wanglab/gogpt-training-data huggingface dataset:
Protein: Protostadienol synthase helA (EC 5.4.99.32) (Helvolic acid biosynthesis cluster protein A) (Oxidosqualene cyclase) (Oxidosqualene:protostadienol cyclase) (OSPC) (Q4WR16)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Protostadienol synthase; part of the gene cluster that mediates the biosynthesis of helvolic acid, an antibacterial nortriterpenoid. Protostadienol synthase helA cyclizes (3S)-oxidosqualene to (17Z)-protosta-17(20),24-dien-3-beta-ol (protostadienol). The synthesis of protostadienol is followed by several steps of monooxygenation, dehydrogenation, and acyl transfer to yield the final helvolic acid. Following the cyclization to the tetracyclic protostadienol by helA, cytochrome P450 monooxygenases helB1-mediated and helB2-mediated oxidation at C-4 and C-16, acyltransferase helD2-dependent acetylation of 16-OH, oxidation of C-21 by cytochrome P450 monooxygenase helB4, and short chain dehydrogenase helC-dependent oxidative decarboxylation yield the fusidane skeleton. This intermediate is further modified in three additional steps mediated by the cytochrome P450 monooxygenase helB3, the acyltransferase helD1, and the 3-ketosteroid 1-dehydrogenase helE to give helvolic acid. Compared with the late stages in the biosynthesis of helvolic acid, enzymes involved in the early stage modifications act in a relatively strict order. The hydroxylation of C-16 by helB1 and subsequent acetylation by helD2 should occur before the helB3-mediated oxidation of C-21. C-4 demethylation in fusidane-type antibiotics proceeds in an unusual manner though it is also achieved by oxidative decarboxylation. The methyl group at C-4 beta position is oxidized by helB1 and subsequently removed by the short chain dehydrogenase helC.
Interaction partners:
- Squalene epoxidase erg1
- Cytochrome P450 monooxygenase helB1
- Sterol 14-alpha demethylase cyp51A
- Sterol 14-alpha demethylase cyp51B
- 3-keto-steroid reductase erg27
Sequence:
MATDSSMPGTVIGKAEFSDTKAASEFGTDLSRWRLNVDNGRHMWEYLESEDEARKRPQSFLEKYWLGLPYELPARPRATCALEAVENGWEFFKRLQTADGHWGCNDDGPLFVTSGMVIARYIVGIPIDSHMKQEMCRYLLNVVNEDGGWGLFIQSPSTVFGTVMNYCMLRILGLGPEHPAMAKARNTLHRLGSARATPTWGKFWLCVLGVYEWEGMVPLPPEPLLVPASLPFNPGKWWVHTRNVYISMSYLYGHRFSMPPNKLVQALRDELYDIPYQQINWPAQRTNVSAADRLTDPTWIQRSFTSALTMYETFKIPFLRRRALNEALFQIETETRNTHYLCIAPVSFASNMLALYHAHGRDSHWIRGMRDRFIDPMWLCREGLAASGTNGTSLWDTALTVQATIDAGLAARPENQAILRKALEFIDNSQIREDPLGVHHVYRQPTRGAWPFSTRDQSYAVSDTTAEAVKVIVLLQRIEGFPSRISDERLQQAIDLILGMENAGGGFSAYEPVRGPKFLELLNITELYENVMTDNLYPECTSSVIMCLTTFAREYPTYRPRDIQACLSRSIDYLLRSQYPNGGWFASWGVCFTYATMFALQGLACMGWNESNCAACQRACSFLLQHQNPDGGWGESLDTVRFKQYLPHPDGSQVTNTAYAVIGLLAARCGNHEAIRRGVAYLVKEQQDTGEWLPGPLEGVFAPPGGMRYPNYKFHFTLMALGRYVAIHGNECLAI
Protein: SMP-LTD domain-containing protein (Q869R5)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- SMP-LTD domain-containing protein
- Bacterial surface antigen
- Casein kinase II subunit beta
- Cysteine proteinase 4
- Reticulon-like protein
Sequence:
