wanglab/gogpt-training-data huggingface dataset:
Protein: Protein ASI2 (Amino acid sensor-independent protein 2) (P53895)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Part of the nuclear inner membrane (INM)-specific branch of the ER-associated degradation (ERAD) pathway, required for the elimination of misfolded proteins in the INM, a specialized ER subdomain. Required for ERG11 degradation. Negative regulator of SPS-sensor signaling. Together with ASI2 and ASI3, prevents the unprocessed precursor forms of STP1 and STP2 that escape cytoplasmic anchoring from inducing SPS-sensor-regulated genes in the absence of inducing signals. Controls amino acid permease (AAP) gene expression in response to amino acid availability, a process mediated by the transcription factors STP1 and STP1.
Subcellular location: Nucleus inner membrane {ECO:0000269|PubMed:17085444}; Multi-pass membrane protein {ECO:0000269|PubMed:17085444}.
Interaction partners:
- Probable ERAD-associated E3 ubiquitin-protein ligase ASI1
- ERAD-associated E3 ubiquitin-protein ligase ASI1
- E3 ubiquitin-protein ligase complex SLX5-SLX8 subunit SLX8
- Anaphase-promoting complex subunit 9
- E3 ubiquitin-protein ligase complex SLX5-SLX8 subunit SLX5
- Anaphase-promoting complex subunit SWM1
- Anaphase-promoting complex subunit MND2
- Anaphase-promoting complex subunit CDC27
- Anaphase-promoting complex subunit 1
- Anaphase-promoting complex subunit DOC1
Sequence:
MARPQNHRRSNWTERDDNDDYLFQRFLEESETRHSREPSPVTEQSQQELQQDVQQAIDGIFNSLRRNMSSTSNINRAANMDATTNGNGGINADTIRATNANTADSPFTARQQSPLRTFLRNLFILDYFIGLILFPFSVYNILRSGFNSMTFSENDFIIEIVGYWKFAKIFGSGGTTLIAYKDTGKLGLLGKFHNIIVFYSSPVIKHIMKSRDGNEPNLNWIRLMFAKAFELFVKVSTILIYLAYGVSGTVYMVTAGFFFVLCLLFTVIRRYKGVHRMLVSQRITGPGVF
Protein: Growth arrest and DNA damage-inducible protein GADD45 alpha (A0A087WZQ0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTLEEFSAGEQKTERMDKVGDALEEVLSKALSQRTITVGVYEAAKLLNVDVALQIHFTLIQAFCCENDINILRVSNPGRLAELLLLETDAGPAASEGAEQPPDLHCVLVTNPHSSQWKDPALSQLICFCRESRYMDQWVPVINLPER
Protein: Fibroblast growth factor 20 (FGF-20) (Q9NP95)
Organism: Homo sapiens (Human)
Function: Neurotrophic factor that regulates central nervous development and function.
Subcellular location: Secreted {ECO:0000269|PubMed:11306498}.
Interaction partners:
- Fibroblast growth factor receptor 1
- Fibroblast growth factor receptor 2
- Fibroblast growth factor receptor 4
- Klotho
- Pro-epidermal growth factor
- Fibroblast growth factor receptor 3
- Basement membrane-specific heparan sulfate proteoglycan core protein
- Fibroblast growth factor-binding protein 1
- Decorin
- Vascular endothelial growth factor receptor 2
Sequence:
MAPLAEVGGFLGGLEGLGQQVGSHFLLPPAGERPPLLGERRSAAERSARGGPGAAQLAHLHGILRRRQLYCRTGFHLQILPDGSVQGTRQDHSLFGILEFISVAVGLVSIRGVDSGLYLGMNDKGELYGSEKLTSECIFREQFEENWYNTYSSNIYKHGDTGRRYFVALNKDGTPRDGARSKRHQKFTHFLPRPVDPERVPELYKDLLMYT
Protein: Layilin (Q6UX15)
Organism: Homo sapiens (Human)
Function: Receptor for hyaluronate.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Colocalizes with TLN1 at the membrane ruffles. {ECO:0000250}.
