wanglab/gogpt-training-data huggingface dataset:
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (M9PIK8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDDFGSTASDLEEATCPMQANATFSIDWRVTLLDHWLDLYLGYMNRLHMLLSLAGRLHLLSRHILGTLGQDPIFMGVLQGSLLMLFLFLMHLLRLWSCGYAVERPLNPTPDVAKELSCDFNFVSEQEKRAAQEAATEALLEVEEKKRRKRFTKKRNCVSAGPILIALRHQSKRPKHHRHAALPFEPVTPGEIILDTYLPPRELPLTIRLPQLAEPVKEEEVEYIELKSEPRGTLSTTDEIYPDSSDSSLYVSDEEQEDASQYCRGGYHPVVIGDIFDNRFRVVRKLGWGHFSTVWLCRDLKDEKYVALKVVKSAPHYIETAADEIRLLEAIRDADPMDVKRERIVRLMNHFTVRGVNGMHTCLVFEALGCSLYKLIVKNNYQGLAIAQVRNIIRQVLEGLDYLHSKCSIIHTDIKPENILLVIDNAAAMNQQIDDEINSLRVKGVDFPDSYISSIEKQTKSRAKWPLIEPNGSTNTNTNTSNSTATNSNSSTPLAAVIMSTLDKEDTTTTTSSTLNSNTTSSLASKYSSLLGDSECNGGLGGSANINNRYRTEKKITAKSSGDCDEDAESDTLGEQSTLASTMDSPTDLDPEPELDSKPNTVPEPSEGPIPEPTPNSTNSSCPSHNTATIAKSKINSNILSTCTSLTSTNEYCFTNTNTTTASTPSAPPSATPSSAPALASATPPSTCTPSFTQIAPSATAPATSTTCTTSAEFYDGDHKTTSTSTTTTSNAISSATTTTATTTTAIAKLNVHANAIPSQNQSQSSQNNTYTIQSLIDNSNVRVKIADLGNACYDYHHFTEDIQTRQYRSIEVLLGAPYNYTADIWSTACLAFELATGDYLFDPHAGESYSRDEDHLAHIVELLGSIPQSVIFRGKHGLKYFTSYGSLRNITKLKPWSLMNVLVEKYDWDPVEAKKFSDFLLPMLEYNPVIRASAAECLQHPWLEQEEFV
Protein: tRNA-uridine aminocarboxypropyltransferase 2 (EC 2.5.1.25) (DTW domain-containing protein 2) (Q9VI85)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the formation of 3-(3-amino-3-carboxypropyl)uridine (acp3U) at position 20a in the D-loop of several cytoplasmic tRNAs (acp3U(20a)).
Interaction partners:
- tRNA
Sequence:
MEDDAWLDLVGISADPPNRRNKCEKCKRPVVVCWCPALPHPPEAVSSQIVILQHPAEEKRSLRTALMLQLGLEPGKCVVYKGKRFPNHRNHADLQRILDSPQTLLLYPSRDSVPLEEVDHSAGPYTLVLIDGTWPQAKAIYASSPALHRLRQVKLIAVGISDYIIRTQPTEGCLSTLETAAQCLAVLESRPELRQTLVRPLHTLCKYQLDNGAVEHQSKEFLLKNNQYPKPIGKRLSRLLRNTACDGNEET
Protein: Prostate stem cell antigen (P57096)
Organism: Mus musculus (Mouse)
Function: May be involved in the regulation of cell proliferation.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O43653}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:O43653}.
