| UniProt ID | RMRP_YEAST | |
|---|---|---|
| UniProt AC | P40993 | |
| Protein Name | Ribonuclease MRP protein subunit SNM1 | |
| Gene Name | SNM1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 198 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Essential component of the MRP ribonucleoprotein endoribonuclease that cleaves mitochondrial primer RNA sequences.. | |
| Protein Sequence | MNKDQAEKYQERSLRQKYNLLHVLPTLNSRALSGLYYKNFHNSVKRYQIMLPEQLKSGKFCSHCGCVYVPNFNASLQLTTNTEQGDSDELGGESMEGPKKCIQVNCLNCEKSKLFEWKSEFVVPTFGQDVSPMINSTSSGKVSYAVKKPQKSKTSTGKERSKKRKLNSLTNLLSKRNQEKKMEKKKSSSLSLESFMKS | |
| 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 |
|---|---|---|---|---|---|
| 147 | Acetylation | GKVSYAVKKPQKSKT CEEEEEEECCCCCCC | 51.03 | 25381059 | |
| 148 | Acetylation | KVSYAVKKPQKSKTS EEEEEEECCCCCCCC | 46.19 | 25381059 | |
| 168 | Phosphorylation | SKKRKLNSLTNLLSK HHHHHHHHHHHHHHH | 47.18 | 22369663 | |
| 170 | Phosphorylation | KRKLNSLTNLLSKRN HHHHHHHHHHHHHHH | 24.52 | 21440633 | |
| 174 | Phosphorylation | NSLTNLLSKRNQEKK HHHHHHHHHHHHHHH | 32.51 | 22369663 | |
| 187 | Phosphorylation | KKMEKKKSSSLSLES HHHHHHHHCCCCHHH | 33.76 | 28889911 | |
| 188 | Phosphorylation | KMEKKKSSSLSLESF HHHHHHHCCCCHHHH | 44.15 | 21440633 | |
| 189 | Phosphorylation | MEKKKSSSLSLESFM HHHHHHCCCCHHHHH | 29.12 | 24961812 |
| 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 RMRP_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RMRP_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 RMRP_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| 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-168 AND SER-188, ANDMASS SPECTROMETRY. | |
| "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-168, AND MASSSPECTROMETRY. | |
