| UniProt ID | H2B1_YEAST | |
|---|---|---|
| UniProt AC | P02293 | |
| Protein Name | Histone H2B.1 | |
| Gene Name | HTB1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 131 | |
| Subcellular Localization | Nucleus. Chromosome. | |
| Protein Description | Core component of nucleosome. 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 | MSAKAEKKPASKAPAEKKPAAKKTSTSTDGKKRSKARKETYSSYIYKVLKQTHPDTGISQKSMSILNSFVNDIFERIATEASKLAAYNKKSTISAREIQTAVRLILPGELAKHAVSEGTRAVTKYSSSTQA | |
| 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 |
|---|---|---|---|---|---|
| 4 | Acetylation | ----MSAKAEKKPAS ----CCCCCCCCCCC | 50.17 | 24489116 | |
| 7 | Sumoylation | -MSAKAEKKPASKAP -CCCCCCCCCCCCCC | 69.76 | - | |
| 7 | Acetylation | -MSAKAEKKPASKAP -CCCCCCCCCCCCCC | 69.76 | 16598039 | |
| 8 | Sumoylation | MSAKAEKKPASKAPA CCCCCCCCCCCCCCC | 37.00 | - | |
| 8 | Acetylation | MSAKAEKKPASKAPA CCCCCCCCCCCCCCC | 37.00 | 16598039 | |
| 11 | Phosphorylation | KAEKKPASKAPAEKK CCCCCCCCCCCCCCC | 37.57 | 29136822 | |
| 12 | Acetylation | AEKKPASKAPAEKKP CCCCCCCCCCCCCCC | 61.57 | 11545749 | |
| 17 | Acetylation | ASKAPAEKKPAAKKT CCCCCCCCCCCCCCC | 67.19 | 15186774 | |
| 18 | Acetylation | SKAPAEKKPAAKKTS CCCCCCCCCCCCCCC | 31.24 | 19113941 | |
| 22 | Acetylation | AEKKPAAKKTSTSTD CCCCCCCCCCCCCCC | 59.70 | 19113941 | |
| 22 | Butyrylation | AEKKPAAKKTSTSTD CCCCCCCCCCCCCCC | 59.70 | 19113941 | |
| 23 | Acetylation | EKKPAAKKTSTSTDG CCCCCCCCCCCCCCC | 42.87 | 19113941 | |
| 23 | Methylation | EKKPAAKKTSTSTDG CCCCCCCCCCCCCCC | 42.87 | 19113941 | |
| 25 | Phosphorylation | KPAAKKTSTSTDGKK CCCCCCCCCCCCCCH | 29.28 | 27214570 | |
| 26 | Phosphorylation | PAAKKTSTSTDGKKR CCCCCCCCCCCCCHH | 40.66 | 27214570 | |
| 27 | Phosphorylation | AAKKTSTSTDGKKRS CCCCCCCCCCCCHHH | 25.03 | 27214570 | |
| 28 | Phosphorylation | AKKTSTSTDGKKRSK CCCCCCCCCCCHHHH | 49.19 | 27214570 | |
| 35 | Succinylation | TDGKKRSKARKETYS CCCCHHHHHHHHHHH | 57.13 | 22389435 | |
| 38 | Acetylation | KKRSKARKETYSSYI CHHHHHHHHHHHHHH | 60.30 | 24489116 | |
| 38 | Methylation | KKRSKARKETYSSYI CHHHHHHHHHHHHHH | 60.30 | 19113941 | |
| 40 | Phosphorylation | RSKARKETYSSYIYK HHHHHHHHHHHHHHH | 31.57 | 20377248 | |
| 41 | Phosphorylation | SKARKETYSSYIYKV HHHHHHHHHHHHHHH | 9.19 | 21440633 | |
| 42 | Phosphorylation | KARKETYSSYIYKVL HHHHHHHHHHHHHHH | 24.88 | 20377248 | |
| 43 | Phosphorylation | ARKETYSSYIYKVLK HHHHHHHHHHHHHHH | 12.72 | 21440633 | |
| 44 | Phosphorylation | RKETYSSYIYKVLKQ HHHHHHHHHHHHHHH | 11.43 | 28889911 | |
| 47 | Ubiquitination | TYSSYIYKVLKQTHP HHHHHHHHHHHHHCC | 31.37 | 23749301 | |
