HIST1H2AB

Histone H2A type 1-B/E is a protein that in humans is encoded by the HIST1H2AB gene.[5][6][7][8]

H2AC4
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2CV5, 3A6N, 3AFA, 3AN2, 3AV1, 3AV2, 3AYW, 3AZE, 3AZF, 3AZG, 3AZH, 3AZI, 3AZJ, 3AZK, 3AZL, 3AZM, 3AZN, 3W96, 3W97, 3W98, 3W99, 3WKJ, 3WTP, 5CPJ, 5B0Z, 4YM5, 5AV9, 5AVB, 5AV5, 4YM6, 5CPI, 3X1V, 5AV6, 3X1S, 5AV8, 5CPK, 5AVC, 5B0Y, 4Z5T, 5B24, 2RVQ, 5B40, 5AY8, 5B2I, 5B2J
Identifiers
Aliases	H2AC4, H2A/m, H2AFM, histone cluster 1, H2ab, histone cluster 1 H2A family member b, HIST1H2AB, H2A clustered histone 4, H2AC8
External IDs	OMIM: 602795 MGI: 2448293 HomoloGene: 135982 GeneCards: H2AC4
Gene location (Human) Chr. Chromosome 6 (human)[1] Band 6p22.2 Start 26,033,176 bp[1] End 26,033,568 bp[1]
Gene location (Mouse) Chr. Chromosome 13 (mouse)[2] Band 13|13 A3.1 Start 22,042,460 bp[2] End 22,042,944 bp[2]
Gene ontology Molecular function • DNA binding • protein heterodimerization activity • GO:0001948 protein binding Cellular component • nuclear chromatin • nucleosome • extracellular exosome • cell nucleus • chromosome Biological process • chromatin silencing • negative regulation of cell proliferation • chromatin organization Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	8335	319167
Ensembl	ENSG00000278463	ENSMUSG00000069301
UniProt	P04908	C0HKE2 B2RVF0 C0HKE1 C0HKE3 C0HKE4 C0HKE5 C0HKE6 C0HKE7 C0HKE8 C0HKE9
RefSeq (mRNA)	NM_003513	NM_178186
RefSeq (protein)	NP_003504	NP_001171015.1 NP_783591.2 NP_835489.1 NP_835491.1 NP_835492.1 NP_835493.1 NP_835494.1 NP_835495.1 NP_835496.1 NP_835493 NP_835496 NP_835489 NP_835495 NP_835494 NP_835492 NP_835491 NP_783591 NP_001171015 NP_783591 NP_835493 NP_835496 NP_835489 NP_835495 NP_835494 NP_835491 NP_835492 NP_783591 NP_001171015 NP_835489 NP_001171015 NP_835496 NP_835491 NP_835493 NP_835494 NP_835495 NP_835492 NP_783591 NP_835494 NP_835489 NP_835495 NP_835491 NP_835492 NP_783591 NP_001171015 NP_835493 NP_835496 NP_835495 NP_835489 NP_835494 NP_835491 NP_835492 NP_783591 NP_001171015 NP_835493 NP_835496 NP_835492 NP_835491 NP_835489 NP_835495 NP_835494 NP_783591 NP_001171015 NP_835493 NP_835496 NP_835491 NP_835489 NP_835495 NP_835494 NP_835492 NP_783591 NP_001171015 NP_835493 NP_835496 NP_783591 NP_835489 NP_835495 NP_835494 NP_835491 NP_835492 NP_001171015 NP_835493 NP_835496 NP_783591 NP_835489 NP_835495 NP_835494 NP_835491 NP_835492 NP_001171015 NP_835493 NP_835496
Location (UCSC)	Chr 6: 26.03 – 26.03 Mb	Chr 13: 22.04 – 22.04 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. This structure consists of approximately 146 bp of DNA wrapped around a nucleosome, an 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 lack polyA tails; instead, they contain a palindromic termination element. This gene is found in the large histone gene cluster on chromosome 6p22-p21.3.[8]

References

1. GRCh38: Ensembl release 89: ENSG00000278463 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000069301 - 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. 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.
6. Albig W, Kioschis P, Poustka A, Meergans K, Doenecke D (Apr 1997). "Human histone gene organization: nonregular arrangement within a large cluster". Genomics. 40 (2): 314–22. doi:10.1006/geno.1996.4592. PMID 9119399.
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: HIST1H2AB histone cluster 1, H2ab".

Further reading

• Zhong R, Roeder RG, Heintz N (1984). "The primary structure and expression of four cloned human histone genes". Nucleic Acids Res. 11 (21): 7409–25. doi:10.1093/nar/11.21.7409. PMC 326492. PMID 6647026.
• 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. 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.
• Citterio E, Papait R, Nicassio F, et al. (2004). "Np95 is a histone-binding protein endowed with ubiquitin ligase activity". Mol. Cell. Biol. 24 (6): 2526–35. doi:10.1128/MCB.24.6.2526-2535.2004. PMC 355858. PMID 14993289.
• 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.
• Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.
• 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.