wanglab/gogpt-training-data huggingface dataset:
Protein: DNA-directed RNA polymerase I subunit 2 (DNA-directed RNA polymerase I subunit RPA2) (DNA polymerase I subunit A2) (EC 2.7.7.6) (Nuclear RNA polymerase A2) (F4I366)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol I is composed of mobile elements and NRPA2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P22138}.
Interaction partners:
- DNA-directed RNA polymerases II, IV and V subunit 10
- DNA binding / DNA-directed RNA polymerase
- DNA-directed RNA polymerase family protein
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerases II, IV and V subunit 6A
- DNA-directed RNA polymerases II and V subunit 6B
- RNApolymerase 14 kDa subunit
- DNA-directed RNA polymerase I subunit 1
- DNA-directed RNA polymerases II and V subunit 8A
- DNA-directed RNA polymerases I and III subunit RPAC1
Sequence:
MVVNAKDSTVPTMEDFKELHNLVTHHIESFDYMTLKGLDVMFNRIKPVSVYDPNTENELSIWLENPLVFAPQKESFKSTSRKEPLLPFECRQAKISYTGTFMADVCFKYNDGVVVRDKFDFGQFPIMLMSKLCSLKGADCRKLLKCKESTSEMGGYFILNGIERVFRCVIAPKRNHPTSMIRNSFRDRKEGYSSKAVVTRCVRDDQSSVTVKLYYLRNGSARVGFWIVGREYLLPVGLVLKALTNSCDEEIYESLNCCYSEHYGRGDGAIGTQLVRERAKIILDEVRDLGLFTREQCRKHLGQHFQPVLDGVKKESLSIVAEAVLRDYLFVHLDNDHDKFNLLIFIIQKLYSLVDQTSLPDNPDSLQNQEILVPGHVITIYLKEKLEEWLRKCKSLLKDELDNTNSKFSFESLADVKKLINKNPPRSIGTSIETLLKTGALKTQSGLDLQQRAGYTVQAERLNFLRFLSFFRAVHRGASFAGLRTTTVRKLLPESWGFLCPVHTPDGTPCGLLNHMTRTSRITSQFDSKGNIRDFLKIRKSVVDVLTGAGMVPSLPKLVRAGPPKVIHVLLDGQVVGTLSSNLVTKVVSYIRRLKVEAPSVIPEDLEVGYVPTSMGGSYPGLYLASCPARFIRPVKNISIPSDNIELIGPFEQVFMEISCPDGGNGGRNNSSLATHEEIHPTGMISVVANLTPWSDHNQSPRNMYQCQMAKQTMAYSTQALQFRADQKIYHLQTPQSPVVRTKTYTTYSIDENPTGTNAIVAVLAHTGFDMEDAMILNKSSVERGMCHGQIYQTENIDLSDQNSRFDSGSKSFRRSTNKAEHFRIDADGLPSVGQKLYPDEPYCSIYDEVTNKTRHMKRKGTDPVIVDFVSVDMKSKKHPQRANIRFRHARNPIIGDKFSSRHGQKGVCSQLWPDIDMPFNGVTGMRPDLIINPHAFPSRMTIAMLLESIAAKGGSLHGKFVDATPFRDAVKKTNGEEESKSSLLVDDLGSMLKEKGFNHYGTETLYSGYLGVELKCEIFMGPVYYQRLRHMVSDKFQVRSTGQVDQLTHQPIKGRKRGGGIRFGEMERDSLLAHGASYLLHDRLHTSSDHHIADVCSLCGSLLTSSVVNVQQKKLIQEIGKLPPGRTPKKVTCYSCKTSKGMETVAMPYVFRYLAAELASMNIKMTLQLSDREGVTD
Protein: 5-OH-xanthotoxin synthase (EC 1.14.14.-) (Cytochrome P450 CYP71AZ6) (A0A2Z5D852)
Organism: Pastinaca sativa (Wild parsnip) (Anethum pastinaca)
Function: Involved in the biosynthesis of coumarins and furanocoumarins (FCs), natural products required for defense responses against attacks by predators with potential medical and agroindustrial usages such as anticoagulant, rodenticide and artificial vanilla substitutes. Catalyzes the conversion of xanthotoxin into 5-hydroxyxanthotoxin.