Interaction partners:
- Talin-1
- Talin-2
- Merlin
- Radixin
Sequence:
MRPGTALQAVLLAVLLVGLRAATGRLLSASDLDLRGGQPVCRGGTQRPCYKVIYFHDTSRRLNFEEAKEACRRDGGQLVSIESEDEQKLIEKFIENLLPSDGDFWIGLRRREEKQSNSTACQDLYAWTDGSISQFRNWYVDEPSCGSEVCVVMYHQPSAPAGIGGPYMFQWNDDRCNMKNNFICKYSDEKPAVPSREAEGEETELTTPVLPEETQEEDAKKTFKESREAALNLAYILIPSIPLLLLLVVTTVVCWVWICRKRKREQPDPSTKKQHTIWPSPHQGNSPDLEVYNVIRKQSEADLAETRPDLKNISFRVCSGEATPDDMSCDYDNMAVNPSESGFVTLVSVESGFVTNDIYEFSPDQMGRSKESGWVENEIYGY
Protein: Uncharacterized protein At1g33050 (Q8VYZ1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MKHYSHGIDGLRSGLSPSAKPFAIGSSSSPAFSLKSEHEDSIWGDYTLDLSFLSSDDQRSGLDDDDSLSNLSRDVETNKEGLVLEEKIASSGKVLVNPNPSFSKLPEVLMKSSDVVGDAKLGLSCVSEKSSTESDLDESEEDSPCWKGMLSHKSLASGTKSMTSRRSTDDLSGFRKLNPLAPQFIPSSSKKKLETDGEKCEETSSSSLKKSLSSTFPSSSGEFDLTDPPLEDGRNDAAEKTSILTHNADEILGFVTSDSVSKTVSMLDSRNEFQPSKRLDPLAPVFVPSSAKLGPSVHEKLGDFVVNAYSTSALASSHVKSLDKGKVVTSSGEVGHSFKSQYGGHDFGSTSSYGPWIESEVGITEYAKLGSSNKSQGQRRLNPLARQFSLADAKQKPYGYGKNQAADDLSLVVNTSGLYIPARYREDHNVVDADLAQSSVNVERFLPNMSHGGSSLITPKADSNFGSTKWIAVEPNPTFSVKGNRDFKHHLPFHVVETAASSSTSDMKALPGPSPKMDVKKLLTTMHGLSELLTLAHGSESSDSPNAEELDLINSTVQNLNLYIQNNSQEHAGNQSVAQYNSYDLKLLPNKSKLSIRDHQFPTANNMTVDLDVKRKDKYSVVSRETVPGSRSYQYGATEDNGFGQVVPTNGYQQHQGVEQINQNALFYKSLWLKAEADRCLMVYETSLSNPYP
Protein: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4 (Complex I-B15) (CI-B15) (NADH-ubiquinone oxidoreductase B15 subunit) (O95168)
Organism: Homo sapiens (Human)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:12611891}; Single-pass membrane protein {ECO:0000255}; Matrix side {ECO:0000305}.
