HIST2H4A

HIST2H4A
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	4H9O, 3WKJ, 3AYW, 3WA9, 5B0Z, 5AVB, 2CV5, 5AV5, 3AV2, 3WTP, 3AV1, 3AZK, 3X1V, 5AV8, 1F66, 4QUU, 3CFS, 4YYK, 4QUT, 3NQJ, 3A6N, 3W99, 5AVC, 2RS9, 3F9Z, 3QZT, 3QBY, 3W97, 4M38, 4YM6, 3CFV, 4HGA, 1EQZ, 2RJE, 3QZV, 1HQ3, 4H9P, 3AZL, 3AFA, 1TZY, 3UVY, 5CPK, 3JPX, 4U9W, 4N3W, 4YYJ, 4YYD, 4H9N, 4H9R, 3AZI, 4LD9, 3UVX, 3AZH, 5BNX, 4N4F, 1U35, 4YYG, 3O36, 2ARO, 5AV9, 4H9S, 3AZF, 3W98, 4GQB, 4H9Q, 5BNV, 3WAA, 3AZG, 3AZE, 2RNY, 1ZKK, 2QQS, 2LVM, 3X1T, 3AN2, 2KWO, 3QZS, 3F9W, 5FFW, 5CPJ, 3F9X, 3IJ1, 4YM5, 3AZJ, 4YY6, 3AZN, 2IG0, 4YYH, 4YYI, 5CPI, 3W96, 3R45, 2KWN, 3F9Y, 5AV6, 3AZM, 5BO0, 3X1S, 4QYD, 4KGC, 3UVW, 4YYN, 3X1U, 3UW9, 2F8N, 3NQU, 5B0Y, 4YYM, 5C3I, 4Z5T, 5B24, 5FA5, 4Z2M, 5E5A, 5FWE, 5B2I, 5B40, 5B2J, 5JA4, 5AY8, 4ZUX
Identifiers
Aliases	HIST2H4A, FO108, H4, H4/n, H4F2, H4FN, HIST2H4, histone cluster 2, H4a, histone cluster 2 H4 family member a
External IDs	MGI: 2448420 HomoloGene: 134466 GeneCards: HIST2H4A
Gene location (Human)
Chr.	Chromosome 1 (human)[1]
End	149,839,767 bp[1]
Gene location (Mouse)
Chr.	Chromosome 13 (mouse)[2]
End	23,757,409 bp[2]
Gene ontology
Molecular function	• protein domain specific binding; • protein binding; • protein heterodimerization activity; • DNA binding; • histone binding; • RNA binding;
Cellular component	• membrane; • chromosome; • protein complex; • nucleoplasm; • extracellular region; • nuclear chromosome; • nucleosome; • extracellular exosome; • cell nucleus; • nuclear chromosome, telomeric region; • extracellular matrix; • nuclear nucleosome;
Biological process	• telomere organization; • cellular protein metabolic process; • positive regulation of gene expression, epigenetic; • protein heterotetramerization; • negative regulation of megakaryocyte differentiation; • CENP-A containing nucleosome assembly; • DNA replication-dependent nucleosome assembly; • chromatin silencing at rDNA; • negative regulation of gene expression, epigenetic; • DNA-templated transcription, initiation; • DNA replication-independent nucleosome assembly; • double-strand break repair via nonhomologous end joining; • beta-catenin-TCF complex assembly; • telomere capping; • nucleosome assembly; • regulation of gene silencing by miRNA; • regulation of megakaryocyte differentiation; • regulation of hematopoietic stem cell differentiation;
	Sources:Amigo / QuickGO
Orthologs
	8370
	326620
	ENSG00000270882
	ENSMUSG00000069266
	P62805
	P62806
	NM_003548
	NM_178193
	NP_003530
	NP_835582
	Wikidata
View/Edit Human	View/Edit Mouse

Histone H4 is a protein that in humans is encoded by the HIST2H4A gene.^[5]^[6]^[7]^[8]

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. This structure consists of approximately 146 bp of DNA wrapped around a nucleosome, an octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4). The chromatin fiber is further compacted through the interaction of a linker histone, H1, with the DNA between the nucleosomes to form higher order chromatin structures. This gene is intronless and encodes a member of the histone H4 family. Transcripts from this gene lack polyA tails; instead, they contain a palindromic termination element. This gene is found in a histone cluster on chromosome 1. This gene is one of four histone genes in the cluster that are duplicated; this record represents the centromeric copy.^[8]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000270882 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000069266 - Ensembl, May 2017
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Pauli U, Chrysogelos S, Stein G, Stein J, Nick H (Jul 1987). "Protein-DNA interactions in vivo upstream of a cell cycle-regulated human H4 histone gene". Science. 236 (4806): 1308–11. doi:10.1126/science.3035717. PMID 3035717.
↑ Sierra F, Stein G, Stein J (Dec 1983). "Structure and in vitro transcription of a human H4 histone gene". Nucleic Acids Res. 11 (20): 7069–86. doi:10.1093/nar/11.20.7069. PMC 326439. PMID 6314274.
↑ Braastad CD, Hovhannisyan H, van Wijnen AJ, Stein JL, Stein GS (Nov 2004). "Functional characterization of a human histone gene cluster duplication". Gene. 342 (1): 35–40. doi:10.1016/j.gene.2004.07.036. PMID 15527963.
1 2 "Entrez Gene: HIST2H4A histone cluster 2, H4a".

