| UniProt ID | H2A2_YEAST | |
|---|---|---|
| UniProt AC | P04912 | |
| Protein Name | Histone H2A.2 | |
| Gene Name | HTA2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 132 | |
| Subcellular Localization | Nucleus. Chromosome. | |
| Protein Description | Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. 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.. | |
| Protein Sequence | MSGGKGGKAGSAAKASQSRSAKAGLTFPVGRVHRLLRRGNYAQRIGSGAPVYLTAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDDELNKLLGNVTIAQGGVLPNIHQNLLPKKSAKTAKASQEL | |
| 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 | ------MSGGKGGKA ------CCCCCCCCH | 57.14 | 12915400 | |
| 2 | Phosphorylation | ------MSGGKGGKA ------CCCCCCCCH | 57.14 | 27717283 | |
| 5 | Acetylation | ---MSGGKGGKAGSA ---CCCCCCCCHHHH | 68.93 | 10082517 | |
| 8 | Acetylation | MSGGKGGKAGSAAKA CCCCCCCCHHHHHHH | 59.24 | 11545749 | |
| 11 | Phosphorylation | GKGGKAGSAAKASQS CCCCCHHHHHHHHHC | 29.88 | 27717283 | |
| 14 | Succinylation | GKAGSAAKASQSRSA CCHHHHHHHHHCCCH | 48.57 | 22389435 | |
| 20 | Phosphorylation | AKASQSRSAKAGLTF HHHHHCCCHHCCCCC | 39.09 | 21440633 | |
| 22 | Succinylation | ASQSRSAKAGLTFPV HHHCCCHHCCCCCCH | 44.21 | 22389435 | |
| 22 | Ubiquitination | ASQSRSAKAGLTFPV HHHCCCHHCCCCCCH | 44.21 | 23749301 | |
| 26 | Phosphorylation | RSAKAGLTFPVGRVH CCHHCCCCCCHHHHH | 25.60 | 27214570 | |
| 97 | Ubiquitination | RNDDELNKLLGNVTI CCHHHHHHHHCCEEE | 58.68 | 23749301 | |
| 106 | Methylation | LGNVTIAQGGVLPNI HCCEEECCCCCCCCH | 45.37 | 24352239 | |
| 120 | Acetylation | IHQNLLPKKSAKTAK HHHHCCCHHHHHHHH | 60.37 | 25381059 | |
| 120 | Malonylation | IHQNLLPKKSAKTAK HHHHCCCHHHHHHHH | 60.37 | 22389435 | |
| 121 | Acetylation | HQNLLPKKSAKTAKA HHHCCCHHHHHHHHH | 54.42 | 23572591 | |
| 122 | Phosphorylation | QNLLPKKSAKTAKAS HHCCCHHHHHHHHHH | 40.92 | 21440633 | |
| 124 | Acetylation | LLPKKSAKTAKASQE CCCHHHHHHHHHHHC | 56.99 | 23572591 | |
| 125 | Phosphorylation | LPKKSAKTAKASQEL CCHHHHHHHHHHHCC | 32.86 | 22890988 | |
| 127 | Acetylation | KKSAKTAKASQEL-- HHHHHHHHHHHCC-- | 54.52 | 23572591 | |
| 127 | Ubiquitination | KKSAKTAKASQEL-- HHHHHHHHHHHCC-- | 54.52 | 23749301 | |
| 127 | Sumoylation | KKSAKTAKASQEL-- HHHHHHHHHHHCC-- | 54.52 | - | |
| 129 | Phosphorylation | SAKTAKASQEL---- HHHHHHHHHCC---- | 24.39 | 22369663 |
| 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 H2A2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 106 | Q | Methylation |
| 24352239 |
* 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 H2A2_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "An Nalpha-acetyltransferase responsible for acetylation of the N-terminal residues of histones H4 and H2A."; Song O.-K., Wang X., Waterborg J.H., Sternglanz R.; J. Biol. Chem. 278:38109-38112(2003). Cited for: ACETYLATION AT SER-2. | |
| "Highly specific antibodies determine histone acetylation site usagein yeast heterochromatin and euchromatin."; Suka N., Suka Y., Carmen A.A., Wu J., Grunstein M.; Mol. Cell 8:473-479(2001). Cited for: ACETYLATION AT LYS-8. | |
| "Esa1p is an essential histone acetyltransferase required for cellcycle progression."; Clarke A.S., Lowell J.E., Jacobson S.J., Pillus L.; Mol. Cell. Biol. 19:2515-2526(1999). Cited for: ACETYLATION AT LYS-5 AND LYS-8. | |
| 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-129, AND MASSSPECTROMETRY. | |
| "A role for Saccharomyces cerevisiae histone H2A in DNA repair."; Downs J.A., Lowndes N.F., Jackson S.P.; Nature 408:1001-1004(2000). Cited for: FUNCTION, MUTAGENESIS OF SER-129, AND PHOSPHORYLATION AT SER-129. | |
| Sumoylation | |
| Reference | PubMed |
| "Histone sumoylation is a negative regulator in Saccharomycescerevisiae and shows dynamic interplay with positive-acting histonemodifications."; Nathan D., Ingvarsdottir K., Sterner D.E., Bylebyl G.R.,Dokmanovic M., Dorsey J.A., Whelan K.A., Krsmanovic M., Lane W.S.,Meluh P.B., Johnson E.S., Berger S.L.; Genes Dev. 20:966-976(2006). Cited for: SUMOYLATION AT LYS-127. | |
