UniProt ID | CCC1_YEAST | |
---|---|---|
UniProt AC | P47818 | |
Protein Name | Protein CCC1 | |
Gene Name | CCC1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 322 | |
Subcellular Localization |
Golgi apparatus membrane . Vacuole membrane Multi-pass membrane protein . |
|
Protein Description | Has a role in both calcium and manganese homeostasis. Involved in the transfer of iron and Mn(2+) from the cytosol to the vacuole for storage of these metals.. | |
Protein Sequence | MSIVALKNAVVTLIQKAKGSGGTSELGGSESTPLLRGSNSNSSRHDNLSSSSSDIIYGRNSAQDLENSPMSVGKDNRNGDNGSDNEKANLGFFQSVDPRVISDLIIGLSDGLTVPFALTAGLSSLGDAKLVITGGFAELISGAISMGLGGYLGAKSESDYYHAEVKKEKRKFYDNSNLINREIEDILLEINPNFSDETIVSFIKDLQRTPELMVDFIIRYGRGLDEPAENRELISAVTIGGGYLLGGLVPLVPYFFVSDVGTGLIYSIIVMVVTLFWFGYVKTKLSMGSGSSTSKKVTEGVEMVVVGGVAAGAAWFFVKLLG | |
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 |
---|---|---|---|---|---|
16 | Ubiquitination | AVVTLIQKAKGSGGT HHHHHHHHHCCCCCC | 45.10 | 22817900 | |
18 | Ubiquitination | VTLIQKAKGSGGTSE HHHHHHHCCCCCCCC | 61.72 | 23749301 | |
20 | Phosphorylation | LIQKAKGSGGTSELG HHHHHCCCCCCCCCC | 33.09 | 22369663 | |
23 | Phosphorylation | KAKGSGGTSELGGSE HHCCCCCCCCCCCCC | 23.66 | 21440633 | |
24 | Phosphorylation | AKGSGGTSELGGSES HCCCCCCCCCCCCCC | 33.81 | 22369663 | |
29 | Phosphorylation | GTSELGGSESTPLLR CCCCCCCCCCCCCCC | 26.95 | 22369663 | |
31 | Phosphorylation | SELGGSESTPLLRGS CCCCCCCCCCCCCCC | 36.70 | 22369663 | |
32 | Phosphorylation | ELGGSESTPLLRGSN CCCCCCCCCCCCCCC | 17.57 | 22369663 | |
38 | Phosphorylation | STPLLRGSNSNSSRH CCCCCCCCCCCCCCC | 30.56 | 30377154 | |
40 | Phosphorylation | PLLRGSNSNSSRHDN CCCCCCCCCCCCCCC | 39.52 | 30377154 | |
42 | Phosphorylation | LRGSNSNSSRHDNLS CCCCCCCCCCCCCCC | 28.68 | 23749301 | |
43 | Phosphorylation | RGSNSNSSRHDNLSS CCCCCCCCCCCCCCC | 37.57 | 23749301 | |
49 | Phosphorylation | SSRHDNLSSSSSDII CCCCCCCCCCHHHEE | 34.13 | 22369663 | |
50 | Phosphorylation | SRHDNLSSSSSDIIY CCCCCCCCCHHHEEC | 37.09 | 22369663 | |
51 | Phosphorylation | RHDNLSSSSSDIIYG CCCCCCCCHHHEECC | 30.41 | 22369663 | |
52 | Phosphorylation | HDNLSSSSSDIIYGR CCCCCCCHHHEECCC | 33.70 | 22369663 | |
53 | Phosphorylation | DNLSSSSSDIIYGRN CCCCCCHHHEECCCC | 34.47 | 22369663 | |
57 | Phosphorylation | SSSSDIIYGRNSAQD CCHHHEECCCCCHHH | 15.46 | 22890988 | |
61 | Phosphorylation | DIIYGRNSAQDLENS HEECCCCCHHHHCCC | 26.41 | 22369663 | |
68 | Phosphorylation | SAQDLENSPMSVGKD CHHHHCCCCCCCCCC | 16.77 | 22369663 | |
71 | Phosphorylation | DLENSPMSVGKDNRN HHCCCCCCCCCCCCC | 30.97 | 22369663 | |
74 | Ubiquitination | NSPMSVGKDNRNGDN CCCCCCCCCCCCCCC | 50.07 | 23749301 | |
83 | Phosphorylation | NRNGDNGSDNEKANL CCCCCCCCCCHHHCC | 43.44 | 17330950 | |
87 | Ubiquitination | DNGSDNEKANLGFFQ CCCCCCHHHCCCCCC | 49.15 | 23749301 | |
95 | Phosphorylation | ANLGFFQSVDPRVIS HCCCCCCCCCHHHHH | 24.27 | 29136822 | |
171 | Ubiquitination | EVKKEKRKFYDNSNL HHHHHHHHHCCCCCC | 60.38 | 23749301 | |
176 | Phosphorylation | KRKFYDNSNLINREI HHHHCCCCCCCCHHH | 30.07 | 27214570 |
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 CCC1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CCC1_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 CCC1_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 SER-29; SER-49; SER-51;SER-52; SER-53; SER-68; SER-71 AND SER-83, 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-50; SER-51; SER-52;SER-53; SER-68; SER-71 AND SER-83, 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-83, AND MASSSPECTROMETRY. | |
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae."; Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.; Nat. Biotechnol. 20:301-305(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49 AND SER-52, AND MASSSPECTROMETRY. | |
"A proteomics approach to understanding protein ubiquitination."; Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.; Nat. Biotechnol. 21:921-926(2003). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-32, AND MASSSPECTROMETRY. |