| UniProt ID | OPI1_YEAST | |
|---|---|---|
| UniProt AC | P21957 | |
| Protein Name | Transcriptional repressor OPI1 | |
| Gene Name | OPI1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 404 | |
| Subcellular Localization | Endoplasmic reticulum . Nucleus . Maintained at the endoplasmic reticulum by SCS2 (PubMed:12727870). In response to elevated inositol levels, translocates to the nucleus (PubMed:15192221). | |
| Protein Description | Negative regulator of the transcriptional complex INO2-INO4 in response to phospholipid precursor availability. When precursors become limiting, OPI1 is retained at the endoplasmic reticulum (ER) and INO2-INO4 activates INO1 and other genes required for phospholipid biosynthesis, whereas abundant precursor availability results in targeting of OPI1 to the nucleus to repress transcription of these genes. Binds directly to phosphatidic acid, which is required for ER targeting and may act as sensing mechanism for precursor availability, as phosphatidic acid becomes rapidly depleted upon phospholipid biosynthesis.. | |
| Protein Sequence | MSENQRLGLSEEEVEAAEVLGVLKQSCRQKSQPSEDVSQADKMPASESSTTPLNILDRVSNKIISNVVTFYDEINTNKRPLKSIGRLLDDDDDEHDDYDYNDDEFFTNKRQKLSRAIAKGKDNLKEYKLNMSIESKKRLVTCLHLLKLANKQLSDKISCLQDLVEKEQVHPLHKQDGNARTTTGAGEDETSSDEDDDDEEFFDASEQVNASEQSIVVKMEVVGTVKKVYSLISKFTANSLPEPARSQVRESLLNLPTNWFDSVHSTSLPHHASFHYANCEEQKVEQQQQQQQQQQQQQLLQQQLLQQQQQKRNKDGDDSASPSSSVTANGKVLILAKESLEMVRNVMGVVDSTLGKAEEWVKQKQEVKEMIRERFLQQQQQYRQQQQKDGNYVKPSQDNVDSKD | |
| 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 |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MSENQRLGL ------CCHHHCCCC | 45.30 | 19823750 | |
| 10 | Phosphorylation | ENQRLGLSEEEVEAA HHHCCCCCHHHHHHH | 40.96 | 22369663 | |
| 24 | Acetylation | AEVLGVLKQSCRQKS HHHHHHHHHHHHHCC | 37.45 | 25381059 | |
| 24 | Ubiquitination | AEVLGVLKQSCRQKS HHHHHHHHHHHHHCC | 37.45 | 17644757 | |
| 26 | Phosphorylation | VLGVLKQSCRQKSQP HHHHHHHHHHHCCCC | 15.07 | 11395523 | |
| 31 | Phosphorylation | KQSCRQKSQPSEDVS HHHHHHCCCCCCCCH | 38.70 | 28889911 | |
| 38 | Phosphorylation | SQPSEDVSQADKMPA CCCCCCCHHHHCCCC | 31.79 | 23749301 | |
| 42 | Acetylation | EDVSQADKMPASESS CCCHHHHCCCCCCCC | 50.20 | 24489116 | |
| 46 | Phosphorylation | QADKMPASESSTTPL HHHCCCCCCCCCCCC | 31.94 | 23749301 | |
| 48 | Phosphorylation | DKMPASESSTTPLNI HCCCCCCCCCCCCHH | 30.41 | 27017623 | |
| 49 | Phosphorylation | KMPASESSTTPLNIL CCCCCCCCCCCCHHH | 32.04 | 28889911 | |
| 51 | Phosphorylation | PASESSTTPLNILDR CCCCCCCCCCHHHHH | 27.94 | 21551504 | |
| 82 | Acetylation | NTNKRPLKSIGRLLD HCCCCCCHHHCCCCC | 42.59 | 25381059 | |
| 109 | Ubiquitination | DDEFFTNKRQKLSRA CCHHHHHHHHHHHHH | 53.82 | 17644757 | |
| 109 | Acetylation | DDEFFTNKRQKLSRA CCHHHHHHHHHHHHH | 53.82 | 24489116 | |
| 147 | Ubiquitination | VTCLHLLKLANKQLS HHHHHHHHHHCHHHH | 52.49 | 17644757 | |
| 151 | Ubiquitination | HLLKLANKQLSDKIS HHHHHHCHHHHHHHH | 47.19 | 23749301 | |
| 205 | Phosphorylation | DEEFFDASEQVNASE CHHHCCHHHHCCCCC | 30.33 | 28889911 | |
| 224 | Phosphorylation | VKMEVVGTVKKVYSL EEEEEECHHHHHHHH | 19.97 | 27017623 | |
| 227 | Ubiquitination | EVVGTVKKVYSLISK EEECHHHHHHHHHHH | 41.91 | 23749301 | |
| 229 | Phosphorylation | VGTVKKVYSLISKFT ECHHHHHHHHHHHHH | 13.46 | 27017623 | |
| 230 | Phosphorylation | GTVKKVYSLISKFTA CHHHHHHHHHHHHHH | 23.39 | 17563356 | |
| 233 | Phosphorylation | KKVYSLISKFTANSL HHHHHHHHHHHHCCC | 27.32 | 27017623 | |
| 234 | Ubiquitination | KVYSLISKFTANSLP HHHHHHHHHHHCCCC | 39.48 | 23749301 | |
| 234 | Acetylation | KVYSLISKFTANSLP HHHHHHHHHHHCCCC | 39.48 | 24489116 | |
| 239 | Phosphorylation | ISKFTANSLPEPARS HHHHHHCCCCHHHHH | 42.72 | 28889911 | |
| 251 | Phosphorylation | ARSQVRESLLNLPTN HHHHHHHHHHCCCCC | 27.82 | 28889911 | |
| 314 | Ubiquitination | QQQQKRNKDGDDSAS HHHHHHCCCCCCCCC | 68.10 | 23749301 | |
| 319 | Phosphorylation | RNKDGDDSASPSSSV HCCCCCCCCCCCCCC | 35.07 | 28889911 | |
| 321 | Phosphorylation | KDGDDSASPSSSVTA CCCCCCCCCCCCCCC | 29.30 | 22369663 | |
| 323 | Phosphorylation | GDDSASPSSSVTANG CCCCCCCCCCCCCCC | 32.52 | 22369663 | |
| 324 | Phosphorylation | DDSASPSSSVTANGK CCCCCCCCCCCCCCE | 32.01 | 22369663 | |
| 325 | Phosphorylation | DSASPSSSVTANGKV CCCCCCCCCCCCCEE | 28.02 | 22369663 | |
| 388 | Ubiquitination | QYRQQQQKDGNYVKP HHHHHHHHCCCCCCC | 64.36 | 17644757 | |
| 394 | Ubiquitination | QKDGNYVKPSQDNVD HHCCCCCCCCCCCCC | 28.70 | 23749301 | |
| 396 | Phosphorylation | DGNYVKPSQDNVDSK CCCCCCCCCCCCCCC | 44.44 | 25752575 | |
| 403 | Ubiquitination | SQDNVDSKD------ CCCCCCCCC------ | 64.09 | 17644757 |
| 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 OPI1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of OPI1_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 OPI1_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-49 AND SER-230, AND MASSSPECTROMETRY. | |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, 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-10, AND MASSSPECTROMETRY. | |
