| UniProt ID | H2A1_SCHPO | |
|---|---|---|
| UniProt AC | P04909 | |
| Protein Name | Histone H2A-alpha | |
| Gene Name | hta1 | |
| Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission 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 | MSGGKSGGKAAVAKSAQSRSAKAGLAFPVGRVHRLLRKGNYAQRVGAGAPVYLAAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGHVTIAQGGVVPNINAHLLPKTSGRTGKPSQEL | |
| 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 | ------MSGGKSGGK ------CCCCCCCHH | 57.14 | - | |
| 5 | Acetylation | ---MSGGKSGGKAAV ---CCCCCCCHHHHH | 49.83 | 21516229 | |
| 9 | Acetylation | SGGKSGGKAAVAKSA CCCCCCHHHHHHHHH | 36.38 | 21516229 | |
| 20 | Phosphorylation | AKSAQSRSAKAGLAF HHHHHHCHHHHCCCC | 39.09 | 25720772 | |
| 106 | Methylation | LGHVTIAQGGVVPNI HCCEEECCCCCCCCC | 45.37 | 24352239 | |
| 121 | Phosphorylation | NAHLLPKTSGRTGKP CEEECCCCCCCCCCC | 34.18 | 25720772 | |
| 122 | Phosphorylation | AHLLPKTSGRTGKPS EEECCCCCCCCCCCC | 32.19 | 29996109 | |
| 125 | Phosphorylation | LPKTSGRTGKPSQEL CCCCCCCCCCCCCCC | 53.75 | 24763107 | |
| 129 | Phosphorylation | SGRTGKPSQEL---- CCCCCCCCCCC---- | 39.51 | 28889911 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 122 | S | Phosphorylation | Kinase | BUB1 | O94751 | GPS |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of H2A1_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 H2A1_SCHPO !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| H2A2_SCHPO | hta2 | genetic | 15226425 | |
| RNA1_SCHPO | rna1 | physical | 16540522 | |
| RHP9_SCHPO | crb2 | physical | 20679488 | |
| CND2_SCHPO | cnd2 | physical | 21633354 | |
| HRP3_SCHPO | hrp3 | genetic | 22681890 | |
| TSC2_SCHPO | tsc2 | genetic | 22681890 | |
| PYP1_SCHPO | pyp1 | genetic | 22681890 | |
| PROB_SCHPO | SPAC17H9.13c | genetic | 22681890 | |
| YAC5_SCHPO | cph1 | genetic | 22681890 | |
| PLB2_SCHPO | SPAC1A6.03c | genetic | 22681890 | |
| ARP8_SCHPO | arp8 | genetic | 22681890 | |
| DAD1_SCHPO | dad1 | genetic | 22681890 | |
| RAV1_SCHPO | rav1 | genetic | 22681890 | |
| CSN1_SCHPO | csn1 | genetic | 22681890 | |
| YO48_SCHPO | SPBC36B7.08c | genetic | 22681890 | |
| ERS1_SCHPO | ers1 | genetic | 22681890 | |
| RM01_SCHPO | SPAC1610.02c | genetic | 22681890 | |
| ASK1_SCHPO | ask1 | genetic | 22681890 | |
| FFT3_SCHPO | fft3 | genetic | 22681890 | |
| YA99_SCHPO | SPAC13G6.09 | genetic | 22681890 | |
| RCD1_SCHPO | rcd1 | genetic | 22681890 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Histone H2A phosphorylation controls Crb2 recruitment at DNA breaks,maintains checkpoint arrest, and influences DNA repair in fissionyeast."; Nakamura T.M., Du L.-L., Redon C., Russell P.; Mol. Cell. Biol. 24:6215-6230(2004). Cited for: FUNCTION, MUTAGENESIS OF SER-129, AND PHOSPHORYLATION AT SER-129. | |