Subcellular location: Microsome membrane {ECO:0000250|UniProtKB:Q6QNI4}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MDPVVIFLVLAFPIASVYLLFYHKKRVGGLSSPPGPRGLPFIGNFFQLYKAPCIHEYLWNLSKKYGSLMTLHMGSVPILVVSSPKMAKEVLKTQDLIYCSRPRMTGMRKLSYDGLDVAFSTYSEHWRHVRKLCTLELFTQKRAQLCFRLVHEQEVSRMIVRLSETAAASKDVNAFECFSNLSTSIISRVAFGKRYDEDGIGKERLQRMLSEIDAMLAGIFVSDFFPMFGWIDRLSGMRARLDRTFKEMDMFYEELIDEHLKPNRPESPTEDLIDVMLKNKGSSCLLTMDSIKAILLNVFNGGTGTSATLLVWAMTALMRNQGVMKKAQEDIRRVIGRKGNVDEDDIQNLSYLRAVVKETMRLYPTGPLLIPRETMESSIIGEDKDHMYMIKPKTLVYVSMWAIGRDPEIWKNPMEFVPERFLERPDLNYKGQQFEYIPFGAGRRICAGIHLGVTTVELALANLLYTFDWEPPAGTRFEDIDDETLNGLTLQKKNALYIRPKKYICP
Protein: NAD-dependent epimerase/dehydratase domain-containing protein (A0A1D8PJA6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit
- NADH-ubiquinone oxidoreductase 78 kDa subunit, mitochondrial
- Fesur1p
- 4Fe-4S ferredoxin-type domain-containing protein
- Zinc finger CHCC-type domain-containing protein
- Uncharacterized protein
- Ribosomal protein/NADH dehydrogenase domain-containing protein
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
Sequence:
MLKLSARPISRSIGVFSRRSVYTSVLESDINITKNGKVNVAVGAGGRSSRTGYTATVFGASGFLGRYVTSKLARHGTTTIVPFRDDMKKRFLKVTGDLGVVNFVEIDARNLQSIEDSVAHSDIVINCIGVDYDTKNFKMADVNIALAERIAEATKKANVPRYIHVSSYNADPNSESVFYATKGIAEQVVRDIIPDTTIVRPAPMYGREDSLLNYLGPKVKMWTPNKNAKEVWPVYVLDVARALERIAYDDSTAGQTFELYGPEKVTFQEIRNMIHGITENYAQVGPWSYQFADYAIPLPLAKAIAKVQQLVWWKLTNPDQVQRLVINQKIDPNAKTFHDLGIDDLTRLPDVLFSYVKQWRHPLIAQKGAPGKKELERLRDVQHFTP
Protein: Pleckstrin homology domain-containing family H member 2 (Q8IVE3)
Organism: Homo sapiens (Human)
Function: In the kidney glomerulus may play a role in linking podocyte foot processes to the glomerular basement membrane. May be involved in stabilization of F-actin by attenuating its depolymerization. Can recruit TGFB1I1 from focal adhesions to podocyte lamellipodia.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22832517}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:22832517}. Cell membrane {ECO:0000269|PubMed:22832517}; Peripheral membrane protein {ECO:0000269|PubMed:22832517}; Cytoplasmic side {ECO:0000269|PubMed:22832517}. Cell projection, lamellipodium {ECO:0000269|PubMed:22832517}. Note=Localizes to foot process of podocytes. Localization to peripheral regions of lamellipodia seems to be dependent on PI3K.
