wanglab/gogpt-training-data huggingface dataset:
Protein: Poly-beta-1,6-N-acetyl-D-glucosamine export protein (PGA export protein) (Poly-beta-1,6-GlcNAc export protein) (P69434)
Organism: Escherichia coli (strain K12)
Function: Exports the biofilm adhesin polysaccharide poly-beta-1,6-N-acetyl-D-glucosamine (PGA) across the outer membrane. The PGA transported seems to be partially N-deacetylated since N-deacetylation of PGA by PgaB is needed for PGA export through the PgaA porin.
Subcellular location: Cell outer membrane {ECO:0000305|PubMed:18359807}; Multi-pass membrane protein {ECO:0000305|PubMed:18359807}.
Interaction partners:
- Poly-beta-1,6-N-acetyl-D-glucosamine synthase
- Biofilm PGA synthesis protein PgaD
- Carbon storage regulator
- Poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase
- Cellulose synthase operon protein C
- Transcriptional activator protein NhaR
Sequence:
MYSSSRKRCPKTKWALKLLTAAFLAASPAAKSAVNNAYDALIIEARKGNTQPALSWFALKSALSNNQIADWLQIALWAGQDKQVITVYNRYRHQQLPARGYAAVAVAYRNLQQWQNSLTLWQKALSLEPQNKDYQRGQILTLADAGHYDTALVKLKQLNSGAPDKANLLAEAYIYKLAGRHQDELRAMTESLPENASTQQYPTEYVQALRNNQLAAAIDDANLTPDIRADIHAELVRLSFMPTRSESERYAIADRALAQYAALEILWHDNPDRTAQYQRIQVDHLGALLTRDRYKDVISHYQRLKKTGQIIPPWGQYWVASAYLKDHQPKKAQSIMTELFYHKETIAPDLSDEELADLFYSHLESENYPGALTVTQHTINTSPPFLRLMGTPTSIPNDTWLQGHSFLSTVAKYSNDLPQAEMTARELAYNAPGNQGLRIDYASVLQARGWPRAAENELKKAEVIEPRNINLEVEQAWTALTLQEWQQAAVLTHDVVEREPQDPGVVRLKRAVDVHNLAELRIAGSTGIDAEGPDSGKHDVDLTTIVYSPPLKDNWRGFAGFGYADGQFSEGKGIVRDWLAGVEWRSRNIWLEAEYAERVFNHEHKPGARLSGWYDFNDNWRIGSQLERLSHRVPLRAMKNGVTGNSAQAYVRWYQNERRKYGVSWAFTDFSDSNQRHEVSLEGQERIWSSPYLIVDFLPSLYYEQNTEHDTPYYNPIKTFDIVPAFEASHLLWRSYENSWEQIFSAGVGASWQKHYGTDVVTQLGYGQRISWNDVIDAGATLRWEKRPYDGDREHNLYVEFDMTFRF
Protein: Chemosensory protein B 42b (A1Z6S1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MIFVLLLLLGVTSSWATDYELLLEDPDIFSTCTDGPPGSINIRQALNLDDIVIDQKGDILHVSGNATVVWDVQPTDRITARLDVFHFNRGTWEPTVFSMATQNFCSIMYDKNQYWYKYWTRFITNRHEVEKKCFRGPDTVLVHEPFDLILKFENFRGPLLRGRHKLVILFNALDERNIPRPNPICLEIIGEPLKLQ
Protein: Cactin, spliceosome C complex subunit (K7ENY9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XKQEQGVESEPLFPILKQEPQSPSRSLEPEDAAPTPPGPSSEGGPAEAEVDGATPTEGDGDGDGEGEGEGEAVLMEEDLIQQSLDDYDAGRYSPRLLTAHELPLDAHVLEPDEDLQRLQLSRQQLQVTGDASESAEDIFFRRAKEGMGQDEAQFSVEMPLTGKAYLWADKYRPRKPRFFNRVHTGFEWNKYNQTHYDFDNPPPKIVQGYKFNIFYPDLIDKRSTPEYFLEACADNKDFAILRFHAGPPYEDIAFKIVNREWEYSHRHGFRCQFANGIFQLWFHFKRYRYRR
Protein: Protein CutA 1, chloroplastic (OsCutA1) (Q109R6)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
Sequence:
MPLLPSPLGSLSAAATAAPRRAAAAAGLSPLLLRRRAPIAGALLFLSLGAFAGVRSLSSSASARMESTSTTVPSIVVYVTVPNKEAGKRLAGSIISEKLAACVNIVPGIESVYWWEGKVQTDAEELLIIKTRESLLDALTEHVKANHEYDVPEVIALPIKGGNLKYLEWLKNSTRES
Protein: E3 ubiquitin-protein ligase listerin (EC 2.3.2.27) (RING-type E3 ubiquitin transferase listerin) (Q385R6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}.
