HIST2H2AC

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 149,886,918 bp [1] End 149,887,411 bp [1]
Gene location (Mouse) Chr. Chromosome 3 (mouse) [2] Band 3|3 F2.1 Start 96,127,677 bp [2] End 96,128,196 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Achilles tendon bone marrow cells corpus callosum sural nerve blood thymus cervix monocyte right adrenal gland gastric mucosa Top expressed in uterus spermatocyte mesencephalon yolk sac bone marrow morula stomach mirror neural tube testicle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein heterodimerization activity DNA binding molecular function Cellular component nucleosome nucleus chromosome extracellular exosome Biological process 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: 96.13 – 96.13 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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

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. S2CID   7732783.
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. S2CID   38539096.
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. Bibcode:2002PNAS...99.8707L. 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. Bibcode:2002PNAS...9916899M. 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. S2CID   25223336.
• 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. Bibcode:2004Natur.431..873W. doi:10.1038/nature02985. PMID   15386022. S2CID   4344378.
• 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.