HIST2H2AB

Histone cluster 2, H2ab, also known as HIST2H2AB, is a human gene.cite web | title = Entrez Gene: HIST2H2AB histone cluster 2, H2ab| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=317772| accessdate = ]

PBB_Summary
section_title =
summary_text = 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 contain a palindromic termination element.cite web | title = Entrez Gene: HIST2H2AB histone cluster 2, H2ab| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=317772| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=El Kharroubi A, Piras G, Zensen R, Martin MA |title=Transcriptional activation of the integrated chromatin-associated human immunodeficiency virus type 1 promoter. |journal=Mol. Cell. Biol. |volume=18 |issue= 5 |pages= 2535–44 |year= 1998 |pmid= 9566873 |doi=
*cite journal | author=Deng L, de la Fuente C, Fu P, "et al." |title=Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. |journal=Virology |volume=277 |issue= 2 |pages= 278–95 |year= 2001 |pmid= 11080476 |doi= 10.1006/viro.2000.0593
*cite journal | author=Deng L, Wang D, de la Fuente C, "et al." |title=Enhancement of the p300 HAT activity by HIV-1 Tat on chromatin DNA. |journal=Virology |volume=289 |issue= 2 |pages= 312–26 |year= 2001 |pmid= 11689053 |doi= 10.1006/viro.2001.1129
*cite journal | author=Chen A, Kleiman FE, Manley JL, "et al." |title=Autoubiquitination of the BRCA1*BARD1 RING ubiquitin ligase. |journal=J. Biol. Chem. |volume=277 |issue= 24 |pages= 22085–92 |year= 2002 |pmid= 11927591 |doi= 10.1074/jbc.M201252200
*cite journal | author=Marzluff WF, Gongidi P, Woods KR, "et al." |title=The human and mouse replication-dependent histone genes. |journal=Genomics |volume=80 |issue= 5 |pages= 487–98 |year= 2003 |pmid= 12408966 |doi=
*cite journal | author=Lusic M, Marcello A, Cereseto A, Giacca M |title=Regulation of HIV-1 gene expression by histone acetylation and factor recruitment at the LTR promoter. |journal=EMBO J. |volume=22 |issue= 24 |pages= 6550–61 |year= 2004 |pmid= 14657027 |doi= 10.1093/emboj/cdg631
*cite journal | author=Zhang Y, Griffin K, Mondal N, Parvin JD |title=Phosphorylation of histone H2A inhibits transcription on chromatin templates. |journal=J. Biol. Chem. |volume=279 |issue= 21 |pages= 21866–72 |year= 2004 |pmid= 15010469 |doi= 10.1074/jbc.M400099200
*cite journal | author=Aihara H, Nakagawa T, Yasui K, "et al." |title=Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 during mitosis in the early Drosophila embryo. |journal=Genes Dev. |volume=18 |issue= 8 |pages= 877–88 |year= 2004 |pmid= 15078818 |doi= 10.1101/gad.1184604
*cite journal | author=Wang H, Wang L, Erdjument-Bromage H, "et al." |title=Role of histone H2A ubiquitination in Polycomb silencing. |journal=Nature |volume=431 |issue= 7010 |pages= 873–8 |year= 2004 |pmid= 15386022 |doi= 10.1038/nature02985
*cite journal | author=Hagiwara T, Hidaka Y, Yamada M |title=Deimination of histone H2A and H4 at arginine 3 in HL-60 granulocytes. |journal=Biochemistry |volume=44 |issue= 15 |pages= 5827–34 |year= 2005 |pmid= 15823041 |doi= 10.1021/bi047505c
*cite journal | author=Cao R, Tsukada Y, Zhang Y |title=Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing. |journal=Mol. Cell |volume=20 |issue= 6 |pages= 845–54 |year= 2006 |pmid= 16359901 |doi= 10.1016/j.molcel.2005.12.002
*cite journal | author=Bergink S, Salomons FA, Hoogstraten D, "et al." |title=DNA damage triggers nucleotide excision repair-dependent monoubiquitylation of histone H2A. |journal=Genes Dev. |volume=20 |issue= 10 |pages= 1343–52 |year= 2006 |pmid= 16702407 |doi= 10.1101/gad.373706
*cite journal | author=Gregory SG, Barlow KF, McLay KE, "et al." |title=The DNA sequence and biological annotation of human chromosome 1. |journal=Nature |volume=441 |issue= 7091 |pages= 315–21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727

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