Interaction partners:
- Translation-associated element 2
- Transcription factor 25
- E3 ubiquitin-protein ligase TRIP12
- Ubiquitin-protein ligase, putative
- HECT-type E3 ubiquitin transferase
- Ubiquitin-protein ligase, putative
- Large ribosomal subunit protein uL5
Sequence:
MPPRPAKGRAALSFVASRGIPDSLESFLGDFSQPVKSNTEGSAMMEVNLKLLQKSNETTVLKALVELNRGASAMSEEELVHYLPQVVEAVVRHAEHSNASVRSGVFALLHEFLLRGSLLQQAVTKRLPKLASAWVSRMCDMEPSVRRDASDAFNAAYTTEVLKQHADSIVTDLISNYEEIIAQSRGKPLQDDTLDRRSNALYSCVCAMGHMLRVGAPASACHKVIEFVEGNSVQPIMPPPEGVTKGSMVVKAPVVRSASLILLRDILSSKLATLRVHQQVSTALYNAMSDRCAVVLRRAWELQLLWFGSDSSSALSHMQGGFLRVVMNSITDCNDPEVAEIIYPSLVPLLVPVTRSSAFASAIEEFSEVLQRKILNVSDVVQREWDLVLSSLMRVWELRCVRSAKLGEGHEREGATMFSSIVATLATALEQPARRGRLLSTTASVVAQTLERVARHTECFSECVQLLCGPTDSFSQRTGGGASAALVESFDVLQAALIGSSVSLPGVLVGAETLMAKYVEKKQWNILAELLQSMTDAYGSCVREEHAHSPVGIPSKEIQKLVTNGVLRAVRLSISAERKDSDGVEPMHPLQRVLSYVLQWSDDDALSELQQIAATVGPGPFWLKDLLRSHELRDPERLITLFSKACEEADFRTVELCVDSLLGEQEVNPRPLTSAEKKGLRQAVQESLRKLHLLVSVDNDESEEEAEESSKEGDSGSGYDGSGAGDSSGDEGSEGAAEADGSGNEGDSNSGTLVQQQLIAWARFLRSGEPFASLLEVSSEDIDLPMVFRIVASIAPRLHAEQYMSIKALRMALQMEEDPLLVAMSKKIHSIDSKAFNVVVESIEQLLNSYGVSVEERDTVSLELFDSVMSDPQSSIAACGRLQHIVPFASCSLIQGIACSGDVWLEHQVHLRANVAATGTGKVPFALLDQYSPLCGIVPSMLRCVRTSQLIHLLASSVELNSASAAVVGRPLLHAAHVQEVLAEPTRRLLVTKLLPRVLLSISSPKEVDTLLLRGEEVHKLLFTLAVVIRDTAVHSSGDAFNSSVRCIVSTITQWIAEAALLHVGDAPTHEEAIRHYRALFSTLDEAADIVGDSFLAKVPSGEAASAIQESMCMIPTLHPNTGLLAMTLHRHLSHLPVVRGDTVRQVIDYARKKKPLDGLEFLAELTSSRIIDTEAYNELVHVFTRLLASSFRLRYMPPNNCLVSQAPNDAPISLCDTQRAVVAVVSARRGINLHNRVDDTLRSSINLVLFDAVAGSVVSLKQANEEELSLMTKLIAFTSNCLSDLGSSDVTVLRASEVSVTKVAAVMNYAYQWLCATSITRLDSIGMETVTSAIRAIALLSNLTLVRSGFVLLPIMRPITGRRSMKDIREEFSSKSPAKAIIFRRQAAVIAKTNKQKLTLFPHLLAWCVTLSGPVQERVSKEWREEVFQLLDVLCALLLSPAVPGSKRVENTYLCNGNGSSGAGEQLGFEIIALTRPNAADPMRELAKGAAAVFALLLQSSTLSIVKSWLETVERKLQDYFYTFVEEHLSPCLIRESLLMVLSKNPTGGSTFDVNERYTVSVCTLRNRITLKYTVEDTDSTVHIEFKPDFPLRPPVVTCEKTRGCGVSADKWHVWMRKMTVLLFGGSSNVWDCVMLFGRNMDEHFSGKDPCPICFAIVSASSNRLPDMQCAVCRNSAIHSDCLYSWWATGGRTVCPLCRSPWVAT
Protein: Chaperone protein DNAJ, putative (Q4GZ23)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Heat shock protein 70
- Hsp70 protein
- Heat shock protein 70, putative
- Heat shock 70 kDa protein, putative
Sequence:
MIVLPTFDFPQLEDGHEPLTLRQQQQQPPRGELVNLVHVLPFGLAIQQRALLTARLLMEERQKPSRRHEDPNAAGASDGEDDSEGDGDGSGEYGRGGGGSFQQQQSYASRRKKFVKLTEEDLQVDWYEILGLEQSGGATDEQIRTAYRRRCLETHPDKQKDRSDAAFKKVQRALDILGDPETRLTYDSSRPFDDTIPAETLPTGADFYAIFGPVFERNKRWSTDPSLPSIGNDKTSLEEVNRFYDRWVRFQSWRDFSHMVELDEIDDSMCREEKRYYMRENERQLNCLRREEQQRLRTLVERARKNDPRLRRKREEDEAKRQREQKEREDRRRQAREEGERRRAEEMERERQKREEEKRKITDTKNAIRQAKDDLIVFLEEHGLLDETATNKLLRHAVRRPNIGWIFSKINTAEEAAGVVSEVKNKDTTRRATSTKSGTSSNVASRTTDESEEDTEVEAVICFNELVEEKERQIGLTRYGEAVKARPEPKPQEAKKKTVPESVNKHAKEWDEEDLTRLQKATAKFPPGTVERWSKIAEQLRGKFTEEEAMQKVNEITAGLHRSGGQTGVASAKQPTSAVEGNGATAAAAPSAGGANSQVASVEDWTVKQQKMLELGLRDLKDYKEKDKFQKIAAMVDGKNARECFERFKYLCAMNKRK
Protein: Olfactory receptor 6B2 (Olfactory receptor OR2-1) (Q6IFH4)
Organism: Homo sapiens (Human)
Function: Odorant receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
Sequence:
MSGENVTKVSTFILVGLPTAPGLQYLLFLLFLLTYLFVLVENLAIILIVWSSTSLHRPMYYFLSSMSFLEIWYVSDITPKMLEGFLLQQKRISFVGCMTQLYFFSSLVCTECVLLASMAYDRYVAICHPLRYHVLVTPGLCLQLVGFSFVSGFTISMIKVCFISSVTFCGSNVLNHFFCDISPILKLACTDFSTAELVDFILAFIILVFPLLATILSYWHITLAVLRIPSATGCWRAFSTCASHLTVVTVFYTALLFMYVRPQAIDSQSSNKLISAVYTVVTPIINPLIYCLRNKEFKDALKKALGLGQTSH
