAAQGALEEANRGEDKPNQLKASNNYKKARARLQAAGGAV