Interaction partners:
- Glutamate carboxypeptidase 2
- Mesothelin
- STEAP1 protein
Sequence:
MKTVFFLLLATYLALHPGAALQCYSCTAQMNNRDCLNVQNCSLDQHSCFTSRIRAIGLVTVISKGCSSQCEDDSENYYLGKKNITCCYSDLCNVNGAHTLKPPTTLGLLTVLCSLLLWGSSRL
Protein: Zinc finger protein 534 (KRAB domain only protein 3) (Q76KX8)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MALTQGQLSFSDVAIEFSQEEWKCLDPGQKALYRDVMLENYRNLVSLGEDNVRPEACICSGICLPDLSVTSMLEQKRDPWTLQSEVKIINNPDGRECIKGVNTEKSSKLGSSAGNKSLKNQHGLTLQLHLTEWQPFQAVRNIYGCKHVEKSISDNSSVSPVQISFFSVKTHIFNNYRNDFLFSTLLPQEQKVHIREKPYGCNEHGKVFRVSSSLTNRQVIHIADKTYKCSDCGEIFSSNSNFAQHQRIHTGEKPYKYNECGKVFNQNSHLAQHQKIHTGQKPYNNKECGKVFSHHAYLAQHRKIHTGEKPYKCSECGKAFSVCSSLTAHLVIHTGEKPYDCKECGKVFRHKSSLTTHQTVHTGERPYKCNECGKGFSRIAFLARHRKVHTGEKPYKCNECGKVFIGNSRLARHRKIHTGGRRYKCNECGKAFRTCSDLTAHLLIHTGEKPYECIDCGKVFRHKSSLTYHCRIHTGEKPYKCNECGKVFSQNSNLQRHRKIHTGEKLYKCNECGKVFRQNSHLAQHRDIHTGEKPYSCNECGKVFRRNSHLVRHRNVHTGEKPYSCNECGKVFSRNSHLARHRNIHTGEKPHSCNECGKVFSRNSHLARHRKIHTGEKLYKCNECSKVFSRNSRLAQHRNIHTGVKPYSCNECGKVFSKNSILVQHCSIHTREKP
Protein: Transcriptional regulator (Q7MFA2)
Organism: Vibrio vulnificus (strain YJ016)
Interaction partners:
Sequence:
MPKRSKEDTEITIQKIMDAVVDQLLRLGYDKMSYTTLSQQTGVSRTGISHHFPKKTDFTAALDGRIFKLFVEHLEFNKGLNEFSQSWVVALEDEEFRAILRLLFHHIVTAERAHEFAANGIDRLYKMTESQFGEESKKELEWLFGKSLVRISQ
Protein: Testin (TES1/TES2) (P47226)
Organism: Mus musculus (Mouse)
Function: Scaffold protein that may play a role in cell adhesion, cell spreading and in the reorganization of the actin cytoskeleton. Plays a role in the regulation of cell proliferation. May act as a tumor suppressor (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21278383}. Cell junction, focal adhesion {ECO:0000250}. Note=Detected along actin stress fibers (By similarity). Detected at the subacrosomal layer in round spermatids. {ECO:0000250}.
Interaction partners:
Sequence:
MSATHPTRLGTRTKESNACASQGLVRKPPWANEGEGFELHFWRKICRNCNVVKKSMTVLLSNEEDRKVGRLFEDTKYTTLIAKLKSDGIPMYKRNVMILTNPVAAKKNVSINTVTYEWAPPVQNQALARQYMQMLPKEKQPVAGSEGAQYRKKQLAKQLPAHDQDPSKCHELSPKEVKEMEQFVKKYKSEALGVGDVKFPSEMNAQGDKVHNCGNRHAPAAVASKDKSAESKKTQYSCYCCKHTTNEGEPAIYAERAGYDKLWHPACFICSTCGELLVDMIYFWKNGKLYCGRHYCDSEKPRCAGCDELIFSNEYTQAENQNWHLKHFCCFDCDHILAGKIYVMVTDKPVCKPCYVKNHAVVCQGCHNAIDPEVQRVTYNNFSWHASTECFLCSCCSKCLIGQKFMPVEGMVFCSVECKRMMS
Protein: C-type natriuretic peptide [Cleaved into: CNP-22; CNP-29; CNP-53] (Q61839)
Organism: Mus musculus (Mouse)
Function: Hormone which plays a role in endochondral ossification through regulation of cartilaginous growth plate chondrocytes proliferation and differentiation. May also be vasoactive and natriuretic (By similarity). Acts by specifically binding and stimulating NPR2 to produce cGMP. Binds the clearance receptor NPR3 (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Atrial natriuretic peptide receptor 2
- Atrial natriuretic peptide receptor 3
- Natriuretic peptides A
- Atrial natriuretic peptide receptor 1
- Natriuretic peptides B
Sequence:
MHLSQLIACALLLALLSLRPSEAKPGTPPKVPRTPPGEELADSQAAGGNQKKGDKTPGSGGANLKGDRSRLLRDLRVDTKSRAAWARLLHEHPNARKYKGGNKKGLSKGCFGLKLDRIGSMSGLGC
Protein: Vomeronasal 2, receptor 82 (A0A3B2WDB0)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MLLSWLLIVWFLQMPTFTWIIATHICPTDTKHLIHSDGTVVIGAFFPILHNSRVSKIIDWRYFPMDSDDYFGINARNYQLVLAMLFAVNEINLNSHILPNTSLGLEIYNLPAIGRNIFRTVFSWLTGLSSVIPNYTCRKESKSAATLTGLSWKTSETIWTILDLYKFPQLHPFLKKIQVKNSVGDDVVLDWKRKADPEYDITNIWNFPTGLSLLVKVGTFVPSAPKGKQLSMSEYMINWPIGFTEIPHSVCSESCNPGFRKVALESKPTCCFDCTPCPDNEISNETGEGQVSQRIFHSFYSALTKLSKGKK
