HIST3H2A

H2AW
Identifiers
Aliases	H2AW , histone cluster 3 H2A, HIST3H2A, H2A.W histone
External IDs	OMIM: 615015 MGI: 2448458 HomoloGene: 137357 GeneCards: H2AW
Gene location (Human) Chr. Chromosome 1 (human) [1] Band 1q42.13 Start 228,434,777 bp [1] End 228,457,873 bp [1]
Gene location (Mouse) Chr. Chromosome 11 (mouse) [2] Band 11|11 B1.3 Start 58,845,511 bp [2] End 58,847,656 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in cerebellar hemisphere ganglionic eminence right adrenal gland nucleus accumbens prefrontal cortex putamen left ventricle Brodmann area 9 caudate nucleus vagina Top expressed in spermatocyte retinal pigment epithelium medial ganglionic eminence mirror external carotid artery ciliary body olfactory bulb trigeminal ganglion neural tube supraoptic nucleus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function DNA binding protein heterodimerization activity protein binding Cellular component nucleosome extracellular exosome nucleus chromosome Biological process nucleosome disassembly UV-damage excision repair chromatin organization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 92815 319162 Ensembl ENSG00000181218 ENSG00000284841 ENSMUSG00000078851 UniProt Q7L7L0 Q8BFU2 RefSeq (mRNA) NM_033445 NM_178218 RefSeq (protein) NP_254280 NP_835736 Location (UCSC) Chr 1: 228.43 – 228.46 Mb Chr 11: 58.85 – 58.85 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Histone H2A type 3 is a protein that in humans is encoded by the HIST3H2A gene. ^{[5] [6]}

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. ^[6]

References

1. ENSG00000284841 GRCh38: Ensembl release 89: ENSG00000181218, ENSG00000284841 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000078851 - 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. 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.
6. "Entrez Gene: HIST3H2A histone cluster 3, H2a".

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.
• 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.
• 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.
• 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.
• 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.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID   16189514. S2CID   4427026.
• Cao R, Tsukada Y, Zhang Y (2006). "Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing". Mol. Cell. 20 (6): 845–54. doi: 10.1016/j.molcel.2005.12.002 . PMID   16359901.
• Bergink S, Salomons FA, Hoogstraten D, et al. (2006). "DNA damage triggers nucleotide excision repair-dependent monoubiquitylation of histone H2A". Genes Dev. 20 (10): 1343–52. doi:10.1101/gad.373706. PMC   1472908 . PMID   16702407.
• Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. Bibcode:2006Natur.441..315G. doi: 10.1038/nature04727 . PMID   16710414.