HIST2H2AB

H2AC21
Identifiers
Aliases	H2AC21 , H2AB, histone cluster 2, H2ab, histone cluster 2 H2A family member b, H2A clustered histone 21, HIST2H2AB
External IDs	OMIM: 615014 MGI: 2448314 HomoloGene: 111318 GeneCards: H2AC21
Gene location (Human) Chr. Chromosome 1 (human) [1] Band 1q21.2 Start 149,887,469 bp [1] End 149,887,965 bp [1]
Gene location (Mouse) Chr. Chromosome 3 (mouse) [2] Band 3|3 F2.1 Start 96,219,865 bp [2] End 96,220,308 bp [2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • DNA binding • protein heterodimerization activity • molecular function Cellular component • nucleosome • extracellular exosome • nucleus • chromosome Biological process • chromatin silencing • chromatin organization • biological process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	317772	621893
Ensembl	ENSG00000184270	ENSMUSG00000063689
UniProt	Q8IUE6	Q64522
RefSeq (mRNA)	NM_175065	NM_178213
RefSeq (protein)	NP_778235	NP_835585
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

Histone H2A type 2-B is a protein that in humans is encoded by the HIST2H2AB 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. GRCh38: Ensembl release 89: ENSG00000184270 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000063689 - 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: HIST2H2AB histone cluster 2, H2ab".

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.
• 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.
• 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.
• 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.
• 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.