wanglab/gogpt-training-data huggingface dataset:
Protein: Formate dehydrogenase 1 (FDH) (EC 1.17.1.9) (NAD-dependent formate dehydrogenase) (Q08911)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the NAD(+)-dependent oxidation of formate to carbon dioxide. Formate oxidation is the final step in the methanol oxidation pathway in methylotrophic microorganisms. Has a role in the detoxification of exogenous formate in non-methylotrophic organisms.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000269|PubMed:11921099}.
Interaction partners:
- S-formylglutathione hydrolase
- Fumarate hydratase, mitochondrial
- Malate dehydrogenase, mitochondrial
- Malate dehydrogenase, peroxisomal
- Kynurenine formamidase
- NAD-dependent malic enzyme, mitochondrial
- Malate synthase 1
- Malate dehydrogenase, cytoplasmic
- Malate synthase 2
- Pyruvate carboxylase 2
Sequence:
MSKGKVLLVLYEGGKHAEEQEKLLGCIENELGIRNFIEEQGYELVTTIDKDPEPTSTVDRELKDAEIVITTPFFPAYISRNRIAEAPNLKLCVTAGVGSDHVDLEAANERKITVTEVTGSNVVSVAEHVMATILVLIRNYNGGHQQAINGEWDIAGVAKNEYDLEDKIISTVGAGRIGYRVLERLVAFNPKKLLYYDYQELPAEAINRLNEASKLFNGRGDIVQRVEKLEDMVAQSDVVTINCPLHKDSRGLFNKKLISHMKDGAYLVNTARGAICVAEDVAEAVKSGKLAGYGGDVWDKQPAPKDHPWRTMDNKDHVGNAMTVHISGTSLDAQKRYAQGVKNILNSYFSKKFDYRPQDIIVQNGSYATRAYGQKK
Protein: Vitellogenin-2 (P05690)
Organism: Caenorhabditis elegans
Function: Precursor of the egg-yolk proteins that are sources of nutrients during embryonic development (Probable). Together with other vitellogenins, may play a role in modulating life-span, acting via induction of autophagy and lysosomal lipolysis.
Subcellular location: Secreted {ECO:0000305|PubMed:26671266}.
Interaction partners:
- Vitellogenin-5
- Vitellogenin-6
- Vitellogenin-4
- EGF-like domain-containing protein
- Secreted protein
- DUF1525 domain-containing protein
- Microsomal triglyceride transfer protein homolog
- Vitellogenin-1
- Chitinase-like protein C25A8.4
Sequence:
MRSIIIASLVALALASSPAFERTFEPKTDYHYKFDGLVLSGLPSASSELSQSRISARARIQAVDDRYIHLQLVNIRMAASHLPESEQMPSLNSMEQRELSEEYKQMLELPLRAQLRNGLISELQFDKEDAEWSKNMKRAVVNMISFNPIAPRNEIEKIESSYDKEEQSEENTSFFTNEKTLEGDCQVAYTVIREQKKTIITKSINFDKCTERSEIAYGLRYSSECPECEKDTELIRPQTVYTYVLENEELKESEVRSLYTVNVNGQEVMKTETRSKLVLEENHSIKSHIKKVNGEKESIIYSSRWEQLVEDFFKNGDKAEFAPFEKFPLDKKMHLIKTITEQIQEVENNMPETSHFLARLVRIFRTTSTSQLKEIHETLYVKADKKIQSLMEHALAIAGTKNTIQHILVHMENEDILPLGQILKTIQETPFPSQSIAEALIKFAESRVAKNNLVVRQAAWLAAGSVVRGIVDYKNIRPLVREDKRELKEKFLRVFMQQYKDAETTYEKILALKTIGNAGLDISVNQLNEIIVDKRQPLPVRKEAIDALRLLKDTMPRKIQKVLLPIYKNRQYEPEIRMLALWRMMHTRPEESLLVQVVSQMEKETNQQVAALTHQMIRHFAMSTNPCYQRVAIVCSKVLSFTRYQPQEQMIASSYAQLPLFLQNSFSGAQFDFAAIFEKNSFLPKDLHASLDAVFGGNWNKYFAQIGFSQQHMDKYVQMALEKLESLEKESTTVVRGRRIQTGIKLLKELAQKMNIRARPATYTEKDAFAMVYLRYKDMDYAFLPIDRQLVENLIEKFTSNGKVQFSEIRRLLNQELEFETHHAAYFYEAIRKFPTTLGLPLTISGKIPTVISAEGQFSLELEGTELRLTVEARPSVAATHVYEMRMFTPLFEQGVKSVQSVRAYTPIKIQAVAGMKRNFEIVYKVVVPENQKSIVSLTTRPVVFLRFPGFSKFEYIEAEERTVVVPQWQQKTQEIEKVFNFLGLEVSTRGNILNQHTLENWLLAEQDFEVSVENKNRPAEFTARLTVGQLEKTELSQIKYNKIFEKEFELEQENTESRREYFNKMVKNIQKEQGYKSVISLKLEAPRDYTMNTELTTVCDKQVRMCQWEVEIRRSPILEETKEWTLRSQLLVVRPEMPSSLRQLRDQPHREVQLSLTSTWGSQKKSEVTVNAQLQQSKEQKKYERNMDRQFNGMPEYELLIKAARLNQINAVAEYKLTRETEQVLARYFDLVKTYNYWTVSSRPENNENDRVVVQLTVEPMSRQYVNITMQSPMERIELKNVQVPRVYLPSIAQRSVKHQLTEASGSVCKVQKNQIRTFDDVLYNTPLTTCYSLIAKDCSEEPTFAVLSKKTEKNSEEMIIKVIRGEQEIVAQLQNEEIRVKVDGKKIQSEDYSAYQIERLGESAIVIELPEGEVRFDGYTIKTQLPSYSRKNQLCGLCGNNDDESTNEFYTSDNTETEDIEEFHRSYLLKNEECEAEEERLSEKKNYRKYERDEEQSDEYSSEETYDYEQENTKKSQKNQRSQKKSDLVEKTQIKEFSHRICFSVEPVAECRRGYEVEQQQQRKIRFTCLQRHNRDASRLLKESRQQPLQLDDYPVSFVESVKVPTACVAY
Protein: E3 ubiquitin-protein ligase ATL42 (EC 2.3.2.27) (RING-H2 finger protein ATL42) (RING-type E3 ubiquitin transferase ATL42) (Q5XF85)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin-protein ligase able to catalyze polyubiquitination with ubiquitin-conjugating enzyme E2 UBC8 in vitro.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- RING/FYVE/PHD zinc finger superfamily protein
- U-box domain-containing protein 15
- UDP-glycosyltransferase 82A1
Sequence:
MYQIFFFFLPLLHSYASAQTPPPFRNGDLVANFEPSLAVVTGVLAIMFALTFVLLVYAKCCHIDLRSGSGDRRRHDRRLRQGIFFNRSTASSDRFSGLDKTAIESLPLFRFSALKGSKQGLDCSVCLSKFESVEILRLLPKCRHAFHIGCIDQWLEQHATCPLCRDRVSMEEDSSVLTNGNSFRFLNQSEIREDSSLELYIEREEEEERIHREELSGSSRFSIGESFRKILKLGNKEKTLLDEHVNDKDEKKLMHKFNHRIVVSDVVFKNRWSNVSSSDLMFLNSEMVNSISSERFSSLDHVKRGDEEDQIGILRIKEEMEAKRMLENKLTSMTTMFSSENGDSGSKSRSVMIEPGRRSVSDITAVPRLSISIHGDCSGSAAETASALQNGGNETEERRRRLWLPIARKTAQWFANREKRSQINTTHQHFDV
Protein: Guanylate kinase (EC 2.7.4.8) (GMP kinase) (P60546)
Organism: Escherichia coli (strain K12)
Function: Essential for recycling GMP and indirectly, cGMP.
Subcellular location: Cytoplasm.
