HIST1H2AE

Histone cluster 1, H2ae
File:PBB Protein HIST1H2AE image.jpg PDB rendering based on 1aoi.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1aoi​, 1eqz​, 1hio​, 1hq3​, 1kx3​, 1kx4​, 1kx5​, 1m18​, 1m19​, 1m1a​, 1p34​, 1p3a​, 1p3b​, 1p3f​, 1p3g​, 1p3i​, 1p3k​, 1p3l​, 1p3m​, 1p3o​, 1p3p​, 1s32​, 1tzy​, 1zbb​, 1zla​, 2aro​, 2cv5​, 2f8n​, 2fj7​, 2hio​, 2nzd​
Identifiers
Symbols	HIST1H2AE ; H2A.1; H2A.2; H2A/a; H2AFA
External IDs	Template:OMIM5 Template:MGI HomoloGene: 88879
Gene ontology Molecular function Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Histone cluster 1, H2ae, also known as HIST1H2AE, is a human gene.

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone 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 H2A family. Transcripts from this gene lack polyA tails; instead, they contain a palindromic termination element. This gene is found in the large histone gene cluster on chromosome 6p22-p21.3.

Further reading

• Albig W, Kardalinou E, Drabent B; et al. (1991). "Isolation and characterization of two human H1 histone genes within clusters of core histone genes". Genomics. 10 (4): 940–8. PMID 1916825.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Albig W, Kioschis P, Poustka A; et al. (1997). "Human histone gene organization: nonregular arrangement within a large cluster". Genomics. 40 (2): 314–22. doi:10.1006/geno.1996.4592. PMID 9119399.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Albig W, Doenecke D (1998). "The human histone gene cluster at the D6S105 locus". Hum. Genet. 101 (3): 284–94. 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. PMID 9566873.CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Galasinski SC, Louie DF, Gloor KK; et al. (2002). "Global regulation of post-translational modifications on core histones". J. Biol. Chem. 277 (4): 2579–88. doi:10.1074/jbc.M107894200. PMID 11709551.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Marzluff WF, Gongidi P, Woods KR; et al. (2003). "The human and mouse replication-dependent histone genes". Genomics. 80 (5): 487–98. PMID 12408966.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 12477932.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Mungall AJ, Palmer SA, Sims SK; et al. (2003). "The DNA sequence and analysis of human chromosome 6". Nature. 425 (6960): 805–11. doi:10.1038/nature02055. PMID 14574404.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Lusic M, Marcello A, Cereseto A, Giacca M (2004). "Regulation of HIV-1 gene expression by histone acetylation and factor recruitment at the LTR promoter". EMBO J. 22 (24): 6550–61. doi:10.1093/emboj/cdg631. PMID 14657027.CS1 maint: Multiple names: authors list (link)
• Zhang Y, Griffin K, Mondal N, Parvin JD (2004). "Phosphorylation of histone H2A inhibits transcription on chromatin templates". J. Biol. Chem. 279 (21): 21866–72. doi:10.1074/jbc.M400099200. PMID 15010469.CS1 maint: Multiple names: authors list (link)
• Aihara H, Nakagawa T, Yasui K; et al. (2004). "Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 during mitosis in the early Drosophila embryo". Genes Dev. 18 (8): 877–88. doi:10.1101/gad.1184604. PMID 15078818.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Wang H, Wang L, Erdjument-Bromage H; et al. (2004). "Role of histone H2A ubiquitination in Polycomb silencing". Nature. 431 (7010): 873–8. doi:10.1038/nature02985. PMID 15386022.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Hagiwara T, Hidaka Y, Yamada M (2005). "Deimination of histone H2A and H4 at arginine 3 in HL-60 granulocytes". Biochemistry. 44 (15): 5827–34. doi:10.1021/bi047505c. PMID 15823041.CS1 maint: Multiple names: authors list (link)
• Bonenfant D, Coulot M, Towbin H; et al. (2006). "Characterization of histone H2A and H2B variants and their post-translational modifications by mass spectrometry". Mol. Cell Proteomics. 5 (3): 541–52. doi:10.1074/mcp.M500288-MCP200. PMID 16319397.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Cao R, Tsukada Y, Zhang Y (2006). "Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing". Mol. Cell. 20 (6): 845–54. doi:10.1016/j.molcel.2005.12.002. PMID 16359901.CS1 maint: Multiple names: authors list (link)
• Boyne MT, Pesavento JJ, Mizzen CA, Kelleher NL (2006). "Precise characterization of human histones in the H2A gene family by top down mass spectrometry". J. Proteome Res. 5 (2): 248–53. doi:10.1021/pr050269n. PMID 16457589.CS1 maint: Multiple names: authors list (link)