Interaction partners:
Sequence:
MAELSEPEGPVDWKERCVALESQLMKFRVQASKIRELLAEKMQQLERQVIDAERQAEKAFQQVQVMEDKLKAANIQTSESETRLYNKCQDLESLIQEKDDVIQNLELQLEEQKQIRIQEAKIIEEKAAKIKEWVTVKLNELELENQNLRLINQNQTEEIRTMQSKLQEVQGKKSSTVSTLKLSEGQRLSSLTFGCFLSRARSPPQVVKSEEMSKISSKEPEFTEGKDMEEMEIPEKSVDNQVLENNRGQRTLHQTPCGSEQNRKTRTSFATDGGISQNSGAPVSDWSSDEEDGSKGRSKSRCTSTLSSHTSEEGVQCSRMGSEMYLTASDDSSSIFEEETFGIKRPEHKKLYSWQQEAQWKALNSPLGKGNSELSKKEQDSSSDELNKKFQSQRLDYSSSSSEANTPSPILTPALMPKHPNSLSGKGTQLVPSSHLPPPKLRIPNVFSISVALAKRHLSQPQLSSDRMFGTNRNAISMIRPLRPQETDLDLVDGDSTEVLENMDTSCDDGLFSYDSLDSPNSDDQEHCDSAKKVAYSKPPTPPLHRFPSWESRIYAVAKSGIRMSEAFNMESVNKNSAATLSYTTSGLYTSLIYKNMTTPVYTTLKGKATQISSSPFLDDSSGSEEEDSSRSSSRTSESDSRSRSGPGSPRAMKRGVSLSSVASESDYAIPPDAYSTDTEYSQPEQKLPKTCSSSSDNGKNEPLEKSGYLLKMSGKVKSWKRRWFVLKGGELLYYKSPSDVIRKPQGHIELSASCSILRGDNKQTVQLTTEKHTYYLTADSPNILEEWIKVLQNVLRVQAANPLSLQPEGKPTMKGLLTKVKHGYSKRVWCTLIGKTLYYFRSQEDKFPLGQIKLWEAKVEEVDRSCDSDEDYEASGRSLLSTHYTIVIHPKDQGPTYLLIGSKHEKDTWLYHLTVAAGSNNVNVGSEFEQLVCKLLNIDGEPSSQIWRHPTLCHSKEGIISPLTTLPSEALQTEAIKLFKTCQLFINAAVDSPAIDYHISLAQSALQICLTHPELQNEICCQLIKQTRRRQPQNQPGPLQGWQLLALCVGLFLPHHPFLWLLRLHLKRNADSRTEFGKYAIYCQRCVERTQQNGDREARPSRMEILSTLLRNPYHHSLPFSIPVHFMNGIYQVVGFDASTTVEEFLNTLNQDTGMRKPAQSGFALFTDDPSGRDLEHCLQGNIKICDIISKWEQASKEQQPGKCEGTRTVRLTYKNRLYFSVQARGETDREKLLLMYQTNDQIINGLFPLNKDLALEMAALLSQVEIGDFERPFSTPAGHVTNQCKVNQTLKQVIEKFYPKRYRDGCSEEQLRQLCQRLSTRWMALRGHSAADCVRIYLTVARKWPFFGAKLFLAKPITPSSLGSTFLWLAVHEDGLSLLEYNSMRLIVSYVYKSLMTFGGYQDDFMVVINNTHSKDKPTEKLLFAMAKPKILEITLLIASYINNFHQQKAAFHHLSAPALLSAQTRGPQARMMGSQPLLSSSRPTKGPTLL
Protein: Solute carrier family 2, facilitated glucose transporter member 4 (Glucose transporter type 4, insulin-responsive) (Q9DFV2)
Organism: Salmo trutta (Brown trout)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}.