Protein: Glutathione S transferase D10, isoform A (EC 2.5.1.18) (Glutathione S transferase D10, isoform B) (IP02193p) (IP02196p) (Q9VGA1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Glutathione S-transferase D2
- Glutathione S-transferase D7
- Glutathione S-transferase D1
- Glutathione S transferase D8
- Glutathione S-transferase D4
- Glutathione S transferase D9, isoform A
- Bifunctional glutamate/proline--tRNA ligase
- Probable maleylacetoacetate isomerase 2
- Glutathione S-transferase D5
- FI01423p
Sequence:
MDLYYRPGSAPCRSVLMTAKALGVEFDKKTIINTRAREQFTPEYLKINPQHTIPTLHDHGFALWESRAIMVYLVEKYGKDDKLFPKDVQKQALINQRLYFDMGTLYKSFSEYYYPQIFLKKPANEENYKKIEVAFEFLNTFLEGQTYSAGGDYSLADIAFLATVSTFDVAGFDFKRYANVARWYENAKKLTPGWEENWAGCQEFRKYFDN
Protein: Lrg1p (A0A1D8PRQ6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- GTP-binding protein RHO1
- Rho family GTPase
- Cell division control protein 42 homolog
- GTP-binding protein RHO3
- Rho family GTPase
- Rho family GTPase
- Rho family guanine nucleotide exchange factor
- Rga2p
- Protein kinase C-like 1
- Rho family guanine nucleotide exchange factor
Sequence:
MKHSFDTPQRGNSIHHSFGNPNASNTTRSTINIVESPDNRGSIIATTEPSSPPPPQQPLKDSGSSPRRKFNPFGHSRSHSHTSNNGKRLFYPVHHDGRYHNMNDQYPPISTVSQSMHPSSPVPSSPTPTPAPAPTTTSSSKPKREQSLRYYIPRDTPPQTPPMSQLPKPVGKSPQPNWTNLIPPLPGKPQPSYNSPDSFQQQKQNKLIDTDDFNFGTEPIISSPESSSRQHPDPLSNQSNFNNNTINNYSNYRSSTRSGLDPSQRHSIAVSPTPEKQDSATQSTDTINTSSIRPVPSVYVAGSSSSLPHKQQQQQEPSSPSKSERKPGRKKSRKVCAKCGLEITSQFVRALNNAYHVDCFTCHECGKQCSAKFFPYEITNEQDGTKTQVALCEYDYFKKLDLICYVCNSALRGPYITALGNKYHLEHFRCNVCQRVFESDESYYEHDNNIYCHFHYSKLYASHCEGCQSSIVKQFVELFRGGRNQHWHPECYMVHKFWNVCITPDSVGLQKLFDLPDDVLNGLKLVKDDNESHISVDSAMLMSIEQQIEQVVLKCWVTLSGYEEITAKCISDMLLCACTGNKFNGIVVTGKLVLNVEVLFNALDYVILMCKSSHELLHKKFGTPPNKDDSESSSTEEEYFQMLKKEPRNITGKIMSYLAILRKSDHIAKSGSLSAELLSVITGCAHYLKLLIRLGLYNALKLNRLYGTTNAIEKFLQLTSEHEAISLLAGDSKTQLSLINSKLTIPASSTDACSSCAKSIEKSCLKLDNNRWHVRCFVCSLCKRTIPSIEASETKFDVIHQSIVCRECPCEHFDTGFHLVSDLSQLIYLLKIALFRSRSVMKVDLTKVPRSYLSDSQSDTDTVDVAQDNYSQTLNDVTSLRSKRQSQKLSKSIKKKARKSIIVEAPEADKARKEDIKTHPLGMKSSGVGTNDTSRSSGINDETTIADELNDLSFDSQTSKQQGSRKTSSASQLSYNPGGDENLSVTRKSLKIRDEPQRQTTNTHLDRTSDLLKNEKSLTLDDIPRIVAAEQAREQRPNAFKHHNSLYQRQTAPHRLKATGHTSTVITPTGVLDNILNTSQPHPEEPVAVRKQKYYSELTKDEHFIIRHIAVEALSHISKSYSNKEELLSLIQTKKQPTFWDKFKFGGGDGKKDKVMAVFGVDLQVLTKKYGIDSDLGVGPSKLRIPIVVDDIIAALRQKDMSVEGIFRLNGNIKKLRELTEQINKNPLKSPDFSIQNAVQLAALMKKWLRELPNPLLTFGLYDMWVSSQRQVNPVLRKRVLQLTYCMLPRSHRNLVEVLLYFFSWVASFSEIDEETGSKMDIHNLATVIAPNILISKQSSNSSSGNSSNSGTNNSDSQQASGDNYFLAIEVVNQLIEQHEEFSIIPSDILEFYEKCGFDKFDSTKKEITTRDVMIKIDKELKEKPDYFDNFELKNPTGSLTSQEVKRNSVSRIESKIQNRELNGISER
Protein: Matrix metalloproteinase-17 (MMP-17) (EC 3.4.24.-) (Membrane-type matrix metalloproteinase 4) (MT-MMP 4) (MTMMP4) (Membrane-type-4 matrix metalloproteinase) (MT4-MMP) (MT4MMP) (Q9R0S3)
Organism: Mus musculus (Mouse)
Function: Endopeptidase that degrades various components of the extracellular matrix, such as fibrin. May be involved in the activation of membrane-bound precursors of growth factors or inflammatory mediators, such as tumor necrosis factor-alpha. May also be involved in tumoral process. Not obvious if able to proteolytically activate progelatinase A. Does not hydrolyze collagen types I, II, III, IV and V, gelatin, fibronectin, laminin, decorin nor alpha1-antitrypsin.