| 47 | Acetylation | TYSSYIYKVLKQTHP HHHHHHHHHHHHHCC | 31.37 | 24489116 | |
| 47 | Succinylation | TYSSYIYKVLKQTHP HHHHHHHHHHHHHCC | 31.37 | 22389435 | |
| 50 | Ubiquitination | SYIYKVLKQTHPDTG HHHHHHHHHHCCCCC | 57.02 | 23749301 | |
| 50 | Acetylation | SYIYKVLKQTHPDTG HHHHHHHHHHCCCCC | 57.02 | 22865919 | |
| 50 | Succinylation | SYIYKVLKQTHPDTG HHHHHHHHHHCCCCC | 57.02 | 22389435 | |
| 59 | Phosphorylation | THPDTGISQKSMSIL HCCCCCCCHHHHHHH | 32.66 | 30377154 | |
| 61 | Ubiquitination | PDTGISQKSMSILNS CCCCCCHHHHHHHHH | 41.14 | 23749301 | |
| 62 | Phosphorylation | DTGISQKSMSILNSF CCCCCHHHHHHHHHH | 15.32 | 28889911 | |
| 83 | Acetylation | RIATEASKLAAYNKK HHHHHHHHHHHHCCC | 49.55 | 24489116 | |
| 83 | Ubiquitination | RIATEASKLAAYNKK HHHHHHHHHHHHCCC | 49.55 | 23749301 | |
| 83 | 2-Hydroxyisobutyrylation | RIATEASKLAAYNKK HHHHHHHHHHHHCCC | 49.55 | - | |
| 89 | Ubiquitination | SKLAAYNKKSTISAR HHHHHHCCCCCCCHH | 35.11 | 23749301 | |
| 89 | Acetylation | SKLAAYNKKSTISAR HHHHHHCCCCCCCHH | 35.11 | 24489116 | |
| 89 | Succinylation | SKLAAYNKKSTISAR HHHHHHCCCCCCCHH | 35.11 | 23954790 | |
| 90 | 2-Hydroxyisobutyrylation | KLAAYNKKSTISARE HHHHHCCCCCCCHHH | 49.55 | - | |
| 112 | 2-Hydroxyisobutyrylation | ILPGELAKHAVSEGT HCCHHHHHHHHHHHC | 44.73 | - | |
| 112 | Ubiquitination | ILPGELAKHAVSEGT HCCHHHHHHHHHHHC | 44.73 | 23749301 | |
| 112 | Acetylation | ILPGELAKHAVSEGT HCCHHHHHHHHHHHC | 44.73 | 24489116 | |
| 116 | Phosphorylation | ELAKHAVSEGTRAVT HHHHHHHHHHCHHHH | 30.96 | 21440633 | |
| 123 | Phosphorylation | SEGTRAVTKYSSSTQ HHHCHHHHHHCCCCC | 24.23 | 23749301 | |
| 124 | Ubiquitination | EGTRAVTKYSSSTQA HHCHHHHHHCCCCCC | 36.21 | 14660635 | |
| 124 | Acetylation | EGTRAVTKYSSSTQA HHCHHHHHHCCCCCC | 36.21 | 22865919 | |
| 127 | Phosphorylation | RAVTKYSSSTQA--- HHHHHHCCCCCC--- | 34.02 | 23749301 | |
| 128 | Phosphorylation | AVTKYSSSTQA---- HHHHHCCCCCC---- | 20.71 | 23749301 | |
| 129 | Phosphorylation | VTKYSSSTQA----- HHHHCCCCCC----- | 30.39 | 25521595 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of H2B1_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 H2B1_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| 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: MASS SPECTROMETRY, SUMOYLATION AT LYS-7; LYS-8; LYS-17 AND LYS-18,ACETYLATION AT LYS-7; LYS-8 AND LYS-17, MUTAGENESIS OF 7-LYS-LYS-8 AND17-LYS-LYS-18, AND FUNCTION. | |
| "Mapping global histone acetylation patterns to gene expression."; Kurdistani S.K., Tavazoie S., Grunstein M.; Cell 117:721-733(2004). Cited for: ACETYLATION AT LYS-12 AND LYS-17. | |
