wanglab/gogpt-training-data huggingface dataset:
Protein: Aconitate hydratase B (ACN) (Aconitase) (EC 4.2.1.3) ((2R,3S)-2-methylisocitrate dehydratase) ((2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase) (2-methyl-cis-aconitate hydratase) (EC 4.2.1.99) (Iron-responsive protein-like) (IRP-like) (RNA-binding protein) (P36683)
Organism: Escherichia coli (strain K12)
Function: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. Also catalyzes the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The apo form of AcnB functions as a RNA-binding regulatory protein. During oxidative stress inactive AcnB apo-enzyme without iron sulfur clusters binds the acnB mRNA 3' UTRs (untranslated regions), stabilizes acnB mRNA and increases AcnB synthesis, thus mediating a post-transcriptional positive autoregulatory switch. AcnB also decreases the stability of the sodA transcript.
Interaction partners:
- Citrate synthase
- Aconitate hydratase A
- Isocitrate dehydrogenase
- 2-methylcitrate dehydratase
- Succinate--CoA ligase subunit beta
- Isocitrate lyase
- 2-oxoglutarate dehydrogenase E1 component
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
- Malate dehydrogenase
- Fumarate hydratase class I, aerobic
Sequence:
MLEEYRKHVAERAAEGIAPKPLDANQMAALVELLKNPPAGEEEFLLDLLTNRVPPGVDEAAYVKAGFLAAIAKGEAKSPLLTPEKAIELLGTMQGGYNIHPLIDALDDAKLAPIAAKALSHTLLMFDNFYDVEEKAKAGNEYAKQVMQSWADAEWFLNRPALAEKLTVTVFKVTGETNTDDLSPAPDAWSRPDIPLHALAMLKNAREGIEPDQPGVVGPIKQIEALQQKGFPLAYVGDVVGTGSSRKSATNSVLWFMGDDIPHVPNKRGGGLCLGGKIAPIFFNTMEDAGALPIEVDVSNLNMGDVIDVYPYKGEVRNHETGELLATFELKTDVLIDEVRAGGRIPLIIGRGLTTKAREALGLPHSDVFRQAKDVAESDRGFSLAQKMVGRACGVKGIRPGAYCEPKMTSVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVNTHHTLPDFIMNRGGVSLRPGDGVIHSWLNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLVHAIPLYAIKQGLLTVEKKGKKNIFSGRILEIEGLPDLKVEQAFELTDASAERSAAGCTIKLNKEPIIEYLNSNIVLLKWMIAEGYGDRRTLERRIQGMEKWLANPELLEADADAEYAAVIDIDLADIKEPILCAPNDPDDARPLSAVQGEKIDEVFIGSCMTNIGHFRAAGKLLDAHKGQLPTRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIEIPGCSLCMGNQARVADGATVVSTSTRNFPNRLGTGANVFLASAELAAVAALIGKLPTPEEYQTYVAQVDKTAVDTYRYLNFNQLSQYTEKADGVIFQTAV
Protein: NADH-quinone oxidoreductase subunit A (EC 7.1.1.-) (NADH dehydrogenase I subunit A) (NDH-1 subunit A) (NUO1) (Q9K1C3)
Organism: Neisseria meningitidis serogroup B (strain ATCC BAA-335 / MC58)
Subcellular location: Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01394}; Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01394}. Cell membrane {ECO:0000256|RuleBase:RU003639}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU003639}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- NADH-quinone oxidoreductase subunit B
- NADH-quinone oxidoreductase subunit C
- NADH-quinone oxidoreductase subunit H
- NADH-quinone oxidoreductase subunit I
- NADH-quinone oxidoreductase
- NADH-quinone oxidoreductase subunit D
- NADH-quinone oxidoreductase subunit L
- NADH dehydrogenase I, M subunit
- NADH-quinone oxidoreductase subunit K
- NADH-quinone oxidoreductase subunit F
Sequence:
MLSAYFPVFVFILIGLAAGVLFILLGTILGPKRHYAEKDAPYECGFEAFENARMKFDVRYYLVAILFILFDLEVAFMLPWAVVFKDLGAYGFWSMLVFIVVLTVGFVYEWKKGALEWE
Protein: Protein WWC3 (Q9ULE0)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:24682284}.