MSFKLSWGGFDEKFYETLKTSLNTTLNSGPPIPNITDKLLVHNIHLGDIAPNIQLLEVDPSINRLKFVFKIKYNGNGLLELRTMVQANPIYMATTITSSKQERELIKRLKFGSAANPHIVPLSITIRDIEFDGVLSVSILNNDNNNNNNNNNNNNNNIAGSAGGSSSSSSSSNNNNNSNNSNNSNNNNGGGKIEAFFTEDPLKKVNIVTSFDDFPAAAKFVSTLVEGQLRDFITKEFPTIVGSITIPVGPTAVVPTSTSNEITLLPTTTTTTTTTTTTTTTNNNNIISIDNNTNNSNNNNNSPNISTSTSTSSSPQLSFDGSNNSSINSSPQLISITPLPISPLLENNISFDNPFEKQNKKGFIN
Protein: Carboxylic ester hydrolase (EC 3.1.1.-) (G5EC03)
Organism: Caenorhabditis elegans
Interaction partners:
- Uncharacterized protein ZC84.1
- BPTI/Kunitz inhibitor domain-containing protein
- BPTI/Kunitz inhibitor domain-containing protein
- Acyl-CoA synthetase 7
- C-type LECtin
- C-type LECtin
Sequence:
MHTLHVLYYILFVFTLNGSGQRIISTTYGKLEGKTVNVDQHMFKNVPFAKPPLGKLRFSLPEWTNPWKNIRNATEYSPSCFSNSSMRTDSNFFPMSEDCLYLNVFTNEYCLKSKNCSTVVYYHGGGINMDSAVQFNDTFILERYVKENVVFIIPAYRLGIFGLLYFGSNNLVPQNLAIHDCELALRFIHQEISNFGGHKDDINLMGHSAGAHISLIFGFSRHIDPDHKLINRIIVLSPVPSYDMPELLIKNCYDFAERVGCYKRNVTARDTEIVKCLRKKDARGLMSMQRLMENDRLYFWNFLAGEPFMYRDESIADFKEYAVKRDMLIGNTVDEVKWKRLKKENPAIAGSFMDWENPYEVAHKFNFYHDSAPVNSTYESFTQGIFVSTATYAEAQANAGGTVYLFQSNQQPSSHVSDMQYFVGTHREDYHTSDMDIMDTFYSKMIVNFTKFGSPSPVWEPLVPSRMNYYALEVNTEKGIWPRMEEDFHESDVNFWFINMTAFDREVTRQKKTSNGTSLTWSPMHPGPVILPTKTNESSSFDISSQWWFFAIIVVVALILFYLIYVLKRAILKHKEPQDDDETTTLFK
Protein: GHMYB9 (Myb-related protein 308-like) (Q9ATD1)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGRSPCCEKAHTNKGAWTKEEDDRLIAYIRAHGEGCWRSLPKAAGLLRCGKSCRLRWINYLRPDLKRGNFTEEEDELIIKLHSLLGNKWSLIAGRLPGRTDNEIKNYWNTHIRRKLLSRGIDPATHRPLNEASQDVTTISFSGAKEEKEKINTNSNNNPIGFITKDEKKIPVQERCPDLNLDLRISPPYYQQTQPESFKTGGRTLCFICSLGVKNSKDCTCSTITTAAGSSSSSSSHSNSNNSSGYDFLGLKSGILEYRSLEMK
Protein: Rho GTPase activating protein 32 (A0A8I6GIC6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MKSSIHSEEDDFVPELHRNVHPRERPDWEETLSAMARGADVPEIPGDLTLKSCGSTASMKVKHVKKSTPPGLMGCDNIHRLPFTKGHFPKMAECAHFHYENVEFGSIQLSLSEEQNEIMKNGCESKELVYLVQIACQGKSWIVKRSYEDFRVLDKHLHLCIYDRRFSQLSELPRSDILKDSPESVTQMLAAYLSRLSTIAGNKINCGPALTWMEIDNKGNHLLVHEESSINTPAVGAAHVIKRYTARAPDELTLEVGDIVSVIDMPPKVLSTWWRGKHGFQVGLFPGHCVELINQKVPQSVTNSVPKPVSKKHGKLITFLRTFMKSRPTKQKLKQRGILKERVFGCDLGEHLLNSGFEVPQVLQSCTAFIERYGIVDGIYRLSGVASNIQRLRHEFDSEHVPDLTKEPYVQDIHSVGSLCKLYFRELPNPLLTYQLYEKFSDAVSAATDEERLIKIHDVIQQLPPPHYRTLEFLMRHLSLLADYCSITNMHAKNLAIVWAPNLLRSKQIESACFSGTAAFMEVRIQSVVVEFILNHVDVLFSGKISAVMQEGAASLTRPKSLLVSSPSTKLLTLEEAQARTQAQVNSPIVTENKYIEVGEGPAALQGKFHTIIEFPLERKRPQNKMKKSPVGSWRSFFNLGKSSSVSKRKLQRNESEPSEMKAMALKGGRAEGTLRSAKSEESLTSLHAVDGDSKLFRPRRPRSSSDALSASFNGEVLGNRCNSYDNLPHDNESEEEVGLLHIPALVSPHSAEDVDLSPPDIGVASLDFDPMSFQCSPPKAESECLESGASFLDSLGFTRDKLGASKKDVEAGGSQSQTPGSTASSEPVSPVQEKLSPFFTLDLSPTEDKSSKPSSFTEKVVYAFSPKIGRKLSKSPSMNISEPISVTLPPRVSEVIGTVSNTVSQNASPPSWDKSVEERDVINRSPTQLGKMKPGEREAQERCEPEAQPQEQGAAEEVELPGTEERPVSSSQSKAVPSGQSQTGAVTHDPPQDPVPVSSVSLIPPPPPPKNVARMLALALAESAQQASTQTLKRPGPSQAGCTSYGDMAVATSEEKLPSSYSSVTLDKTYFQTDRPAEQFHLQINGLGNCDQPLPETAAMGGPTHPNTTDSGEQLHQVDLIGNSLHRNHLSGDPEKARSTSAPLADSEKSDGHGSFPEDHAGKTSVSTVSFVGQGQSPLHFSSGDQPLSYLGTSMDKPHHSSELTEKSPMPSTLPRDKAHPLSGSPEENTSTATMAYMMTTPPRAETSTREASRAMAEQPTAADFVAATLQRAHRTNRPLPPPPSQRPTEQPPGVGQVQEAPSIGVNNSHKQVQGAAPAPERPPEPRAMADPAPIFVSDGSAAAQCPMAISAAQPGLPEKVRESSRAPPLHLRAETFPGHSCGFAAPVPPTRTVESKMAAAMHSSAAEANNSSNYHSFVPSSASADDVLPLPPPIAQPKHASQKIAYSSFARPDVTTEPFGPENCLHFNMTPNCQFRPQSVPPHHNKLEPHQVYGTRSEPPASMGPRYNTYVAPGRSMSGHHSKPCSRVEYVSSLGSSVRNPCCPEDILPYPTIRRVQSLHAPPPSMIRSVPISRTEVPPDDEPAYCPRPVYQYKPYQSSQARSDYHVTQLQPYFENGRVHYRYSPYSSSSSSYYSPDGALCDVDAYGTVQLRPLHRLSNRDFAFYNPRLQGKNAYNYAALPPRPRASATGYFSSNDHNVVNMPPTADVKHTYTSWDLEDMEKYRMQSIRRESRARQKVKGPIMSQYDNMAPAVQDDLGGIYVIHLRSKSDPGKTGLLSVAEGKEGRHPAKAVSPEGDERFYRKHPESEFDRAHHHGGYGSQQVEKPSLPQKQSSLRNRKLHDMGCSLPEHRAHQEASHRQLCESKNGPPYPQGAGQLDYGSKGMPDASEPNSYHNSGKYVTSGQESLRLNHKEVRLSKDVDRPRARQPPAPEKHSRDCYKEEEHFTQSVVPPPKPERSHSLKLHHTQNLERDPSMLYPYQTHSKRQSSVTVVSQYDNLEDYHSLPQHQRGGFGGGGMGAYVPSGFVHPQSRTYATALGQGAFLPTELSLPHPDTQIHAE
Protein: Ras-related protein SEC4 (Suppressor of RHO3 protein 6) (P07560)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in exocytosis. Maybe by regulating the binding and fusion of secretory vesicles with the cell surface. The GTP-bound form of SEC4 may interact with an effector, thereby stimulating its activity and leading to exocytotic fusion. SEC4 may be an upstream activator of the 19.5S SEC8/SEC15 particle. SEC4 probably interacts directly with SEC8; it could serve as the attachment site for the SEC8/SEC15 particle.
Subcellular location: Cytoplasmic vesicle, secretory vesicle membrane; Lipid-anchor; Cytoplasmic side. Cell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasm. Note=A small fraction is soluble.
Interaction partners:
- Myosin-2
- Rab guanine nucleotide exchange factor SEC2
- Exocyst complex component SEC15
- Rab GDP-dissociation inhibitor
- GTP-binding protein YPT1
- Vacuolar protein sorting-associated protein 16
- Exocyst complex component SEC6
- Protein transport protein SEC9
- Exocyst complex component SEC3
- Lethal
Sequence:
MSGLRTVSASSGNGKSYDSIMKILLIGDSGVGKSCLLVRFVEDKFNPSFITTIGIDFKIKTVDINGKKVKLQLWDTAGQERFRTITTAYYRGAMGIILVYDVTDERTFTNIKQWFKTVNEHANDEAQLLLVGNKSDMETRVVTADQGEALAKELGIPFIESSAKNDDNVNEIFFTLAKLIQEKIDSNKLVGVGNGKEGNISINSGSGNSSKSNCC
Protein: Endoribonuclease ToxN (EC 3.1.-.-) (Toxin ToxN) (Q3YN09)
Organism: Bacillus thuringiensis subsp. kurstaki
Function: Toxic component of a type III toxin-antitoxin (TA) system. An endoribonuclease which cleaves between the first and second A of AAAAA sequences; it tolerates other nucleotides in positions +2 and +4 of the consensus. Digests cognate antitoxin RNA ToxI as shown by the 2'-3'-cyclic phosphate at the 3' end of the 34-nt repeats and probably other RNAs. Inhibits growth when expressed in E.coli without causing cell lysis; this bacteriostatic effect is neutralized by cognate RNA antitoxin ToxI, which has 2.9 nearly identical 34 nucleotide-long repeats. Non-cognate antitoxin RNA from P.atrosepticum does not inhibit this toxin. The toxin-antitoxin pair function in plasmid maintenance (a plasmid addiction system), but unlike its P.atrosepticum homolog it is not seen to confer resistance to bacteriophages.
