wanglab/gogpt-training-data huggingface dataset:
Protein: Protein lingerer (Q86S05)
Organism: Drosophila melanogaster (Fruit fly)
Function: Acts in the nervous system to mediate the control of copulatory organs during courtship.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12524348}. Note=Found in the cytoplasm of many neuronal and glial cells in the brain and ventral ganglion, and in imaginal disks. {ECO:0000269|PubMed:12524348}.
Interaction partners:
- Raptor, isoform B
- Serine/threonine-protein kinase mTor
- AT27578p
- Fragile X messenger ribonucleoprotein 1 homolog
Sequence:
MSTQTRSGGGGGGGHARNQKKSNASNSGGGGTGHHDGVSHAAAAGKKGGQDASKTDKPEKAQPKATTEQLRIAQITNSTTEDPQINEKVLLLLTMTQRSEEEVCCALNECDYDLEAAANFLIEELPQGAFAKYEKKRKNKAANNTADGAAGDGDWADGNGNADRREKSRNRSSNRGGTRGSSDSRGWRGRETRENERNQRESREPWSGQNAGQDRGDDRANDNYRGQRNGGGRSGPGGGGRGGGFVSRSGRGGGRMGGRTGGPRGDRGSGGPGGAYGSGRGGNANEDHHEVELWDNTIAQNAEKQQQAHDDAWGDWNNEEYEGSLKDSKVFTTSNLATQSAANVVSGTGASVTAVPAAAGTEISAPPGLEHQLVQQGSHLEESSSSGPAAVTPPATLSGSATTPLLQYSAAVSNPPPQLQSQGTQSGAGTGASAAAGGGAGSTPSSFVSASPDTFSSAASAAATLVHQAQKQQQLQQQTTPIKPSATLSVEQSQYFNSLASQGVSPGSVPVQSAPAGYAQNPVAAYSQTSTSVGVSQYPNTYANVFASGTAAGAGTAEQSQQQPQIRRARVKLPPPSKIPASAVEMPGDNALNNIGYLDVQFGALDFGTDDGFEPLPEKVGSGFSIDGQQQQQQPDDYQSKSQQQQQVTLAAGLQSSQISDALNAAGYTSRSTSQQQQGVSSAVNATIDQLTKSDPYGQTGGSGNAYQNAYQSSGASKTASGFPTTAPGGYSSSTYANVQSSVANSYQQQGYGSYQPSSYQQQAGSGAQSGTGAVSGGGGTATQNIPVGGSSSQNSTSGNASSAYLTSGYSTPQSAYQSSQSVYGNTGLSNSSGFSGSASNASSQYANFSASAKLKDATTASSAAHYDSVSTSSGVSSNSGSTGNGGVVSGQTGANQAAVSNNNSVSGSSSVSNVTAGVASGNVAGVGGGVSQSGVSSGVGVPGGSASSVGVNVNNNSSSASSVGAATVAQTATGTTAAVLASLTNKNTSSSNSSGSGGSAATTTGNASGQGAGASTGGVGSSSGAGGAGSGGGSGSGLVPTNIQMVSQYIQTGLPYYQQPVYSYEELQMMQQRVPHVQGYYDLNYPPASLGAGRDNLGSVTYSAMNDGRFARTDNNSSPVGNVSSTMSQQAGSSAPMLNVPYAYFYGGNVMPGSFQYGTPAIYPQIPAANTASGQQFPKPSYSAGYGSTSYDTLSQTTQDYSKGGYSSSVNQQSKTQTVSNQSQAGTGSDLTSSMYGKGHVALNKVNSYEKQSFHSGTPPPFNMPNTQTAGGTSAQPYGMYLPMPAAGHHNMIHQPIHQVHSELPLQVVVGGGTESHVLIHGNVNGPQVTYHRIWQTEPVQCQNQLVAAHCNNFEPNIDCCVHDNNNDLSFFAD
Protein: Fibrillarin (M0R0P1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKPGFSPRGGGFGGRGGFGDRGGRGGFHSGGNRGRGRGGKRGNQSGKNVMVEPHRHEGVFICRGKEDALVTKNLVPGESVYGEKRVSISEGDDKIEYRAWNPFRSKLAAAILGGVDQIHIKPGAKVLYLGAASGTTVSHVSDIVGPDGLVYAVEFSHRSGRDLINLAKKRTNIIPVIEDARHPHKYRMLIAMVDVIFADVAQPDQTRIVALNAHTFLRNGGHFVISIK
Protein: Arrestin domain-containing protein 1 (Alpha-arrestin 1) (Q8N5I2)
Organism: Homo sapiens (Human)
Function: Functions as an adapter recruiting ubiquitin-protein ligases to their specific substrates. Through an ubiquitination-dependent mechanism plays for instance a role in the incorporation of SLC11A2 into extracellular vesicles. More generally, plays a role in the extracellular transport of proteins between cells through the release in the extracellular space of microvesicles. By participating in the ITCH-mediated ubiquitination and subsequent degradation of NOTCH1, negatively regulates the NOTCH signaling pathway.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22315426, ECO:0000269|PubMed:27462458}. Note=Also found in extracellular vesicles different from exosomes. {ECO:0000269|PubMed:22315426, ECO:0000269|PubMed:27462458}.
