wanglab/gogpt-training-data huggingface dataset:
Protein: Cytochrome c oxidase subunit 1 (EC 7.1.1.9) (Cytochrome c oxidase polypeptide I) (Q9MIY8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00396}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P00396}.
Interaction partners:
- NADH-ubiquinone oxidoreductase chain 4
- NADH-ubiquinone oxidoreductase chain 5
- NADH-ubiquinone oxidoreductase chain 4L
- NADH-ubiquinone oxidoreductase chain 2
- NADH-ubiquinone oxidoreductase chain 6
- Cytochrome b
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- NADH-ubiquinone oxidoreductase chain 1
Sequence:
MTITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPILIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTTINMKPPTISQYQTPLFVWAVLVTAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYAGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGAIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGYTLNSVWTKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYALWNTVSSIGSLISLVAVIMFLFILWEAFTAKREVLSVELTATNVEWLHGCPPPYHTFEEPAFVQIQSN
Protein: Nucleoporin 98-96 (Q86G43)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
SKYGLGDSDEEDELPTDPKKAKIATLEAQQRANAEKMTLNSLRQAQKISEDAARNLDPKALVAGVASGFRPMDDTAEFLLMDKTQFFQAGGNSDFSMFDPPRQRPTITSPTAVLAQEMVGNEAHKMQLMKSSFFVEDNAPEDEPMETTGRLLRHRKFFNVEPLVWKDGASESSSQYDFEHPSPALPISSSGSEASLMCDAHXXETSSMATGSIVAAVKETKFEMPVTKAFKFVCKPKVAPIKLRATTVPLPRSIAYEMRDNWIADLGFYKGRSFKLSFGPQNSLVLPSTYNNMQNLKEFTGPSLPVSMVFAPRSATDLSPSVMQLVEFNMVKGNEGFRESIIPHLEVQLNDCLSVNVEGSECPCIHPDSGTKLISKHFSESLKQRNAGLKEDYSVSVWSLLFALWGDHDELVDLEKNSHYMVMCRRNLLSEWLENTLLGKDLLSKKVSTHSYLEHMLDLLSCHRVNEACELAFSYDDANLALVLSQLSSGAVFRLLMEEQLFAWQQSKSDKYIDLERLKMYMLAAGAPMMQSSHGAINLLENKNWLTALALQLWYFTAPTSSITDALNAYNDAFQAEECYAEPPKPSYRDAPIDTKKPVYDLRYHLLQLHSKRMHSLEETLNPITHTADAMDFRLSWLLLQTLRALGYRHCSPLTEARLSVDFASQLENEGLWQWGIFVLLHIKQQTQRERAVQQMLQRNVSVSAKVALYAEERFIVEELGIPMSWVDYAKAVKAGASGKHHLQAKYLLKAKHFATAHDVIFQHIAPDAIINGKMKYLHSLLIQFEDTEGSSIRVPNWANQGQIFLDFIDISAKFKQIRSVTNIADINARWENLKPQLSELCSRISLLPCPTSKHRLCQSEISQSLSCLVHGMCIVCPEMESSTVLKVALERLPLPQEFASKELRIWLEELLDKIQNEPPFSERQQPTMMEI
Protein: Adenylate dimethylallyltransferase (EC 2.5.1.27) (Dimethylallyl transferase) (Isopentenyl transferase) (Trans-zeatin producing protein) (P58758)
Organism: Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
Function: Transfers dimethylallyl groups to AMP as part of the biosynthesis of cytokinin phytohormones.
Interaction partners:
Sequence:
MLLHLIYGPTCSGKTDMAIQIAQETGWPVVALDRVQCCPQIATGSGRPLESELQSTRRIYLDSRPLTEGILDAESAHRRLIFEVDWRKSEEGLILEGGSISLLNCMAKSPFWRSGFQWHVKRLRLGDSDAFLTRAKQRVAEMFAIREDRPSLLEELAELWNYPAARPILEDIDGYRCAIRFARKHDLAISQLPNIDAGRHVELIEAIANEYLEHALSQERDFPQWPEDGAGQPVCPVTLTRIR
Protein: Methyltransferase (P71873)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MMLDRLRQGGYWLVRGKINLIDRAFTSCRIESFADLGAVWGVEGAYTFRALDKYPVKEAVLVDGRITPTVAARANSYPQLRVIEGNFGDQEIADKVGNVDALFLFDVLLHQVSPDWDTILDMYAKNVRCLLIYNQQWIGSTTTVRLLDLGEKHYFRNVPHSKLNKAYRDLFQKLDKKHPDHDKPWRDIPDIWQWGITDADLESKASELGFKLLYKEDCRGFGWLPNIQNRAFLFARQ
Protein: Sterile alpha motif domain containing 8 (Q5JSC9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAGPNQLCIRRWTTKHVAVWLKDEGFFEYVDILCNKHRLDGITLLTLTEYDLRSPPLEIKVLGDIKRLMLSVRKLQKIHIDVLEEMGYNSDSPMGSMTPFISALQSTDWLCNGELSHDCDGPITDLNSDQYQYMNGKNKHSVRRLDPEYWKTILSCIYVFIVFGFTSFIMVIVHERVPDMQTYPPLPDIFLDSVPRIPWAFAMTEVCGMILCYIWLLVLLLHKHRSILLRRLCSLMGTVFLLRCFTMFVTSLS
Protein: Complement C1r subcomponent-like protein (C1r-LP) (C1r-like protein) (EC 3.4.21.-) (C1r-like serine protease analog protein) (CLSPa) (Q9NZP8)
Organism: Homo sapiens (Human)
Function: Mediates the proteolytic cleavage of HP/haptoglobin in the endoplasmic reticulum.
