wanglab/gogpt-training-data huggingface dataset:
Protein: V-type proton ATPase subunit e 2 (V-ATPase subunit e 2) (Vacuolar proton pump subunit e 2) (Q5EB76)
Organism: Rattus norvegicus (Rat)
Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000269|PubMed:32165585}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:32165585}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase 116 kDa subunit a 1
- V-type proton ATPase subunit S1
- V-type proton ATPase subunit C 1
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase subunit E 1
- V-type proton ATPase subunit F
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit D
- V-type proton ATPase subunit B, brain isoform
Sequence:
MTAHSFALPVIIFTTFWGLIGIAGPWFVPKGPNRGVIITMLVATAVCCYLFWLIAILAQLNPLFGPQLKNETIWYVRFLWE
Protein: Centrosomal protein 135kDa, isoform B (M9MSL4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000256|ARBA:ARBA00004114}.
Interaction partners:
- Spindle assembly abnormal protein 6 homolog
- Spindle assembly abnormal 4
- Serine/threonine-protein kinase PLK4
- Anastral spindle 2, isoform A
- Anastral spindle 1, isoform A
- Asterless
- Centriolar coiled coil protein 110kDa, isoform B
- POC1 centriolar protein homolog
- Centrosomin
- BcDNA.LD24702
Sequence:
MNINDGDFKDLRCKLDIMGFTQTLPVLAIPLVQAVFGDLIKTTECLRDTKKKVAELLEEKTCWELGVEPYKCDNSRLLAECNELHLQFLRDREDYELRLCESERKIRNLELDKQHLQSHNDGLQRQLDALLTKQMVSSVTNKKATAGIGRQTKKPFITTVRSGIAMPTTLGTSSSALKCTKCNAGVFQKTTTTTKDGVTVTQTSGQEELDKMQNDLTAAGEQLEFFKRKVEARNREIRRLNDMLAGGRPLAALAKDCCYKDVGALSQDIDLLQREKSDLMMQVREFQDKMHDAMQRALSSEEDKIKLQTQLEELKEAALQVEQQANAEIDAKESELRQLQLELKKKGKDHRLTGGFASNQSDKHNLNERLNLLTRREEELQATNEKHKKKIQKMQAKILELQKELKDQNKHSNVTLDEEKIRLSSERDFFQKEYLRLMSKTGSESEIAFLHAQIKSKDEELKALRSELFHGGKQQFSPQKSVQYETLPPPTASSITSTVTSNTSDCVQAAIARVERERDCARTELERVRCERDTLREKQLSTVQLHADELQALRLRNEELNDRLRQMERDNRELNSARLPTETNLVLLKEDLLQMRQRVASMQTEIDQLKTENDQITMLNDQNERIIADYQSKLLVAERQRQSADVRASTLDSSRESNRSEVTQLRMDLGALRQTYISLEHEKDTLLHQLDTKTERVYKLEYELKDCKEKRNALEQNVKDLEDQLRKLANRNRQRDSELTETSTESKTLRQQIVALKASRDEAIAENRRLMDKLSDAQVEARTLQKKLTDSELQVANMKQQLHKYVQEVKKAEDLLIQKVSSKFKEKERDDMLDQYHCLTQGQATLEGNNQSLECEAVEFRRQICELECEVHSLKEQLQLRQCALHDMEVQLTAARASVRCLERELENARDDIRVQKVDLEARKELCDKLDVERSKLNAELNDVNEIRKKLEKQCEKLRDELQQSLAINQVTNETTDLMLGRLHNDQQHQEDDDIRSKHEMDRLQRQLQQTLDQLQEERVRCRHHEELAEKWEQQVRDLRRNLADDRYNQARTREVSPRVPSKTL
Protein: Archaetidylserine synthase (EC 2.7.8.38) (CDP-2,3-di-O-geranylgeranyl-sn-glycerol:L-serine O-archaetidyltransferase) (O27106)
Organism: Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Function: Involved in the lipid biosynthesis. Catalyzes the formation of unsaturated archaetidylserine from CDP-unsaturated archaeol and L-serine. Activity with ester-linked substrate analogs containing straight aliphatic chains (typical bacterial substrates) is two to three times higher than that with the corresponding ether-type substrate (typical archaeal substrates). Both enantiomers of CDP-unsaturated archaeols with ether-linked geranylgeranyl chains and CDP-saturated archaeol with ether-linked phytanyl chains are similarly active. The enzyme also accepts D-serine, although activity is only about third of that with L-serine.
