HIST2H2AC

From Wikipedia, the free encyclopedia

Histone cluster 2, H2ac

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)

HIST2H2AC; H2A; H2A/q; H2A-GL101; H2AFQ; MGC74460

External IDs

OMIM: 602797 MGI: 2448316 HomoloGene: 68327

Gene ontology
Molecular Function:	• DNA binding
Cellular Component:	• nucleosome • nucleus • chromosome
Biological Process:	• nucleosome assembly • chromosome organization and biogenesis (sensu Eukaryota)

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_003517 (mRNA)
NP_003508 (protein)

NM_175662 (mRNA)
NP_783593 (protein)

Location

Chr 1: 148.13 - 148.13 Mb

Chr 3: 96.31 - 96.31 Mb

Pubmed search

[1]

[2]

Histone cluster 2, H2ac, also known as HIST2H2AC, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: HIST2H2AC histone cluster 2, H2ac.

[edit] Further reading

Collart D, Romain PL, Huebner K, et al. (1993). "A human histone H2B.1 variant gene, located on chromosome 1, utilizes alternative 3' end processing.". J. Cell. Biochem. 50 (4): 374-85. doi:10.1002/jcb.240500406. PMID 1469070.
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.
Kimura A, Horikoshi M (1999). "Tip60 acetylates six lysines of a specific class in core histones in vitro.". Genes Cells 3 (12): 789-800. PMID 10096020.
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.
Chen A, Kleiman FE, Manley JL, et al. (2002). "Autoubiquitination of the BRCA1*BARD1 RING ubiquitin ligase.". J. Biol. Chem. 277 (24): 22085-92. doi:10.1074/jbc.M201252200. PMID 11927591.
Lahn BT, Tang ZL, Zhou J, et al. (2002). "Previously uncharacterized histone acetyltransferases implicated in mammalian spermatogenesis.". Proc. Natl. Acad. Sci. U.S.A. 99 (13): 8707-12. doi:10.1073/pnas.082248899. PMID 12072557.
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.
Yoon HG, Chan DW, Huang ZQ, et al. (2003). "Purification and functional characterization of the human N-CoR complex: the roles of HDAC3, TBL1 and TBLR1.". EMBO J. 22 (6): 1336-46. doi:10.1093/emboj/cdg120. PMID 12628926.
Fujita K, Shimazaki N, Ohta Y, et al. (2004). "Terminal deoxynucleotidyltransferase forms a ternary complex with a novel chromatin remodeling protein with 82 kDa and core histone.". Genes Cells 8 (6): 559-71. PMID 12786946.
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.
Braastad CD, Hovhannisyan H, van Wijnen AJ, et al. (2005). "Functional characterization of a human histone gene cluster duplication.". Gene 342 (1): 35-40. doi:10.1016/j.gene.2004.07.036. PMID 15527963.
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.