wanglab/gogpt-training-data huggingface dataset:
Protein: Histone deacetylase 8 (HD8) (EC 3.5.1.98) (Protein deacetylase HDAC8) (EC 3.5.1.-) (Protein decrotonylase HDAC8) (EC 3.5.1.-) (Q8VH37)
Organism: Mus musculus (Mouse)
Function: Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Also involved in the deacetylation of cohesin complex protein SMC3 regulating release of cohesin complexes from chromatin. May play a role in smooth muscle cell contractility. In addition to protein deacetylase activity, also has protein-lysine deacylase activity: acts as a protein decrotonylase by mediating decrotonylation ((2E)-butenoyl) of histones.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9BY41}. Chromosome {ECO:0000250|UniProtKB:Q9BY41}. Cytoplasm {ECO:0000250|UniProtKB:Q9BY41}. Note=Excluded from the nucleoli. Found in the cytoplasm of cells showing smooth muscle differentiation. {ECO:0000250|UniProtKB:Q9BY41}.
Interaction partners:
- Nuclear receptor corepressor 2
- Structural maintenance of chromosomes protein 3
- Paired amphipathic helix protein Sin3a
- Structural maintenance of chromosomes protein 1A
- Histone-lysine N-methyltransferase EZH2
- Nipped-B-like protein
- Nuclear receptor corepressor 1
- Histone H2A.Z
- NAD-dependent protein deacetylase sirtuin-1
- F-box-like/WD repeat-containing protein TBL1X
Sequence:
MEMPEEPANSGHSLPPVYIYSPEYVSICDSLVKVPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDEDHPDSIEYGLGYDCPATEGIFDYAAAIGGGTITAAQCLIDGKCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFDRILYVDLDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDMSDVGLGKGRYYSVNVPIQDGIQDEKYYHICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYVLQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCRPDRNEPHRIQQILNYIKGNLKHVV
Protein: RNA helicase (EC 3.6.4.13) (Q22308)
Organism: Caenorhabditis elegans
Interaction partners:
- Nuclear pore complex protein 14
- MIF4G domain-containing protein
- Nsp1_C domain-containing protein
- mRNA export factor rae-1
- Nuclear pore complex protein Nup98-Nup96
- Glycine Rich Secreted Protein
Sequence:
MADWGIAFDEQCRSEGLEVPEKTEKVQSGSEMDQNEENKGSNGWGISRGGMFGGPKASNAPPPQTSFGSTSGTRVGGSFGGQAGVDGRGAPLGSAEELIGGGNIISVGIHKEKPACKRGGGFGTNRSMAPCPPAIIKNNHEGGRFGVLAPRTLSGSIPQTSTNLEDSTPKTSTGGRFGASISQGGAFGAKTQSSSVAPSVGGGFGVKSPNIVSNDMPKVPVMKSVGGGFGSSMKSPATTGGSFGSSTVVASIRSEESFGIKSSASAGGSFNSSSASASQSRTVASFGSKPSNENISSNSSALSSSSSCFAAKPTSTSAGGSFGNQPSSFSSKPSFGGAFGASTSVTGSSSMGGSFGNKSTKVPDVESLSPPEILRNPSNTSGGAFGSKPSFAASSSELPANKHVVGGGFGRSTAPTVNTSVGNESGRLPFVETRNPNTEQETSSSVRPYGANFNSKSEPAQKNPFGGNSSSTKPEFKENEMKNSSVPIMPGQSQPMRGGFQGAYRGGRGSGGGQMDFGAPGQGQSMGRGRGQQNPAFVPRPRDTPPQYGGHQAAQQFVKPDSKYKFTKPATEEAHEQVPVPADIALLNKFIQKEVKMMKDVVVDVQRQDPKSPLYSISSFRELRLKPEVLKALDTMNFQFPTRIQETALPLLLMEPPSNLIAQAQSGTGKTAAFVLTMLCRIDVNLMCPQCICLAPTLELAKQIGEVVEKMGKFIDNLKIHYAIKGGNMAAMRGRKLTEQIVIGTPGITRDYLQKYKCIDPSKIRCLVLDEADVMIYHQGFTDISTTIYNMVEDASDSVQSMLFSATYDEPVINFATKIIKNAIVVMLKREEQALPNIKQFYVQCACRDSKYAAIVNLYSGLAVASSVIFCHTKASVMWLYENMRARGHQVDVLHGDMTVVERADTIIHFKRGDFKVLITTNVFARGIDVAQVSVVINYDLPIKYTDEGTPMVVDGFTQPDCETYLHRIGRTGRFGKTGIAINLIDSEDSMNMINVLENHFQMKIARMDPSNLVELEAIEMA
Protein: Putative aminodeoxychorismate lyase (EC 4.1.3.38) (4-amino-4-deoxychorismate lyase) (ADC lyase) (ADCL) (O42951)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Converts 4-amino-4-deoxychorismate into 4-aminobenzoate (PABA) and pyruvate.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Putative aminodeoxychorismate synthase
- Folic acid synthesis protein fol1
- V-type proton ATPase subunit c'
- Probable anthranilate synthase component 1
Sequence:
MEESNLFETTLYDGELFLLPSHLQRMKASAKSLGYSWPGEQYIENKLREAVQDTSMARVRWELSKAGDVTVQIVPIQTLEKAPYTLILDKQPSSTEKNPSCINKMTNRAIYIEAMNRNDAQYSKAQDVLLYNHQGFVTEATIFNVAFHRNGQWITPSLKHGLLSGTMRKNLLENGSIHEDDKGLLQKDNLKNGEQVLLFNSFRKVCKGVLIIQPEKACELLKKKDSSEKLS
Protein: SGCZ protein (Sarcoglycan zeta) (Q08AT0)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane, sarcolemma {ECO:0000256|ARBA:ARBA00004274}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004274}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MTREQYILATQQNNLPRTENAQLYPVGIYGWRKRCLYFFVLLLLVTMIVNLAMTIWILKVMNFTVDSPLVLQSDRNVTVNARNHMGQLTGQLTIGADAVEAQCKRFEVRASEDGRVLFSADEDEITIGAEKLKVTGTEGAVFGHSVETPHIRAEPSQDLRLESPTRSLIMEAPRGVQVSAAAGDFKATCRKELHLQSTEGEIFLNAETIKLGNLPTGSFSSSSPSSSSSRQTVYELCVCPNGKLYLSPAGVGSTCQSSSNICLWS
Protein: Sorting nexin-17 (Q8BVL3)
Organism: Mus musculus (Mouse)
Function: Critical regulator of endosomal recycling of numerous surface proteins, including integrins, signaling receptor and channels. Binds to NPxY sequences in the cytoplasmic tails of target cargos (By similarity). Associates with retriever and CCC complexes to prevent lysosomal degradation and promote cell surface recycling of numerous cargos such as integrins ITGB1, ITGB5 and their associated alpha subunits (By similarity). Also required for maintenance of normal cell surface levels of APP and LRP1. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q15036}. Early endosome {ECO:0000250|UniProtKB:Q15036}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q15036}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q15036}; Cytoplasmic side {ECO:0000250|UniProtKB:Q15036}.
Interaction partners:
- Krev interaction trapped protein 1
- P-selectin
- Vacuolar protein sorting-associated protein 35
- Sorting nexin-2
- Sorting nexin-1
- Vacuolar protein sorting-associated protein 29