Interaction partners:
- Tumor susceptibility gene 101 protein
- NEDD4-like E3 ubiquitin-protein ligase WWP2
- E3 ubiquitin-protein ligase NEDD4
- E3 ubiquitin-protein ligase Itchy homolog
- NEDD4-like E3 ubiquitin-protein ligase WWP1
- Vacuolar protein sorting-associated protein 37A
- E3 ubiquitin-protein ligase HECW2
- Transcriptional coactivator YAP1
Sequence:
MGRVQLFEISLSHGRVVYSPGEPLAGTVRVRLGAPLPFRAIRVTCIGSCGVSNKANDTAWVVEEGYFNSSLSLADKGSLPAGEHSFPFQFLLPATAPTSFEGPFGKIVHQVRAAIHTPRFSKDHKCSLVFYILSPLNLNSIPDIEQPNVASATKKFSYKLVKTGSVVLTASTDLRGYVVGQALQLHADVENQSGKDTSPVVASLLQKVSYKAKRWIHDVRTIAEVEGAGVKAWRRAQWHEQILVPALPQSALPGCSLIHIDYYLQVSLKAPEATVTLPVFIGNIAVNHAPVSPRPGLGLPPGAPPLVVPSAPPQEEAEAEAAAGGPHFLDPVFLSTKSHSQRQPLLATLSSVPGAPEPCPQDGSPASHPLHPPLCISTGATVPYFAEGSGGPVPTTSTLILPPEYSSWGYPYEAPPSYEQSCGGVEPSLTPES
Protein: Cytochrome P450 2C2 (EC 1.14.14.1) (CYPIIC2) (Cytochrome P450 PBc2) (Cytochrome P450 PHP2) (Laurate omega-1 hydroxylase) (P00181)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. In the epoxidation of arachidonic acid it generates only 14,15- and 11,12-cis-epoxyeicosatrienoic acids.
Subcellular location: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Interaction partners:
- Cytochrome P450 1A2
- Cytochrome P450 7A1
- Cytochrome P450 26B1
- Epoxide hydrolase 1
- Cytochrome P450 family 4 subfamily F member 2
- Uncharacterized protein
- Cytochrome P450 26A1
- Cytochrome P450 4A7
- 3-beta hydroxysteroid dehydrogenase/isomerase domain-containing protein
- Cytochrome P450 1A1
Sequence:
MDLVVVLGLCLSCLLLPSLWKQSHGGGKLPPGPTPFPILGNVLQLDFKDLSKSLTNLSKVYGPVFTVYLGMKPTVVVHGYEAVKEALVDLGHELSGRSRFLVTAKLNKGFGVIFSNGKRWTETRRFSLMTLRNFGMGKRSIEERVQEEAHCLVEELRKTNASPCDPTFILGAAPCNVICSVIFQNRFDYTDQDFLSLMGKFNENFKILNSPWVQFCNCFPILFDYFPGSHRKAVKNIFYVKNYITEQIKEHQKSLDINNPRDFIDCFLIKMEQEKCNQQSEFTIENLLTTVSDVFMAGTETTSTTLRYGLLLLMKHPEVIAKVQEEIERVIGRHRSPCMQDRSRMPYTDATVHEIQRYINLIPNNVPHTTICNLKFRNYLIPKGTDVLTSLSSVLHDDKEFPNPDRFDPGHFLDASGNFRKSDYFMPFSTGKRVCVGEALARMELFLFLTAILQNFTPKPLVNPNNVDENPFSSGIVRVPPLYRVSFIPV
Protein: Phospholipase C (PLC) (EC 3.1.4.3) (Alpha-toxin) (Hemolysin) (Lecithinase) (Phosphatidylcholine cholinephosphohydrolase) (P0C216)
Organism: Clostridium perfringens (strain 13 / Type A)
Function: Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture. Constitutes an essential virulence factor in gas gangrene. Binds to eukaryotic membranes where it hydrolyzes both phosphatidylcholine and sphingomyelin. The diacylglycerol produced can activate both the arachidonic acid pathway, leading to modulation of the inflammatory response cascade and thrombosis, and protein kinase C, leading to activation of eukaryotic phospholipases and further membrane damage. Acts on human and mouse erythrocytes, but not on rabbit or horse erythrocytes.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Cardiolipin synthase