Interaction partners:
- Serine/threonine-protein kinase LATS1
- Tyrosine-protein phosphatase non-receptor type 14
Sequence:
MPWLSGGRRRRRGQPREAPREPPPSAQPQREPPPAPPAAVPTPPAPSAPPPRARESAELPLPAGWEEARDYDGRVFYIDHNTRQTSWIDPRDRITKPLTFADCVGDELPLGWETVYDKQIGVYYMDHINKLTQIEDPREQWRREQERMLKEYLIVAQEALNAKKEIYQIKQQRFELAQEEYQQLHKMCEDDSRSYASSFSGYSTNTKYDPHQIKAEIASRRDRLSRLKRELTQMKQELQYKEKGVETLQEIDRKMSSTHTSYKLDEAQAIMSELRTIKKAICTGEKERRDLMHSLAKLTDSFKNSCSVTDSLVDFPHHVGVPGDAGVPQQFCDAGSQTDIIGEFVFDDKTRLVDRVRLNWQYEEARKRVANIQQQLARLDNESWPSTAEADRDRLQLIKEKEALLQELQLIIAQRRSAGDVARLEEERERLEEELRRARATSAQGATERILLQEKRNCLLMQLEEATRLTSYLQSQLKSLCASTLTVSSGSSRGSLASSRGSLASSRGSLSSVSFTDIYGLPQYEKPDAEGSQLLRFDLIPFDSLGRDAPFSEPPGPSGFHKQRRSLDTPQSLASLSSRSSLSSLSPPSSPLDTPFLPASRDSPLAQLADSCEGPGLGALDRLRAHASAMGDEDLPGMAALQPHGVPGDGEGPHERGPPPASAPVGGTVTLREDSAKRLERRARRISACLSDYSLASDSGVFEPLTKRNEDAEEPAYGDTASNGDPQIHVGLLRDSGSECLLVHVLQLKNPAGLAVKEDCKVHIRVYLPPLDSGTPNTYCSKALEFQVPLVFNEVFRIPVHSSALTLKSLQLYVCSVTPQLQEELLGIAQINLADYDSLSEMQLRWHSVQVFTSSEPSRTREAGCAGESSARDPAHTISISGKTDAVTVLLARTTAQLQAVERELAEERAKLEYTEEEVLEMERKEEQAEAISERSWQADSVDSGCSNCTQTSPPYPEPCCMGIDSILGHPFAAQAGPYSPEKFQPSPLKVDKETNTEDLFLEEAASLVKERPSRRARGSPFVRSGTIVRSQTFSPGARSQYVCRLYRSDSDSSTLPRKSPFVRNTLERRTLRYKQSCRSSLAELMARTSLDLELDLQASRTRQRQLNEELCALRELRQRLEDAQLRGQTDLPPWVLRDERLRGLLREAERQTRQTKLDYRHEQAAEKMLKKASKEIYQLRGQSHKEPIQVQTFREKIAFFTRPRINIPPLPADDV
Protein: Auxin-responsive protein SAUR78 (Protein SMALL AUXIN UP RNA 78) (Q9C9E1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the regulation of ethylene receptor signaling. Promotes cell expansion and plant growth.
Interaction partners:
- AT4g00880 protein
- AT4G30480 protein
- Auxin-responsive protein SAUR50
Sequence:
MAKVGKLTKLKSAMKKWPSFAKNHHHSTSSAAVSDELSEDNNLHVVYVGQTRRPYMLRPDIISHPLFQELVDRSSSRSIEQDREIVVACEVVLFEHLLWMLKSGQEGGSVEELAEFYTY
Protein: Developmental pluripotency-associated protein 2 (Pluripotent embryonic stem cell-related gene 1 protein) (Q7Z7J5)
Organism: Homo sapiens (Human)
Function: Binds to target gene promoters, including NKX2-5 and SYCE1, but not GATA4, and may be involved in the maintenance of the active epigenetic status of these genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:15583978}.