Protein: Protein TIFY 7 (Jasmonate ZIM domain-containing protein 9) (Q8W4J8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Repressor of jasmonate responses. Jasmonoyl-isoleucine (JA-Ile) specifically promotes COI1-TIFY7/JAZ9 interaction. Interacts with and suppresses RHD6 and RSL1 transcription factor activities to negatively regulate jasmonate-stimulated root hair development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:23169619}.
Interaction partners:
- Transcription factor MYC2
- Transcription factor MYC3
- Coronatine-insensitive protein 1
- Transcription factor MYC4
- Protein TIFY 9
- Protein TIFY 11B
- DELLA protein RGA
- Protein TIFY 5B
- Protein TIFY 11A
- AFP homolog 2
Sequence:
MERDFLGLSDKQYLSNNVKHEVNDDAVEERGLSTKAAREWGKSKVFATSSFMPSSDFQEAKAFPGAYQWGSVSAANVFRRCQFGGAFQNATPLLLGGSVPLPTHPSLVPRVASSGSSPQLTIFYGGTISVFNDISPDKAQAIMLCAGNGLKGETGDSKPVREAERMYGKQIHNTAATSSSSATHTDNFSRCRDTPVAATNAMSMIESFNAAPRNMIPSVPQARKASLARFLEKRKERLMSAMPYKKMLLDLSTGESSGMNYSSTSPT
Protein: Pre-mRNA leakage protein 39 (39 kDa pre-mRNA leakage protein) (Q03760)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the nuclear retention of improperly spliced pre-mRNAs.
Subcellular location: Nucleus membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16162818}; Peripheral membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16162818}; Lumenal side {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16162818}. Note=Associated with a subset of nuclear pores opposite to the nucleolus.
Interaction partners:
- Pre-mRNA leakage protein 1
- Silent chromatin protein ESC1
- Dihydroorotase
- Nucleoporin NUP60
Sequence:
MEKDALEVRLKSIRHSLDKNTKLLPGKYRNTLGERLITKWRYKKKSHNGSSMLPEKCKSHVQLYDDLVQESSKHFVGFRLHDLRALLKRICSIQNYTRHVLIEWDVRWVNPLTLASKGWEPYQSASQSQVPFKCCCCHAIMTIPLLKNGDDVADYTMKLNEKIWNSNIIGNHLQKCPWRENQVDLNKEYYLSSQNLIREIERIHTEIDRIVSGSNEFSLKRNSSRIFHYLSEKEIQKLAFFFDCKDYSLVGLLLLGYTKFQKDDLVQCTACFHRASLKKLEYTEFNGHALWCRYYNKELLPTMLLELIGKEDKLITKLGVGERLNKLEAVLQTL
Protein: Protein translocase subunit SecY (P0AGA2)
Organism: Escherichia coli (strain K12)
Function: The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. SecY is required to insert newly synthesized SecY into the inner membrane. Overexpression of some hybrid proteins has been thought to jam the protein secretion apparatus resulting in cell death; while this may be true, overexpression also results in FtsH-mediated degradation of SecY.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Large ribosomal subunit protein uL6
- Protein translocase subunit SecE
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL4
- Small ribosomal subunit protein uS13
- Signal recognition particle receptor FtsY
- Large ribosomal subunit protein uL15
- Large ribosomal subunit protein uL24
- Protein translocase subunit SecF
- Small ribosomal subunit protein uS10
Sequence:
MAKQPGLDFQSAKGGLGELKRRLLFVIGALIVFRIGSFIPIPGIDAAVLAKLLEQQRGTIIEMFNMFSGGALSRASIFALGIMPYISASIIIQLLTVVHPTLAEIKKEGESGRRKISQYTRYGTLVLAIFQSIGIATGLPNMPGMQGLVINPGFAFYFTAVVSLVTGTMFLMWLGEQITERGIGNGISIIIFAGIVAGLPPAIAHTIEQARQGDLHFLVLLLVAVLVFAVTFFVVFVERGQRRIVVNYAKRQQGRRVYAAQSTHLPLKVNMAGVIPAIFASSIILFPATIASWFGGGTGWNWLTTISLYLQPGQPLYVLLYASAIIFFCFFYTALVFNPRETADNLKKSGAFVPGIRPGEQTAKYIDKVMTRLTLVGALYITFICLIPEFMRDAMKVPFYFGGTSLLIVVVVIMDFMAQVQTLMMSSQYESALKKANLKGYGR
Protein: 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44) (Q17761)
Organism: Caenorhabditis elegans
Function: Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH.