Subcellular location: Secreted {ECO:0000269|PubMed:15358180}.
Interaction partners:
- Scavenger receptor cysteine-rich type 1 protein M130
Sequence:
MPGPRVWGKYLWRSPHSKGCPGAMWWLLLWGVLQACPTRGSVLLAQELPQQLTSPGYPEPYGKGQESSTDIKAPEGFAVRLVFQDFDLEPSQDCAGDSVTISFVGSDPSQFCGQQGSPLGRPPGQREFVSSGRSLRLTFRTQPSSENKTAHLHKGFLALYQTVAVNYSQPISEASRGSEAINAPGDNPAKVQNHCQEPYYQAAAAGALTCATPGTWKDRQDGEEVLQCMPVCGRPVTPIAQNQTTLGSSRAKLGNFPWQAFTSIHGRGGGALLGDRWILTAAHTIYPKDSVSLRKNQSVNVFLGHTAIDEMLKLGNHPVHRVVVHPDYRQNESHNFSGDIALLELQHSIPLGPNVLPVCLPDNETLYRSGLLGYVSGFGMEMGWLTTELKYSRLPVAPREACNAWLQKRQRPEVFSDNMFCVGDETQRHSVCQGDSGSVYVVWDNHAHHWVATGIVSWGIGCGEGYDFYTKVLSYVDWIKGVMNGKN
Protein: Ferredoxin--NADP reductase, leaf isozyme 1, chloroplastic (FNR) (EC 1.18.1.2) (Leaf FNR 1) (FNR-1) (Os-LFNR1) (P41344)
Organism: Oryza sativa subsp. japonica (Rice)
Function: May play a key role in regulating the relative amounts of cyclic and non-cyclic electron flow to meet the demands of the plant for ATP and reducing power.
Subcellular location: Plastid, chloroplast stroma {ECO:0000250|UniProtKB:Q9FKW6}. Plastid, chloroplast thylakoid membrane {ECO:0000250|UniProtKB:Q9FKW6}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9FKW6}; Stromal side {ECO:0000250|UniProtKB:Q9FKW6}. Note=In the vicinity of the photosystem I in the non-stacked and fringe portion of the membrane. {ECO:0000250|UniProtKB:Q9FKW6}.
Interaction partners:
- Protein TIC 62, chloroplastic
- Ferredoxin--NADP reductase, leaf isozyme 2, chloroplastic
- Probable 5'-adenylylsulfate reductase 1, chloroplastic
- Ferredoxin-1, chloroplastic
- Nitrate reductase
- Nitrate reductase 1
- Nitrate reductase
- Os05g0503300 protein.
- Ferredoxin--NADP reductase, embryo isozyme, chloroplastic
- Ferredoxin--NADP reductase, root isozyme, chloroplastic
Sequence:
MAAVTAAAVSTSAAAAVTKASPSPAHCFLPCPPRTRAAHQRGLLLRAQVSTTDAAAVAAAPAKKEKISKKHDEGVVTNKYRPKEPYVGKCLLNTKITADDAPGETWHMVFSTEGEIPYREGQSIGVIADGVDKNGKPHKLRLYSIASSALGDFGDSKTVSLCVKRLVYTNDQGEIVKGVCSNFLCDLKPGSDVKITGPVGKEMLMPKDPNANIIMLATGTGIAPFRSFLWKMFFEKYDDYKFNGLAWLFLGVPTSSSLLYKEEFDKMKAKAPENFRVDYAVSREQTNAQGEKMYIQTRMAEYKEELWELLKKDHTYVYMCGLKGMEKGIDDIMVSLAAKDGIDWADYKKQLKKGEQWNVEVY
Protein: Peroxisome proliferator-activated receptor delta (PPAR-delta) (Nuclear hormone receptor 1) (NUC1) (Nuclear receptor subfamily 1 group C member 2) (Peroxisome proliferator-activated receptor beta) (PPAR-beta) (P35396)
Organism: Mus musculus (Mouse)
Function: Ligand-activated transcription factor key mediator of energy metabolism in adipose tissues. Receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Has a preference for poly-unsaturated fatty acids, such as gamma-linoleic acid and eicosapentanoic acid. Once activated by a ligand, the receptor binds to promoter elements of target genes. Regulates the peroxisomal beta-oxidation pathway of fatty acids. Functions as transcription activator for the acyl-CoA oxidase gene. Decreases expression of NPC1L1 once activated by a ligand (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:35675826}.