Interaction partners:
Sequence:
MPPGFQHLGGETVTGTLALSVFTAVLGSFQFGYNIGVINAPQKIIEADYNATWVHRYGELIPTATLTTPWSLSVAIFSIGGMISSFCVGVISEWLGRRKAMLINNLFAFIGGSLMGMAKISRSFEMMILGRFVIGAYCGLASGLVPMYVGEIAPTSLRGALGTLHQLAIVTGILIAQVLGLESLLGSEELWPVLVGVTVLPTVLQMALLPFCPESPRFLYIIRCQEHHAKSGLRRLTGRQEVGDMLAEMKEEKRRMDMERKVSIAELFRSPMYRQPIIIAILLQLSQQLSGVNAVFYYSTSIFQKAGVQSPVYATIGAGVVNSAFTVVSLFLVERTGRRTLHMLGLFGMCGCAIVMTIALALLDSVPWMSYISMLAIFGFVAFFEVGPGPIPWFFVAELFSQGPRPAAMAVAGFSNWTANFIIGFGFQYLAELCGPYVFLIFAVLLLFFLIFTFFRVPETRGKTFDQISTSFSQHPPAMMDLDMELGKRSTELDYLGGEGSLD
Protein: Nucleotide sugar transporter SLC35B4 (Solute carrier family 35 member B4) (UDP-xylose and UDP-N-acetylglucosamine transporter) (YEA4 homolog) (Q969S0)
Organism: Homo sapiens (Human)
Function: Antiporter that transports nucleotide sugars across the endoplasmic reticulum (ER) membrane in exchange for another nucleotide sugar. May couple UDP-alpha-D-glucuronate (UDP-GlcA) or UDP-alpha-D-xylose (UDP-Xyl) efflux to UDP-alpha-D-glucuronate (UDP-GlcA) influx into the ER lumen, which in turn stimulates glucuronidation and excretion of endobiotics and xenobiotics.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30458018}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Nucleotide sugar transporter SLC35D2
- UDP-N-acetylglucosamine transporter
- Nucleotide sugar transporter SLC35D1
- Solute carrier family 35 member D3
- AMP deaminase 2
- AMP deaminase 3
- AMP deaminase 1
- Solute carrier family 35 member C2
Sequence:
MRPALAVGLVFAGCCSNVIFLELLARKHPGCGNIVTFAQFLFIAVEGFLFEADLGRKPPAIPIRYYAIMVTMFFTVSVVNNYALNLNIAMPLHMIFRSGSLIANMILGIIILKKRYSIFKYTSIALVSVGIFICTFMSAKQVTSQSSLSENDGFQAFVWWLLGIGALTFALLMSARMGIFQETLYKRFGKHSKEALFYNHALPLPGFVFLASDIYDHAVLFNKSELYEIPVIGVTLPIMWFYLLMNIITQYVCIRGVFILTTECASLTVTLVVTLRKFVSLIFSILYFQNPFTLWHWLGTLFVFIGTLMYTEVWNNLGTTKSEPQKDSKKN
Protein: Vacuolar protein sorting-associated protein 33B (hVPS33B) (Q9H267)
Organism: Homo sapiens (Human)
Function: May play a role in vesicle-mediated protein trafficking to lysosomal compartments and in membrane docking/fusion reactions of late endosomes/lysosomes. Required for proper trafficking and targeting of the collagen-modifying enzyme lysyl hydroxylase 3 (LH3) to intracellular collagen. Mediates phagolysosomal fusion in macrophages. Proposed to be involved in endosomal maturation implicating VIPAS39. In epithelial cells, the VPS33B:VIPAS39 complex may play a role in the apical recycling pathway and in the maintenance of the apical-basolateral polarity. Seems to be involved in the sorting of specific cargos from the trans-Golgi network to alpha-granule-destined multivesicular bodies (MVBs) promoting MVBs maturation in megakaryocytes (By similarity).
Subcellular location: Late endosome membrane {ECO:0000269|PubMed:15052268}; Peripheral membrane protein; Cytoplasmic side. Lysosome membrane {ECO:0000269|PubMed:15052268}; Peripheral membrane protein; Cytoplasmic side. Early endosome {ECO:0000269|PubMed:21411634}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:21411634}. Recycling endosome {ECO:0000269|PubMed:22753090}. Note=Colocalizes in clusters with VIPAS39 at cytoplasmic organelles (PubMed:19109425, PubMed:31479177). Colocalizes with RAB11A and VIPAS39 on recycling endosomes (PubMed:22753090). Colocalizes with AP-3, clathrin, Rab5 and Rab7b (PubMed:21411634). Colocalizes with M.tuberculosis PtpA in the cytosol of tuberculosis-infected macrophages and associates with phagosomes (PubMed:18474358). {ECO:0000269|PubMed:18474358, ECO:0000269|PubMed:19109425, ECO:0000269|PubMed:21411634, ECO:0000269|PubMed:22753090}.
