wanglab/gogpt-training-data huggingface dataset:
Protein: Natriuretic peptide Coa_NP2 (B3EWY2)
Organism: Crotalus lutosus abyssus (Grand Canyon rattlesnake) (Crotalus oreganus abyssus)
Function: Snake venom natriuretic peptide that exhibits hypotensive and vasorelaxant effects. Produces a dose-dependent hypotension in rats, followed by significant increases in concentrations of markers of nitric oxide (NO) formation measured in the plasma and vasorelaxation in a thoracic aortic ring bath. The peptide may exert its hypotensive action, at least in part, through stimulation of NO production. The vasorelaxant effect is endothelium-dependent and does not appear to be mediated by the natriuretic peptide receptor-A, as its action is not modified by isatin (a potent NPR1 antagonist). May act by activating the natriuretic peptide receptor-B (NPR2).
Subcellular location: Secreted {ECO:0000269|PubMed:22617223}.
Interaction partners:
Sequence:
SYGISSGCFGLKLDRIGTMSGLGCWRLLQDSP
Protein: High affinity cationic amino acid transporter 1 (CAT-1) (CAT1) (Ecotropic retroviral leukemia receptor) (Ecotropic retrovirus receptor) (ERR) (EcoR) (Solute carrier family 7 member 1) (System Y+ basic amino acid transporter) (Q09143)
Organism: Mus musculus (Mouse)
Function: High-affinity, low capacity permease involved in the transport of the cationic amino acids (arginine, lysine and ornithine) in non-hepatic tissues.
Subcellular location: Cell membrane {ECO:0000269|PubMed:25683716, ECO:0000269|PubMed:28973536}; Multi-pass membrane protein {ECO:0000255}. Note=In the absence of SCO1 in cardiomyocytes a mislocalization to the cytoplasm is seen. {ECO:0000269|PubMed:28973536}.
Interaction partners:
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Peroxisome proliferator-activated receptor gamma coactivator 1-beta
- Nuclear receptor-interacting protein 1
- Neutral amino acid transporter B
- Steroid hormone receptor ERR1
- Steroid hormone receptor ERR2
- Neutral amino acid transporter A
- Solute carrier family 7 member 12
Sequence:
MGCKNLLGLGQQMLRRKVVDCSREESRLSRCLNTYDLVALGVGSTLGAGVYVLAGAVARENAGPAIVISFLIAALASVLAGLCYGEFGARVPKTGSAYLYSYVTVGELWAFITGWNLILSYIIGTSSVARAWSATFDELIGKPIGEFSRQHMALNAPGVLAQTPDIFAVIIIIILTGLLTLGVKESAMVNKIFTCINVLVLCFIVVSGFVKGSIKNWQLTEKNFSCNNNDTNVKYGEGGFMPFGFSGVLSGAATCFYAFVGFDCIATTGEEVKNPQKAIPVGIVASLLICFIAYFGVSAALTLMMPYFCLDIDSPLPGAFKHQGWEEAKYAVAIGSLCALSTSLLGSMFPMPRVIYAMAEDGLLFKFLAKINNRTKTPVIATVTSGAIAAVMAFLFELKDLVDLMSIGTLLAYSLVAACVLVLRYQPEQPNLVYQMARTTEELDRVDQNELVSASESQTGFLPVAEKFSLKSILSPKNVEPSKFSGLIVNISAGLLAALIITVCIVAVLGREALAEGTLWAVFVMTGSVLLCMLVTGIIWRQPESKTKLSFKVPFVPVLPVLSIFVNIYLMMQLDQGTWVRFAVWMLIGFTIYFGYGIWHSEEASLAAGQAKTPDSNLDQCK
Protein: Cytosolic phospholipase A2 delta (cPLA2-delta) (EC 3.1.1.4) (Phospholipase A2 group IVD) (Q86XP0)
Organism: Homo sapiens (Human)
Function: Calcium-dependent phospholipase A2 that selectively hydrolyzes glycerophospholipids in the sn-2 position. Has a preference for linoleic acid at the sn-2 position.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q50L43}. Membrane {ECO:0000250|UniProtKB:Q50L43}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q50L43}; Cytoplasmic side {ECO:0000250|UniProtKB:Q50L43}. Note=Translocates to perinuclear membranes that may correspond to endoplasmic reticulum or Golgi in a calcium-dependent fashion. {ECO:0000250|UniProtKB:Q50L43}.