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side. Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Proheparin-binding EGF-like growth factor
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Metalloproteinase inhibitor 2
- Metalloproteinase inhibitor 1
Sequence:
MGRRPRGPGSPRGPGPPRPGPGLPPLLLVLALAAHGGCAAPAPRAEDLSLGVEWLSRFGYLPPADPASGQLQTQEELSKAITAMQQFGGLETTGILDEATLALMKTPRCSLPDLPPGAQSRRKRQTPPPTKWSKRNLSWRVRTFPRDSPLGRDTVRALMYYALKVWSDITPLNFHEVAGNAADIQIDFSKADHNDGYPFDGPGGTVAHAFFPGDHHTAGDTHFDDDEPWTFRSSDAHGMDLFAVAVHEFGHAIGLSHVAAPSSIMQPYYQGPVGDPLRYGLPYEDRVRVWQLYGVRESVSPTAQLDTPEPEEPPLLPEPPNNRSSTPPQKDVPHRCTAHFDAVAQIRGEAFFFKGKYFWRLTRDRHLVSLQPAQMHRFWRGLPLHLDSVDAVYERTSDHKIVFFKGDRYWVFKDNNVEEGYPRPVSDFSLPPGGIDAVFSWAHNDRTYFFKDQLYWRYDDHTRRMDPGYPAQGPLWRGVPSMLDDAMRWSDGASYFFRGQEYWKVLDGELEAAPGYPQSTARDWLVCGEPLADAEDVGPGPQGRSGAQDGLAVCSCTSDAHRLALPSLLLLTPLLWGL
Protein: Cytoplasmic linker associated protein 1 (A0A0G2JTD7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Chromosome, centromere, kinetochore {ECO:0000256|ARBA:ARBA00004629}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}. Golgi apparatus, trans-Golgi network {ECO:0000256|ARBA:ARBA00004601}.
Interaction partners:
Sequence:
MEPRMESCLAQVLQKDVGKRLQVGQELIDYFSDKQKSADLEHDQTMLDKLVDGLATSWVNSSNYKVVLLGMDILSALVTRLQDRFKAQIGTVLPSLIDRLGDAKDSVREQDQTLLLKIMDQAANPQYVWDRMLGGFKHKNFRTREGICLCLIATLNASGAQTLTLSKIVPHICNLLGDPNSQVRDAAINSLVEIYRHVGERVRADLSKKGLPQSRLNVIFTKFDEVQKSGNMIQSANDKNFDDEDSVDGNRPSSASSSSSKAPSSSRRNVSMGTTRRLMASSLGSKSSAAKEGAGAVDEEDFIKAFDDVPVVQIYSSRDLEESINKIREILSDDKHDWEQRVNAVSLKKIRSLLLAGAAEYDNFFQHLRLLDGAFKLSAKDLRSQVVREACITLGSERRNCGPRAVFACASMHHTHIPRLIPVITSNCTSKSVAVRRRCFEFLDLLLQEWQTHSLERHISVLAETIKKGIHDADSEARIEARKCYWGFHSHFSREAEHLYHTLESSYQKALQSHLKNSDSIVSLPQSDRSSSSSQESLNRPLSAKRSPTGSTASRGSTVSTKSMSTTGSLQRSRSDIDVNAAASAKSKVSSSSGSTAFSSAAALPPGSYASLGRIRTRRQSSGSTTNVASTSSDSRGRSRAKVVSQSQPGSRSSSPGKLLGSGYGGLAGGSSRGPPVTPSSEKRSKIPRSQGCSRETSPNRIGLDRFGLGQSGRIPGSVSAMRVLSTSTDLEAAVADALLLGDARSKKKPVRRRYEPYGMYSDDDANSDASSVCSERSYGSRNGGIPHYLRQTEDVAEVLNHCASSNWSERKEGLLGLQNLLKSQRTLSRVELKRLCEIFTRMFADPHSKVFSMFLETLVDFIIIHKDDLQDWLFVLLTQLLKKMGADLLGSVQAKVQKALDVTRDSFPFDQQFNILMRFIVDQTQTPNLKVKVAILKYIESLARQMDPTDFVNSSETRLAVSRIITWTTEPKSSDVRKAAQIVLISLFELNTPEFTMLLGALPKTFQDGATKLLHNHLKNSSNAGVGSPSNTIGRTPSRHPSSRTSPLTSPTNCSHGGLSPSMLDYDTENLNSEEIYSSLRGVTEAIEKFSFRSQEDLNEPIKRDGKKDCDIVSRDGGAASPATEGRGGSEVEGGRMALDNKTSLLNTQPPRAFPGPRAREYNPYPYSDTINTYDKTALKEAVFDDDMEQLRDVPIDHSDLVADLLKELSNHNERVEERKGALLELLKITREDSLGVWEEHFKTILLLLLETLGDKDHSIRALALRVLREILRNQPARFKNYAELTIMKTLEAHKDSHKEVVRAAEEAASTLASSIHPEQCIKVLCPIIQTADYPINLAAIKMQTKVVERITKESLLQLLVDIIPGLLQGYDNTESSVRKASVFCLVAIYSVIGEDLKPHLAQLTGSKVCIVLPAVACT