Interaction partners:
- Spermatogenesis-defective protein 39 homolog
- Vacuolar protein sorting-associated protein 11 homolog
- Vacuolar protein sorting-associated protein 41 homolog
- Vacuolar protein sorting-associated protein 16 homolog
- Vacuolar protein sorting-associated protein 18 homolog
- Vam6/Vps39-like protein
- Transforming growth factor-beta receptor-associated protein 1
- Vacuolar protein sorting-associated protein 8 homolog
- Syntaxin-7
- Ras-related protein Rab-11A
Sequence:
MAFPHRPDAPELPDFSMLKRLARDQLIYLLEQLPGKKDLFIEADLMSPLDRIANVSILKQHEVDKLYKVENKPALSSNEQLCFLVRPRIKNMRYIASLVNADKLAGRTRKYKVIFSPQKFYACEMVLEEEGIYGDVSCDEWAFSLLPLDVDLLSMELPEFFRDYFLEGDQRWINTVAQALHLLSTLYGPFPNCYGIGRCAKMAYELWRNLEEEEDGETKGRRPEIGHIFLLDRDVDFVTALCSQVVYEGLVDDTFRIKCGSVDFGPEVTSSDKSLKVLLNAEDKVFNEIRNEHFSNVFGFLSQKARNLQAQYDRRRGMDIKQMKNFVSQELKGLKQEHRLLSLHIGACESIMKKKTKQDFQELIKTEHALLEGFNIRESTSYIEEHIDRQVSPIESLRLMCLLSITENGLIPKDYRSLKTQYLQSYGPEHLLTFSNLRRAGLLTEQAPGDTLTAVESKVSKLVTDKAAGKITDAFSSLAKRSNFRAISKKLNLIPRVDGEYDLKVPRDMAYVFGGAYVPLSCRIIEQVLERRSWQGLDEVVRLLNCSDFAFTDMTKEDKASSESLRLILVVFLGGCTFSEISALRFLGREKGYRFIFLTTAVTNSARLMEAMSEVKA
Protein: Putative amidase AmiC (EC 3.5.1.4) (P9WQ95)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Aspartyl/glutamyl-tRNA
- Elongation factor Ts
- Acylphosphatase
- Small ribosomal subunit protein uS2
- Cholesterol ring-cleaving hydrolase IpdA subunit
- Glutamyl-tRNA
- Peptidase M20 domain-containing protein 2
- Peptidoglycan endopeptidase RipA
- N-acetylmuramoyl-L-alanine amidase Rv3717
- Nudix hydrolase domain-containing protein
Sequence:
MSRVHAFVDDALGDLDAVALADAIRSGRVGRADVVEAAIARAEAVNPALNALAYAAFDVARDAAAMGTGQEAFFSGVPTFIKDNVDVAGQPSMHGTDAWEPYAAVADSEITRVVLGTGLVSLGKTQLSEFGFSAVAEHPRLGPVRNPWNTDYTAGASSSGSGALVAAGVVPIAHANDGGGSIRIPAACNGLVGLKPSRGRLPLEPEYRRLPVGIVANGVLTRTVRDTAAFYREAERLWRNHQLPPVGDVTSPVKQRLRIAVVTRSVLREASPEVRQLTLKLAGLLEELGHRVEHVDHPPAPASFVDDFVLYWGFLALAQVRSGRRTFGRTFDPTRLDELTLGLARHTGRNLHRLPLAIMRLRMLRRRSVRFFGTYDVLLTPTVAEATPQVGYLAPTDYQTVLDRLSSWVVFTPVQNVTGVPAISLPLAQSADGMPVGMMLSADTGREALLLELAYELEEARPWARIHAPNIAE
Protein: Fibroblast growth factor 9 (FGF-9) (Glia-activating factor) (GAF) (HBGF-9) (P36364)
Organism: Rattus norvegicus (Rat)
Function: Plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration. May have a role in glial cell growth and differentiation during development, gliosis during repair and regeneration of brain tissue after damage, differentiation and survival of neuronal cells, and growth stimulation of glial tumors.
Subcellular location: Secreted.
