wanglab/gogpt-training-data huggingface dataset:
Protein: Histone acetyltransferase ESA1 (EC 2.3.1.48) (Protein 2-hydroxyisobutyryltransferase ESA1) (EC 2.3.1.-) (Protein acetyltransferase ESA1) (EC 2.3.1.-) (Protein crotonyltransferase ESA1) (EC 2.3.1.-) (Q08649)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalytic component of the NuA4 histone acetyltransferase (HAT), a multiprotein complex involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A variant H2A.Z. Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, histone H2B to form H2BK16ac, histone H2A to form H2AK4ac and H2AK7ac, and histone variant H2A.Z to form H2A.ZK14ac. Acetylation of histones gives a specific tag for epigenetic transcription initiation and elongation. Acetylation of histone H4 is essential for DNA double-strand break repair through homologous recombination. Involved in cell cycle progression. Recruitment to promoters depends on H3K4me. Also acetylates non-histone proteins, such as ATG3 and PAH1. Regulates autophagy by acetylating ATG3, controlling interaction the interaction between ATG3 and ATG8 and ATG8 lipidation. Acts as a regulator of fatty-acid-induced triacylglycerol synthesis by catalyzing acetylation of PAH1, thereby promoting the synthesis of diacylglycerol. In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA) or (2E)-butenoyl-CoA (crotonyl-CoA), and is able to mediate protein 2-hydroxyisobutyrylation and crotonylation, respectively. Catalyzes histone crotonylation.
Interaction partners:
- Enhancer of polycomb-like protein 1
- Chromatin modification-related protein EAF1
- Actin-related protein 4
- SAGA complex/NuA4 acetyltransferase complex subunit TRA1
- Chromatin modification-related protein YNG2
- Chromatin modification-related protein EAF6
- SWR1-complex protein 4
- Protein AF-9 homolog
- Chromatin modification-related protein EAF3
- Histone H4
Sequence:
MSHDGKEEPGIAKKINSVDDIIIKCQCWVQKNDEERLAEILSINTRKAPPKFYVHYVNYNKRLDEWITTDRINLDKEVLYPKLKATDEDNKKQKKKKATNTSETPQDSLQDGVDGFSRENTDVMDLDNLNVQGIKDENISHEDEIKKLRTSGSMTQNPHEVARVRNLNRIIMGKYEIEPWYFSPYPIELTDEDFIYIDDFTLQYFGSKKQYERYRKKCTLRHPPGNEIYRDDYVSFFEIDGRKQRTWCRNLCLLSKLFLDHKTLYYDVDPFLFYCMTRRDELGHHLVGYFSKEKESADGYNVACILTLPQYQRMGYGKLLIEFSYELSKKENKVGSPEKPLSDLGLLSYRAYWSDTLITLLVEHQKEITIDEISSMTSMTTTDILHTAKTLNILRYYKGQHIIFLNEDILDRYNRLKAKKRRTIDPNRLIWKPPVFTASQLRFAW
Protein: Pituitary adenylate cyclase-activating polypeptide (PACAP) [Cleaved into: PACAP-related peptide (PRP-48); Pituitary adenylate cyclase-activating polypeptide 27 (PACAP-27) (PACAP27); Pituitary adenylate cyclase-activating polypeptide 38 (PACAP-38) (PACAP38)] (Q29W19)
Organism: Bos taurus (Bovine)
Function: Binding to its receptor activates G proteins and stimulates adenylate cyclase in pituitary cells (By similarity). Promotes neuron projection development through the RAPGEF2/Rap1/B-Raf/ERK pathway (By similarity). In chromaffin cells, induces long-lasting increase of intracellular calcium concentrations and neuroendocrine secretion (By similarity). Involved in the control of glucose homeostasis, induces insulin secretion by pancreatic beta cells (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Pituitary adenylate cyclase-activating polypeptide type I receptor
- Vasoactive intestinal polypeptide receptor 1
- Vasoactive intestinal polypeptide receptor 2
- Secretin
- Secretin receptor
- Pro-glucagon
- Somatoliberin
- Pro-neuropeptide Y
- Corticoliberin
- Galanin peptides
Sequence:
MTMCSGARLALLVYGILMHSSVYGSPAASGLRFPGIRPENEVYDEDGNPQQDFYDSESLGVGSPASALRDAYALYYPAEERDVAHGILNKAYRKVLDQPSARRSPADAHGQGLGWDPGGSADDDSEPLSKRHSDGIFTDSYSRYRKQMAVKKYLAAVLGKRYKQRVKNKGRRIPYL
Protein: Inwardly rectifying potassium channel 2, isoform C (E1JIU5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003822}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003822}.