Interaction partners:
- Retinoic acid receptor RXR-alpha
- Fatty acid-binding protein 5
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Nuclear receptor corepressor 1
- Retinoic acid receptor RXR-beta
- Nuclear receptor corepressor 2
- Retinoic acid receptor RXR-gamma
- Peroxisome proliferator-activated receptor alpha
- Peroxisome proliferator-activated receptor gamma
- Nuclear receptor coactivator 1
Sequence:
MEQPQEETPEAREEEKEEVAMGDGAPELNGGPEHTLPSSSCADLSQNSSPSSLLDQLQMGCDGASGGSLNMECRVCGDKASGFHYGVHACEGCKGFFRRTIRMKLEYEKCDRICKIQKKNRNKCQYCRFQKCLALGMSHNAIRFGRMPEAEKRKLVAGLTASEGCQHNPQLADLKAFSKHIYNAYLKNFNMTKKKARSILTGKSSHNAPFVIHDIETLWQAEKGLVWKQLVNGLPPYNEISVHVFYRCQSTTVETVRELTEFAKNIPNFSSLFLNDQVTLLKYGVHEAIFAMLASIVNKDGLLVANGSGFVTHEFLRSLRKPFSDIIEPKFEFAVKFNALELDDSDLALFIAAIILCGDRPGLMNVPQVEAIQDTILRALEFHLQVNHPDSQYLFPKLLQKMADLRQLVTEHAQMMQWLKKTESETLLHPLLQEIYKDMY
Protein: MAX dimerization protein MGA a (F1R7N7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00201}.
Interaction partners:
Sequence:
MADTEKQGAMVLHEEGVTAPTLAPPTTTPPSIFVVLKQLQSSDSGNDKANLMAISEANKMGKSSIGTTVAGIQPTSSTFADTNSTTPSENLPADARCRGITVTLDNNNMWNEFHRCKTEMILTKQGRRMFPYCRFRLSGMEPFQNYVLAMDIKPADNCRYKWSGKGWEPNGKAEPHISRLFVHPESPASGLHWMQYPVSFYRLKLCNTLDQEGHIILHSMHRYLPQIHIIPADKVSKDILILDRPNVVTLSFAQTEFFAVTAYQNLCITQLKIDYNPFAKGFREDAVNARSSKAKNGLSTDETESELKLSKEMTTLNNLKTLFMKRKASVKVNVNQNVPNPTNGENKVVNGAAPAVDTNVQSLCNKKRPSSLAFSDFIKGAHVKVKRLSLENINKTGGATEPSTACTSKQKEAADISSITENSLQVDQKDGNGAGDVLRCESTDTSLKTGVLKANEIKKEIDEHSADKNTLKSSDQNLSCSDEKKMETVSSLSTEAKPEAQMKKTLPHKRPERVPLPLLAKFLKQRRPILPKPVSHSSLSDSEKSCEPAQTSESSSVLMSFVPCVTTNLDSQPAVTSLSQTVTSSTTDANNMTSLSTTLSYSSTTVPLIPSETQLCDRFSASPVGSDPFSAPNTTSPSKPNSNPALDISNNTDAIFTPDHDNTLRSQSDISSDSTCDVVHDSCPPTVNTDTVETPVVPSPTSVFDVPSSTDNDMNSYQDINSMPDVAEGDSISDCLLDSSTGSCPEFFSEEIPQNTLFTNEESLSLPLDDASSPAFSLPSPAPSSPDPFPPSLFCDRPVPPRKALDSFPERLLDCTAASARDPFPLGFFNDGREPPRQIFDLPERPLIGTVASRESLSSSVNNGPEHPMETGDLFSQSHCPDRANSLNDLESAASCETAVSDNSISKPTKPSPHGSSCKKYKGKQKKVGMLKLGEDSEVFDGPVPVPLQPSLEDVEGQLFVSFMSKKALRIHLGDDDDDKPETAQENTDNPDGNNEEKIEKKIEGLEKVLLHDLKFMKNRQVIHPVLQEVGLKLNLLDVTLEIDLQYLGVQLPIPPPALSPEETSSQAQFVSRTGKTSDFTQIKGWRDKFAPSASLSEGVSSTDAGQSNLSAFCSDMLDEYLASEGKLIDERAASLSQADCTPVAYQLPTKSTSYVRTLDSVLKKQVPAILTPTTNKVKPTFKSKVENKSKKPLKPGKGKQTKPVISDAKPLCTKKPQQNKKYKSRKEFKSPEKPDVAEVPASNTTPMAEDSGSTSSTCAGGRSPGLPKTLVKLLDVEDGAVWEGRHRSYITEERAAIALATLVTAEGASTGSADAIRIIRRRAPPCLNVFCRLGCVCASLVHLRRHHHCGKPQCMLGCSCLRRKVVALKTPKQEEGTADDSDPQGMSEENKAKWRKKNKMRKTYVLTDPEIAPEPAKRVSTLWDRTRGNFDKEVLYCPPPPRSPQPQLLSQELQHDLESFLSPSKQKRVEERNLSTSEDNIEINLTCARSRPFHSNCHDKPKADDNKHHISQVSTPDIEEGELVPLNLSGPAKRLEMMSECTWTSIDMRNNVMRIVCEHMAQDRLNQPFWIGKYFIKPVSKTLEEEENGSVEIYKVIISQPMEKKTENEKVTQKEEELEKHVKTSEVKGLPFLSKCCPAGLLKAEKKSPDAPGQIMVNGKHYPQAKLELGHMGALHPANRLAAYITGRICPTVSAITKPPVTTVPSSTLTTVSKVTCTPASTTTSVSKSLGGSTLTTTTSASSPGLTSPAKKTVYITVASRNTGLSNSGTQIKKIVSPTGPPQTSGQKMLLQVVKTADGNTLYRNPNGQLMQLVPLSQIKALKPNLLSQGQPTIIRLPAPPTVSMNKPQGGSATIVTSSIPTTQTLAKPSGTVPVSTSSSMGGKLISPPSSKSVSLSSLPSTLKVVQGFLGQSGTCTLRILPPTTSTSSTVLSQSGLTLLKSASSMPPTQDSSNSETNVSFSSQSTEKTVVQVLKQSTIDPAKQNSSDNANVKEKHFNKAPDPEEKEIGSDSTELTDDSDLYSDDDQEDASCMSASDREEKIEDTDGMDSEKKGYAEMVVDIETIEESAEQNRIAKFRASALRRNQYRRNQKRIHDEMLEVRVQKVRKERKRRQTLSECFIKLQGTLGMSSKKFEVSRMRILTKANKEVEYLVKLEDYLVEKKAKLQFKKERYIQTLSQLCDKSTESIGLKLNEIISKQKALEAQSKTKETHPKPIQAKSKAKPKPKSKPKSKVVDVCDKPKGLAVQNKVNDVSKVTYSPSKPIDLSIKKQKSPEMTESVPKSTPSVSVPADLDGNKNTLNVLDTNTVTTTSTPIQPSFNSTLVMKPVSIPSPIKHPPITRERMRPNILSRASSQAMQGSPVKESLLTNVCIPQVLPLMNTMVPCNQIITINNSLQPIGITSVGQQSSTPGVASVSIVPTISHPLRVENTLPMLHPQFIKITNSPVNINTKVDSASLPNISNVISLAENLVVPRKVVEDKPVFQAQPTSVDNQQNSSNDKIPDLEQKTDEAPSTNVPKQSVVEDQKGASVPKSNPEVPENKSPDDSDDPEDENLLSLLDELVLLSQQLTNEDEDERIAVPGDVQSCSDKPEDQEPADDRALSPLFLTLDEDLMSPDSKDEIDIPPKVDDLVKVIFGSDSPSVSSESGVAQSTNASSPHASTCNATGDGLTPPPLLHMKAAYEAASGQSANEGTSVTWRPMPKLVPLGLKAQDAGKVINPSIPNLDSSEQDTPQM
Protein: Inactive tyrosine-protein kinase PRAG1 (PEAK1-related kinase-activating pseudokinase 1) (Pragmin) (Sugen kinase 223) (SgK223) (Q86YV5)
Organism: Homo sapiens (Human)
Function: Catalytically inactive protein kinase that acts as a scaffold protein. Functions as an effector of the small GTPase RND2, which stimulates RhoA activity and inhibits NGF-induced neurite outgrowth (By similarity). Promotes Src family kinase (SFK) signaling by regulating the subcellular localization of CSK, a negative regulator of these kinases, leading to the regulation of cell morphology and motility by a CSK-dependent mechanism (By similarity). Acts as a critical coactivator of Notch signaling (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:D3ZMK9}. Cell junction, focal adhesion {ECO:0000269|PubMed:27116701}. Nucleus {ECO:0000250|UniProtKB:Q571I4}. Note=Colocalized with NOTCH1 in the nucleus. {ECO:0000250|UniProtKB:Q571I4}.