Interaction partners:
Sequence:
MTNKDNPKFHTISTEYIDYLREADSKVPFNKDEQHSRPYVGVLEKINGHDYFVPLTSRNDKNFNSQVSVKLFDNDEKRIGVLLVNNMIPVPEKECKEIDIAEKTAADPQYGNLMLKQYLFLKENMDRVTNKVEKVYKDVTVQGKPSHKQKFLKGVCCDFPKLEEKCQEYKERDQAKERDKARRIAYMRQMGRER
Protein: Allantoate amidohydrolase (AAH) (EC 3.5.3.9) (Allantoate deiminase) (O32149)
Organism: Bacillus subtilis (strain 168)
Function: Involved in the anaerobic nitrogen utilization via the assimilation of allantoin. Catalyzes specifically the hydrolysis of allantoate to yield CO2, NH3 and S-ureidoglycine, which is unstable and readily undergoes a second deamination by S-ureidoglycine aminohydrolase AllE to yield S-ureidoglycolate and NH3 (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P77425}.
Interaction partners:
- Allantoinase
- Uric acid degradation bifunctional protein PucL
- (S)-ureidoglycine--glyoxylate transaminase (UGXT) ((S)-ureidoglycine--glyoxylate aminotransferase) (Purine catabolism protein PucG)
- Probable xanthine dehydrogenase subunit C
- 5-hydroxyisourate hydrolase
- Probable xanthine dehydrogenase subunit D
- Allantoin permease
- Purine catabolism regulatory protein
- Probable xanthine dehydrogenase subunit E
- Uric acid permease PucJ
Sequence:
MEKQKLSVKNSITDYIEWLAQYGASADGGVTRLLYTKEWMDAQLAVKTEMSSFGLETRFDDVGNVFGRLSGTQSPDEVIVTGSHIDTVINGGKYDGAYGVLAAMLALKQLKETYGAPKKTLEAVSLCEEEGSRFPMTYWGSGNMTGVFSEQDAKEPRDESGVSLQTAMHESGFGKGVFQSAYRTDISAFVELHIEQGKTLEMSGRDLGIVTSIAGQRRYLVTLEGECNHAGTTSMKWRKDPLAASSRIIHELLLRSDELPDELRLTCGKITAEPNVANVIPGRVQFSIDIRHQHQHVLEQFHQDMVALINGICLQKGIRAVIDEYMRIEPVPMDERLKAAAFETALENGFSCEEMVSGAGHDAQMIGRRYPACMLFVPSRGGVSHSPKEYTSARQLEIGVRALTDLLYKLAY
Protein: Histone H3 K4-specific methyltransferase SET7/9 family protein (Putative phosphatidylinositol-4-phosphate 5-kinase) (T26F17.15) (Q9SFE3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At2g39980/T28M21.14
- F21B7.2
- PR5-like receptor kinase
- ENTH/VHS family protein
- Clathrin interactor EPSIN 3
- Two pore calcium channel protein 1
- Clathrin interactor EPSIN 1
- Clathrin interactor EPSIN 2
Sequence:
MEKQAKLTRTQSSLLRSSSNLRSSYQSLSSIVEGEQDLEAGEKEEKQRRKPPKPFGSPNPKTGLTRINPGLAFTMVSLSFLSLSSFFFFVVFSQTDEILTSENLLLALIFVAVALFFASKNISLLNQTVIAIKNLGFQNRDSKSKPVQWYIGDDSKPEKKVIKRFVKEGVQFYSNGDFYEGEFNKGKCNGSGVYYYFVRGRYEGDWLDGRYDGHGIESWARGSRYKGQYRQGLRHGFGVYRFYTGDCYAGEWFNGQSHGFGVQSCSDGSSYLGESRFGVKHGLGSYHFRNGDKYAGEYFGDKIHGFGVYRFANGHCYEGAWHEGRKQGFGAYSFRNGDAKSGEWDSGVLVTSLPLTSEPVSRAVQAARETANKAVNRRRVDEQVSRAVAAANKAATAARVAAVRAVQNQMDGKFCQS
Protein: 3-oxoacyl-(Acyl-carrier-protein) reductase (EC 1.1.1.100) (O53665)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MAPKRSSDLFSQVVNSGPGSFLARQLGVPQPETLRRYRAGEPPLTGSLLIGGAGRVVEPLRAALEKDYDLVGNNLGGRWADSFGGLVFDATGITEPAGLKGLHEFFTPVLRNLGRCGRVVVVGGTPEAAASTNERIAQRALEGFTRSLGKELRRGATTALVYLSPDAKPAATGLESTMRFLLSAKSAYVDGQVFSVGADDSTPPADWEKPLDGKVAIVTGAARGIGATIAEVFARDGAHVVAIDVESAAENLAETASKVGGTALWLDVTADDAVDKISEHLRDHHGGKADILVNNAGITRDKLLANMDDARWDAVLAVNLLAPLRLTEGLVGNGSIGEGGRVIGLSSIAGIAGNRGQTNYATTKAGMIGITQALAPGLAAKGITINAVAPGFIETQMTAAIPLATREVGRRLNSLLQGGQPVDVAEAIAYFASPASNAVTGNVIRVCGQAMIGA
Protein: Protein DEHYDRATION-INDUCED 19 homolog 7 (AtDi19-7) (Protein HYPERSENSITIVE TO RED AND BLUE 1) (Q9FJ17)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in both red and blue light signaling.