Interaction partners:
- DNA-directed RNA polymerase subunit omega
- GMP synthase
- Bifunctional
- Xanthine-guanine phosphoribosyltransferase
- Hypoxanthine phosphoribosyltransferase
- Adenine phosphoribosyltransferase
- Nucleoside diphosphate kinase
- GMP reductase
- Guanosine-inosine kinase
- Triosephosphate isomerase
Sequence:
MAQGTLYIVSAPSGAGKSSLIQALLKTQPLYDTQVSVSHTTRQPRPGEVHGEHYFFVNHDEFKEMISRDAFLEHAEVFGNYYGTSREAIEQVLATGVDVFLDIDWQGAQQIRQKMPHARSIFILPPSKIELDRRLRGRGQDSEEVIAKRMAQAVAEMSHYAEYDYLIVNDDFDTALTDLKTIIRAERLRMSRQKQRHDALISKLLAD
Protein: Pentatricopeptide repeat-containing protein At5g10690 (CBS domain-containing protein CBSPPR1) (Q8VYD6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Probable arabinose 5-phosphate isomerase
- Putative DUF21 domain-containing protein At3g13070, chloroplastic
- At1g29530
- Polyketide cyclase/dehydrase and lipid transport superfamily protein
- 25S rRNA
- Secreted protein
- DUF21 domain-containing protein At4g14240
- CBS domain-containing protein CBSCBSPB4
- CBS domain-containing protein CBSCBSPB5
- CBS domain-containing protein CBSCBSPB2
Sequence:
MNRISAISTLVTPLPLLPSCSFVPTRRCYPRRATPYSRRINLKPLTSRIVLLTRRRQLGQIVEEVEAAKKRYGRLNTIVMNSVLEACVHCGNIDLALRMFHEMAEPGGIGVDSISYATILKGLGKARRIDEAFQMLETIEYGTAAGTPKLSSSLIYGLLDALINAGDLRRANGLLARYDILLLDHGTPSVLIYNLLMKGYVNSESPQAAINLLDEMLRLRLEPDRLTYNTLIHACIKCGDLDAAMKFFNDMKEKAEEYYDDFLQPDVVTYTTLVKGFGDATDLLSLQEIFLEMKLCENVFIDRTAFTAVVDAMLKCGSTSGALCVFGEILKRSGANEVLRPKPHLYLSMMRAFAVQGDYGMVRNLYLRLWPDSSGSISKAVQQEADNLLMEAALNDGQLDEALGILLSIVRRWKTIPWTTSGGMAAVRLETLLGFSKSILRPHLLSKVIPSEPIESIMIRFEATRPLLGTLQLKNVAMRFFKEQVVPIVDDRGSCIGLLHREDCNNLDAPLVSMMRSPPTCVSTTTSIGRVVDLVLEKKLKMVIVVHCGNFSGSGYSSKAVGAFTRAQLYRLFESEQKLL
Protein: Type II secretion system protein K (T2SS protein K) (General secretion pathway protein K) (Q00518)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Plays a role in pseudopilus assembly and seems to control its length. Interacts with the pseudopilus tip complex that is critical for the recognition and binding of secretion substrates. Type II pseudopilus confers increased bacterial adhesive capabilities.
Subcellular location: Cell inner membrane {ECO:0000305}.
Interaction partners:
- Type II secretion system protein I
- Type II secretion system protein J
- Type II secretion system protein H
- Type II secretion system core protein G
- Type II secretion system protein L
- Type II secretion system protein E
- Type II secretion system protein M
- Type II secretion system protein F
- Secretin XcpQ
- Type II secretion system protein K
Sequence:
MRRGQNGVALITVLLVVAVVTIVCAGLIIRQQLAIRSSANQLHVRQAWHYALGGERLAEAVLRRDLRQGGENTREPVDHLGEAWARPMTPFKLDDGGELRVRIEDPSGRFNLNGLVRKRKVKPDSVKQFRRLLATLGMKEEIVQGLPDRLADWLDADQNPQGEQGAEDNQYLLEAPAYRAANRSFKDVSELRLLKLSEADYRRLLPFVSALPEDAPLNVNTASVPVLAAMFEIDPGQAENIVDARGREGFQSKDDFTKHLTQLGSKTGNVSYAVGTRYFQVISEVSLGDRRQVLVSTLQRGKDGKIRVMARDMGQGGLPIPSTGGDDWKKDER