Interaction partners:
- NADH-ubiquinone oxidoreductase chain 4
- NADH dehydrogenase 1 beta subcomplex subunit 5, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- NADH dehydrogenase 1 subunit C2
- NADH dehydrogenase 1 beta subcomplex subunit 3
- Acyl carrier protein, mitochondrial
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
- NADH dehydrogenase flavoprotein 2, mitochondrial
- NADH dehydrogenase 1 subunit C1, mitochondrial
- NADH-ubiquinone oxidoreductase chain 5
Sequence:
MSFPKYKPSSLRTLPETLDPAEYNISPETRRAQAERLAIRAQLKREYLLQYNDPNRRGLIENPALLRWAYARTINVYPNFRPTPKNSLMGALCGFGPLIFIYYIIKTERDRKEKLIQEGKLDRTFHLSY
Protein: Small ribosomal subunit protein eS19z (40S ribosomal protein S19-1) (Q9SGA6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Small ribosomal subunit protein uS12y
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Small ribosomal subunit protein eS24y
- Small ribosomal subunit protein eS30z/eS30y/eS30x
- Small ribosomal subunit protein eS7y
- Small ribosomal subunit protein eS7z
- Small ribosomal subunit protein eS21z
- Small ribosomal subunit protein eS8z
- Small ribosomal subunit protein eS24z
- Small ribosomal subunit protein uS17y
Sequence:
MATGKTVKDVSPHDFVKAYASHLKRSGKIELPTWTDIVKTGKLKELAPYDPDWYYIRAASMARKVYLRGGLGVGAFRRIYGGSKRNGSRPPHFCKSSGGIARHILQQLETMNIVELDTKGGRRITSSGQRDLDQVAGRIAVEP
Protein: High-affinity zinc uptake system membrane protein ZnuB (P39832)
Organism: Escherichia coli (strain K12)
Function: Involved in the high-affinity zinc uptake transport system.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Zinc import ATP-binding protein ZnuC
- High-affinity zinc uptake system protein ZnuA
- Metal-binding protein ZinT
- Zinc transporter ZupT
- Divalent metal cation transporter MntH
Sequence:
MIELLFPGWLAGIMLACAAGPLGSFVVWRRMSYFGDTLAHASLLGVAFGLLLDVNPFYAVIAVTLLLAGGLVWLEKRPQLAIDTLLGIMAHSALSLGLVVVSLMSNIRVDLMAYLFGDLLAVTPEDLISIAIGVVIVVAILFWQWRNLLSMTISPDLAFVDGVKLQRVKLLLMLVTALTIGVAMKFVGALIITSLLIIPAATARRFARTPEQMAGVAVLVGMVAVTGGLTFSAVYDTPAGPSVVLCAALLFILSMMKKQAS
Protein: Ktr system potassium uptake protein B (K(+)-uptake protein KtrB) (O32081)
Organism: Bacillus subtilis (strain 168)
Function: Integral membrane subunit of the KtrAB potassium uptake transporter. The 2 major potassium transporter complexes KtrAB and KtrCD confer resistance to both suddenly imposed and prolonged osmotic stress.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Ktr system potassium uptake protein A
- Ktr system potassium uptake protein C
- Putative Na
Sequence:
MTLQKDKVIKWVRFTPPQVLAIGFFLTIIIGAVLLMLPISTTKPLSWIDALFTAASATTVTGLAVVDTGTQFTVFGQTVIMGLIQIGGLGFMTFAVLIVMILGKKIGLKERMLVQEALNQPTIGGVIGLVKVLFLFSISIELIAALILSIRLVPQYGWSSGLFASLFHAISAFNNAGFSLWPDNLMSYVGDPTVNLVITFLFITGGIGFTVLFDVMKNRRFKTFSLHTKLMLTGTLMLNAIAMLTVFILEYSNPGTLGHLHIVDKLWASYFQAVTPRTAGFNSLDFGSMREGTIVFTLLLMFIGAGSASTASGIKLTTFIVILTSVIAYLRGKKETVIFRRSIKYPIIIKALAVSVTSLFIVFLGIFALTITEQAPFLQIVFETFSAFGTVGLTMGLTPELTTAGKCIIIVIMFIGRIGPLTFVFSFAKTEQSNIRYPDGEVFTG
Protein: Doublesex- and mab-3-related transcription factor 1Y (Y-linked doublesex- and mab-3-related transcription factor) (Y-specific doublesex- and mab-3-related transcription factor) (DMY) (Q8JIR6)
Organism: Oryzias latipes (Japanese rice fish) (Japanese killifish)
Function: Transcription factor that plays a key role in male sex determination and differentiation by controlling testis development and germ cell proliferation. Acts both as a transcription repressor and activator.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00070}.
