UniProt ID | RFM1_YEAST | |
---|---|---|
UniProt AC | Q12192 | |
Protein Name | Repression factor of MSEs protein 1 | |
Gene Name | RFM1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 310 | |
Subcellular Localization | Nucleus. | |
Protein Description | Tethering factor required for histone deacetylase HST1-mediated repression. Probably involved in targeting HST1 to a subset of SUM1-regulated genes.. | |
Protein Sequence | MSTNTEIIKNSDLQSLINDKRRLINEIKDFNKSIKPLEFESYQDYFLIKTFKKGISASGHVDIDSLRNKEYGIYYKKIKRNSTQEVGEPIPRNTSSSSSSTRSNSSADISDTEYSGENTPTTTGAASRRRRTRSRAIQRENSLPASLPSISEANANNDDVTISEINGSELPFPIPISEVENIDIASDITERDGIRRRSSRISERDKRRSQSRLGSEEDEEGDGHDGDEGETKIQDLYESLVPKILESRRRSDWILPPKARYTPEKQMRTKPSFKSIKINELVGNKRIRSILSRFEGGVAGIRKRDWDSTQ | |
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 |
---|---|---|---|---|---|
82 | Phosphorylation | YKKIKRNSTQEVGEP EEECCCCCCCCCCCC | 35.19 | 23749301 | |
83 | Phosphorylation | KKIKRNSTQEVGEPI EECCCCCCCCCCCCC | 32.09 | 30377154 | |
103 | Phosphorylation | SSSSSTRSNSSADIS CCCCCCCCCCCCCCC | 40.95 | 28132839 | |
105 | Phosphorylation | SSSTRSNSSADISDT CCCCCCCCCCCCCCC | 28.31 | 19779198 | |
106 | Phosphorylation | SSTRSNSSADISDTE CCCCCCCCCCCCCCC | 33.92 | 23749301 | |
110 | Phosphorylation | SNSSADISDTEYSGE CCCCCCCCCCCCCCC | 38.74 | 28152593 | |
112 | Phosphorylation | SSADISDTEYSGENT CCCCCCCCCCCCCCC | 29.99 | 28152593 | |
114 | Phosphorylation | ADISDTEYSGENTPT CCCCCCCCCCCCCCC | 24.86 | 27738172 | |
119 | Phosphorylation | TEYSGENTPTTTGAA CCCCCCCCCCCCCHH | 20.08 | 23749301 | |
186 | Phosphorylation | VENIDIASDITERDG EECEECCCCCCHHHC | 29.85 | 27214570 | |
209 | Phosphorylation | SERDKRRSQSRLGSE CHHHHHHHHHHCCCC | 36.22 | 21551504 | |
211 | Phosphorylation | RDKRRSQSRLGSEED HHHHHHHHHCCCCCC | 30.62 | 23749301 | |
215 | Phosphorylation | RSQSRLGSEEDEEGD HHHHHCCCCCCCCCC | 42.26 | 19823750 | |
231 | Phosphorylation | HDGDEGETKIQDLYE CCCCCCCHHHHHHHH | 44.28 | 19823750 | |
274 | Acetylation | MRTKPSFKSIKINEL HCCCCCCCCCCHHHH | 56.46 | 25381059 | |
285 | Acetylation | INELVGNKRIRSILS HHHHHCCHHHHHHHH | 43.18 | 25381059 |
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 RFM1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RFM1_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 RFM1_YEAST !! |
Kegg Drug | ||||||
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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-215, 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-215, AND MASSSPECTROMETRY. |