Protein: Ecotin-like protein 3 (Q4QFD3)
Organism: Leishmania major
Interaction partners:
Sequence:
MPSLQDYHVPYPAAAPGQVRKVIYLPRQNPTVEQQHLRVQIIPGRHENCDDGRLYKLTGSVTEETLQGWGYSYYVVTLGDIYAAHRSSSDPARATTFVALDESPVIAYNSKLPIVVYVPEGAELRYRIWTDDASLAQSIQQKPEAPALPQPHLVPVTEGQECPQELPRCGAPSEYVRQDYKASMLSVEEVHRLSNNTPPLIPSAVHESAHEAHAAPPLHSAVLEEHGRPGMEHLEVCPKNNGSEGREQPAEEASTLKQRSSSSSSNPRHHSANESSPSRPRLSSTAYWPQENSKTKRSPSATHKPRRSTDSAAIEETGVGTPKKNRSSSGSASNKRKAEDDVYEKTMKNFWNRARSDSPRKASASSTKSGNGSKADPVDGK
Protein: Cell division cycle 5, isoform A (Cell division cycle 5, isoform B) (LD21614p) (Q9W0R0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Pleiotropic regulator 1
- Pre-mRNA-processing factor 19
- Pre-mRNA-splicing factor syf1 homolog
- Puff-specific protein Bx42
- Pre-mRNA-splicing factor SPF27
- RE31520p
- Protein CWC15 homolog
- RNA helicase aquarius
- Pre-mRNA-processing factor 17
- Pre-mRNA-splicing factor Syf2
Sequence:
MPRIMIKGGVWRNTEDEILKAAVMKYGKNQWSRIASLLHRKSAKQCKARWYEWLDPSIKKTEWSREEDEKLLHLAKLMPTQWRTIAPIIGRTAAQCLERYEYLLDQAQRKEDGEDTMDDPRKLKPGEIDPNPETKPARPDPKDMDEDELEMLSEARARLANTQGKKAKRKAREKQLEEARRLATLQKRRELRAAGIGSGNRKRIKGIDYNAEIPFEKRPAHGFYDTSEEHLQKNEPDFNKMRQQDLDGELRSEKEERERKRDKQKLKQRKENEVPTAMLQNMEPERKRSKLVLPTPQISDMELQQVVKLGRASEMAKEIAGESGIETTDALLADYSITPQVAATPRTPAPYTDRIMQEAQNMMALTHTETPLKGGLNTPLHESDFSGVLPKAASIATPNTVIATPFRTQREGGAATPGGFQTPSSGALVPVKGAGGATGVVNTPAYVRDKLSINPEESMGVTETPAHYKNYQKQLKSTLRDGLSTLPAPRNDYEIVVPEQEESERIETNSEPAVEDQADVDARLLAEQEARRKRELEKRSQVIQRSLPRPTEVNTKILRPQSEKQNLTEQQQAEELIKHEMITMQLYDSVKDPVPGQSQHKLEQLQSYFKANPYEDISQQELAKAKQMLTEEMEVVKERMAHGELPLDVYAQVWQECLGQVLYLPSQHRYTRANLASKKDRLESAEKRLETNRRHMAKEAKRCGKIEKKLKILTGGYQARAQVLIKQLQDTYGQIEQNSVSLSTFRFLGEQEAIAVPRRLESLQEDVRRQMDREKELQQKYASLVEERDSLYSQIEHITGVRPTAQQLLPDQEA
Protein: Homeobox protein Hox-A4 (Homeobox protein Hox-1.4) (Homeobox protein MH-3) (P06798)
Organism: Mus musculus (Mouse)
Function: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Binds to sites in the 5'-flanking sequence of its coding region with various affinities. The consensus sequences of the high and low affinity binding sites are 5'-TAATGA[CG]-3' and 5'-CTAATTTT-3'.
Subcellular location: Nucleus.
Interaction partners:
- Homeobox protein Hox-A3
- Homeobox protein Hox-A2
Sequence:
MTMSSFLINSNYIEPKFPPFEEFAPHGGPGGGDGAVGGGPGYPRPQSAPHLPAPNPHAARQPPAYYAPRAREPSYPGGLYPAPAAACPYACRGASPGRPEQSPAPGAHPSPAPQPPVPLGHCAPGPTTPAVATGGSAPACPLLLADQGPAGPKGKEPVVYPWMKKIHVSAVNSSYNGGEPKRSRTAYTRQQVLELEKEFHFNRYLTRRRRIEIAHTLCLSERQVKIWFQNRRMKWKKDHKLPNTKMRSSNTASAPAGPPGKAQTHSPHHHPHPLPGASTPIPSSI
Protein: Sorting nexin/Vps5-like C-terminal domain-containing protein (D9PTP8)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MFKLKKVESRSSNDEELKLGDTLHYFARDTQAAKDLLYRRMRCLANYEAANKNLERARAKNREIPKAEAEQSEACKKFEEITGLSKNELKELKTRRVQAFKKNLTDLAELEIKHSKAEISLLRDVVERLKSSQ
Protein: Draculin-like, tandem duplicate 3 (B0R156)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- GATA-binding protein 1b.