Interaction partners:
- Phospholipase A2 group V
- Mitogen-activated protein kinase 3
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
- Guanine nucleotide-binding protein G
- Mitogen-activated protein kinase 1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2
- Guanine nucleotide-binding protein G
- Cholinephosphotransferase 1
- Lysosomal phospholipase A and acyltransferase
- Patatin-like phospholipase domain-containing protein 6
Sequence:
MESLSPGGPPGHPYQGEASTCWQLTVRVLEARNLRWADLLSEADPYVILQLSTAPGMKFKTKTLTDTSHPVWNEAFRFLIQSQVKNVLELSIYDEDSVTEDDICFKVLYDISEVLPGKLLRKTFSQSPQGEEELDVEFLMEETSDRPENLITNKVIVARELSCLDVHLDSTGSTAVVADQDKLELELVLKGSYEDTQTSFLGTASAFRFHYMAALETELSGRLRSSRSNGWNGDNSAGYLTVPLRPLTIGKEVTMDVPAPNAPGVRLQLKAEGCPEELAVHLGFNLCAEEQAFLSRRKQVVAKALKQALQLDRDLQEDEVPVVGIMATGGGARAMTSLYGHLLALQKLGLLDCVTYFSGISGSTWTMAHLYGDPEWSQRDLEGPIRYAREHLAKSKLEVFSPERLASYRRELELRAEQGHPTTFVDLWALVLESMLHGQVMDQKLSGQRAALERGQNPLPLYLSLNVKENNLETLDFKEWVEFSPYEVGFLKYGAFVPPELFGSEFFMGRLMRRIPEPRICFLEAIWSNIFSLNLLDAWYDLTSSGESWKQHIKDKTRSLEKEPLTTSGTSSRLEASWLQPGTALAQAFKGFLTGRPLHQRSPNFLQGLQLHQDYCSHKDFSTWADYQLDSMPSQLTPKEPRLCLVDAAYFINTSSPSMFRPGRRLDLILSFDYSLSAPFEALQQTELYCRARGLPFPRVEPSPQDQHQPRECHLFSDPACPEAPILLHFPLVNASFKDHSAPGVQRSPAELQGGQVDLTGATCPYTLSNMTYKEEDFERLLRLSDYNVQTSQGAILQALRTALKHRTLEARPPRAQT
Protein: Inositol polyphosphate-5-phosphatase F (A0A3B3ITL0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEPQDLELELCKKHHFGINKPEKIIPSPDDSKFLLKTFTHIKSNVSAPNKKKVKESKEKEKLERRLLEELLKMFMDSESFYYSLTYDLTNSVQRQSTGERDGRPLWQKVDDRFFWNKYMIQDLTEIGTPDVDFWIIPMIQGFVQIEELVVNYTESSDDEKSSPETPPQESTCVDDIHPRFLVALISRRSRHRAGMRYKRRGVDKNGNVANYVETEQLIHVHNHTLSFVQTRGSVPVFWSQVGYRYNPRPRLDRSEKETVAYFCAHFEEQLNIYKKQVIINLVDQAGREKIIGDAYLKQVLLFNNSHLTYVSFDFHEHCRGMKFENVQTLTDAIYDIILDMKWCWVDEAGVICKQEGIFRVNCMDCLDRTNVVQAAIARVVMEQQLKKLGVMPPEQPLPVKCNRIYQIMWANNGDSISRQYAGTAALKGDFTRTGERKLAGVMKDGVNSANRYYLNRFKDAYRQAVIDLMQGIPVTEDLYSIFTKEKEHEALHKENQRSHQELISQLLQSYMKLLLPDDEKFHGGWALIDCDPSLIDATHRDVDVLLLLSNSAYYVAYYDDEVDKVNQYQRLSLENLEKIEIGPEPTLFGKPKFSCMRLHYRYKEASGYFHTLRAVMRNPEEDGKDTLQCIAEMLQITKQAMGSDLPIIEKKLERKSSKPHEDIIGIRSQNQGSLAQGKNFLMSKFSSLNQKVKQTKSNVNIGNLRKLGNFTKPEMKVNFLKPNLKVNLWKSDSSLETMENTGVMDKVQAESDGDMSSDNDSYHSDEFLTNSKSDEDRQLANSLESVGPIDYVLPSCGIIASAPRLGSRSQSLSSTDSSVHAPSEITVAHGSGLGKGQESPLKKSPSAGDVHILTGFAKPMDIYCHRFVQDAQNKVTHLSETRSVSQQASQERNQMTNQVSNETQSESTEQTPSRPSQLDVSLSATGPQFLSVEPAHSVASQKTPTSASSMLELETGLHVTPSPSESSSSRAVSPFAKIRSSMVQVASITQAGLTHGINFAVSKVQKSPPEPEIINQVQQNELKKMFIQCQTRIIQI
Protein: Glutamate receptor ionotropic, kainate 2 (GluK2) (Glutamate receptor 6) (GluR-6) (GluR6) (Q38PU3)
Organism: Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Function: Ionotropic glutamate receptor. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. Modulates cell surface expression of NETO2.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P42260}; Multi-pass membrane protein {ECO:0000255}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P42260}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Glutamate ionotropic receptor kainate type subunit 5.