Interaction partners:
- Developmental pluripotency-associated protein 4
- Developmental pluripotency-associated 5 protein
Sequence:
MSDANLDSSKKNFLEGEVDDEESVILTLVPVKDDANMEQMEPSVSSTSDVKLEKPKKYNPGHLLQTNEQFTAPQKARCKIPALPLPTILPPINKVCRDTLRDWCQQLGLSTNGKKIEVYLRLHRHAYPEQRQDMPEMSQETRLQRCSRKRKAVTKRARLQRSYEMNERAEETNTVEVITSAPGAMLASWARIAARAVQPKALNSCSIPVSVEAFLMQASGVRWCVVHGRLLSADTKGWVRLQFHAGQAWVPTTHRRMISLFLLPACIFPSPGIEDNMLCPDCAKRNKKMMKRLMTVEK
Protein: Tubulin-specific chaperone E (Tubulin-folding cofactor E) (Q8CIV8)
Organism: Mus musculus (Mouse)
Function: Tubulin-folding protein; involved in the second step of the tubulin folding pathway and in the regulation of tubulin heterodimer dissociation. Required for correct organization of microtubule cytoskeleton and mitotic splindle, and maintenance of the neuronal microtubule network (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Tubulin-specific chaperone D
- Tubulin-specific chaperone A
- Tubulin-specific chaperone C
- Tubulin-folding cofactor B
- ADP-ribosylation factor-like protein 2
Sequence:
MSDILPLDVIGRRVEVNGEYATVRFCGAVPPVAGLWLGVEWDNPERGKHDGSHEGTMYFKCRHPTGGSFVRPSKVNFGDDFLTALKKRYVLEDGPDDDENSCSLKVGSKQVQTIGFEHITKKQSQLRALQDISLWNCAVSHAGEQGRIAEACPNIRVVNLSKNLLSTWDEVVLIAEQLKDLEALDLSENKLQFPSDSPTLTRTFSTLKTLVLNKTGITWTEVLHCAPSWPVLEELYLKSNNISISERPVNVLQKMRLLDLSSNPSIDESQLSLIADLPRLEHLVLSDIGLSSIHFPDAEIGCKTSMFPALKYLIVNDNQISEWSFINELDKLQSLQALSCTRNPLSKADKAEEIIIAKIAQLRTLNRCQILPEERRGAELDYRKAFGNEWRKAGGHPDPDKNRPNAAFLSAHPRYQLLCCKYGAPEDEELKTQQPFMLKKQLLTLKIKCSNQPERQILEKQLPDSMTVQKVKGLLSRLLKVPVSELLLSYESSKMPGREIELENDLQPLQFYSVENGDCLLVRW
Protein: C2HC/C3H-type domain-containing protein (Q387B6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTMSDTSATYSLHNHYGRINNVCTISPQASPSPSALPQTVEEHFDAEALLKEQRHLLESSPAAEIRASPFLRFRLNAQQKFTMQHNQYLERCAQREASDRNPHPLTASATGLREQFTQHLGRQSISQGQNQSYQDGEGLCCSGCQNRFVDAIALNRHKSTCSEYAALVLQRRGSEKLHYTARCFSTRETAVTPSNTDIRPILSIRERAEDPQPIPDVLTARGGHFSYRNQLSTHGGYQGNEGENAAAVAVFSPKAGSGSLSRSLPTPTSLREDMHSEFEARDTKHNIRARTQSQELTPPTPTSTWHQPSTSLRVTSIDEVPASVAARQSVDATMPTTPLGYQLGERFDVDISVDKSSFGAGTFQGMVSYSHLGGGVDSLRESSEPPDEPLKPCPSCGRQFFAYSRWPRHVAVCDNKRQQINSRGGGSVSSISSFRFPSGNANRLPQTALEKSTELGGTTTTTTTTTTATKLTRTNTSEKRKSLGASYVEPSIERRPLSASNRGRDAMEGPNFVRTSTYSSETFAEEDGQVVDDRVPCPSCGRRFATHVAERHIPHCRERSEGNPPIRL
Protein: Tyrosine-protein kinase yes (EC 2.7.10.2) (p61-Yes) (A1A5H8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Non-receptor protein tyrosine kinase that is involved in the regulation of cell growth and survival, apoptosis, cell-cell adhesion, cytoskeleton remodeling, differentiation, G2/M progression and cytokinesis (By similarity). Required for convergent extension cell movements during gastrulation, acting with fyna via rhoa. May be required for epiboly to occur, possibly through its effects in calcium signaling. During embryonic development, phosphorylates ptk2.1/fak.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15572145}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Cell junction {ECO:0000250|UniProtKB:Q28923}.