Subcellular location: Membrane {ECO:0000305|PubMed:12562787}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Putative archaetidylserine decarboxylase proenzyme
- CDP-archaeol synthase
- Flp pilus assembly protein RcpC/CpaB domain-containing protein
Sequence:
MMNDKKITSFIALPDLLSMLNASSGYLSILLSIDGSLNAACILMLLAVLFDSLDGWVARKTGRIDIHGFGKNMDSLSDVISFGVAPAILIYSAAVDFRYINILVGPLIVLCGILRLSRFNVLTGGGKNFTGLPIPVAAVTISSFYLTGFYSELSAAFIMIAVSVLMISSIEYPRVDGMGASTALILIIATIISVAAVEILQAASVVAGPVAIILFIATLTYIAVPILPKRDVI
Protein: Cell division protein FtsZ (Q47QW6)
Organism: Thermobifida fusca (strain YX)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00909}. Note=Assembles at midcell at the inner surface of the cytoplasmic membrane. {ECO:0000256|HAMAP-Rule:MF_00909}.
Interaction partners:
- Cell division protein SepF
- UDP-N-acetylglucosamine--N-acetylmuramyl-
- Protein translocase subunit SecA 1
- Cell division protein FtsQ
- Probable peptidoglycan glycosyltransferase FtsW
- UDP-N-acetylmuramate--L-alanine ligase
- Protein translocase subunit SecA 2
- Cell wall synthesis protein Wag31
- Probable cell division protein WhiA
- UDP-N-acetylmuramoylalanine--D-glutamate ligase
Sequence:
MAAPQNYLAVIKVVGIGGGGVNAVNRMIEEGLKGVEFIAINTDAQALLMSDADVKLDVGRELTRGLGAGANPDVGRKAAEDHREEIEEVLKGADMVFVTAGEGGGTGTGGAPVVANIARSLGALTIGVVTRPFSFEGKRRATQAEAGIAMLREEVDTLIVIPNDRLLSISDRQVSVLDAFKAADQVLLSGVQGITDLITTPGLINLDFADVKSVMSGAGSALMGIGSARGDDRAVAAAEMAISSPLLEASIDGAHGVLLSIQGGSDLGLFEINEAAQLVANSAAAEANIIFGAVIDDALGDEVRVTVIAAGFDEPQVESPSPTPSRAVSAPTTPAAPERFTPPPPPPPPLRTVEPPRSEPPTPSLARDPRPTTEPDSGAETAAEPAATEEPQSDSAAASEAKETKDTPANRDEDRPYRPGGLYPMGGEGGYTRPRVSDSPFSRSGEIPTPRRRVVFDEGDDLDVPDFLK
Protein: Matrix protein (Q15EM2)
Organism: Avian paramyxovirus 1 (NDV) (Avian orthoavulavirus 1)
Subcellular location: Virion {ECO:0000256|ARBA:ARBA00004328}.
Interaction partners:
Sequence:
MDSSRTIGLYFDSALPSSNLLAFPIVLRDVGDGKKQITPQYRIRRLDSWTDSKEDSVFITTYGFIFQVGNEEVTVGMINDNPKRELLSAAMLCLGSVPNVGDPVELARACLTMVVTCKKSATNTERMVFSVVQAPRVLQSCRVVADKYSSVNAVKHVKAPEKIPGSETLEYKVNFVSLTVVPKKDVYKIPTAVLKVSGSSLYNLALNVTIDVEVDPKSPLVKSLSRSDSGYYANLFLHIGLMSTVDKRGKKVTFDQLERKIRRLDLSVGLSDVLGPSVLVKARGARTRLLAPFFSNSGTACYPIANASPQVAKILWSQTACLRSVKIIIQAGTQRAVAVTADHEVTSTKIEKRHTIAKYNPFKK
Protein: Inosine-5'-monophosphate dehydrogenase 1 (IMP dehydrogenase 1) (IMPD 1) (IMPDH 1) (EC 1.1.1.205) (D3ZLZ7)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03156}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03156}.