- Cardiolipin synthase
- Probable diacylglycerol kinase
- Cardiolipin synthase
- Phosphatidylserine decarboxylase proenzyme
- Cardiolipin synthase
- CDP-diacylglycerol--serine O-phosphatidyltransferase
- Perfringolysin O
Sequence:
MKRKICKALICATLATSLWAGASTKVYAWDGKIDGTGTHAMIVTQGVSILENDLSKNEPESVRKNLEILKENMHELQLGSTYPDYDKNAYDLYQDHFWDPDTDNNFSKDNSWYLAYSIPDTGESQIRKFSALARYEWQRGNYKQATFYLGEAMHYFGDIDTPYHPANVTAVDSAGHVKFETFAEERKEQYKINTAGCKTNEDFYADILKNKDFNAWSKEYARGFAKTGKSIYYSHASMSHSWDDWDYAAKVTLANSQKGTAGYIYRFLHDVSEGNDPSVGKNVKELVAYISTSGEKDAGTDDYMYFGIKTKDGKTQEWEMDNPGNDFMTGSKDTYTFKLKDENLKIDDIQNMWIRKRKYTAFPDAYKPENIKIIANGKVVVDKDINEWISGNSTYNIK
Protein: Pyrin domain-containing protein 2 (Pyrin-only protein 2) (cellular POP2) (cPOP2) (Q56P42)
Organism: Homo sapiens (Human)
Function: May play a role in innate immunity by disrupting the interaction between PYCARD and NLRP3, thereby regulating the NLRP3 inflammasome. May also inhibit NF-kappa-B signaling distally by affecting the nuclear accumulation of RELA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17178784, ECO:0000269|PubMed:17339483}. Nucleus {ECO:0000269|PubMed:17178784, ECO:0000269|PubMed:17339483}. Note=Recruited to specks formed by PYCARD within the cytoplasm. {ECO:0000269|PubMed:17178784}.
Interaction partners:
- Apoptosis-associated speck-like protein containing a CARD
Sequence:
MASSAELDFNLQALLEQLSQDELSKFKSLIRTISLGKELQTVPQTEVDKANGKQLVEIFTSHSCSYWAGMAAIQVFEKMNQTHLSGRADEHCVMPPP
Protein: Proline-rich acidic protein 1 (Pregnancy-specific uterine protein) (Uterine-specific proline-rich acidic protein) (Q80XD8)
Organism: Mus musculus (Mouse)
Function: Lipid-binding protein which promotes lipid absorption by facilitating MTTP-mediated lipid transfer (mainly triglycerides and phospholipids) and MTTP-mediated apoB lipoprotein assembly and secretion. Protects the gastrointestinal epithelium from irradiation-induced apoptosis. May play an important role in maintaining normal growth homeostasis in epithelial cells (By similarity). Involved in p53/TP53-dependent cell survival after DNA damage (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:33168624}. Endoplasmic reticulum {ECO:0000269|PubMed:33168624}.
Interaction partners:
Sequence:
MKRFLLATCLVAALLWEAGAAPAHQVPVKTKGKHVFPEQETEKVWDTRALEPLEKDNQLGPLLPEPKQKPAAAEEKRPDAMTWVETEDILSHLRSPLQGPELDLDSIDHPMSDDVQDEEVPQSRPILYRQVLQGPEEDLDHLAHSMEDS
Protein: Glycolipid sulfotransferase Rv1373 (EC 2.8.2.-) (P9WGB9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the synthesis of cell wall sulfolipids with activity towards mycobacterial trehalose glycolipids and eukaryotic glycolipids such as glucosylceramide and galactosylceramide (type I and II) but not towards eukaryotic 3'-sulfate galactosylceramide.
