Histone H3.2 (HIST2H3D)
The protein contains 136 amino acids for an estimated molecular weight of 15388 Da.
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. (updated: April 1, 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.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- 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.
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:rs2664732 | |
| dbSNP:rs2664731 |
Biological Process
Amyloid fibril formation
Blood coagulation
Cellular protein metabolic process
Chromatin organization
DNA methylation on cytosine
Gene expression
Interleukin-7-mediated signaling pathway
Negative regulation of gene expression, epigenetic
Negative regulation of transcription by RNA polymerase II
Nucleosome assembly
Positive regulation of gene expression, epigenetic
RDNA heterochromatin assembly
Regulation of androgen receptor signaling pathway
Regulation of gene expression, epigenetic
Regulation of gene silencing by miRNA
Regulation of hematopoietic stem cell differentiation
Regulation of megakaryocyte differentiation
Molecular Function
DNA binding
Histone binding
Nucleosomal DNA binding
Protein heterodimerization activity
The reference OMIM entry for this protein is 142780
Histone gene cluster 2, h3 histone family, member c; hist2h3c
Histone gene cluster 2, h3c
Hist2 cluster, h3c
H3 histone, family 2; h3f2
H3 histone family, member n; h3fn
H3 histone family, member m; h3fm
H3/m
H3.2
For background information on histones, histone gene clusters, and the H3 histone family, see HIST1H3A (602810).
CLONING
By genomic sequence analysis, Marzluff et al. (2002) identified the human HIST2H3C gene. The protein encoded by HIST2H3C, designated H3.2, differs from H3.1, which is encoded by multiple H3 genes (see 602810), at only 1 residue, and from histone H3.3, which is encoded by both H3F3A (601128) and H3F3B (601058), at a few residues. Using Northern blot analysis, Frank et al. (2003) assayed for expression of the replacement histones H3.3A (H3F3A) and H3.3B (H3F3B) and the cell cycle-dependent histone H3/m in human tissues and cell lines. All 6 cell lines expressed H3.3A, H3.3B, and H3/m at high levels. Conversely, fetal liver predominantly expressed H3/m, likely due to its rapid cell growth, whereas adult liver, kidney, and heart predominantly expressed H3.3A and H3.3B. The H3/m transcript was detected at 0.6 kb.MAPPING
By study of mouse-human cell hybrids and by in situ hybridization, Green et al. (1984) showed that H3 and H4 histone genes are on chromosome 1q, probably 1q21. The nomenclature committee of the Human Gene Mapping Workshops designated the histone genes on chromosome 1q21 as H3 histone, family 2, and H4 histone, family 2 (HIST2H4A; 142750) (McAlpine, 1989). By genomic sequence analysis, Marzluff et al. (2002) determined that the histone gene cluster on chromosome 1q21, which they called histone gene cluster-2 (HIST2), contains 6 histone genes, including HIST2H3C. The cluster also contains 2 H3 pseudogenes, designated HIST2H3A and HIST2H3B.GENE FUNCTION
See HIST1H3A (602810) for functional information on the H3 histone family. - H3.2 Histone Hake et al. (2006) noted that most studies on expression or posttranslational modifications of H3 histones do not differentiate between the H3.1, H3.2, and H3.3 proteins, in part due to their high degree of amino acid identity. By quantitative PCR of 5 human cell lines, they found that the 9 H3.1 genes, 1 H3.2 gene, and 2 H3.3 genes examined were expressed in a cell line-specific manner. All 3 types of H3 genes were highly expressed during S phase in human cell lines, whereas the H3.3 genes were also highly expressed outside of S phase, consistent with their status as replication-independent genes. Using a combination of isotopic labeling and quantitative tandem mass spectrometry, Hake et al. (2006) showed that the H3.1, H3.2, and H3.3 proteins differed in their posttranslational modifications. H3.1 was enriched in marks associated with both gene activation and gene silencing, H3.2 was enriched in repressive marks associated with gene silencing and the formation of facultative heterochromatin, and H3.3 was enriched in marks associated with transcriptional activation. Hake et al. (2006) concluded that H3.1, H3.2, and H3.3 likely have unique functions and should not be treated as equivalent proteins. ... 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 25, 2017: Additional information
No protein expression data in P. Mayeux work for HIST2H3D
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 142780 was added.