Interaction partners:
- GMP synthase
- Adenylosuccinate synthetase isozyme 2
- Adenylosuccinate synthetase isozyme 1
- Bifunctional purine biosynthesis protein ATIC
- Inosine-5'-monophosphate dehydrogenase 2
- AMP deaminase 3
- AMP deaminase 2
- AMP deaminase 1
- 5'-nucleotidase
- Hypoxanthine-guanine phosphoribosyltransferase
Sequence:
MADYLISGGTGYVPEDGLTAQQLFANADGLTYNDFLILPGFIDFIADEVDLTSALTRKITLKTPLISSPMDTVTEADMAIAMALMGGIGFIHHNCTPEFQANEVRKVKKFEQGFITDPVVLSPSHTVGDVLEAKIQHGFSGIPITATGTMGSKLVGIVTSRDIDFLAEKDHTTLLSEVMTPRIELVVAPAGVTLKEANEILQRSKKGKLPIVNDQDELVAIIARTDLKKNRDYPLASKDSHKQLLCGAAVGTREDDKYRLDLLTQAGADVIVLDSSQGNSVYQIAMVHYIKQKYPHLQVIGGNVVTAAQAKNLIDAGVDGLRVGMGCGSICITQEVMACGRPQGTAVYKVAEYARRFGVPVIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEYFFSDGVRLKKYRGMGSLDAMEKSSSSQKRYFSEGDKVKIAQGVSGSIQDKGSIQKFVPYLIAGIQHGCQDIGAQSLSVLRSMMYSGELKFEKRTMSAQIEGGVHGLHSYEKRLY
Protein: Diamine acetyltransferase 1 (EC 2.3.1.57) (Polyamine N-acetyltransferase 1) (Putrescine acetyltransferase) (Spermidine/spermine N(1)-acetyltransferase 1) (A0A8J8XCW9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MYYFTYDPWIGKLLYLEDFFVMSDYRGFGIGSEILKNLSQVAMKCRCSSMHFLVAEWNEPSINFYKRRGASDLSSEEGWRLFKIDKEYLLKMAAEE
Protein: Transmembrane protein 53 (Q54YR8)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Nucleus outer membrane {ECO:0000256|ARBA:ARBA00034303}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00034303}.
Interaction partners:
Sequence:
MGAQKLPILEYLQAENDSPLPYEGEDRPLVVVLGWMGCRREHLLKYVDQWRKRGFNTFSFCSKPIQLLVPGVIQNKGDEMLEQIKKYLKENRNCKSVIFNAFSNGGGFYYAHMIRQIHEREDCKWMAPLVKGTVLDSLPAIRPLSIYSAFRLTSPNMFVTFLLALVVPLFVVLFWSKMSSYQQILTSKKNQWQHLIFYSKADTIVHSDDIDNLVGKIKNNLSDVNHLDYKCFDDSPHVLHMRSHPKIYEDKLNHFVTSIKNSNLKKLQNK
Protein: Cecropin-A1 (C0HKQ7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. Functions in the imd/NF-kappa-B (Imd) epithelial and humoral immune response to Gram-negative bacteria.
Subcellular location: Secreted {ECO:0000269|PubMed:16510152}.