Interaction partners:
- Probable conserved membrane protein
- Fumarate reductase subunit C
- Fumarate reductase iron-sulfur subunit
- Alpha-pyrone synthesis polyketide synthase-like Pks18
Sequence:
MNSEHPMTDRVVYRSLMADNLRWDALQLRDGDIIISAPSKSGLTWTQRLVSLLVFDGPDLPGPLSTVSPWLDQTIRPIEEVVATLDAQQHRRFIKTHTPLDGLVLDDRVSYICVGRDPRDAAVSMLYQSANMNEDRMRILHEAVVPFHERIAPPFAELGHARSPTEEFRDWMEGPNQPPPGIGFTHLKGIGTLANILHQLGTVWVRRHLPNVALFHYADYQADLAGELLRPARVLGIAATRDRARDLAQYATLDAMRSRASEIAPNTTDGIWHSDERFFRRGGSGDWQQFFTEAEHLRYYHRINQLAPPDLLAWAHEGRRGYDPAN
Protein: Aromatic amino acid aminotransferase C569.07 (EC 2.6.1.57) (Q9Y7S6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has aromatic amino acid transaminase activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Aspartate aminotransferase, mitochondrial
- Tryptophan synthase
- Aspartate aminotransferase, cytoplasmic
- Putative prephenate dehydratase
- Probable prephenate dehydrogenase [NADP
- Chorismate mutase
- Chorismate synthase
- Homoisocitrate dehydrogenase
- L-2-aminoadipate reductase
- Multifunctional tryptophan biosynthesis protein
Sequence:
MDNLKKKYQHHLSLESASREYGPFQMLGRIQSDSDIKMLSFAGGEPNPSKFPIHKLSVSFPEVNSWEKDTNKDATVSYELSNNANEGSLDLLGALQYGQCQGIPELVKFIKDHVGQIHMPQYKDWDIKITNGNTIGLEYCLRLLVNRGDCILIEKYTYPAAITAMRPLGVKFIPIDMDENGMLPESFEKVMETWDSSLGARPHVLYTIPTGQNPTGSTLTLERRKKFLTLAKKYDIIIVEDEPYYFLQMEKYDANWKPDKQAFNISSFKKKLIPSLLHLDTDGRVLRVDSFSKLIVPGLRLGWITGNSLFIDRITRYAEVCTESPSGVSQVVLYAILNRWGQNGFLEWLQDLQNSYTMRRNALLLAADKHLPKSVCKYHSPKAGLFLWVELDKNRLICSNMDKSISEIEMEIFVELVNNGVKPVCGQLFMGEPNSADKIFFRFAYSLADLSTFEAGLERFTSTIQKYFQL
Protein: Vesicle-fusing ATPase (EC 3.6.4.6) (B7ZV62)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU367045}.
Interaction partners:
- Synaptosomal-associated protein 25-A
- Sec1 family domain-containing 1
- UBX domain protein 7.
- N-ethylmaleimide-sensitive factor attachment protein, gamma b.