Interaction partners:
- Glucose-6-phosphate 1-dehydrogenase
- Ribulose-phosphate 3-epimerase
- Putative 6-phosphogluconolactonase
- Probable-ribose 5-phosphate isomerase
- transketolase
- Transaldolase
- Gluconokinase
- Probable phosphoglycerate kinase
- Glucosamine-6-phosphate deaminase
- Ribokinase
Sequence:
MAEADIAVIGLAVMGQNLILNMNDHGFTVCAFNRTVKLVDDFLANEAKGTKIIGAHSIEEMCKKLKRPRRVMMLIKAGTPVDMMIDAIVPHLEEGDIIIDGGNSEYTDSNRRSEQLAAKGIMFVGCGVSGGEEGARFGPSLMPGGNPKAWPHLKDIFQKIAAKSNGEPCCDWVGNAGSGHFVKMVHNGIEYGDMQLIAEAYHLLSKAVELNHDQMAEVLDDWNKGELESFLIEITANILKYRDEQGEPIVPKIRDSAGQKGTGKWTCFAALEYGLPVTLIGEAVFARCLSALKDERVRASKQLPRPQVSPDTVVQDKRVFIKQISKALYASKIVSYAQGFMLLAEASKQFNWNLNFGAIALMWRGGCIIRSRFLGDIEHAFQKNKQLSNLLLDDFFTKAITEAQDSWRVVVCAAVRLGIPVPAFSSALAFYDGYTSEVVPANLLQAQRDYFGAHTYELLAKPGTWVHTNWTGTGGRVTSNAYNA
Protein: Acetylglutamate kinase, putative (EC 1.2.1.38) (Q4WCZ1)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173, ECO:0000256|PIRNR:PIRNR036440}.
Interaction partners:
- acetylornithine transaminase
- Arginine biosynthesis bifunctional protein ArgJ
- argininosuccinate lyase
- Argininosuccinate synthase
- Ornithine aminotransferase
- Ornithine aminotransferase
- Ornithine carbamoyltransferase, mitochondrial
- Onanonoxo-7-onima-8-eninoihtemlysoneda
- Acyl-CoA:6-aminopenicillanic-acid-acyltransferase, putative
- Amino-acid acetyltransferase, mitochondrial
Sequence:
MLVDKMFSLRTTVRRASTSKPLRALSAPHAVSSARLSSPRHALKASAVPLLQSRSYSRAADPHLSSTRSTVVQLLSNIGSKREVQQYLSHFTSVSSQQFAVIKVGGAIITEHLQTLSSALAFLNHVGLYPIVVHGAGPQLNRMLEAAGVEPHFEDGIRVTDGKTLALARKLFLEENLKLIEELERMGVRARPINAGVFYADYLDKEKYNLVGKINGVNKKPIESAIEAGCLPILTSMAETPDGQVLNVNADVAAGELARALQPLKIVYLAEKGGLFNGDTGEKISVINLDEEYDHLMTQWWVRHGTRLKIKEMKELLNDLPRTSSVAIIHPADLQKELFTDSGAGTLIRRGNKVHTKTSLSEFEDLEKLKDVLVRDREGLDARATVDRYVEGLKERDFKVYYDEPMEALAVVLPPSKDNSSSFPHLATFTITKSGWLSNVADNVFAAIKKDFPQLVWTVKENDENLTWFFDKADGSLSRDGEVLFWYGIESGEEVKQLVQEFNQHGRQMFGDINLEARLQRAAQAATNIGKGFGASGASVEQKRAFSSTANALRAARFGRPAVSPRVVRSYSTTNPNPPLGEKNMSNNRPSKVALIGARGYTGQALINLLNAHPYMDLRHVSSRELAGKKLQGYDKREIIYENLSPEDVKRMSANGDVDCWVMALPNGVCKPFVDAVDQGSETGNVIVDLSADYRFDDKWTYGLPELVNRGKIAQATRISNPGCYATAAQIGIAPLVPYLGGQPTVFGVSGYSGAGTKPSPKNDVQNLTNNIIPYSLTDHIHEREISAQLGTSIAFIPHVAVWFQGIHHTISIPLNQEMTSRDIRNIYQERYAGEKLVKIIGEAPLVKNIAGRHGIEVGGFAVHSSGKRVVVCATIDNLLKGAATQCLQNMNLALGYGEYEGIPLE
Protein: Fcr1p (Q5ADM4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- SEC14 homolog 3
- NADH-ubiquinone oxidoreductase
- Uncharacterized protein
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- NADH-ubiquinone oxidoreductase chain 2
- NADH-ubiquinone oxidoreductase chain 4L
- Nuc2p
Sequence:
MSDDHSIHSHTQGLHHIKKKRVGKACDSCRIKKTKCDGKKPCNRCTLDNKICVFTEKKKTKEKKHPSGYVELLEARLDILTRSLEKLIELSRPHLQFIDDIITEEKSVNQEKSSPASSTPNSSSSDHHDDVEEQNSTGVVAPINKVVSYLIKEQGLLKNIPLEWEQGTEIAANFDPNRNLKSSSRLFAEHKGEAFIGSPVTSPQQMPTSNPFRRTSMFKEELESPSSDHYNESIFSQSVDEPYIKKEPNSVQFSKGTFSPQQQQLQQQQQMLNQFSLNTFRDISDIESDSSNKEDGLNSGSVSPPTSNYRSFSLFSDSNGEPILGKTSSLTSLTNKYENHSLSSPQTAINPVFNNSTTGPILTTLRRNSSSHSQKTLGSIQLQQKPRGSVHKPVRNHSRVSSFDKRMESTATAAATVAAVSGSVQLSQNTTPQNLPHLDNSQNNNYLRDNGMNNIGAGSVGGGLTFGAPSFTQPLSPSDDAIVYPTNQFTNRPATVSTFGGGLDVLVDNSLDPFFNI
Protein: Cyclin-dependent kinase C-1 (CDKC;1) (EC 2.7.11.22) (EC 2.7.11.23) (Q9LFT8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Cyclin-T1-3
- Cyclin-T1-4
- Cyclin-T1-5
- Putative cyclin-T1-1
- Cyclin-T1-2
- Transmembrane protein
- Protein phosphatase 2C and cyclic nucleotide-binding/kinase domain-containing protein
- Probable protein phosphatase 2C 2
Sequence:
MAMASFGQLNLEEPPPIWGSRSVDCFEKLEQIGEGTYGQVYMAKEIKTGEIVALKKIRMDNEREGFPITAIREIKILKKLHHENVIQLKEIVTSPGRDRDDQGKPDNNKYKGGIYMVFEYMDHDLTGLADRPGLRFTVPQIKCYMKQLLTGLHYCHVNQVLHRDIKGSNLLIDNEGNLKLADFGLARSYSHDHTGNLTNRVITLWYRPPELLLGATKYGPAIDMWSVGCIFAELLHAKPILPGKNEQEQLNKIFELCGSPDEKLWPGVSKMPWFNNFKPARPLKRRVREFFRHFDRHALELLEKMLVLDPAQRISAKDALDAEYFWTDPLPCDPKSLPTYESSHEFQTKKKRQQQRQNEEAAKRQKLQHPPLQHSRLPPLQHGGQSHAAPHWPAGPNHPTNNAPPQVPAGPSHNFYGKPRGPPGPNRYPPSGNQSGGYNQSRGGYSSGSYPPQGRGAPYVAGPRGPSGGPYGVGPPNYTQGGQYGGSGSSGRGQNQRNQQYGWQQ
Protein: FAD-linked oxidoreductase afoF (EC 1.-.-.-) (Asperfuranone biosynthesis protein B) (Q5BEJ5)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of asperfuranone, a probable antitumor agent. The polyketide synthase afoG is responsible for producing the 3,5-dimethyloctadienone moiety from acetyl-CoA, three malonyl-CoA, and two S-adenosyl methionines (SAM). The 3,5-dimethyloctadienone moiety is then loaded onto the SAT domain of afoE and extended with four malonyl-CoA and one SAM, which leads to the formation of 2,4-dihydroxy-6-(5,7-dimethyl-2-oxo-trans-3-trans-5-nonadienyl)-3-methylbenzaldehyde (compound 2) after reductive release and aldol condensation. AfoD is the next enzyme in the biosynthesis sequence and hydroxylates the side chain at the benzylic position of compound 2. After benzylic hydroxylation, a furan ring is formed after five-member ring hemiacetal formation and water elimination. AfoF and afoC are proposed to oxidize the R-diketone proton and to reduce the unconjugated carbonyl group, respectively, to generate asperfuranone. Since no intermediates could be isolated from afoF and afoC deletants, the sequence of these two enzymes is not fully understood. Moreover, since afoC deletant still produces a small amount of asperfuranone, other endogenous oxidoreductases might catalyze the same reaction with much less efficiency.