Interaction partners:
- Nuclear factor NF-kappa-B p110 subunit
- Dorsal-related immunity factor Dif
- Defensin
- Diptericin B
- Diptericin A
- Protein immune deficiency
- Attacin-A
- Drosocin antimicrobial peptides
- Metchnikowin
- Cecropin-C
Sequence:
MNFYNIFVFVALILAITIGQSEAGWLKKIGKKIERVGQHTRDATIQGLGIAQQAANVAATARG
Protein: Ift88 (Intraflagellar transport protein 88 homolog) (Q6RUQ9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MENVHLVPEEEEDDLYTGYNDYNPTFDSEDLHNDVAFQQAVRTSHGRRPPMTAKYPGTAIGGRPIGTAYGSRVPIGTAMGRPMTGAVQDGAARPMTAVRAAGYSSSIARGSAFDPLGQAKGPAPPLETKNEDTPEEKIKILEKKVNDLIEDSCLAHARGDLQVSLEKAKEAGRKERALVRQREQTGTADHINLDLTYSVLFNLANQYANNDMYTEALNTCQVIVKNKMFNNAGRLKVNMANIYFKQKNYTKAIKFYRMALDQISNAHNAMRIKIMQNIGVVFIHMGQYSDAITSFEYIMTESPNIKTGFNLILCYYAIGDRERMKKAFQKLICVPLGVDDDDKYIPPNDDPHANMVIEAIKNDKLHQMERERKALAEKYIMTSAKLIAPAIEMSFAAGFDWCVDMVKGSQYVELANDLEINKAITYLRQRDFKQAVETLKMFEKKDSRVKSAAATNLSFLYFLEKDFDQADRYAELAMSADRYNPAALINKGNTLFVKEDYEKAAEFYKESLRNDSSCTEALYNLGLTYKRLGRLEEALDCFLKLHAILRNSAQVMYQLANLYEMLEDPHQAIEWLMQLTSVTPTDAQVLAKLGDLYDNEGDKSQAFQYYYESYRYFPSNISVIEWLGAYYIDTQFCEKAIQYFERATLIQPTQVKWQLMVASCYRRSGNYQKALETYKEIHRKFPENVECLRFLVRLCTDMGLKEVQDYATKLKKVEKMKEIREQRVRSGRDSSARSRREGSAGSDSGQSNHGTSAKGERLSVKLKTLPGSNEPYEASTQQEIDASYVDPLGPQTQRPKTAARKRNEEDEFADEELGDDLLPE
Protein: Glutaminyl-peptide cyclotransferase (EC 2.3.2.5) (Glutaminyl cyclase) (Q84WV9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Converts glutamine and N-terminal glutamyl residues in peptides to 5-oxoproline and 5-oxoproline residues. Not involved in the major pathway for 5-oxoproline production.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Transcription regulator
- AT5g35440/MOK9_2
- Transcription regulator NOT2/NOT3/NOT5 family protein
- Protein kinase superfamily protein
- At5g19300
- AAA-ATPase At3g50940
- FACT complex subunit SSRP1
- Probable NOT transcription complex subunit VIP2
- Thioredoxin-like 4, chloroplastic
- NOT2 / NOT3 / NOT5 family
Sequence:
MATRSPYKRQTKRSMIQSLPASSSASSRRRFISRKRFAMMIPLALLSGAVFLFFMPFNSWGQSSGSSLDLSHRINEIEVVAEFPHDPDAFTQGLLYAGNDTLFESTGLYGKSSVRKVDLRTGKVEILEKMDNTYFGEGLTLLGERLFQVAWLTNTGFTYDLRNLSKVKPFKHHMKDGWGLATDGKALFGSDGTSTLYRMDPQTMKVTDKHIVRYNGREVRYLNELEYINNEVWANVWQSDCIARISPKDGSLLGWILLSKLSRGLLKSGHRGIDVLNGIAWDSDKQRLFVTGKLWPKLYQIKLKQASAKSGNYIEQQCLV
Protein: Serine protease filzig (EC 3.4.21.-) (Lumens interrupted) (B7YZU2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probable endopeptidase. In tracheal terminal cells, acts downstream of ich to regulate seamless tube growth and/or maintenance probably by processing lumenal matrix proteins.
