HIST1H2AH

HIST1H2AH

Histone cluster 1, H2ah, also known as HIST1H2AH, is a human gene.cite web | title = Entrez Gene: HIST1H2AH histone cluster 1, H2ah| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=85235| accessdate = ]

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summary_text = Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. This gene is intronless and encodes a member of the histone H2A family. Transcripts from this gene lack polyA tails but instead contain a palindromic termination element. This gene is found in the histone microcluster on chromosome 6p21.33.cite web | title = Entrez Gene: HIST1H2AH histone cluster 1, H2ah| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=85235| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
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*cite journal | author=Albig W, Trappe R, Kardalinou E, "et al." |title=The human H2A and H2B histone gene complement. |journal=Biol. Chem. |volume=380 |issue= 1 |pages= 7–18 |year= 1999 |pmid= 10064132 |doi=
*cite journal | author=Ahn J, Gruen JR |title=The genomic organization of the histone clusters on human 6p21.3. |journal=Mamm. Genome |volume=10 |issue= 7 |pages= 768–70 |year= 1999 |pmid= 10384058 |doi=
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*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
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*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
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*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
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*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=Bonenfant D, Coulot M, Towbin H, "et al." |title=Characterization of histone H2A and H2B variants and their post-translational modifications by mass spectrometry. |journal=Mol. Cell Proteomics |volume=5 |issue= 3 |pages= 541–52 |year= 2006 |pmid= 16319397 |doi= 10.1074/mcp.M500288-MCP200
*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=Kimura H, Takizawa N, Allemand E, "et al." |title=A novel histone exchange factor, protein phosphatase 2Cgamma, mediates the exchange and dephosphorylation of H2A-H2B. |journal=J. Cell Biol. |volume=175 |issue= 3 |pages= 389–400 |year= 2006 |pmid= 17074886 |doi= 10.1083/jcb.200608001

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