Interaction partners:
Sequence:
MRFLLQSITLVAAARAASIDLESLFGPYVSPETEIAEVGDADFDEVVSPRWSEWRPPTWTGAIKPQTEEDLQEIVRIAVANNVSFMATSGGHGTSLIYGTVKGLDINLANFNNVDIDLESNTVTVGAGAKLGDITEPLYKAGKAIQTARGNSPCVGVIGATIGGGIGYETGLFGLGVDALVSVRIITATGELITANETCNSDLLWAIRGAGANFGIITAATFKMFDQPNNGDAVIGTFVYNSSKSLGVFEYLSVLDNVLPPELGVQLSIGYDRTINETLLTVDIKHFAPWATFVDHWEHAEALGPISRNVSNVTLVELYAGLDGPCQTGAYVSGGTVGLGRTDAATMQEVFDDMTAFYEQYPGYLGQSLFQRYANNNTLKTPAHTAVYPWRDTKMFWLHENIFLNPELEAPTNELLVSLREKLHATSGFPADQPHIYVNYAFGDEGPEAWWSKENLPKLSYLKRKWDPKGVFGKGTPIPRF
Protein: NAD(P)H oxidoreductase RTN4IP1, mitochondrial (EC 1.6.5.-) (NOGO-interacting mitochondrial protein) (Reticulon-4-interacting protein 1) (Q924D0)
Organism: Mus musculus (Mouse)
Function: Plays a role in the regulation of retinal ganglion cell (RGC) neurite outgrowth, and hence in the development of the inner retina and optic nerve. Appears to be a potent inhibitor of regeneration following spinal cord injury.
Subcellular location: Mitochondrion matrix {ECO:0000305|PubMed:12067236}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q8WWV3}. Note=Mainly localizes to the mitochondrial matrix. Also colocalizes with the endoplasmic reticulum HSPA5 at spots corresponding to contacts with mitochondria. {ECO:0000250|UniProtKB:Q8WWV3}.
Interaction partners:
- Reticulon-4
Sequence:
MGVLKTCVLRRSACAAACFWRRTVIPKPPFRGISTTSARSTVMPAWVIDKYGKNEVLRFTQNMMLPIIHYPNEVIIKVHAASVNPIDVNMRSGYGATALNMKRDPLHMKTKGEEFPLTLGRDVSGVVMECGLDVKYFQPGDEVWAAVPPWKQGTLSEFVVVSGNEVSHKPKSLTHTQAASLPYVALTAWSAINKVGGLSDKNCKGKRALILGASGGVGTFAIQVMKAWGAHVTAVCSKDASELVRKLGADEVIDYTLGSVEEQLKSLKLFDFILDNVGGSTETWALNFLKKWSGATYVTLVTPFLLNMDRLGVADGMLQTGVTVGTKALKHLWQGVHYRWAFFMASGPYLDEIAELVDAGKIRPVIERTFPFSEVPEAFLKVERGHARGKTVVNVV
Protein: FCH and mu domain containing endocytic adaptor 1 (FCH domain only 1, isoform CRA_b) (A0A0C3SFZ9)
Organism: Homo sapiens (Human)
Subcellular location: Membrane, clathrin-coated pit {ECO:0000256|ARBA:ARBA00004283}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004283}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004283}.
Interaction partners:
Sequence:
MSYFGEHFWGEKNHGFEVLYHSVKQGPISTKELADFIRERATIEETYSKAMAKLSKLASNGTPMGTFAPLWEVFRVSSDKLALCHLELTRKLQDLIKDVLRYGEEQLKTHKKCKEEVVSTLDAVQVLSGVSQLLPKSRENYLNRCMDQERLRRESTSQKEMDKAETKTKKAAESLRRSVEKYNSARADFEQKMLDSALRFQAMEETHLRHMKALLGSYAHSVEDTHVQIGQVHEEFKQNIENVSVEMLLRKFAESKGTGREKPGPLDFEAYSAAALQEAMKRLRGAKAFRLPGLSRREREPEPPAAVDFLEPDSGTCPEVDEEGFTVRPDVTQNSTAEPSRFSSSDSDFDDEEPRKFYVHIKPAPARAPACSPEAAAAQLRATAGSLILPPGPGGTMKRHSSRDAAGKPQRPRSAPRTSSCAERLQSEEQVSKNLFGPPLESAFDHEDFTGSSSLGFTSSPSPFSSSSPENVEDSGLDSPSHAAPGPSPDSWVPRPGTPQSPPSCRAPPPEARGIRAPPLPDSPQPLASSPGPWGLEALAGGDLMPAPADPTAREGLAAPPRRLRSRKVSCPLTRSNGDLSRSLSPSPLGSSAASTALERPSFLSQTGHGVSRGPSPVVLGSQDALPIATAFTEYVHAYFRGHSPSCLARVTGELTMTFPAGIVRVFSGTPPPPVLSFRLVHTTAIEHFQPNADLLFSDPSQSDPETKDFWLNMAALTEALQRQAEQNPTASYYNVVLLRYQFSRPGPQSVPLQLSAHWQCGATLTQVSVEYGYRPGATAVPTPLTNVQILLPVGEPVTNVRLQPAATWNLEEKRLTWRLPDVSEAGGSGRLSASWEPLSGPSTPSPVAAQFTSEGTTLSGVDLELVGSGYRMSLVKRRFATAAPPQGCTW
