HIST1H2AE

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Histone cluster 1, H2ae
PDB rendering based on 1aoi.
Available structures: 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
Symbol(s) HIST1H2AE; H2A.1; H2A.2; H2A/a; H2AFA
External IDs OMIM: 602786 MGI: 2448309 HomoloGene: 88879
Orthologs
Human Mouse
Entrez 3012 319173
Ensembl n/a ENSMUSG00000061991
Uniprot n/a Q08AU5
Refseq NM_021052 (mRNA)
NP_066390 (protein)		 NM_175661 (mRNA)
NP_783592 (protein)
Location n/a Chr 13: 23.54 - 23.54 Mb
Pubmed search [1] [2]

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

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.[1]

[edit] References

  1. ^ a b Entrez Gene: HIST1H2AE histone cluster 1, H2ae.

[edit] 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. 
  • 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. 
  • 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. 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. 
  • 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. 
  • 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. 
  • 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. 
  • Marzluff WF, Gongidi P, Woods KR, et al. (2003). "The human and mouse replication-dependent histone genes.". Genomics 80 (5): 487-98. 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. PMID 12477932. 
  • 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. 
  • 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. 
  • 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. 
  • 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. 
  • 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. 
  • 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. 
  • 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. 
  • 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. 
  • 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. 
  • 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. 
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