Interaction partners:
- Fibroblast growth factor receptor
- Fibroblast growth factor receptor 1
- Fibroblast growth factor receptor
- Fibroblast growth factor receptor 4
- Klotho
- Pro-epidermal growth factor
- Vascular endothelial growth factor receptor 2
- Vascular endothelial growth factor receptor 3
- Fibroblast growth factor 23
- Platelet-derived growth factor receptor alpha
Sequence:
MAPLGEVGSYFGVQDAVPFGNVPVLPVDSPVLLSDHLGQSEAGGLPRGPAVTDLDHLKGILRRRQLYCRTGFHLEIFPNGTIQGTRKDHSRFGILEFISIAVGLVSIRGVDSGLYLGMNEKGELYGSEKLTQECVFREQFEENWYNTYSSNLYKHVDTGRRYYVALNKDGTPREGTRTKRHQKFTHFLPRPVDPDKVPELYKDILSQS
Protein: Vesicle-fusing ATPase (EC 3.6.4.6) (N-ethylmaleimide-sensitive factor A) (NEM-sensitive fusion protein A) (Vesicular-fusion protein nfsA) (Q75JI3)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Required for vesicle-mediated transport. Involved in endocytosis and endosome-endosome fusion. May be required for transport from the endoplasmic reticulum to the Golgi stack, and for the fusion of transport vesicles within the Golgi cisternae. Required for cell polarity, locomotion and chemotaxis.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:10727946}; Peripheral membrane protein {ECO:0000269|PubMed:10727946}; Cytoplasmic side {ECO:0000269|PubMed:10727946}. Endosome membrane {ECO:0000269|PubMed:10727946}; Peripheral membrane protein {ECO:0000269|PubMed:10727946}; Cytoplasmic side {ECO:0000269|PubMed:10727946}.
Interaction partners:
- Alpha-soluble NSF attachment protein
- Sec1 family domain-containing protein 1 homolog
- Syntaxin-7A
- Gamma-soluble NSF attachment protein
- t-SNARE family protein
- t-SNARE family protein
- Vesicle-trafficking protein SEC22b
- Synaptobrevin-A
- Synaptobrevin-B
- UBX domain-containing protein 7 homolog
Sequence:
MSYPPPVGDSIKLKVQASNDPEEAFTNRAYLPISSFSFLFPNVQSNLYTTNTNYIKIRVGANEYILSASPNKNMKPDSIALSKALRGWMYVSNNEEVYVEFYDPNPNICGSMKVSIDYLTKGKQGPKQDSQEIIGKIIDNFNSQYFTFGQLFYIKNSNSTFELRVEAVETNEVPTKDKGWAIISPATKIILQKMPGSLIDIETNGPLVVNQIFTSDWDFENMGIGGLDAEFRDIFRRAFSSRIFPPAIVKKLGVNHVKGMLLYGPPGTGKTLIARQIGKMLNGREPKVVSGPSILNKYVGQSEENIRMLFRDAEIEQKAKGDDSGLHIIIFDELDAICKSRGSRQGDSGVGDSVVNQLLAMIDGVESLNNILVIGMTNRKDMIDEALLRPGRLEVHVEISLPDEHGREQIFKIHTAKMRDQNALDKDVNLANYAHTTRNYSGAEIEGVVKSAASYAFSRQVDTKNIKNVEIKPEDIKVCDQDFKRAITEVTPSFGSTDNQFESYAENGIINYGPVFDKLLQSGNAFVEQVKKSNRTPMMSVLLSGRPGCGKSSLAATLAKSSEFPFTRIISPNDLLGYNESAKASKITKVFEDSYKSPMSCVVVDEIERLIEYVPIGPRFSNLILQTLAVLFKRTPPKGRKLLVIATTSNPDILKDMDIMDCFATVLSVPSISTAKEFQTVCFELGFTQKEASEAASFFTSPITIKQIIMIVEMARQEEGNFIDNFKMCLEDFNIRNF
Protein: Intrinsically Disordered Protein, class C (Q22262)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MERRSHQTIITGLLIIMQTFSALLLALSLFSGASAQLAAWPSQSYSPFYQALFGGASTPVLSAPVAKTAPSAIPLAAPALPVPIAAAPFFTPPAPVLAAPAPLLAPPAPVFAAPRPVFASPALAPVAPMAPILRGPAFAYAPSPVLAPVGVAPVAPAPVFAAPALAPVAPVLAAPRFVPAYAPFARAAMFIGSNKAKTA
Protein: H(+)-transporting two-sector ATPase (EC 7.1.2.2) (Mitochondrial protein YMF19) (O04723)
Organism: Oryza sativa (Rice)
Subcellular location: Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004304}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004304}.