Sequence:
MEIEESENMKDTTEPCRTEHCDDTEGQRDHMEGNKEGETEAKKSVACFHCKKRFTCKAHLQVHMRVHNKKKQKDRKATAEKLHTCDKSGKSFAYKSSLKKHMINHSGEKKHTCDQCGKSFPFKVYLEQHMLIHTGETLHECDQCGKSFRSKGEVKIHMLIHTGEKPHKCDQCGKSFRSKGEVKIHMLIHTGEKPHECDQCGKSFRSKGEVKIHMLIHTRKKPHECDQCGKSFRSKGEVKQHMSIHTGLKPYKCEECGKFFAQKNNLQVHMKVHTGEKPYRCDQCGKCFPYKQSLKLHLEIHAKGNPYTCDECGKSFKTCLQFRSHMTLHPEYKPYKCDQCEKSYGREDHLQRHMKLHTGEKPHKCEHCGKSFPMRDLLRSHLMVHREVKPYTCDQCGKGFTLKKCYNEHMNIHTGERPYTCDQCGKGFPYEQSLNLHMRFHRGEKPFTCDQCGQSFSQKGAYNIHMKIHTGEKPYTCDQCGMSFRHGSSLKLHMTHHTGEKPFHCDQCDKCYSTALFLKNHMKTHNKDQIYSCLTCGKTFNLLGCLRMHEKRHTLVKPFMCFDCGKCYFTDTELKQHLSVHSNERPYMCSLCFKSFSRMDSLKKHEKTHNRKIQNHHHDEGEHDQTSLLKG
Protein: Pyrin and HIN domain-containing protein 1 (Interferon-inducible protein 209) (Ifi-209) (Interferon-inducible protein X) (Interferon-inducible protein p209) (Q8BV49)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MVNEYKRIVLLTGLMGINDHDFRMVKSLLSKELKLNRMQDQYDRVKIADLMEDKFPKDAGVDQLIKLYKQIPGLGDIANKLKNEKAKAKRTRTGKRKTAAKRQRQEEPSTSQPMSTTNEDAEPESGRSTPDTQVAQLSLPTASRRNQAIQISPTIASSSGQTSSRSSETLQSIIQSPKTPKRPSSSILDPPVSSGTASSSAQALGVPLATIAKRQRLKNVPKEPSEENGHQQGSKKVMVLKVTEPFSYDVTEEKMFHATVATETEFFRVKVFDIVLKEKFIPNKVLTISNYVGCNGFINIYSASSVSEVNDGEPMNIPLSLRKSANRTPKINYLCSKKRGIFVNGVFTVCKKEEKWNYICYEIGDDTGMMEVEVYGRLTNIACNPGDKLRLICFKLIPDEEKAQLRSTTHSNMQVIKAKN
Protein: Photosystem I reaction center subunit IX (PSI-J) (Q6ENF3)
Organism: Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea)
Function: May help in the organization of the PsaE and PsaF subunits.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00522}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00522}.
Interaction partners:
- Photosystem I reaction center subunit VIII
- Photosystem I reaction center subunit psaK, chloroplastic
- Chlorophyll a-b binding protein
- Photosystem I iron-sulfur center
- Chlorophyll a-b binding protein
- Photosystem I P700 chlorophyll a apoprotein A2
- Chlorophyll a-b binding protein
- Photosystem I P700 chlorophyll a apoprotein A1
- Photosystem I reaction center subunit III
- Photosystem I reaction center subunit XI, chloroplastic
Sequence:
MRDIKTYLSVAPVLSTLWFGALAGLLIEINRLFPDALSFPFFSF
Protein: Nucleoside diphosphate kinase, mitochondrial (NDK) (NDP kinase, mitochondrial) (EC 2.7.4.6) (Nucleoside diphosphate kinase D) (NDPKD) (nm23-H4) (O00746)
Organism: Homo sapiens (Human)
Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Through the catalyzed exchange of gamma-phosphate between di- and triphosphonucleosides participates in regulation of intracellular nucleotide homeostasis. Binds to anionic phospholipids, predominantly to cardiolipin; the binding inhibits its phosphotransfer activity. Acts as mitochondria-specific NDK; its association with cardiolipin-containing mitochondrial inner membrane is coupled to respiration suggesting that ADP locally regenerated in the mitochondrion innermembrane space by its activity is directly taken up via ANT ADP/ATP translocase into the matrix space to stimulate respiratory ATP regeneration. Proposed to increase GTP-loading on dynamin-related GTPase OPA1 in mitochondria. In vitro can induce liposome cross-linking suggesting that it can cross-link inner and outer membranes to form contact sites, and promotes intermembrane migration of anionic phosphoplipids. Promotes the redistribution of cardiolipin between the mitochondrial inner membrane and outer membrane which is implicated in pro-apoptotic signaling.
Subcellular location: Mitochondrion intermembrane space {ECO:0000269|PubMed:18635542}; Peripheral membrane protein. Mitochondrion matrix {ECO:0000305|PubMed:18635542}. Note=Predominantly localized in the mitochondrion intermembrane space (PubMed:18635542). Colocalizes with OPA1 in mitochondria (PubMed:24970086). {ECO:0000269|PubMed:18635542, ECO:0000269|PubMed:24970086}.