Interaction partners:
Sequence:
MQVPLSDVQVLQDPTDAETLVGGDKEETFAHMKEWKRQYMRGISHTPSQAGVYYEALKGSSHSLAKGSRNFRPGSMRRVRRRAVFKNGDCNVVQKHLQRRRVRFLQDMYTTMVDWQWRWTLLAFALSFILSWLFFALIWWLIIYTHGDLEEPHLPENQEESGWAPCVSAIDGFTSCFLFSIETQHTIGYGVRTTSPECPEAIFMMCFQSIYGVMSSAFMAGIVFAKMTRAKQRAQTLLFSKHAVICQRDGTLSLMFRVGDMRKSHIIGAGVRAQLIRTKSTKEGEVMTQYFTELEIGTDDSGSDLFFIWPMVIEHKIDENSPLYNLNATDMLQDKFEIVVILEGTVESTGQSTQARSSYINTEILWGHRFDPVVLYNKDLQAYEIDYARFNETTQVDTPLCSARELNEIYKIQEGFRTPASPSTQSRCSCSSGYQTPGRQSRLRWQLSVPL
Protein: Rap guanine nucleotide exchange factor 1 (A0A8I5ZQV4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSGKIEKADSQRSHLSSFTMKLMDKFHSPKIKRTPSKKGKPAEVSKTPEKPVSKEARDRFLPEGYPIPLDLEQQAVEFMSTSAVDSRSQRQKNLCWLEEKEKEVVSALRYFKTIVDKMAIDKKVLEMLPGSASKVLEAILPLVQTDPRIQHSSALSSCYSRVYQSLANLIRWSDQVMLEGVNSEDKEMVTTVKGVIKAVLDGVKELVRLTIEKQGRPSPTSPVKPSSPASKPDGQPELPLTEREMEILNKTSVSPSTELLPDSTSEEVAPPKPPLPGIRVVDNSPPALPPKKRQSAPSPTRVAVVAPMSRAVSGSSLPVGINRQDFDVECYTQRRLSGGSRSCGGESPRLSPCSSTGKLSRSDEQLSSLDRDSGQCSRNTSCETLDHYDPDYEFLQQDLSNADQTPPQAACNLSPLPESMGESGPPFVGYSFQLPLGSCLQQDGQQTDTPPALPEKKRRSAVSQTTDSSGCRVSYERHPSQYDNISEDDLQNPAQPVSYPPFAAILPFQQGASSTPVEFVGDFSVPESAGDPEKPPPLPEKKNKHMLAYMQLLEDYSEPQPSMFYQTPQSEHIYQQKNKMLMEVYGFSDSFCGSDSTQELAPPPALPPKQRQLQASYAASSFSVSHCVQQTKVAFTPEDGSAAQGLSVSVSNSFLNRHGSLPVPSEPPSGKDGHPRDLSVSSASGKDSRENGERSPKSLDALESAQSEEEVDELSLIDHNEIMARLTLKQEGDDGPDVRGGSGDILLVHATETDRKDLVLYCEAFLTTYRTFISPEELIKKLQCRYEKFSPFADTFKKRVSKNTFFVLVRVVDELCLVELTEEILKLLMELVFRLVCSGELSLARVLRKNILDKVDQKKLLRCAHSDQPLAARGVAARPGTLHDFHSHEIAEQLTLLDAELFYKIEIPEVLLWAKEQNEEKSPNLTQFTEHFNNMSYWVRSVIMLQEKAQDRERLLLKFIKIMKHLRKLNNFNSYLAILSALDSAPIRRLEWQRQTSEGLAEYCTLIDSSSSFRAYRAALSEVEPPCIPYLGLILQDLTFVHLGNPDYIDGKVNFSKRWQQFNILDSMRCFQQVHYEIRRNDDIINFFNDFSDHLAEEALWELSLKIKPRNITRRKTDREEKT
Protein: Meiosis-specific transcription factor mei4 (O13606)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Functions as a meiosis-specific transcription factor. Binds to the 5'-GTAAAYA-3' consensus sequence of the promoter of the spo6 gene.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- NURS complex subunit red1
- RNA binding exosome specificity factor Mmi1
- Sporulation-specific protein 5
- Meiotic recombination protein rec8
- Negative regulator of sexual conjugation and meiosis
- Enhancer of rudimentary homolog 1
- Sporulation-specific protein 6
- Exosome complex exonuclease rrp6
- Meiosis-specific cyclin crs1
- Meiosis protein mei2
Sequence:
MVENQGNVEAHGKPKKVILSLSLKESSKINDSQNVSNVSSKEKCETEALLREENKENLSSDSIRQMIFGDEMAGFVDTGEKPPCSYATLIGLAILQSHNKQLTLSGIYTWIRNTFRYYLNHDGGWQNSIRHNLSLNKAFIKVEKPKGKTLKGHYWTIDPDHMQNFVSVRLHRSHSTDSNSKKRPSSKCHEIKPLTTREIPLARKRSRLNSFNSSTSTSGSSSNVAAEVSNDASQPSNQDSSLNSNIVKPPLPPSNVQSNSSSSENVPKPNAETQEDLPTIDAHESSLYENVNDSRLYEVPACRNMALNTGYSDADPGYLRTSFRSNSHNSLPYSANEEEDVLQADFLVSQQSSMVSSYVSSRDPHSMPYYRREPIPLRPSSRFYEYTRPTYGRTDTSCSAPGAFCSTQINSPSSYINYSKCAPSSPTLSLQKHREHVKSLLYVPDLTPSFDGSDPWNPSSQLLSEPLFDQHSFQSSLDDLMSVTCFRDSPELNHESSGYSSAPLMPSNRAFINDFSL
Protein: Importin beta-like protein kap113 (Karyopherin-113) (O94545)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope. Involved in the export of mRNA from the nucleus to the cytoplasm. May play a role in mitotic spindle formation and/or function.
Subcellular location: Nucleus {ECO:0000269|PubMed:15116432, ECO:0000269|PubMed:16823372}. Note=Nuclear rim.
Interaction partners:
- Importin subunit beta-5
- Importin subunit beta-1
Sequence:
MQVDPVVYQLQRAVSQDPIAVKDAEGHLNNWKKEPGFFGKLYSIFLDKQNDMSLRWIAIIQLRNSIDIIWRKNTKMSLLPEERDFIRCNALLGSIKSENLLSIQNALVVSRIARLDYPTEWPSLFHDLLGKLQQSLGTGDYDVALRLLITLHHIIKAMAGNRLLRSRQIFYKLAPELLTILQPILHSSLSSWMMILESSKEIKDSTLLSYMQISRYTLKACRRLVVFGFQNPSESEFSERMLAFCAVHQRKLLSMLGTMLQSSRSPIVVGECLEMAFAHAFLFNKPFFDFSFYSPCLTKFPATIDYISLHYDFLGQISSHLSSYKEKFEESSKNFEKLVIMSLRVFILVIQEFCNTKSSHPETAQVLYNSFLVDNRINNLLDLLITKLLILKEEDFEEWTDSPQQWVLEQSTQDVEFNVRPCAEKLLKCFFDAYGDIIVSPFKDMIYSVFECPKTLTQAVQQDTLISSFGVGYTQLKSIFPFAKWLQEAAVPNMASINDIGISRVYRRRIAIFLSQWIEDSSSEQLLEVIYKLYCSFLNLTDPCNDAVVILTTIDAFKTVLDDWNFSENSFLSIKENLFVHVLSLFKAFESVDARTSILSLLGTLLARAGEHVAPMESTIASLLSQLWDGWKKEPLLRARVLAVMHQFVNAIKAKSFEFSTFLYTVIEYCVNPESPEHVIFEADAMELWSTFLMYIQKLPETFTLLIPHLLYHLSQATSTLPFVLMIVSSYQLLDNTVLMKDYSFTIFEKLNDLLDDVKNETLQALCKTVCLLIETTPMDMIYESLLNSSLLSRLLLSIATNDKHPQVLIEYLLVVSRISLREPELILKVCQTKNINIAMLIGNWILLNDHINHSKDRKLNTLALSSLLRTNHPDVLAVLDSIMNLWFSVLSEVEEDANGDATIYYKNDDYSAVGFYLDETSEEMTRRKQLLLKDPVHSVNSRSFFISVFMFCRDANGGMENFQNQYLSTVNPALLEQFQSML
Protein: Hydroxycarboxylic acid receptor 2 (G-protein coupled receptor 109A) (G-protein coupled receptor HM74A) (Niacin receptor 1) (Nicotinic acid receptor) (Q8TDS4)
Organism: Homo sapiens (Human)
Function: Acts as a high affinity receptor for both nicotinic acid (also known as niacin) and (D)-beta-hydroxybutyrate and mediates increased adiponectin secretion and decreased lipolysis through G(i)-protein-mediated inhibition of adenylyl cyclase. This pharmacological effect requires nicotinic acid doses that are much higher than those provided by a normal diet. Mediates nicotinic acid-induced apoptosis in mature neutrophils. Receptor activation by nicotinic acid results in reduced cAMP levels which may affect activity of cAMP-dependent protein kinase A and phosphorylation of target proteins, leading to neutrophil apoptosis. The rank order of potency for the displacement of nicotinic acid binding is 5-methyl pyrazole-3-carboxylic acid = pyridine-3-acetic acid > acifran > 5-methyl nicotinic acid = acipimox >> nicotinuric acid = nicotinamide.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17932499}; Multi-pass membrane protein {ECO:0000269|PubMed:17932499}.
Interaction partners:
- Hydroxycarboxylic acid receptor 3
- Density-regulated protein
- Pro-neuropeptide Y
- Sodium-coupled monocarboxylate transporter 1
- Free fatty acid receptor 2
- Appetite-regulating hormone
- Succinate receptor 1
Sequence:
MNRHHLQDHFLEIDKKNCCVFRDDFIVKVLPPVLGLEFIFGLLGNGLALWIFCFHLKSWKSSRIFLFNLAVADFLLIICLPFLMDNYVRRWDWKFGDIPCRLMLFMLAMNRQGSIIFLTVVAVDRYFRVVHPHHALNKISNRTAAIISCLLWGITIGLTVHLLKKKMPIQNGGANLCSSFSICHTFQWHEAMFLLEFFLPLGIILFCSARIIWSLRQRQMDRHAKIKRAITFIMVVAIVFVICFLPSVVVRIRIFWLLHTSGTQNCEVYRSVDLAFFITLSFTYMNSMLDPVVYYFSSPSFPNFFSTLINRCLQRKMTGEPDNNRSTSVELTGDPNKTRGAPEALMANSGEPWSPSYLGPTSP
Protein: Myocardin-related transcription factor (Q6B4I4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSEGEQRLHATFLGSSDDGNNSDCYDARQSPPKAIVDSSPLQPAMDKNKESLKVKLMVRRPHSQLVEQGIIPSLKTSPAIHEQCKQLERAKTSDLLKAKIQQRPNREDLERLHILEEDECHIDPSLAEKQRMLKKARLADQLNSQIQHRPGPLELIKKNILHTEKPIEKIVKEGLVSFKATGEGLLTRPQHPHSYVTFDDDSLSSESDTRQTPPRLDEAMVATSSSPTDVLQAAAASAGIVTMALTMPTAGQLVVTSPQILPQQQQPKAIVVKQETANLYEELCQSVTGTTASPVNHLYSPCSLASSTSTLSPLSSIASPPPPPMTTTRLHLAPVSVKSDAPGKDKNRKKSKSKPVSKARTIKFHEYKGPPSAAGQKQDQTQPEETSYQLMLEQQNCLLKFLENLNKNQSIIPAPSAPGVMLPAAPGATNNSITVTTKTVPALASQSAPAPAPISLPNTISITSSSGGAPLNFGDATMLTPTPAATPTPPTLSLIAAPQQQLQLHQQHQQLHQPTPVQHPPPLPSPALSVSSSIPPSPATSYAESTTSSITDLARLEKMKVSDLKQHLKRRNLPVSGPKPHLIERLKPYLPLEPLDSNVTPAPTSNNSNTTPEVITISDAMDTSNCGLLEQPPPVTMLVSDASMEHEQMDVVQQQMDNTHPMTLQTILPPQPQTATIILTNEELLREQQRKIDELQRQLQRSQQELQKIRQRQQQQQHQQQQTVTAQVVNALPSQQITLITTTSNGPQQTLTVMPQQVEKNFPAKVTVKATGGNSNHKVNGLQQQGSAAKKPASSNSNSNSNISSSNPPPINQKMVVKQQLEAKIQKQKAAAAAAAQQQQQQQQQQQQQQQQQALQQQQQQQQQQQQVRLLTQKTQTVFIPFNNNNHINNASAKTTTKKSNVPANNTNTTTATMMQAAKPAAVAAAAASPGNQHHNNLGLLWNEGNQTILLLGLNDQHMTAHTLGNISLTATTTTTAAPPAATPVAASTIAPPKKILNGHQRTNSLPSIVFPIETKSIITQQQLQQLQQQQQQQQQFQPVQQPKQQQLNQVDIKPAPAPPPQYEEATKQLAASKAAALNGLLPLVKIKEEPVQSPAPSAAPLPQTAPLCKRKTASIKSEQVSDVLDILIKQGELPESAALEPITPLTPLPELSMFNGATPTTAAGGASIVPLVPKLETPVTPVQNLDVAMDTNVQHVGFASNQAPNHVFIESIDMASPLQTDSSAIDAESVAKTLDIFLEQHHATPPPSTPPKSCHSGSEKPNSPDAKLNHFDEYELLELMSQQLEMDMGDDSSGYCHASAAKSSNNNGNLRRDLNPSLQPSINELLDASSPDNVLLNNNTGADVDFDADSFVAQLSQHVTGNGNSPGVNCNGSIESSSSAVNSHFGSHSTPMDCDDFESTLNSFMQAVTQPQAGQHVEYATSTSMANGTGGGMGVDNGTGGAVDAFNASGDIFDLFNMDDYKMNWAAGDFTV
Protein: BLOC-3 complex member HPS1 (Hermansky-Pudlak syndrome 1 protein homolog) (O08983)
Organism: Mus musculus (Mouse)
Function: Component of the BLOC-3 complex, a complex that acts as a guanine exchange factor (GEF) for RAB32 and RAB38, promotes the exchange of GDP to GTP, converting them from an inactive GDP-bound form into an active GTP-bound form. The BLOC-3 complex plays an important role in the control of melanin production and melanosome biogenesis and promotes the membrane localization of RAB32 and RAB38.
Interaction partners:
- BLOC-3 complex member HPS4
- BLOC-2 complex member HPS3
- BLOC-2 complex member HPS6
- BLOC-2 complex member HPS5
- Biogenesis of lysosome-related organelles complex 1 subunit 6
- Biogenesis of lysosome-related organelles complex 1 subunit 3
- Dysbindin
- Biogenesis of lysosome-related organelles complex 1 subunit 4
- Biogenesis of lysosome-related organelles complex 1 subunit 2
- Biogenesis of lysosome-related organelles complex 1 subunit 1
Sequence:
MKCVLVATEGAEVLFYWTDEEFAESLRLKLQQSEDEEEELPVLEDQLSTLLAPVIISSMTMLEKLSDTYTCFSTENDNHLYVLHLFGEYLFVAINGDHSESEGDLRRKLCVLKYLFEVHFGLVTVDGQLIRKELRPPDLEERARVWKHFQRLLGTYSYLRDREQSFAVEAVERLIHPQLCEQSIETLERHVVQAINASPERGGEEVLHAFLLVHCKLLAFYSGHGASTLRPADLLALILLVQDLQPSPGTTEEEEEEEDSDSPQRRPKSSQNIPVQQARSQSTSVPTRSSRETDTDSISLPEEYFTPAPSPGDQSSGSLVWLDGGTPPSDALQMAEDTPEGLASHSPELPSPRRIFLDANIKENYCPLVPHTMYCLPLWPGINMVLLTKSPSTPLALILYQLLDGFSLLEKKLKEGQEAGSALRSQPFVADLRQKMDKFIKNRVGQEIQNTWLEFKSKAFSRSEPGSSWELLQVCGKLKRQLCVIYRLSFLVTAPSRGGPHLPQHLQDRAQKLMKERLLDWKDFLLVKSRRNVTMVSYLEDFPGLVHFIYVDRTTGQMVAPSLSPNEKMSSELGKGPLAAFVKAKVWALVRLARRYLQKGCTTLLFQEGDFRCSYFLWFENDMGYKLQMIEVPVLSDDSVPIGVLGGDYYRKLLRYYSKSHPSEPVRCYELLTLHLSVIPTDLLVQQASQLARRLGEASRVTLP
Protein: Mitochondrial tRNA-specific 2-thiouridylase 1 (EC 2.8.1.14) (Q9DAT5)
Organism: Mus musculus (Mouse)
Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14746906}.
Interaction partners:
- 5-taurinomethyluridine-[tRNA] synthase subunit MTO1, mitochondrial
- 5-taurinomethyluridine-[tRNA] synthase subunit GTPB3, mitochondrial
- tRNA dimethylallyltransferase
- Elongation factor Ts, mitochondrial
- Cytoplasmic tRNA 2-thiolation protein 1
- Pseudouridylate synthase 1 homolog
- Methionyl-tRNA formyltransferase, mitochondrial
- Cysteine desulfurase
- Adenylyltransferase and sulfurtransferase MOCS3
- Elongation factor Tu, mitochondrial
Sequence:
MSALRHVVCALSGGVDSAVAALLLRRRGYQVTGVFMKNWDSLDEQGVCAADKDCEDAYKVCQILDIPFHQVSYVKEYWNDVFSDFLNEYEKGRTPNPDINCNKHIKFSCFYHYAVDNLGADAVATGHYARTSLEDEEVFEQKHTKKPDGLFRNRFEVRNPVKLLQAADSFKDQTFFLSQVSQDALRRTIFPLGELTKDFVKKIAAENSLHHVLQKRESMGICFIGKRNLEHFLLQYLQPRPGKFVSIEDNTVLGTHKGWFLYTLGQRAKISGLREPWYVVEKDGTKGDVLVAPRVDHPALYRDLLRTNRVHWIAEEPPAALVRDKMMECHFRFRHQMALVPCVLTLNQDGTVWVTAVKAVRGLALGQFAVFYKGEECLGSGKILRLGPSAYTLQKGKNRTRVAPEASSDSPGLHPTS
Protein: Transcriptional activator NphR (B1Q2A8)
Organism: Rhodococcus sp
Function: Transcriptional activator of nphA1 and nphA2 involved in the degradation of 4-nitrophenol (4-NP).
Interaction partners:
Sequence:
MAEREQSNDSARTDVPAIVSLRTRELDTGEGRMQWASTLERLYCETDVAWPEPRRHFDAEWGGRPFGDLHVSTIRADAHTVVRSPAMIQSDSGEGYLVCLVTDGSVEVRQSGRATVVEPGSFALLDCAAPFVFHSPAPFRQVVVRSPREVLTSRLPGRIVEHGTARSIHGDTGAGGLVGRLFVDIADMDAPMSQGAAVSFASSAVDMLATALTEGLLATSAADLHRTEDLTRVQRVIEQNLHDADITLSDIAAAAGMSLRTVHKLFNAEGTTTRAWLYQARLEAARRYLLTTDLSVADVSECAGFRDVSHFSRLFRSTFGSSPGLYRKEHARIGS
Protein: Bifunctional cytochrome P450/NADPH--P450 reductase 2 (CYP102A3) (Fatty acid hydroxylase CypB) (Flavocytochrome P450 102A3) [Includes: Cytochrome P450 102A3 (EC 1.14.14.1); NADPH--cytochrome P450 reductase (EC 1.6.2.4)] (O08336)
Organism: Bacillus subtilis (strain 168)
Function: Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of a range of medium to long-chain fatty acids, with a preference for long-chain unsaturated and branched-chain fatty acids over saturated fatty acids. Hydroxylation of myristic acid occurs mainly at the omega-2 and omega-3 positions, in approximately equal proportions. Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Polyketide synthase PksJ
- HTH-type transcriptional repressor FatR
- Surfactin synthase subunit 3
- Dimodular nonribosomal peptide synthase
- Polyketide synthase PksN
- Bifunctional cytochrome P450/NADPH--P450 reductase 1
- Sulfite reductase hemoprotein beta-component
- Putative aldehyde dehydrogenase AldY
- Putative aldehyde dehydrogenase DhaS
- Putative aldehyde dehydrogenase AldX
Sequence:
MKQASAIPQPKTYGPLKNLPHLEKEQLSQSLWRIADELGPIFRFDFPGVSSVFVSGHNLVAEVCDEKRFDKNLGKGLQKVREFGGDGLFTSWTHEPNWQKAHRILLPSFSQKAMKGYHSMMLDIATQLIQKWSRLNPNEEIDVADDMTRLTLDTIGLCGFNYRFNSFYRDSQHPFITSMLRALKEAMNQSKRLGLQDKMMVKTKLQFQKDIEVMNSLVDRMIAERKANPDENIKDLLSLMLYAKDPVTGETLDDENIRYQIITFLIAGHETTSGLLSFAIYCLLTHPEKLKKAQEEADRVLTDDTPEYKQIQQLKYIRMVLNETLRLYPTAPAFSLYAKEDTVLGGEYPISKGQPVTVLIPKLHRDQNAWGPDAEDFRPERFEDPSSIPHHAYKPFGNGQRACIGMQFALQEATMVLGLVLKHFELINHTGYELKIKEALTIKPDDFKITVKPRKTAAINVQRKEQADIKAETKPKETKPKHGTPLLVLFGSNLGTAEGIAGELAAQGRQMGFTAETAPLDDYIGKLPEEGAVVIVTASYNGAPPDNAAGFVEWLKELEEGQLKGVSYAVFGCGNRSWASTYQRIPRLIDDMMKAKGASRLTAIGEGDAADDFESHRESWENRFWKETMDAFDINEIAQKEDRPSLSITFLSEATETPVAKAYGAFEGIVLENRELQTAASTRSTRHIELEIPAGKTYKEGDHIGILPKNSRELVQRVLSRFGLQSNHVIKVSGSAHMAHLPMDRPIKVVDLLSSYVELQEPASRLQLRELASYTVCPPHQKELEQLVSDDGIYKEQVLAKRLTMLDFLEDYPACEMPFERFLALLPSLKPRYYSISSSPKVHANIVSMTVGVVKASAWSGRGEYRGVASNYLAELNTGDAAACFIRTPQSGFQMPNDPETPMIMVGPGTGIAPFRGFIQARSVLKKEGSTLGEALLYFGCRRPDHDDLYREELDQAEQDGLVTIRRCYSRVENEPKGYVQHLLKQDTQKLMTLIEKGAHIYVCGDGSQMAPDVERTLRLAYEAEKAASQEESAVWLQKLQDQRRYVKDVWTGM
Protein: D-mannonate dehydratase Caul1427 (ManD) (EC 4.2.1.8) (B0T0B1)
Organism: Caulobacter sp. (strain K31)
Function: Catalyzes the dehydration of D-mannonate. Has no detectable activity with a panel of 70 other acid sugars (in vitro).
Interaction partners:
- Mannitol dehydrogenase domain
- Altronate dehydratase
- Altronate dehydratase
- 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase
- D-xylose 1-dehydrogenase
- D-xylose 1-dehydrogenase
- D-xylose 1-dehydrogenase
- D-mannonate dehydratase Caul1835
- PfkB domain protein
- Ribose-5-phosphate isomerase A
Sequence:
MLKIIDAKVIVTCPGRNFVTLKITTSDGVTGVGDATLNGRELAVVSYLRDHMIPCLIGRDAHRIEDVWQFFYRGSYWRGGPVAMTALAAVDMALWDIKAKLAGMPLYQLLGGACREGVMVYGHANGETIEDTIAEARKYQALGYKAIRLQSGVPGLPSTYGVSGDKMFYEPADGNLPTENVWSTSKYLKHAPKLFEAAREALGDDVHLLHDVHHRLTPIEAGRLGKDLEPYRLFWLEDAVPAENQAGFRLIRQHTTTPLAVGEIFSHVWDCKQLIEEQLIDYLRATVLHAGGITNLRKIAAFADLHHVRTGCHGATDLSPITMAAALHFDLSVSNFGLQEYMRHTPETDAVFPHAYSYKDGMLHPGEAPGLGVDIDEALAGQYPYKRAYLPVNRLEDGTMYNW
Protein: Kinesin-like protein (V9HW29)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MADLAECNIKVMCRFRPLNESEVNRGDKYIAKFQGEDTVVIASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGSTYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTLLFGQRAKTIKNTVCVNVELTAEQWKKKYEKEKEKNKILRNTIQWLENELNRWRNGETVPIDEQFDKEKANLEAFTVDKDITLTNDKPATAIGVIGNFTDAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLAEIGIAVGNNDVKQPEGTGMIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDALSEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKAKLITDLQDQNQKMMLEQERLRVEHEKLKATDQEKSRKLHELTVMQDRREQARQDLKGLEETVAKELQTLHNLRKLFVQDLATRVKKSAEIDSDDTGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENASRDRKRYQQEVDRIKEAVRSKNMARRGHSAQIAKPIRPGQHPAASPTHPSAIRGGGAFVQNSQPVAVRGGGGKQV
Protein: Hemagglutinin-esterase (HE protein) (EC 3.1.1.53) (E3 glycoprotein) (Q70KP1)
Organism: Porcine torovirus (strain P10) (PoTV)
Function: Structural protein that makes short spikes at the surface of the virus. Contains receptor binding and receptor-destroying activities. Mediates de-O-acetylation of N-acetyl-9-O-acetylneuraminic acid, which is probably the receptor determinant recognized by the virus on the surface of erythrocytes and susceptible cells. This receptor-destroying activity is important for virus release as it probably helps preventing self-aggregation and ensures the efficient spread of the progeny virus from cell to cell. May serve as a secondary viral attachment protein for initiating infection, the spike protein being the major one. Seems to be a 'luxury' protein that is not absolutely necessary for virus infection in culture. However, its presence in the virus may alter its pathogenicity. May become a target for both the humoral and the cellular branches of the immune system.
Subcellular location: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=In infected cells becomes incorporated into the envelope of virions during virus assembly at the endoplasmic reticulum and cis Golgi. However, some may escape incorporation into virions and subsequently migrate to the cell surface (By similarity). {ECO:0000250}.
Interaction partners:
Sequence:
MLRMRVRPPSAIPVFLIFVLLPFVLTSKPITPHYGPGHITSDWCGFGDSRSDCGNQHTPKSLDIPQELCPKFSSRTGSSMFISMHWNNDSDFNAFGYSNCGVEKVFYEGVNFSPYRNYTCYQEGSFGWVSNKVGFYSKLYSMASTSRCIKLINLDPPTNFTNYRNGTCTGNGGTAKMPDNPQLVIFNSVVKVSTQFVLPSSSDGFSCTKHLVPFCYIDGGCFEMSGVCYPFGYYYQSPSFYHAFYTNGTAGLHRYICDYLEMKPGVYNATTFGKFLIYPTKSYCMDTMNYTVPVQAVQSIWSENRQSDDAIGQACKSPYCIFYNKTKPYLAPNGADENHGDEEVRQMMQGLLVNSSCVSPQGSTPLALYSSEMIYTPNYGSCPQYYKLFETSSDENVDVTSSAYFVATWVLLVLVIILIFILISFCLSSY
Protein: RAMP-like triterpene glycoside receptor (D7FB54)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MYLDIIDMVETCLFSSFAIFSKIFPGLLLIFSPHHAFCIWGNMRALLKYTWTHFFVKYEDALKVTVLKFVKHLELIFIPEFQLCLYELCFSITDCLK