Interaction partners:
- Tyrosine-protein kinase fyna
- Tyrosine-protein kinase fynb
- Catenin
- Tyrosine-protein kinase
Sequence:
MGCVKSKEDKGPTQKYRPDPTNPTPGSHMGLYGPDPTQMGQSPALKGPTNNYNSRSSGLTPFGGSSSVITPFGGASSSFSTVAVNNPFPGVVTGGVTFFVALYDYEARTSDDLSFSKGDRFQIINNTEGDWWEARSINTGQKGYIPSNYVAPADSIQAEEWYFGKMGRKDAERLLLLPGNQRGTFLVRESETTKGAYSLSIRDWDEMKGDNVKHYKIRKLDSGGYYITTRAQFDTLQKLVKHYTEHADGLCYRLTTVCPTVKPQTQGLAKDAWEIPRESLRLELKLGQGCFGEVWMGTWNGTTKVAIKTLKPGTMSPEAFLQEAQIMKKLRHDKLVPLYAVVSEEPIYIVTEYMGKGSLLDFLKEGEGKYLKLPQLVDMAAQIADGMAFIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMVNREVLEQVERGYRMPCPQGCPESLHEMMRLCWKKEPDERPTFEYIQSFLEDYFTATEPQYQPGDNL
Protein: Protein vav-1 (Q45FX5)
Organism: Caenorhabditis elegans
Function: Acts as guanine nucleotide exchange factor (GEF) for Rho GTPase. Has a critical roles in the generation of rhythmic behaviors: feeding, defecation and ovulation by dynamically regulating the concentration of intracellular calcium. Plays a role in male tail tip morphogenesis.
Interaction partners:
- Ras-like GTP-binding protein rhoA
- E3 ubiquitin-protein ligase CBL
- Ras-related protein ced-10
- Cell division control protein 42 homolog
- Sex muscle abnormal protein 5
- Receptor tyrosine-protein kinase let-23
- Mss4 protein
- Ras-related protein rac-2
- DH domain-containing protein
- Tyrosine protein-kinase src-1
Sequence:
MSRRSTTTSTNFGLSWSLVDVISSSTAVFKVPMNGGCDLWIGCARWLRDMKVLTTDKNGTMLEFASVLRDGILLCRLANTLVPNGIDQKKIMRTNQPSPFLCCNNINYFAMFCKTYFNLEDADLFTAEDLYYMNGFQKVLKTLSFLSHTKESLSRGVDPFPDTDNNQEGTSNGSEFEDDVEIYQSLHDNIENVDPNRTIYGPITSADPEEQQSEQLYDRIVTNRKPSMNENDLQNTPTLKRNRCIRELYDTEKNYVAQALVTIIKTFYEPLKGIIPTSDYNIIFGNIEEINVLHTALLADLEYPVKVALGLSDATPPRPISLNECVPQTIGEVFIKYRDQFLAYGKYCSNLPDSRKLSNELLKTNEFISRNINELTAQGNCKFGMNDLLCVPFQRLTKYPLLLKELQKKTDLASPDRKSLEEAVEVMEDVCNYINEESRDTNAIKVIDEIEQSITDLSMPLNVKLHDYGRVNLDGEVKMAESTLTQAGKPKQRYIFLFDKVIVVCKAANKVMAAKTTGASARTNTFTYKNAYVMSELTIDKNASLDVKSGGTITRRTQYVIIMTRDRNENNEITQLTFYFKNEATRNNWMTALLLSKSNVSPTDYLRDTNHKVAFHSFRVDVKNPATCDVCDKLMKGLQYQGYKCESCNMSMHKECLGLKKCEAVRKSTHETRSSQSFNCNRPRFHIHEGDIVVANSNSTPSDLSYLQFAKGDRIEVIKMQGHNRFTGCLINNRNRTGLVHLDHVSQSRTTSMIGLSPIDSPAGSIAPRVVRNESTVLPNKLLSDGSSRSLSGPHGSRSSRNSSSSTINGSMDSVPRQQDYVNTEISEFLWYMGEMERAKAESTLKGTPNGTFLVRYSKNRKQTAISLSYKNDVKHMIIEQNSDGKVYLDEDYIFNSTVELVQYYRSNNLIEIFAALDTCLKNPYSQCKVFKAVHDYDAPSPNNEGKFLSFKTGDIVVLLDTVGEDRGWWKGQVNNKSGFFPLSYVKPYDPATEGSSSPVTPTSSSS