Subcellular location: Nucleus {ECO:0000269|PubMed:15705950, ECO:0000269|PubMed:16786289}.
Interaction partners:
- Serine/threonine-protein phosphatase 7
- Apoptosis inhibitory protein 5
- RNA binding
- Small ribosomal subunit protein mS86
- RNA-binding
- DNA repair metallo-beta-lactamase family protein
- Flavin mononucleotide hydrolase 1, chloroplatic
- Sm-like protein LSM6A
- Cysteine proteinase inhibitor 2
- At1g78070/F28K19_28
Sequence:
MDSNSWINCPPVFSSSPSSRRYQSRSDLYLGDVEGEDDLKAEFMCPFCADEFDIVGLCCHIDVNHPVEAKNGVCPVCTKKVGLDIVGHITTQHGNVFKVQRRRRLRKGGYSSTYLTLKKELREANLQSLGGSSTFIPSSNIDSDPLLSSFMFKPPSAIPITEGDSVAQVSPKDTSKSKIQQESFSNEDQEKAKKSKFVRGLLWSTMLEDKF
Protein: exo-alpha-sialidase (EC 3.2.1.18) (I3ITP7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MIDNMASKSYPEAQRPPPARTVLFQQKDGKTYRIPALIYISDGQTFLAFAEERSTPRDSDAKVLVMRKGSLHNGSLQWTSAQTLTSACLPDHRTMNPCPVYERKSKTIYLFFICISGNTTEYHQIAMGRNRARLCYITSADYGETWSELTDLTNSVIGDEIHNWATFAVGPGHGIQMKSGRLIIPAYVYYVHCRCFPFNFPLIVRPHALSFYSDDCGVTWQMGGKIQMKSCECEMAEIIDHADQSHLYCNARSTCGYRIEALSETSGAAFDNPHVARKLVEPRHGCQGSVLSFPVPQPLDEEEKKATDCLTQSDSKTWLLYSHPTNKKKRKDLGVYLNKSPLNASGWSRPWIIYKGPSGYSDLTQCEERFGCLMECGEKSEIEGIAFVEFKLNDLLCS
Protein: Mesencephalic astrocyte-derived neurotrophic factor homolog (DmMANF) (MANF/CDNF-like protein) (Q9XZ63)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required during the maturation of the embryonic nervous system for maintenance of neuronal and cuticular connectivity. Essential for maintenance of dopaminergic neurons and dopamine levels.
Subcellular location: Secreted {ECO:0000269|PubMed:19164766}.
Interaction partners:
- Endoplasmic reticulum chaperone BiP
- X-box-binding protein 1
- DnaJ homolog shv
- BcDNA.GH08312
- ER lumen protein-retaining receptor
- Ubiquitin-conjugating enzyme E2 N
- Calreticulin
- AT16033p
- Hypoxia up-regulated protein 1
Sequence:
MKTWYMVVVIGFLATLAQTSLALKEEDCEVCVKTVRRFADSLDDSTKKDYKQIETAFKKFCKAQKNKEHRFCYYLGGLEESATGILNELSKPLSWSMPAEKICEKLKKKDAQICDLRYEKQIDLNSVDLKKLKVRDLKKILNDWDESCDGCLEKGDFIKRIEELKPKYSRSEL
Protein: Calmodulin-5 (CaM-5) (Q682T9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
Interaction partners:
- IQ domain-containing protein IQM1
- Late embryogenesis abundant
- Probable calcium-binding protein CML48
Sequence:
MADQLTDDQISEFKEAFSLFDKDGDGCITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLNLMARKMKDTDSEEELKEAFRVFDKDQNGFISAAELRHVMTNLGEKLTDEEVDEMIKEADVDGDGQINYEEFVKVMMAK