Subcellular location: Cell membrane {ECO:0000305|PubMed:29309404}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Ichor
- Dusky-like, isoform A
Sequence:
MFKWVTPASTATLSRCTLPATTAATTTTTAMAATRTATTTTRTTRPQLLSIALTSLIIIVASFVPTTSGFRSIETNGGGRKLFGGYRITPKHCRATKTLPSSDPRANGPTICMFNHECAQRGGEVVGACMDGFLFGACCQIPPTHELASTLINEAQNAYFQQHQQQTKLQQSAAQSSFESYGEQQQSLSEEQVAQQPSQNIYDQQNLDKVYQQLDSSSSISPPNGAYGDEPQQQEYQSESEQPVRDENAYPTSSSSTEATQSQSSSASVEFEQEPSQPADASNDQTTQKINKQPVQPPNFHVHKHSVTINSPSSPPQNDDFVMQVLSTLPPEHADDHHIVFTTEVPTKITSGLQDQTSSESNSFEEVSSTPAATQKPKPKPTQMPTQKTTQKATQKPTPKPTQKAKPKPVPQLAESMKRPIQQKPQQVAKPKPSPKPAQSTNNHHHNHLILDGGEFTHSDITHPGADADLVEDLQFSTGYGPQPVYAEPPKQQQQQQPAEQSYISSSTSAKRPTTGHNSPTTVSSITTHVDSIESIILQLNNTSHGPSYNVVSQQTPSYGYPGAAVVQTEPAAQNPTFYQENESEKVQESDSQSDYGYTTTVNYESFYDKVSDEQDASAAVSQSAEMPTARPGYGEDVSAVLEDHTMPANGYHDAEAPVAPQTSEFNKMPVMGIAYPVDMSYMEEEGNLPATAAGYGQMSSDSYEASTESTYQKLSTVQTEEPQPTYVRPTTNANKQNRPVASYIGMVTMQHYNPQPGNGDYQAQVPPEVSVSSHTTKVQEQMDETSNGYQQSETTSGYVSPPTAVPAPAQRPQYDAVQGDASSERPVLVTASPRPRPKPSTKRPAVKRPISGESTKKKPQPQPSAGAYNQEKISEHSTRKPVSNGYDKVPESPITHIQIKKPSATQHKEQEQTGYPRPASPAGYEQTTAAAPAPAAPSLNYDKPDAPPSQYDQPSAPSASYDQLAPMPSLNYNEQHASSPGRKPSTAKPISTSYVTGPSTPRPPATVDYHYDNVPPLFMADDKLDAFIQSTAENIVGSTPGNYQPPLVATASTPAYAHRPTSSGSYGHKKPGFVQINGTPKPPRPTVLITPKPTAINLVTYSSLSDDSNKLASSTSSYVTGRPGVQGVSSNDFKDPGYFGSSPVHVAFTQSTTEAVYAVPSDDKPAFPGYFGPTPSYPAFSVPGEKVGQNVMEETYTSPNDFVNFPPVRNPNLNMSAASSAVTSDLDLSTPAFVEDVVLKDKMHTLVHKLVASLQGNFEALADMIEEPGSNKTVATYQAGAGGTAKPVRVVTTRKPVRTATTTRPKVTTKKPVTRVTTKAPNKKTSAVSTTTRKPATRRTTVAAKVTTTTRRPATKKPTRRVSSTVKTTTVSSARPADDEIVDEEDEEDVNPNPSDNEIDQGATLSSYGGANGRKIHSTSRTLPTPNLAFHSPSTECGVRPHVKSGRIVGGKGSTFGAYPWQVLVRESTWLGLFTKNKCGGVLITSRYVITAAHCQPGFLASLVAVMGEFDISGDLESKRSVTKNVKRVIVHRQYDPATFENDLALLELDSPVQFDTHIVPICMPNDVADFTGRMATVTGWGRLKYGGGVPSVLQEVQVPIIENSVCQEMFHTAGHNKKILTSFLCAGYANGQKDSCEGDSGGPLVLQRPDGRYELAGTVSHGIKCAAPYLPGVYMRTTFYKPWLRSITGVK
Protein: Protein Wnt-6 (P22727)
Organism: Mus musculus (Mouse)
Function: Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters.