Interaction partners:
- Tyrosine-protein kinase CSK
- Rho-related GTP-binding protein RhoN
Sequence:
MHQTLCLNPESLKMSACSDFVEHIWKPGSCKNCFCLRSDHQLVAGPPQPRAGSLPPPPRLPPRPENCRLEDEGVNSSPYSKPTIAVKPTMMSSEASDVWTEANLSAEVSQVIWRRAPGKLPLPKQEDAPVVYLGSFRGVQKPAGPSTSPDGNSRCPPAYTMVGLHNLEPRGERNIAFHPVSFPEEKAVHKEKPSFPYQDRPSTQESFRQKLAAFAGTTSGCHQGPGPLRESLPSEDDSDQRCSPSGDSEGGEYCSILDCCPGSPVAKAASQTAGSRGRHGGRDCSPTCWEQGKCSGPAEQEKRGPSFPKECCSQGPTAHPSCLGPKKLSLTSEAAISSDGLSCGSGSGSGSGASSPFVPHLESDYCSLMKEPAPEKQQDPGCPGVTPSRCLGLTGEPQPPAHPREATQPEPIYAESTKRKKAAPVPSKSQAKIEHAAAAQGQGQVCTGNAWAQKAASGWGRDSPDPTPQVSATITVMAAHPEEDHRTIYLSSPDSAVGVQWPRGPVSQNSEVGEEETSAGQGLSSRESHAHSASESKPKERPAIPPKLSKSSPVGSPVSPSAGGPPVSPLADLSDGSSGGSSIGPQPPSQGPADPAPSCRTNGVAISDPSRCPQPAASSASEQRRPRFQAGTWSRQCRIEEEEEVEQELLSHSWGRETKNGPTDHSNSTTWHRLHPTDGSSGQNSKVGTGMSKSASFAFEFPKDRSGIETFSPPPPPPKSRHLLKMNKSSSDLEKVSQGSAESLSPSFRGVHVSFTTGSTDSLASDSRTCSDGGPSSELAHSPTNSGKKLFAPVPFPSGSTEDVSPSGPQQPPPLPQKKIVSRAASSPDGFFWTQGSPKPGTASPKLNLSHSETNVHDESHFSYSLSPGNRHHPVFSSSDPLEKAFKGSGHWLPAAGLAGNRGGCGSPGLQCKGAPSASSSQLSVSSQASTGSTQLQLHGLLSNISSKEGTYAKLGGLYTQSLARLVAKCEDLFMGGQKKELHFNENNWSLFKLTCNKPCCDSGDAIYYCATCSEDPGSTYAVKICKAPEPKTVSYCSPSVPVHFNIQQDCGHFVASVPSSMLSSPDAPKDPVPALPTHPPAQEQDCVVVITREVPHQTASDFVRDSAASHQAEPEAYERRVCFLLLQLCNGLEHLKEHGIIHRDLCLENLLLVHCTLQAGPGPAPAPAPAPAPAAAAPPCSSAAPPAGGTLSPAAGPASPEGPREKQLPRLIISNFLKAKQKPGGTPNLQQKKSQARLAPEIVSASQYRKFDEFQTGILIYELLHQPNPFEVRAQLRERDYRQEDLPPLPALSLYSPGLQQLAHLLLEADPIKRIRIGEAKRVLQCLLWGPRRELVQQPGTSEEALCGTLHNWIDMKRALMMMKFAEKAVDRRRGVELEDWLCCQYLASAEPGALLQSLKLLQLL
Protein: Nicotinate phosphoribosyltransferase (NAPRTase) (EC 6.3.4.21) (FHA-HIT-interacting protein) (Nicotinate phosphoribosyltransferase domain-containing protein 1) (Q6XQN6)
Organism: Homo sapiens (Human)
Function: Catalyzes the first step in the biosynthesis of NAD from nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate. Helps prevent cellular oxidative stress via its role in NAD biosynthesis.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:17604275}.