- Vacuolar protein sorting-associated protein 26C
- Sorting nexin-3
- Low-density lipoprotein receptor-related protein 8
- Sorting nexin-12
Sequence:
MHFSIPETESRSGDSGGSAYVAYNIHVNGVLHCRVRYSQLLGLHEQLRKEYGANVVPAFPPKKLFSLTPAEVEQRREQLEKYMQAVRQDPLLGSSETFNSFLRRAQQETQQVPTEEVSLEVLLSNGQKVLVTVLTSDQTEDVLEAVAAKLDLPDDLIGYFSLFLVREKEDGAFSFVRKLQEFELPYVSVTSLRSQEYKIVLRKSYWDSAYDDDVMENRVGLNLLYAQTVSDIEHGWILVTKEQHRQLKSLQEKVSKKEFLRLAQTLRHYGYLRFDACVADFPEKDCPVVVSAGNSELSLQLRLPGQQLREGSFRVTRMRCWRVTSSVPLPSGGTSSPSRGRGEVRLELAFEYLMSKDRLQWVTITSPQAIMMSICLQSMVDELMVKKSGGSIRKMLRRRVGGTLRRSDSQQAVKSPPLLESPDASRESMVKLSSKLSAVSLRGIGSPSTDASASAVHGNFAFEGIGDEDL
Protein: Uncoordinated 79, isoform B (E1JIP9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTGSFKVQLINMGTRAAAFQAKLRALHEYHVRLLHNVLPAPSGVDIANNIKYFSQTLLTVLKDVRTSPHELIRDPLEDPTRMSAYPNLEYGNLYNALTMLIDVAPCIQYGQIVFGKALLQCLSCILPFLDKDLIDNLPYLVSSTISVLPPALHQCIINALCYYILPFTITRRSSDEQECQACQSVSSVIMMVLQYSNNPAHHCQLLECLMTLKHNVVKDILCVVAYGTAVSRTSAAKLLFYYWPAFNANLFDRKVLLSKLTNDLVPFTCQREHCPNSGNAEAAKVCYDHSISIAYAPDCPPPLYLCIECANEIHREHGSLEFGDILHPMQQVSMVCENKNCRSNEKSAFSICFSTECASFNGNHPIRYCSQCHSNRHNSRRGGDHVVHRSLQPAWQMDPEMQMHMVESVVSLLREAKPLNFEPGKESSSSESKKNGSGITADNISLEERQRLGRYGIWLLVGRCTPTADTPVEVLGRILSMLFHWFHVTAYSYDAAGQVESTIEKLKVDHVCNWLKDICRIHYNVFISCLLPHPPEYARVGGHWETLASRTSHLKEGLQRLICLVPYEVITSEIWDYVMPHWMEAITNDVAEKELNELKIVLSKILDPEMSPLGFDAKTMYNFVAIRFEKTTAKVQQQALHWLQILTKLEILIPLVQLFAMFGDGVRIMKYGIQHELMREKDAQSQSLAKAPKTPCKESKETKADMANPPRRSSISPVVEDDSGNTSAISDDEAPTNRHTEFSTDAEHNLTCCILMLDILLKQMELQDVEQHMGIHTSVCENVSRLIKCMVTAARVGLSSHVCALKVAECAYCEASIMWHQLATKLVQFMAPLNPVRPPDVPIEDIIEEEKSSRKSPPESDKEKTRDRDVSLSMAPLPIPLGPLGGFADIFKLDQFFSDDGKIIIMAGPVPVAVPQPEPHSVGGVLVHMPHVCSNNENGHSVDSNELRKVHATDEIMTATVETVSEQLDLASILPTDRAIARSITLSDADVGSANVSVTKASVMGENGANGGGACGGGENGSGSEEDEEEEDSDDFWHTSVGKFKFTLDTLPQPLQYIHQLLTEIPTIKKPEILYYVLQCLNTMALHGDALAKAAREQRGFFIWCQENLLIKNLWELCNAEHSHICQVGVPLLLHCITLPLGSDVFWRVVQEAFHDTDWRVRFTAVERVTVITRFMDSTPLRSEVGLQTALATAFCHLIASMDDINVYVAQRATLYIGTIHDTAIRSLLFCLESQFDLFIVDRPVVLQSVYQLHNSLSDRKMLGWEFFLNRFDTLFVEAQINLEKCGDISYLRDLRNSDNGSEALSAKIQKAREALSQSDTSGGMAKTLSASFGTKWPYKRTMSAPASMAPRQDSKFVPEKEKIYSRQVSAPILKRKTSRFGLDGHIHSLGGLNDDNLIGLLSRITELEESDRETIHLLVFMLMQFMSRTDQAYPSEEKPMTKTQNIVLKHLFLLLGHNQIDKTFHTTPESLRVSAVFNAFLANLPQVLDQNHLIGGLILPSVMQIILYAPNPTSTSGESYQNIVFNYSLWHLEQYPRRNWLFTLLVVLYKYSYTQPPLSGYVIAGIRLIMNSLRGHFHQCRRIPTTTILDIQGVGGAARSRDVSQPSLGTDPDDKEASPPASPMFPSEGTSAASKSKGNVAFTPKLQHAFRKYNDSSLDADETESELVAIPESDLSDSTLHGSSAPGSFDDTIHFEDVMPRNRRALEYTEEKSTKSHKSMITTKVGDTYTTKIKATTTSETLVTTHTRHSLQEGVRMIVTPLSLENAAASTSKMFAAIATNHLKALGALQDMPAAVERKAASSSGSGSRSANGSGNGSGGSAPAAIQASSSAAASKPIGRHKTIVECSAGNSSSSADDSRQKKSQTKSLRRTDKNYGSPDSPLSKMSVMPNPRDEMDESMQSLPPPKSIAALEIPTPERLLPIGTQDTVATLVERVRDGLNLPDISHLKQDSLDVSESTKDDVTPSSRTNSPRRLIKQVALESPPNPNAQLPSQPSADLHTSILKNVQQDLKQNAPEGNGLTTSNSIKRPRQKLAPFNVDSNAIPDIRSRFAGSWPPPPFQPVDPEPDDDDEIGAEASNGHGIHSTPHAPRGSSRRVGDYTIVERCSDCGAHIEEYTDEEIGIFIVILGTFIHREPAMAAPFLPEILTMTSRICLSSTHAWQGENGPPLASSAQAVACQFFRCVLHQLAPNGIFLQVFQTQMKMKIRHHHFRSIAKALQDFQDLNSTSPIYMVCESLTSKKSLPIEQLPVIFRNMAEYLNLQCVPTEAGVGLAVWSQAMQAMESLLRQVIVIMPSLTNAEYMLDIMAATLRLNCVPKTLLDPYSKIMAYCVQHTNLEYQTLYELCTLNIRSFSKDRDKNLLCRQMIFEFVQALKFKSNIPDHNLLTIIGFVLLDAGGTLPPGAAPGLPDAAPMMTTNSADCLRQYINDVIDFLADFHTLSKIKNFKNGQTSSGLGEDTLGGVLKGAVAQYLALEMSRGNSRDNKAVSRYLPWLNNAPSSLQQGPKEFTECVGHMRLLSWLLLGSLTHMALMQRRQETHSIPTPLPQQNSQGTGPAASVHYQHQGVTYSQPVPQEASCHIADHIQVIFAGFAEQSKTSVLHMSSLFHAFTLCQLWTVYLEQMAHNTNSNAEGSTLGVLFEFWAKVTPCILQLVSHAKPTVNKDQPQTPLDFQTQSANSKLSEMVNLHFLSLLEALKDTNSTVLGKLLPMWSPVLSSQTQLSDTLHVRLQNVRDYAPDYEEQQTYKSEALLKWLQRLQFKMGQIELQASTATQFYSI
Protein: Acyl-CoA synthetase short-chain family member 3, mitochondrial (EC 6.2.1.1) (Acetate--CoA ligase 3) (Propionate--CoA ligase) (EC 6.2.1.17) (Q14DH7)
Organism: Mus musculus (Mouse)
Function: Catalyzes the synthesis of acetyl-CoA from short-chain fatty acids (By similarity). Propionate is the preferred substrate but can also utilize acetate and butyrate with a much lower affinity (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:A0A0G2K047}.
Interaction partners:
- Propionyl-CoA carboxylase alpha chain, mitochondrial
- Peroxisomal acyl-coenzyme A oxidase 1
- Ethylmalonyl-CoA decarboxylase
- Propionyl-CoA carboxylase beta chain, mitochondrial
- Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- Peroxisomal acyl-coenzyme A oxidase 3
- Acetyl-coenzyme A synthetase, cytoplasmic
- Acetyl-coenzyme A synthetase 2-like, mitochondrial
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
Sequence:
MKPSWLQCRKVTGAGTLGAPLPGSPSVRGAAVTRRALVAGFGGRGCRALTTGSGGEYKTHFAASVADPERFWGKAAEQISWYKPWTKTLESRYPPSTSWFVEGMLNICYNAIDRHIENGQGDKIAIIYDSPVTDTKATISYKEVLEQVSKLAGVLVKQGVKKGDTVVIYMPMIPQAIYTMLACARIGAIHSLIFGGFASKELSTRIDHAKPKVVVTASFGIEPGRKVEYIPLLEEALRIGQHRPDRVLIYSRPNMEKVPLMSGRDLDWEEEMAKAQSHDCVPVLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALGKQYSLTRFKTLFVAGERCDVETLEWSKKVFRVPVLDHWWQTETGSPITASCIGLGNSKTPPPGQAGKCVPGYNVMILDDNMQKLKARSLGNIVVKLPLPPGAFSGLWKNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESVLSHGTVADCAVVGKEDPLKGHVPLALCVLKKDVNASEEQVLEEIVKHVRQSIGPVAAFRNAVFVKQLPKTRSGKIPRSTLSALVNGKPYKVTPTIEDPSIFGHIEEVLKQAV
Protein: Putative indole-3-acetic acid-amido synthetase GH3.10 (EC 6.3.2.-) (Auxin-responsive GH3-like protein 10) (OsGH3-10) (Q6ZLA7)
Organism: Oryza sativa subsp. japonica (Rice)
Function: May catalyze the synthesis of indole-3-acetic acid (IAA)-amino acid conjugates, providing a mechanism for the plant to cope with the presence of excess auxin.