Interaction partners:
- Nucleoside diphosphate kinase A
- GTP:AMP phosphotransferase AK3, mitochondrial
- UMP-CMP kinase 2, mitochondrial
- Thymidylate kinase
- Nucleoside diphosphate kinase
- Inosine triphosphate pyrophosphatase
- Nucleoside diphosphate kinase 3
- Guanylate kinase
- Adenylate kinase 9
- Guanosine-3',5'-bis
Sequence:
MGGLFWRSALRGLRCGPRAPGPSLLVRHGSGGPSWTRERTLVAVKPDGVQRRLVGDVIQRFERRGFTLVGMKMLQAPESVLAEHYQDLRRKPFYPALIRYMSSGPVVAMVWEGYNVVRASRAMIGHTDSAEAAPGTIRGDFSVHISRNVIHASDSVEGAQREIQLWFQSSELVSWADGGQHSSIHPA
Protein: Phosphatidylinositol-4-phosphate 3-kinase, catalytic subunit type 2 alpha (L7RRS0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAQISSNSGFKECPSSHPEPTRAKDVDKEEALQMEAEALAKLQKDRQVTDNQRGFELSSSTRKKAQVYNKQDYDLMVFPESDSQKRALDIDVEKLTQAELEKLLLDDSFETKKTPVLPVTPILSPSFSAQLYFRPTIQRGQWPPGLPGPSTYALPSIYPSTYSKQAAFQNGFNPRMPTFPSTEPIYLSLPGQSPYFSYPLTPATPFHPQGSLPIYRPVVSTDMAKLFDKIASTSEFLKNGKARTDLEITDSKVSNLQVSPKSEDISKFDWLDLDPLSKPKVDNVEVLDHEEEKNVSSLLAKDPWDAVLLEERSTANCHLERKVNGKSLSVATVTRSQSLNIRTTQLAKAQGHISQKDPNGTSSLPTGSSLLQEVEVQNEEMAAFCRSITKLKTKFPYTNHRTNPGYLLSPVTAQRNICGENASVKVSIDIEGFQLPVTFTCDVSSTVEIIIMQALCWVHDDLNQVDVGSYVLKVCGQEEVLQNNHCLGSHEHIQNCRKWDTEIRLQLLTFSAMCQNLARTAEDDETPVDLNKHLYQIEKPCKEAMTRHPVEELLDSYHNQVELALQIENQHRAVDQVIKAVRKICSALDGVETLAITESVKKLKRAVNLPRSKTADVTSLFGGEDTSRSSTRGSLNPENPVQVSINQLTAAIYDLLRLHANSGRSPTDCAQSSKSVKEAWTTTEQLQFTIFAAHGISSNWVSNYEKYYLICSLSHNGKDLFKPIQSKKVGTYKNFFYLIKWDELIIFPIQISQLPLESVLHLTLFGILNQSSGSSPDSNKQRKGPEALGKVSLPLFDFKRFLTCGTKLLYLWTSSHTNSVPGTVTKKGYVMERIVLQVDFPSPAFDIIYTTPQVDRSIIQQHNLETLENDIKGKLLDILHKDSSLGLSKEDKAFLWEKRYYCFKHPNCLPKILASAPNWKWVNLAKTYSLLHQWPALYPLIALELLDSKFADQEVRSLAVTWIEAISDDELTDLLPQFVQALKYEIYLNSSLVQFLLSRALGNIQIAHNLYWLLKDALHDVQFSTRYEHVLGALLSVGGKRLREELLKQTKLVQLLGGVAEKVRQASGSARQVVLQRSMERVQSFFQKNKCRLPLKPSLVAKELNIKSCSFFSSNAVPLKVTMVNADPMGEEINVMFKVGEDLRQDMLALQMIKIMDKIWLKEGLDLRMVIFKCLSTGRDRGMVELVPASDTLRKIQVEYGVTGSFKDKPLAEWLRKYNPSEEEYEKASENFIYSCAGCCVATYVLGICDRHNDNIMLRSTGHMFHIDFGKFLGHAQMFGSFKRDRAPFVLTSDMAYVINGGEKPTIRFQLFVDLCCQAYNLIRKQTNLFLNLLSLMIPSGLPELTSIQDLKYVRDALQPQTTDAEATIFFTRLIESSLGSIATKFNFFIHNLAQLRFSGLPSNDEPILSFSPKTYSFRQDGRIKEVSVFTYHKKYNPDKHYIYVVRILREGQIEPSFVFRTFDEFQELHNKLSIIFPLWKLPGFPNRMVLGRTHIKDVAAKRKIELNSYLQSLMNASTDVAECDLVCTFFHPLLRDEKAEGIARSADAGSFSPTPGQIGGAVKLSISYRNGTLFIMVMHIKDLVTEDGADPNPYVKTYLLPDNHKTSKRKTKISRKTRNPTFNEMLVYSGYSKETLRQRELQLSVLSAESLRENFFLGGVTLPLKDFNLSKETVKWYQLTAATYL
Protein: Terephthalate 1,2-dioxygenase, terminal oxygenase component subunit alpha 2 (TPADO terminal oxygenase component) (EC 1.14.12.15) (TER dioxygenase system) (TERDOS) (Terephthalate 1,2-dioxygenase large subunit 2) (Q3C1D5)
Organism: Comamonas sp
Function: Component of the terephthalate 1,2-dioxygenase multicomponent enzyme system which catalyzes the dioxygenation of terephthalate (TER/TPA) to 1,2-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylic acid (DCD). It can also use 2,5-dicarboxypyridine (PDC) and 1,4-napthalenedicarboxylic acid (NDC) as substrates, and preferentially uses NADPH which is the physiological electron donor.