Protein: Thioredoxin domain-containing protein (Q57WB6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDCKLQHVLAPYVVARRAVKRYGCCRGASNSINVDCSASTCRGRFEEDFCGIESVADAGPAGFGHNDQHTERGLDVEYFPASRLSGRYVLVYLTSPSGSSFTNHGPDCVMRTTESLCSPLLTASPRVGTPVPSASSSTGRGSSASLPILTQEKTGTSPSAPLCPVASLLSRFCIYFGCQTESRDAERMSRFVVLEVRQGISVEPRWESLHNMETRNRASASFGDAGAISFSRAVSPKGVDGAAFTEDFKVNDALTDLSTADQKFGGWFYLENSAAYRCVIQKYNVSSWPAILLFDPAGELLTARAYDHIEREISTLSTSDDPNILAVVDSRAEQHMQEVVGIGPYAGFRSGFPWMTPDAGRDEDRGSNAVDDEVEGAPLLSLVRWLLRHARRVGESCEVGATYPPEDSCNVPEQRCLDSCMDGATHLALYFGAVWHPATKRFLPKLKRLWSAACEGGDDCCVLDDDAGRNSSDGEGAAAWEGGKRALSAFVADTGSLYEPLGIESWRRGMTNDVCASVSTADSDAPYIPSRCSAVETPMGSPKEHPPSFQSPTPTVEGPLVSPRVFRSELAEEKQPEGSHHFQVVFVSCDMDVSQLKSSLTSMPSSWLFVSSVLAPQAQGVIRACLEFFDVRVFPRLVVLDTSHRVGLQHDDGGLSKVWSRYPIALKVVRSHGERSVLNGSGLRELLSGDDLNDNVVPQREASTGECGIDGSARLLAHGIITNELLHQGYLHSMMRSVLGQGGSLFVLCCIGSICPDLHQECVASLREACTSWAQETGRFSEGVPRHTLGSLTLGKPSQMTVMEASTVCAGDLTGPATLATVSPLSCFIRADLTISNSGRSSGEVASPPLERVTTSVDDNRSSAVYFVDAISLVRGHEGNSGEGAGEGITRSGRRSELCTEGGLSQEDKSLLQEYVISEVLEANEHFVPPFEGEPFLVYLQWPERRVDVLRRIDDSEPPLNTGGPSARSPSVTASANTLIPASGTPSPGAVEVGAPAEVPRRSPLCSSALVKSFIVRCNMKRTC
Protein: L-proline trans-4-hydroxylase (P4H) (EC 1.14.11.57) (R9UTQ8)
Organism: Streptomyces griseoviridis
Function: Involved in the biosynthesis of the peptidolactone antibiotic etamycin (viridogrisein). Catalyzes the hydroxylation of free L-proline at the C-4 position to yield trans-4-hydroxy-L-proline.
Interaction partners:
Sequence:
MSVSAPLLDAKVRYGRDGWLPLPHTLSDPDVRKLRQRIEGISREQRPEVVLEEGSSAVRALHGCHDFDEVCARLVRLPALVGLAEQLLGGPVYVYQFKVNMKQAHEGAAWPWHQDFAFWHHEDGMGAPDAVNIAIFLDDVTDENGPLEVIPGSQHAGIVEDTARPGRERSHDWRHHVSAKLEYVVPDEIAGRLAGTFGVRRLTGPAGTAVAFHPSIIHSSSNNTSAQRRCVLLITYNRVTNTPAHPVRPPFLVSRDSTPVVPVDADRL
Protein: Bromodomain PHD finger transcription factor (A2A655)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MRGRRGRPPKQPAAPAAERCAPAPPPPPPPPPPPPPPPPPPPPASGPIGGLRSRHRGSSRGRWAAAQAEVAPKTRLSSPRGGGRRKQPPPPPPASGSSASGPGRGGRGGGGGRTGGGGGHLARTTPARRAVNKVVYDDHESDDDDEEEDMVSEEDEEEEEDGDAEETQDSEDEEEDDMEEDDDDSDYPEEMEDDDDDASYCTESSFRSHSTYSSTPGRRKPRVHRPRSPILEEKDIPPLEFPKSSEDLMVPNEHIMNVIAIYEVVRNFGNVLRLSPFCFEDFCAALVSQEQCTLMAEMHVALLKAVLREEDTSNTTFGPADLKDSVNSTLYFIDGMTWPEVLRVYCESDKEYHHVLPYQEAEDYPYGPVENKIKVLQFLVDQFLTTNIAREELMSEGVIQYDDHCRVCHKLGDLLCCETCSAVYHLECVKPPLEEVPEDEWQCEVCVAHKVPGVTDCVAEVQKNKPYVRHEPIGYDRSRRKYWFLNRRLIIEEDTDNENEKKVWYYSTKVQLAELIDCLDKGYWEAELCRVLEDIREEMQQHMDVTEDLTNKARGSNKSFLAAANEEILDSLRIKRGEDIDCDQSPEDPEKDKHEGENNSSKDAEKSREEAEDPSADKDADSKGLEEEPGHGKPEEDSNRTCDSSNTSATTASSQPNLETCSSSELTSSQSDSAKAADDPEIGERDSHTPVSVHEEIGDFRLEKSNGEVSESPGAGKGTSGSTRIITRLRNPESKLSQLKSQQVAAAAHEANKLFKEGKEVLVVNSQGEVSRLSTKKEVVMKGNINNYFKLGQEGKYRVYHNQYSTNSFALNKHQHREDHDKRRHLAHKFCLTPAGEFKWNGSVHGSKVLTISTLRLTITQLESNIPSSFLHPNWASHRANWIKAVQMCSKPREFALALAILECAVKPVVMLPIWRESLGHTRLHRMTSIEREEKEKVKKKEKKQEEEETMQQATWVKYTFPVKHQVTGYGGWSWISKTHVYRFLPKLPGNTNVNYRKPLDGAKNNTDENKDESEKRKSPRSPKKMKTECDSEQGETRDADATAGAAAGAMELSKEPEKKDQDVKELLDSDNDKSFKEEPMEIDDTIKTESHVSSLESTEVDVVNVSEGFHLRTSYKKKTKSSKLDGLLERRIRQFTLEEKQRLEKLKLESGVKGAGKPPMGALKSSSESPGSTKASEGHQGDSLRQEQSPSSSQASTVDLGLGGSQSDPLVLGISPPSLSTHKPDPKDQVLDDVSIQSPGPNCQRQNSVESDLDARISEPAGKGLELSQTKTEVTDSSSDDSKPTSADDVGILICKSRKLHSQDDSSTVVSSSKSTLPASVPKSPRDRDARAFSKAVDFDGRLGGDSEYSSTLENSSDNMCIRDSAEEDMVVQNSSEATSKRFIAPEQGGESVESTKCQVVSKSTENCEDKLQGKVTEANGKKLGQHPPKPEERAVNRCTDQVSLRHSVDRKNSEPRESEKKGQKANKFQINGKDSKAKGYLKGPGTKDGSDGKVVSSAVEPKVNNINKVIPGNTKSLAGKESAAKPFINGDIIMEELSEQNTSETNSYSLSSSDAKGNHQDGLHTLPSTKESASTQVITPRAPCPDRNSLSQVEDMETESPEVKRVIPSPVRTGEGSNLSKGFMDDNGLPSSKDENVNGESQRKTVITEVTTMTSTVATESKTVIKVAKGDKQTVVSSTENCARSTVTTTTTTVTKLSTPSPDTGVDTISVKEQSKTVVTTTVTDSLTTAGSTLVTSMTVSKEYSTRDRVKLMKFSRPKKTRSGTALPSYRKFVTKSSKKSIFVLPNDDLKKLARKGGIREVPYFNYNAKPALDIWPYPSPRPTFGITWRYRLQTVKSLAGVSLMLRLLWASLRWDDMAAKAPPGGGSTRTETSETEITTTEIIKRRDVGPYGIRSEYCIRKIICPIGVPEAPKETPTPQRKGLRSSALRPKRPETPKQTGPVIIESWVAEEELELWEIRAFAERVEKEKAQAAEQQTKKRLEQQKPAVIAASTTSPANNTSSTVSPAQKVMVAPLSGSVTPGTKMVLATKVGSPATVTFQQNKNFHQTFATWVKQGQSNSGMVQVQQKVLGIIPSTTGPSQQTFTSFQPRTATVTIRPNTSASAGTTTTSQVITGPQIRPGMTVIRTPLQQPALGKAIIRTPVVVQPGTPQQVVTQIIRGQPVSTAISAPSTASSAPVQKGLTPGAAAGPLQPSAPHSPRPQQGQVKLTMAQLTQLTQGHGGNQGLTVVIQGQGQTTGQLQLIPQGMTVLPGPGQQLMQAAMPNGTVQRFLFTPLSTSATAASSSSNSSSTTTNATAAGSGEQKQSKILPQTQVQPATTLAPTQSSSVSPAEAQPQPAQPAAQPQPQPQPPAQPEVQTQPAVSSHVPSETQPSQAQTSKPLVATQCQPQSSVQGQSPVRVQSPPLTRIRPSTPSQVTPGQQPQVQTTASQPIPIPPPTSLQAPSQGQPQSQPQVQSSTQTLSSGQTLNQVTVLSPSCPQPQPQVIAVPQLQQVQVLSQIQSQVVAQIQAQQSGVPQQIKLQLPIQVQQNSAAQTQSVVTVQAASVQEQLQRVQQLRDQQQKKKQQIETEREHTLQASNQSEIIQKQVVMKHNAVIEHLKQKKTMTPAEREENQRMIVCNQVMKYILDKIDKEEKQAAKKRKREESVEQKRSKQNASKLSALLFKHKEQLKAEILRKRALLDKELQIQVQEELKRDLKMKREREMAQAVQANAASVPTPSVPAPVPAPAPAAPPAPPRSPPPSTHSLPPAGHPTAPLPVTSQKRKREEEKDSKSKKKKMISTTSKEAKKDTRLYCICKTPYDESKFYIGCDRCQNWYHGRCVGILQSEADLIDEYVCPQCQSTEDAMTVLTPLTEKDYEGLKRVLRSLQAHKMAWPFLEPVDPNDAPDYYGVIKEPMDLATMEERIQKRYYEKLTEFVADMTKIFDNCRYYNPRDTPFYQCAEVLESFFVQKLKGFKASRSHNNKLQSTAP