Protein: Putative alpha,alpha-trehalose-phosphate synthase [UDP-forming] 106 kDa subunit (EC 2.4.1.15) (Trehalose-6-phosphate synthase) (UDP-glucose-glucosephosphate glucosyltransferase) (O14081)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Cytosolic neutral trehalase
- Probable UTP--glucose-1-phosphate uridylyltransferase
- Alpha,alpha-trehalose-phosphate synthase
- Trehalose-phosphatase
- Probable UTP--glucose-1-phosphate uridylyltransferase
- Trehalose-phosphatase
- Putative alpha,alpha-trehalose-phosphate synthase 100 kDa subunit
- Phosphoglucomutase
- Hexokinase-2
- Heat shock protein 78
Sequence:
MGRILIAHLFLPSSVGFSFDTVPHDEVGSKFMQKEESKDWIADTPLDESAIVSEEESDDDSLLSDLPEEIDSTNAQSNIATPSPGTVAAAISGIQPPPKTPSSDSPSLENSLSNLNDLFKSRGRHMAFSKNDGTNLSLPPSRHQSPPPSSVLASQRHHRRHDSELEEFARRASRSLSFSMNGTPQRRMTFDAEAWKNVIFKIKPSSFGNASFYNAISAATRSKQFDDHLFVGTCGIPTDSLPDSLKERISHDYITEHSSLVVYPTDTDFVGHYNHYCKNILWPTFHYQIPDNPKSKAYEDHSWANYVKVNKAFADTIVDNYEQDDMIWINDYHLLLVPEMVRERLPRAKIGFFLHIPFPSSEVFRCLATRQEILKGMLGANILGFQIPEFAYHFLQTCSRLVNIDIRKNGVVSFENRQIDVIALPISIDPGFIDRCLASPPVEHWAKVLQDRFRGKHIILSHDKLDPIRGLRSKLISFERFLQKYPEYRENTILLQVAPESLQDSEHLPHISDIVTRINSAYSNIASRHVPVILLRQKLGYAQFLALMMISDALIDNSLREGISLTSHQFIYVQRKRHRPLILSEFVGSASILNDNAIIVNPWDYSKTAEAFRTALTMSEEECQKRNKAMCNLILRHDAASWAVTFQSLIKESWKEQIDMQRIPAFTAQLIKEPYQNAQKRLILLYFEGTISTWGSQYHNVMTSLQRTINLLNMLTSDPKNTVYVFSALSCQELEQLFQRVPKLGIVAENGCFVRSPPKGDATMPVSKKEIAELWKNKVLGTDLTWMKTVSEIFEYYAERTTGAYVENKDATVILHLREAEDDEAAMWAAKECCESVNNFNVPCSATIQNDMVVCRSNKVSKRLAAEDIYSANGGDYDFIFAASNDPDDDTVFSWMKNFKQSKKEVVPFTFSVCVSEHGNSTNADAESSGVFGFLQALEKVYSA
Protein: DNA methyltransferase 1-associated protein 1 (Q7K3D8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in transcription repression and activation (By similarity). Required for larvae and pupal development, and for normal innate immune responses. Involved in modulating the activation of the immune deficiency pathway (Imd), acting either downstream of, or at the level of, the NF-kappa-B factor Rel. Possibly functions with akirin to regulate Rel, and its interaction with the Brahma complex protein Bap55 suggests that it may regulate the IMD pathway at the level of chromatin remodeling.
Subcellular location: Nucleus {ECO:0000269|PubMed:24947515}. Cytoplasm {ECO:0000269|PubMed:24947515}.