Interaction partners:
Sequence:
MAAKGISTIGAASRSLSSSLMAAAKEPDVENLRLIEELTSNVDAVQERVLAEILGRNADAEYLDKCGLDASDTDRATFRAKVPVASYDDLKPYVKRIANGDRSPILSTHPIIEFFTSSGTSAGERKLMPIVTDEMARREVLSSLATSVLNVYVPGLHTGKGLYFLFARSETKTPGGLTAQPALTSVYKSEHFKRAYAYTSPMAAILCEDASQSMYAQMLCGLCQRHDVLRVGAVFAAALVRAIRFLQLNWAQLAADIETGELNPRVTDPSDRECSRGDWTGIVTRLWPKTKCLNVVVTGVMAQYIPTLQYYSGGLPIVSGMYASSECFFGLNLRPLCGPSEVSYTIMPNTAYFEFLPVGEAVDASNLVELARVEDGREYEVVVTTYAGLNRYRVGDVLCVTGFHNAAPQFRFVRRQSVLLSIEADKTDEAELQRAVERASSALLRPRGASIVEYTSRACTERVPGHFSPALPHWTLAP
Protein: O-acyltransferase (Q59Z52)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|PIRNR:PIRNR000439}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|PIRNR:PIRNR000439}.
Interaction partners:
- Phospholipid:diacylglycerol acyltransferase
- diacylglycerol O-acyltransferase
- Lysophospholipid acyltransferase
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- Lysophosphatidic acid acyltransferase
Sequence:
MGRTNTSDQLNAISDKNTKRKSLALDNEYHNNSSSEDDSSKIELSYTIPDNNNIISQETTTSVEDVLSVSSAPQNELRLRKQKSNNQDSPVDLNGVIVDVSKREKIFLKRKRQIDNKHGSDKSKYLSRFNDITFKAKSSTIFESDEFYKTDFFGMYVLFWLATAFAMVNNLIHTYFENSTPILQWTVVKVFKRDLFKVGLVDLAMYLSTYFAFFVQYACKNGYLSWKKVGWWLQAAFDGLFLFFWLWIASEYCLDFPWIAKVFLVLHSLVFIMKMHSYAFYNGYLWSIYKEGLYSEKYLDKLTNGKVTLPKGHTKNETEKVLQESIAFTKYELEYQSHATTENPDDHHVFDIDQTDKSIAKLQQEGLIKFPQNITLFNYFEYSMFPTLVYTLNFPRTKRIRWSYVFGKTFGIFGLIFLMILIAENNLYPIVLRCEIARKLPVSERIPQYFFLLMDMIPPFLMVYLFTFFLIWDAILNAIAELSKFADRDFYGPWWSCTDFSEFANQWNRCVHKFLLRHVYHSSISAFDVNKQSAAIITFLLSSLVHELVMYVIFGTLRGYLLLFQMSQIPLIIMSRSKFMKDKKVLGNIICWFGFISGPSIICTLYLVF
Protein: Cytochrome P450 monooxygenase PikC (EC 1.14.15.33) (Cytochrome P450 monooxygenase PicK) (Narbomycin C-12 hydroxylase) (Pikromycin synthase CYP107L1) (O87605)
Organism: Streptomyces venezuelae
Function: Catalyzes the hydroxylation of narbomycin to give rise to pikromycin, and of 10-deoxymethymycin (YC-17) to give rise to methymycin and neomethymycin during macrolide antibiotic biosynthesis. In addition, produces low amounts of neopicromycin, novapikromycin and novamethymycin. Requires the participation of a ferredoxin and a ferredoxin reductase for the transfer of electrons from NADPH to the monooxygenase.