Protein: Transmembrane protein 71 (Q6P5X7)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MYRISQLMSTPVASSSRLEREYAGELSPTCIFPSFTCDSLDGYHSFECGSIDPLTGSHYTCRRSPRLLTNGYYIWTEDSFLCDKDGNITLNPSQTSVMYKENLVRIFRKKKRICHSFSSLFNLSTSKSWLHGSIFGDINSSPSEDNWLKGTRRLDTDHCNGNADDLDCSSLTDDWESGKMNAESVITSSSSHIISQPPGGNSHSLSLQSQLTASERFQENSSDHSETRLLQEVFFQAILLAVCLIISACARWFMGEILASVFTCSLMITVAYVKSLFLSLASYFKTTACARFVKI
Protein: Cytoplasmic envelopment protein 2 (Tegument protein BGLF2) (P0CK53)
Organism: Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Function: Plays a critical role in cytoplasmic virus egress. Participates in the final step of tegumentation and envelope acquisition within the host cytoplasm by directly interacting with the capsid. Upon virion binding to target cell, a signaling cascade is triggered to disrupt the interaction with the capsid, thereby preparing capsid uncoating. Activates the AP-1 pathway and enhances EBV reactivation and virus release. Inhibits type I IFN-induced TYK2, STAT1 and STAT3 phosphorylation, thereby impairing type I IFN signaling and counteracting the ability of type I IFN to suppress the reactivation of EBV. Recruits SHP1 phosphatase to dephosphorylate STAT1. Mediates STAT2 ubiquitination and proteasomal degradation. Also suppresses type II and type III IFN signaling. Contributes to G1/S arrest in the host cell. Acts as an miRNA regulator that interferes with the function of RISC in miRNA-mediated mRNA silencing. As a result, SUMOylation is increased. When encapsulated in the exosomes released by EBV-infected host cells, may facilitate the infection in recipient cells (By similarity).
Subcellular location: Virion tegument {ECO:0000255|HAMAP-Rule:MF_04039, ECO:0000269|PubMed:15534216}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04039, ECO:0000269|PubMed:28904200, ECO:0000269|PubMed:32038519}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04039, ECO:0000269|PubMed:28904200, ECO:0000269|PubMed:32038519}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04039, ECO:0000269|PubMed:32038519}. Note=Localizes in the host nucleus up to 18 hours postinfection, but at later times localizes to punctate, cytoplasmic structures. Associates with the capsid before the final envelopment. Recruited to the TGN via the interaction with BBLF1 (PubMed:32038519). Also found in the exosomes released by the host cell (PubMed:35729616). {ECO:0000255|HAMAP-Rule:MF_04039, ECO:0000269|PubMed:32038519, ECO:0000269|PubMed:35729616}.