Interaction partners:
- MRG/MORF4L binding protein
- Enhancer of polycomb-like protein
- Transcription-associated protein 1
- Brahma associated protein 55kD
- YEATS domain-containing protein 4
- NuA4 complex subunit EAF3 homolog
- RuvB-like helicase 2
- Chromatin modification-related protein MEAF6
- RuvB-like helicase 1
- Inhibitor of growth protein
Sequence:
MSADVRDILDMERANTPEVTRDSFLATKKRNFERTKTASRRPEGMHREVFALLYTDKKDAPPLLPTDTALGIGAGYKETKARLGMKKVRKWEWAPFSNPARNDSAVFHHWKRVTDNSTDYPFAKFNKQLEVPSYTMTEYNAHLRNNINNWSKVQTDHLFDLARRFDLRFIVMADRWNRQQHGTKTVEELKERYYEVVALLAKAKNQTSEKKVFVYDVEHERRRKEQLEKLFKRTTQQVEEENMLINEMKKIEARKKERERKTQDLQKLISQADQQNEHASNTPSTRKYEKKLHKKKVHQQPRPSRVDSVVNAIEIGSSGIKFADLRGSGVSLRSQRMKLPANIGQRKVKALEQAIQEFKVDPAPPPTEDICTSFNELRSDMVLLCELRTALSTCVYEMESLKHQYEAACPGKTLNIPPSLVPIKTEALDNSTN
Protein: Peptidase S9 prolyl oligopeptidase catalytic domain-containing protein (Q19086)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MATEAVYGSWDSPITPDLFGKCNCKSICEMQVVGGNVYWIEQNSVTGKRELYSKPTNGDTRTRWADGQSVQTAIHEYGGGALHVLADGSVLFATIEGVFYQKSADSGVEQLAEGNNRMFRFSDFSATDTHVFCVNETHQADAKFPENRLISIDRATKNQNVIAHGADFYAYPRVSPDGKKLVWMQWSLPNMPWDETSIRMADLKGGESSNEVTLKDGTGKQINYSEPTWDGDELLTVNDSTNWWNVYKSAAEPNSVEKNLNPIQREISYPLWQLGFRNYVLNKKYLVMNADGILYVRSGDVTVEIPTPGYTVFGYLSLDQNGSDLFAIASGPKRASSVISIDLANKNFPLKVHRESRDSSEIDALEISEPEEFVFKSDGVDVSGYFYPPKNCSYSAPAGTLPPVLLLGHGGPTAPAQNNLDLKKQFFTSRGIAVFDVNYRGSTGFGTEFRRMLYKNCGVADRDDMLNGAKALVEQGKVDAEKVLITGSSSGGYLILSCLISPKNIIKAAVSVYGVADLLALDEDTHKLERCYNEMLIGKYPEQASIYEERSPIYHIDKIRTPIAFLHGREDTVVPMSQSITMYEKIRASGVTTALMLFDGEGHGFRNGQVIKESTEATFYFLMKAVGIEPSISSKIEIVNPKH
Protein: Protein BMRF2 (P03192)
Organism: Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Function: Facilitates virus attachment to oral epithelial cells by binding to host beta1 integrin family. Participates in rearrangement of cellular actin to increase intercellular contacts by binding BDLF2 and thereby promote virus cell-to-cell spreading.
Subcellular location: Virion membrane {ECO:0000269|PubMed:15534216}; Multi-pass membrane protein {ECO:0000255}. Host cell membrane {ECO:0000269|PubMed:18995876}; Multi-pass membrane protein {ECO:0000255}. Note=In EBV-infected polarized oral epithelial cells, is transported to the basolateral membranes and colocalizes with beta1 integrin. {ECO:0000269|PubMed:17945327}.
Interaction partners:
Sequence:
MFSCKQHLSLGACVFCLGLLASTPFIWCFVFANLLSLEIFSPWQTHVYRLGFPTACLMAVLWTLVPAKHAVRAVTPAIMLNIASALIFFSLRVYSTSTWVSAPCLFLANLPLLCLWPRLAIEIVYICPAIHQRFFELGLLLACTIFALSVVSRALEVSAVFMSPFFIFLALGSGSLAGARRNQIYTSGLERRRSIFCARGDHSVASLKETLHKCPWDLLAISALTVLVVCVMIVLHVHAEVFFGLSRYLPLFLCGAMASGGLYLGHSSIIACVMATLCTLTSVVVYFLHETLGPLGKTVLFISIFVYYFSGVAALSAAMRYKLKKFVNGPLVHLRVVYMCCFVFTFCEYLLVTFIKS
Protein: Bacterial microcompartment assembly protein PduM (Propanediol utilization protein PduM) (Q9XDN4)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Plays an essential role in assembly and/or stability of the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation. Overexpression impairs BMC formation.
Subcellular location: Bacterial microcompartment {ECO:0000269|PubMed:22343294}.
