UniProt ID | ERG6_YEAST | |
---|---|---|
UniProt AC | P25087 | |
Protein Name | Sterol 24-C-methyltransferase | |
Gene Name | ERG6 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 383 | |
Subcellular Localization | ||
Protein Description | Catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol.. | |
Protein Sequence | MSETELRKRQAQFTRELHGDDIGKKTGLSALMSKNNSAQKEAVQKYLRNWDGRTDKDAEERRLEDYNEATHSYYNVVTDFYEYGWGSSFHFSRFYKGESFAASIARHEHYLAYKAGIQRGDLVLDVGCGVGGPAREIARFTGCNVIGLNNNDYQIAKAKYYAKKYNLSDQMDFVKGDFMKMDFEENTFDKVYAIEATCHAPKLEGVYSEIYKVLKPGGTFAVYEWVMTDKYDENNPEHRKIAYEIELGDGIPKMFHVDVARKALKNCGFEVLVSEDLADNDDEIPWYYPLTGEWKYVQNLANLATFFRTSYLGRQFTTAMVTVMEKLGLAPEGSKEVTAALENAAVGLVAGGKSKLFTPMMLFVARKPENAETPSQTSQEATQ | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSETELRKR ------CCHHHHHHH | 53.91 | 24909858 | |
2 | Acetylation | ------MSETELRKR ------CCHHHHHHH | 53.91 | 9298649 | |
4 | Phosphorylation | ----MSETELRKRQA ----CCHHHHHHHHH | 32.77 | 24909858 | |
26 | Phosphorylation | GDDIGKKTGLSALMS CCCCCHHHCHHHHHC | 47.01 | 22369663 | |
29 | Phosphorylation | IGKKTGLSALMSKNN CCHHHCHHHHHCCCC | 22.24 | 22369663 | |
33 | Phosphorylation | TGLSALMSKNNSAQK HCHHHHHCCCCHHHH | 32.84 | 22369663 | |
34 | Acetylation | GLSALMSKNNSAQKE CHHHHHCCCCHHHHH | 46.30 | 24489116 | |
34 | Ubiquitination | GLSALMSKNNSAQKE CHHHHHCCCCHHHHH | 46.30 | 23749301 | |
45 | Acetylation | AQKEAVQKYLRNWDG HHHHHHHHHHHCCCC | 39.39 | 24489116 | |
54 | Phosphorylation | LRNWDGRTDKDAEER HHCCCCCCCCCHHHH | 53.59 | 28889911 | |
56 | Acetylation | NWDGRTDKDAEERRL CCCCCCCCCHHHHHH | 59.22 | 24489116 | |
96 | Ubiquitination | FHFSRFYKGESFAAS EEHHEECCCCCHHHH | 54.19 | 23749301 | |
96 | Acetylation | FHFSRFYKGESFAAS EEHHEECCCCCHHHH | 54.19 | 24489116 | |
99 | Phosphorylation | SRFYKGESFAASIAR HEECCCCCHHHHHHH | 28.93 | 28889911 | |
103 | Phosphorylation | KGESFAASIARHEHY CCCCHHHHHHHHHHH | 17.22 | 30377154 | |
114 | Ubiquitination | HEHYLAYKAGIQRGD HHHHHHHHCCCCCCC | 34.23 | 23749301 | |
114 | Acetylation | HEHYLAYKAGIQRGD HHHHHHHHCCCCCCC | 34.23 | 22865919 | |
157 | Ubiquitination | NNDYQIAKAKYYAKK CCCHHHHHHHHHHHH | 47.22 | 23749301 | |
175 | Acetylation | SDQMDFVKGDFMKMD HHHCHHHCCCCCCCC | 53.40 | 24489116 | |
190 | Ubiquitination | FEENTFDKVYAIEAT CCCCCCCEEEEEEEE | 32.71 | 23749301 | |
202 | Acetylation | EATCHAPKLEGVYSE EEEECCCCCHHHHHH | 61.01 | 24489116 | |
240 | Ubiquitination | ENNPEHRKIAYEIEL CCCHHHHHEEEEEEC | 33.33 | 23749301 | |
253 | Ubiquitination | ELGDGIPKMFHVDVA ECCCCCCCCHHHHHH | 52.88 | 17644757 | |
295 | Ubiquitination | YPLTGEWKYVQNLAN EECCCCHHHHHHHHH | 31.10 | 17644757 | |
326 | Ubiquitination | AMVTVMEKLGLAPEG HHHHHHHHHCCCCCC | 29.74 | 17644757 | |
335 | Ubiquitination | GLAPEGSKEVTAALE CCCCCCCHHHHHHHH | 68.04 | 23749301 | |
335 | Acetylation | GLAPEGSKEVTAALE CCCCCCCHHHHHHHH | 68.04 | 24489116 | |
353 | Ubiquitination | VGLVAGGKSKLFTPM HHHHHCCCCCCCCCE | 43.42 | 17644757 | |
355 | Ubiquitination | LVAGGKSKLFTPMML HHHCCCCCCCCCEEE | 51.62 | 23749301 | |
358 | Phosphorylation | GGKSKLFTPMMLFVA CCCCCCCCCEEEEEE | 22.25 | 19779198 | |
367 | Ubiquitination | MMLFVARKPENAETP EEEEEECCCCCCCCC | 47.12 | 23749301 | |
373 | Phosphorylation | RKPENAETPSQTSQE CCCCCCCCCCCCCHH | 26.32 | 22369663 | |
375 | Phosphorylation | PENAETPSQTSQEAT CCCCCCCCCCCHHHC | 54.21 | 22369663 | |
377 | Phosphorylation | NAETPSQTSQEATQ- CCCCCCCCCHHHCC- | 36.39 | 22369663 | |
378 | Phosphorylation | AETPSQTSQEATQ-- CCCCCCCCHHHCC-- | 20.56 | 22369663 | |
382 | Phosphorylation | SQTSQEATQ------ CCCCHHHCC------ | 33.78 | 22369663 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of ERG6_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ERG6_YEAST !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of ERG6_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"Proteome studies of Saccharomyces cerevisiae: identification andcharacterization of abundant proteins."; Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,Kobayashi R., Schwender B., Volpe T., Anderson D.S.,Mesquita-Fuentes R., Payne W.E.; Electrophoresis 18:1347-1360(1997). Cited for: ACETYLATION AT SER-2. | |
Phosphorylation | |
Reference | PubMed |
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99 AND THR-373, AND MASSSPECTROMETRY. | |
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae."; Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.; Nat. Biotechnol. 20:301-305(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375 AND SER-378, ANDMASS SPECTROMETRY. |