- Synaptotagmin
- N-ethylmaleimide-sensitive factor attachment protein, beta b
- Synaptosomal-associated protein 25-B
- N-ethylmaleimide sensitive fusion protein attachment protein alpha
- Vesicle-associated membrane protein 3
- Synaptobrevin homolog YKT6
Sequence:
MATRTMQAARCPTDELSLTNCAVVSEKDLQSGQHVTVRTTPTHKFVFTVKGHHSVLPGTIAFSLPQRKWAGLSIGQEIEVSNYNFDKSRQCIGAMTIEIDFLQKKSTDSSPYDSDKMAAEFIQHFNNQSFSVGQQLVFSFCDKLFGLLIKDIEAMDSSILKGEPASGKKQKIEVGLLVGNSQVIFEKSESSSLTLVGKAKTKEARQTIINPDWNFEKMGIGGLDKEFSDIFRRAFASRVFPPDIVEQMGCKHVKGILLFGPPGCGKTLMARQIGKMLNAREPKIVNGPEILNKYVGESEANIRKLFADAEEEQKRLGANSGLHIIIFDELDAICKQRGTGASSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRPDLIDEALMRPGRFEVKMEIGLPDEKGRVQILNIHTAKMREFKLLASDVDVKELAAETKNYSGAELEGLVRAAQSTAMNRHIKATSTVEVDMERAEKLQVTRTDFMASLNNDIKPAFGTNQEDYSSYIMNGIIKWGDPVTRVLEDGELLVQQTKNSDRTPLVSVLLEGPPHSGKTALAAKISEDSQFPFIKICSPDKMIGHSEISKCQAIKKIFDDAYKSQLSCVVVDDIERLLDYVPIGPRFSNLVLQALLVLLKKTPPHGRKLLIIGTTSRKDVLQEMEMLDAFSTTIHVQNISSGDHLVEALELLGSFTDAERTTIAQHVKGKRVWIGIKKLLMLIEMSLQMDQEYRVSKFLSLLKDEGADRGFFE
Protein: AP2 domain transcription factor AP2-G (Q8I5I9)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MTAKILNPFDIPVYPSSKACKYEFNFPTRKESTFDYIPGKSIETNCSKENMVQPKHLNLLKMLKKYMYEIIEESCFDIKSFNNISNGKRACNEVFYNLEDTIINDSRMNIKNKILQSNENVSNSCMDKKAICKKLDMLLNHRIEGNYCQDDVSNNASLQLMQKGKEDKGNERIYCCTTKDVILHAHKPTMNYMNSYKLSSDYISKLHLFIVKKEKVLFFPILYAEMIIRYNMKFFPLSKLYNIKNTASLMKCKRVFSYVIILHFLMNSICVTYSDDIHSSLYKNNDVMYFYVIKGKEVGLYEITKFPMNHISYDMNIFNDSKTYIGNMNYILEKNIEEHLFDNMYFILSSISYKNVFHMNIMHIHMKCYSNQTCMDLNKCFNFVKDIYISRKQNMCIIIGTIKIDHMFCTCSCGSTANSNMENKNSNNNNNNNNNTGSKQSVNNSRASNNRKRINNTSSNNGNDDDEDEKYQNKRKKYFDDCNMKDEHKKEGKNKQKNKKNNKNKKNNKNNNINNINNINNNNNNNNNNSNNNNNNNNNNNNNNNNNNNSFYNDCVLTNNSFKGYMEENNFILNSHSSNSLDMGTHICYNYQNKINHNITKQCNDNNNTVFHNNYSHKDNVKVLNNIYNNIITDKERESNDNDSTKQSMLNDDDADKLDNIKLNNYIYSNMNDYFTICDPNINIDKTTLHENYLRFQPNVLEKDVNGGNKHMTMRYIDNFKHNSISNHNNNNNNSNNNNNSNNSNNNNNSNNSNNSNRLYNISSEALNSLKKNDSLYMRLQNIISFSSGHNNTKIKVININNFNNNANKFKNLNMDNMNAPNGVTNLNVGINNEVVKEEKTNTCLNINEQIHSHTKLKCIKNGKPRNINQKENNVVYIESDNSHNDNNNNNNNNNNNNNNNNNNNNNNNNNNSFENNMLLLCKSKNVKNQNRMNNLFRKEENKDTKLKSLNYNILINPCYNKNNVINELFMNTKEKSLYGNTNKFHNTLNNNMNMNNYNNQNINNIYPLTHNISIVNHILNHSYYNENTEQNNKNLFHNTILVPKNCNNIMNNSDKYNYLNAYNQNYTLYNNTLNNNNSLVQPSDVNNMNCSYESINGNMPINDQSCDTYNDEYNDTYNDTYNDTYNDTYNDTHNDTHNDTHNDTYNDEYNDTYNEINNETYNDTLNDTPNDTLYDTLNGITNDTPYITPTNACNLSYEELMYKMQNNNNIYCKKHDSNYIISNGINNHICAHKEVNYNVLNHVTNINTYVNSKNIFSNVAVTNDTDLHACNNEQRNNISNHNINKNVVNLNNVHSINKELNNYPINSTQDYNTNYDKNGCLGTLTCDIKNKNNKNNKNNKNNKNNKNNKNNKNKNNNDNNNNNNNNNNNSNNNKDIIILNKNNINNANIFNINSLKEKLLNDDISKNKEKKKKKCVIRKIKKRNKVNPKRNNNINNRNKNNGSYKCDTKRVNKINNGFMKNFKNKYTSSCINYNMCAISDLSTNIKNKENFVIGNYPYTNGVSYITNGENNTTNNGKKNDDHRNKKKEYNSNENNNYCNNNSNRNNNNNNNNSHFGGNKNNRGDDNDEDDQEKNNKRNIYGKNGDDEEEDYDGEDDNNEENDHNNKKNIKRKNKKSNKAYNNNDDENKCINNKDTFHLPKKHNYEYTMNNNYNMNNEYNKDDEEIKNNYEDNQDNGDIKHKSCTNGNDVDGVKSKYHKNDHSGDNNNDINNNSDSNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNSCTNNCATVDDLMNLNSSNLGKFSYLTNVLSHNINNINFINNNNHKMNFLNNENVNQFFNNMNYKDYVNNMNYLEPNNYINHNINELNYFNKNMILNNLNYINYVNGINNDRYMNGINNSQMSYNNHFRNDIISNVLKGVRVINKESHYKNKNNKNGNSNNNNNNNNNNNNEDEDDDNNQNNNNDNDGDDNNDNDNNEENNNIDDRIPFKHHNMNNVSMKNNDGKNEDNNNNKNNNNNNNNNNNNNNNNSNDNNNNRNGNNNIINPFFLYNKMFCMNNNANNFNNGNIINNFTNNGMAHNHNPNMNINSFRNNNMHLFHKYGIQYKDLIPMNMFPTAYLNLGRERRSSKYENSSYNKKKDLMKRRYELQKAILLNVDENLKEVIDEIIRNSTILPQKGIRGRNTLDCNHPIHSVWKDTTRGHCSWRCRWWENGRRLSKNFNVKRFGNDGALRMAITMKLKKSNPKEQMQLLKQQREYLKLCYGDNWEKKIKELQNVNNANQTVNNNNNNINKNNIDNNNQNDNNSSKSNNSNNSNNNSNNQHYVSANADINNDATITFNNPLNNKNVPYQYLNLKDKKQTFQQYNHIKDRENSYPYMHIKGETQQNGMKLKNDINNHHSQNQLSLSKQENNIYKNNVMDEKLLIQNLKACINESNNNNNNNNYNVQKRIQNNYYHKGGNNRNI
Protein: Isocitrate dehydrogenase [NADP] (IDH) (EC 1.1.1.42) (IDP) (NADP(+)-specific ICDH) (Oxalosuccinate decarboxylase) (P39126)
Organism: Bacillus subtilis (strain 168)
Interaction partners:
- Aconitate hydratase A
- Malate dehydrogenase
- Citrate synthase 2
- 2-oxoglutarate dehydrogenase E1 component
- Citrate synthase 1
- Citrate/2-methylcitrate synthase
- Succinate--CoA ligase subunit beta
- Succinate--CoA ligase subunit alpha
- Cryptic catabolic NAD-specific glutamate dehydrogenase GudB
- Succinate dehydrogenase iron-sulfur subunit
Sequence:
MAQGEKITVSNGVLNVPNNPIIPFIEGDGTGPDIWNAASKVLEAAVEKAYKGEKKITWKEVYAGEKAYNKTGEWLPAETLDVIREYFIAIKGPLTTPVGGGIRSLNVALRQELDLFVCLRPVRYFTGVPSPVKRPEDTDMVIFRENTEDIYAGIEYAKGSEEVQKLISFLQNELNVNKIRFPETSGIGIKPVSEEGTSRLVRAAIDYAIEHGRKSVTLVHKGNIMKFTEGAFKNWGYELAEKEYGDKVFTWAQYDRIAEEQGKDAANKAQSEAEAAGKIIIKDSIADIFLQQILTRPNEFDVVATMNLNGDYISDALAAQVGGIGIAPGANINYETGHAIFEATHGTAPKYAGLDKVNPSSVILSGVLLLEHLGWNEAADLVIKSMEKTIASKVVTYDFARLMDGATEVKCSEFGEELIKNMD
Protein: Torsin-2A (Torsin family 2 member A) (Q8R1J9)
Organism: Mus musculus (Mouse)
Subcellular location: Endoplasmic reticulum lumen {ECO:0000269|PubMed:20015956}.