Subcellular location: Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Protein-serine O-palmitoleoyltransferase porcupine
- Wnt inhibitory factor 1
- Frizzled-9
- Palmitoleoyl-protein carboxylesterase NOTUM
- Low-density lipoprotein receptor-related protein 5
- Frizzled-2
- Frizzled-4
- Frizzled-5
- Frizzled-3
- Glypican-3
Sequence:
MLPPVPSRLGLLLLLLCPAHVDGLWWAVGSPLVMDPTSICRKARRLAGRQAELCQAEPEVVAELARGARLGVRECQFQFRFRRWNCSSHSKAFGRVLQQDIRETAFVFAITAAGASHAVTQACSMGELLQCGCQAPRGRAPPRPSGLLGTPGPPGPTGSPDASAAWEWGGCGDDVDFGDEKSRLFMDAQHKRGRGDIRALVQLHNNEAGRLAVRSHTRTECKCHGLSGSCALRTCWQKLPPFREVGARLLERFHGASRVMGTNDGKALLPAVRTLKPPGRADLLYAADSPDFCAPNRRTGSPGTRGRACNSSAPDLSGCDLLCCGRGHRQESVQLEENCLCRFHWCCVVQCHRCRVRKELSLCL
Protein: Cytochrome b translation regulator cbp7 (O74361)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:34634819}.
Interaction partners:
- Mitochondrial translation factor sls1
- Cytochrome b translation regulator cbp8
- Mitochondrial translation ATP-dependent RNA helicase mrh5
- Small ribosomal subunit protein L51-b
- Probable 2-dehydropantoate 2-reductase
- Pentatricopeptide repeat-containing protein 7
- CBP3-like protein
Sequence:
MADVIKRCILGPTEAGWFVAKSQIKKPVDQRPVILTHCKLHSKMLEPKAIVYKKNSSAIPKRVDNILLRSQKPKHIECLLVDSKITKTRSLLKRFGSCLDETSTIVLLNQSVSLWEDCYSLFPKTETRPRIYLGRFQTLFKSFPFNLISDSFSYRLNLSKLPRTPLEKCTVARACKQFPLNQRSPLLDLMGSFERDYVNFSNFSQMLSAQLCDSMAFLIQIFPTPLLRQKAANAWIEVLSKLPYFHILDKSFFSPHLLLQSSENQACKFFNIGPQVYFDPRERLLHVKELLKFALKHIDSNDSLFTFLKQTCYTCDSPYAKVFQPDKQSFHSIISRKRLAHLEKEYFDKDVSKLVL
Protein: Metallothionein-3 (MT-3) (Growth inhibitory factor) (GIF) (Metallothionein-III) (MT-III) (P28184)
Organism: Mus musculus (Mouse)
Function: Binds heavy metals. Contains three zinc and three copper atoms per polypeptide chain and only a negligible amount of cadmium. Inhibits survival and neurite formation of cortical neurons in vitro (By similarity).
Interaction partners:
- Metallothionein-4
- Metallothionein-2
- Probable proton-coupled zinc antiporter SLC30A3
Sequence:
MDPETCPCPTGGSCTCSDKCKCKGCKCTNCKKSCCSCCPAGCEKCAKDCVCKGEEGAKAEAEKCSCCQ
Protein: Glutathione S-transferase U17 (AtGSTU17) (EC 2.5.1.18) (GST class-tau member 17) (Glutathione S-transferase 30) (Protein EARLY RESPONSIVE TO DEHYDRATION 9) (Q9FUS8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in light signaling, mainly phyA-mediated photomorphogenesis and in the integration of various phytohormone signals to modulate various aspects of plant development by affecting glutathione pools. In vitro, possesses glutathione S-transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and benzyl isothiocyanate (BITC).
Subcellular location: Cytoplasm, cytosol {ECO:0000305}.