- Disks large homolog 4
- Glutamate receptor ionotropic, kainate 1
- Glutamate receptor
- Glutamate receptor ionotropic, kainate 3
- Discs large MAGUK scaffold protein 3
- Metabotropic glutamate receptor 2
Sequence:
MKIIFPILSNPVFRRTVKLLLCLLWIGYSQGTTHVLRFGGIFEYVESGPMGAEELAFRFAVNTINRNRTLLPNTTLTYDTQKINLYDSFEASKKACDQLSLGVAAIFGPSHSSSANAVQSICNALGVPHIQTRWKHQVSDNKDSFYVSLYPDFSSLSRAILDLVQFFKWKTVTVVYDDSTGLIRLQELIKAPSRYNLRLKIRQLPADTKDAKPLLKEMKRGKEFHVIFDCSHEMAAGILKQALAMGMMTEYYHYIFTTLDLFALDVEPYRYSGVNMTGFRILNTENTQVSSIIEKWSMERLQAPPKPDSGLLDGFMTTDAALMYDAVHVVSVAVQQFPQMTVSSLQCNRHKPWRFGTRFMSLIKEAHWEGLTGRITFNKTNGLRTDFDLDVISLKEEGLEKIGTWDPASGLNMTESQKGKPANITDSLSNRSLIVTTILEEPYVLFKKSDKPLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQDDANGQWNGMVRELIDHKADLAVAPLAITYVREKVIDFSKPFMTLGISILYRKPNGTNPGVFSFLNPLSPDIWMYVLLACLGVSCVLFVIARFSPYEWYNPHPCNPDSDVVENNFTLLNSFWFGVGALMRQGSELMPKALSTRIVGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGAVEDGATMTFFKKSKISTYDKMWAFMSSRRQSVLVKSNEEGIQRVLTSDYAFLMESTTIEFVTQRNCNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGKLHMMKEKWWRGNGCPEEESKEASALGVQNIGGIFIVLAAGLVLSVFVAVGEFLYKSKKNAQLEKRSFCSAMVEELRMSLKCQRRLKHKPQAPVIVKTEEVINMHTFNDRRLPGKETMA
Protein: Proton-coupled zinc antiporter SLC30A1 (Solute carrier family 30 member 1) (Zinc transporter 1) (ZnT-1) (Q62720)
Organism: Rattus norvegicus (Rat)
Function: Zinc ion:proton antiporter that could function at the plasma membrane mediating zinc efflux from cells against its electrochemical gradient protecting them from intracellular zinc accumulation and toxicity. Alternatively, could prevent the transport to the plasma membrane of CACNB2, the L-type calcium channels regulatory subunit, through a yet to be defined mechanism. By modulating the expression of these channels at the plasma membrane, could prevent calcium and zinc influx into cells. By the same mechanism, could also prevent L-type calcium channels-mediated heavy metal influx into cells. In some cells, could also function as a zinc ion:proton antiporter mediating zinc entry into the lumen of cytoplasmic vesicles. In macrophages, can increase zinc ions concentration into the lumen of cytoplasmic vesicles containing engulfed bacteria and could help inactivate them (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:24951051, ECO:0000269|PubMed:7882967}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:24951051}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q9Y6M5}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y6M5}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Y6M5}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9Y6M5}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:Q9Y6M5}; Multi-pass membrane protein {ECO:0000255}. Note=Localization to the plasma membrane is regulated by cellular zinc status. Recruitment to the plasma membrane from an internal pool is stimulated by zinc while in absence of zinc the plasma membrane pool is endocytosed and degraded (By similarity). Localizes to the basolateral surface of enterocytes (PubMed:24951051). Localizes to zinc-containing intracellular vesicles in macrophages (By similarity). Localizes in the cytoplasm and to the ER, Golgi and nucleus membranes in keratinocytes (By similarity). {ECO:0000250|UniProtKB:Q9Y6M5, ECO:0000269|PubMed:24951051}.
