| UniProt ID | CP51_YEAST | |
|---|---|---|
| UniProt AC | P10614 | |
| Protein Name | Lanosterol 14-alpha demethylase | |
| Gene Name | ERG11 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 530 | |
| Subcellular Localization |
Membrane Single-pass membrane protein. |
|
| Protein Description | Catalyzes C14-demethylation of lanosterol which is critical for ergosterol biosynthesis. It transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol.. | |
| Protein Sequence | MSATKSIVGEALEYVNIGLSHFLALPLAQRISLIIIIPFIYNIVWQLLYSLRKDRPPLVFYWIPWVGSAVVYGMKPYEFFEECQKKYGDIFSFVLLGRVMTVYLGPKGHEFVFNAKLADVSAEAAYAHLTTPVFGKGVIYDCPNSRLMEQKKFVKGALTKEAFKSYVPLIAEEVYKYFRDSKNFRLNERTTGTIDVMVTQPEMTIFTASRSLLGKEMRAKLDTDFAYLYSDLDKGFTPINFVFPNLPLEHYRKRDHAQKAISGTYMSLIKERRKNNDIQDRDLIDSLMKNSTYKDGVKMTDQEIANLLIGVLMGGQHTSAATSAWILLHLAERPDVQQELYEEQMRVLDGGKKELTYDLLQEMPLLNQTIKETLRMHHPLHSLFRKVMKDMHVPNTSYVIPAGYHVLVSPGYTHLRDEYFPNAHQFNIHRWNKDSASSYSVGEEVDYGFGAISKGVSSPYLPFGGGRHRCIGEHFAYCQLGVLMSIFIRTLKWHYPEGKTVPPPDFTSMVTLPTGPAKIIWEKRNPEQKI | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 86 | Ubiquitination | FFEECQKKYGDIFSF HHHHHHHHHHCHHHH | 28.70 | 17644757 | |
| 87 | Phosphorylation | FEECQKKYGDIFSFV HHHHHHHHHCHHHHH | 27.37 | 19823750 | |
| 92 | Phosphorylation | KKYGDIFSFVLLGRV HHHHCHHHHHHHCCE | 18.12 | 19823750 | |
| 101 | Phosphorylation | VLLGRVMTVYLGPKG HHHCCEEEEEECCCC | 11.80 | 19823750 | |
| 103 | Phosphorylation | LGRVMTVYLGPKGHE HCCEEEEEECCCCCC | 9.22 | 19823750 | |
| 107 | Ubiquitination | MTVYLGPKGHEFVFN EEEEECCCCCCEEEE | 71.72 | 23749301 | |
| 116 | Ubiquitination | HEFVFNAKLADVSAE CCEEEEEECCCCCHH | 45.36 | 23749301 | |
| 136 | Ubiquitination | LTTPVFGKGVIYDCP CCCCCCCCCEEEECC | 38.24 | 23749301 | |
| 151 | Ubiquitination | NSRLMEQKKFVKGAL CCHHHHHHHHHHHHC | 34.57 | 22817900 | |
| 152 | Ubiquitination | SRLMEQKKFVKGALT CHHHHHHHHHHHHCC | 55.90 | 22817900 | |
| 155 | Ubiquitination | MEQKKFVKGALTKEA HHHHHHHHHHCCHHH | 41.41 | 23749301 | |
| 160 | Ubiquitination | FVKGALTKEAFKSYV HHHHHCCHHHHHHHH | 48.14 | 23749301 | |
| 164 | Acetylation | ALTKEAFKSYVPLIA HCCHHHHHHHHHHHH | 48.18 | 24489116 | |
| 164 | Ubiquitination | ALTKEAFKSYVPLIA HCCHHHHHHHHHHHH | 48.18 | 23749301 | |
| 176 | Ubiquitination | LIAEEVYKYFRDSKN HHHHHHHHHHHHCCC | 42.99 | 23749301 | |
| 182 | Ubiquitination | YKYFRDSKNFRLNER HHHHHHCCCEECCCC | 65.48 | 15699485 | |
| 215 | Ubiquitination | ASRSLLGKEMRAKLD ECHHHCCHHHHHHCC | 48.59 | 23749301 | |
| 220 | Ubiquitination | LGKEMRAKLDTDFAY CCHHHHHHCCCCHHH | 36.21 | 24961812 | |
| 220 | Acetylation | LGKEMRAKLDTDFAY CCHHHHHHCCCCHHH | 36.21 | 24489116 | |
| 234 | Ubiquitination | YLYSDLDKGFTPINF HHHHCCCCCCCCEEE | 64.32 | 17644757 | |