Interaction partners:
Sequence:
MSKEKQCRPGPRVPKCSRCRNHSLKTPLKGHKRFCRWKDCHCLKCKLIVDRQRVMAAQVALRRQQAQEEELGICSPEASSGPEVVVKNEAGADCLFSVEGRSGTPAPPPNPNPLSVAGSYSASSSSPSAAARVYSEEASDQPLETSYYNFYQPSRYSSYYGNLYNYQQYQQMPPSDGRLSGHSMPSQYRMHSFYPGTAYLPQGLGSPVPPYFSLEDNDGAAASFFPSSLTSTHDSTLTYRSISSLVNDGVKAEFESGGQPPSSRPTP
Protein: BHLH-PAS protein similar to human NXF (Q2WGN8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPNAIGASSITKWISQIESFEQRELVTNICKRAIDDMYADNKRGLDKVTAATPPTHALQQQQQQQHPHQQQQHLQHVLQLQQQQQQHLQQQQHHLQHQMHTHHNFQQHETSPTVSQQQHMQQQQPQTTQQQHATQQQQQQQQQTAGMFTRFDANKSTKGASKMRRDLINAEIANLRDLLPLPQSTRQRLSQLQLMALVCVYVRKANYFQQVFKRHNAMHHLHHQTATPNIGFSKALSGFLMMLTQNGKLLYISDNAAEYLGHSMEDLLIHGDSVYDIIDKQDHANIQAELNRNVPPQPGGSSQASSGGAGGAGGAGDSTSSNGSAAGAGGAGGASSLEGEHRMFLCRMNVSRNARRQMRFGDQKVVLVQGHYLSFLPLCSRNEPVFLATCTPIAMPETRECVVQGATNVFTTIHSMDMKIAHIDKNGEFHLGYDKSTLQGTSWYNLIHSDNLTEAQKKHSLIIQSEQDRSCILLVRMQRSSGEYTWVHVVLQVRDSPDSTQQPVIVCTNQVLNDREASIMLANSWLYHYYTVQSKIQFGMPLDSGIRVPPGTPSSGYYSPHSSHPPATPGGATPNLGIASSFGPHHHPHHSHHPHHHHHHHHPATAYHHHPHMGTYGGVYHAKAAIELKEDQPLFCFQEPVDYSQVNSHVNPPNATSTPNPPISKSSTPPPPKKRARKLEPLYLHAERSPAAAITPEPDCYAIHTHPAAAYATSSVVSSDASVIYATIVPTRPRLPNKSLPPDPADFIEQWNPSPPWSESAQKASLDSFGSSHELSPCITTTPPTPTSATPHQSGLGTTQTIGPAFSFEWMSDPLVPVTYQQWPPTGDHHQHLSQHLSQSQNHQNPLQQQQQHEQLLLGQQPHLHQQHQHLALHHGRGEHSLEGESQGVVVVPPIPISIPIPTATGHGDAGQPVEDRG
Protein: Histone H3-like centromeric protein hcp-3 (CENP-A homolog) (CeCENP-A) (Holocentric chromosome-binding protein 3) (P34470)
Organism: Caenorhabditis elegans
Function: Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. Required for recruitment and assembly of kinetochore proteins, mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division (By similarity). Might promote cleavage furrow stability during cytokinesis. Not required for chromosome segregation during meiosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:10524621, ECO:0000269|PubMed:11402065}. Chromosome, centromere {ECO:0000269|PubMed:12080088, ECO:0000269|PubMed:15767665, ECO:0000269|PubMed:17339379, ECO:0000269|PubMed:26904949}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:11402065}. Note=Requires knl-2 and lin-53 for chromatin localization (PubMed:17339379, PubMed:26904949). Co-localizes with hcp-6 at prophase, metaphase, and anaphase chromosomes (PubMed:12080088, PubMed:15767665). {ECO:0000269|PubMed:11402065, ECO:0000269|PubMed:12080088, ECO:0000269|PubMed:15767665, ECO:0000269|PubMed:17339379, ECO:0000269|PubMed:26904949}.