Interaction partners:
- Transmembrane channel-like protein
- Zinc transporter ZIP6
- Metal cation symporter ZIP8
- Metallothionein 2, pseudogene 1
- Metallothionein
- Zinc transporter 6
- Zinc transporter ZIP13
- Zinc transporter ZIP11
- Solute carrier family 39 member 10
- Zinc transporter ZIP9
Sequence:
MGCWGRNRGRLLCMLLLTFMFMVLEVVVSRVTASLAMLSDSFHMLSDVLALVVALVAERFARRTHATQKNTFGWIRAEVMGALVNAIFLTGLCFAILLEAVERFIEPHEMQQPLVVLSVGVAGLLVNVLGLCLFHHHSGEGQGAGHGHSHGHGHGHLAKGARKAGRAGGEAGAPPGRAPDQEPDQEETNTLVANTSNSNGLKADQAEPEKLRSDDPVDVQVNGNLIQESDSLESEDNRAGQLNMRGVFLHVLGDALGSVIVVVNALVFYFSWKGCTEDDFCVNPCFPDPCKSSVELMNSTQAPMHEAGPCWVLYLDPTLCIIMVCILLYTTYPLLKESALILLQTVPKQIDIKHLVKELRDVEGVEEVHELHVWQLAGSRIIATAHIKCEDPASYMQVAKTIKDVFHNHGIHATTIQPEFASVGSKSSVVPCELACRTQCALKQCCGTRPQVHSGKEAEKAPTVSISCLELSENLEKKPRRTKAEGSVPAVVIEIKNVPNKQPESSL
Protein: RNA pseudouridylate synthase (RNA-uridine isomerase) (O07166)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Possible esterase lipoprotein LpqC
- Probable arylsulfatase AtsB
- Phosphate-specific transport system accessory protein PhoU homolog 1
- Glycerol-3-phosphate dehydrogenase 2
- NAD
- Ribosomal silencing factor RsfS
- Large ribosomal subunit protein bL21
- Large ribosomal subunit protein uL11
- Large ribosomal subunit protein bL17
- Large ribosomal subunit protein uL3
Sequence:
MALRPEDRLLSVHDVLGPVRVRLLGGSVLAELTARFGVAARAKVLAGEVVDDDGAVVDSGTVLPPGSVVHLYRDLPDEVPVPFDVPVLHQDADIVVVDKPHFLATMPRGRHVAQTALVRLRRELGLPELSPAHRLDRLTAGVLLFTTRREVRGSYQTMFARGLVRKTYLARAPVAPGLALPRLVRSRIVKRRGHLQAVCEPGVPNAETLVERIARDGLYRLTPTTGRTHQLRVHMAALGIPIMGDPLYPNVISVAAHDFSTPLQLLAQRIEFDDPLTGSHREFASTRTLTGATLPTWSAAADCRP
Protein: Integral membrane protein (P95129)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MTSTKVEDRVTAAVLGAIGHALALTASMTWEILWALILGFALSAVVQAVVRRSTIVTLLGDDRPRTLVIATGLGAASSSCSYAAVALARSLFRKGANFTAAMAFEIGSTNLVVELGIILALLMGWQFTAAEFVGGPIMILVLAVLFRLFVGARLIDAAREQAERGLAGSMEGHAAMDMSIKREGSFWRRLLSPPGFTSIAHVFVMEWLAILRDLILGLLIAGAIAAWVPESFWQSFFLANHPAWSAVWGPIIGPIVAIVSFVCSIGNVPLAAVLWNGGISFGGVIAFIFADLLILPILNIYRKYYGARMMLVLLGTFYASMVVAGYLIELLFGTTNLIPSQRSATVMTAEISWNYTTWLNVIFLVIAAALVVRFITSGGLPMLRMMGGSPDAPHDHHDRHDDHLGH
Protein: Cyclin-dependent kinase inhibitor 1C (Q69DC1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Cyclin-dependent kinase 2
- Cyclin-A2
- cyclin-dependent kinase
- G1/S-specific cyclin-D1
- G1/S-specific cyclin-E1
- Cyclin-dependent kinase 4
- Cyclin-A1
- S-phase kinase-associated protein 2