Interaction partners:
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
- Nicotinamide riboside kinase 1
- Nicotinamide riboside kinase 2
- Nicotinamide phosphoribosyltransferase
- Purine nucleoside phosphorylase
- NAD-capped RNA hydrolase NUDT12
- Cytosolic 5'-nucleotidase 1A
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
Sequence:
MAAEQDPEARAAARPLLTDLYQATMALGYWRAGRARDAAEFELFFRRCPFGGAFALAAGLRDCVRFLRAFRLRDADVQFLASVLPPDTDPAFFEHLRALDCSEVTVRALPEGSLAFPGVPLLQVSGPLLVVQLLETPLLCLVSYASLVATNAARLRLIAGPEKRLLEMGLRRAQGPDGGLTASTYSYLGGFDSSSNVLAGQLRGVPVAGTLAHSFVTSFSGSEVPPDPMLAPAAGEGPGVDLAAKAQVWLEQVCAHLGLGVQEPHPGERAAFVAYALAFPRAFQGLLDTYSVWRSGLPNFLAVALALGELGYRAVGVRLDSGDLLQQAQEIRKVFRAAAAQFQVPWLESVLIVVSNNIDEEALARLAQEGSEVNVIGIGTSVVTCPQQPSLGGVYKLVAVGGQPRMKLTEDPEKQTLPGSKAAFRLLGSDGSPLMDMLQLAEEPVPQAGQELRVWPPGAQEPCTVRPAQVEPLLRLCLQQGQLCEPLPSLAESRALAQLSLSRLSPEHRRLRSPAQYQVVLSERLQALVNSLCAGQSP
Protein: GDSL esterase/lipase 22 (EC 3.1.1.-) (Extracellular lipase At1g54000) (GDSL esterase/lipase At1g54000) (Q1H583)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Jacalin-related lectin 33
- CASP-like protein 1A1
- Cytochrome b561 and DOMON domain-containing protein At4g17280
- Jacalin-related lectin 34
- Proline-tRNA ligase
- Cytochrome b561 and DOMON domain-containing protein At5g47530
- PYK10-binding protein 2
- Protein RALF-like 22
- Beta-glucosidase 23
- Jacalin-related lectin 35
Sequence:
MMANNCNLVSVLCVILVLTLFHNPITVAGQNSPVVALFTFGDSNFDAGNKQTLTKTLVAQGFWPYGKSRDDPNGKFSDGLITPDFLAKFMKIPLAIAPALQPNVNVSRGASFAVEGATLLGAPVESMTLNQQVKKFNQMKAANWNDDFVAKSVFMIYIGANDYLNFTKNNPTADASAQQAFVTSVTNKLKNDISALYSSGASKFVIQTLAPLGCLPIVRQEYNTGMDQCYEKLNDLAKQHNEKIGPMLNEMARNSPASAPFQFTVFDFYNAVLTRTQRNQNFRFFVTNASCCGVGSHDAYGCGLPNVHSKLCEYQRSFLFFDGRHNSEKAQEMFAHLLFGADTNVVQPMNVRELTVYPVDEPMREFWVPPTPATVHASDSSSSTSRGYEYY
Protein: Vps39 protein (Q5PQS9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MHDAFEPVPILEKLPLQIDCLAAWEEWLLVGTKQGHLLLYRIRKDVGCNRFEVTLEKSNKNFSKKIQQIHVVSQFKILVSLLENNIYVHDLLTFQQITTVSKAKGASLFTCDLQHTETGEEVLRMCVAVRKKLQLYFWKDREFHELQGDFSVPDVPKSMAWCENSICVGFKRDYYLIRVDAKGSIKELFPTGKQLEPLVAPLADGKVAVGQDDLTVVLNEEGICTQKCALNWTDIPVAMEHQPPYIVAVLPRYVEIRTLEPRLLVQSIELQRPRFITSGGSNIIYVASNHFVWRLIPVPMATQIQQLLQDKQFELALQLAEMKDDSDSEKQQQIHHIKNLYAFNLFCQKRFDESMQVFAKLGTDPTHVMGLYPDLLPTDYRKQLQYPNPLPTLSGAELEKAHLALIDYLTQKRSQLVKKLNDSDHQSSTSPLMEGTPTIKSKQKLLQIIDTTLLKCYLHVSCRHASPALKVSGPSRGLCWTPTRETLQRDPT
Protein: [Skp1-protein]-hydroxyproline N-acetylglucosaminyltransferase (EC 2.4.1.229) (Glycosyltransferase GnT51) (Skp1-HyPro GlcNAc-transferase) (UDP-GlcNAc:Skp1-hydroxyproline GlcNAc-transferase) (Skp1 GlcNAc-Tase) (UDP-GlcNAc:hydroxyproline polypeptide GlcNAc-transferase) (Q8T1C6)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Catalyzes the attachment of N-acetylglucosamine (GlcNAc) in alpha-linkage onto the 'hydroxyPro-143' residue of Skp1 (fpaA/fpaB). Is the first glycosyltransferase in the Skp1 HyPro modification pathway, which results in a pentasaccharide-linked 'HyPro-143'.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10593934}.