Protein: Nuclear protein EAST (Q9NGR9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGPNHCDSNWTQSASDRREQQEVVEQQARRRRGSGHHRSSNVGSSSQGPSRMSSRKVPGGSGGADESTAATAPLDDNANASVEIPASSEEPAMGVGEEMSIISKTRTSTLSVEPAKEPTVTAELEGEKELESNPVSKTPRSTPTPTLTPAVTPTASDGVAAKSVRVTRHSSPLLQIISPTTSRREVGDGELDTEEPTGSGGQRKSSVERSLAPVIRGRKSIKDLKEAKEVKSEEPPAAASESRAASGVTPGQVKEQHDADGNEMESLPITDKKDHKDTKDKGDERETNQEEEKEKSADTEIIADTEKTSEKQKYTEKDKAADKDGGKEKDIDANKDIDKEKEKVKEVLPPVVPIAPVTPTCNRVTRKFTLPRSRRLTTRVTSQFVASPLPVGANSTASLVAASSSVTEQPPPSRGRRKKPVVVAPPLEPAVKRKRSQDVEADSDANNSTKYSKVEVVKSEEAEAPEEDSSAVPIKQESVDGNEVSSISPTVTPTPTPAPTPAPVPGSRRGRGRPQNRNSSSPATTTRATRLSKAGSPVILTPVAQEPAPPKRRRVGSSTRKTVSASSLAPSSQGGAGDEDSKDSMASSMDDLLMAAADIKQEKLTPDFDDSLMPEGLPSTSGASSANGHSCTEPLTVDTEINVKPADSKVKPKESPVVAVEESPSQSETQSAKVSAHAGKAPSLSPDMISEGVSAVSVRKFYKKPEFLENNLGIEKDPELGEIVQTVSNNDTETDVEMAVDGEVNQPSTPKSQDKKKEEQEKNQKSGLKAAKKAPAKLEPKAEDISEILTDVPVDISTEAVEIIEEAEEDTCSNSSIKPGELRLDESNDEPELLLEDALIVNGDENETPDQPEEKEDQVEFFHTGEYDDFEHEIMVELAKEGVLDASGNALSQQKVELEHPEDVTLHESKNDIEAEESVERKPLKDPSVADEMEDMNEESYIDIKDQTNQLLVEHLGRRGHGSDCGPEDNKKNLSTSASSTAADGLDIQLAIKEDDDEEKPLAVIADEQKPGLLLTNDMKVDEKPNGKQESVCDEHVQLVPNLRQEQEIHLQNLGLLTHQAAEHRRKCLLEAQARQAQMQLQQHHHHQHKRQGARGGGSATHVESSGTLKTVIKLNRSSNGGVSGSGGLPTGTVIHGGCGSSSASSTSSSSVGSATRKSSGTLGSGAGAGAGVRRQSLKMTFQKGRARGHGAADRSADQYGAHAEDSYYTIQNENEDSSHSESQGQTDHGFYQMVKKDEKEKILIPEKASSFKFHPGRLCEDQCYYCSGKFGLYDTPCHVGQIKSVERQQKILANEEKLTVDNCLCDACFRHVDRRANVPSYKKRLSASGHLEMGSAAGSALEKQFAGDSGVITESGGEAGSTAAVAVQQRSCGVKDCVEAARHSLRRKCIRKRVKKYQLSLEIPAGSSNVGLCEAHYNTVIQFSGCVLCKRRLGKNHMYNITTQDTIRLEKALSEMGIPVQLGMGTAVCKLCRYFANLLIKPPDSTKAQKAEFVKNYRKRLLKVHNLQDGCHELSEADEEEAPNATETERPTSDGHEDPEMPMVADYDGPTDSNSSSSSTAALDTSKQMSKLQAILQQNVGADAAGAAGTGTVAASPGEADLGQISLTYCEGIRTFPCANFSTARKSWVCSSRCRSDAAAASVLRRAGHECRLSYNTMSRRAASGRSCKSRTKSELISAPVDTIREVLPKRRSRPSTHASSNASVYTETVRQRLNSFDHGHCGGLNIAGSPSSSGSGKRSGVPQPTGASVLATALTTPLTSHSSSSASISSEQHSSVDPVIPLVDLNDDDEGEDGAGGAGERESTNRQQDVILECLRTASVDKLTKQLSSNAVTIIARPKDKSQLSCNSGSSTSISSSSSAISSPEKWPSLRLQQSHQSSPRMHRHWPPASSGVSNSRSILKTNLLGMNKAVELVPLTTAPHAYKPTGCHKPEKQQKILDVANKQPGSQGEPVPSSALLGLQSKLKPPTHQQQVSGSGAGTSGSQKPSNVAQLLSSPPELISLHRRQTSGAAAGSSSFLQGKRLQLPRSGAGPSGAGTGTGAGAAGSRSAGGPPPPNVVILPDALTPQERHESKSWKPTLIPLEDQHKVPNKSHALYQTADGRRLPALVQVQSGGKPYLISIFDYNRMCILRREKLMRDQLLKSNAKPKPQNQQQQQGQTHQQQQNSAACAAFSNMVKLAQQHTARQQLQQLQQKPQQQQQLPTLQPGGVRLARLPQKLLMPPLTNPQIGSQAPNLQPLLSSTLDNSNNCWLWKNFPDPNQYLLNGNGGGAGSSSSKLPHLTAKPATATSSSGAANKSAGSLFTLKQQQHQQKLIDNAIMSKIPKSLTVIPQQMGGNTGGDMGGSSSPARTDDGEGGRHGH
Protein: Glucoamylase, intracellular sporulation-specific (EC 3.2.1.3) (1,4-alpha-D-glucan glucohydrolase) (Glucan 1,4-alpha-glucosidase) (P08019)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Glycogen phosphorylase
- Glycogen debranching enzyme
- 1,4-alpha-glucan-branching enzyme
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein eL32
- Oligo-1,6-glucosidase IMA5