Interaction partners:
Sequence:
MPQLDKLTYFSQFFWLCLFLFSFYILLLNNNNGILGISRILKLRNQLLSHRGNKIRFKDPKNLEDISRKGFSTGLSYMYSSLSEVSQWCKTVDYLGKRRKITLISDFGEISGSRGMERQILYLISKSSYNTSSSRITCWKKIMLTHVPHGQGSII
Protein: Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (EC 6.2.1.4) (EC 6.2.1.5) (Succinyl-CoA synthetase subunit alpha) (SCS-alpha) (p36) (P36967)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and specificity for either ATP or GTP is provided by different beta subunits.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03222}.
Interaction partners:
- Succinate--CoA ligase subunit beta, mitochondrial
- Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Succinate dehydrogenase cytochrome b560 subunit
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- Succinate dehydrogenase cytochrome b small subunit
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Probable 2-oxoadipate dehydrogenase complex component E1 homolog
Sequence:
MISAGMIARNFGKRFFSTKPSVLINKHTKVICQGFTGNQGTFHSKQAIEYGTNMVGGVSPGKGGQKHLDLPVFNTVKEAKEATGANATVIYVPPPHAAAAIKEAIDAEMELVVCITEGIPQQDMVKVKYLLNKQNKTRLIGPNCPGIIKPGECKIGIMPGHIHKPGKIGIVSRSGTLTYEAVAQTTAVGLGQSTCIGIGGDPFNGTNFIDCLKMFTQDPQTEGIILIGEIGGEAEEEAAQWLIDNPTDKPVVSFIAGLSAPPGRRMGHAGAIISGGKGDANSKIEALKAAGVTVTFSPAKLGETILQKMNEKKNK
Protein: Protein-arginine N-acetylglucosaminyltransferase SseK2 (Arginine GlcNAcyltransferase SseK2) (EC 2.4.1.-) (Salmonella secreted effector K2) (Q8ZNP4)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Protein-arginine N-acetylglucosaminyltransferase effector that catalyzes the transfer of a single N-acetylglucosamine (GlcNAc) to a conserved arginine residue in the death domain of host proteins such as FADD: arginine GlcNAcylation prevents homotypic/heterotypic death domain interactions. Also acts on host proteins without a death domain: catalyzes arginine GlcNAcylation of host small Rab1 GTPase, thereby preventing GTPase activity and leading to impaired host vesicular protein transport (By similarity). In contrast to Ssek1, not able to disrupt TNF signaling in infected cells.
Subcellular location: Secreted {ECO:0000269|PubMed:15322005}. Host Golgi apparatus {ECO:0000269|PubMed:28069818}. Note=Secreted via the type III secretion system (T3SS). {ECO:0000269|PubMed:15322005}.
Interaction partners:
Sequence:
MARFNAAFTRIKIMFSRIRGLISCQSNTQTIAPTLSPPSSGHVSFAGIDYPLLPLNHQTPLVFQWFERNPDRFGQNEIPIINTQKNPYLNNIINAAIIEKERIIGIFVDGDFSKGQRKALGKLEQNYRNIKVIYNSDLNYSMYDKKLTTIYLENITKLEAQSASERDEVLLNGVKKSLEDVLKNNPEETLISSHNKDKGHLWFDFYRNLFLLKGSDAFLEAGKPGCHHLQPGGGCIYLDADMLLTDKLGTLYLPDGIAIHVSRKDNHVSLENGIIAVNRSEHPALIKGLEIMHSKPYGDPYNDWLSKGLRHYFDGSHIQDYDAFCDFIEFKHENIIMNTSSLTASSWR
Protein: Next to BRCA1 gene 1 protein (Cell migration-inducing gene 19 protein) (Membrane component chromosome 17 surface marker 2) (Neighbor of BRCA1 gene 1 protein) (Protein 1A1-3B) (Q14596)
Organism: Homo sapiens (Human)
Function: Ubiquitin-binding autophagy adapter that participates in different processes including host defense or intracellular homeostasis. Possesses a double function during the selective autophagy by acting as a shuttle bringing ubiquitinated proteins to autophagosomes and also by participating in the formation of protein aggregates. Plays a role in the regulation of the innate immune response by modulating type I interferon production and targeting ubiquitinated IRF3 for autophagic degradation. In response to oxidative stress, promotes an increase in SQSTM1 levels, phosphorylation, and body formation by preventing its autophagic degradation (By similarity). In turn, activates the KEAP1-NRF2/NFE2L2 antioxidant pathway (By similarity). Plays also non-autophagy role by mediating the shuttle of IL-12 to late endosome for subsequent secretion (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19427866, ECO:0000269|PubMed:35914352}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:19250911, ECO:0000269|PubMed:24879152}. Lysosome {ECO:0000269|PubMed:19250911}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000250|UniProtKB:Q501R9}. Note=In cardiac muscles localizes to the sarcomeric M line (By similarity). Is targeted to lysosomes for degradation (PubMed:19250911). {ECO:0000250|UniProtKB:Q501R9, ECO:0000269|PubMed:19250911}.
