| UniProt ID | CALM_YEAST | |
|---|---|---|
| UniProt AC | P06787 | |
| Protein Name | Calmodulin | |
| Gene Name | CMD1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 147 | |
| Subcellular Localization | Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body . | |
| Protein Description | Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. Component of the spindle pole body (SPB) required for the proper execution of spindle pole body (SPB) duplication.. | |
| Protein Sequence | MSSNLTEEQIAEFKEAFALFDKDNNGSISSSELATVMRSLGLSPSEAEVNDLMNEIDVDGNHQIEFSEFLALMSRQLKSNDSEQELLEAFKVFDKNGDGLISAAELKHVLTSIGEKLTDAEVDDMLREVSDGSGEINIQQFAALLSK | |
| 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 | ------MSSNLTEEQ ------CCCCCCHHH | 28.12 | 24909858 | |
| 27 | Phosphorylation | FDKDNNGSISSSELA HCCCCCCCCCHHHHH | 22.78 | 24909858 | |
| 29 | Phosphorylation | KDNNGSISSSELATV CCCCCCCCHHHHHHH | 29.52 | 24909858 | |
| 31 | Phosphorylation | NNGSISSSELATVMR CCCCCCHHHHHHHHH | 29.82 | 25752575 | |
| 35 | Phosphorylation | ISSSELATVMRSLGL CCHHHHHHHHHHCCC | 27.71 | 23749301 | |
| 39 | Phosphorylation | ELATVMRSLGLSPSE HHHHHHHHCCCCCHH | 14.53 | 21700874 | |
| 43 | Phosphorylation | VMRSLGLSPSEAEVN HHHHCCCCCHHHHHH | 25.28 | 21700874 | |
| 45 | Phosphorylation | RSLGLSPSEAEVNDL HHCCCCCHHHHHHHH | 46.17 | 21700874 | |
| 67 | Phosphorylation | GNHQIEFSEFLALMS CCCEEEHHHHHHHHH | 18.04 | 21700874 | |
| 74 | Phosphorylation | SEFLALMSRQLKSND HHHHHHHHHHHHCCC | 20.09 | 21700874 | |
| 78 | Ubiquitination | ALMSRQLKSNDSEQE HHHHHHHHCCCCHHH | 38.58 | 23749301 | |
| 79 | Phosphorylation | LMSRQLKSNDSEQEL HHHHHHHCCCCHHHH | 55.23 | 22369663 | |
| 82 | Phosphorylation | RQLKSNDSEQELLEA HHHHCCCCHHHHHHH | 45.49 | 22369663 | |
| 91 | Ubiquitination | QELLEAFKVFDKNGD HHHHHHHHHHCCCCC | 49.38 | 24961812 | |
| 91 | Acetylation | QELLEAFKVFDKNGD HHHHHHHHHHCCCCC | 49.38 | 24489116 | |
| 95 | Acetylation | EAFKVFDKNGDGLIS HHHHHHCCCCCCCCC | 51.90 | 24489116 | |
| 95 | Ubiquitination | EAFKVFDKNGDGLIS HHHHHHCCCCCCCCC | 51.90 | 23749301 | |
| 102 | Phosphorylation | KNGDGLISAAELKHV CCCCCCCCHHHHHHH | 26.86 | 27214570 | |
| 107 | Acetylation | LISAAELKHVLTSIG CCCHHHHHHHHHHHH | 24.15 | 24489116 | |
| 111 | Phosphorylation | AELKHVLTSIGEKLT HHHHHHHHHHHHHCC | 19.74 | 22369663 | |
| 112 | Phosphorylation | ELKHVLTSIGEKLTD HHHHHHHHHHHHCCH | 25.16 | 22369663 | |
| 116 | Acetylation | VLTSIGEKLTDAEVD HHHHHHHHCCHHHHH | 52.02 | 24489116 | |
| 116 | Ubiquitination | VLTSIGEKLTDAEVD HHHHHHHHCCHHHHH | 52.02 | 23749301 | |
| 130 | Phosphorylation | DDMLREVSDGSGEIN HHHHHHCCCCCCCCC | 31.34 | 30377154 | |
| 133 | Phosphorylation | LREVSDGSGEINIQQ HHHCCCCCCCCCHHH | 37.94 | 21700874 |
| 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 CALM_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CALM_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 CALM_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-29; SER-82; SER-102 ANDSER-112, AND MASS 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-112, AND MASSSPECTROMETRY. | |
