UniProt ID | KCC1_YEAST | |
---|---|---|
UniProt AC | P27466 | |
Protein Name | Calcium/calmodulin-dependent protein kinase I | |
Gene Name | CMK1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 446 | |
Subcellular Localization | ||
Protein Description | Important in cellular regulation.. | |
Protein Sequence | MDDKVSEKESSPKQTEEDSEGKMAHVQPASYVNKKKYVFGKTLGAGTFGVVRQAKNTETGEDVAVKILIKKALKGNKVQLEALYDELDILQRLHHPNIVAFKDWFESKDKFYIITQLAKGGELFDRILKKGKFTEEDAVRILVEILSAVKYMHSQNIVHRDLKPENLLYIDKSDESPLVVADFGIAKRLKSDEELLYKPAGSLGYVAPEVLTQDGHGKPCDIWSIGVITYTLLCGYSAFRAERVQDFLDECTTGEYPVKFHRPYWDSVSNKAKQFILKALNLDPSKRPTAAELLEDPWIICTELKTHNLLPGLKEGLDARQKFRNSVERVRLNMKIQKLRDLYLEQTESDSDFDEGSQANGSVPPLKATDTSQLSKKLSEEEQSKLKSELTSKAFAQLVNTVLAEKEKFLNINRVCSSDSDLPGSDIKSLDEAKEKPEGKDTKTEE | |
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 |
---|---|---|---|---|---|
6 | Phosphorylation | --MDDKVSEKESSPK --CCCCCCCCCCCCC | 49.01 | 29136822 | |
10 | Phosphorylation | DKVSEKESSPKQTEE CCCCCCCCCCCCCCC | 64.11 | 29136822 | |
11 | Phosphorylation | KVSEKESSPKQTEED CCCCCCCCCCCCCCC | 36.89 | 25752575 | |
13 | Ubiquitination | SEKESSPKQTEEDSE CCCCCCCCCCCCCCC | 72.33 | 24961812 | |
22 | Ubiquitination | TEEDSEGKMAHVQPA CCCCCCCCCCCCCCH | 28.94 | 24961812 | |
41 | Acetylation | KKKYVFGKTLGAGTF CCEEEEEEECCCCCH | 29.16 | 24489116 | |
42 | Phosphorylation | KKYVFGKTLGAGTFG CEEEEEEECCCCCHH | 30.70 | 27017623 | |
57 | Phosphorylation | VVRQAKNTETGEDVA EEEECCCCCCCHHHH | 33.93 | 27017623 | |
110 | Acetylation | DWFESKDKFYIITQL HHHHCCCCEEEEEEH | 43.75 | 24489116 | |
173 | Phosphorylation | NLLYIDKSDESPLVV HCEEEECCCCCCEEE | 42.75 | 27017623 | |
176 | Phosphorylation | YIDKSDESPLVVADF EEECCCCCCEEEEEC | 28.64 | 27017623 | |
271 | Acetylation | YWDSVSNKAKQFILK CHHHCCHHHHHHHHH | 49.83 | 22865919 | |
343 | Phosphorylation | IQKLRDLYLEQTESD HHHHHHHHHHCCCCC | 16.69 | 22369663 | |
347 | Phosphorylation | RDLYLEQTESDSDFD HHHHHHCCCCCCCCC | 28.25 | 22369663 | |
349 | Phosphorylation | LYLEQTESDSDFDEG HHHHCCCCCCCCCCC | 45.89 | 22369663 | |
351 | Phosphorylation | LEQTESDSDFDEGSQ HHCCCCCCCCCCCCC | 49.83 | 20377248 | |
357 | Phosphorylation | DSDFDEGSQANGSVP CCCCCCCCCCCCCCC | 24.87 | 29734811 | |
362 | Phosphorylation | EGSQANGSVPPLKAT CCCCCCCCCCCCCCC | 31.12 | 22369663 | |
369 | Phosphorylation | SVPPLKATDTSQLSK CCCCCCCCCHHHHHH | 37.92 | 28889911 | |
371 | Phosphorylation | PPLKATDTSQLSKKL CCCCCCCHHHHHHHC | 17.64 | 25521595 | |
372 | Phosphorylation | PLKATDTSQLSKKLS CCCCCCHHHHHHHCC | 31.75 | 24961812 | |
375 | Phosphorylation | ATDTSQLSKKLSEEE CCCHHHHHHHCCHHH | 21.80 | 24961812 | |
379 | Phosphorylation | SQLSKKLSEEEQSKL HHHHHHCCHHHHHHH | 52.41 | 23749301 | |
384 | Phosphorylation | KLSEEEQSKLKSELT HCCHHHHHHHHHHHH | 43.14 | 30377154 | |
417 | Phosphorylation | LNINRVCSSDSDLPG HCCCCCCCCCCCCCC | 34.03 | 22369663 | |
418 | Phosphorylation | NINRVCSSDSDLPGS CCCCCCCCCCCCCCC | 35.69 | 22369663 | |
420 | Phosphorylation | NRVCSSDSDLPGSDI CCCCCCCCCCCCCCC | 42.89 | 22369663 | |
425 | Phosphorylation | SDSDLPGSDIKSLDE CCCCCCCCCCCCHHH | 33.93 | 22890988 | |
429 | Phosphorylation | LPGSDIKSLDEAKEK CCCCCCCCHHHHHHC | 41.19 | 17330950 |
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 KCC1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KCC1_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 KCC1_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-379; SER-417; SER-418;SER-420 AND SER-429, AND MASS SPECTROMETRY. | |
"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-417; SER-420 ANDSER-429, AND MASS SPECTROMETRY. |