wanglab/gogpt-training-data huggingface dataset:
Protein: Non-structural polyprotein pORF1 [Includes: Methyltransferase (EC 2.1.1.-) (EC 2.7.7.-); Putative protease (EC 3.4.-.-) (Putative papain-like cysteine protease) (PCP); NTPase/helicase (EC 3.6.4.-); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48)] (Q9WC28)
Organism: Hepatitis E virus genotype 1 (isolate Human/India/Hyderabad) (HEV-1)
Function: Methyltransferase: Displays a capping enzyme activity. This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus. The enzymatic reaction involves a covalent link between 7-methyl-GMP and the methyltransferase, whereas eukaryotic capping enzymes form a covalent complex only with GMP. Methyltransferase catalyzes transfer of a methyl group from S-adenosylmethionine to GTP and GDP to yield m(7)GTP or m(7)GDP. GDP is a better substrate than GTP. This enzyme also displays guanylyltransferase activity to form a covalent complex, methyltransferase-m(7)GMP, from which 7-methyl-GMP is transferred to the mRNA to create the cap structure.
Subcellular location: Host cytoplasm {ECO:0000250|UniProtKB:Q81862}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:Q81862}.
Interaction partners:
Sequence:
MEAHQFLKAPGITTAVEQAALATANSALANAVVVRPFLSHQQIEILINLMQPRQLVFRPEVFWNQPIQRVIHNELELYCRARSGRCLEIGAHPRSINDNPNVVHRCFLRPVGRDVQRWYTAPTRGPAANCRRSALRGLPAADRTYCFDGFSGCSCPAETGIALYSLHDMSPSDVAEAMFRHGMTRLYAALHLPPEVLLPPGTYRTASYLLIHDGRRVVVTYEGDTSAGYNHDVSNLRSWIRTTKVTGDHPLVIERVRAIGCHFVLLLTAAPEPSPMPYVPYPRSTEVYVRSIFGPGGTPSLFPTSCSTKSTFHAVPAHIWDRLMLFGATLDDQAFCCSRLMTYLRGISYKVTVGTLVANEGRNASEDALTAVITAAYLTICHQRYLRTQAISKGIRRLEREHDQKFITRLYSWLFEKSGRDYIPGRQLEFYAQCRRWLSAGFHLDPRVLVFDESAPCHCRTVIRKALSKFCCFMKWLGQECTCFLQPAEGVVGDQGHDNESYEGSDVDPAESAISDISGSYVVPGTALQPLYQALDLPDEIVARACRLTATVKVSQVDGRIDCETLLGNKTFRTSFVDGAVLETNGPERHNLSFDASQSTMAAGPFSLTYAASAAGLEVRYVGAGLDHRAIFAPGVSPRSNPGEVTAFCSALYRFNREAQRHSLTGNLWFHPEGLIGLFAPFSPGHVWESAKPFCGESTLYTRTWSEVDAVSSPTRPDLGFMSEPPIPSRAATPTLAAPLPPLAPDPSPPSSAPALDEPASAATSGVPAITHQTARHRRLLFTYPDGSKVFAGSLFESTCTWLVNASNVDHCPGGGLCHAFYQRYPASFDAACFVMRDGAAAYTLTPRPIIHRVAPDYRLEHNPKRLEAAYRETCSRLGTAAYPLLGTGIYQVPIGPSFDAWERNHRPGDELYLPELAARWFEANRPTRPTLTITEDAARTANLAIELDSATDVGRACAGCRVTPGVVQYQFTAGVPGSGKSRSITRADVDVVVVPTRELRNAWRRRGFAAFTPHTAARVTDGRRVVIDEAPSLPPHLLLLHMQRAATVHLLGDPNQIPAIDFEHPGLVPAIRPDLAPTSWWHVTHRCPADVCELIRGAYPMIQTTSRVLRSLFWGEPAVGQKLVFTQAAKPANPGSVTVHDSQGATYTYTTIIATADARGLIQSSRAHAIVALTRHTEKWVIIDAPGLLREVGISDAIVNNFFLAGGEIGHQRPSVIPRGNPDANVDTLAAFPPSCQISAFHQLAEELGHRPAPVAAVLPPCPELEQGLLYLPQELTTCDSVVTFELTDIVHCRMAAPSQRKAVVSTLVGRYGRRTKLYNASHSDVRDSLARFIPAIGPVQVTTCELYELVEAMVEKGQDGSAVLELDLCNRDVSRITFFQKDCNKFTTGETIAHGKVGQGISAWSKTFCALFGPWFRAIEKAILALLPQGVFYGDAFDDTVFSAAVAAAKASMVFENDFSEFDSTQNNFSLGLECAIMEECGMPQGLIRLYHLIRSAWILQAPKESLLGFWKKHSGEPGTLLWNTVWNMAVITHCYDFRDLQVAAFKGDDSIVLCSEYRQSPGAAVLIAGCGLKLKVDFRPMRLYAGVVVAPGLGALPDVVRFAGRLTEKNWGPGPERADELRIAVSDFLRKLTNVAQMCVDVVSRVYGVSPGLVHNLIGMLQAVADGKAHFTESVKPVLDLTNSILCRVE
Protein: glucan endo-1,3-beta-D-glucosidase (EC 3.2.1.39) (G8B5S1)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Interaction partners:
- chitinase
Sequence:
MNLKVLLIAVLPFMAAKVTAETEEDETLTVTRTHFVTNPCASYFASSLLPNNPEGLTTGIPVVFVQVPKANANQKEKIQVTSTITRTNTHIVYKTGVPKSKGGIQSKTNNDASCSTITAYSTITHETSTCSSDKCQVHTYTTVLPSVYTITGDTTAEETSTAKVKSNPESQKATNKIQGSLSLSGVVGDASRDTQLASPSTTSVDVAETTTTSTIFSATKTPESTYSPSTSLESLPTTKSAPVTSQSVVSESKSVTIDISSITDDVTISNNATEVSTINSNSTSASQSTSSNPLSESLQPLETTLSTILISASATGPYFNSSIVSTSYLTSAISTESFETSISSSQSPSEESSGESSSTPTSSKETEVAIATDTCYSGDLFSPIDTNAPPSIFPRQQLPLSIPSGVNNNGAPIQTNKFYANLFLGDQDLMVYTYPYGLYWSKESYYGFGVQHTNVSDRVFGSQNTNNRGVSSYYFNPTNNGEIILSATEFAHSSMHMGLSDMTEMAAKVKLSTTAGQDLNYLEIPIVQGMGFVTGVYNGNLVPELNSLYGFRTLELEESDALLSNILKYRATLFNGVNWLIYITLPTENDDFELIAEDSYHLKASKSVDGLIIQVAIAPETSKDQFYDAAAGMYVTDASIQGSVVCSSSALYSFVYETSGSSSSGNPIVFTLPHHLQTLTTTSGATGITVSSQTKGEMTAFLTKKLSFSDTIDKNIKFLPYIAGKTGQLSYSSDQLTLLATSANDELAVDIASTVANMNSNYFSGKVLDKYAQILLVVSEIINDDAVTNATLAELKDAFETFLSNQQYFPLMYDTKFGGVTSTAAQNGDDGADFGSAFYNDHHFHYGYFVHAAAVVGHIDKKLGGTWAEDNKDWVNSLVRDVANPSRSDSYFPVSRSFSWYDGHSWAAGLYESNDGRNQESSSEDIHFAYGMKLWGNVIEDYAMEARGGLMLSIMSRAFNLYFYYKSDNTVQPQEILPNKVSGIFFENKVEYTTYFGTPDQHPEYVHGIHMLPITAASSSVRIPSYVQEEWRDQISTFIDNVNSGWTGILRLNQAIIDPRSSFEFFSSKDWSDRYLDNGQSRTWSLAFSGGVL
Protein: RNA polymerase sigma factor SigF (Sigma factor SigF) (Alternative RNA polymerase sigma factor SigF) (RNA polymerase sigma-F factor) (Sigma-F factor) (Stress response/stationary phase sigma factor SigF) (P9WGI3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Held in an inactive form by a cognate anti-sigma factor RsbW (UsfX) until released. Increased expression decreases growth rate, and after 3 days increases the expression of 51 loci encoding 33 protein-coding genes as well as some non-coding RNA.
Interaction partners:
- Anti-sigma-F factor RsbW
- Multidomain regulatory protein Rv1364c
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit beta'
- Osmosensory protein A
- ECF RNA polymerase sigma factor SigH
- ECF RNA polymerase sigma factor SigL
- DNA-directed RNA polymerase subunit alpha
- ECF RNA polymerase sigma factor SigD
- ECF RNA polymerase sigma factor SigC
Sequence:
MTARAAGGSASRANEYADVPEMFRELVGLPAGSPEFQRHRDKIVQRCLPLADHIARRFEGRGEPRDDLIQVARVGLVNAAVRFDVKTGSDFVSFAVPTIMGEVRRHFRDNSWSVKVPRRLKELHLRLGTATADLSQRLGRAPSASELAAELGMDRAEVIEGLLAGSSYHTLSIDSGGGSDDDARAITDTLGDVDAGLDQIENREVLRPLLEALPERERTVLVLRFFDSMTQTQIAERVGISQMHVSRLLAKSLARLRDQLE
Protein: Uncharacterized protein (Q54W34)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Uncharacterized protein
- Probable tRNA N6-adenosine threonylcarbamoyltransferase
- N
Sequence:
MKIKNVSKNLILYLFILHFLLVNIVHSNGLFDQLFKIQHTTNIDVRLIGFDSLEQDELKILLNKLNKDYSPTILYPKLQTIDLIKQNHKFNITEGSHNLNEEIKASVKKYISEFQHRSTLKQDEYLVPFDIVDNIIAQDYKQQNHISYVVYIINTIYDREDSIEKYTYSQLNSTTINTLHRDGINVVDHLCNVKLWQSKSESPNNPNNSNDGSGRYVWIDIGAETCTYGPQTKGTGLISNQQLPHTNSRFTKKLYDISTFFYHTIRQLISPPIYEIPEKYGWIDLEIQLIMIHDHLVGQLEVSEQFDWESIKEQLGEKMPLLPNQRITFSKREVSLLNNLYAAQIKQSSLKTHHSVLKGTQQFLDSKELHHWFKVHIQKFIPSYLDDSSKTIIPIFLFDISYKELLLLDRYYQAVSFPDMVIGIQTQSGLMKIDYQCDKQLGINPMDATKPILQSLLMTIWGVGSNSLVVNENSKQIENNFIWNIGYNPSNMFTNLKDLSFSQTDSAIRNYLYFDIISSIDSLKSIMDHIGDDETWEEFTHSIDNPSVRSIDSFFKSINSTITQINSNLQLHQYSKAYDRINQLSDLAMNISSVIHKIHSSKHSYLECEKSTFLLSEFISISFTTIIVIYFLYKVLRKSLF
Protein: Bardet-Biedl syndrome 8 (Q9VPP9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Bardet-Biedl syndrome 1
- Bardet-Biedl syndrome 9
- BBSome complex member BBS4 homolog
- BBSome complex member BBS5
- BBSome interacting protein 1
- Protein claret segregational
- Very long-chain fatty acid transport protein
- long-chain-fatty-acid--CoA ligase
- long-chain-fatty-acid--CoA ligase
Sequence:
MASAMLATLELDYFRAVSLYRRRSYERCAELCNALLQAGHDGHVQLFTTKEEEEEEQHQQQQAEHSRFGSNLQRIGPRPRGAAGGGAGAVDSGPSIMMPTWLMEGVWQLKMRALTQRVYVDDLDEDDGGNEATEEVEFERIATAARPGSSIKTAFQPRPLTSQRAQQARSRGAGVAHSSDGRLNSSRPGSAAVARPGTSLSRPGSSLGSRCGTASRIRATSAAAFNVGDATSKLYQASRLNPTIYAERETLVKALFQFLYYHEADVQKAHSLCQAVLEVERQKPSGSTGCTLSWWWQQQMGRCLLALHYPRRAEPFLQQSLTSFPHPDTYLLLSRVYQRIKQPERALLVIGEVVDSRPFDVTYRLEQARIHQAMEQQEDALQLYRLAAKLHPINVESLASIAVGYFYDNNPEMALMYYRRILSLGAQSPELYCNIALCCLYGGQIDLVLPCFQRALATATQPGQKSDIWYNLSFVAVTSGDFNLAKRCLQLCLTSDAQNGAALNNLAVLAAQSGDILGAKSYLNAAKDVMPDAAEVTTNLQFMDVHYKL
Protein: Aquaporin-11 (AQP-11) (Q8BHH1)
Organism: Mus musculus (Mouse)
Function: Channel protein that facilitates the transport of water, glycerol and hydrogen peroxide across membrane of cell or organelles guaranteeing intracellular homeostasis in several organes like liver, kidney and brain. In situation of stress, participates in endoplasmic reticulum (ER) homeostasis by regulating redox homeostasis through the transport of hydrogen peroxide across the endoplasmic reticulum membrane thereby regulating the oxidative stress through the NADPH oxidase 2 pathway. Plays a role by maintaining an environment suitable for translation or protein foldings in the ER lumen namely by participating in the PKD1 glycosylation processing resulting in regulation of PKD1 membrane trafficking thereby preventing the accumulation of unfolding protein in ER. Plays a role in the proximal tubule function by regulating its endosomal acidification. May play a role in postnatal kidney development.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16107722, ECO:0000269|PubMed:21118806, ECO:0000269|PubMed:24854278}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8NBQ7}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q8NBQ7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8NBQ7}. Cell membrane {ECO:0000250|UniProtKB:F6S3G9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8NBQ7}. Note=Localizes mainly to the periphery of lipid droplets. Localizes to cytoplasmic vesicles in maturing spermatozoa. It accumulates partly in mitochondrial-associated endoplasmic reticulum membranes. {ECO:0000250|UniProtKB:Q8NBQ7}.
Interaction partners:
- Aquaporin-7
- Aquaporin-8
- Lens fiber major intrinsic protein
- Aquaporin-3
- Aquaporin-6
- Aquaporin-4
- Aquaporin-5
- Aquaporin-1
- Aquaporin-9
- Aquaporin-2
Sequence:
MSALLGLRPEVQDTCISLGLMLLFVLFVGLARVIARQQLHRPVVHAFVLEFLATFQLCCCTHELQVLSEQDSAHPTWTLTLIYFFSLVHGLTLVGTASNPCGVMMQMILGGMSPEMGAVRLLAQLVSALCSRYCISALWSLSLTKYHYDERILACRNPIHTDMSKAIIIEAICSFIFHSALLHFQEVRTKLRIHLLAALITFLAYAGGSLTGALFNPALALSLHFPCFDELFYKFFVVYWLAPSVGVLMMILMFSFFLPWLHNNQMTNKKE
Protein: Enoyl-acyl carrier reductase (EC 1.3.1.9) (C6KSZ2)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Nodulation protein E
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase
- Malonyl CoA-acyl carrier protein transacylase
- 3-oxoacyl-[acyl-carrier-protein] reductase
- Bifunctional dihydrofolate reductase-thymidylate synthase
- 3-oxo-5-alpha-steroid 4-dehydrogenase, putative
- NADH-cytochrome b5 reductase, putative
- Inactive lipoate--protein ligase 2
- Adrenodoxin-type ferredoxin, putative
- Ferredoxin, apicoplast
Sequence:
MNKISQRLLFLFLHFYTIVCFIQNNTQKTFHNVLQNEQIRGKEKAFYRKEKRENIFIGNKMKHLNNMNNTHNNNHYMEKEEQDASNINKIKEENKNEDICFIAGIGDTNGYGWGIAKELSKRNVKIIFGIWPPVYNIFMKNYKNGKFDNDMIIDKDKKMNILDMLPFDASFDTANDIDEETKNNKRYNMLQNYTIEDVANLIHQKYGKINMLVHSLANAKEVQKDLLNTSRKGYLDALSKSSYSLISLCKYFVNIMKPQSSIISLTYHASQKVVPGYGGGMSSAKAALESDTRVLAYHLGRNYNIRINTISAGPLKSRAATAINKLNNTYENNTNQNKNRNSHDVHNIMNNSGEKEEKKNSASQNYTFIDYAIEYSEKYAPLRQKLLSTDIGSVASFLLSRESRAITGQTIYVDNGLNIMFLPDDIYRNENE
Protein: Protein Shroom3 (Q9QXN0)
Organism: Mus musculus (Mouse)
Function: Controls cell shape changes in the neuroepithelium during neural tube closure. Induces apical constriction in epithelial cells by promoting the apical accumulation of F-actin and myosin II, and probably by bundling stress fibers. Induces apicobasal cell elongation by redistributing gamma-tubulin and directing the assembly of robust apicobasal microtubule arrays (By similarity).
Subcellular location: Cell junction, adherens junction {ECO:0000269|PubMed:10589677}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10589677}. Apical cell membrane {ECO:0000269|PubMed:22493320}; Peripheral membrane protein {ECO:0000305}. Note=Colocalizes with F-actin in stress fibers and adherens junctions.
Interaction partners:
- Rho-associated protein kinase 2
- Rho-associated protein kinase 1
- 14-3-3 protein sigma
Sequence:
MKTPENLEEPSATPNPSRTPTERFVYLEALLEGGAPWGFTLKGGLERGEPLIISKIEEGGKADSVSSGLQAGDEVIHINEVALSSPRREAVSLVKGSYKTLRLVVRRDVCAAPGHADPGTSKSLSSELLTCSPQHRKATWSGGVKLRLKQRCSEPATRPHSWHTTKFGETQPDVSMMQISQGTMGPPWHQSYHSSSSTSDLSNYDHAYLRRSPDQCSSQGSMESLEPSGGYPPCHLLSPAKSTSSIDQLGHLHNKRDSAYSSFSTSSSIFEYPPPGGSARERSGSMDVISARGGLLEGMRQADIRYVKTVYDTRRGVSSEYEVNPSALLLQGRDAHASADSQGCAKWHSIPRGKGTPSPSWSQQCSGSLETATDNLPQKAGAPLPPTRSDSYAAFRHRERPSSWSSLDQKRFCRPQTNSSGSQKTPFAEDQLHTVPERSPENSPPVKSKHNYTQKAQPGQPLLPTGIYPVPSPEPHFAQVPQPSVSSNGTVYPALVKESGYTAAQGTCNKMATLDENGNQNEASRPGFAFCQPLEHNSVTPVEKRPEPTAKYIYKVHFSSVPENEDSSLKRHITPPHGHSPYPSERKNIHGGSRACSNHHSLSSPQAQALHVGDDRRPSRLSQPWEGDFQEDHNANLRQKVEREGQGQGLSGNSGRTRSAFSSLQNIPESLRRQSNVELGEAQEVHPGGRSKVEDPGRKAGASDIRGYLDRSVSYPRPEGKMNAVDSVHSADSRYEESPAPALPQTSGASQRRLSSSSSAAPQYRKPHCSVLEKVSRIEEREQGRHRPLSVGSSAYGPGYRPGRTGPTPSTSSSDLDDPKAGSVHFSESTEHLRNGEQNPPNGEAKQEEASRPQCSHLIRRAPADGRGPPARGGEPSRPEARLLRSQSTFQLYSEAEREASWSEDRPGTPESPLLDAPFSRAYRNSIKDAQSRVLGATSFRRRDLEPGTPATSRPWRPRPASAHVGMRSPEAAVPSSSPHTPRERHSVTPAAPQAARRGPRRRLTVEQKKRSYSEPEKMNEVGVSEEAEPTPCGPPRPAQPRFSESTVADRRRIFERDGKACSTLSLSGPELKQFQQSALADYIQRKTGKRPTGAACTPEAGLRERAQSAYLQAGPAAPDGPGLASACSLSSLREPEALPRKEHTHPSAADGPQAPRDRSSSFASGRLVGERRRWDPQVPRQLLSGANCEPRGVQRMDGAPGGPPSWGMVAGKAGKSKSAEDLLERSDTLAVPVHVRSRSSPTSDKKGQDVLLREGSNFGFVKDPCCLAGPGPRSLSCSDKGQNELALPLHHPTPCWNGSGCKATVASSAPPESSGAADHLKQRRAPGPRPLSAGMHGHFPDARAASLSSPLPSPVPSASPVPSSYRSQLAMDQQTGQQPPSSPASAVTQPTSPRSPELSSPAYGLGEGMWKRTSLPQRPPPPWVKWAHAVREDGLAEDTLAPEFANLKHYRNQPSRPSSCSTSDPDTPGRISLRISESALQPSPPPRGDYDDEVFMKDLHPKVTSSPTFEALPPPPPPSPPSEEPLVNGTDDFPPPPPPQALCEVLLDGEASTEAGSGPCRIPRVMVTREGHVPGAAHSEGSQIMTATPPQTSAKGSEAESNTPSSASAQPQLNGSPGKQLCPSQTRNLTYEPVERTQDLGKKTHAEPQKTSEDIRTEALAKEIVHQDKSLADILDPDSRMKTTMDLMEGLFPGDASVLMDSGAKRKALDITARRAGCEAKASDHKEAVSVLVNCPAYYSVSAAKAELLNKIKDMPEELQEEEGQEDVNEKKAELIGSLTHKLESLQEAKGSLLTDIKLNNALGEEVEALISELCKPNEFDKYKMFIGDLDKVVNLLLSLSGRLARVENVLRGLGEDASKEERSSLNEKRKVLAGQHEDARELKENLDRRERVVLDILANYLSAEQLQDYQHFVKMKSTLLIEQRKLDDKIKLGQEQVRCLLESLPSDFRPKAGAISLPPALTGHATPGGTSVFGGVFPTLTSPL
Protein: Copine-B (Q86K21)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MTTPISLSKPRVELRFKCSHLKNLDICSKSDPLIMVFDKRGEHGESIFVGQTEKINNNLNPEFKKSVIIDYHFENIQNLSFIVVDIDKEIKRVGDLEGNDIIGQYTTTLGNIISKPNKKVISEIKHKGKETGVIEITAEEIRETGHNFLFKINGTKLDKKDLFTSDPYFKIYKTSSSGNVLVYQSVVIKNTLNPNYEPVMMKLEELNNGDMFRELVFEFWDHDSVGEHDFIGLFTTNADTVLKGITREFPLINAKKAAKKSGSYKNSGVITFTDCRLVGQPTFIDYLSGGCEINLMVAIDCTASNGSPSTSTSLHYHTPSHPSQYAKSIFSVGSVLAPYDSDGNIEVLGFGGIHRGSTSHCFQFGSKKEVRGVEGVLLTYGEVIPSMSLSYPTNFKDIISYAAKKSLDGVTSKSQKYTILLILTDGEISDMNETVHEIVKASKQSPLSIVIIGIGEATFDNMNRLDGDDGNSLTDSSGQTATRDIVQFVPFNNFSANPEALATETLREIPQQLLGFMNQNNYLPMSHRLK
Protein: Platelet-activating factor acetylhydrolase IB subunit alpha1 (EC 3.1.1.47) (PAF acetylhydrolase 29 kDa subunit) (PAF-AH 29 kDa subunit) (PAF-AH subunit gamma) (PAFAH subunit gamma) (Q61205)
Organism: Mus musculus (Mouse)
Function: Alpha1 catalytic subunit of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)) heterotetrameric enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and modulates the action of PAF. The activity and substrate specificity of PAF-AH (I) are affected by its subunit composition. Both alpha1/alpha1 homodimer (PAFAH1B3/PAFAH1B3 homodimer) and alpha1/alpha2 heterodimer(PAFAH1B3/PAFAH1B2 heterodimer) hydrolyze 1-O-alkyl-2-acetyl-sn-glycero-3-phosphoric acid (AAGPA) more efficiently than PAF, but they have little hydrolytic activity towards 1-O-alkyl-2-acetyl-sn-glycero-3-phosphorylethanolamine (AAGPE). Plays an important role during the development of brain.
Subcellular location: Cytoplasm.
Interaction partners:
- Platelet-activating factor acetylhydrolase IB subunit beta
- Platelet-activating factor acetylhydrolase IB subunit alpha2
- Platelet-activating factor acetylhydrolase 2, cytoplasmic
- Lysophosphatidylcholine acyltransferase 1
- Platelet-activating factor acetylhydrolase
- Lysophosphatidylcholine acyltransferase 2
- Lysophospholipid acyltransferase LPCAT4
- Lysophosphatidylcholine acyltransferase 2B
- Cholinephosphotransferase 1
- Choline/ethanolaminephosphotransferase 1
Sequence:
MSGEGENPASKPTPVQDVQGDGRWMSLHHRFVADSKDKEPEVVFIGDSLVQLMHQCEIWRELFSPLHALNFGIGGDSTQHVLWRLENGELEHIRPKIVVVWVGTNNHSHTAEQVTGGIKAIVQLVNKLQPQARVVVLGLLPRGQHPNPLREKNRQVNELVRAALAGYPRAHFLDADPGFVHSDGTISHHDMYDYLHLSRLGYTPVCRALHSLLLRLLAQDQGQGIPLPETAS
Protein: Histidine--tRNA ligase, cytoplasmic (EC 6.1.1.21) (Histidyl-tRNA synthetase) (B4DDD8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MAERAALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDESKQKFVLKTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKDFDIAGNFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQDPKLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPAQAGEEPLGVGSVAAGGRYDGLVGMFDPKGRKVPCVGLSIGVERIFSIVEQRLEALEEKIRTTETQVLVASAQKKLLEERLKLVSELWDAGIKAELLYKKNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEIKRRTGQPLCIC
Protein: DDB1- and CUL4-associated factor 12-like protein 1 (WD repeat-containing protein 40B) (Q5VU92)
Organism: Homo sapiens (Human)
Interaction partners:
- DNA damage-binding protein 1
- DDB1- and CUL4-associated factor 12-like protein 2
- DDB1- and CUL4-associated factor 8-like protein 1
- DDB1- and CUL4-associated factor 8-like protein 2
- DDB1- and CUL4-associated factor 11
- Cullin-4B
Sequence:
MAQQQTGSRKRKAPAVEADAESSPSQGLAAADGEGPLLLKRQRRPATYRSMAHYLKVREVGGWGPARLQGFDGELRGYAVQRLPELLTERQLELGTVNKVFASQWLNSRQVVCGTKCNTLFVVDVESGHIARIPLLRDSEARLAQDQQGCGIHAIELNPSKTLLATGGENPNSLAIYQLPSLDPLCLGDRHGHKDWIFAVAWLSDTVAVSGSRDGTVALWRMDPDKFDDTVAWHSEVGLPVYAHIRPRDVEAIPRAIINPSNRKVRALACGGKNQELGAVSLDGYFHLWKAGSALSRLLSIRLPYFRDNVCLTYCDDMSVYAVGSHSHVSFLDLRQDQQNIRPLCSREGGTGVRSLSFYRHIITVGTGQGSLLFYDVRAQKFLEERASATLESSSGPARRKLRLACGRGWLNHNDFWVNYFGGMEVFPNALYTHCYNWPEMKLFVAGGPLPAGLHGNYAGLWS
Protein: Palmitoyltransferase (EC 2.3.1.225) (A1Z833)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGNDDHRRRKTPCGFCMAVFKWIPVLFITAVIAWSYYAYVVELCIRNSENRIGMIFMLLFYHLFLTLFMWSYWRTIMTSVGRIPDQWRIPDEEVSRLFRADSPDTQKRILNNFARDLPVTNRTMNGSVRFCEKCKIIKPDRAHHCSVCSCCVLKMDHHCPWVNNCVNFYNYKYFVLFLGYALVYCLYVAFTSLHDFVEFWKVGAGQLNASGMGRFHILFLFFIAIMFAISLVSLFGYHIYLVLVNRTTLESFRAPIFRVGGPDKNGYNLGRYANFCEVFGDDWQYWFLPVFSSRGDGYSYPTSSDQSRVSTSSPTQRYDAMGDTTTSRLDGNPTDKLIGASPLDTTNHHHNQSPHQVRSTSVLPTQLLQIQPPSTCRDELNERQQKLANGQSLDCSTPAAMSSPDERGVNGAAVYIEMIGDHPLTSADPAKGFPRPPNGDLPV
Protein: Serine/threonine-protein kinase 32C (EC 2.7.11.1) (PKE) (Yet another novel kinase 3) (Q86UX6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRSGAERRGSSAAASPGSPPPGRARPAGSDAPSALPPPAAGQPRARDSGDVRSQPRPLFQWSKWKKRMGSSMSAATARRPVFDDKEDVNFDHFQILRAIGKGSFGKVCIVQKRDTEKMYAMKYMNKQQCIERDEVRNVFRELEILQEIEHVFLVNLWYSFQDEEDMFMVVDLLLGGDLRYHLQQNVQFSEDTVRLYICEMALALDYLRGQHIIHRDVKPDNILLDERGHAHLTDFNIATIIKDGERATALAGTKPYMAPEIFHSFVNGGTGYSFEVDWWSVGVMAYELLRGWRPYDIHSSNAVESLVQLFSTVSVQYVPTWSKEMVALLRKLLTVNPEHRLSSLQDVQAAPALAGVLWDHLSEKRVEPGFVPNKGRLHCDPTFELEEMILESRPLHKKKKRLAKNKSRDNSRDSSQSENDYLQDCLDAIQQDFVIFNREKLKRSQDLPREPLPAPESRDAAEPVEDEAERSALPMCGPICPSAGSG
Protein: Microcin C7 self-immunity protein MccF (Q47511)
Organism: Escherichia coli
Function: Involved in specific self-immunity to microcin C7.
Interaction partners:
Sequence:
MMIQSHPLLAAPLAVGDTIGFFSSSAPATVTAKNRFFRGVEFLQRKGFKLVSGKLTGKTDFYRSGTIKERAQEFNELVYNPDITCIMSTIGGDNSNSLLPFLDYDAIIANPKIIIGYSDTTALLAGIYAKTGLITFYGPALIPSFGEHPPLVDITYESFIKILTRKQSGIYTYTLPEKWSDESINWNENKILRPKKLYKNNCAFYGSGKVEGRVIGGNLNTLTGIWGSEWMPEILNGDILFIEDSRKSIATIERLFSMLKLNRVFDKVSAIILGKHELFDCAGSKRRPYEVLTEVLDGKQIPVLDGFDCSHTHPMLTLPLGVKLAIDFDNKNISITEQYLSTEK
Protein: ALX homeobox protein 1 (Cartilage homeoprotein 1) (CART-1) (Q8C8B0)
Organism: Mus musculus (Mouse)
Function: Sequence-specific DNA-binding transcription factor that binds palindromic sequences within promoters and may activate or repress the transcription of a subset of genes. Most probably regulates the expression of genes involved in the development of mesenchyme-derived craniofacial structures. Early on in development, it plays a role in forebrain mesenchyme survival. May also induce epithelial to mesenchymal transition (EMT) through the expression of SNAI1 (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:12929931}.
Interaction partners:
Sequence:
MEFLSEKFALKSPPSKNSDFYMGTGGALEHVMETLDNESFYGKATAGKCVQAFGPLPRAEHHVRLDRTSPCQDSSVNYGITKVEGQPLHTELNRAMDNCNNLRMSPVKGMPEKSELDELGDKCDSNVSSSKKRRHRTTFTSLQLEELEKVFQKTHYPDVYVREQLALRTELTEARVQVWFQNRRAKWRKRERYGQIQQAKSHFAATYDISVLPRTDSYPQIQNNLWAGNASGGSVVTSCMLPRDASSCMTPYSHSPRTDSSYTGFSNHQNQFSHVPLNNFFTDSLLTGATNGHAFETKPEFERRSSSIAVLRMKAKEHTANISWAM
Protein: Cullin-1 (CUL-1) (Cullin-A) (O60999)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Probable core component of cullin-based SCF-like E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit (By similarity). Required at several stages during development. CulA and fbxA regulate multicellular development by targeting regA for degradation via a pathway that requires erkB function, leading to an increase in cAMP and PKA activity.
Interaction partners:
- RING-box protein 1
- Cullin-associated NEDD8-dissociated protein 1
- Elongin-C
- Cullin-5
- Cullin-2
- F-box/WD repeat-containing protein A
- COP9 signalosome complex subunit 5
- Ubiquitin-like protein NEDD8
- UDP-galactose:fucoside alpha-3-galactosyltransferase
- NEDD8-conjugating enzyme Ubc12
Sequence:
MSMMTSTPTKRSVKLDDIWPELEEGIYKIITDLNKGFPKQKWIALYTHVYDYCAASQSKSSAKVGMPKQQASGANYVGEDLYNRLNLFLKKHMSQLLKLTETKMDEPLLNYYYTEWDRYTSAMKYINNIFQYMNRYWIKREIDDGKKEVYEIFILSLVIWRDCLFTPLKQRLTNSLLDIIESERNGYQINTHLIKGVINGYVSLGLNREKPKETILQVYKSGFEELFLTATENYYTNESAKFISENSVADYMKKVETRLNEEVKRVQQYLHQNTESELIAKCEKVLIEKHVEVIWNEFQTLLEKDKIPDLTRMYSLLSRIPRGLEPLRTTLEKHVQNVGLQAVSSIATNGVIEPKVYIETLLKVFKKYNELVTGAFRSDTGFVASLDKACRRFINENAVTIAAKSSSKSPELLARFTDFLLKKSPNNPEESEMEQLLNDVMIVFKYIEDKDVFQDFYSKMLAKRLIHGTSTSEDLEGTMIGKLKSTCGYEYTSKLQRMFTDMSLSRELLDRFNNHIEQVERSSLNIDFSVLVLATGSWPLQPPSTNFSIPKELQACEQLFQKFYQNQHSGRKLNWLHHLSKGELKTKYLQTSKSGYTLQCSTYQIGVLLQFNQYETLTSEEIQESTQLIDSVLKGTLTSLAKSKILLADPPLDDEEIAKTTKFSLNKQFKNKKTKIFINVPVLTQVKEEIDSIHKTVEEDRKLQIQAAIVRIMKMRKQLAHSGLMTEVISQLQTRFNPKVNIIKKCIDILIEKEYLMRVEGKKDHYSYVA
Protein: Geranyl-CoA carboxylase, beta-subunit (Q9HZV9)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Citronellyl-CoA dehydrogenase involved in catabolism of citronellol
- Biotin carboxylase
- Isohexenylglutaconyl-CoA hydratase
- Peroxisomal trans-2-enoyl-CoA reductase
- Expressed protein with apparent function in citronellol catabolism
- Biotin carboxylase
- Short chain dehydrogenase involved in catabolism of citronellol
- Repressor of atu genes
- Very-long chain acyl-CoA synthetase
- Probable acyl-CoA dehydrogenase
Sequence:
MPAIQSELDVNGEDFARNREAMLAAVAGFRELEQKVLDKAAEARPKFEKRGQLLPRERLALLLDPGAPFLELSSLAGYKLHDDKDGTQAGGGIIAGIGYIAGVRCLVSASNSAIKGGTISPTGLKKTLRLQQIAMENKLPVVTLTESGGANLNYAAEIFVEGARGFANQARISAMGIPQVTVVHGSSTAGGAYQPGLSDYVVVVRGKAKMFLAGPPLLKAATGEIASDEELGGAELHAQVAGTAEYLAENDADGVRLAREIVGMLPWNAQLPARPARSWREPLYPVEELLGVVPADPKKPYDVREIVARIADGSEFLDFKNEFDGQTVCGHLRIEGHACGLIGNNGPITPQGAAKAAQFIQLCEQSNTPLLFLHNTTGFMVGTESERQGVIKHGSKMIQAVANARVPKLTLVVGGSYGAGNYAMCGRGLDPRFIFAWPNSRTAVMGGAQAGKVLRIVTEEKHAKEGKEADPKMLEMLETVTAQKLDSQSTALYGTASLWDDGLVDPRDSRRLLGYLLDICAEAEARPLKGNSFGVARF
Protein: 5'-nucleotidase domain-containing protein 3 (EC 3.1.3.-) (GRP94-neighboring nucleotidase) (Q3UHB1)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MATVAAAARGAGARAAAGLRSCGGAVARERPRSGCARRLCSAPAAPAAVDMKSYLWARYHEAKRSTDELVPSIMNNLLNPDAIFSNNEMSLSDIEIYGFDYDYTLVFYSKHLHTLIFNAARDLLINEHRYPVEIRKYEYDPSFAIRGLHYDVQRAVLMKIDAFHYIQMGTVYRGLSVVPDEEVIDMYEGSHVPLEQMSDFYGKSSHGNTMKQFMDIFSLPEMTLLSCVNEHFLKNNIDYEPVHLYKDVKDSIRDVHIKGIMYRAIEADIEKYICYADQTRAVLAKLAAHGKKMFLITNSPSSFVDKGMRYIVGKDWRDLFDVVIVQAEKPNFFNDKRRPFRKVNEKGVLLWDKIHKLQKGQIYKQGNLYEFLKLTGWRGSKVLYFGDHIYSDLADLTLKHGWRTGAIIPELRSELRIMNTEQYIQTMTWLQTLTGLLEQMQVHRDAESQLVLQEWKKERKEMREMTKSFFNAQFGSLFRTDQNPTYFLRRLSRFADIYMASLSCLLNYDVHHTFYPRRTPLQHELPAWSDSPSAFKAPLLQEAQAK