H3S10ph
H3S10 phosphorylation is a mitosis specific modification and is essential for the onset of mitosis. Basal c-Jun N-terminal kinases (JNK) play a key role in controlling histone H3 phosphorylation for mitotic entry at G2/M phase (PMID: 18256527). Loss of p53, directly or indirectly, perturbs the normal regulation of S10 phosphorylation which may contribute toward the development of abnormal chromosomes and aneuploidy in p53 deficient cancers (PMID: 14583461).
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Modified variants | Histone H3.1, Histone H3.2, Histone H3.3 |
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Writer/s | Inhibitor of nuclear factor kappa-B kinase subunit alpha, Mitogen-activated protein kinase kinase kinase 8, Ribosomal protein S6 kinase alpha-5, Serine/threonine-protein kinase 12, Serine/threonine-protein kinase PAK 2, Serine/threonine-protein kinase tousled-like 1 |
Eraser/s | Dual specificity protein phosphatase 1 |
Disease associations | X linked genetic disorder: Coffin-Lowry syndrome (CLS); PMID: 10436156 Neurological disorders: Alzheimer's disease; PMID: 12677454 Cancer: Breast carcinomas; PMID: 16651411 |
Sites of serine/threonine/tyrosine phosphorylation H1S171ph, H1S172ph, H1S17ph, H1S186ph, H1S188ph, H1S26ph, H1T10ph, H1T137ph, H1T145ph, H1T153ph, H1T154ph, H1T17ph, H1T30ph, H2AS137ph, H2AS139ph, H2AS1ph, H2AT120ph, H2AY142ph, H2BS14ph, H3S10ph, H3S28ph, H3S31ph, H3S6ph, H3T11ph, H3T3ph, H3T45ph, H3T6ph, H3Y41ph, H4S1ph