Interaction partners:
- Glutathione S-transferase DHAR2
- Glutathione S-transferase DHAR1, mitochondrial
- Glutathione S-transferase DHAR3, chloroplastic
- Glutathione S-transferase TCHQD
- Glutathione S-transferase F2
- Probable phospholipid hydroperoxide glutathione peroxidase 6, mitochondrial
- Glutathione synthetase, chloroplastic
- Probable glutathione peroxidase 3, mitochondrial
- Phospholipid hydroperoxide glutathione peroxidase 1, chloroplastic
- Glutathione S-transferase L3
Sequence:
MASSDVKLIGAWASPFVMRPRIALNLKSVPYEFLQETFGSKSELLLKSNPVHKKIPVLLHADKPVSESNIIVEYIDDTWSSSGPSILPSDPYDRAMARFWAAYIDEKWFVALRGFLKAGGEEEKKAVIAQLEEGNAFLEKAFIDCSKGKPFFNGDNIGYLDIALGCFLAWLRVTELAVSYKILDEAKTPSLSKWAENFCNDPAVKPVMPETAKLAEFAKKIFPKPQA
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q32LI4)
Organism: Bos taurus (Bovine)
Interaction partners:
Sequence:
MASSSGSKAEFIVGGKYKLVRKIGSGSFGDIYLAINITNGEEVAVKLESQKARHPQLLYESKLYKILQGGVGIPHIRWYGQEKDYNVLVMDLLGPSLEDLFNFCSRRFTMKTVLMLADQMISRIEYVHTKNFIHRDIKPDNFLMGIGRHCNKLFLIDFGLAKKYRDNRTRQHIPYREDKNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRTSLPWQGLKAATKKQKYEKISEKKMSTPVEVLCKGFPAEFAMYLNYCRGLRFEEAPDYMYLRQLFRILFRTLNHQYDYTFDWTMLKQKAAQQAASSSGQGQQAQTPTGLKDEKLDPLS
Protein: ASC-1 (TRIP4/RQT4 C2HC5-type zinc finger domain-containing protein) (G5EDK1)
Organism: Caenorhabditis elegans
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 15
- Mediator of RNA polymerase II transcription subunit 11
- Mediator of RNA polymerase II transcription subunit 8
- Mediator of RNA polymerase II transcription subunit 4
- DNA-directed RNA polymerase II subunit RPB1
- Mediator of RNA polymerase II transcription subunit 23
- Mediator of RNA polymerase II transcription subunit 17
- Activating signal cointegrator 1 complex subunit 3
- Bromodomain associated domain-containing protein
- K Homology domain-containing protein
Sequence:
MGKKQAGGKGGVAGRQNVLAAKTEISFADTLRKGRHECLCQARTHKLILNCLGCGRIVCEQEGSGPCFTCGTLVCTREEREILNRGTNKSRDLLARLTGDGSDIGSLKQISSSYQNATEFRNKLLEADADTERRTKVNDLQSDYSTIENSPFLSASDREALKLRREELKALREKERKKFVVSLDFDGGVVHEMTRRSGTEALQDKNDPVIQRIMERVDEKHRIQEALHNSTADARWNPIGFVPRYMTEDGDHPQQECSDGDIIDADSLMIVSDELAAQITEEKGYVLALAQPTASFLVNGLCRFIRWPTDLNLKGPLFITAKAGGTNEKMIREFAKKYVRDVNKISELDFSDGAVLGRAFLQECMMLEDFLDKYGSKSAIPGGDGQFVLCFSAFEPLVSTIPHISTADSYIYEMDRQLKRSLTKW
Protein: Leukocyte immunoglobulin-like receptor subfamily A member 2 (CD85 antigen-like family member H) (Immunoglobulin-like transcript 1) (ILT-1) (Leukocyte immunoglobulin-like receptor 7) (LIR-7) (CD antigen CD85h) (Q8N149)
Organism: Homo sapiens (Human)
Function: Part of the innate immune responses against microbial infection. Specifically recognizes a set of N-terminally truncated immunoglobulins that are produced via cleavage by proteases from a range of pathogenic bacteria and fungi, including L.pneumophila, M.hyorhinis, S.pneumoniae, S.aureus and C.albicans. Recognizes epitopes that are in part in the variable region of the immunoglobulin light chains, but requires also the constant region for signaling. Binds to a subset of cleaved IgM, IgG3 and IgG4 molecules, but does not bind cleaved IgA1. Binding of N-terminally truncated immunoglobulins mediates activation of neutrophils. In monocytes, activation leads to the release of CSF2, CF3, IL6, CXCL8 and CCL3 and down-regulates responses to bacterial lipopolysaccharide (LPS), possibly via down-regulation of TLR4 expression and reduced signaling via TLR4. In eosinophils, activation by ligand binding leads to the release of RNASE2, IL4 and leukotriene C4. Does not bind class I MHC antigens.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12529506, ECO:0000269|PubMed:22479404, ECO:0000269|PubMed:27572839}; Single-pass type I membrane protein {ECO:0000305|PubMed:12529506, ECO:0000305|PubMed:22479404}.; SUBCELLULAR LOCATION: [Isoform 4]: Secreted {ECO:0000303|PubMed:19658091}.
