Histone H1.2 (HIST1H1C)
The protein contains 213 amino acids for an estimated molecular weight of 21365 Da.
Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). (updated: March 4, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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| Variant | Description |
|---|---|
| dbSNP:rs2230653 | |
| dbSNP:rs34810376 | |
| dbSNP:rs12111009 |
Biological Process
Chromosome condensation
Histone H3-K27 trimethylation
Histone H3-K4 trimethylation
Negative regulation of chromatin silencing
Negative regulation of DNA recombination
Negative regulation of transcription by RNA polymerase II
Nucleosome assembly
Nucleosome positioning
Regulation of transcription, DNA-templated
The reference OMIM entry for this protein is 142710
Histone gene cluster 1, h1 histone family, member c; hist1h1c
Histone gene cluster 1, h1c
Hist1 cluster, h1c
H1c
H1.2
H1 histone family, member 2, formerly; h1f2; formerly
For background information on histones, histone gene clusters, and the H1 histone family, see HIST1H1A (142709).
CLONING
Eick et al. (1989) cloned the genes encoding H1.2 and H1.1 (HIST1H1A; 142709).GENE FUNCTION
Several reports described an activity that modifies nitrotyrosine-containing proteins and their immunoreactivity to antibodies against nitrotyrosine (e.g., Kamisaki et al., 1998). Without knowing the product of the reaction, this activity has been called a 'denitrase.' These studies used some nonspecific proteins that have multiple tyrosine residues, e.g., albumin, as substrate to study the mechanism of the reaction. Irie et al. (2003) developed an assay strategy for determining the substrate for denitrase combining 2D-gel electrophoresis and an on-blot enzyme assay. They found that histone H1.2, an isoform protein of linker histone, was one such substrate. H1.2 has only 1 tyrosine residue in the entire molecule, which ensured the exact position of the substrate to be involved. It had been reported that histones are the most prominent nitrated proteins in cancer tissues. It was also demonstrated that tyrosine nitration of histone H1 occurs in vivo. Conceiving that H1.2 might be an intrinsic substrate for denitrase, they performed further experiments demonstrating that the denitrase activity behaves as an enzymatic activity because the reaction was time-dependent and was destroyed by heat or trypsin treatment. The activity was shown to be specific for histone H1.2, to differ from proteasome activity, and to require no additional cofactors. Konishi et al. (2003) found that histone H1.2 was a cytochrome c-releasing factor that appeared in the cytoplasm after exposure of cells to x-ray irradiation. While all nuclear histone H1 forms were released into the cytoplasm in a p53 (TP53; 191170)-dependent manner after irradiation, only H1.2 induced cytochrome c release from isolated mitochondria in a BAK (BAK1; 600516)-dependent manner. Reducing H1.2 expression enhanced cellular resistance to apoptosis induced by x-ray irradiation or etoposide, but not that induced by other apoptotic stimuli. Thymocytes and small intestines of H1.2-deficient mice exhibited increased cellular resistance to x-ray-induced apoptosis. Konishi et al. (2003) concluded that histone H1.2 has a role in transmitting apoptotic signals from the nucleus to the mitochondria following DNA double-strand breaks. See HIST1H1A (142709) for additional functional information on H1 histones.MAPPING
By PCR analysis of chromosomal DNA from a panel of human/rodent somatic cell hybrids and by fluorescence in situ hybridization, Albig et al. (1993) demonstrated that 6 human histone H1 genes, including H1.2, are located on chromosome 6p22.2-p21.1. By analysis of a YAC contig, Albig et al. (1997) mapped the H1.2 gene to chromosome 6p21.3 within a cluster of 35 histone genes, including H1.1 to H1.4 (HIST1H1E; 142220) and H1T (HIST1H1T; 142712). The H1.5 gene (HIST1H1B; 142711) is part of a separate subcluster within the same chromosomal region. By genomic sequence analysis, Marzluff et al. (2002) determined that the histone gene cluster on chromosome 6p22-p21, which they called histone gene cluster-1 (HIST1), contains 55 histone genes, including HIST1H1C. ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 142710 was added.