| UniProt ID | H2B1_SCHPO | |
|---|---|---|
| UniProt AC | P04913 | |
| Protein Name | Histone H2B-alpha | |
| Gene Name | htb1 | |
| Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). | |
| Sequence Length | 126 | |
| 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 | MSAAEKKPASKAPAGKAPRDTMKSADKKRGKNRKETYSSYIYKVLKQVHPDTGISNQAMRILNSFVNDIFERIATEASKLAAYNKKSTISSREIQTAVRLILPGELAKHAVTEGTKSVTKYSSSAQ | |
| 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 | Phosphorylation | ------MSAAEKKPA ------CCHHHCCCC | 35.87 | 25720772 | |
| 6 | Acetylation | --MSAAEKKPASKAP --CCHHHCCCCCCCC | 60.37 | 21516229 | |
| 7 | Acetylation | -MSAAEKKPASKAPA -CCHHHCCCCCCCCC | 37.00 | - | |
| 10 | Phosphorylation | AAEKKPASKAPAGKA HHHCCCCCCCCCCCC | 37.57 | 25720772 | |
| 11 | Acetylation | AEKKPASKAPAGKAP HHCCCCCCCCCCCCC | 61.57 | 21516229 | |
| 16 | Acetylation | ASKAPAGKAPRDTMK CCCCCCCCCCHHHHH | 58.27 | 21516229 | |
| 120 | Ubiquitination | EGTKSVTKYSSSAQ- CCCCCCCCCCCCCC- | 40.76 | PubMed |
| 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 H2B1_SCHPO !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of H2B1_SCHPO !! | ||||||
* 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_SCHPO !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| CENPA_SCHPO | cnp1 | genetic | 16688222 | |
| MIS6_SCHPO | mis6 | genetic | 16688222 | |
| MIS12_SCHPO | mis12 | genetic | 16688222 | |
| DIS1_SCHPO | dis1 | genetic | 16688222 | |
| PP11_SCHPO | dis2 | genetic | 16688222 | |
| CLR6_SCHPO | clr6 | genetic | 16688222 | |
| KAPB_SCHPO | pka1 | genetic | 16688222 | |
| RNA1_SCHPO | rna1 | physical | 16540522 | |
| PDP1_SCHPO | pdp1 | physical | 19250904 | |
| CDK9_SCHPO | cdk9 | physical | 22876190 | |
| CDK9_SCHPO | cdk9 | genetic | 22876190 | |
| SPT5_SCHPO | spt5 | genetic | 22876190 | |
| CDC73_SCHPO | cdc73 | genetic | 24385927 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Ubiquitylation | |
| Reference | PubMed |
| "Histone H2B mutations in inner region affect ubiquitination,centromere function, silencing and chromosome segregation."; Maruyama T., Nakamura T., Hayashi T., Yanagida M.; EMBO J. 25:2420-2431(2006). Cited for: MUTAGENESIS OF GLU-35; GLY-53; PRO-103 AND LYS-120, AND UBIQUITINATIONAT LYS-120. | |