Interaction partners:
- Kinetochore null protein 2
- Kinetochore protein Nuf2 homolog
- CENP-C-like protein HCP-4
- Aurora/IPL1-related protein kinase 2
- Mitotic checkpoint serine/threonine-protein kinase bub-1
- Probable histone-binding protein lin-53
- JmjC domain-containing protein
- Nucleosome-remodeling factor subunit NURF301-like
- Kinetochore protein ndc-80
- Securin-like protein
Sequence:
MADDTPIIEEIAEQNESVTRIMQRLKHDMQRVTSVPGFNTSAAGVNDLIDILNQYKKELEDDAANDYTEAHIHKIRLVTGKRNQYVLKLKQAEDEYHARKEQARRRASSMDFTVGRNSTNLVDYSHGRHHMPSYRRHDSSDEENYSMDGTNGDGNRAGPSNPDRGNRTGPSSSDRVRMRAGRNRVTKTRRYRPGQKALEEIRKYQKTEDLLIQKAPFARLVREIMQTSTPFGADCRIRSDAISALQEAAEAFLVEMFEGSSLISTHAKRVTLMTTDIQLYRRLCLRHL
Protein: Membrane selenoprotein (Q86KP5)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Selenoprotein F
- Selenoprotein K homolog
Sequence:
MSLFNLPKVDLGEDCEGGVUARPSSSSSSINNASDESTPLISKTNDEEKANIGISSTSNSPQEEQTKKPLFISILTLLISIPALVGSUCWPVLIASLSGVAVSAGSVELAHSLTFAITLSILSNLAQYHFHKCKKRPSDRGHWIKFGPFYLTAIAVPLATFDILRHILVDNSIWTIHSFISPAAYRPGCENENITCLSVMGWFSAIVFTYTGYACLLVGTIWAADLIPKIKKVWTQLRPSKKN
Protein: Ribosomal protein S4 (O63697)
Organism: Oryza sativa (Rice)
Interaction partners:
Sequence:
MPALRFKTCRLLPGNVRNRELSLIQRRILRRLRNKRRSIKRNLSQRENLNSNIKSQTTRKLSLYYGDLPIREMHRGRERTSYIPFLLNQETRSDVIPVRLHFCDTLPQARQPISHRRVCLNNGLVTITHLKVSHGDLISFQENDARTRGEEIRRSFYIDISVGKIIGKLLPVRIWRKTKTEWFRLLTTQRVCRLLLKSWFLQELRSYMQEEDLERTKKFGSAKVCLGSSFAEHNRMKRNLFHFKYFFLLKRRKEEEELIRTIGEAENRKRAISPFVYKSSLYRNSTYCSGSPFTRKIRIKRIELPTHYSEVNHRTLKAVVSYGPNIGHIPHDIRLKDPNLPLRSGNGRGQNI
Protein: Bradyzoite-formation deficient protein 1 (S8GIB3)
Organism: Toxoplasma gondii (strain ATCC 50611 / Me49)
Function: Master transcription factor that controls the differentiation of acute-stage tachyzoite parasites into chronic-stage bradyzoites, which form intracellular cysts resistant to immune clearance and existing therapies. Sufficient to drive differentiation into bradyzoite stage. Following translation in response to stress conditions, binds to the promoter of many chronic stage-specific genes and promotes their expression, thereby driving differentiation into bradyzoites.
Subcellular location: Nucleus {ECO:0000269|PubMed:31955846}.
