| UniProt ID | H2AZ_YEAST | |
|---|---|---|
| UniProt AC | Q12692 | |
| Protein Name | Histone H2A.Z | |
| Gene Name | HTZ1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 134 | |
| Subcellular Localization | Nucleus . Chromosome . | |
| Protein Description | Variant histone H2A which can replace H2A in some nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. This variant is enriched at promoters, it may keep them in a repressed state until the appropriate activation signal is received. Near telomeres, it may counteract gene silencing caused by the spread of heterochromatin proteins. Required for the RNA polymerase II and SPT15/TBP recruitment to the target genes. Involved in chromosome stability.. | |
| Protein Sequence | MSGKAHGGKGKSGAKDSGSLRSQSSSARAGLQFPVGRIKRYLKRHATGRTRVGSKAAIYLTAVLEYLTAEVLELAGNAAKDLKVKRITPRHLQLAIRGDDELDSLIRATIASGGVLPHINKALLLKVEKKGSKK | |
| 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 | ------MSGKAHGGK ------CCCCCCCCC | 49.34 | 22814378 | |
| 4 | Acetylation | ----MSGKAHGGKGK ----CCCCCCCCCCC | 29.87 | 16543222 | |
| 9 | Acetylation | SGKAHGGKGKSGAKD CCCCCCCCCCCCCCC | 68.69 | 16543222 | |
| 11 | Acetylation | KAHGGKGKSGAKDSG CCCCCCCCCCCCCCC | 49.56 | 16543222 | |
| 15 | Acetylation | GKGKSGAKDSGSLRS CCCCCCCCCCCCCCC | 56.82 | 16543222 | |
| 17 | Phosphorylation | GKSGAKDSGSLRSQS CCCCCCCCCCCCCCC | 29.58 | 24961812 | |
| 19 | Phosphorylation | SGAKDSGSLRSQSSS CCCCCCCCCCCCCCH | 25.26 | 21440633 | |
| 22 | Phosphorylation | KDSGSLRSQSSSARA CCCCCCCCCCCHHCC | 39.44 | 24961812 | |
| 24 | Phosphorylation | SGSLRSQSSSARAGL CCCCCCCCCHHCCCC | 27.75 | 24961812 | |
| 25 | Phosphorylation | GSLRSQSSSARAGLQ CCCCCCCCHHCCCCC | 22.00 | 24961812 | |
| 26 | Phosphorylation | SLRSQSSSARAGLQF CCCCCCCHHCCCCCC | 27.33 | 24961812 | |
| 104 | Phosphorylation | RGDDELDSLIRATIA CCCHHHHHHHHHHHH | 38.02 | 27214570 | |
| 121 | Acetylation | GVLPHINKALLLKVE CCHHHCCHHHHHHHH | 39.55 | 24489116 | |
| 126 | Acetylation | INKALLLKVEKKGSK CCHHHHHHHHHCCCC | 48.60 | 24489116 | |
| 126 | Sumoylation | INKALLLKVEKKGSK CCHHHHHHHHHCCCC | 48.60 | - | |
| 133 | Sumoylation | KVEKKGSKK------ HHHHCCCCC------ | 71.78 | - |
| 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 H2AZ_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of H2AZ_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 H2AZ_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Acetylation of H2AZ Lys 14 is associated with genome-wide geneactivity in yeast."; Millar C.B., Xu F., Zhang K., Grunstein M.; Genes Dev. 20:711-722(2006). Cited for: PROTEIN SEQUENCE OF 2-21, ACETYLATION AT SER-2; LYS-4; LYS-9; LYS-11AND LYS-15, MASS SPECTROMETRY, AND FUNCTION. | |
| "Telomeric heterochromatin boundaries require NuA4-dependentacetylation of histone variant H2A.Z in Saccharomyces cerevisiae."; Babiarz J.E., Halley J.E., Rine J.; Genes Dev. 20:700-710(2006). Cited for: ACETYLATION AT LYS-4; LYS-9; LYS-11 AND LYS-15, MASS SPECTROMETRY, ANDFUNCTION. | |