- G1/S-specific cyclin-D2
- G1/S-specific cyclin-D3
Sequence:
MGMSDVYLRSRTAMERLASSDTFPVIARSSACRSLFGPVDHEELGRELRMRLAELNAEDQNRWDFNFQQDVPLRGPGRLQWMEVDSESVPAFYRETVQVGRCRLQLGPRPPPVAVAVIPRSGPPAGEGPDGLEEAPEQPPSAPASAVVAEPTPPATPAPASDLTSDPIPDVTPVATSDSTPDPIPDVATQDGEEQVPEQVSEQVSEQGEESGAEPGDELGAEPVSEQGKQQGAEPVEEKDEEPVEEQGAEPVEEKDEEPVEGQNGELVEEQDENQELKDQPLSGIPGRPAAGTAAANANGAIKKLSGPLISDFFAKRKRTAQENKASNDVPAGCPSPNVAPGVGAVEQTPRKRLR
Protein: NFU1 iron-sulfur cluster scaffold homolog, mitochondrial (Q21915)
Organism: Caenorhabditis elegans
Interaction partners:
- cysteine desulfurase
- Iron-sulfur cluster assembly 1 homolog
- NIF system FeS cluster assembly NifU N-terminal domain-containing protein
- 2Fe-2S ferredoxin-type domain-containing protein
- NADPH:adrenodoxin oxidoreductase, mitochondrial
- 2O16
- Selenocysteine lyase
- Frataxin, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Probable NADH dehydrogenase iron-sulfur protein 8, mitochondrial
Sequence:
MISSKMLTRLNRSFVQAARSMYIQVQETPNPLSLKFLPGQQLLPDASKTYDFSSAATAKQSPLAIKLLRVDGVKRVFFGEDFVTVTKSDETVDWALLRPEIFSTIADHIQTGKPVINEAATVSDQVEEDDEVVMMIKEILETRIRPMVQEDGGDITYVGFDDGVVKLKMQGSCTGCPSSGVTLKNGIENMLTFYVPEVKEVIEVKDESDDLVEQELKKFEQSKGIKD
Protein: Rho-related BTB domain containing, isoform C (M9PIB5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPKMDNEQPHQELVKCVLVGDTAVGKTRLICARACNKHVSLSQLLSTHVPTVWAIDQYRIYKDVLERSWEVVDGVNVSLRLWDTFGDHDKDRRFAYGRSDVVLLCFSIASPISLRNCKMMWYPEIRRFCPDVPVILVGCKNDLRYMYRDENYLSYFGEKGTFVRAALKSDLVMPDEARAVAKELGVAYYETSVFTYFGVNEVFENAIRSALIARRQQRFWMTNLKKVQKPLLQAPFRPPKPPPPEVTVMVGNYRQDIYNMFLSQAYTDLVLVGAGGTKFAVHRFMLAAASSIFQRLLSTELTDMGGRSSSESSMVSSTFGEATIADFNDDTEALIRYESRTQRMWEHLKRRSSYQALPLMESKRSNDLYRELHHPVLQSIRLVHVENHRGVNGLQTIVTLSKLISPQALHQCLRFIYTGTIDKDCDNIEEIREAADLLELPQLTQLLSRPQTVMENSSDEPNPHICLRIKESMERHCIGDGCFSDVTFELDDGLMKAHRAVLVGRCDVMRAMLLGDFREAHSNVIVFPGVTIYTFHKLLCYLYTDQIPPISAVKCLNLLELANRLCLPRLLNLVECRVIEDLTLISQNETNETVDHCLKLLEPVKLHNAHQLAEWCMSYLCVNYNLICKFSLKGLKALHQDNQEYLREHRWPPVWYLKDYDYYQRCLNELNKELKLKTSRRESPSDDEGCLCFTGGKSKRSADVSGTTDNSNADNQIFNSAGNSLNHIDLEADMDLNL
Protein: RH70248p (Q8SXD7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSLKSVFLSALRSITMPAVPLQTSRIHTSACWRKAEDRKEMLAFLPAKDEGTVGEKTVDIDTLINELPICNIRVSPNNTIISVTDHKGVLRLIRSCGIEGFKNTRKGTNIAAQATAVTISGKAIELGWKTVRVKVRGLGPGRMSAIKGLQMGGLNIVSITDNTHVSFNPPRPRKQRSL
Protein: Transcription elongation factor SPT5 (E9PTB2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR036945}.