Interaction partners:
- Torsin-1A-interacting protein 2
Sequence:
MAVARHGYRPWGSILGLLGLALAAAAAWDVASLRCTFGSFCECDFWPDLPGLECDLAQHLAGQHLAKALVVKSLKAFVQDPAPSKPLVLSLHGWTGTGKSYVSSLLAQHLFRDGLRSPHVHHFSPIIHFPHPSRTEQYKKELKSWVQGNLTACGRSLFLFDEMDKLPPGLMEVLQPFLGPSWVVYGTNYRKAIFIFISNAGGEQINQVALEAWRSHRDREEISLQEVEPVISRAVMDNPQHGFWRSGIMEEHLLDAVVPFLPLQRHHVRHCVLNELAQLGLEPSEEVVQAVLDSTTYFPEVEQLFSSNGCKTVASRLTFFL
Protein: Protein unc-13 homolog D (Munc13-4) (Q70J99)
Organism: Homo sapiens (Human)
Function: Plays a role in cytotoxic granule exocytosis in lymphocytes. Required for both granule maturation and granule docking and priming at the immunologic synapse. Regulates assembly of recycling and late endosomal structures, leading to the formation of an endosomal exocytic compartment that fuses with perforin-containing granules at the immunologic synapse and licences them for exocytosis. Regulates Ca(2+)-dependent secretory lysosome exocytosis in mast cells.
Subcellular location: Cytoplasm. Membrane; Peripheral membrane protein. Late endosome. Recycling endosome. Lysosome. Note=Colocalizes with cytotoxic granules at the plasma membrane. Localizes to endosomal exocytic vesicles.
Interaction partners:
- Ras-related protein Rab-27A
- Syntaxin-11
- Syntaxin-binding protein 2
- Perforin-1
- Ras-related protein Rab-27B
- Syntaxin-19
- Four and a half LIM domains protein 2
- Lysosomal-trafficking regulator
- Protein S100-A10
- SH2 domain-containing protein 1A
Sequence:
MATLLSHPQQRPPFLRQAIKIRRRRVRDLQDPPPQMAPEIQPPSHHFSPEQRALLYEDALYTVLHRLGHPEPNHVTEASELLRYLQEAFHVEPEEHQQTLQRVRELEKPIFCLKATVKQAKGILGKDVSGFSDPYCLLGIEQGVGVPGGSPGSRHRQKAVVRHTIPEEETHRTQVITQTLNPVWDETFILEFEDITNASFHLDMWDLDTVESVRQKLGELTDLHGLRRIFKEARKDKGQDDFLGNVVLRLQDLRCREDQWYPLEPRTETYPDRGQCHLQFQLIHKRRATSASRSQPSYTVHLHLLQQLVSHEVTQHEAGSTSWDGSLSPQAATVLFLHATQKDLSDFHQSMAQWLAYSRLYQSLEFPSSCLLHPITSIEYQWIQGRLKAEQQEELAASFSSLLTYGLSLIRRFRSVFPLSVSDSPARLQSLLRVLVQMCKMKAFGELCPNTAPLPQLVTEALQTGTTEWFHLKQQHHQPMVQGIPEAGKALLGLVQDVIGDLHQCQRTWDKIFHNTLKIHLFSMAFRELQWLVAKRVQDHTTVVGDVVSPEMGESLFQLYISLKELCQLRMSSSERDGVLALDNFHRWFQPAIPSWLQKTYNEALARVQRAVQMDELVPLGELTKHSTSAVDLSTCFAQISHTARQLDWPDPEEAFMITVKFVEDTCRLALVYCSLIKARARELSSGQKDQGQAANMLCVVVNDMEQLRLVIGKLPAQLAWEALEQRVGAVLEQGQLQNTLHAQLQSALAGLGHEIRTGVRTLAEQLEVGIAKHIQKLVGVRESVLPEDAILPLMKFLEVELCYMNTNLVQENFSSLLTLLWTHTLTVLVEAAASQRSSSLASNRLKIALQNLEICFHAEGCGLPPKALHTATFQALQRDLELQAASSRELIRKYFCSRIQQQAETTSEELGAVTVKASYRASEQKLRVELLSASSLLPLDSNGSSDPFVQLTLEPRHEFPELAARETQKHKKDLHPLFDETFEFLVPAEPCRKAGACLLLTVLDYDTLGADDLEGEAFLPLREVPGLSGSEEPGEVPQTRLPLTYPAPNGDPILQLLEGRKGDREAQVFVRLRRHRAKQASQHALRPAP
Protein: Ubiquinone biosynthesis O-methyltransferase, mitochondrial (3-demethylubiquinol 3-O-methyltransferase) (EC 2.1.1.64) (3-demethylubiquinone 3-O-methyltransferase) (EC 2.1.1.-) (Polyprenyldihydroxybenzoate methyltransferase) (EC 2.1.1.114) (Q9NZJ6)
Organism: Homo sapiens (Human)
Function: O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Subcellular location: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03190, ECO:0000269|PubMed:27499296}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03190}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03190}.
Interaction partners:
- NADPH-dependent 3-demethoxyubiquinone 3-hydroxylase, mitochondrial
- Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial
- Ubiquinone biosynthesis protein COQ9
- 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
- Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial
- Atypical kinase COQ8A, mitochondrial
- Atypical kinase COQ8B, mitochondrial
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- All trans-polyprenyl-diphosphate synthase PDSS1
- dTDP-D-glucose 4,6-dehydratase
Sequence:
MWSGRKLGSSGGWFLRVLGPGGCNTKAARPLISSAVYVKNQLSGTLQIKPGVFNEYRTIWFKSYRTIFSCLNRIKSFRYPWARLYSTSQTTVDSGEVKTFLALAHKWWDEQGVYAPLHSMNDLRVPFIRDNLLKTIPNHQPGKPLLGMKILDVGCGGGLLTEPLGRLGASVIGIDPVDENIKTAQCHKSFDPVLDKRIEYRVCSLEEIVEETAETFDAVVASEVVEHVIDLETFLQCCCQVLKPGGSLFITTINKTQLSYALGIVFSEQIASIVPKGTHTWEKFVSPETLESILESNGLSVQTVVGMLYNPFSGYWHWSENTSLNYAAYAVKSRVQEHPASAEFVLKGETEELQANACTNPAVHEKLKK
Protein: Delta-9 acyl-lipid desaturase 2 (EC 1.14.19.75) (Q9SID2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in delta-9 desaturation of fatty acids (Probable). Plays a role in the production of very-long-chain monounsaturated fatty acids (VLCMUFAs) in seed lipids and in membrane phospholipids and sphingolipids. Acts as C-16:0 desaturase for monogalactosyl diacylglycerol (MGDG) and phosphatidylglycerol (PG). Is an essential component for cold adaptation. Is essential to adjust the acyl composition of organelle membrane lipid composition in response to cold stress.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23175755}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Delta
- Delta
- sn-2 acyl-lipid omega-3 desaturase
- very-long-chain 3-oxoacyl-CoA synthase
- Omega-6 fatty acid desaturase, chloroplastic
- Sphinganine C4-monooxygenase 1
- Acyl-lipid omega-3 desaturase
- Dihydroceramide fatty acyl 2-hydroxylase FAH2
- Delta
- Fatty acid desaturase 4, chloroplastic
Sequence:
MSVTSTVEENHQKNPSTPAAVEEKKKRRWVFWDRRWRRLDYVKFSASFTVHSLALLAPFYFTWSALWVTFLFYTIGGLGITVSYHRNLAHRSFKVPKWLEYLLAYCALLAIQGDPIDWVSTHRYHHQFTDSERDPHSPKEGFWFSHLLWIYDSAYLVSKCGRRANVEDLKRQWFYRFLQKTVLFHILGLGFFLFYLGGMSFVTWGMGVGAALEVHVTCLINSLCHIWGTRTWKTNDTSRNVWWLSVFSFGESWHNNHHAFESSARQGLEWWQIDISWYIVRFFEIIGLATDVKVPTEAQRRRMAIVR
Protein: Ferric transport regulator protein (Q9A1M6)
Organism: Streptococcus pyogenes serotype M1
Interaction partners:
Sequence:
MDIHSHQQALDAYENVLEHLREKHIRITETRKAIISYMIQSTEHPSADKIYRDLQPNFPNMSLATVYNNLKVLVDEGFVSELKISNDLTTYYDFMGHQHVNVVCEICGKIADFMDVDVMDIAKEAHEQTGYKVTRIPVIAYGICPDCQAKDQPDF