| UniProt ID | CHZ1_YEAST | |
|---|---|---|
| UniProt AC | P40019 | |
| Protein Name | Histone H2A.Z-specific chaperone CHZ1 | |
| Gene Name | CHZ1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 153 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Forms a chaperone-bound H2A.Z-H2B complex that acts as a source for SWR1 complex-dependent H2A to H2A.Z histone replacement in chromatin.. | |
| Protein Sequence | MSDEAKEKRELESQKESSHNKSEKSVEPKPKRRRRRNYDDYDAEVAKEETKAKNGLTKSENNGTVEDSESDMDDAKLDALMGNEGEEEEDDLAEIDTSNIITSGRRTRGKVIDYKKTAEELDKKEPSTGSKDDVGYGEKEEDDEDEEDDDFKE | |
| 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 | Acetylation | ------MSDEAKEKR ------CCHHHHHHH | 44.13 | 22814378 | |
| 6 | Acetylation | --MSDEAKEKRELES --CCHHHHHHHHHHH | 62.82 | 25381059 | |
| 13 | Phosphorylation | KEKRELESQKESSHN HHHHHHHHHHHHHCC | 60.21 | 30377154 | |
| 15 | Acetylation | KRELESQKESSHNKS HHHHHHHHHHHCCCC | 69.69 | 24489116 | |
| 17 | Phosphorylation | ELESQKESSHNKSEK HHHHHHHHHCCCCCC | 43.89 | 30377154 | |
| 18 | Phosphorylation | LESQKESSHNKSEKS HHHHHHHHCCCCCCC | 31.97 | 30377154 | |
| 22 | Phosphorylation | KESSHNKSEKSVEPK HHHHCCCCCCCCCCC | 56.42 | 29136822 | |
| 24 | Acetylation | SSHNKSEKSVEPKPK HHCCCCCCCCCCCCC | 67.88 | 25381059 | |
| 25 | Phosphorylation | SHNKSEKSVEPKPKR HCCCCCCCCCCCCCH | 27.88 | 24909858 | |
| 29 | Acetylation | SEKSVEPKPKRRRRR CCCCCCCCCCHHHCC | 50.06 | 24489116 | |
| 47 | Acetylation | DYDAEVAKEETKAKN HHHHHHHHHHHHHHC | 62.35 | 24489116 | |
| 51 | Acetylation | EVAKEETKAKNGLTK HHHHHHHHHHCCCCC | 61.72 | 22865919 | |
| 59 | Phosphorylation | AKNGLTKSENNGTVE HHCCCCCCCCCCCCC | 40.08 | 21126336 | |
| 64 | Phosphorylation | TKSENNGTVEDSESD CCCCCCCCCCCCHHH | 23.89 | 22369663 | |
| 68 | Phosphorylation | NNGTVEDSESDMDDA CCCCCCCCHHHCCHH | 26.03 | 22369663 | |
| 70 | Phosphorylation | GTVEDSESDMDDAKL CCCCCCHHHCCHHHH | 42.03 | 22369663 | |
| 97 | Phosphorylation | DDLAEIDTSNIITSG CCHHCCCCCCCCCCC | 29.36 | 22369663 | |
| 98 | Phosphorylation | DLAEIDTSNIITSGR CHHCCCCCCCCCCCC | 23.45 | 22369663 | |
| 102 | Phosphorylation | IDTSNIITSGRRTRG CCCCCCCCCCCCCCC | 22.72 | 22369663 | |
| 103 | Phosphorylation | DTSNIITSGRRTRGK CCCCCCCCCCCCCCC | 21.64 | 22369663 | |
| 110 | Acetylation | SGRRTRGKVIDYKKT CCCCCCCCEEEHHHH | 32.50 | 25381059 | |
| 117 | Phosphorylation | KVIDYKKTAEELDKK CEEEHHHHHHHHHCC | 34.84 | 30377154 | |
| 123 | Acetylation | KTAEELDKKEPSTGS HHHHHHHCCCCCCCC | 72.21 | 24489116 | |
| 124 | Acetylation | TAEELDKKEPSTGSK HHHHHHCCCCCCCCC | 74.62 | 25381059 | |
| 131 | Acetylation | KEPSTGSKDDVGYGE CCCCCCCCCCCCCCC | 60.33 | 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 CHZ1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CHZ1_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 CHZ1_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-68; SER-70 AND SER-98,AND MASS SPECTROMETRY. | |