Interaction partners:
- Transcription elongation factor SPT4
- Transcription elongation factor spt6
- RNA polymerase-associated protein LEO1
- FACT complex subunit
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase subunit beta
- RNA polymerase-associated protein RTF1 homolog
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerase II subunit RPB7
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
Sequence:
MSDSEDSNFSEEEDSERSSEAEEAEVEEDRRSAAGSEKEEEPEEEEEEEEEEYDEEEEEEDDDRPPKKPRHGGFILDEADVDDEYEDEDQWEDGAEDILEKASNIDNVVLDEDRSGARRLQNLWRDQREEELGEYYMKKYAKSSVGETVYGGSDELSDDITQQQLLPGVKDPNLWTVKCKIGEERATAISLMRKFIAYQFTDTPLQIKSVVAPEHVKGYIYVEAYKQTHVKQAIEGVGNLRLGYWNQQMVPIKEMTDVLKVVKEVANLKPKSWVRLKRGIYKDDIAQVDYVEPSQNTISLKMIPRIDYDRIKARMSLKDWFAKRKKFKRPPQRLFDAEKIRSLGGDVASDGDFLIFEGNRYSRKGFLFKSFAMSAVITEGVKPTLSELEKFEDQPEGIDLEVVTESTGKEREHNFQPGDNVEVCEGELINLQGKVLSVDGNKITIMPKHEDLKDMLEFPAQELRKYFKMGDHVKVIAGRFEGDTGLIVRVEENFVILFSDLTMHELKVLPRDLAEISAFTSLCGADNQTQLHAYSDSTDLRVVLNMHGKVVTVRHQAVTQKKDNRFAVALDSDQNNIHVKDIVKVIDGPHSGREGEIRHLYRSFAFLHCKKLVENGGMFVCKARHLVLAGGSKPRDVTNLTVGGFTPMSPRISSPMHPSAEGQHGGFGSPGGMSRGRGRRDNELIGQTVRISQGPYKGYIGVVKDATESTARVELHSTCQTISVDRQRLTTVDSQRPGGMTSTYGRTPMYGSQTPMYGSGSRTPMYGSQTPLQDGSRTPHYGSQTPLHDGSRTPAQSGAWDPNNPNTPSRAEEEYEYAFDDEPTPSPQAYGGTPNPQTPGYPDPSSPQVNPQYNPQTPGTPAMYNTDQFSPYAAPSPQGSYQPSPSPQSYHQVAPSPAGYQNTHSPASYHPTPSPMAYQASPSPSPVGYSPMTPGAPSPGGYNPHTPGSGIEQNSSDWVTTDIQVKVRDTYLDTQIVGQTGVIRSVTGGMCSVYLKDSEKVVSISSEHLEPITPTKNNKVKVILGEDREATGVLLSIDGEDGIIRMDLEDQQIKILNLRFLGKLLEA
Protein: Ribonuclease 4 (RNase 4) (EC 3.1.27.-) (P34096)
Organism: Homo sapiens (Human)
Function: This RNase has marked specificity towards the 3' side of uridine nucleotides.
Subcellular location: Secreted {ECO:0000269|PubMed:33818125}. Note=Detected in urine. {ECO:0000269|PubMed:33818125}.
Interaction partners:
- Angiogenin
Sequence:
MALQRTHSLLLLLLLTLLGLGLVQPSYGQDGMYQRFLRQHVHPEETGGSDRYCNLMMQRRKMTLYHCKRFNTFIHEDIWNIRSICSTTNIQCKNGKMNCHEGVVKVTDCRDTGSSRAPNCRYRAIASTRRVVIACEGNPQVPVHFDG
Protein: DIMBOA UDP-glucosyltransferase BX8 (EC 2.4.1.202) (2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one 2-D-glucosyltransferase BX8) (Protein BENZOXAZINLESS 8) (Q8W2B7)
Organism: Zea mays (Maize)
Function: Glucosyltransferase involved in the last step of benzoxazinoid glucoside biosynthesis. Catalyzes the glucosylation of hydroxamic acids utilizing UDP-glucose as glucose doner, reducing the toxicity of these natural insecticides for storage. Can use DIMBOA and DIBOA as substrates, HMBOA (2-hydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one) and HBOA (2-hydroxy-2H-1,4-benzoxazin-3(4H)-one) with a lower efficiency, but not indole acetic acid or quercitin.