Green L, Van Antwerpen R, Stein J, et al. (1984). "A major human histone gene cluster on the long arm of chromosome 1". Science. 226 (4676): 838–40. doi:10.1126/science.6494913. PMID 6494913.
Pelicci G, Lanfrancone L, Salcini AE, et al. (1995). "Constitutive phosphorylation of Shc proteins in human tumors". Oncogene. 11 (5): 899–907. PMID 7675449.
Díaz-Jullien C, Pérez-Estévez A, Covelo G, Freire M (1996). "Prothymosin alpha binds histones in vitro and shows activity in nucleosome assembly assay". Biochim. Biophys. Acta. 1296 (2): 219–27. doi:10.1016/0167-4838(96)00072-6. PMID 8814229.
Rodriguez P, Munroe D, Prawitt D, et al. (1997). "Functional characterization of human nucleosome assembly protein-2 (NAP1L4) suggests a role as a histone chaperone". Genomics. 44 (3): 253–65. doi:10.1006/geno.1997.4868. PMID 9325046.
Albig W, Doenecke D (1998). "The human histone gene cluster at the D6S105 locus". Hum. Genet. 101 (3): 284–94. doi:10.1007/s004390050630. PMID 9439656.
El Kharroubi A, Piras G, Zensen R, Martin MA (1998). "Transcriptional activation of the integrated chromatin-associated human immunodeficiency virus type 1 promoter". Mol. Cell. Biol. 18 (5): 2535–44. doi:10.1128/mcb.18.5.2535. PMC 110633. PMID 9566873.
Kimura A, Horikoshi M (1999). "Tip60 acetylates six lysines of a specific class in core histones in vitro". Genes Cells. 3 (12): 789–800. doi:10.1046/j.1365-2443.1998.00229.x. PMID 10096020.
Deng L, de la Fuente C, Fu P, et al. (2001). "Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones". Virology. 277 (2): 278–95. doi:10.1006/viro.2000.0593. PMID 11080476.
Seo SB, McNamara P, Heo S, et al. (2001). "Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the set oncoprotein". Cell. 104 (1): 119–30. doi:10.1016/S0092-8674(01)00196-9. PMID 11163245.
Deng L, Wang D, de la Fuente C, et al. (2001). "Enhancement of the p300 HAT activity by HIV-1 Tat on chromatin DNA". Virology. 289 (2): 312–26. doi:10.1006/viro.2001.1129. PMID 11689053.
Andersen JS, Lyon CE, Fox AH, et al. (2002). "Directed proteomic analysis of the human nucleolus". Curr. Biol. 12 (1): 1–11. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298.
Weinmann AS, Yan PS, Oberley MJ, et al. (2002). "Isolating human transcription factor targets by coupling chromatin immunoprecipitation and CpG island microarray analysis". Genes Dev. 16 (2): 235–44. doi:10.1101/gad.943102. PMC 155318. PMID 11799066.
Marzluff WF, Gongidi P, Woods KR, et al. (2003). "The human and mouse replication-dependent histone genes". Genomics. 80 (5): 487–98. doi:10.1016/S0888-7543(02)96850-3. PMID 12408966.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Hovhannisyan H, Cho B, Mitra P, et al. (2003). "Maintenance of open chromatin and selective genomic occupancy at the cell cycle-regulated histone H4 promoter during differentiation of HL-60 promyelocytic leukemia cells". Mol. Cell. Biol. 23 (4): 1460–9. doi:10.1128/MCB.23.4.1460-1469.2003. PMC 141140. PMID 12556504.
Yoon HG, Chan DW, Huang ZQ, et al. (2003). "Purification and functional characterization of the human N-CoR complex: the roles of HDAC3, TBL1 and TBLR1". EMBO J. 22 (6): 1336–46. doi:10.1093/emboj/cdg120. PMC 151047. PMID 12628926.
Pivot-Pajot C, Caron C, Govin J, et al. (2003). "Acetylation-dependent chromatin reorganization by BRDT, a testis-specific bromodomain-containing protein". Mol. Cell. Biol. 23 (15): 5354–65. doi:10.1128/MCB.23.15.5354-5365.2003. PMC 165724. PMID 12861021.
Coleman MA, Miller KA, Beernink PT, et al. (2004). "Identification of chromatin-related protein interactions using protein microarrays". Proteomics. 3 (11): 2101–7. doi:10.1002/pmic.200300593. PMID 14595808.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000270882 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000069266 - Ensembl, May 2017

[3] "Human PubMed Reference:".

[4] "Mouse PubMed Reference:".

[pmid3035717-5] Pauli U, Chrysogelos S, Stein G, Stein J, Nick H (Jul 1987). "Protein-DNA interactions in vivo upstream of a cell cycle-regulated human H4 histone gene". Science. 236 (4806): 1308–11. doi:10.1126/science.3035717. PMID 3035717.

[pmid6314274-6] Sierra F, Stein G, Stein J (Dec 1983). "Structure and in vitro transcription of a human H4 histone gene". Nucleic Acids Res. 11 (20): 7069–86. doi:10.1093/nar/11.20.7069. PMC 326439. PMID 6314274.

[pmid15527963-7] Braastad CD, Hovhannisyan H, van Wijnen AJ, Stein JL, Stein GS (Nov 2004). "Functional characterization of a human histone gene cluster duplication". Gene. 342 (1): 35–40. doi:10.1016/j.gene.2004.07.036. PMID 15527963.

[entrez-8] 1 2 "Entrez Gene: HIST2H4A histone cluster 2, H4a".

HIST2H4A

References

Further reading