Interaction partners:
Sequence:
MASAANSSREQLRKFLNKECLWVLSDASTPQMKVYTATTAVSAVYVPQIAGPPKTYMNVTLIVLKPKKKPTYVTVYINGTLATVARPEVLFTKAVQGPHSLTLMYFGVFSDAVGEAVPVEIRGNPVVTCTDLTTAHVFTTSTAVKTVEELQDITPSEIIPLGRGGAWYAEGALYMFFVNMDMLMCCPNMPTFPSLTHFINLLTRCDNGECVTCYGAGAHVNILRGWTEDDSPGTSGTCPCLLPCTALNNDYVPITGHRALLGLMFKPEDAPFVVGLRFNPPKMHPDMSRVLQGVLANGKEVPCTAQPWTLLRFSDLYSRAMLYNCQVLKRQVLHSY
Protein: Acetyl-coenzyme A synthetase, cytoplasmic (EC 6.2.1.1) (Acetate--CoA ligase) (Acetyl-CoA synthetase) (ACS) (AceCS) (Acetyl-CoA synthetase 1) (AceCS1) (Acyl-CoA synthetase short-chain family member 2) (Acyl-activating enzyme) (Propionate--CoA ligase) (EC 6.2.1.17) (Q9QXG4)
Organism: Mus musculus (Mouse)
Function: Catalyzes the synthesis of acetyl-CoA from short-chain fatty acids. Acetate is the preferred substrate but can also utilize propionate with a much lower affinity.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:11150295, ECO:0000269|PubMed:28552616}. Cytoplasm {ECO:0000269|PubMed:28562591}. Nucleus {ECO:0000269|PubMed:28552616, ECO:0000269|PubMed:28562591}. Note=Glucose deprivation results in its AMPK-dependent phosphorylation and subsequent nuclear translocation. Phosphorylation at Ser-659, leads to exposure of its nuclear localization signal which is required for its interaction with KPNA1 and subsequent translocation to the nucleus (By similarity). Found in the cytoplasm in undifferentiated neurons and upon differentiation, translocates to nucleus (PubMed:28562591). {ECO:0000250|UniProtKB:Q9NR19, ECO:0000269|PubMed:28562591}.
Interaction partners:
- Acetyl-CoA carboxylase 1
- Citrate synthase, mitochondrial
- Citrate synthase
- Acetyl-CoA carboxylase 2
- Acetyl-coenzyme A thioesterase
- Acetyl-CoA acetyltransferase, cytosolic
- Peroxisomal acyl-coenzyme A oxidase 1
- Acetyl-CoA acetyltransferase, mitochondrial
- Peroxisomal acyl-coenzyme A oxidase 3
- Aldehyde dehydrogenase, mitochondrial
Sequence:
MGLPEERRKSGSGSRAREETGAEGRVRGWSPPPEVRRSAHVPSLQRYRELHRRSVEEPREFWGNIAKEFYWKTACPGPFLQYNFDVTKGKIFTEWMKGATTNICYNVLDRNVHEKKLGDKVAFYWEGNEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCLLITTDAFYRGEKLVNLKELADESLEKCREKGFPVRCCIVVKHLGRAELGMNDSPSQSPPVKRPCPDVQICWNEGVDLWWHELMQQAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQNDHDLGDTSTVADPSVINHLFSHRCLTTQ
Protein: Germacrene A synthase long form (CiGASlo) (EC 4.2.3.23) (Q8LSC3)
Organism: Cichorium intybus (Chicory)
Function: Involved in sesquiterpene lactone biosynthesis. Produces exclusively (+)-germacrene A.
Interaction partners:
Sequence:
MALVRNNSSNGREPVLSPRSLTSPRGLTSPRPLSVQPTPEPVRPLANFPPSIWADRFISFSLDNSQLEAYANALEEPKEAVKSLITDTTIDANTKLKLIYSVHRLGLSYLYPDEIDAELNKLFEKIDLQYYEQVDLYTIAVQFQVFRHHGYKISSDVFKKFKDSTTGTFTDDVTKDVKGMLSLYESAHLRLHGEDILDEALAFTEAHLKKILTTLEGDLARQVNQVLKRPFHTGMPMVEARLYFITHEEDFSSHESVVKLAKVHFNYLQLQQKEELRLVSQWWKDMQFQQSVPYIRDRVPEIYLWILGLYFEPYYSRARIIATKITLFLVVLDDTYDAYATIDEIRSITDAINRWEISAIDQLPEYIKPFYRILLNEYDDLEKEYSKDGRAFSVHASKQAFQEIARGYLEEAEWLHNGYVATFPEYMKNGLITSAYNVISKSALVGMGAIADEEALAWYETHPKILKASELISRLQDDVMTFQFERKRGQSATGVDAYIKEYNVSEEVAIKELMKMIENAWKDINEGCLKPTEVSVALLTPILNLARMIDVVYKFDDGFTFPGKTLKDYITLLFVSPPPSLEN
Protein: Nuclear transcription factor Y subunit (Q9VSY9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU367155}.