Interaction partners:
- DIBOA-glucoside dioxygenase BX6
- TRIBOA-glucoside O-methyltransferase BX7
- indole-2-monooxygenase
- Indole-3-glycerol phosphate lyase, chloroplastic
- Cytochrome P450 71C3
- O-methyltransferase ZRP4
- Benzoxazinone synthesis2
- Indolin-2-one monooxygenase
- 3-hydroxyindolin-2-one monooxygenase
Sequence:
MAASCGGRVVVFPFPFQGHFNPVMRLARALHARGVGITVFHTAGARAPDPADYPADYRFVPVPVEVAPELMASEDIAAIVTALNAACEAPFRDRLSALLSAADGEAGEAGGRVRCVLTDVSWDAVLSAARGLGVPALGVMTASAATFRVYMAYRTLVDKGYLPVREERKDDAVAELPPYRVKDLLRHETCDLEEFADLLGRVIAAARLSSGLIFHTFPFIEAGTLGEIRDDMSVPVYAVAPLNKLVPAATASLHGEVQADRGCLRWLDAQRARSVLYVSFGSMAAMDPHEFVELAWGLADAGRPFVWVVRPNLIRGFESGALPDGVEDRVRGRGVVVSWAPQEEVLAHPAVGGFFTHCGWNSTVEAVSEGVPMICHPRHGDQYGNARYVCHVWKVGTEVAGDQLERGEIKAAIDRLMGGSEEGEGIRKRMNELKIAADKGIDESAGSDLTNLVHLINSY
Protein: Nucleoprotein (O12369)
Organism: Orthohantavirus negraense
Subcellular location: Host Golgi apparatus, host cis-Golgi network {ECO:0000256|ARBA:ARBA00033737}. Host cytoplasm, host perinuclear region {ECO:0000256|ARBA:ARBA00004407}. Virion {ECO:0000256|ARBA:ARBA00004328}.
Interaction partners:
Sequence:
MSNLQEVQEGITLHEQQLVAARQKLKDAEKAVEVDPDDVNKSTLQSRRAAVSALENKLAELKRQLADLVAAQKLAAKPVDPTGLEPDDHLKEKSALRYGNVLDVNAIDLEEPSGQTADWKAIGAYILGFVIPIILKALYMLSTRGRQTVKENKGTRIRFKDDSSFEEVNGIRKPKHLYVSMPTAQSTMKADEITPGRFRTIACGLFPAQIKARNIISPVMGVIGFGHFVKDWMERIDNFLGEDCPFLPKARVQSEAFMSTNRAYFLNRQRQVDESRIQDIVDLIQAAEASSATLFNDIATPHSAWVFACAPDRCPPTALYVAGVPELGAFFAILQDMRNTIMASKSVGTAEEKLKKKSAFYQSYLRRTQSMGIQLDQKIIILYMLSWGKEAVNHFHLGDDMDPELRQLAQTLIDAKVKEISNQEPLKL
Protein: Scavenger receptor (Q58SM4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
TCDRDGRLRGEKPFCASRGCARPEDPENGHVENLSLRADVVCHDGYVLVGGRTAYCDGERWSTQLGSCRRSNHTRDHSCDFESEDQCGWEAETTFRRPWKRVSTVSDIHSLRTGPRHDHTFKNESGGHYMRMETQMGAYGSYHLLSPIYPRSLTLKTACCFRFHYFMFGAGVDNLVVSVKPVSMPMATMWNRFRANCSKFEISGQQGTQWLEHTISIDEMQEDFQVIFTATDARSQFGDIAIDDVKLMTGSECGTNGFSTTTEPTAPTGSNEQPLVYDMMSCSGRCGTSISASNITNNGIVMGCGCNDECLSDETCCLNYLEECTKELLTTTEDDISSLPPTVTSTSTSTTRKSTTTTTTSTTTTSTTTTKRPTTTTTTTKATTTKRTTTTKKPTTTSTTPKPTTTTSTTPKSTTSTTSTTSTTPTTTTTINVFTTKKTTIMIPTSSTEKTTGINTTMKTRKRITWNVDPQDIEGHMDTSGSTPNPALVVLYLLLAIVLVVVLANVVNRWIIPITGSKTSSEKAVRFKKAFDSLKKQRKRNSMDDQPLCDSDNDDVEYFEEMGVDIRHRTDL
Protein: V-type proton ATPase subunit D 1 (V-ATPase subunit D 1) (Vacuolar H+ ATPase subunit 36-1) (Vacuolar proton pump subunit D 1) (dV-ATPase D) (Q9V7D2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity).