| "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-12 AND LYS-17. | |
| Phosphorylation | |
| Reference | PubMed |
| "H2B (Ser10) phosphorylation is induced during apoptosis and meiosisin S. cerevisiae."; Ahn S.-H., Henderson K.A., Keeney S., Allis C.D.; Cell Cycle 4:780-783(2005). Cited for: PHOSPHORYLATION AT SER-11, AND FUNCTION. | |
| "Sterile 20 kinase phosphorylates histone H2B at serine 10 duringhydrogen peroxide-induced apoptosis in S. cerevisiae."; Ahn S.-H., Cheung W.L., Hsu J.-Y., Diaz R.L., Smith M.M., Allis C.D.; Cell 120:25-36(2005). Cited for: PHOSPHORYLATION AT SER-11, MUTAGENESIS OF SER-11, AND FUNCTION. | |
| 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: MASS SPECTROMETRY, SUMOYLATION AT LYS-7; LYS-8; LYS-17 AND LYS-18,ACETYLATION AT LYS-7; LYS-8 AND LYS-17, MUTAGENESIS OF 7-LYS-LYS-8 AND17-LYS-LYS-18, AND FUNCTION. | |
| Ubiquitylation | |
| Reference | PubMed |
| "A tandem affinity tag for two-step purification under fullydenaturing conditions: application in ubiquitin profiling and proteincomplex identification combined with in vivocross-linking."; Tagwerker C., Flick K., Cui M., Guerrero C., Dou Y., Auer B.,Baldi P., Huang L., Kaiser P.; Mol. Cell. Proteomics 5:737-748(2006). Cited for: UBIQUITINATION AT LYS-124. | |
| "Rad6-Bre1-mediated histone H2B ubiquitylation modulates the formationof double-strand breaks during meiosis."; Yamashita K., Shinohara M., Shinohara A.; Proc. Natl. Acad. Sci. U.S.A. 101:11380-11385(2004). Cited for: FUNCTION, UBIQUITINATION AT LYS-124 BY THE UBC2-BRE1 COMPLEX, ANDMUTAGENESIS OF LYS-124. | |
| "Carbohydrates induce mono-ubiquitination of H2B in yeast."; Dong L., Xu C.W.; J. Biol. Chem. 279:1577-1580(2004). Cited for: UBIQUITINATION AT LYS-124, AND MUTAGENESIS OF LYS-124. | |
| "Bre1, an E3 ubiquitin ligase required for recruitment and substrateselection of Rad6 at a promoter."; Wood A., Krogan N.J., Dover J., Schneider J., Heidt J., Boateng M.A.,Dean K., Golshani A., Zhang Y., Greenblatt J.F., Johnston M.,Shilatifard A.; Mol. Cell 11:267-274(2003). Cited for: UBIQUITINATION AT LYS-124. | |
| "A conserved RING finger protein required for histone H2Bmonoubiquitination and cell size control."; Hwang W.W., Venkatasubrahmanyam S., Ianculescu A.G., Tong A.,Boone C., Madhani H.D.; Mol. Cell 11:261-266(2003). Cited for: UBIQUITINATION AT LYS-124. | |
| "Rad6-dependent ubiquitination of histone H2B in yeast."; Robzyk K., Recht J., Osley M.A.; Science 287:501-504(2000). Cited for: UBIQUITINATION AT LYS-124, AND MUTAGENESIS OF LYS-124. | |
