wanglab/gogpt-training-data huggingface dataset:
Protein: POU domain, class 2, transcription factor 3 (Octamer-binding protein 11) (Oct-11) (Octamer-binding transcription factor 11) (OTF-11) (Transcription factor PLA-1) (Transcription factor Skn-1) (Q9UKI9)
Organism: Homo sapiens (Human)
Function: Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3') and regulates cell type-specific differentiation pathways. Involved in the regulation of keratinocytes differentiation. The POU2F3-POU2AF2/POU2AF3 complex drives the expression of tuft-cell-specific genes, a rare chemosensory cells that coordinate immune and neural functions within mucosal epithelial tissues.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P31362}.
Interaction partners:
- POU domain, class 2, transcription factor 1
- POU domain, class 2, transcription factor 2
- DDB1- and CUL4-associated factor 11
- Phospholipase A1 member A
- Lipase member H
- Endothelial lipase
- Small proline-rich protein 2A
- Transient receptor potential cation channel subfamily M member 5
- ETS-related transcription factor Elf-3
- Lysophosphatidic acid receptor 3
Sequence:
MVNLESMHTDIKMSGDVADSTDARSTLSQVEPGNDRNGLDFNRQIKTEDLSDSLQQTLSHRPCHLSQGPAMMSGNQMSGLNASPCQDMASLHPLQQLVLVPGHLQSVSQFLLSQTQPGQQGLQPNLLPFPQQQSGLLLPQTGPGLASQAFGHPGLPGSSLEPHLEASQHLPVPKHLPSSGGADEPSDLEELEKFAKTFKQRRIKLGFTQGDVGLAMGKLYGNDFSQTTISRFEALNLSFKNMCKLKPLLEKWLNDAESSPSDPSVSTPSSYPSLSEVFGRKRKKRTSIETNIRLTLEKRFQDNPKPSSEEISMIAEQLSMEKEVVRVWFCNRRQKEKRINCPVATPIKPPVYNSRLVSPSGSLGPLSVPPVHSTMPGTVTSSCSPGNNSRPSSPGSGLHASSPTASQNNSKAAVNSASSFNSSGSWYRWNHSTYLH
Protein: lysozyme (EC 3.2.1.17) (Q7JYZ0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- lysozyme
- lysozyme
- lysozyme
- Uncharacterized protein, isoform B
Sequence:
MAANKLCCTLAIGALLCLGFAALIQAQDKPVTDVCLGCICEAISGCNQTRYCGGGVCGLFRITWAYWADGGKLTLGNESPQSEDAYANCVNDPYCAANTIQNYMTKFGQDCNGDNAIDCYDFAAIHKLGGYGCKGELSYQYQTQLTNCLNSFQQIDVRSSI
Protein: Regulator of G-protein signaling egl-10 (F5GUC9)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MALPRLRVNASNEERLVHPNHMVYRKMEMLVNQMLDAEAGVPIKTVKSFLSKVPSVFTGQDLIGWIMKNLEMTDLSDALHLAHLIASHGYLFQIDDHVLTVKNDGTFYRFQTPYFWPSNCWDPENTDYAVYLCKRTMQNKAHLELEDFEAENLAKLQKMFSRKWEFVFMQAEAQYKVDKKRDRQERQILDSQERAFWDVHRPVPGCVNTTEVDFRKLSRSGRPKYSSGGHAALAASTSGIGCTQYSQSVAAAHASLPSTSNGSATSPRKNDQEPSTSSGGESPSTSSAAAGTATTSAPSTSTPPVTTITATINAGSFRNNYYTRPGLRRCTQVQDTLKLEIVQLNSRLSKNVLRTSKVVENYLAYYEQRRVFDPLLTPPGSQADPFQSQPNPWINDTVDFWQHDKITGDIQTRRLKLWEDSFEELLADSLGRETLQKFLDKEYSGENLRFWWEVQKLRKCSSRMVPVMVTEIYNEFIDTNAATSPVNVDCKVMEVTEDNLKNPNRWSFDEAADHIYCLMKNDSYQRFLRSEIYKDLVLQSRKKTTFTSLIARKASRRIGSTMSRSSQSNKTLHASASLGSALSGHGSSTSSMLTAGGAASSQNLLLAPPQHHLYVPSLSLSYTHTQHSLPMKCRMNVVF
Protein: IQ motif and SEC7 domain-containing protein 2 (Q5JU85)
Organism: Homo sapiens (Human)
Function: Is a guanine nucleotide exchange factor for the ARF GTP-binding proteins.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- ADP-ribosylation factor 1
- BAR/IMD domain-containing adapter protein 2
- Disks large homolog 4
- Lysine-specific demethylase 5C
- Structural maintenance of chromosomes protein 1A
Sequence:
MEAGSGPPGGPGSESPNRAVEYLLELNNIIESQQQLLETQRRRIEELEGQLDQLTQENRDLREESQLHRGELHRDPHGARDSPGRESQYQNLRETQFHHRELRESQFHQAARDVGYPNREGAYQNREAVYRDKERDASYPLQDTTGYTARERDVAQCHLHHENPALGRERGGREAGPAHPGREKEAGYSAAVGVGPRPPRERGQLSRGASRSSSPGAGGGHSTSTSTSPATTLQRKSDGENSRTVSVEGDAPGSDLSTAVDSPGSQPPYRLSQLPPSSSHMGGPPAGVGLPWAQRARLQPASVALRKQEEEEIKRSKALSDSYELSTDLQDKKVEMLERKYGGSFLSRRAARTIQTAFRQYRMNKNFERLRSSASESRMSRRIILSNMRMQFSFEEYEKAQNPAYFEGKPASLDEGAMAGARSHRLERGLPYGGSCGGGIDGGGSSVTTSGEFSNDITELEDSFSKQVKSLAESIDEALNCHPSGPMSEEPGSAQLEKRESKEQQEDSSATSFSDLPLYLDDTVPQQSPERLPSTEPPPQGRPEFWAPAPLPPVPPPVPSGTREDGSREEGTRRGPGCLECRDFRLRAAHLPLLTIEPPSDSSVDLSDRSDRGSVHRQLVYEADGCSPHGTLKHKGPPGRAPIPHRHYPAPEGPAPAPPGPLPPAPNSGTGPSGVAGGRRLGKCEAAGENSDGGDNESLESSSNSNETINCSSGSSSRDSLREPPATGLCKQTYQRETRHSWDSPAFNNDVVQRRHYRIGLNLFNKKPEKGIQYLIERGFLSDTPVGVAHFILERKGLSRQMIGEFLGNRQKQFNRDVLDCVVDEMDFSSMDLDDALRKFQSHIRVQGEAQKVERLIEAFSQRYCVCNPALVRQFRNPDTIFILAFAIILLNTDMYSPSVKAERKMKLDDFIKNLRGVDNGEDIPRDLLVGIYQRIQGRELRTNDDHVSQVQAVERMIVGKKPVLSLPHRRLVCCCQLYEVPDPNRPQRLGLHQREVFLFNDLLVVTKIFQKKKILVTYSFRQSFPLVEMHMQLFQNSYYQFGIKLLSAVPGGERKVLIIFNAPSLQDRLRFTSDLRESIAEVQEMEKYRVESELEKQKGMMRPNASQPGGAKDSVNGTMARSSLEDTYGAGDGLKRGALSSSLRDLSDAGKRGRRNSVGSLDSTIEGSVISSPRPHQRMPPPPPPPPPEEYKSQRPVSNSSSFLGSLFGSKRGKGPFQMPPPPTGQASASSSSASSTHHHHHHHHHGHSHGGLGVLPDGQSKLQALHAQYCQGPGPAPPPYLPPQQPSLPPPPQQPPPLPQLGSIPPPPASAPPVGPHRHFHAHGPVPGPQHYTLGRPGRAPRRGAGGHPQFAPHGRHPLHQPTSPLPLYSPAPQHPPAHKQGPKHFIFSHHPQMMPAAGAAGGPGSRPPGGSYSHPHHPQSPLSPHSPIPPHPSYPPLPPPSPHTPHSPLPPTSPHGPLHASGPPGTANPPSANPKAKPSRISTVV
Protein: Acyl-CoA dehydrogenase family member 10 (ACAD-10) (EC 1.3.99.-) (Q6JQN1)
Organism: Homo sapiens (Human)
Function: Acyl-CoA dehydrogenase only active with R- and S-2-methyl-C15-CoA.
Interaction partners:
- Methylthioribose-1-phosphate isomerase
- Hydroxysteroid dehydrogenase-like protein 2
- Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
Sequence:
MCVRSCFQSPRLQWVWRTAFLKHTQRRHQGSHRWTHLGGSTYRAVIFDMGGVLIPSPGRVAAEWEVQNRIPSGTILKALMEGGENGPWMRFMRAEITAEGFLREFGRLCSEMLKTSVPVDSFFSLLTSERVAKQFPVMTEAITQIRAKGLQTAVLSNNFYLPNQKSFLPLDRKQFDVIVESCMEGICKPDPRIYKLCLEQLGLQPSESIFLDDLGTNLKEAARLGIHTIKVNDPETAVKELEALLGFTLRVGVPNTRPVKKTMEIPKDSLQKYLKDLLGIQTTGPLELLQFDHGQSNPTYYIRLANRDLVLRKKPPGTLLPSAHAIEREFRIMKALANAGVPVPNVLDLCEDSSVIGTPFYVMEYCPGLIYKDPSLPGLEPSHRRAIYTAMNTVLCKIHSVDLQAVGLEDYGKQGDYIPRQVRTWVKQYRASETSTIPAMERLIEWLPLHLPRQQRTTVVHGDFRLDNLVFHPEEPEVLAVLDWELSTLGDPLADVAYSCLAHYLPSSFPVLRGINDCDLTQLGIPAAEEYFRMYCLQMGLPPTENWNFYMAFSFFRVAAILQGVYKRSLTGQASSTYAEQTGKLTEFVSNLAWDFAVKEGFRVFKEMPFTNPLTRSYHTWARPQSQWCPTGSRSYSSVPEASPAHTSRGGLVISPESLSPPVRELYHRLKHFMEQRVYPAEPELQSHQASAARWSPSPLIEDLKEKAKAEGLWNLFLPLEADPEKKYGAGLTNVEYAHLCELMGTSLYAPEVCNCSAPDTGNMELLVRYGTEAQKARWLIPLLEGKARSCFAMTEPQVASSDATNIEASIREEDSFYVINGHKWWITGILDPRCQLCVFMGKTDPHAPRHRQQSVLLVPMDTPGIKIIRPLTVYGLEDAPGGHGEVRFEHVRVPKENMVLGPGRGFEIAQGRLGPGRIHHCMRLIGFSERALALMKARVKSRLAFGKPLVEQGTVLADIAQSRVEIEQARLLVLRAAHLMDLAGNKAAALDIAMIKMVAPSMASRVIDRAIQAFGAAGLSSDYPLAQFFTWARALRFADGPDEVHRATVAKLELKHRI
Protein: Prenylcysteine oxidase 1-like (EC 1.8.3.-) (Q8NBM8)
Organism: Homo sapiens (Human)
Function: Probable oxidoreductase.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MARAAPLLAALTALLAAAAAGGDAPPGKIAVVGAGIGGSAVAHFLQQHFGPRVQIDVYEKGTVGGRLATISVNKQHYESGAASFHSLSLHMQDFVKLLGLRHRREVVGRSAIFGGEHFMLEETDWYLLNLFRLWWHYGISFLRLQMWVEEVMEKFMRIYKYQAHGYAFSGVEELLYSLGESTFVNMTQHSVAESLLQVGVTQRFIDDVVSAVLRASYGQSAAMPAFAGAMSLAGAQGSLWSVEGGNKLVCSGLLKLTKANVIHATVTSVTLHSTEGKALYQVAYENEVGNSSDFYDIVVIATPLHLDNSSSNLTFAGFHPPIDDVQGSFQPTVVSLVHGYLNSSYFGFPDPKLFPFANILTTDFPSFFCTLDNICPVNISASFRRKQPQEAAVWRVQSPKPLFRTQLKTLFRSYYSVQTAEWQAHPLYGSRPTLPRFALHDQLFYLNALEWAASSVEVMAVAAKNVALLAYNRWYQDLDKIDQKDLMHKVKTEL
Protein: Golgin-45 (Basic leucine zipper nuclear factor 1) (Q8R2X8)
Organism: Mus musculus (Mouse)
Function: Required for normal Golgi structure and for protein transport from the endoplasmic reticulum (ER) through the Golgi apparatus to the cell surface.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9H2G9}.
Interaction partners:
- Golgi reassembly-stacking protein 2
- Golgi reassembly-stacking protein 1
- Ras-related protein Rab-2A
- Golgi resident protein GCP60
- Golgin subfamily A member 5
- General vesicular transport factor p115
Sequence:
MEKMTTLKSSENKGILTSTPIRGAGDGMETEEPPKSVEVTHGVQPINQHVLPSPRKKVSSDSPGVLQLGKILNERTVEVEAVRIFVPKAAITHDIPTKNTKVKSLGHHREELHNQAEVVTDPRKELSEVKKVLEKLKNSERRLLQDKEGLSNQLRVQTEINRELKKLLVASVGDDPQYHFERLAREKNQLILENEALGRNTAQLSEQLERMSIQCDVWRSKFLASRVMADELTNFRVVLQRQNRDAQSAIQDLLSEREQFRQEMTSTQKFLEELLVSLQWGREQTYSPNTQPHSTADLALTNHGLAQAIHAHLLGNVGISHQKKIPTTVEFCSTPAEKMAEKVLRILDPVACTESSPDNQFAESSPTTLLTTKKNIGRFHPYTRYENITFNCCNHCQGELIAL
Protein: Ankyrin 2 (A0A5F9ZGS5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MTTMLQKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLENDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDTLKVVTEEVTTTTTTITEKHKLNVPETMTEVLDVSDEEGDDTMTGDGGEYLRPEDLKELGDDSLPSSQFLDGMNYLRYSLEGGRSDSLRSFSSDRSHTLSHASYLRDSAVMDDSVVIPSHQVSTLAKEAERNSYRLSWGTENLDNVALSSSPIHSGFLVSFMVDARGGAMRGCRHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGPVIVEIPHFAALRGKERELVVLRSENGDSWKEHFCDYTEDELNEILNGMDEVLDSPEDLEKKRICRIITRDFPQYFAVVSRIKQDSNLIGPEGGVLSSTVVPQVQAVFPEGALTKRIRVGLQAQPMHSELVKKILGNKATFSPIVTLEPRRRKFHKPITMTIPVPKASSDVMLNGFGGDAPTLRLLCSITGGTTPAQWEDITGTTPLTFVNECVSFTTNVSARFWLIDCRQIQESVTFASQVYREIICVPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSFFAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLPIYTKESESDQEQEEEIDMTSEKNPQDEQERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIVHLMETNTEPLQERISHSYAEIEQTITLDHSEGFSVLQEELCTAQHKQKEEQAVSKESETCDHPPIVSEEDISVGYSTFQDGVPKTEGDSSATALFPQTHKEQVQQDFSGKMQDLPEESSLEYQQEYFVTTPGTETSETQKAMIVPSSPSKTPEEVSTPAEEEKLYLQTPTSSERGGSPIIQEPEEPSEHREESSPRKTSLVIVESADNQPETCERLDEDAAFEKGDDMPEIPPETVTEEEYIDEHGHTVVKKVTRKIIRRYVSSEGTEKEEIMVQGMPQEPVNIEEGDGYSKVIKRVVLKSDTEQSEVTLCEPSILSSTSQFQAEPVEGRRVSKVVKTTVVLGERMEKHLGDSSLATDLPSAKDDFEEDNNE
Protein: ESX-1 secretion system ATPase EccB1 (EC 3.6.-.-) (ESX conserved component B1) (Type VII secretion system protein EccB1) (T7SS protein EccB1) (P9WNR7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: An ATPase. Part of the ESX-1 specialized secretion system, which delivers several virulence factors to host cells during infection, including the key virulence factors EsxA (ESAT-6) and EsxB (CFP-10).
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:26396239}; Single-pass membrane protein {ECO:0000255}. Note=Resides at or near the cell wall, the protein is susceptible to extracellular proteases (PubMed:26396239). {ECO:0000269|PubMed:26396239}.
Interaction partners:
- ESX-1 secretion system protein EccCa1
- ESX-1 secretion system protein EccD1
- ESX-1 secretion system protein EccCb1
- ESX-1 secretion system protein EccE1
- ESX-1 secretion system protein EccA1
- ESX-1 secretion-associated protein EspG1
- 6 kDa early secretory antigenic target
- ESX-1 secretion-associated protein EspF
- ESX-1 secretion-associated protein EspK
- ESX-1 secretion-associated protein EspH
Sequence:
MGLRLTTKVQVSGWRFLLRRLEHAIVRRDTRMFDDPLQFYSRSIALGIVVAVLILAGAALLAYFKPQGKLGGTSLFTDRATNQLYVLLSGQLHPVYNLTSARLVLGNPANPATVKSSELSKLPMGQTVGIPGAPYATPVSAGSTSIWTLCDTVARADSTSPVVQTAVIAMPLEIDASIDPLQSHEAVLVSYQGETWIVTTKGRHAIDLTDRALTSSMGIPVTARPTPISEGMFNALPDMGPWQLPPIPAAGAPNSLGLPDDLVIGSVFQIHTDKGPQYYVVLPDGIAQVNATTAAALRATQAHGLVAPPAMVPSLVVRIAERVYPSPLPDEPLKIVSRPQDPALCWSWQRSAGDQSPQSTVLSGRHLPISPSAMNMGIKQIHGTATVYLDGGKFVALQSPDPRYTESMYYIDPQGVRYGVPNAETAKSLGLSSPQNAPWEIVRLLVDGPVLSKDAALLEHDTLPADPSPRKVPAGASGAP
Protein: Putative protein tag-76 (P34681)
Organism: Caenorhabditis elegans
Interaction partners:
- Endoribonuclease dcr-1
- DRBM domain-containing protein
- Major sperm protein
- PAZ domain-containing protein
- Coiled-coil domain-containing protein
- Argonaute
- Piwi-like protein ergo-1
- Small RNA 2'-O-methyltransferase
- RNA-directed RNA polymerase
Sequence:
MSRRNATSFVDNNTLTSSGISGSGSMSPPITSRPASGQASPLTSNGSLSPPQYADDQGSVSYNLDSPRDLSPLLLSELACLNMREVVARPGLGTIGRQIPVKSNFFAMDLKNPKMVVIQYHVEIHHPGCRKLDKDEMRIIFWKAVSDHPNIFHNKFALAYDGAHQLYTVARLEFPDDQGSVRLDCEASLPKDNRDRTRCAISIQNVGPVLLEMQRTRTNNLDERVLTPIQILDIICRQSLTCPLLKNSANFYTWKSSCYRIPTAAGQALDLEGGKEMWTGFFSSAHIASNYRPLLNIDVAHTAFYKTRITVLQFMCDVLNERTSKPNRNNPRGPGGPGGPGGYRGGRGGGRGGSYGNFGNRGPPGANVRDDFGGNGLTFTMDTLSRDTQLSSFETRIFGDAIRGMKIRAAHRPNAIRVYKVNSLQLPADKLMFQGIDEEGRQVVCSVADYFSEKYGPLKYPKLPCLHVGPPTRNIFLPMEHCLIDSPQKYNKKMSEKQTSAIIKAAAVDATQREDRIKQLAAQASFGTDPFLKEFGVAVSSQMIQTTARVIQPPPIMFGGNNRSVNPVVFPKDGSWTMDNQTLYMPATCRSYSMIALVDPRDQTSLQTFCQSLTMKATAMGMNFPRWPDLVKYGRSKEDVCTLFTEIADEYRVTNTVCDCIIVVLQSKNSDIYMTVKEQSDIVHGIMSQCVLMKNVSRPTPATCANIVLKLNMKMGGINSRIVADKITNKYLVDQPTMVVGIDVTHPTQAEMRMNMPSVAAIVANVDLLPQSYGANVKVQKKCRESVVYLLDAIRERIITFYRHTKQKPARIIVYRDGVSEGQFSEVLREEIQSIRTACLAIAEDFRPPITYIVVQKRHHARIFCKYQNDMVGKAKNVPPGTTVDTGIVSPEGFDFYLCSHYGVQGTSRPARYHVLLDECKFTADEIQSITYGMCHTYGRCTRSVSIPTPVYYADLVATRARCHVKRKLGLADNNDCDTNSRSSTLASLLNVRTGSGKGKKSYAPSVDDESYSLSDATSDQILQDCVSVATDFKSRMYFI
Protein: F21B7.34 (Protein kinase superfamily protein) (Q9LR53)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Pentatricopeptide repeat-containing protein At4g35850
- Putative lipid-binding protein AIR1
- DExH-box ATP-dependent RNA helicase DExH9
Sequence:
MGCVNSRHRPFRRKSTTLKESSEEKRSSRIDSSRRIDDWIQPEDGFDRLSNSGDAKVRLIESEMFSTSRCHDHQIGKILENPATVAHMDRVVHDQELRRASSAVVDSDLDIDPKVVKAKLDRWNSKDSKVRLIESEKLSSSMFSEHHQIEKGVEKPEVEASVRVVHRELKRGSSIVSPKDAERKQVAAGWPSWLVSVAGESLVDWAPRRANTFEKLEKIGQGTYSSVYRARDLLHNKIVALKKVRFDLNDMESVKFMAREIIVMRRLDHPNVLKLEGLITAPVSSSLYLVFEYMDHDLLGLSSLPGVKFTEPQVKCYMRQLLSGLEHCHSRGVLHRDIKGSNLLIDSKGVLKIADFGLATFFDPAKSVSLTSHVVTLWYRPPELLLGASHYGVGVDLWSTGCILGELYAGKPILPGKTEVEQLHKIFKLCGSPTENYWRKQKLPSSAGFKTAIPYRRKVSEMFKDFPASVLSLLETLLSIDPDHRSSADRALESEYFKTKPFACDPSNLPKYPPSKEIDAKMRDEAKRQQPMRAEKQERQDSMTRISHERKFVPPVKANNSLSMTMEKQYKDLRSRNDSFKSFKEERTPHGPVPDYQNMQHNRNNQTGVRISHSGPLMSNRNMAKSTMHVKENALPRYPPARVNPKMLSGSVSSKTLLERQDQPVTNQRRRDRRAYNRADTMDSRHMTAPIDPSWYNPSDSKIYMSGPLLAQPSRVDQMLEEHDRQLQEFNRQALKTPQG
Protein: Glutathione S-transferase A2 (EC 2.5.1.18) (GST class-alpha member 2) (Glutathione S-transferase GT41A) (P10648)
Organism: Mus musculus (Mouse)
Function: Catalyzes the conjugation of glutathione to a large variety of electrophilic compounds.
Interaction partners:
- Glutathione S-transferase omega-1
- Glutathione S-transferase theta-2
- Hematopoietic prostaglandin D synthase
- Cytochrome P450 2B10
- Glutathione S-transferase theta-3
- Glutathione S-transferase omega-2
- Glutathione peroxidase 2
- Glutathione S-transferase theta-1
- Epoxide hydrolase 1
- Cytochrome P450 1A1
Sequence:
MAGKPVLHYFNARGRMECIRWLLAAAGVEFEEKFIQSPEDLEKLKKDGNLMFDQVPMVEIDGMKLVQTRAILNYIATKYDLYGKDMKERALIDMYTEGILDLTEMIGQLVLCPPDQREAKTALAKDRTKNRYLPAFEKVLKSHGQDYLVGNRLTRVDVHLLELLLYVEELDASLLTPFPLLKAFKSRISSLPNVKKFLHPGSQRKPPLDAKQIEEARKVFKF
Protein: cDNA FLJ52081, highly similar to Regulatory-associated protein of mTOR (B7Z3S8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MESEMLQSPLLGLGEEDEADLTDWNLPLAFMKKRHCEKIEGSKSLAQSWRMKDRMKTVSVALVLCLNVGVDPPDVVKTTPCARLECWIDPLSMGPQKALETIGANLQKQYENWQPRARYKQSLDPTVDEVKKLCTSLRRNAKEERVLFHYNGHGVPRPTVNGEVWVFNKNYTQYIPLSIYDLQTWMGSPSIFVYDCSNAGLIVKSFKQFALQREQELEVAAINPNHPLAQMPLPPSMKNCIQLAACEATELLPMIPDLPADLFTSCLTTPIKIALRWFCMQKCVSLVPGVTLDLIEKIPGRLNDRRTPLGELNWIFTAITDTIAWNVLPRDLFQKLFRQDLLVASLFRNFLLAERIMRSYNCTPVSSPRLPPTYMHAMWQAWDLAVDICLSQLPTIIEEGTAFRHSPFFAEQLTAFQVWLTMGVENRNPPEQLPIVLQVLLSQVHRLRALDLLGRFLDLGPWAVSLALSVGIFPYVLKLLQSSARELRPLLVFIWAKILAVDSSCQADLVKDNGHKYFLSVLADPYMPAEHRTMTAFILAVIVNSYHTGQEACLQGNLIAICLEQLNDPHPLLRQWVAICLGRIWQNFDSARWCGVRDSAHEKLYSLLSDPIPEVRCAAVFALGTFVGNSAERTDHSTTIDHNVAMMLAQLVSDGSPMVRKELVVALSHLVVQYESNFCTVALQFIEEEKNYALPSPATTEGGSLTPVRDSPCTPRLRSVSSYGNIRAVATARSLNKSLQNLSLTEESGGAVAFSPGNLSTSSSASSTLGSPENEEHILSFETIDKMRRASSYSSLNSLIGVSFNSVYTQIWRVLLHLAADPYPEVSDVAMKVLNSIAYKRRSLGVSPRLVSNSSVRVILLPWPPEVLGLQAWATTPRLFFPF
Protein: Nucleoporin p54 (54 kDa nucleoporin) (Q7Z3B4)
Organism: Homo sapiens (Human)
Function: Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P70582}. Nucleus membrane {ECO:0000250|UniProtKB:P70582}; Peripheral membrane protein {ECO:0000250|UniProtKB:P70582}; Cytoplasmic side {ECO:0000250|UniProtKB:P70582}. Nucleus membrane {ECO:0000250|UniProtKB:P70582}; Peripheral membrane protein {ECO:0000250|UniProtKB:P70582}; Nucleoplasmic side {ECO:0000250|UniProtKB:P70582}. Note=Biased towards cytoplasmic side. Central region of the nuclear pore complex, within the transporter. {ECO:0000250|UniProtKB:P70582}.
Interaction partners:
- Nuclear pore complex protein Nup98-Nup96
- E3 SUMO-protein ligase RanBP2
- Nucleoporin p58/p45
- Nuclear pore complex protein Nup93
- Nuclear pore complex protein Nup155
- Nuclear pore complex protein Nup205
- Nuclear pore glycoprotein p62
- Nuclear pore complex protein Nup107
- Nuclear pore complex protein Nup133
- Nuclear pore complex protein Nup85
Sequence:
MAFNFGAPSGTSGTAAATAAPAGGFGGFGTTSTTAGSAFSFSAPTNTGTTGLFGGTQNKGFGFGTGFGTTTGTSTGLGTGLGTGLGFGGFNTQQQQQTTLGGLFSQPTQAPTQSNQLINTASALSAPTLLGDERDAILAKWNQLQAFWGTGKGYFNNNIPPVEFTQENPFCRFKAVGYSCMPSNKDEDGLVVLVFNKKETEIRSQQQQLVESLHKVLGGNQTLTVNVEGTKTLPDDQTEVVIYVVERSPNGTSRRVPATTLYAHFEQANIKTQLQQLGVTLSMTRTELSPAQIKQLLQNPPAGVDPIIWEQAKVDNPDSEKLIPVPMVGFKELLRRLKVQDQMTKQHQTRLDIISEDISELQKNQTTSVAKIAQYKRKLMDLSHRTLQVLIKQEIQRKSGYAIQADEEQLRVQLDTIQGELNAPTQFKGRLNELMSQIRMQNHFGAVRSEERYYIDADLLREIKQHLKQQQEGLSHLISIIKDDLEDIKLVEHGLNETIHIRGGVFS
Protein: RNA polymerase II holoenzyme cyclin-like subunit (Q5A4H9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Component of the SRB8-11 complex. The SRB8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The SRB8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by Mediator. It may inhibit the association of the Mediator complex with RNA polymerase II to form the holoenzyme complex. The SRB8-11 complex phosphorylates the C-terminal domain (CTD) of the largest subunit of RNA polymerase II (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Serine/threonine-protein kinase SSN3
- Mediator of RNA polymerase II transcription subunit 13
- Mediator of RNA polymerase II transcription subunit 12
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 16
- Mediator of RNA polymerase II transcription subunit 21
- Mediator of RNA polymerase II transcription subunit 31
Sequence:
MSADYWNSSQRNQWQLTRFSLLEARRRVLLLERKMIQNGLIKDYPNIIYDYNMRIYLHNLLIKLGRRLNIRQIALATAEIYLTRFLTRVSLKEINVYLLITTCIYVACKIEECPQHIRLILSEARNIWPEYIPHDVTKLAEFEFYLIEEMDSYLLLHHPYKSLMQINEFLSNNYNVFGFKLTVEELQNAWSLINDSYITDLHLLLPPHTIAVAAIYITVVLKKNLSRVRQGNNNDNNININTMHISTGSSTNPININNNNNTNTSNNNGTTSTTTTTTAQETQVLGQDDNTEMNIDDLMNLTKSSNNSQDKSDDKMDIDNPLQSQVNLSQIQNQTQHQHQESTHNNTSSTNTGRNGINGQISQSNQELNNFDLDILDEDTIKINKFMNFLEHSHINLDEVVEAVQDMMNMYVLWNRYNEQGVKKALQVMLLNRI
Protein: Gap junction alpha-5 protein (Connexin-40) (Cx40) (P33725)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
Subcellular location: Cell membrane; Multi-pass membrane protein. Cell junction, gap junction.
