| UniProt ID | CMS1_YEAST | |
|---|---|---|
| UniProt AC | Q07897 | |
| Protein Name | Protein CMS1 | |
| Gene Name | CMS1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 291 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | May play a role in the regulation of DNA replication and cell cycle control.. | |
| Protein Sequence | MSNPDDLDDGLAYDFDAEHEVIFDAKDGSPPTKKVQKRSIEQDDDDVDDIDGKKEERNSEDDSNRPISKRQKKLQKKSKLIEKKKEESQYIVSQRKALPASSPEKIIEYLTTLIREKNPDLSVLELEELYFKRNDFLSTEKFDAERRLSNFPAFIQKFSVAPKKIVFSMSNIRVADVYRSLNGGKNCVKLFSKSKLKDDIATVERLLTDSSKKSNKNKDSLYFIATPTRMQKIIEATDLLFQGKEKLDIILDASYLDPKDNTILSFENAAVLCQVLKTFLNKKSSVKILLY | |
| 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 | ------MSNPDDLDD ------CCCHHHCCC | 58.00 | 28152593 | |
| 29 | Phosphorylation | IFDAKDGSPPTKKVQ EEECCCCCCCCHHHH | 37.53 | 25752575 | |
| 39 | Phosphorylation | TKKVQKRSIEQDDDD CHHHHCCCCCCCCCC | 37.20 | 17563356 | |
| 53 | Acetylation | DVDDIDGKKEERNSE CCCCCCCCCHHCCCC | 53.95 | 24489116 | |
| 54 | Acetylation | VDDIDGKKEERNSED CCCCCCCCHHCCCCC | 71.04 | 24489116 | |
| 59 | Phosphorylation | GKKEERNSEDDSNRP CCCHHCCCCCCCCCC | 48.93 | 19823750 | |
| 63 | Phosphorylation | ERNSEDDSNRPISKR HCCCCCCCCCCCHHH | 47.24 | 19795423 | |
| 68 | Phosphorylation | DDSNRPISKRQKKLQ CCCCCCCHHHHHHHH | 25.19 | 27214570 | |
| 69 | Acetylation | DSNRPISKRQKKLQK CCCCCCHHHHHHHHH | 60.61 | 25381059 | |
| 88 | Phosphorylation | IEKKKEESQYIVSQR HHHHHHHHHHHHHHH | 29.40 | 30377154 | |
| 93 | Phosphorylation | EESQYIVSQRKALPA HHHHHHHHHHCCCCC | 18.08 | 27017623 | |
| 141 | Acetylation | NDFLSTEKFDAERRL CCCCCCCCCCHHHHH | 48.94 | 24489116 | |
| 157 | Acetylation | NFPAFIQKFSVAPKK CCHHHHHHHCCCCCE | 34.49 | 24489116 | |
| 168 | Phosphorylation | APKKIVFSMSNIRVA CCCEEEEEECCCCHH | 15.48 | 27017623 | |
| 170 | Phosphorylation | KKIVFSMSNIRVADV CEEEEEECCCCHHHH | 28.10 | 27017623 | |
| 178 | Phosphorylation | NIRVADVYRSLNGGK CCCHHHHHHHHCCCC | 8.60 | 27017623 | |
| 195 | Acetylation | VKLFSKSKLKDDIAT HHHHCCCCCHHHHHH | 64.39 | 24489116 | |
| 197 | Acetylation | LFSKSKLKDDIATVE HHCCCCCHHHHHHHH | 58.03 | 24489116 | |
| 216 | Acetylation | DSSKKSNKNKDSLYF CCCCCCCCCCCCEEE | 72.90 | 24489116 | |
| 218 | Acetylation | SKKSNKNKDSLYFIA CCCCCCCCCCEEEEE | 50.75 | 24489116 | |
| 218 | Succinylation | SKKSNKNKDSLYFIA CCCCCCCCCCEEEEE | 50.75 | 23954790 | |
| 232 | Acetylation | ATPTRMQKIIEATDL ECHHHHHHHHHHHHH | 35.99 | 24489116 | |
| 244 | Acetylation | TDLLFQGKEKLDIIL HHHHHCCHHHCCEEE | 40.67 | 24489116 |
| 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 CMS1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CMS1_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 CMS1_YEAST !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of CMS1_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-59, 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-39 AND SER-59, AND MASSSPECTROMETRY. | |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, AND MASSSPECTROMETRY. | |