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Histones are basic nuclear proteins responsible for nucleosome structure of the chromosomal fiber in eukaryotes. Additionally we are shipping HIST1H1C Antibodies (37) and HIST1H1C Kits (1) and many more products for this protein.
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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.
Histone H1.2-T165 post translational modifications are dispensable for chromatin binding and cell proliferation while the H1.4-K26 (show KRT26 Proteins) modifications are essential for proper cell cycle progression.
H1.2 interacts with Cul4A (show CUL4A Proteins) and PAF1 (show PEX2 Proteins) to activate developmental regulatory genes.
H1.2 is less abundant than other histone H1 (show H1F0 Proteins) variants at the transcription start sites of inactive genes, and promoters enriched in H1.2 are different from those enriched in other histone H1 (show H1F0 Proteins) variants and tend to be repressed.
Mutations in linker histone genes HIST1H1 B, C, D, and E; OCT2 (POU2F2); IRF8; and ARID1A underlying the pathogenesis of follicular lymphoma.
These data suggest that p53 (show TP53 Proteins) acetylation-H1.2 phosphorylation cascade serves as a unique mechanism for triggering p53 (show TP53 Proteins)-dependent DNA damage response pathways.
confirmed N-terminal acetylation on all isoforms plus a single internal acetylation site; phosphorylation sites were located on peptides containing the cyclin dependent kinase (show CDK1 Proteins) (CDK (show CDK4 Proteins)) consensus motif
The binding of histone H1 (show H1F0 Proteins) to a general amyloid-like motif indicates that histone H1 (show H1F0 Proteins) may play an important common role in diseases associated with amyloid-like fibrils.
Histone H1.2 was translocated from the nucleus to the mitochondria after treatment with bleomycin and co-localized with Bak (show BAK1 Proteins) in mitochondria.
that the recruitment of YB1 (show YBX1 Proteins), PURalpha (show PURA Proteins), and H1.2 to the p53 (show TP53 Proteins) target gene Bax (show BAX Proteins) is required for repression of p53 (show TP53 Proteins)-induced transcription.
Histone H1c gene expression is developmentally up-regulated to promote facultative heterochromatin in mature rod photoreceptors.
These results integrate the localization of an understudied type of chromatin proteins, namely the H1 variants, into the epigenome map of mouse ESCs (show NR2E3 Proteins).
The N-terminal domain contributes toward the differential chromatin binding affinity, whereas the C-terminal domain contributes toward distinct nucleosomal interface of isotypes H10 (show H1F0 Proteins) and H1c.
The amount of the linker histone H1c is strongly reduced in nuclear extracts of SCA7 retinas and that the cellular distribution of H1c is particularly altered in the facultative heterochromatin compartment.
The modular pattern of DNA methylation (show HELLS Proteins) in the Ig heavy chain locus and histone modifications appears to be determined by at least 2 factors: the B-cell-specific transcription factor Pax5 (show PAX5 Proteins) and linker histone H1 (show H1F0 Proteins).
These observations reveal a mode of p53 (show TP53 Proteins) regulation mediated by CHD8, which may set a threshold for induction of apoptosis during early embryogenesis by counteracting p53 (show TP53 Proteins) function through recruitment of histone H1 (show H1F0 Proteins).
H1 isoforms H1.0, H1.1, and H1.2 are non-responsive to hormone whereas prolonged dexamethasone treatment effectively dephosphorylated the H1.3, H1.4, and H1.5 isoforms
Histones are basic nuclear proteins responsible for nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. This gene is intronless and encodes a member of the histone H1 family. Transcripts from this gene lack polyA tails but instead contain a palindromic termination element. This gene is found in the large histone gene cluster on chromosome 6.
, histone H1.1
, histone H1.2
, histone H1d
, histone 1, H1c
, histone H1.11L
, H1 histone family, member 2
, histone H1c
, histone H1s-1
, H1 VAR.1
, histone H1
, H1 histone family, member 4
, Histone 1d
, histone H1.4