Interaction partners:
Sequence:
MRRTQQGTTASPPVLDLGALGQDFAADPYPTYARLRAEGPAHRVRTPEGDEVWLVVGYDRARAVLADPRFSKDWRNSTTPLTEAEAALNHNMLESDPPRHTRLRKLVAREFTMRRVELLRPRVQEIVDGLVDAMLAAPDGRADLMESLAWPLPITVISELLGVPEPDRAAFRVWTDAFVFPDDPAQAQTAMAEMSGYLSRLIDSKRGQDGEDLLSALVRTSDEDGSRLTSEELLGMAHILLVAGHETTVNLIANGMYALLSHPDQLAALRADMTLLDGAVEEMLRYEGPVESATYRFPVEPVDLDGTVIPAGDTVLVVLADAHRTPERFPDPHRFDIRRDTAGHLAFGHGIHFCIGAPLARLEARIAVRALLERCPDLALDVSPGELVWYPNPMIRGLKALPIRWRRGREAGRRTG
Protein: Cytochrome c oxidase assembly protein COX11, mitochondrial (Q9Y6N1)
Organism: Homo sapiens (Human)
Function: Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:15229189, ECO:0000269|PubMed:9878253}; Single-pass membrane protein {ECO:0000269|PubMed:9878253}; Intermembrane side {ECO:0000269|PubMed:9878253}.
Interaction partners:
- Protoheme IX farnesyltransferase, mitochondrial
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit 3
- Cytochrome c oxidase subunit 1
- Protein SCO1 homolog
- Cytochrome c oxidase copper chaperone
- Heme A synthase COX15
- Protein SCO2 homolog
- Surfeit locus protein 1
- Cytochrome c oxidase assembly protein COX19
Sequence:
MGGLWRPGWRCVPFCGWRWIHPGSPTRAAERVEPFLRPEWSGTGGAERGLRWLGTWKRCSLRARHPALQPPRRPKSSNPFTRAQEEERRRQNKTTLTYVAAVAVGMLGASYAAVPLYRLYCQTTGLGGSAVAGHASDKIENMVPVKDRIIKISFNADVHASLQWNFRPQQTEIYVVPGETALAFYRAKNPTDKPVIGISTYNIVPFEAGQYFNKIQCFCFEEQRLNPQEEVDMPVFFYIDPEFAEDPRMIKVDLITLSYTFFEAKEGHKLPVPGYN
Protein: 4-hydroxybenzoate polyprenyltransferase, mitochondrial (4-HB polyprenyltransferase) (EC 2.5.1.39) (Para-hydroxybenzoate--polyprenyltransferase) (PHB:PPT) (PHB:polyprenyltransferase) (Q66JT7)
Organism: Mus musculus (Mouse)
Function: Mediates the second step in the final reaction sequence of coenzyme Q (CoQ) biosynthesis. Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl donor (such as all-trans-nonaprenyl diphosphate). The length of the polyprenyl side chain varies depending on the species, in humans, the side chain is comprised of 10 isoprenyls producing CoQ10 (also known as ubiquinone), whereas rodents predominantly generate CoQ9. However, this specificity is not complete, human tissues have low amounts of CoQ9 and rodent organs contain some CoQ10 (By similarity). Plays a central role in the biosynthesis of CoQ9. CoQ9 is a vital molecule that transports electrons from mitochondrial respiratory chain complexes. CoQs also function as cofactors for uncoupling protein and play a role as regulators of the extracellularly-induced ceramide-dependent apoptotic pathway (By similarity). Regulates mitochondrial permeability transition pore (mPTP) opening and ROS production (pivotal events in cell death) in a tissue specific manner (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03189}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03189}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03189}.