Interaction partners:
Sequence:
MEGASTQPMPHSQRERQAPVHAISGTWENCDQAGEYKGTACCVVERQVYSTETHAVEGCCSTRWNGVKEEKGGGEVSSRTALAGVVHLYTNSDGNAYTHISDQGMRQDEAVAGQEQRHLNCEGEHEKKGNVAAGGGTLMVTKSEIEPCDDYYSVQRGQSCAGERAPRDGCCRLLDGSRVDPAEGGSEEDENCYTHVLQKHLGQMPTAPYQGDDRLQTDLRLGDFQSGPSDALSGHHVTRTPILSPHGRYSEYISERLAWQYAERPGHGIAAENTVVMHSHTGEATGSLRADAPSQWSTESRLQFHVGSQFTTENPELFAGIVGLDTEQFDARNAEALHWRQQGEARSTETECIADITPERGNRSTIRQWNKPEAARQEYHRASASARGPEETNIITRGAHSDDQSIDAAAPGCWAARHLTSRQHPNPRPRMKEEHCGREREVLSSEQPSDCGETQKTPASHSLVLDSKSRADASQTSPYTRNDEIQTIRAFEEQCLEVQLPQSRLRRGIDYEAGMSQLAPTTQELKAKVLTTGLSPSCPNAAVLRASVPLSMDTTVTVHLADVEDPSSKRHTPIENSISSGHCDPPCSSPGGMMEPRVSVSGLGSPHNCVEDREIARHGDGIGRDILERRPLPFSPAALLTGCSSTAASSVVSGDVFTSVAASARANACRSSTDTQEESGCGDAPRYVLLFPDEQDERLGHAQTSIATPSGSGQSKCMFKGDGNAEATFREEVKSSELRTPSRIQTRRLLPGVQLQGMDCDGCGASDPQKGRPAPETGFLPEICHFSPQHPWQPGSEVNQGYRAGADYGTSRVQQSLENCSWEESVDEGEQPRTTSSSSYGQDTQKRDSFLQSIDNRIASEPVDPTGTCGYNSTPETFRSGCIMRDQMLGVKPHLSHVSLTREGKHRGQQTHLRKTGVPTWSAEEDASLAELVSRKGFKWALISSQLTGAFGIPRTGKQCRERWFNHVNPEVKKGDWSAEEDAMILMLQNELGNRWATIAKKLRGRTENAVKNRFISLSNARLGYGRPKRDGSSADCFSNRRTGSGKSSGITGMPNLCQSVCSAGTTKKDSSESGNHFVMSVATKVFEFSDVAVDSGVSRPRQCTGTSPSCGHPSAGEGDPSHLKNTDVVGREQPIQRNNNESGKAAEQTAFSGVKTGTLSVSQDAVPVGRLVVASVGPQHIRRSFPTDETLPKFAAKEHNNQQLNDEREHLEQSNSTSEGSFLASAHEHADIARSDPDEDTLEPHQKRRRKRCAIAYQGEERGDSNGLDSIADRAEQAGNFQAMRKANTDNGKVDYLEPHRYEKLSPCEQVIQPSLRPACDHRGAPQNSVESGEQSPDAQRQLCNQGCRTSNRTVHSSVYSNEVESNELRGVFRLAEQSLPSQSGDPAWSTAGFQLSILPQKVEVHSRNKCDGQNVMYRCSPGSLPTTHQQTVFHYDRDSSRFPCAAKPAAASGAQGTIEENDGLVKEGPSMIVTGSSVEVVHCCSVSLRRRDRSLPSAQLWTSQETESDTNPSPNQQHESCHQYCKRHAAWCGKTDQFSKLTSSHQENSSGKDACLVSVSPTVTLDDLQKQSRGTVLSAKEEIGKPETWSHVVDNTYSKTDHQRASLCAENSSGCAEGSTELVRFSGGSVKSGSSMSVDCGNGNPDDCQDCKAEEIWRGEQRYAERGHSVESRGAGSVGRSTDLTITDSGSMPLCASPIGRPPADNDTLFLSDARCNVVAQLNHQDNSRISRLASCEEEFLACGGERLINASGGFKPDGGCLYRMQQAGACNTKLHRPVHSCSTIDSEQLEDLPSVEKAVGDRSFSSKRKGDIPPFAEWKKNDELRELYRGVSEAVSHGQPGDWNGSWPGISGRAHQTSSCFPDRVNASDRRELNSWRLHVSAAAELGSSHIWNSQSYASASVSRDKQREPPKNGLTGCDVPEYLGTSQSAGLPAANAHERGNFYGHDRCRPREGERVRWVGLQRNRKPEASVSSGASNSATTARPKDSTEPDEGNSEGVSTRRKDSGSTAATISRAVSLGMVTPSAACENSSSLTDTSPPLSHRPSFSFTHCCEETLSRCNSSNYLCPPATCHTSDDGRSLGPSREAQALRSLSLASGYGYPGIPAEATSFWQGSSLEHSIMEPQMVPSDDELRLWVHPRDAANWSQSTLKPVAVVSGTDAGDDQHKTPENLTPESGQAHRRDGHDMQRVQRCDDEGECPPTTVELTFPHSHSSDEMQDLPSKVQGNFLLRRELSDSLQHETAESVAGYGWMRIRNAGDIPNSKVPCAWEQCMPASERERGVNDHMSSEASRMSKAASSSFVPSSCTDAPVVRVGEDTTKSVCEEQQLCEGGNRGSLSPEATGFESLGPPLQLLLVDGYTPFEPVVEKVSQTMEQTLFPVPGQETDTRDEDGRYNCECLQNRQPPLHSGGLM
Protein: trypsin (EC 3.4.21.4) (Q9VRS9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted, extracellular space {ECO:0000256|ARBA:ARBA00004239}.