Interaction partners:
- V-type proton ATPase subunit B
- V-type proton ATPase subunit C
- V-type proton ATPase subunit E
- V-type proton ATPase subunit F 1
- V-type proton ATPase subunit H
- V-type proton ATPase catalytic subunit A isoform 2
- V-type proton ATPase catalytic subunit A isoform 1
- V-type proton ATPase subunit d 1
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase subunit G
Sequence:
MSGKDRLPIFPSRGAQMLMKARLAGAQKGHGLLKKKADALQMRFRLILGKIIETKTLMGDVMKEAAFSLAEAKFTSGDINQVVLQNVTKAQIKIRTKKDNVAGVTLPVFESYQDGSDTYELAGLARGGQQLAKLKKNYQSAVKLLVELASLQTSFVTLDEVIKITNRRVNAIEHVIIPRIDRTLAYIISELDELEREEFYRLKKIQDKKREARIKADAKKAELLQQGIDVRQQANILDEGDDDVLF
Protein: Zinc finger Y-chromosomal protein 2 (P20662)
Organism: Mus musculus (Mouse)
Function: Probable transcriptional activator. Binds to the consensus sequence 5'-AGGCCY-3' (By similarity).
Subcellular location: Nucleus.
Interaction partners:
Sequence:
MDEDEIELTPEEEKSLFDGIGADAVHMDSDQISVEVQETVFLSNSDVTVHNFVPDDPDSVIIQDVIENVLIEDVHCSHILEETDISDNVIIPEQVLDLDTAEEVSLAQFLIPDILTSSITSTSLTMPEHVLMSEAIHVSNVGHFEQVIHDSLVEREIITDPLTADISDILVADWASEAVLDSSGMPLEQQDDARINCEDYLMMSLDEPSKTDHEGSSEVTMNAESETDSSKLDEASPEVIKVCILKADSEVDDVGETIQAVESETDNGNEAEVTDQRTSIHVPRVNIYMLASDSQKEEEDTKVIVGDEDAGGTAADTPEHEQQMDVSEIKAAFLPIAWTAAYDNNSDEIEVQNATASAMLHHDESGGLDRVPKQKSKKKKRPESKQYQSAIFVAPDGQTLRVYPCMFCGKKFKTKRFLKRHIKNHPEYLANKKYHCTECDYSTNKKISLHNHMESHKLTIKTEKTTECDDCRKNLSHAGTMHTEKGVNKTCKCKFCDYETAEQTLLNHHLLVVHRKKFPHICGECGKGFRHPSALKKHIRVHTGEKPYECQYCEYKSADSSNLKTHIKSKHSKEIPLKCGICLLTFSDTKEAQQHAVLHQESRTHQCSHCNHKSSNSSDLKRHIISVHTKAYPHKCDMCSKGFHRPSELKKHVATHKSKKMHQCRHCDFKSPDPFLLSHHILSAHTKNVPFKCKRCKKEFQQQCELQTHMKTHSSRKVYQCEYCEYSTKDASGFKRHVISIHTKDYPHRCDFCKKGFRRPSEKNQHIMRHHKEVGLA
Protein: Tyrosine-protein phosphatase non-receptor type 7 (EC 3.1.3.48) (Hematopoietic protein-tyrosine phosphatase) (HEPTP) (Q8BUM3)
Organism: Mus musculus (Mouse)
Function: May play a role in the regulation of T and B-lymphocyte development and signal transduction.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20157115}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20157115}. Note=Oxidized form is preferentially associated with actin cytoskeleton.
Interaction partners:
- Mitogen-activated protein kinase 1
- Dual specificity protein phosphatase 3
- Mitogen-activated protein kinase 14
- Mitogen-activated protein kinase 3
- Mitogen-activated protein kinase 11
- Mitogen-activated protein kinase 12
- Mitogen-activated protein kinase 13
- Stress-activated protein kinase JNK
- Receptor-type tyrosine-protein phosphatase R
- Tyrosine-protein phosphatase non-receptor type 5
Sequence:
MVQACEGRSRAQLPTLSLGADMTQPPPTKAPAKKHVRLQERRGSSVALMLDVQSLGTVEPICSVNTPREVTLHFLRTAGHPLTRWTLQHQPPSPKQLEEEFLKIPSNFVNPEDLDIPGHASKDRYKTILPNPQSRVCLGRAQSQEDSDYINANYIRGYDGKEKVYIATQGPMPNTVADFWEMVWQEDVSLIVMLTQLREGKEKCVHYWPTEEEAYGPFQIRIQDMKEHPEYTVRQLTIQHQQECRSVKHILFSAWPDHQTPESAGPLLRLVAEVETPETAANSGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLALYAAQLPPEPNP