wanglab/gogpt-training-data huggingface dataset:
Protein: adenylate cyclase (EC 4.6.1.1) (Q9VXU0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MPPGVLVNDSRANSTDDIQIALAPHIQTYLSQTGRRHSCCSVMLPVAFERAAAKSWLDPKFDSPVLEEQYQASVFPHVRMRYRFTLSYILLCSLMWCLYFVVDGGSEDFWRPISSSFSMLSLVTIMALCFTHWDLYREHRTVTSAVTALLLCGASLAFLTYTGRAFSPLGHFAICLEIVLLIYTALPMPLWLGASTAISYSIAFEMVSHMVIGCSAIHGGPMHGGGGAAGGSGMEANGDPSNRILILRIMAHLSVHLVGVHVLIMNLVRMRGTFMKVGQNLLVRRQLEMEKQLKEKMIHSVMPPKVADMLLNEGGPSGLDAGGLPPESHYMRPRASNDVKSLFRPFHMHSMENVSILFADIVGFTRMSSTKTAEQLVEILNDLFERFDDLCSLSGCEKISTLGDCYYCVSGCPEPRADHAICCVEMGLGMIDAMRCFDAQRHEGVKMRVGVHTGTVLCGIVGTRRVKFDVWSNDVSLANKMESSGKPEQVHISQETSSFLGDAYYLEEGEEVFGHRTYFVVGRRRDFTRTNSLSPSMPANATGSSLLLPGAHGASLSQSATNVSAVQPNVPPASPVGQLSSSLNPSPVLSMRPRLTSLSMKMRKKSQSRDRDVERGIIHPAAAGIPPVIVVRERPKIIITTKSLPGSLDSDEQPPVSPPLLPPANPPAAETRSKIKLKVWKIPRFLKRFEDLTNRSSCGGSSSAGHLDKEREREREKEKEELHQHNQLNPEETLAFMDNQMQNGNGCGYQQLPVLVESNHRTQTLDIPAARPVLHHAATSTALASSVLRSPEAGVSGGGGCCSPGQYSMYDDIIDVRSYISQSRSDISPFGRSGSYRSQCGRQSTGGVNGAGPAGVGAEGRAGTSQTAPPVEQSPLPRPRASTLATGRPTPNSLEPGPSSTSPCCLPAPGNSVGGGGIFPPTHSRQSSICPSATSRKDSGIKSNSRRSSIQQQIYALNQTAISQHRVSGYFTSSTSSISNLGEVQGLGLPLAVQPPPPLLMPACSSQMADPLAACLQQLRKQSDLQLIRCVRDNARSQRSYLVKPPLRKFSLYFKSRQLERDFRSKAHRFGAENETEGPPTLATPRYNTYIDIFVGIAVYLCISVSLFLMTQNTVSPSFRLWVTLFSCFTGIQVFALFLFTRQMCRRQSGSNVSNRFRSKSTTSEDLERDERGAAPGGRPHFESCADRIFEAISSWYPWHICLAVLMAMPVLLIIANFLLLDLEQLEAFEYHYGFLIFVCIVHFCNFTQLNCWVRNVLAFLAALCFIGIAVSQLMVYSHNRSDQQQDQEASNFIQEIKWFQDYHVEIYLDLLLILVLVWFLNREFEIGYRLTFYGNAVANQDKVRVQNMKNQADMLLHNIIPKHVAEHLKNTAKYSENHHNIAIIFASIVNFNEMYDESYLGGKEFLRVLNELIGDFDELLSRPEFRAVEKIKTIGSTFMAASGLDPSHRGTGDEHIHTLMEFSIAMQEVVDAFNKDLLEFNLILRIGMNIGDVTAGVIGTSKLYYDIWGDAVNVASRMDSTGLPNRIQVGKDCLPFLTNRYEFEPRGSVYVKGKDHMEVFLYTTRRDNPLDDDEADKVEQLGTKKMEHEGRDEDVVQGEQQAEDKDEEEEEEEEDDDLHSSETTTLFKSQESLQANGGSHLAPNAAATSHTHTITLTNNNNHNSSNINNNIATSNTTTTANNNSMPVET
Protein: Rhoptry neck protein 4 (Q8IIK5)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Gametocyte-specific protein
Sequence:
MSSVRFFLCIFLVLFTFIDIVKPFKGNYGEANFSFFQATPASHIEEPQKTESTDAQSNITQNEEINNTKPLQENITNNQQNSNEQQNNNEQQNNIEQQNNNIQQNNIDTSISHVPNDTIKNPIDNSNISNLDKSNDTNNVIKHEENNQTKENNLETIKHTEPLTNQNTNEVKINDHNEHEKNTEENKIEEQYNNINHHSHDINKNQSINNNMNNENADKNVPHLDQSAMSNEKHINEHTTNHPIESHTGENNHDKINEPIPIEHATTPTNEPIPIEHAATPTNEPIPIEHAATPTNEPIHIEHVATPANEPTHSEHATTTTNEPIHIEHAATPTNEHIHNEHATTTTNEPTHNEHAATITHEPTHNEHTTTPTNEPIHNEHATTPTNEPIPIEHIATPANEPTHNEHATTTTNEPTHNEHTTTPTNEPIHNEHATTPTNEPIPIEHIATPANEPTHNEHATTTTNEPTHNEHATTTTNEPTHNEHATTTTNEPIHNEHATATTNESTHNEHATTTTNEPTHNEHSTTPTNESTHSENATTSTNEQHSHDQNTEVHPNDKLALVPFQGIKNPIPSNESQPIISFPNEDDNHAQNEGSINAPSEGEHNNTDNKEGPIITPLEGEQAGTAHKEDVTHKHMVGEHVPPQKTHHGPIITPVGGNHVPPQTHHAHIITPVGGEHAHGQGNNDTTYVTMNTDESSSSDTKGEHSNLRSYNKNMNNNHAQRDQYDSDTLNSEGSDDAYSSMQQNFEKNGIDSFKGKGLHVSLRERIIIEIMESAKNGIDGLLKLKDSKDSGKLFMEALEKLNINMKDLKKDKNLISLEVYDKILSTMFKILTEMSFYEDSKFYETLGIKKDILNQSLKDIKIKMLRKLGVSYSRLPPIIKHTEGKCAIKDIIISISSKELAQRMAIMFTKWLAPDEYGAVVDYENNVELNVLCSGAPILIQQWKYYQNMLGFEEDKDHAYLGLIDELLVMNKRYSQNKDYVETLEKIKKSKVFKHCTKIMRIGGKVSSVPFNYENVKKPSSSIIGSLGNLIKANISTYYKATAQRINSYFHYTEKKSKKSSPLKIISVCTLLHLTDMLYKCSDENSNGVMDLYNLQLNTLNMKGKMVLQYLVHLKFLTQEKKNQLKEICEPQNGLIDETLTKMLILLSTDSHELLSHELENKGFDEDYIQDEIKNINESDNNIRDKEEDDAEKMIFDDL
Protein: GMP synthase [glutamine-hydrolyzing] (EC 6.3.5.2) (GMP synthetase) (Glutamine amidotransferase) (Q9P772)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Inosine-5'-monophosphate dehydrogenase
- Adenine phosphoribosyltransferase
- Guanylate kinase
- Inosine triphosphate pyrophosphatase
- CTP synthase
- Dihydroorotate dehydrogenase
- 3',5'-cyclic-nucleotide phosphodiesterase
- Probable arginine--tRNA ligase, cytoplasmic
- Golgi apyrase
- Glutamyl-tRNA
Sequence:
MSSTEVPGEVSTSVSSYFDTILILDFGSQYSHLIARRLREIHVYAELLPCTQKIEALPFKPIGVILSGGPYSVYDDIAPHVDPAVFELGVPVLGICYGMQEIAWLNGRCVEPGIEREYGPATVSMEPEIKTEVFKSFFNSMPKEFEVWMSHGDRLSALPNGYETIGRTKNSPFAVIAHVTKPIIGLQFHPEVTHTPLGLQLIKNFAIEICHAKPNWSMENFVDKEILRIRKMIGPSDHVIGAVSGGVDSTVASKVLKEAIGDRFHAIMVDNGLLRLNEAEIVRETLNKHLGIQLTVVDASEEFIGKLKGVTDPEKKRKIIGNTFIHVFEREAERIVKETNGKVEYLLQGTLYPDVIESISFKGPSQTIKTHHNVGGLLKDMKLKLIEPLRELFKDEVRALGELLGIEHSLVWRHPFPGPGLGIRILGEVNAAQLEIARKADHIFITEIRNHGYYDKISQAFAALLPVKAVGVMGDKRTHEQVIALRAITTSDFMTADWYDGFSIKFLKLVSSRICNEVSGVNRVLYDISSKPPATVEME
Protein: Chaperone protein YscY (Yop proteins translocation protein Y) (P61417)
Organism: Yersinia pestis
Function: Required for Yop secretion. Functions probably as a chaperone which stabilizes YscX within the cell, before its secretion.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10714987}.
Interaction partners:
Sequence:
MNITLTKRQQEFLLLNGWLQLQCGHAERACILLDALLTLNPEHLAGRRCRLVALLNNNQGERAEKEAQWLISHDPLQAGNWLCLSRAQQLNGDLDKARHAYQHYLELKDHNESP
Protein: Interferon-related developmental regulator 2 (Protein SKMC15) (Q12894)
Organism: Homo sapiens (Human)
Interaction partners:
- Ubiquitin-like protein FUBI
- Large ribosomal subunit protein eL36
- Small ribosomal subunit protein eS7
- Large ribosomal subunit protein eL20
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein uL2
- Small ribosomal subunit protein eS26
- Small ribosomal subunit protein uS2
- Small ribosomal subunit protein eS28
- Small ribosomal subunit protein uS5
Sequence:
MPRARKGNTLRKGGQRRGGGARSSAQADSGSSDDEAASEARSTASECPSLLSTTAEDSLGGDVVDEQGQQEDLEEKLKEYVDCLTDKSAKTRQGALESLRLALASRLLPDFLLERRLTLADALEKCLKKGKGEEQALAAAVLGLLCVQLGPGPKGEELFHSLQPLLVSVLSDSTASPAARLHCASALGLGCYVAAADIQDLVSCLACLESVFSRFYGLGGSSTSPVVPASLHGLLSAALQAWALLLTICPSTQISHILDRQLPRLPQLLSSESVNLRIAAGETIALLFELARDLEEEFVYEDMEALCSVLRTLATDSNKYRAKADRRRQRSTFRAVLHSVEGGECEEEIVRFGFEVLYMDSWARHRIYAAFKEVLGSGMHHHLQNNELLRDIFGLGPVLLLDATALKACKVPRFEKHLYNAAAFKARTKARSRVRDKRADIL
Protein: Chibby, isoform E (B9A0M5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Armadillo segment polarity protein
- CBY1-interacting BAR domain-containing protein homolog
- 14-3-3 protein zeta
- Exportin-1
- RAC serine/threonine-protein kinase
Sequence:
MQLATFCCPSSISDSQPLPFKQLFAMPLFNKKFESKPIPVRQGRCNIGHPVATEDLDDFRQISLTLGNKELRFADGIWMHSTRKGDVDDMLRLNKKFRALEEENNMCNLKIEVMLDLLAEHATELSELKPKEK
Protein: Spectrin beta chain, non-erythrocytic 4 (Beta-IV spectrin) (Spectrin, non-erythroid beta chain 3) (Q9H254)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}.
Interaction partners:
- Ankyrin-3
- Ankyrin-2
- Ankyrin-1
- Neuronal cell adhesion molecule
- Spectrin alpha chain, non-erythrocytic 1
- Neurofascin
- Spectrin alpha chain, erythrocytic 1
- Spectrin beta chain, non-erythrocytic 5
- Spectrin beta chain, non-erythrocytic 2
- Potassium voltage-gated channel subfamily KQT member 2
Sequence:
MAQVPGEVDNMEGLPAPNNNPAARWESPDRGWEREQPAASTAAASLFECSRIKALADEREAVQKKTFTKWVNSHLARVGCHIGDLYVDLRDGFVLTRLLEVLSGEQLPRPTRGRMRIHSLENVDKALQFLKEQRVHLENVGSHDIVDGNHRLTLGLVWTIILRFQIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLVDFSKLTKSNANYNLQRAFRTAEQHLGLARLLDPEDVNMEAPDEKSIITYVVSFYHYFSKMKALAVEGKRIGKVLDQVLEVGKIIERYEELAAELLAWIHRTVGLISNQKFANSLSGVQQQLQAFTAYCTLEKPVKFQEKGNLEVLLFSIQSKLRACNRRLFVPREGCGIWDIDKAWGELEKAEHEREAALRAELIRQEKLELLAQRFDHKVAMRESWLNENQRLVSQDNFGYELPAVEAAMKKHEAIEADIAAYEERVQGVAELAQALAAEGYYDIRRVAAQRDSVLRQWALLTGLVGARRTRLEQNLALQKVFQEMVYMVDWMEEMQAQLLSRECGQHLVEADDLLQKHGLLEGDIAAQSERVEALNAAALRFSQLQGYQPCDPQVICNRVNHVHGCLAELQEQAARRRAELEASRSLWALLQELEEAESWARDKERLLEAAGGGGAAGAAGAAGTAGGAHDLSSTARLLAQHKILQGELGGRRALLQQALRCGEELVAAGGAVGPGADTVHLVGLAERAASARRRWQRLEEAAARRERRLQEARALHQFGADLDGLLDWLRDAYRLAAAGDFGHDEASSRRLARQHRALTGEVEAHRGPVSGLRRQLATLGGASGAGPLVVALQVRVVEAEQLFAEVTEVAALRRQWLRDALAVYRMFGEVHACELWIGEKEQWLLSMRVPDSLDDVEVVQHRFESLDQEMNSLMGRVLDVNHTVQELVEGGHPSSDEVRSCQDHLNSRWNRIVELVEQRKEEMSAVLLVENHVLEVAEVRAQVREKRRAVESAPRAGGALQWRLSGLEAALQALEPRQAALLEEAALLAERFPAQAARLHQGAEELGAEWGALASAAQACGEAVAAAGRLQRFLHDLDAFLDWLVRAQEAAGGSEGPLPNSLEEADALLARHAALKEEVDQREEDYARIVAASEALLAADGAELGPGLALDEWLPHLELGWHKLLGLWEARREALVQAHIYQLFLRDLRQALVVLRNQEMALSGAELPGTVESVEEALKQHRDFLTTMELSQQKMQVAVQAAEGLLRQGNIYGEQAQEAVTRLLEKNQENQLRAQQWMQKLHDQLELQHFLRDCHELDGWIHEKMLMARDGTREDNHKLHKRWLRHQAFMAELAQNKEWLEKIEREGQQLMQEKPELAASVRKKLGEIRQCWAELESTTQAKARQLFEASKADQLVQSFAELDKKLLHMESQLQDVDPGGDLATVNSQLKKLQSMESQVEEWYREVGELQAQTAALPLEPASKELVGERQNAVGERLVRLLEPLQERRRLLLASKELHQVAHDLDDELAWVQERLPLAMQTERGNGLQAVQQHIKKNQGLRREIQAHGPRLEEVLERAGALASLRSPEAEAVRRGLEQLQSAWAGLREAAERRQQVLDAAFQVEQYYFDVAEVEAWLGEQELLMMSEDKGKDEQSTLQLLKKHLQLEQGVENYEESIAQLSRQCRALLEMGHPDSEQISRRQSQVDRLYVALKELGEERRVALEQQYWLYQLSRQVSELEHWIAEKEVVAGSPELGQDFEHVSVLQEKFSEFASETGMAGRERLAAVNQMVDELIECGHTAAATMAEWKDGLNEAWAELLELMGTRAQLLAASRELHKFFSDARELQGQIEEKRRRLPRLTTPPEPRPSASSMQRTLRAFEHDLQLLVSQVRQLQEGAAQLRTVYAGEHAEAIASREQEVLQGWKELLSACEDARLHVSSTADALRFHSQVRDLLSWMDGIASQIGAADKPRDVSSVEVLMNYHQGLKTELEARVPELTTCQELGRSLLLNKSAMADEIQAQLDKLGTRKEEVSEKWDRHWEWLQQMLEVHQFAQEAVVADAWLTAQEPLLQSRELGSSVDEVEQLIRRHEAFRKAAAAWEERFSSLRRLTTIEKIKAEQSKQPPTPLLGRKFFGDPTELAAKAAPLLRPGGYERGLEPLARRASDTLSAEVRTRVGYVRQELKPERLQPRIDRLPEIPGRVEPAALPAAPEDAAETPATPAAAEQVRPRPERQESADRAEELPRRRRPERQESVDQSEEAARRRRPERQESAEHEAAHSLTLGRYEQMERRRERRERRLERQESSEQEMPIRGDLVKGKATLADIVEQLQEKEAGPGLPAGPSLPQPRELPPGRLPNGLELPERTPRPDRPRARDRPKPRRRPRPREGGEGGGSRRSRSAPAQGGSAPAPPPPPTHTVQHEGFLLRKRELDANRKSSNRSWVSLYCVLSKGELGFYKDSKGPASGSTHGGEPLLSLHKATSEVASDYKKKKHVFKLQTQDGSEFLLQAKDEEEMNGWLEAVASSVAEHAEIARWGQTLPTTSSTDEGNPKREGGDRRASGRRK
Protein: Sal-like protein 1 (Zinc finger protein Spalt-3) (Sal-3) (mSal-3) (Q9ER74)
Organism: Mus musculus (Mouse)
Function: Transcriptional repressor involved in organogenesis. Plays an essential role in ureteric bud invasion during kidney development.
Subcellular location: Nucleus {ECO:0000269|PubMed:11836251, ECO:0000269|PubMed:19483677}.
Interaction partners:
- DNA helicase
- Chromodomain-helicase-DNA-binding protein 4
- Homeobox protein NANOG
- Histone deacetylase 1
- Histone-binding protein RBBP4
- Histone-binding protein RBBP7
- Metastasis-associated protein MTA2
- Chromodomain-helicase-DNA-binding protein 5
- Histone deacetylase 2
- Transcription factor SOX-2
Sequence:
MSRRKQAKPQHFQSDPEVASLPRRDGDTEKGQPSRPTKSKDAHVCGRCCAEFFELSDLLLHKKSCTKNQLVLIVNESPASPAKTFPPGPSLNDPDDQMKDAANKADQEDCSDLSEPKGLDREESMEVEVPVATTTTTTTGGSGGSGGSTLSGVTNITTPSCHSGCSSGTSAITTSLPQLGDLTTLGNFSVINSNVIIENLQSTKVAVAQFSQEARCGGASGGKLLISTLMEQLLALQQQQIHQLQLIEQIRHQILLLASQSADLPAAPSIPSQGTLRTSANPLTTLSSHLSQQLAVAAGLAQSLASQSANISGVKQLPHVQLPQSSSGTSIVPPSGGTSPNMSIVTAAVPTPSSEKVASNAGASHVSSPAVSASSSPAFAISSLLSPESNPLLPQPTPANAVFPTPLPNIATTAEDLNSLSALAQQRKSKPPNVTAFEAKSTSDEAFFKHKCRFCAKVFGSDSALQIHLRSHTGERPFKCNICGNRFSTKGNLKVHFQRHKEKYPHIQMNPYPVPEHLDNVPTSTGIPYGMSIPSEKPVTSWLDTKPVLPTLTTSVGLPLPPTLPSLTPFIKTEEPAPIPISHSAASPQGSVKSDSGAPDLATRNPSGVPEEVEGSAVPPFGGKGEESNMASSAVPTAGNSTLNSPVADGGPGGTTFTNPLLPLMSEQFKAKFPFGGLLDSAQASETSKLQQLVENIDKKATDPNECIICHRVLSCQSALKMHYRTHTGERPFKCKICGRAFTTKGNLKTHYSVHRAMPPLRVQHSCPICQKKFTNAVVLQQHIRMHMGGQIPNTPVPDNYPESMESDTGSFDEKNFDDLDNFSDENMEECPEGSIPDTPKSADASQDSLSSSPLPLEMSSIAALENQMKMINAGLAEQLQASLKSVENGSMEGDVLTNDSSSVGGDMESQSAGSPAISESTSSMQALSPSNSTQEFHKSPGMEEKPQRVGPGEFANGLSPTPVNGGALDLTSSHAEKIIKEDSLGILFPFRDRGKFKNTACDICGKTFACQSALDIHYRSHTKERPFICTVCNRGFSTKGNLKQHMLTHQMRDLPSQLFEPSSNLGPNQNSAVIPANSLSSLIKTEVNGFVHVSPQDSKDAPTSHVPQGPLSSSATSPVLLPALPRRTPKQHYCNTCGKTFSSSSALQIHERTHTGEKPFACTICGRAFTTKGNLKVHMGTHMWNSTPARRGRRLSVDGPMTFLGGNPVKFPEMFQKDLAARSGSGDPSSFWNQYTAALSNGLAMKANEISVIQNGGIPPIPGSLGSGSSPISGLTGNVEKLGNSEPSAPLAGLEKMASSENGTNFRFTRFVEDSKEIVTS
Protein: Phorbol ester/diacylglycerol-binding protein unc-13 (Uncoordinated protein 13) (P27715)
Organism: Caenorhabditis elegans
Function: May form part of a signal transduction pathway, transducing the signal from diacylglycerol to effector functions. One such function could be the release of neurotransmitter from neurons. Probably by regulating neuronal transmission downstream of lin-3 and receptor lin-23 and phospholipase plc-3 and upstream of innexin unc-7 and egl-4/PKG in ALA neurons, involved in the decrease in pharyngeal pumping during the quiescent state that precedes each larval molt,.
Interaction partners:
- Rab-3-interacting molecule unc-10
- Liprin-alpha
- Syntaxin-1A homolog
- Acetylcholine regulator unc-18
- Variant SH3 domain protein
- Calcium-dependent secretion activator
- Ras-related protein Rab-3
- Synaptotagmin-1
- Vesicular acetylcholine transporter unc-17
- Synaptobrevin-1
Sequence:
MDDVGDYNDDQLSDGMSMRLLCITIKKARLQGAVDEFNSYVTVKLQTVKSTTVAVRGNLPCWEQEFIFETNRPDDGMVLELWAKGVLWDKLIGVHYMPLSEIRYSNAAGSGQWLQMDHELETRNGQTVGTRGPTGHNLLTDVRFELPFDVQGHDEDIQSRLLALNGLIEHDQLGPNNHHRAPFNHSGLSEDSDYTSDVSVPVNHHQLHPNSSAHQYESHLHPHRTRQLLHTREGAASYEDEEDAYHARHQPESDDYNHQDTYDQHSSYYNDEYAPSGSSSQYQRQGYQDQDQQHQNIYEDTVTPVREFGESAVPPAASSSRRQFDQVYGYASSSEERYDTPMSSGRLPRDEPILEHSEPEYVYDQNGYPEEDNYGINPTYSEDHFEGQTNDYSTTHQEPNDFRNDYNSSYQREYWNESEPLSYNSRPPNGHIRTGANTWREPSTSSRPTSSQAWNYQDDTHQYDEVDRGSRVSFTRTPSVDRTDRPSESGGGFYDEMSESGRPGRPDSHHNWRYDSIQEEDNEKDNWKQHVEGYEEGQEEKQKDNQKPNDHSAASPQDHYHRSDSTAQQDFGNNIVRQTIQEEEEKRNYQELWHNAYKRVCADLGIKSSQASLVATTGGTLLQNLFLYRPKLAPAGHGATASQFQSPAGATRFYANHNNNNNNVSKNELDSTTETPPDPSRTPSTSSMNPVPSLAVPMSPGPYLNSDPPSPVSPNPQIKRSIYRIKESYEDRNGGRERIYTTNLVSVYLEKMKPPDELEEGSSGSMRETQNEIKNGTQLHNAESNIFFPQDSVPKSISYNAGNLKNTSITTSKTSSAITNHSSLPPQPPSKPASRDSDPMKQLLTFSKSFKKVRRVRSAMPRRRKRKRVKIKKSRSCPILWKTEKTPHPMKSKSMTCIRIPKKTVIAPLRKEIKIVRMKPPAARCESDSKAHKKKNLLDVYKDMGKSTVLDGNGSSAANAFYKSIDAAPNMNVARTKTSIPLVSELVLKTMATKRAQAGLANAARTTFSDTELKTHVYKKTLQALIYPISATTPHNFATTTFQTPTFCYECEGLLWGLARQGLRCTQCQVKVHDKCRELLSADCLQRAAEKSTKHGEADRTQSLVNVIRDRMKIQEQNKPEVFQMIRTVFDVDENIQKETLKTVKASILEGSSKWSAKITLTVLCAQGLIAKDKTGKSDPYVTAQVGKTKRRTRTIHQELNPVWNEKFHFECHNSTDRIKVRVWDEDNDLKSKLRQKLTRESDDFLGQTVIEVRTLSGEMDVWYNLEKRTDKSAVSGAIRLHINVEIKGEEKLAPYHVQYTCLHEHLFAAHCVDEEVKLPKVRGEDSWKVCFQETGQEIAEEFAMRYGIESIYQAMTHFACLCTRYMCAGVPAVLSTLLANINAYYAHTTATSAVSAPDRFAASNFGKERFVKLLDQLHNSLRIDLSAYRNHFPSSSPAKLQDLKSTVDLLTSITFFRMKVLELASPPRASTVVRECAKACMQQTYQLMFESCAEQFPILDTSVQFWYEFIDYIMRVIEEDQKNYTPALNQFPQELNVGNLSAETLWSMYKNDLKMALEEHAQKKRCKTPEYMNLYFKVKGFYFKYVADLSTYKSSIPEFPAWFIPFVMDWLNENDEHSMDILRNAYNVDKADNFPQTSEHTKFSNSVVDVFTQLNAALKLLKQMDCPNPEVAADMMKRFSKTLNKVLLAYADMVQKDFPKFAHDEKLACILMNNVQQLRVQLEKIYETMGGAELDEHIGQVLTVLQKKLNSVLDRLSAEFVTTLEPHIHEQTIKLGMLLVKIKGPQLQKTQVQPEADAVLEPLMDLLEGSLRRYADQCEKTVLKYILKELWKITIVNMEKRVVLPPLSDKALLKQLPNAKIGDVTKLMSTNIQSIKGMNSVKDMMDMARESEKSLTPRQCTVLDCALDAIKDSFHASGKGLKKSFFEKSPELQSLKYALSLYTQTTEQLIKTFITSQRQQDLPSQEQPVGEVSVQVDLFSHPGTGEQKVTVKILAANDLRWQTSSAFKPFVEVHLVGPHLSDKKRKWSTKTKAGNWAPKFNETFHFFLGNEGEPEHYELMFQVKDYCFARDDRVVGVGVLQLSSVVDQAGSCAMWVQLGTRLHIDETGLILLRILSQRQTDEVAKDFVRLKTECRYETETVMAASASSQNINRT
Protein: Sesquiterpene synthase 2 (TsTPS2) (Alpha-humulene synthase TPS2) (EC 4.2.3.104) (Alpha-selinene synthase TPS2) (EC 4.2.3.198) (Beta-elemene synthase TPS2) (EC 4.2.3.-) (Delta-cadinene synthase TPS2) (EC 4.2.3.-) (I7H727)
Organism: Toona sinensis (Chinese mahogany) (Cedrela sinensis)
Function: Sesquiterpene synthase involved in the biosynthesis of volatile compounds known for their medicinal efficacy for treating enteritis, dysentery, itch and some cancers. Mediates the conversion of (2E,6E)-farnesyl diphosphate (FPP) into beta-elemene, alpha-humulene, delta-cadinene and alpha-selinene.
Interaction partners:
Sequence:
MSVPVSQIPSLKAKGVIMRRNANYHPNIWGDRFINYVPVDKMNHTCHLQAIEELKDAVRRELLTATGLSQLNLIDAIQRLGVGYHFERELEEALQHVYHKNHYHDDTEDNLYSISLRFRLLRQHGYYVSCDILNKFKDEKDNFKESLTTDVPGMLSLYEAAHPGVHGEDILDEAIAFTTTHLKSLAIDHLRNPSLASQVIHALRQPLHRGVPRLENRRYISIYQDEVSHNKALVKLFKLDFNLVQSLHKKELSEISRWWKELDLANKLPFARDRLVECYFWIIGVYYEPQYSLARKILTKTIAMGSIIDDIYDVYGTPEELNLFTDAIERWDASCMDQLPEYMQIFYEALLDLYNEIEKEIAKEGWSYRVHYAKEAMKILARGYHDESKWFHNNYIPTMEEYMHVALVTSGYTMLTTSSFLGMDNIVTKETFDWVFSGPKIIRASGTIARLMDDVKSHKFEQERGHAASAVECYMEQHGVSEQEVCKEFYQQVGNAWKDINQDFLKPTDVPMTILMRVLNLARVIDVVYKEGDGYTHVGKVMKENVASLLIDPIPV
Protein: Hepatic triacylglycerol lipase (HL) (Hepatic lipase) (EC 3.1.1.3) (Lipase member C) (Lysophospholipase) (EC 3.1.1.5) (Phospholipase A1) (EC 3.1.1.32) (O46559)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Catalyzes the hydrolysis of triglycerides and phospholipids present in circulating plasma lipoproteins, including chylomicrons, intermediate density lipoproteins (IDL), low density lipoproteins (LDL) of large size and high density lipoproteins (HDL), releasing free fatty acids (FFA) and smaller lipoprotein particles. Also exhibits lysophospholipase activity (By similarity). Can hydrolyze both neutral lipid and phospholipid substrates but shows a greater binding affinity for neutral lipid substrates than phospholipid substrates (By similarity). In native LDL, preferentially hydrolyzes the phosphatidylcholine species containing polyunsaturated fatty acids at sn-2 position (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P11150}.
Interaction partners:
- Apolipoprotein B
- Triacylglycerol lipase
- triacylglycerol lipase
- Lipase
- Monoglyceride lipase
- Lipoprotein lipase
- Triacylglycerol lipase
- Phosphatidic acid phosphatase type 2/haloperoxidase domain-containing protein
- Triacylglycerol lipase
- Cholesteryl ester transfer protein
Sequence:
MGSPLCVPIFLAVCILIQSSTHGQSLRPEPFGRRARVTATKKTLLETETRFLLFKDKANKGCQIRLHHADTLQECGFNSSLPLVMIVHGWSVDGLLESWIWQMVAALKSQPARPVNVGLVDWISLAHSHYAVAVRNARLVGQEVAALLQWLEESAPFSRSNVHLIGYSLGAHVAGFAGSYISGKHKIGRITGLDAAGPLFEGTSASDRLSPDDATFVDAIHTFTREHMGLSVGIKQPVGHYDFYPNGGSFQPGCHFLELYKHIAQHGLNALSQTIKCAHERSVHLFIDSLLHPSMQSTAYQCSDMDSFSQGLCLGCTKGRCNTLGYHIRQEPLSKGKRLFLVTQAQSPFRVYHYQFKIQFINQIEKPLEPTFTMSLLGTKEEMQKIPITLGEGITSNKTYSFLITLNLDIGELMVIKFKWENSAVWANVWNTVQTIIPWGIKPRNSGLILKTIRVKAGETQQRMTFCSENMDDLQLHPTQEKNFVRCEVNPKKLKLKIK
Protein: Chemokine-like protein MC148 (Q98314)
Organism: Molluscum contagiosum virus subtype 1 (MOCV) (MCVI)
Function: Plays a role in antagonizing the chemotaxis of multiple leukocyte subsets induced by CC and CXC chemokines. Displaces the interaction between CXCL12 and CXCR4 and thereby inactivates the antiviral activity of host CXCL12.
Interaction partners:
Sequence:
MRGGDVFASVVLMLLLALPRPGVSLARRKCCLNPTNRPIPNPLLQDLSRVDYQAIGHDCGREAFRVTLQDGRQGCVSVGNKSLLDWLRGHKDLCPQIWSGCESL
Protein: Lysophosphatidylcholine acyltransferase 2 (LPC acyltransferase 2) (LPCAT-2) (LysoPC acyltransferase 2) (EC 2.3.1.23) (1-acylglycerol-3-phosphate O-acyltransferase 11) (1-AGP acyltransferase 11) (1-AGPAT 11) (EC 2.3.1.51) (1-acylglycerophosphocholine O-acyltransferase) (1-alkenylglycerophosphocholine O-acyltransferase) (EC 2.3.1.25) (1-alkylglycerophosphocholine O-acetyltransferase) (EC 2.3.1.67) (Acetyl-CoA:lyso-platelet-activating factor acetyltransferase) (Acetyl-CoA:lyso-PAF acetyltransferase) (Lyso-PAF acetyltransferase) (LysoPAFAT) (Acyltransferase-like 1) (Q8BYI6)
Organism: Mus musculus (Mouse)
Function: Exhibits both acyltransferase and acetyltransferase activities. Activity is calcium-dependent. Catalyzes the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC). Catalyzes the conversion 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone (By similarity). Involved in platelet-activating factor (PAF) biosynthesis by catalyzing the conversion of the PAF precursor, 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF) into 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine (PAF). Also converts lyso-PAF to 1-O-alkyl-2-acyl-sn-glycero-3-phosphocholine (PC), a major component of cell membranes and a PAF precursor. Under resting conditions, acyltransferase activity is preferred. Upon acute inflammatory stimulus, acetyltransferase activity is enhanced and PAF synthesis increases. Involved in the regulation of lipid droplet number and size (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17182612}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q7L5N7}. Golgi apparatus membrane {ECO:0000269|PubMed:17182612}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q7L5N7}. Cell membrane {ECO:0000305|PubMed:18156367}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q7L5N7}. Lipid droplet {ECO:0000250|UniProtKB:Q7L5N7}.
Interaction partners:
- Platelet-activating factor acetylhydrolase
- Choline/ethanolaminephosphotransferase 1
- Cholinephosphotransferase 1
- Lysocardiolipin acyltransferase 1
- Acyl-CoA:lysophosphatidylglycerol acyltransferase 1
- Platelet-activating factor acetylhydrolase 2, cytoplasmic
- Cardiolipin synthase
- Phosphatidylethanolamine N-methyltransferase
- Lysophospholipid acyltransferase LPCAT4
- Platelet-activating factor acetylhydrolase IB subunit alpha1
Sequence:
MNRCAEAAAVAATVPGSGVGDAGLRPPMVPRQASFFPPPVPNPFVQQTTISASRRLQMFLLGIILLPVRALLVGIILLLAWPFAVISTACCPEKLTHPISNWRRKITRPALTFLARAMFFSMGFTVTVKGKVASPLEAPIFVVAPHSTFFDGIACVVAGLPSLVSRNENAQTPLVGRLLRALQPVLVSRVDPDSRKNTINEIKKRATSGGEWPQILVFPEGTCTNRSCLITFKPGAFIPGVPVQPVLLRYPNKLDTVTWTWQGYTFLQLCVLTFCQLFTKVEIEFMPVQAPSEEEKNDPVLFASRIRNLMAEALEIPVTDHTYEDCRLMISAGQLTLPMEAGLVEFSKISRKLKLDWDGIRKHLDEYASIASSSKGGRIGIEEFAEYLKLPVSDVLRQLFALFDRNNDGSIDFREYVIGLAVLCNPANTEEIIQVAFKLFDVDEDGYITEEEFCTILQASLGVPDLNVSGLFREIAQRDSVSYEEFKSFALKHPEYAKIFTTYLDLQTCHVFSLPEEVQTAPSVASNKVSPESQEEGTSDKKVD
Protein: Outer envelope pore protein 16, chloroplastic (Chloroplastic outer envelope pore protein of 16 kDa) (Q41050)
Organism: Pisum sativum (Garden pea) (Lathyrus oleraceus)
Function: Voltage-dependent high-conductance channel with a slight cation-selectivity; selective for amino acids but excludes triosephosphates or uncharged sugars. Non-essential amino acid-selective channel protein and translocation pore for NADPH:protochlorophyllide oxidoreductase A (PORA) and possibly PORB.
