| UniProt ID | H31_SCHPO | |
|---|---|---|
| UniProt AC | P09988 | |
| Protein Name | Histone H3.1/H3.2 | |
| Gene Name | hht1 | |
| Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). | |
| Sequence Length | 136 | |
| 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 | MARTKQTARKSTGGKAPRKQLASKAARKAAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAIGALQEAVEAYLVSLFEDTNLCAIHGKRVTIQPKDMQLARRLRGERS | |
| 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 |
|---|---|---|---|---|---|
| 5 | "N6,N6,N6-trimethyllysine" | ---MARTKQTARKST ---CCCCCHHHHHHC | 39.85 | - | |
| 5 | Methylation | ---MARTKQTARKST ---CCCCCHHHHHHC | 39.85 | - | |
| 10 | Acetylation | RTKQTARKSTGGKAP CCCHHHHHHCCCCCC | 50.32 | - | |
| 10 | Methylation | RTKQTARKSTGGKAP CCCHHHHHHCCCCCC | 50.32 | 11283354 | |
| 11 | Phosphorylation | TKQTARKSTGGKAPR CCHHHHHHCCCCCCH | 27.08 | 24763107 | |
| 15 | "N6,N6-dimethyllysine" | ARKSTGGKAPRKQLA HHHHCCCCCCHHHHH | 57.47 | - | |
| 15 | Acetylation | ARKSTGGKAPRKQLA HHHHCCCCCCHHHHH | 57.47 | - | |
| 15 | Methylation | ARKSTGGKAPRKQLA HHHHCCCCCCHHHHH | 57.47 | - | |
| 19 | Acetylation | TGGKAPRKQLASKAA CCCCCCHHHHHHHHH | 48.91 | - | |
| 19 | Methylation | TGGKAPRKQLASKAA CCCCCCHHHHHHHHH | 48.91 | - | |
| 24 | Methylation | PRKQLASKAARKAAP CHHHHHHHHHHHHCC | 40.22 | - | |
| 24 | Acetylation | PRKQLASKAARKAAP CHHHHHHHHHHHHCC | 40.22 | - | |
| 28 | Acetylation | LASKAARKAAPATGG HHHHHHHHHCCCCCC | 44.14 | - | |
| 28 | Methylation | LASKAARKAAPATGG HHHHHHHHHCCCCCC | 44.14 | - | |
| 28 | "N6,N6,N6-trimethyllysine" | LASKAARKAAPATGG HHHHHHHHHCCCCCC | 44.14 | - | |
| 37 | Acetylation | APATGGVKKPHRYRP CCCCCCCCCCCCCCC | 64.95 | - | |
| 37 | "N6,N6,N6-trimethyllysine" | APATGGVKKPHRYRP CCCCCCCCCCCCCCC | 64.95 | - | |
| 37 | Methylation | APATGGVKKPHRYRP CCCCCCCCCCCCCCC | 64.95 | 16087749 | |
| 42 | Phosphorylation | GVKKPHRYRPGTVAL CCCCCCCCCCCCHHH | 20.37 | 25720772 | |
| 57 | Acetylation | REIRRYQKSTELLIR HHHHHHHHCHHHHHH | 50.87 | 17369611 | |
| 58 | Phosphorylation | EIRRYQKSTELLIRK HHHHHHHCHHHHHHH | 16.16 | 25720772 | |
| 59 | Phosphorylation | IRRYQKSTELLIRKL HHHHHHCHHHHHHHC | 37.37 | 25720772 | |
| 65 | Acetylation | STELLIRKLPFQRLV CHHHHHHHCCHHHHH | 54.22 | - | |
| 80 | Methylation | REIAQDFKTDLRFQS HHHHHHHHCCHHHHH | 49.79 | - | |
| 80 | "N6,N6,N6-trimethyllysine" | REIAQDFKTDLRFQS HHHHHHHHCCHHHHH | 49.79 | - |
| 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 H31_SCHPO !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of H31_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 H31_SCHPO !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| SWI6_SCHPO | swi6 | physical | 12215653 | |
| SWI6_SCHPO | swi6 | physical | 21211724 | |
| YGI3_SCHPO | SPBC2A9.03 | genetic | 18818364 | |
| RSC4_SCHPO | rsc4 | physical | 22184112 | |
| SNF21_SCHPO | snf21 | physical | 22184112 | |
| PVG2_SCHPO | pvg2 | genetic | 22681890 | |
| TPSY_SCHPO | SPAC22F8.05 | genetic | 22681890 | |
| SWI6_SCHPO | swi6 | physical | 23281010 | |
| H31_SCHPO | hht3 | physical | 18158900 | |
| BIR1_SCHPO | bir1 | physical | 20929775 | |
| CLR4_SCHPO | clr4 | genetic | 27648579 | |
| SMC6_SCHPO | smc6 | genetic | 28718400 | |
| UBC13_SCHPO | ubc13 | genetic | 28718400 | |
| KU70_SCHPO | pku70 | genetic | 28718400 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Methylation | |
| Reference | PubMed |
| "Histone H3 K36 methylation is associated with transcriptionelongation in Schizosaccharomyces pombe."; Morris S.A., Shibata Y., Noma K., Tsukamoto Y., Warren E., Temple B.,Grewal S.I.S., Strahl B.D.; Eukaryot. Cell 4:1446-1454(2005). Cited for: METHYLATION AT LYS-37. | |
| "Role of histone H3 lysine 9 methylation in epigenetic control ofheterochromatin assembly."; Nakayama J., Rice J.C., Strahl B.D., Allis C.D., Grewal S.I.S.; Science 292:110-113(2001). Cited for: METHYLATION AT LYS-10. | |
