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 | ||
* 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 | ||||||
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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-68; SER-70 AND SER-98,AND MASS SPECTROMETRY. |