Subcellular location: Plastid, chloroplast outer membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Plastid, etioplast membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MPRSSFSGSLSSPKLDVVIDMGNPFLNLTVDGFLKIGAVAATRSVAEDTFHIIRKGSISSNDFEKSLKKMCKEGAYWGAIAGVYVGMEYGVERIRGTRDWKNAMFGGAVTGALVSAASNNKKDKIAVDAITGAAIATAAEFINYLT
Protein: UDP-D-xylose:L-fucose alpha-1,3-D-xylosyltransferase (EC 2.4.2.-) (Rhamnogalacturonan xylosyltransferase 2) (Q9ZSJ0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the transfer of D-xylose from UDP-alpha-D-xylose onto L-fucose. Probably involved in the biosynthesis of rhamnogalacturonan II (RG-II) through xylosylation of the internal fucose moiety of the A-chain of RG-II, a structurally complex pectic polysaccharide of the primary cell wall. RG-II is essential for the cell wall integrity of rapidly growing tissues such as roots and pollen tube growth and elongation.
Subcellular location: Golgi apparatus membrane {ECO:0000305|PubMed:17056709}; Single-pass type II membrane protein {ECO:0000305|PubMed:17056709}.
Interaction partners:
- Guanine nucleotide-binding protein subunit beta
- AUGMIN subunit 6
- Xylogalacturonan beta-1,3-xylosyltransferase
- Probable arabinosyltransferase ARAD1
- Xyloglucan 6-xylosyltransferase 1
- Xyloglucan galactosyltransferase MUR3
- Probable pectin methylesterase CGR3
- Polygalacturonate 4-alpha-galacturonosyltransferase
- Xyloglucan glycosyltransferase 4
- GDP-mannose 4,6 dehydratase 2
Sequence:
MAQKQQTLHQQRPFSSSPRSYSSISNRPIFLLSRNGLLLVLLALFLLLGVFLPWPGSPLLLFPNKVSSPSYASSLSPHAKSEWRNYTLAQAAKFVATNGTVIVCAVSSPFLPFLNNWLISVSRQKHQEKVLVIAEDYITLYKVNEKWPGHAVLIPPALDSKTAYSFGSQGFFNFTARRPQHLLQILELGYNVMYNDVDMVWLQDPFQYLEGSHDAYFTDDMPQIKPLNHSHDLPAPDQNGETYICSCMIYLRPTNGAKLLMKKWSEELQSQAWSESIRFKANDQPAFNLALNKTAHQVDLYLLSQVAFPTGGLYFNDAAWVKETKGKHVIVHNNYIIGYDRKMRRFQDYGLWLVDDHALESPLGKLQ
Protein: AT3g23700/MYM9_3 (Nucleic acid-binding proteins superfamily) (Q9LK47)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Uncharacterized protein At3g06530
- Nucleolar protein
- Nucleolar-like protein
- F18K10.11 protein
- KRR1 small subunit processome component
- P-loop containing nucleoside triphosphate hydrolases superfamily protein
- Protein NUCLEOLAR COMPLEX ASSOCIATED 4
- Periodic tryptophan protein 2
- Putative WD-repeat membrane protein
- Ribosomal RNA-processing 7 protein
Sequence:
MAVFSGATTLGSVSFASHLFDQQSTFLSCPLRLLPSSSSSSSNRNSLVCIVKSFSSSATADTDRNSDQSASSSVLSASNSLLRDTSDEASAAGPSDWKTAKAYCKSGDTFEGEVQGFNGGGLLIRFHSLVGFLPYPQLSPSRSCKEPQKSIHEIAKTLVGSKLPVKVVQADEENRKLILSEKLALWPKYSQNVNVGDVFNGRVGSVEDYGAFIHLRFDDGLYHLTGLVHVSEVSWDYVQDVRDVLRDGDEVRVIVTNIDKEKSRITLSIKQLEDDPLLETLDKVILKDSSTGSPSLSSNNGDTIEPLPGLETILEELLKEDGIEAVKINRQGFEKRVVSQDLQLWLSNTPPSDGKFVLLARAGRQVQEIHLTTSLEQGGIKKALQHVLERVP