Interaction partners:
- GABA type A receptor associated protein like 1
- Microtubule-associated protein 1 light chain 3 beta
- Gamma-aminobutyric acid receptor-associated protein
- Sequestosome-1
- Gamma-aminobutyric acid receptor-associated protein-like 2
- Polyubiquitin-C
- Titin
- Ubiquitin-ribosomal protein eS31 fusion protein
- Microtubule-associated protein 1 light chain 3 alpha
- Polyubiquitin-B
Sequence:
MEPQVTLNVTFKNEIQSFLVSDPENTTWADIEAMVKVSFDLNTIQIKYLDEENEEVSINSQGEYEEALKMAVKQGNQLQMQVHEGHHVVDEAPPPVVGAKRLAARAGKKPLAHYSSLVRVLGSDMKTPEDPAVQSFPLVPCDTDQPQDKPPDWFTSYLETFREQVVNETVEKLEQKLHEKLVLQNPSLGSCPSEVSMPTSEETLFLPENQFSWHIACNNCQRRIVGVRYQCSLCPSYNICEDCEAGPYGHDTNHVLLKLRRPVVGSSEPFCHSKYSTPRLPAALEQVRLQKQVDKNFLKAEKQRLRAEKKQRKAEVKELKKQLKLHRKIHLWNSIHGLQSPKSPLGRPESLLQSNTLMLPLQPCTSVMPMLSAAFVDENLPDGTHLQPGTKFIKHWRMKNTGNVKWSADTKLKFMWGNLTLASTEKKDVLVPCLKAGHVGVVSVEFIAPALEGTYTSHWRLSHKGQQFGPRVWCSIIVDPFPSEESPDNIEKGMISSSKTDDLTCQQEETFLLAKEERQLGEVTEQTEGTAACIPQKAKNVASERELYIPSVDLLTAQDLLSFELLDINIVQELERVPHNTPVDVTPCMSPLPHDSPLIEKPGLGQIEEENEGAGFKALPDSMVSVKRKAENIASVEEAEEDLSGTQFVCETVIRSLTLDAAPDHNPPCRQKSLQMTFALPEGPLGNEKEEIIHIAEEEAVMEEEEDEEDEEEEDELKDEVQSQSSASSEDYIIILPECFDTSRPLGDSMYSSALSQPGLERGAEGKPGVEAGQEPAEAGERLPGGENQPQEHSISDILTTSQTLETVPLIPEVVELPPSLPRSSPCVHHHGSPGVDLPVTIPEVSSVPDQIRGEPRGSSGLVNSRQKSYDHSRHHHGSSIAGGLVKGALSVAASAYKALFAGPPVTAQPIISEDQTAALMAHLFEMGFCDRQLNLRLLKKHNYNILQVVTELLQLNNNDWYSQRY
Protein: RutC family protein YoaB (P0AEB7)
Organism: Escherichia coli (strain K12)
Interaction partners:
- 3-aminoacrylate deaminase RutC
- ATP-dependent DNA helicase YoaA
Sequence:
MTIVRIDAEARWSDVVIHNNTLYYTGVPENLDADAFEQTANTLAQIDAVLEKQGSNKSSILDATIFLADKNDFAAMNKAWDAWVVAGHAPVRCTVQAGLMNPKYKVEIKIVAAV