Interaction partners:
- SCF ubiquitin ligase complex protein SKP1a
- Prolyl 4-hydroxylase subunit alpha
- Myosin-2 heavy chain
- SCF ubiquitin ligase complex protein SKP1b
- UDP-galactose:fucoside alpha-3-galactosyltransferase
Sequence:
MNENSIFVSIISYRDSECQWTIKNLIELAKYKENIFIGVCLQYSMNDDSDNKCFQFNFEEEYGKNQIRIIRMNHTEAKGPCYARALVQQQLFKGEKYYLQIDSHMRFVKDWDIEMINQLLQCKKPNDDNGGMVIDEKAILTCYPMGYKLPNLIPTHRFPILLVASGFGENDGFLRLGGKIVSKKLIEPCSSLFWVSGFSFSRSDIINSVPYDPNLQYLFFGEEISMSARLFTHGYNFYSPTKTLIFHLWNRDYRSTFRENNSLEIQKLEENSKKRLLILFNQNNNNINDNDDNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNSSSSSSSSNNNNNNNNNNNNSSSTNNNNNNNNNNDDGIKIELKYNLGKIKSLDDYSNYCGVDFKNKTINNKGKFGGYYEERETFFMNEIMEYVIKSQIGI
Protein: P antigen family member 1 (PAGE-1) (AL5) (G antigen 9) (GAGE-9) (G antigen family B member 1) (Prostate-associated gene 1 protein) (O75459)
Organism: Homo sapiens (Human)
Interaction partners:
- P antigen family member 2
Sequence:
MGFLRRLIYRRRPMIYVESSEESSDEQPDEVESPTQSQDSTPAEEREDEGASAAQGQEPEADSQELVQPKTGCELGDGPDTKRVCLRNEEQMKLPAEGPEPEADSQEQVHPKTGCERGDGPDVQELGLPNPEEVKTPEEDEGQSQP
Protein: Cytochrome P450 93B2 (EC 1.14.19.76) (Flavone synthase II) (FNSII) (Q9XGT9)
Organism: Gerbera hybrida (Daisy)
Function: Functions as flavone synthase II (FNSII) that catalyzes the direct conversion of flavanones to flavones. In vitro, can convert liquiritigenin, naringenin and eriodictyol to 7,4'-dihydroxyflavone, apigenin and luteolin, respectively.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MNTLQLIFLLFFFPTLLFLYCLPYKRNQNHRRLPPSPPSFPIIGHLHHLGPLIHQSFHALSTRYGSLIHLRLGSVPCVVVSTPDLAKDFLKTNELAFSSRKHSLAIDHITYGVAFAFAPYGTYWKFIKKLFTVELLGTQNLSHFLPIRTHEIRELLRTLMVKSRAKERVNLTEELLKLTNNVISQMMMSIRCSGTNSEADEAKNLVREVTKIFGQFNVSDFIWFCKNIDLQGFKKRYEGTHRRYDALLERIIMGREENRRRGKIKDGEGKDFLDMLLDVLEDGKAEIKITRDHIKALILDFLTAGTDTTAIAIEWALVELINNPNALEKARQEIDQVIGDERLVQESDTPNLPYIQAIIKEALRLHPPIPMLIRKSTENVIVQGYDIPAGTLLFVNIWSIGRNPQCWETPLEFKPHRFLDGGDLKSSLDIKGHNFQLLPFGTGRRGCPGVNLAMRELSVVIANLIQCFDWDVVGERLLNTDERAGLTAPRAVDFVCVPLERGNTLKILGSN
Protein: Dual oxidase maturation factor 2 (Dual oxidase activator 2) (Q1HG44)
Organism: Homo sapiens (Human)
Function: Required for the maturation and the transport from the endoplasmic reticulum to the plasma membrane of functional DUOX2. May play a role in thyroid hormone synthesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16651268}; Multi-pass membrane protein {ECO:0000269|PubMed:16651268}.