Interaction partners:
- Tyrosine-protein phosphatase non-receptor type 6
- CMRF35-like molecule 6
- Tyrosine-protein kinase SYK
- High affinity immunoglobulin epsilon receptor subunit gamma
- HLA class I histocompatibility antigen, A alpha chain
- TYRO protein tyrosine kinase-binding protein
Sequence:
MTPILTVLICLGLSLGPRTHVQAGHLPKPTLWAEPGSVIIQGSPVTLRCQGSLQAEEYHLYRENKSASWVRRIQEPGKNGQFPIPSITWEHAGRYHCQYYSHNHSSEYSDPLELVVTGAYSKPTLSALPSPVVTSGGNVTLQCVSQVAFDGFILCKEGEDEHPQRLNSHSHARGWSWAIFSVGPVSPSRRWSYRCYAYDSNSPYVWSLPSDLLELLVPGVSKKPSLSVQPGPMVAPGESLTLQCVSDVGYDRFVLYKEGERDFLQRPGWQPQAGLSQANFTLGPVSPSHGGQYRCYSAHNLSSEWSAPSDPLDILITGQFYDRPSLSVQPVPTVAPGKNVTLLCQSRGQFHTFLLTKEGAGHPPLHLRSEHQAQQNQAEFRMGPVTSAHVGTYRCYSSLSSNPYLLSLPSDPLELVVSEAAETLSPSQNKTDSTTTSLGQHPQDYTVENLIRMGVAGLVLVVLGILLFEAQHSQRSLQDAAGR
Protein: Non-selective voltage-gated ion channel VDAC1 (Brain-derived voltage-dependent anion channel 1) (BR1-VDAC) (Plasmalemmal porin) (Voltage-dependent anion-selective channel protein 1) (VDAC-1) (P45879)
Organism: Bos taurus (Bovine)
Function: Forms a channel through the mitochondrial outer membrane and also the plasma membrane. The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis. It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective. Binds various signaling molecules, including the sphingolipid ceramide, the phospholipid phosphatidylcholine, and the sterol cholesterol. In depolarized mitochondria, acts downstream of PRKN and PINK1 to promote mitophagy or prevent apoptosis; polyubiquitination by PRKN promotes mitophagy, while monoubiquitination by PRKN decreases mitochondrial calcium influx which ultimately inhibits apoptosis. May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis. May mediate ATP export from cells.
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P21796}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P21796}. Cell membrane {ECO:0000250|UniProtKB:P21796}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P21796}. Membrane raft {ECO:0000250|UniProtKB:P21796}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P21796}. Note=Found in a complex with HSPA9 and VDAC1 at the endoplasmic reticulum-mitochondria contact sites. {ECO:0000250|UniProtKB:Q9Z2L0}.
Interaction partners:
- Non-selective voltage-gated ion channel VDAC2
- Peptidyl-prolyl cis-trans isomerase F, mitochondrial
- Stress-70 protein, mitochondrial
- Translocator protein
- Cytochrome c
- ADP/ATP translocase 3
- Non-selective voltage-gated ion channel VDAC3
- Cytochrome c 2
- ADP/ATP translocase 1
- ADP/ATP translocase 2
Sequence:
MAVPPTYADLGKSARDVFTKGYGFGLIKLDLKTKSENGLEFTSSGSANTETTKVTGSLETKYRWTEYGLTFTEKWNTDNTLGTEITVEDQLARGLKLTFDSSFSPNTGKKNAKIKTGYKREHINLGCDVDFDIAGPSIRGALVLGYEGWLAGYQMNFETAKSRVTQSNFAVGYKTDEFQLHTNVNDGTEFGGSIYQKVNKKLETAVNLAWTAGNSNTRFGIAAKYQIDPDACFSAKVNNSSLIGLGYTQTLKPGIKLTLSALLDGKNVNAGGHKLGLGLEFQA