HIST2H2AC

Histone H2A type 2-C is a protein that in humans is encoded by the HIST2H2AC gene.[5][6][7][8]

H2AC20
Identifiers
Aliases	H2AC20, H2A, H2A-GL101, H2A/q, H2AFQ, histone cluster 2, H2ac, histone cluster 2 H2A family member c, H2A clustered histone 20, HIST2H2AC
External IDs	OMIM: 602797 MGI: 2448316 HomoloGene: 128596 GeneCards: H2AC20
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1q21.2 Start 149,886,975 bp[1] End 149,887,364 bp[1]
Gene location (Mouse) Chr. Chromosome 3 (mouse)[2] Band 3|3 F2.1 Start 96,220,361 bp[2] End 96,220,880 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • protein heterodimerization activity • DNA binding • molecular function Cellular component • nucleosome • cell nucleus • chromosome • nuclear chromatin • extracellular exosome Biological process • chromatin silencing • chromatin organization • biological process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	8338	319176
Ensembl	ENSG00000184260	ENSMUSG00000068855
UniProt	Q16777	Q64523
RefSeq (mRNA)	NM_003517	NM_175662
RefSeq (protein)	NP_003508	NP_783593
Location (UCSC)	Chr 1: 149.89 – 149.89 Mb	Chr 3: 96.22 – 96.22 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[8]

References

1. GRCh38: Ensembl release 89: ENSG00000184260 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000068855 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Collart D, Romain PL, Huebner K, Pockwinse S, Pilapil S, Cannizzaro LA, Lian JB, Croce CM, Stein JL, Stein GS (Jan 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.
6. Albig W, Doenecke D (Feb 1998). "The human histone gene cluster at the D6S105 locus". Hum Genet. 101 (3): 284–94. doi:10.1007/s004390050630. PMID 9439656.
7. Marzluff WF, Gongidi P, Woods KR, Jin J, Maltais LJ (Oct 2002). "The human and mouse replication-dependent histone genes". Genomics. 80 (5): 487–98. doi:10.1016/S0888-7543(02)96850-3. PMID 12408966.
8. "Entrez Gene: HIST2H2AC histone cluster 2, H2ac".

Further reading

• 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. doi:10.1128/mcb.18.5.2535. PMC 110633. 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. doi:10.1046/j.1365-2443.1998.00229.x. 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. PMC 124363. PMID 12072557.
• 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. PMC 139241. 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. PMC 151047. 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. doi:10.1046/j.1365-2443.2003.00656.x. 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. PMC 291826. 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. PMC 395847. 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. PMC 528928. 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.