Interaction partners:
- All trans-polyprenyl-diphosphate synthase PDSS2
- All trans-polyprenyl-diphosphate synthase PDSS1
- Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial
- 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- Ubiquinone biosynthesis protein COQ9
- Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial
- NADPH-dependent 3-demethoxyubiquinone 3-hydroxylase, mitochondrial
- Atypical kinase COQ8A, mitochondrial
- Atypical kinase COQ8B, mitochondrial
Sequence:
MLRWGGAGLARGLRAVRSAWLRGPRGLPLALVRSAGVPGARDRRAPAPGTQRGRALSLSAAAVVNSAPRPLQPYLRLMRLDKPIGTWLLYLPCTWSIGLAADPGCFPDWYMLSLFGTGAILMRGAGCTINDMWDRDFDKKVTRTANRPIAAGDISTFQSFVFLGGQLTLALGVLLCLNYYSIAMGAASLLLVVTYPLVKRITFWPQLALGLTFNWGALLGWSAVKGSCDPAVCLPLYFSGVMWTLIYDTIYAHQDKKDDALIGLKSTALLFQENTRQWLSGFGVAMVAALSLAGANNGQTVPYYAAVAAVGAHLAHQIYTVDIHRAEDCWDKFTSNRTVGMLLFLGIVLGNLCKEKTEEAKDAEAVRVGSEQTS
Protein: RE05274p (Sosie, isoform A) (Q9VC30)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uroporphyrinogen decarboxylase
- Protoporphyrinogen oxidase
- Uncharacterized protein
- DUF2428 domain-containing protein
- Frataxin homolog, mitochondrial
Sequence:
MQPLKRFTQCGSLTMLFGIFIILFGVSSTALTTFGKTNNQPPPTHVPIVKGRECSAHDDCTAIDRTSCVKDPNDYKLRCLCGDDSPPSAGSCPDVLKGLRHKCNSNNDCEDGMVCQYENSNRTIGVAKFMSSKTKLCLCDNDNGYVEDILHDICSGANLQGLVSFLVSICSLLAPFLVSAHMRKHF
Protein: L-cysteine desulfhydrase (EC 4.4.1.28) (AtL-CDes1) (L-CDes1) (AtLCD) (Q9M1R1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the production of hydrogen sulfide (H2S) from cysteine. Is mainly responsible for the degradation of cysteine to generate H2S, a regulator of stomatal movement and closure.
Interaction partners:
- Bifunctional cystathionine gamma-lyase/cysteine synthase
- Bifunctional D-cysteine desulfhydrase/1-aminocyclopropane-1-carboxylate deaminase, mitochondrial
- D-cysteine desulfhydrase 2, mitochondrial
- Cysteine synthase 1
- Putative inactive cysteine synthase 2
- Bifunctional L-3-cyanoalanine synthase/cysteine synthase C1, mitochondrial
- Cysteine synthase, mitochondrial
- Cysteine synthase, chloroplastic/chromoplastic
- Bifunctional L-3-cyanoalanine synthase/cysteine synthase D1
- Bifunctional L-3-cyanoalanine synthase/cysteine synthase D2
Sequence:
MEAGERRNGDSMSHNHRAPKKPRLAGLLTESDIDSEFAHHQTGVARINNGSFGCCPGSVLEAQREWQLRYLRQPDEFYFNGLRRGLLASRTVISDLINADDVDEVSLVDNATTAAAIVLQKVGRCFSEGKYKKEDTVVMFHCAFQSVKKSIQAYVSRVGGSTVEVRLPFPVNSNEEIISKFREGLEKGRANGRTVRLAIIDHITSMPCVLMPVRELVKICREEGVEQVFVDAAHAIGSVKVDVKEIGADYYVSNLHKWFFCPPSIAFFYCKKRGSESDVHHPVVSHEFGNGLPIESAWIGTRDYSSQLVVPSVMEFVNRFEGGMEGIMMKNHDEAVRMGLMLADAWGTNLGSPPEMCVGMVMIGLPSKLCVGSDEDAIKLRSYLRVHYSVEVPVFYLGLRDGEEGVKDKDSGLITAYVRISHQVYNKTEDYERLRDAITELVKDQMTCQNLPAL
Protein: Ret finger protein-like 1 (RING finger protein 78) (O75677)
Organism: Homo sapiens (Human)
Function: Negatively regulates the G2-M phase transition, possibly by promoting cyclin B1/CCNB1 and CDK1 proteasomal degradation and thereby preventing their accumulation during interphase.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20725088}. Nucleus {ECO:0000269|PubMed:20725088}. Note=A higher concentration is observed in the cytoplasm compared to the nucleus. {ECO:0000269|PubMed:20725088}.
Interaction partners:
- Paired box protein Pax-6
Sequence:
MKRLSLVTTNRLSPHGNFLPLCTFPLAVDMAALFQEASSCPVCSDYLEKPMSLECGCAVCFKCINSLQKEPHGEDLLCCCCSMVSQKNKIRPSWQLERLASHIKELEPKLKKILQMNPRMRKFQVDMTLDADTANNFLLISDDLRSVRSGCITQNRQDLAERFDVSICILGSPRFTCGRHYWEVDVGTSTEWDLGVCRESVHRKGRIHLTTERGFWTVSLRDGSRLSASTVPLTFLFVDRKLQRVGIFLDMGMQNVSFFDAEGGSHVYTFRSVSAEEPLHLFFAPPSPPNGDKSVLSICPVINPGTTDAPVHPGEAK
Protein: Trefoil factor 1 (Breast cancer estrogen-inducible protein) (PNR-2) (Polypeptide P1.A) (hP1.A) (Protein pS2) (P04155)
Organism: Homo sapiens (Human)
Function: Stabilizer of the mucous gel overlying the gastrointestinal mucosa that provides a physical barrier against various noxious agents. May inhibit the growth of calcium oxalate crystals in urine.