Interaction partners:
- Bacterial microcompartment shell vertex protein PduN
- Bacterial microcompartment shell protein PduU
- Bacterial microcompartment shell protein PduB
- Bacterial microcompartment shell protein PduJ
- Bacterial microcompartment shell protein PduK
- Phosphate propanoyltransferase
- Propanediol dehydratase small subunit
- Propanediol dehydratase large subunit
- 1-propanol dehydrogenase PduQ
- Corrinoid adenosyltransferase PduO
Sequence:
MNGETLQRIVEEIVSRLHRRAQSTATLSVTQLRDADCPALFCQHASLRILLIDLPLLGQLADAETGDAAARKIHDALAFGIRVQLSLHSQLLPVIPVKKLARLPLVFTDEHGLPLVLHAGSVLSYRDVALLSRGRVVVHRKCIVTAMARDAANARNIQLIKQE
Protein: Non-specific lethal 1, isoform L (A0A0B4K6Z4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAPALTAEPLSPKEKLTSTASPSARSSSESGGVGCAVGLVKKPATPTPATATTRITRSSAAAASVTASPHLQQQRSSLAINNKRKSGNAKASNEPMGLSTAPTPHSTTSPNPSTDTAAASTSAVEHNNNDSNSTSAGNSTSADNSSTPKDNSTAQLLADLTINFEETISAEICLRKTLPDVSLGKEPVPPASVLAVATSSTSAGSALSLSAVDEVTKIEIDNIEERLSQLDGNATGRPEEHVAPPSVPVPVQEAPNTPTRPQAPPSAHLESPQPARTQQQSIQQMTPQSTTSSNNFLKDGAAGAVLEDQDIEEVLKALKTFDGGHVNPDTICEFFDEVWEEAAPAAPLPPAPPENVVDVPGAKPSCSGILVSGSNISQPNVIIKQEQRPWQESHAELEQQQHVISRRIEFLLRRMRKLQARAMCRHASEEVVGIMEWSARSSHKAPVPARSSTLTEQEATVLSIVSGRPSSTFWEEQNKHPLPASQMSNVIRHIATAAKHQQICHSASGSSATLAPSSSWYNSCNSSALPMKRPRKNQLDASVATGATPTAPAPGAVTSRQAAGTTGSATGSNTPRADDIVPGYDTYVTNELTHVSGLLHTELREVQNAIDSDATESSSGGESADEMVTYNNNQQLSLPITRRAVWRYSRDRAAIALRWSWLCSQLTDLEMKIRQHSDLYMDLTQSKGEIQLESTAKTSPSLAQPANGIKEEPGSDYLCSRARPLVLSEFRKRKLFQTTNMHTISKKAARPSNIKCGCQWPQVPCTLCTGRTDPTAPRDLVETMMPQNRVALLDAGYHPVLSFASDVSQSVHLEAVARQPDWQYRVMRSQPKAIVKAMWKAERETIASGGVGGQGGSRRSGDAAKRRYIRRKERNNNSNKEAGSGAKAAAVAAGGAGGNGSSSVGGGDSGNGTGTATTSSSTTPTTTPLVANSKLFGQGQAATTTPNWSEQFQLAVARLSPTPTTTPPQSLLNLDLGTERR
Protein: H2-M beta chain (Q31100)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
GGFVAHVESTCVLNDAGTPQDFTYCVSFNKDLLACWDPDVGKIVPCEFGVLSRLAEIISNILNEQESLIHRLQNGLQDCATHTQPFWDVLTHRTRPPSVRVAQTTPFNTREPVMLACYVWSFYPADVTITWMKNGQLVPSHSNKEKTAQPNGDWTYQTVSYLALTPSYGDVYTCVVQHSGTSEPIRGDW
Protein: Cruzioseptin-8 (CZS-8) (A0A193H329)
Organism: Cruziohyla calcarifer (Splendid leaf frog) (Agalychnis calcarifer)
Function: Has antimicrobial activity.
Subcellular location: Secreted {ECO:0000269|PubMed:27321580}.
Interaction partners:
Sequence:
MAFLKKCLFLVLFLGLVSLSICEEEKREEENEEVQEDDDQSEEKRGFLDVIKHVGKAAGKAALNAVTEMVNQGEQ
Protein: L-amino-acid oxidase (ACL-LAO) (LAAO) (EC 1.4.3.2) (P0CC16)
Organism: Agkistrodon contortrix laticinctus (Broad-banded copperhead) (Agkistrodon mokasen laticinctus)
Function: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Is active on L-Ile followed by L-Phe, L-Met, L-Val, L-Arg, L-Leu. Exhibits diverse biological activities, such as hemorrhage (minimum hemorrhagic dose of 10 ug), and apoptosis. May also induce hemolysis, edema, antibacterial and antiparasitic activities. May also regulate platelet aggregation. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions.
Subcellular location: Secreted {ECO:0000269|PubMed:10441379}.
