UniProt ID | CHK1_YEAST | |
---|---|---|
UniProt AC | P38147 | |
Protein Name | Serine/threonine-protein kinase CHK1 | |
Gene Name | CHK1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 527 | |
Subcellular Localization | Nucleus. | |
Protein Description | Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest and activation of DNA repair in response to the presence of DNA damage or unreplicated DNA. May also negatively regulate cell cycle progression during unperturbed cell cycles. Controls phosphorylation and abundance of PDS1 to prevent anaphase entry. Also helps prevent mitotic exit.. | |
Protein Sequence | MSLSQVSPLPHIKDVVLGDTVGQGAFACVKNAHLQMDPSIILAVKFIHVPTCKKMGLSDKDITKEVVLQSKCSKHPNVLRLIDCNVSKEYMWIILEMADGGDLFDKIEPDVGVDSDVAQFYFQQLVSAINYLHVECGVAHRDIKPENILLDKNGNLKLADFGLASQFRRKDGTLRVSMDQRGSPPYMAPEVLYSEEGYYADRTDIWSIGILLFVLLTGQTPWELPSLENEDFVFFIENDGNLNWGPWSKIEFTHLNLLRKILQPDPNKRVTLKALKLHPWVLRRASFSGDDGLCNDPELLAKKLFSHLKVSLSNENYLKFTQDTNSNNRYISTQPIGNELAELEHDSMHFQTVSNTQRAFTSYDSNTNYNSGTGMTQEAKWTQFISYDIAALQFHSDENDCNELVKRHLQFNPNKLTKFYTLQPMDVLLPILEKALNLSQIRVKPDLFANFERLCELLGYDNVFPLIINIKTKSNGGYQLCGSISIIKIEEELKSVGFERKTGDPLEWRRLFKKISTICRDIILIPN | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSLSQVSPL ------CCHHHCCCC | 36.41 | 30377154 | |
4 | Phosphorylation | ----MSLSQVSPLPH ----CCHHHCCCCCC | 22.64 | 30377154 | |
144 | Ubiquitination | GVAHRDIKPENILLD CCCCCCCCHHHEEEC | 51.04 | 23749301 | |
183 | Phosphorylation | VSMDQRGSPPYMAPE EEECCCCCCCCCCCC | 25.53 | 28889911 | |
286 | Phosphorylation | PWVLRRASFSGDDGL HHHHHHCCCCCCCCC | 20.38 | 23749301 | |
288 | Phosphorylation | VLRRASFSGDDGLCN HHHHCCCCCCCCCCC | 38.53 | 28889911 | |
321 | Phosphorylation | NENYLKFTQDTNSNN CCCCEEEEECCCCCC | 24.77 | 18984588 | |
333 | Phosphorylation | SNNRYISTQPIGNEL CCCCEEEECCCCCHH | 28.89 | 18984588 | |
356 | Phosphorylation | HFQTVSNTQRAFTSY EEEECCCCCCEEECC | 16.36 | 18984588 | |
371 | Phosphorylation | DSNTNYNSGTGMTQE CCCCCCCCCCCCCCC | 27.63 | 27017623 | |
373 | Phosphorylation | NTNYNSGTGMTQEAK CCCCCCCCCCCCCEE | 24.49 | 28889911 | |
376 | Phosphorylation | YNSGTGMTQEAKWTQ CCCCCCCCCCEEEEE | 25.30 | 27017623 | |
382 | Phosphorylation | MTQEAKWTQFISYDI CCCCEEEEEEEEEEE | 16.94 | 18984588 | |
439 | Phosphorylation | LEKALNLSQIRVKPD HHHHCCHHHCCCCHH | 23.61 | 30377154 |
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 CHK1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CHK1_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 CHK1_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 THR-373, AND MASSSPECTROMETRY. |