Subcellular location: Secreted {ECO:0000269|PubMed:15924415, ECO:0000269|PubMed:3041593}.
Interaction partners:
- Estrogen receptor
- Protein GREB1
- Hepatocyte nuclear factor 3-alpha
- Gastrokine-2
- Mucin-5AC
- Nuclear receptor coactivator 3
- Trefoil factor 3
- Anterior gradient protein 2 homolog
- Trans-acting T-cell-specific transcription factor GATA-3
- Progesterone receptor
Sequence:
MATMENKVICALVLVSMLALGTLAEAQTETCTVAPRERQNCGFPGVTPSQCANKGCCFDDTVRGVPWCFYPNTIDVPPEEECEF
Protein: Rehydrin (P73348)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
- Thioredoxin
- Peroxiredoxin sll1621
- Thioredoxin-like protein slr1139
- Thioredoxin-like protein slr0233
- Slr0600 protein
- GTPase HflX
- Sll0685 protein
- Thiol:disulfide interchange protein TxlA homolog
- Thylakoid membrane protein slr1796
- Lactose transport system permease protein LacF
Sequence:
MALQLGDVVPDFTQESSQGPISFHEWAGDSWVVLFSHPADYTPVCTTELGTVAKLKPEFDKRNVKVIALSVDDVESHKGWICDIDETQNTTVNYPILADGDKKVSDLYGMIHPNALNNLTVRSVFIIDPAKKLRLTFTYPASTGRNFDEILRVIDSLQLTDYHQVATPANWQDGDKCVVVPSISTEDAKVKFPKGVEEIKPYLRLTPQPNK
Protein: Protein NIS1 (Jumonji domain-interacting protein 1) (Neck protein interacting with septins protein 1) (P53939)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be involved in a mitotic signaling network. Binds sumoylated proteins and may stabilize SUMO chains.
Subcellular location: Bud neck {ECO:0000269|PubMed:11817649}. Cytoplasm, cell cortex {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Nucleosome assembly protein
- Protein NBA1
- Altered inheritance of mitochondria protein 44
- Ubiquitin-like protein SMT3
- Bud site selection protein RAX1
Sequence:
METYETSIGTQSYPPTLFPPPLGTGGFTTSGYIHALVDSTSNSNSNSNTNSNTNSNTNSNSDTKIPIVQISDDSHITHDSFKPYMEYHDASHLRNRNISKADQVESTEVMEQFTQWSNYKMRSRSPTINAKPIRHTSQRRTDFTSKNELSKFSKNHNFIFHKGFLKRQHSIRREDRQAKVRSRFRSKKELTSVLNYIELEQMDIANVLASQPVNLHAIRNLTSRDPAVTPIPFLRSQMYATSSRPPYLRNRSISRKLPKSQPGSLPTTMPATATKTIKQNSTTPTTRSVYNKNVGRSNTSPSVLYHPKRRGKLNTKSHARKEQLLLELWREYLMLVITQRTQLRLTLLCSPGSASNESSVCSSNASDLDMSLLSTPSSLFQMAGETKSNPIIIPDSQDDSILSSDPF
Protein: Protein RER1 (C8V3K9)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MDVPEPEQTPFTAVSAQTSKLARQYQTYLDASTPFTAYRWIGTAVLLFIFFLRIILAQGWYIVAYTVGIYLLNLFLLFLQPKFDPSLTQDEGLEDGDAGAPSLPTKQDDEFRPFIRRLPEFKFWHSATRALAIGFLCTWFSVFDIPVFWPVLVVYWILLFVLTMRRQIQHMIKYRYVPFSFGKARYGRS
Protein: Monothiol glutaredoxin-S8 (AtGrxS8) (Protein ROXY 15) (O23417)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May only reduce GSH-thiol disulfides, but not protein disulfides.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MEKIQKMISEKSVVIFSNNSCCMSHTIKTLFLDLGVNPTIYELDEINRGKEIEYALAQLGCSPTVPVVFIGGQLVGGANQVMSLHLNRSLIPMLKRFGALWL