HIST1H2AB

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Histone cluster 1, H2ab
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) HIST1H2AB; H2A/m; H2AFM
External IDs OMIM: 602795 MGI: 2448287 HomoloGene: 69326
Orthologs
Human Mouse
Entrez 8335 319164


Refseq NM_003513 (mRNA)
NP_003504 (protein)		 NM_178189 (mRNA)
NP_835496 (protein)
Pubmed search [1] [2]

Histone cluster 1, H2ab, also known as HIST1H2AB, is a human gene.[1]

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 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: HIST1H2AB histone cluster 1, H2ab.

[edit] Further reading

  • Zhong R, Roeder RG, Heintz N (1984). "The primary structure and expression of four cloned human histone genes.". Nucleic Acids Res. 11 (21): 7409–25. PMID 6647026. 
  • 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. 
  • 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. 
  • 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. 
  • 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. 
  • Citterio E, Papait R, Nicassio F, et al. (2004). "Np95 is a histone-binding protein endowed with ubiquitin ligase activity.". Mol. Cell. Biol. 24 (6): 2526–35. PMID 14993289. 
  • 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. 
  • Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics.". Nature 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413. 
  • 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. 
  • 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. 
  • Bergink S, Salomons FA, Hoogstraten D, et al. (2006). "DNA damage triggers nucleotide excision repair-dependent monoubiquitylation of histone H2A.". Genes Dev. 20 (10): 1343–52. doi:10.1101/gad.373706. PMID 16702407. 
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