HIST1H1C Antibody

1. results define a network of E2F target genes as susceptible to the regulatory influence of H1.2, where H1.2 augments global association of pRb with chromatin, enhances transcriptional repression by pRb, and facilitates pRb-dependent cell-cycle arrest PMID:28614707
2. BRG1 participates in gene repression by interacting with H1.2, facilitating its deposition and stabilizing nucleosome positioning around the transcription start site. PMID:27390128
3. Results show that histones H1.2 and H1.4 were observed in MDA-MB-231 metastatic breast cancer cells. The phosphorylation at S173 of histone H1.2 and S172, S187, T18, T146, and T154 of H1.4 significantly increases during M phase suggesting that these events are cell cycle-dependent. Also, the study reports the observation of the H1.2 SNP variant A18V in MCF-10A cells. PMID:26209608
4. Integration with apoptotic intermediates (via C-terminal tail interactions) may constitute a more generalized function of linker histone isoforms in apoptotic cascades. PMID:24525734
5. Histone H1.2-T165 post translational modifications are dispensable for chromatin binding and cell proliferation while the H1.4-K26 modifications are essential for proper cell cycle progression. PMID:24873882
6. H1.2 interacts with Cul4A and PAF1 to activate developmental regulatory genes. PMID:24360965
7. H1.2 is less abundant than other histone H1 variants at the transcription start sites of inactive genes, and promoters enriched in H1.2 are different from those enriched in other histone H1 variants and tend to be repressed. PMID:24476918
8. Mutations in linker histone genes HIST1H1 B, C, D, and E; OCT2 (POU2F2); IRF8; and ARID1A underlying the pathogenesis of follicular lymphoma. PMID:24435047
9. These data suggest that p53 acetylation-H1.2 phosphorylation cascade serves as a unique mechanism for triggering p53-dependent DNA damage response pathways. PMID:22249259
10. confirmed N-terminal acetylation on all isoforms plus a single internal acetylation site; phosphorylation sites were located on peptides containing the cyclin dependent kinase (CDK) consensus motif PMID:15595731
11. The binding of histone H1 to a general amyloid-like motif indicates that histone H1 may play an important common role in diseases associated with amyloid-like fibrils. PMID:16854430
12. Histone H1.2 was translocated from the nucleus to the mitochondria after treatment with bleomycin and co-localized with Bak in mitochondria. PMID:17879944
13. that the recruitment of YB1, PURalpha, and H1.2 to the p53 target gene Bax is required for repression of p53-induced transcription. PMID:18258596

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HGNC: 4716

UNIGENE: Hs.7644

KEGG: hsa:3006

STRING: 9606.ENSP00000339566

OMIM: 142710