| 253 | Ubiquitination | LPLEHYRKRDHAQKA CCHHHHHHHHHHHHH | 55.82 | 17644757 | |
| 259 | Ubiquitination | RKRDHAQKAISGTYM HHHHHHHHHHHHHHH | 48.77 | 24961812 | |
| 262 | Phosphorylation | DHAQKAISGTYMSLI HHHHHHHHHHHHHHH | 29.91 | 21440633 | |
| 264 | Phosphorylation | AQKAISGTYMSLIKE HHHHHHHHHHHHHHH | 14.84 | 19823750 | |
| 265 | Phosphorylation | QKAISGTYMSLIKER HHHHHHHHHHHHHHH | 6.55 | 19823750 | |
| 267 | Phosphorylation | AISGTYMSLIKERRK HHHHHHHHHHHHHHH | 19.27 | 19823750 | |
| 270 | Acetylation | GTYMSLIKERRKNND HHHHHHHHHHHHCCC | 50.92 | 24489116 | |
| 270 | Ubiquitination | GTYMSLIKERRKNND HHHHHHHHHHHHCCC | 50.92 | 23749301 | |
| 274 | Ubiquitination | SLIKERRKNNDIQDR HHHHHHHHCCCCCCH | 67.34 | 24961812 | |
| 289 | Ubiquitination | DLIDSLMKNSTYKDG HHHHHHHHCCCCCCC | 53.70 | 24961812 | |
| 294 | Ubiquitination | LMKNSTYKDGVKMTD HHHCCCCCCCCCCCH | 48.36 | 23749301 | |
| 298 | Ubiquitination | STYKDGVKMTDQEIA CCCCCCCCCCHHHHH | 41.43 | 22817900 | |
| 353 | Ubiquitination | RVLDGGKKELTYDLL HHHCCCCCCCCHHHH | 62.32 | 22106047 | |
| 371 | Ubiquitination | PLLNQTIKETLRMHH CCHHHHHHHHHHHCC | 48.29 | 23749301 | |
| 433 | Ubiquitination | FNIHRWNKDSASSYS CEEEECCCCCCCCCC | 46.21 | 23749301 | |
| 435 | Phosphorylation | IHRWNKDSASSYSVG EEECCCCCCCCCCCC | 31.49 | 24961812 | |
| 437 | Phosphorylation | RWNKDSASSYSVGEE ECCCCCCCCCCCCCC | 33.49 | 24961812 | |
| 438 | Phosphorylation | WNKDSASSYSVGEEV CCCCCCCCCCCCCCC | 22.57 | 24961812 | |
| 440 | Phosphorylation | KDSASSYSVGEEVDY CCCCCCCCCCCCCCC | 26.12 | 24961812 | |
| 454 | Ubiquitination | YGFGAISKGVSSPYL CCCCCCCCCCCCCCC | 58.16 | 23749301 | |
| 457 | Phosphorylation | GAISKGVSSPYLPFG CCCCCCCCCCCCCCC | 33.97 | 27214570 | |
| 458 | Phosphorylation | AISKGVSSPYLPFGG CCCCCCCCCCCCCCC | 18.37 | 17330950 | |
| 492 | Ubiquitination | SIFIRTLKWHYPEGK HHHHHHHCCCCCCCC | 31.17 | 17644757 | |
| 499 | Ubiquitination | KWHYPEGKTVPPPDF CCCCCCCCCCCCCCC | 44.69 | 17644757 | |
| 507 | Phosphorylation | TVPPPDFTSMVTLPT CCCCCCCCCEEEECC | 24.24 | 23749301 | |
| 508 | Phosphorylation | VPPPDFTSMVTLPTG CCCCCCCCEEEECCC | 15.96 | 23749301 | |
| 518 | Ubiquitination | TLPTGPAKIIWEKRN EECCCCCEEEEECCC | 37.55 | 15699485 | |
| 523 | Ubiquitination | PAKIIWEKRNPEQKI CCEEEEECCCHHHCC | 42.34 | 17644757 | |
| 529 | Ubiquitination | EKRNPEQKI------ ECCCHHHCC------ | 49.04 | 23749301 |
| 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 CP51_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CP51_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 CP51_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| 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-458, AND MASSSPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, AND MASSSPECTROMETRY. | |