Interaction partners:
Sequence:
MQESIIQWHGATNTRVPFGIYTDTANADQEQQRIYRGEVWNYLCLESEIPGAGDFRTTFAGETPIVVVRDADQEIYAFENRCAHRGALIALEKSGRTDSFQCVYHAWSYNRQGDLTGVAFEKGVKGQGGMPASFCKEEHGPRKLRVAVFCGLVFGSFSEDVPSIEDYLGPEICERIERVLHKPVEVIGRFTQKLPNNWKLYFENVKDSYHASLLHMFFTTFELNRLSQKGGVIVDESGGHHVSYSMIDRGAKDDSYKDQAIRSDNERYRLKDPSLLEGFEEFEDGVTLQILSVFPGFVLQQIQNSIAVRQLLPKSISSSELNWTYLGYADDSAEQRKVRLKQANLIGPAGFISMEDGAVGGFVQRGIAGAANLDAVIEMGGDHEGSSEGRATETSVRGFWKAYRKHMGQEMQA
Protein: Formate channel FocA (Formate transporter FocA) (P0AC25)
Organism: Escherichia coli O157:H7
Function: Involved in the bidirectional transport of formate during mixed-acid fermentation. Functions to maintain relatively constant intracellular formate levels during growth, using different mechanisms for efflux and uptake of the anion (By similarity). Is impermeable to water.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:19940917}; Multi-pass membrane protein {ECO:0000269|PubMed:19940917}.
Interaction partners:
- Formate acetyltransferase
- Formate acetyltransferase
Sequence:
MKADNPFDLLLPAAMAKVAEEAGVYKATKHPLKTFYLAITAGVFISIAFVFYITATTGTGTMPFGMAKLVGGICFSLGLILCVVCGADLFTSTVLIVVAKASGRITWGQLAKNWLNVYFGNLVGALLFVLLMWLSGEYMTANGQWGLNVLQTADHKVHHTFIEAVCLGILANLMVCLAVWMSYSGRSLMDKAFIMVLPVAMFVASGFEHSIANMFMIPMGIVIRDFASPEFWTAVGSAPENFSHLTVMNFITDNLIPVTIGNIIGGGLLVGLTYWVIYLRENDHH
Protein: Uncharacterized oxidoreductase YbbO (EC 1.-.-.-) (P0AFP4)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Thioesterase 1/protease 1/lysophospholipase L1
- Chaperedoxin
- Aldehyde reductase YahK
- Aldehyde reductase Ahr
Sequence:
MTHKATEILTGKVMQKSVLITGCSSGIGLESALELKRQGFHVLAGCRKPDDVERMNSMGFTGVLIDLDSPESVDRAADEVIALTDNCLYGIFNNAGFGMYGPLSTISRAQMEQQFSANFFGAHQLTMRLLPAMLPHGEGRIVMTSSVMGLISTPGRGAYAASKYALEAWSDALRMELRHSGIKVSLIEPGPIRTRFTDNVNQTQSDKPVENPGIAARFTLGPEAVVDKVRHAFISEKPKMRYPVTLVTWAVMVLKRLLPGRVMDKILQG
Protein: Neuroserpin (Peptidase inhibitor 12) (PI-12) (Serpin I1) (Q99574)
Organism: Homo sapiens (Human)
Function: Serine protease inhibitor that inhibits plasminogen activators and plasmin but not thrombin. May be involved in the formation or reorganization of synaptic connections as well as for synaptic plasticity in the adult nervous system. May protect neurons from cell damage by tissue-type plasminogen activator (Probable).
Subcellular location: Secreted {ECO:0000269|PubMed:17040209, ECO:0000269|PubMed:25326458}. Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000305|PubMed:17040209}. Perikaryon {ECO:0000269|PubMed:17040209}.