Interaction partners:
- Jonah 25Biii
- Jonah 65Aii
- Peptidase S1 domain-containing protein
- Jonah 25Bii, isoform A
- Jonah 44E, isoform A
- Serine protease 3
- trypsin
- Zinc carboxypeptidase A 1
- Jonah 99Fii
- trypsin
Sequence:
MKVLAVLLLGVIASATAFEKPVFWKDVPVGKASIEGRITMGYPAYEGKVPYIVGLGFSKNGGGTWCGGSIIGNTWVMTAKHCTDGMESVTIYYGALWRLQAQYTHWVGRSDFIEHGSGDISLIRTPHVDFWSLVNKVELPRYDDRYNNYQGWWALVSGWGKTSDEGGVSEYLNCVDVQIGENSVCENYYGSFSGDLICIPTPENKGTCSGDSGGPLVIHDGNRQVGIVSFGSSAGCLSNGPKGMVRVTSYLDWIRDNTGISY
Protein: Chanoclavine-I dehydrogenase easD (ChaDH) (EC 1.1.1.332) (Ergot alkaloid synthesis protein A) (Q4WZ66)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Chanoclavine-I dehydrogenase; part of the gene cluster that mediates the biosynthesis of fumiclavanine C, a fungal ergot alkaloid. DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan. The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by EasD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde. EasA reduces chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline. EasG then catalyzes the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine. Hydrolysis of festuclavine by easM then leads to the formation of fumigaclavine B which is in turn acetylated by easN to fumigaclavine A. Finally, easL catalyzes the conversion of fumigaclavine A into fumigaclavine C by attaching a dimethylallyl moiety to C-2 of the indole nucleus.
Interaction partners:
- Chanoclavine-I aldehyde reductase easA
- Tryptophan dimethylallyltransferase
- Catalase easC
- FAD-linked oxidoreductase easE
- 4-dimethylallyltryptophan N-methyltransferase easF
- Festuclavine dehydrogenase easG
- Short-chain alcohol dehydrogenase, putative
Sequence:
MASVESRIIAITGGASGIGAATCRLLAERGAAVLCVCDISPKNFDDLKISIKKINPSTKVHCATVDVTSSVEVRQWIEGIISDFGDLHGAVNAAGIAQGAGMRNTPTIAEEVDEEWTRIMNTNLNGVFYCTREEVRAMKGLPATDRSIVNVGSIASVSHMPDVYAYGTSKGACAYFTTCVAADAFPLGIRINNVSPGVTNTPMLPQFAPMAKTFEEIEESYKKEGLSLIEAEDVARTIVWLLSEDSRPVFGANINVGACMP
Protein: Ribonucleases P/MRP protein subunit POP3 (RNA-processing protein POP3) (RNases MRP/P 22.6 kDa subunit) (P53833)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for processing of 5.8S rRNA (short form) at site A3 and for 5'- and 3'-processing of pre-tRNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Ribonuclease P/MRP protein subunit RPP1
- Ribonucleases P/MRP protein subunit POP8
- Ribonucleases P/MRP protein subunit POP1
- RNases MRP/P 32.9 kDa subunit
- Ribonuclease P/MRP protein subunit POP5
- Ribonucleases P/MRP protein subunit POP7
- Ribonuclease MRP protein subunit RMP1
- Ribonuclease P protein subunit RPR2
