| UniProt ID | CCPR_YEAST | |
|---|---|---|
| UniProt AC | P00431 | |
| Protein Name | Cytochrome c peroxidase, mitochondrial | |
| Gene Name | CCP1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 361 | |
| Subcellular Localization | Mitochondrion matrix. Mitochondrion intermembrane space . | |
| Protein Description | Destroys radicals which are normally produced within the cells and which are toxic to biological systems.. | |
| Protein Sequence | MTTAVRLLPSLGRTAHKRSLYLFSAAAAAAAAATFAYSQSQKRSSSSPGGGSNHGWNNWGKAAALASTTPLVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHTSGTWDKHDNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTPEDTTPDNGRLPDADKDADYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGAANNVFTNEFYLNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSLIQDPKYLSIVKEYANDQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL | |
| 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 |
|---|---|---|---|---|---|
| 79 | Acetylation | VHVASVEKGRSYEDF EEEEECCCCCCHHHH | 58.42 | 24489116 | |
| 88 | Acetylation | RSYEDFQKVYNAIAL CCHHHHHHHHHHHHH | 46.83 | 24489116 | |
| 126 | Acetylation | HTSGTWDKHDNTGGS ECCCCCCCCCCCCCC | 44.40 | 24489116 | |
| 141 | Acetylation | YGGTYRFKKEFNDPS CCCEEEEEECCCCCC | 42.25 | 24489116 | |
| 142 | Acetylation | GGTYRFKKEFNDPSN CCEEEEEECCCCCCH | 65.90 | 24489116 | |
| 157 | Acetylation | AGLQNGFKFLEPIHK HHCCCCCHHCCHHHH | 50.90 | 24489116 | |
| 216 | Acetylation | GRLPDADKDADYVRT CCCCCCCCCHHHHHH | 57.44 | 24489116 | |
| 220 | Phosphorylation | DADKDADYVRTFFQR CCCCCHHHHHHHHHH | 8.11 | 2851317 | |
| 301 | Phosphorylation | SGYMMLPTDYSLIQD CCCEECCCCHHHCCC | 43.54 | 27017623 | |
| 316 | Acetylation | PKYLSIVKEYANDQD HHHHHHHHHHCCCHH | 43.25 | 22865919 | |
| 324 | Acetylation | EYANDQDKFFKDFSK HHCCCHHHHHHHHHH | 47.25 | 24489116 | |
| 327 | Acetylation | NDQDKFFKDFSKAFE CCHHHHHHHHHHHHH | 62.08 | 24489116 | |
| 335 | Acetylation | DFSKAFEKLLENGIT HHHHHHHHHHHCCCC | 52.50 | 24489116 | |
| 345 | Acetylation | ENGITFPKDAPSPFI HCCCCCCCCCCCCCC | 63.43 | 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 CCPR_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CCPR_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 CCPR_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 TYR-220, AND MASSSPECTROMETRY. | |