Interaction partners:
- Nuclear transcription factor Y subunit gamma
- Nuclear factor Y-box B, isoform A
- Chromatin accessibility complex 16kD protein
- Grain, isoform C
Sequence:
MENHFSATSRPSATPRMCTTASAVGAAASAAAAAGNNNNNSNSSSNNNATTGNNLSVSTAAGGATNAAATAQPIQVIPMPMLPTGAAQIIIGQQPQGQATATGLQPQLIPLQANQIMLQAAQQQPQMQVMQLPDGQTIFYQTPTIAALDPNAAANAAAAMAAQPTPHYLNINGQLVQINPAPSANQAAPTAGQQIIMVPQTAMAAVNAAAANAGVGAGVGTVVTQQQQQQHQQVQSQTQNQQQQQQQQTVAAVAASAAVNNISADVSTSTTGTNTNSEDESSKGEADEEPLYVNAKQYKRILIRRQARAKLESRIPKERCKYLHESRHRHAMNRARGEGGRFHSAQEKGDQDSSGPEGGSMPMASSGGVTLSRGTARAPPKLIAPHQTPSITITAIKSE
Protein: KIN17-like protein KLP (F4KDD7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May act as repressor of root growth during copper excess and of hypocotyl growth in the dark.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24713636}. Nucleus {ECO:0000269|PubMed:24713636}.
Interaction partners:
- Nuclear protein-like
- At2g32600/T26B15.16
- Splicing factor SF3a60 homolog
- Protein KOKOPELLI
- Serine/threonine-protein phosphatase PP2A-2 catalytic subunit
- Pre-mRNA-splicing factor 38
- At1g31870
- S-adenosyl-L-methionine-dependent methyltransferases superfamily protein
- Zinc finger CCCH domain-containing protein 42
- Transmembrane protein
Sequence:
MFVMSSSSIPNGIFIIDGQERYVNPEGDVESNKSERTSKASMVFQMCEKQCRDENGFKCHCMSESHQRQMQVLGQNPTRVVNGYSQEFEQTFLDLMRRSHRFSRVAATVVYNEYINDRLHVHMNSTKWATLTEFIKYLGKTAEEEKQEREIQKQIERASAGCEGKDVVVDDDDNDDDEKKKDEDFRLKKVGFALGLGVKERGESSKLVFGDEENDKVERGDKRKRSALDELMKEEEKKKERMNRKDYWLFEGIIVKGVVKRVIDKYVGEIEMLESKHVLRVDQVELKTVLPQIGGMVKIVNGAYRGSNTRLLDLDTEKFCAKVQIEKGVYDGRVIKSIEYEDICKLA
Protein: Putative protein-lysine deacylase ABHD14B (Alpha/beta hydrolase domain-containing protein 14B) (F8W9U3)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAASVEQREGTIQVQGQALFFREALPGSGQARFSVLLLHGIRFSSETWQNLGTLHRLAQAGYRAVAIDLPGLKGEPPAQEPLLSQSRASFLAAVVDALELGPPVVISPSLSGMYSLPFLTAPGSQLPGFVPVAPICTDKINAANYASVKTPALIVYGDQDPMGQTSFEHLKQLPNHRVLIMKGAGHPCYLDKPEEWHTGLLDFLQGLQ
Protein: DISC1 scaffold protein (Disrupted in schizophrenia 1 isoform 24) (C4P0B1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPGGGPQGAPAAAGGGGVSHRAGSRDCLPPAACFRRRRLARRPGYMRSSTGPGIGFLSPAVGTLFRFPGGVSGEESHHSESRARQCGLDSRGLLVRSPVSKSAAAPTVTSVRGTSAHFGIQLRGGTRLPDRLSWPCGPGSAGWQQEFAAMDSSETLDASWEAACSDGARRVRAAGSLPSAELSSNSCSPGCGPEVPPTPPGSHSAFTSSFSFIRLSLGSAGERGEAEGCPPSREAESHCQSPQEMGAKAASLDGPHEDPRCLSRPFSLLATRVSADLAQAARNSSRPERDMHSLPDMDPGSSSSLDPSLAGCGGDGSSGSGDAHSWDTLLRKWEPVLRDCLLRNRRQMEVISLRLKLQKLQEDAVENDDYDKAETLQQRLEDLEQEKISLHFQLPSRQPALSSFLGHLAAQVQAALRRGATQQASGDDTHTPLRMEPRLLEPTAQDSLHVSITRRDWLLQEKQQLQKEIEALQARMFVLEAKDQQLRREIEEQEQQLQWQGCDLTPLVGQLSLGQLQEVSKALQDTLASAGQIPFHAEPPETIRSLQERIKSLNLSLKEITTKVCMSEKFCSTLRKKVNDIETQLPALLEAKMHAISGGHGTLWHILPDVSGGIVGAHPTFY
Protein: Non-structural protein NP-1 (NP1) (B9UYK6)
Organism: Human bocavirus 2 (HBoV2) (Human bocavirus type 2)
Function: Required for the expression of the capsid proteins. Performs the splicing and internal polyadenylation of the viral capsid-encoding mRNA precursor, which allows its maturation and expression. Transactivates the viral promoter.