- Ribonuclease MRP protein subunit SNM1
- Ribonucleases P/MRP protein subunit POP6
Sequence:
MSGSLKSLDKKIAKRRQVYKPVLDNPFTNEAHMWPRVHDQPLIWQLLQSSIINKLIHIQSKENYPWELYTDFNEIVQYLSGAHGNSDPVCLFVCNKDPDVPLVLLQQIPLLCYMAPMTVKLVQLPKSAMDTFKSVSKYGMLLLRCDDRVDKKFVSQIQKNVDLLQFPWLNAIKYRPTSVKLLKTTVPIVSKKRQK
Protein: E3 ubiquitin-protein ligase MGRN1 (EC 2.3.2.27) (Mahogunin RING finger protein 1) (RING finger protein 156) (RING-type E3 ubiquitin transferase MGRN1) (O60291)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase. Mediates monoubiquitination at multiple sites of TSG101 in the presence of UBE2D1, but not of UBE2G1, nor UBE2H. Plays a role in the regulation of endosome-to-lysosome trafficking. Impairs MC1R- and MC4R-signaling by competing with GNAS-binding to MCRs and inhibiting agonist-induced cAMP production. Does not inhibit ADRB2-signaling. Does not promote MC1R ubiquitination. Acts also as a negative regulator of hedgehog signaling (By similarity).
Subcellular location: Early endosome {ECO:0000269|PubMed:17229889, ECO:0000269|PubMed:19737927}. Note=The endosomal localization is dependent on the interaction with TSG101.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytosol. Nucleus. Note=Translocation from the cytosol to the nucleus is seen only in the presence of MC1R and MC4R, but not TBXA2R. Excluded from nucleoli.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol. Nucleus. Note=Translocation from the cytosol to the nucleus is seen only in the presence of MC1R and MC4R, but not TBXA2R. Excluded from nucleoli.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm, cytosol. Cell membrane.; SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm, cytosol. Cell membrane.
Interaction partners:
- Attractin
- Multiple epidermal growth factor-like domains protein 8
- Protein smoothened
- Melanocyte-stimulating hormone receptor
- Tumor susceptibility gene 101 protein
- Ankyrin repeat domain-containing protein 46
- E3 ubiquitin-protein ligase AMFR
- Ubiquitin-conjugating enzyme E2 R1
Sequence:
MGSILSRRIAGVEDIDIQANSAYRYPPKSGNYFASHFFMGGEKFDTPHPEGYLFGENMDLNFLGSRPVQFPYVTPAPHEPVKTLRSLVNIRKDSLRLVRYKDDADSPTEDGDKPRVLYSLEFTFDADARVAITIYCQASEEFLNGRAVYSPKSPSLQSETVHYKRGVSQQFSLPSFKIDFSEWKDDELNFDLDRGVFPVVIQAVVDEGDVVEVTGHAHVLLAAFEKHMDGSFSVKPLKQKQIVDRVSYLLQEIYGIENKNNQETKPSDDENSDNSNECVVCLSDLRDTLILPCRHLCLCTSCADTLRYQANNCPICRLPFRALLQIRAVRKKPGALSPVSFSPVLAQSLEHDEHSCPFKKSKPHPASLASKKPKRETNSDSVPPGYEPISLLEALNGLRAVSPAIPSAPLYEEITYSGISDGLSQASCPLAAIDHILDSSRQKGRPQSKAPDSTLRSPSSPIHEEDEEKLSEDVDAPPPLGGAELALRESSSPESFITEEVDESSSPQQGTRAASIENVLQDSSPEHCGRGPPADIYLPALGPDSCSVGIDE