Interaction partners:
- Gap junction gamma-1 protein
- Gap junction alpha-1 protein
- Sodium channel protein
- Hyperpolarization activated cyclic nucleotide gated potassium channel 4.
- Homeobox protein Nkx-2.5
Sequence:
MGDWSFLGEFLEEVHKHSTVIGKVWLTVLFIFRMLVLGTAAESSWGDEQADFQCDTMQPGCGNVCYDQAFPISHIRYWVLQIIFVSTPSLVYMGHAMHTVRMQEKRKLREAERAKEARGAGSYEYPVAEKAELSCWEEVNGRIVLQGTLLNTYVCSILIRTTMEVAFIVGQYLLYGIFLDTLHVCRRSPCPHPVNCYVSRPTEKNVFIVFMLAVAALSLFLSLAELYHLGWKKLRQRFVKSGQGMAECQLPGPSAGIVQNCTPPPDFNQCLENGPGGKFFNPFSNKMASQQNTDNLATEQVQGQEPIPGEGFIHIRYAQKPEVPNGASPGHRLPHGYQSDKRRLSKASSKARSDDLSV
Protein: protein-serine/threonine phosphatase (EC 3.1.3.16) (A0A8I6ATT8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MALVTVQRSPTPSTTSSPCASEADSGEEECRSQPRSISESFLTVKGAALFLPRGNGSSTPRISHRRNKHAGDLQQHLQAMFILLRPEDNIRLAVRLESTYQNRTRYMVVVSTNGRQDTEESIVLGMDFSSNDSSTCTMGLVLPLWSDTLIHLDGDGGFSVSTDNRVHIFKPVSVQAMWSALQSLHKACEVARMHNYYPGSLFLTWVSYYESHINSDQSSVNEWNAMQDVQSHRPDSPALFTDIPTERERTERLIKTKLREIMMQKDLENITSKEIRTELEMQMVCNLREFKEFIDNEMIVILGQMDSPTQIFEHVFLGSEWNASNLEDLQNRGVRYILNVTREIDNFFPGVFEYHNIRVYDEEATDLLAYWNDTYKFISKAKKHGSKCLVHCKMGVSRSASTVIAYAMKEYGWNLDRAYEYVKERRTVTKPNPSFMRQLEEYQGILLASKQRHNKLWRSHSDSDLSDHHEPICKPGLELNKKEMTTSADQITEVKTVESLAAMPPVFMEHVVPQDVNQKGLRTKERVICLEFSSQEFHAGQIEDELNLNDINGCSSGCCLSESKFPLDNCHASKALLQPGQAPDIANKFPDLAVEDLETDALKADVRVHLLPMEELTSRLKDLPMSPDLESPSPQAGCQAAISDFSTDRIDFFSALEKFVELSQETRSRSFSHSRIEELGGGRSEGCRLSVMEMAPSEMVTDDQRSSSLSDTPHASEESSVDEDQPKAVSELVSPDIIMQSHSENAISVKEIVTEIESISQGVGQVQLKGDILSNPCHTPKKNIIHELPLERVQGPENKPGHLEQDESFCSVQLELARDSGKCAPEEGCLATLSSTGDLEEEEPVEGEHDWGPGTHPGAKWCPGSVRRATLEFEERLRQEQENHGTASPGPTLSNRKNSKNDSSVADLMPKWKSDETASEHSLSPKEAEPGKGKGKCSGSEAGPLSHCEHNPAAAAPQLLEHHPSPAPQDCLGSESRSEKQEEDLRKQRTVVSNQECETQAALLPLPKKIEIIEYTPTVTSLDHTEPGGETTPSKESEKQELRKVKMERSITMFCTLDENLNRTLDPSQVSLRPQVLPLPHSSSEYDRLTDPTPMLSSPQDKGDSPSTPFKTPARLVGCSTQGASVSLDCSHRHSVLHLEGCTEQSSTTDSRLSSEHMNWEDSQGDFLSSSTGMAHTSSPLTNEDLSLINKLGDSVGVLPKKLDPSPEACRIPHSSSSENIRDLSHGPGVVKEHAKEIEPRVIFQAAFSKTSQMRRSASLAKLGYLDLCKDYLPDRELGSSESPHLKLLQPFLRTDSGMHALMVHEPSESPGAHPNPQPTKYFVEQLKTTECVVQSKPVERPHVQYAKEFGFSQQCLLPKARPELTSSEGGLPLLQTQGLQYPGPSPGLAVAPRQQHGRTHPLRRLKRANDKKRTTNPFYNTM
Protein: Adenylate cyclase-like protein (Q9Z7J3)
Organism: Chlamydia pneumoniae (Chlamydophila pneumoniae)
Interaction partners:
- S/T Protein Kinase