Subcellular location: Host nucleus {ECO:0000250|UniProtKB:Q3YPH5}.
Interaction partners:
Sequence:
MSSESMKNKHRNSKRTPSPLQKERRRNWESHKSRSRSPIRRHGEKNLEYAHHSNQENRQSSYTALKTSDQATKTKEKTSGGNRTNPYTVFSQHRANHSDAPGWCGFYWHSTRLARDGTNCIFNEMKQEFQELQINGKITWDNARELLFSQKKKLDQKYRNMLYHFRHSPDCPRCDYWDNVYRRHLAHVSSQESEEVTDEEMLSAVESMDTNASN
Protein: Adenylate isopentenyltransferase 1, chloroplastic (AtIPT1) (EC 2.5.1.112) (EC 2.5.1.27) (Adenylate dimethylallyltransferase 1) (Cytokinin synthase 1) (Q94ID3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in cytokinin biosynthesis. Catalyzes the transfer of an isopentenyl group from dimethylallyl diphosphate (DMAPP) to ATP, ADP and AMP. Adenine, adenosine, isopentenylpyrophosphate and 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBDP) are not used as substrates.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:14726522}.
Interaction partners:
- Cytokinin hydroxylase
- Cytokinin hydroxylase
- Cytokinin dehydrogenase 1
- Isopentenyl-diphosphate Delta-isomerase II, chloroplastic
- Isopentenyl-diphosphate Delta-isomerase I, chloroplastic
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase, chloroplastic
- Cytokinin dehydrogenase 3
- Histidine kinase 2
- Histidine kinase 3
- Cytokinin dehydrogenase 7
Sequence:
MTELNFHLLPIISDRFTTTTTTSPSFSSHSSSSSSLLSFTKRRRKHQPLVSSIRMEQSRSRNRKDKVVVILGATGAGKSRLSVDLATRFPSEIINSDKIQVYEGLEITTNQITLQDRRGVPHHLLGVINPEHGELTAGEFRSAASNVVKEITSRQKVPIIAGGSNSFVHALLAQRFDPKFDPFSSGSCLISSDLRYECCFIWVDVSETVLYEYLLRRVDEMMDSGMFEELSRFYDPVKSGLETRFGIRKAIGVPEFDGYFKEYPPEKKMIKWDALRKAAYDKAVDDIKRNTWTLAKRQVKKIEMLKDAGWEIERVDATASFKAVMMKSSSEKKWRENWEEQVLEPSVKIVKRHLVQN
Protein: Phenolic glucoside malonyltransferase 1 (EC 2.3.1.-) (EC 2.3.1.116) (Q940Z5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Malonyltransferase acting on xenobiotic glucosides. Has activity toward 2-Naphthol glucoside (2NAG), 1-Naphthol glucoside (1NAG), kaempferol 7-O-glucoside, kaempferol 3-O-glucoside, hydroxycoumarin glucosides, phenol-glucosides and isoflavone glucoside (daidzin), but not toward 4-coumaroyl glucoside, kaempferol 3,7-O-diglucoside, salicylic acid glucoside and phlorizin. In vivo, seems to be involved in the malonylation of 2-Naphthol glucoside while PMAT2 would be involved in the malonylation of 4-methylumbelliferone glucoside or 4-nitrophenyl glucoside.
Interaction partners:
- UDP-glycosyltransferase 73C6
Sequence:
MVNEEMESSLKVIDVARVTPSNSDSSESLTLPLTFFDLLWYKLHAVERVIFYKLTDASRPFFDSVIVPNLKTSLSSSLSHYLPLAGKLVWEPLDPKPKIVYTPNDAVSFTVAESNADFSRLTGKEPFPTTELYPLVPELHVSDDSASAVSFQVTLFPNQGFCISVNAHHAVLDGKTTTNFLKSWARTCKNQDSFLPQDLIPVYDRTVIKDPMDLDTKILNAWHRVAKVFTGGKEPENPKSLKLLWSPEIGPDVFRYTLNLTREDIQKLRERLKKESSSSSVSSSPKELRLSTFVIVYSYALTCLIKARGGDPSRPVGYGFAVDCRSLMVPPVPSSYFGNCVSACFKMSLTAETFMSEEGFLAAARMVSDSVEALDENVALKIPEILEGFTTLSPGTQVLSVAGSTRFGVYGLDFGWGRPEKVVVVSIDQGEAISFAESRDGSGGVELGFSLKKHEMDVLVDLLHKGLEN