Interaction partners:
- Dual oxidase 2
- Dual oxidase 1
- Iodotyrosine deiodinase 1
- Pendrin
- Sodium/iodide cotransporter
- Thyroid peroxidase
- Thyroglobulin
- NADPH oxidase 5
Sequence:
MTLWNGVLPFYPQPRHAAGFSVPLLIVILVFLALAASFLLILPGIRGHSRWFWLVRVLLSLFIGAEIVAVHFSAEWFVGTVNTNTSYKAFSAARVTARVRLLVGLEGINITLTGTPVHQLNETIDYNEQFTWRLKENYAAEYANALEKGLPDPVLYLAEKFTPSSPCGLYHQYHLAGHYASATLWVAFCFWLLSNVLLSTPAPLYGGLALLTTGAFALFGVFALASISSVPLCPLRLGSSALTTQYGAAFWVTLATGVLCLFLGGAVVSLQYVRPSALRTLLDQSAKDCSQERGGSPLILGDPLHKQAALPDLKCITTNL
Protein: Secreted effector protein (A0A0F6B5H5)
Organism: Salmonella typhimurium (strain 14028s / SGSC 2262)
Subcellular location: Host membrane {ECO:0000256|ARBA:ARBA00004551}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MERSLDSLAGMAKSAFGAGTSAAMRQATSPKTILEYIINFFTCGGIRRRNETQYQELIETMAETLKSTMPDRGAPLPENIILDDMDGCRVEFNLPGENNEAGQVIVRVSKGDHSETREIPLASFEKICRALLFRCEFSLPQDSVILTAQGGMNLKGAVLTGANLTSENLCDADLSGANLEGAVLFMADCEGANFKGANLSGTSLGDSNFKNACLEDSIMCGATLDHANLTGANLQHASLLGCSMIECNCSGANMDHTNLSGATLIRADMSGATLQGATIMAAIMEGAVLTRANLRKASFISTNLDGADLAEANLNNTCFKDCTLTDLRTEDATMSTSTQTLFNEFYSENI
Protein: Protein FAM98A (Q3TJZ6)
Organism: Mus musculus (Mouse)
Function: Positively stimulates PRMT1-induced protein arginine methylation (By similarity). Involved in skeletal homeostasis. Positively regulates lysosome peripheral distribution and ruffled border formation in osteoclasts.
Interaction partners:
- ATP-dependent RNA helicase DDX1
- RNA transcription, translation and transport factor protein
- RNA-splicing ligase RtcB homolog
- FMR1-interacting protein NUFIP2
- Ashwin
- Ataxin-2
- ATP-dependent RNA helicase DHX15
- U4/U6 small nuclear ribonucleoprotein Prp3
- ATP-dependent DNA/RNA helicase DHX36
- Heterogeneous nuclear ribonucleoprotein U-like protein 2
Sequence:
MECDLMETDILESLEDLGYKGPLLDDGALLQAVSAGAASPEFTKLCAWLVSELRVLCKLEENVQATNSPSEAEEFQLEVSGLLGEMNCPYPSLTSGDVTKRLLVEKNCLLLLTYLISELEAARMLCVNAPPKKAQEGGGSEVFQELKGICIALGMSKPPANITMFQFFSGIEKKLKETLAKVPPNHVGKPLLKKPMGPAHWEKIEAINQAIANEYEVRRKLLIKRLDVTVQSFGWSDRAKSQTDKLAKVYQPKRSLLSPKGKVSVAHLLAARQDLSKILRTSSGSIREKTACAINKVLMGRVPDRGGRPNEIEPPPPEMPPWQKRQDGPQQQAGGRGGGRGGYEHSSYGGRGGHEQGGRGGRGSYDHGGRGGGRGNKHQGGWTDGGSGSGGGYQDGAYRDSGFQPGGYHGGHSGGYQAGGYGGFQTSSYTGSGYQGGGYQQDNRYQDGGHHGERGSGRGGRGGRGGRGGRGSQGGGWGGRGSQTYHQGGQFEQHFQHGGYQYSHSGFGQGRHYTS
Protein: Germin-like protein subfamily 2 member 1 (P94014)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in plant defense. Probably has no oxalate oxidase activity even if the active site is conserved.
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000250}.
Interaction partners:
- AICARFT/IMPCHase bienzyme family protein
- Putative Tubby-like protein 4
- Small ribosomal subunit protein uS15c
- non-specific serine/threonine protein kinase
- Ankyrin repeat family protein
- Ankyrin repeat family protein
- Probable S-adenosylmethionine-dependent methyltransferase At5g37970
- Emb|CAB89385.1
- Transmembrane protein
- Putative defensin-like protein 227
Sequence:
MASPTLTLLLLLTTVSFFISSSADPDMLQDLCVADLPSGIKINGFPCKDAATVTSADFFSQGLAKPGLTNNTFGALVTGANVMTIPGLNTLGVSLSRIDYAPGGLNPPHTHPRATEVVFVLEGTLDVGFLTTANKLISQSLKKGDVFAFPKGLVHFQKNNGDVPASVIAAFNSQLPGTQSLGATLFGSTPPVPDNILAQAFQTSPGTVKHIKSKFQPKK