Interaction partners:
Sequence:
ADSRNPLEEEFRETNYEEF
Protein: Adenine DNA glycosylase (EC 3.2.2.31) (A0A5F9ZI14)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRKPRAAVGSGHRKQAASQEGRQKHAKNNSQAKPSACDGLARQPEEVVLQASVSSYHLFRDVAEVTAFRGSLLSWYDQEKRDLPWRRRAEDEMDLDRRAYAVWVSEVMLQQTQVATVINYYTGWMQKWPTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQLLPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQRVEQEQLLASGSLSGSPDVEECAPNTGQCHLCLPPSEPWDQTLGVVNFPRKASRKPPREESSATCVLEQPGALGAQILLVQRPNSGLLAGLWEFPSVTWEPSEQLQRKALLQELQRWAGPLPATHLRHLGEVVHTFSHIKLTYQVYGLALEGQTPVTTVPPGARWLTQEEFHTAAVSTAMKKVF
Protein: Uncharacterized transcriptional regulatory protein C777.02 (O74541)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein mS29
Sequence:
MNKLSCLYCRRRKIKCDKNRPCHNCFVAKRECIIAGDNRKKRHTKTYVEALESQLANMESTLAKIKVAPVEKIPSLLAGISFKDHLSASLPNKTSYEQADTNATSKSLVDLPVSLEVRGRNTVTFYGPTSIFGTSFTSSPRPPPSASIEDTYPIIHCLQLFFKWQYAQFLFIHRESFLFEYFHRSNDNMYCSEHLIYALCAIGCRSSEDSLLVNQADAFYKMAWDALESYGLENSHITSAQCLLCLGFYKIAMGNTSHGWLLCGMAFRMGQDLGFHLDPRDWHINNVPVVSEEQAALRSRIYWGCYVADVFVSFILGRPTTLSKSDTSVPTSDDLPDFSGIEDFMLERGGAHASSITISQLLNLIVSLSNITDAILLNVFAPYSTKYGIDLRLQNVGKYNLELMKWHFELPPNLSWKKTELRDFGQSPELCFLCLYFFLIRLCLNRPFLSKKGLYVNDMTPRNICIDSIEDVKVLIRAYRENLGLHHTPLIIVYACIVSCSTVFMLFDGATPSEIVALEQDIKFFLHVLTKISKNWDLASKSINLIQKKSTMYDTNARANDTDVDFSNDKQNTHDFQISHDENLIQLFNDESNFFNLNDLGDFQSIFGGPQF
Protein: Free fatty acid receptor 1 (G-protein coupled receptor 40) (Q76JU9)
Organism: Mus musculus (Mouse)
Function: G-protein coupled receptor for medium and long chain saturated and unsaturated fatty acids that plays an important role in glucose homeostasis. Fatty acid binding increases glucose-stimulated insulin secretion, and may also enhance the secretion of glucagon-like peptide 1 (GLP-1). May also play a role in bone homeostasis; receptor signaling activates pathways that inhibit osteoclast differentiation. Ligand binding leads to a conformation change that triggers signaling via G-proteins that activate phospholipase C, leading to an increase of the intracellular calcium concentration. Seems to act through a G(q) and G(i)-mediated pathway. Mediates the anti-inflammatory effects of omega-3 polyunsaturated fatty acids (PUFAs) via inhibition of NLRP3 inflammasome activation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16044321, ECO:0000269|PubMed:24130766}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Free fatty acid receptor 4
- Pro-glucagon
- Guanine nucleotide-binding protein subunit alpha-11
- Gastric inhibitory polypeptide
- Glucose-dependent insulinotropic receptor
- G-protein coupled receptor 84
- Probable G-protein coupled receptor 142
- Beta-arrestin-2
Sequence:
MDLPPQLSFALYVSAFALGFPLNLLAIRGAVSHAKLRLTPSLVYTLHLGCSDLLLAITLPLKAVEALASGAWPLPLPFCPVFALAHFAPLYAGGGFLAALSAGRYLGAAFPFGYQAIRRPRYSWGVCVAIWALVLCHLGLALGLETSGSWLDNSTSSLGINIPVNGSPVCLEAWDPDSARPARLSFSILLFFLPLVITAFCYVGCLRALVRSGLSHKRKLRAAWVAGGALLTLLLCLGPYNASNVASFINPDLGGSWRKLGLITGAWSVVLNPLVTGYLGTGPGRGTICVTRTQRGTIQK