Interaction partners:
- Tissue-type plasminogen activator
Sequence:
MAFLGLFSLLVLQSMATGATFPEEAIADLSVNMYNRLRATGEDENILFSPLSIALAMGMMELGAQGSTQKEIRHSMGYDSLKNGEEFSFLKEFSNMVTAKESQYVMKIANSLFVQNGFHVNEEFLQMMKKYFNAAVNHVDFSQNVAVANYINKWVENNTNNLVKDLVSPRDFDAATYLALINAVYFKGNWKSQFRPENTRTFSFTKDDESEVQIPMMYQQGEFYYGEFSDGSNEAGGIYQVLEIPYEGDEISMMLVLSRQEVPLATLEPLVKAQLVEEWANSVKKQKVEVYLPRFTVEQEIDLKDVLKALGITEIFIKDANLTGLSDNKEIFLSKAIHKSFLEVNEEGSEAAAVSGMIAISRMAVLYPQVIVDHPFFFLIRNRRTGTILFMGRVMHPETMNTSGHDFEEL
Protein: Xanthan lyase (EC 4.2.2.12) (Q9AQS0)
Organism: Bacillus sp. (strain GL1)
Function: Plays a role in xanthan depolymerization pathway by cleaving the linkage between the terminal mannosyl and glucuronyl residues of the side chain of xanthan to liberate pyruvylated mannose. Is highly specific for pyruvylated side-chains of xanthan and is not effective with hyaluronate, chondroitin A, gellan, heparin or pectin.
Subcellular location: Secreted {ECO:0000269|PubMed:9758797}.
Interaction partners:
Sequence:
MLSGILIAALLMTLWGGWQPDIAHASDEFDALRIKWATLLTGGPALDPADSDIAARTDKLAQDANDYWEDMDLSSSRTYIWYALRGNGTSDNVNAVYERLRTMALAATTVGSSLYGNADLKEDILDALDWLYVNSYNSTRSRSAYNWWHWQLGIPMSLNDIAVLLYDDISAARMATYMDTIDYFTPSIGLTGANRAWQAIVVGVRAVIVKDAVKLAAARNGLSGTGIFPYATGGDGFYADGSFVQHTTFAYTGGYGSSVLETTANLMYLLSGSTWSVSDPNQSNVWQWIYEAYRPLLYKGAMMDMVRGREISRSYAQDHAVGHGIVASIVRLAQFAPAPHAAAFKQIAKRVIQEDTFSSFYGDVSTDTIRLAKAIVDDPSIAPAAAPNLYKQYAAMDRAVLQRPGFALGLALYSTRISSYESINSENGRGWYTGAGATYLYNQDLAQYSEDYWPTVDAYRIPGTTVASGTPIASGTGTSSWTGGVSLAGQYGASGMDLSYGAYNLSARKSWFMFDDEIVALGSGISSTAGIPIETVVDNRKLNGAGDNAWTANGAALSTGLGVAQTLTGVNWVHLAGNTADGSDIGYYFPGGATLQTKREARTGTWKQINNRPATPSTAVTRNYETMWIDHGTNPSGASYGYVLLPNKTSAQVGAYAADPAIEIVVNTSGVQSVKEKTLGLVGANFWTDTTQTADLITSNKKASVMTREIADERLEASVSDPTQANNGTIAIELARSAEGYSADPGITVTQLAPTIKFTVNVNGAKGKSFHASFQLGEDTSGPVDPGEPELPSVIVDNADSAGVTRTGTWKTASTQTDRYGANYLHDDNAGKGTKSVTFTPNLPIAGSYEVYLMWPAHFNREDAVQVDVGHASGTTRTAVDQRSGGGVWHSIGTYEFLAGSGGSVTIRNDALGSPDGYVVADAVKFVAVG
Protein: DNA polymerase epsilon subunit 3 (Arsenic-transactivated protein) (AsTP) (Chromatin accessibility complex 17 kDa protein) (CHRAC-17) (HuCHRAC17) (DNA polymerase II subunit 3) (DNA polymerase epsilon subunit p17) (Q9NRF9)
Organism: Homo sapiens (Human)
Function: Accessory component of the DNA polymerase epsilon complex. Participates in DNA repair and in chromosomal DNA replication (By similarity). Forms a complex with CHRAC1 and binds naked DNA, which is then incorporated into chromatin, aided by the nucleosome-remodeling activity of ISWI/SNF2H and ACF1. Does not enhance nucleosome sliding activity of the ACF-5 ISWI chromatin remodeling complex.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA polymerase epsilon subunit 2
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5
- DNA polymerase epsilon catalytic subunit A
- Chromatin accessibility complex protein 1
- Bromodomain adjacent to zinc finger domain protein 1A
- DNA polymerase epsilon subunit 4
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 1
- DNA polymerase delta catalytic subunit
- DNA polymerase alpha catalytic subunit
- Protein Dr1
Sequence:
MAERPEDLNLPNAVITRIIKEALPDGVNISKEARSAISRAASVFVLYATSCANNFAMKGKRKTLNASDVLSAMEEMEFQRFVTPLKEALEAYRREQKGKKEASEQKKKDKDKKTDSEEQDKSRDEDNDEDEERLEEEEQNEEEEVDN