HIST1H1C (Ab-26) Antibody

1. Research indicates that a network of E2F target genes is susceptible to the regulatory influence of H1.2. H1.2 enhances the global association of pRb with chromatin, leading to increased transcriptional repression by pRb and facilitating pRb-dependent cell cycle arrest. PMID: 28614707
2. BRG1 participates in gene repression by interacting with H1.2. This interaction facilitates the deposition of H1.2 and stabilizes nucleosome positioning around the transcription start site. PMID: 27390128
3. Studies have shown that histones H1.2 and H1.4 are present in MDA-MB-231 metastatic breast cancer cells. Phosphorylation at S173 of histone H1.2 and S172, S187, T18, T146, and T154 of H1.4 significantly increases during the M phase, suggesting that these events are cell cycle-dependent. The study also 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 represent a 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 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. Promoters enriched in H1.2 are distinct 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 are linked to the pathogenesis of follicular lymphoma. PMID: 24435047
9. Data suggest that the p53 acetylation-H1.2 phosphorylation cascade serves as a unique mechanism for triggering p53-dependent DNA damage response pathways. PMID: 22249259
10. Research has confirmed N-terminal acetylation on all isoforms, along with 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 suggests that histone H1 may play a significant 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. Studies demonstrate 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

OMIM: 142710

KEGG: hsa:3006

STRING: 9606.ENSP00000339566

UniGene: Hs.7644