- Alpha-glucosidase MAL12
- Oligo-1,6-glucosidase IMA1
- Oligo-1,6-glucosidase IMA3
Sequence:
MARQKMFYNKLLGMLSVGFGFAWALENITIYEFDFGKGILDQSYGGVFSNNGPSQVQLRDAVLMNGTVVYDSNGAWDSSALEEWLQGQKKVSIEKIFENIGPSAVYPSISPGVVIASPSQTHPDYFYQWIRDSALTINSIVSHSAGPAIETLLQYLNVSFHLQRSNNTLGAGIGYTNDTVALGDPKWNVDNTAFTEDWGRPQNDGPALRSIAILKIIDYIKQSGTDLGAKYPFQSTADIFDDIVRWDLRFIIDHWNSSGFDLWEEVNGMHFFTLLVQLSAVDKSLSYFNASERSSPFVEELRQTRRDISKFLVDPANGFINGKYNYIVGTPMIADTLRSGLDISTLLAANTVHDAPSASHLPFDINDPAVLNTLHHLMLHMRSIYPINDSSKNATGIALGRYPEDVYDGYGFGEGNPWVLATCTASTTLYQLIYRHISEQHDLVVPMNNDCSNAFWSELVFSNLTTLGNDEGYLILEFNTPAFNQTIQKIFQLADSFLVKLKAHVGTDGELSEQFNKYTGFMQGAQHLTWSYTSFWDAYQIRQEVLQSL
Protein: Phosphopantothenate--cysteine ligase 1 (EC 6.3.2.51) (AtCoaB) (Phosphopantothenoylcysteine synthetase 1) (PPC synthetase 1) (Q8GXR5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the first step in the biosynthesis of coenzyme A from vitamin B5/pantothenate, where cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. The catalytic activity is not CTP- but ATP-dependent.
Interaction partners:
- Pantothenate kinase 1
- Phosphopantothenoylcysteine decarboxylase
- Pantothenate kinase 2
- Probable phosphopantothenoylcysteine decarboxylase
- Phosphopantetheine adenylyltransferase
- Dephospho-CoA kinase
- Pantoate--beta-alanine ligase
- Bifunctional cystathionine gamma-lyase/cysteine synthase
- cysteine synthase
- Bifunctional L-3-cyanoalanine synthase/cysteine synthase D2
Sequence:
MSSISGLVEDEISSFFESSPPLKNKEEIVANLNQFIELNSSCQGGMRRIVCVTSGGTTVPLEQRCVRYIDNFSSGNRGAASTENFVKAGYAVIFLYRRGTCQPYCRYLPDDPFLECFEFPDAKNIQVHGSHSGAVKMAVMDQQAAVAEGRLLKLPFSTIYEYLQMLRLIATILKDVGPCSMFYLAAAVSDFYVPWLSMTEHKIESGSGPLDIRLAQVPKMLSILRSNWAPKAFCISFKLETDSKILLEKATKALQKYKVHAVVANELLTRKEEVVVVSSSGNVVVRRDSNKPESIVEDNLIRLLVDRHSTYIKESLT
Protein: Glutamate--cysteine ligase (EC 6.3.2.2) (Q8W4W3)
Organism: Zea mays (Maize)
Subcellular location: Plastid, chloroplast {ECO:0000256|ARBA:ARBA00004229, ECO:0000256|PIRNR:PIRNR017901}.
Interaction partners:
Sequence:
MTEPLTKEDLVAYLVSGCKPKENWRIGTEHEKFGFEVDTLRPLKYDQIRDILNGLAERFDWDKIMEKNNVIGLKQGKQSISLEPGGQFELSGAPLETLHQTCAEVNSHLYQVKAVGEEMGIGFLGLGFQPKWALSDIPIMPKGRYEIMRNYMPKVGTLGLDMMFRTCTVQVNLDFSSEQDMIRKFRAGLALQPIATAIFANSPFKEGKPNGFLSLRSHIWTDTDNNRAGMLPFVFDDSFGFEQYVDYALEVPMYFVYRNKKYIDCTGMSFRDFMQGKLPQAPGELPTLTDWENHLTTIFPEVRLKRYLEMRGADGGPWRRLCALPAFWVGLLYDEESLQSILDMTFDWTKEEREMLRRKVPSTGLKTPFRDGYVRDLAEEVLKLAKNGLERRGYKEVGFLREVDEVVRTGVTPAERLLSPYETKWQRNVDHVFEHLLY
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q9ARH1)
Organism: Brassica napus (Rape)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004162}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}.