- Flagellar motor switch Domain/YscQ family
- Protein CPn_0713/CP_0033/CPj0713/CpB0740
- Low Calcium Response Protein H
- oxoglutarate dehydrogenase
- Outer membrane secretion protein Q
- Serine/threonine-protein kinase pkn1
- Tetratricopeptide domain protein
- Secretion protein
- Serine/threonine-protein kinase PknD
Sequence:
MAVRLIVDEGPLSGVIFVLEDGISWSIGRDSSANDIPIEDPKLGASQAIINKTDGSYYITNLDDTIPIVVNGVAIQETTQLKNEDTILLGSNQYSFLSDEFDPQDLVYDFDIPEENFSNDSGDLSDSNEQGKDLEPRQTSETNHSPKPKEKLTKDQGSSDPITSGDQELADAFLASAKAEKNQPRAKVAKKGLKESSNESLNPKEQNAKDSPKGEERTNKPQNAIMEDNGASPRQDPQPKSAEPSLKNTARDETPLKENKPVEEKANKKATPDSPEKKDQPEEGSKKEGSKIEATPLDSQKESEDKEAEEAFVQEEEENLTEDNKEDSDSAADANDDTASDHTAEDNKETPKKVENEKSAVLSPFHVQDLFRFDQTIFPAEIDDIAKKNISVDLTQPSRFLLKVLAGANIGAEFHLDSGKTYILGTDPTTCDIVFNDLSVSHQHAKITVGNDGGILIEDLDSKNGVIVEGRKIDKTSTLSSNQVVALGTTLFLLIDHHAPADTIVASLSPDDYSLFGRQQDAEALERQEAQEEEEKQKRATLPAGSFILTLFVGGLAILFGIGTASLFHTKEVVPLENIDYQEDLAQVINQFPTVRYTFNKTNSQLFLIGHVKNSTDKSELLYKVDALSFVKSVDDNVIDDEAVWQEMNILLSKRPEFKGISMHSPEPGKFIITGYVKTEEQAACLVDYLNIHFNYLSLLENKVVVETQMLKAIAGHLLQGGFANIHVAFVNGEVILTGYVNNDDAEKFRAVVQELSGIPGVRLVKNFAVLLPAEEGIIDLNLRYPNRYRVTGYSRYGEISINVVVNGRILTRGDVIDGMTVTSIQPNAIFLEKEGLKYKIDYNK
Protein: N6-Methyl-AMP deaminase (EC 3.5.4.-) (Adenosine deaminase-like protein) (N6-mAMP deaminase) (HsMAPDA) (N6-methyl-AMP aminohydrolase) (Q6DHV7)
Organism: Homo sapiens (Human)
Function: Catalyzes the hydrolysis of the free cytosolic methylated adenosine nucleotide N(6)-methyl-AMP (N6-mAMP) to produce inositol monophosphate (IMP) and methylamine. Is required for the catabolism of cytosolic N6-mAMP, which is derived from the degradation of mRNA containing N6-methylated adenine (m6A). Catalyzes the removal of different alkyl groups not only from N6-substituted purine or 2-aminopurine nucleoside monophosphates but also from O6-substituted compounds in vitro.
Interaction partners:
- Bifunctional epoxide hydrolase 2
- Adenine phosphoribosyltransferase
Sequence:
MIEAEEQQPCKTDFYSELPKVELHAHLNGSISSHTMKKLIAQKPDLKIHDQMTVIDKGKKRTLEECFQMFQTIHQLTSSPEDILMVTKDVIKEFADDGVKYLELRSTPRRENATGMTKKTYVESILEGIKQSKQENLDIDVRYLIAVDRRGGPLVAKETVKLAEEFFLSTEGTVLGLDLSGDPTVGQAKDFLEPLLEAKKAGLKLALHLSEIPNQKKETQILLDLLPDRIGHGTFLNSGEGGSLDLVDFVRQHRIPLELCLTSNVKSQTVPSYDQHHFGFWYSIAHPSVICTDDKGVFATHLSQEYQLAAETFNLTQSQVWDLSYESINYIFASDSTRSELRKKWNHLKPRVLHI