HIST1H2AE

Histone H2A type 1-B/E is a protein that in humans is encoded by the HIST1H2AE gene.[4][5][6][7]

H2AC8
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	H2AC8, H2A.1, H2A.2, H2A/a, H2AFA, histone cluster 1, H2ae, histone cluster 1 H2A family member e, HIST1H2AE, H2A clustered histone 8, H2AC4
External IDs	OMIM: 602786 MGI: 2448457 HomoloGene: 135791 GeneCards: H2AC8
Gene location (Human) Chr. Chromosome 6 (human)[1] Band 6p22.2 Start 26,216,975 bp[1] End 26,217,483 bp[1]
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	3012	319191
Ensembl	ENSG00000277075	n/a
UniProt	P04908	C0HKE2 B2RVF0 C0HKE1 C0HKE3 C0HKE5 C0HKE4 C0HKE6 C0HKE7 C0HKE8 C0HKE9
RefSeq (mRNA)	NM_021052	NM_178182
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_835495 NP_835489 NP_835494 NP_835491 NP_835492 NP_783591 NP_001171015 NP_835493 NP_835496 NP_835494 NP_835489 NP_835495 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: 26.22 – 26.22 Mb	n/a
PubMed search	[2]	[3]
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. 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 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.[7]

References

1. GRCh38: Ensembl release 89: ENSG00000277075 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. 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.
5. Albig W, Kardalinou E, Drabent B, Zimmer A, Doenecke D (Nov 1991). "Isolation and characterization of two human H1 histone genes within clusters of core histone genes". Genomics. 10 (4): 940–8. doi:10.1016/0888-7543(91)90183-F. PMID 1916825.
6. 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.
7. "Entrez Gene: HIST1H2AE histone cluster 1, H2ae".

Further reading

• Rodriguez P, Munroe D, Prawitt D, et al. (1997). "Functional characterization of human nucleosome assembly protein-2 (NAP1L4) suggests a role as a histone chaperone". Genomics. 44 (3): 253–65. doi:10.1006/geno.1997.4868. PMID 9325046.
• Albig W, Doenecke D (1998). "The human histone gene cluster at the D6S105 locus". Hum. Genet. 101 (3): 284–94. doi:10.1007/s004390050630. PMID 9439656.
• 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.
• Galasinski SC, Louie DF, Gloor KK, et al. (2002). "Global regulation of post-translational modifications on core histones". J. Biol. Chem. 277 (4): 2579–88. doi:10.1074/jbc.M107894200. PMID 11709551.
• 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.
• Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6". Nature. 425 (6960): 805–11. doi:10.1038/nature02055. PMID 14574404.
• 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.
• 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.
• 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.
• Boyne MT, Pesavento JJ, Mizzen CA, Kelleher NL (2006). "Precise characterization of human histones in the H2A gene family by top down mass spectrometry". J. Proteome Res. 5 (2): 248–53. doi:10.1021/pr050269n. PMID 16457589.