Interaction partners:
Sequence:
MSSAPSPGTGSPPSPPSNSTTTTPPPASAPPPTTPSSPPPPSTIPTSPPPSSRSTPSAPPPSPPTPSTPGSPPPLPQPSPPAPTTPGSPPAPVTPPTRNPPPSVPGPPSNPSREGGSPRPPSSPSPPSPSSDGLSTGVVVGIAIGGVALLVIVTLICLLCKKKRRRDEEDAYYVPPPPPPGPKAGGPYGGQQQQWRQQNATPPSDHVVTSLPPPPKAPSPPRQPPPPPPPPFMSSSGGSDYSDRPVLPPPSPGLVLGFSKSTFTYEELARATNGFSEANLLGQGGFGYVHKGVLPSGKEVAVKQLKVGSGQGEREFQAEVEIISRVHHRHLVSLVGYCIAGAKRLLVYEFVPNNNLELHLHGEGRPTMEWSTRLKIALGSAKGLSYLHEDCNPKIIHRDIKASNILIDFKFEAKVADFGLAKIASDTNTHVSTRVMGTFGYLAPEYAASGKLTEKSDVFSFGVVLLELITGRRPVDANNVYVDDSLVDWARPLLNRASEQGDFEGLADAKMNNGYDREEMARMVACAAACVRHSARRRPRMSQIVRALEGNVSLSDLNEGMRPGQSNVYSSYGGSTDYDSSQYNEDMKKFRKMALGTQEYNATGEYSNPTSDYGLYPSGSSSEGQTTREMEMGKIKRTGQGYSGPSL
Protein: Homeobox protein ceh-6 (P20268)
Organism: Caenorhabditis elegans
Function: Vital for embryonic development and essential for the proper function of the excretory cell. Required for the transdifferentiation of the Y rectal epithelial cell to the PDA motor neuron during larval development.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Spalt-like protein sem-4
- Egg-laying defective protein 27
- Transcription factor sox-2
Sequence:
MLIPSSSSIPSSLSASASDSEPSSLNGSGISDQNILPNYHLHHHLINENEMEAANYAQVIKPTCEAFQDWPHTPMLYQQPQLHFMLPQHDWAYPHLAQSLPPPHHLTPSTAAVAAATIASQSSIINQTSVVTSTPSCQIKQEVERPEIIQRLMPPWPPAYQFSCDDSGSVSGAGGPHQPLSDISDDSEQTCPDDLEGFAKQFKQRRIKLGYTQADVGVALGTLYGNIFSQTTICRFEALQLSFKNMCKLKPLLFKWLEEADSTTGSPNSTFEKMTGQAGRKRKKRTSIEVNVKSRLEFHFQSNQKPNAQEITQVAMELQLEKEVVRVWFCNRRQKEKRIAPNQYDAPHPMALNNGYPMTADLFPYQAVVNHYTQQSPRQQ
Protein: Signal transducer and activator of transcription 5A (Mammary gland factor) (P42230)
Organism: Mus musculus (Mouse)
Function: Carries out a dual function: signal transduction and activation of transcription. Mediates cellular responses to the cytokine KITLG/SCF and other growth factors. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Binds to the GAS element and activates PRL-induced transcription. Regulates the expression of milk proteins during lactation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16837552}. Nucleus {ECO:0000269|PubMed:16837552}. Note=Translocated into the nucleus in response to phosphorylation.
Interaction partners:
Sequence:
MAGWIQAQQLQGDALRQMQVLYGQHFPIEVRHYLAQWIESQPWDAIDLDNPQDRGQATQLLEGLVQELQKKAEHQVGEDGFLLKIKLGHYATQLQNTYDRCPMELVRCIRHILYNEQRLVREANNCSSPAGVLVDAMSQKHLQINQRFEELRLITQDTENELKKLQQTQEYFIIQYQESLRIQAQFAQLGQLNPQERMSRETALQQKQVSLETWLQREAQTLQQYRVELAEKHQKTLQLLRKQQTIILDDELIQWKRRQQLAGNGGPPEGSLDVLQSWCEKLAEIIWQNRQQIRRAEHLCQQLPIPGPVEEMLAEVNATITDIISALVTSTFIIEKQPPQVLKTQTKFAATVRLLVGGKLNVHMNPPQVKATIISEQQAKSLLKNENTRNECSGEILNNCCVMEYHQATGTLSAHFRNMSLKRIKRADRRGAESVTEEKFTVLFESQFSVGSNELVFQVKTLSLPVVVIVHGSQDHNATATVLWDNAFAEPGRVPFAVPDKVLWPQLCEALNMKFKAEVQSNRGLTKENLVFLAQKLFNISSNHLEDYNSMSVSWSQFNRENLPGWNYTFWQWFDGVMEVLKKHHKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAWKFDSPDRNLWNLKPFTTRDFSIRSLADRLGDLNYLIYVFPDRPKDEVFAKYYTPVLAKAVDGYVKPQIKQVVPEFVNASTDAGASATYMDQAPSPVVCPQPHYNMYPPNPDPVLDQDGEFDLDESMDVARHVEELLRRPMDSLDARLSPPAGLFTSARSSLS