HIST1H2AC

H2AC6
Identifiers
Aliases	H2AC6, H2A/l, H2AFL, dJ221C16.4, histone cluster 1, H2ac, histone cluster 1 H2A family member c, HIST1H2AC, H2A clustered histone 6
External IDs	OMIM: 602794 MGI: 2448302 HomoloGene: 130459 GeneCards: H2AC6
Gene location (Human)
Chr.	Chromosome 6 (human)[1]
End	26,139,116 bp[1]
Gene location (Mouse)
Chr.	Chromosome 13 (mouse)[2]
End	21,995,114 bp[2]
RNA expression pattern
	Top expressed in
	monocyte; ; blood; ; pericardium; ; jejunal mucosa; ; optic nerve; ; bone marrow; ; prostate; ; bone marrow cells; ; periodontal fiber; ; corpus callosum;
	Top expressed in
	neural tube; ; urinary bladder; ; blastocyst; ; morula; ; bone marrow; ; mesencephalon; ; spermatocyte; ; limb; ; white adipose tissue; ; stomach;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	protein heterodimerization activity; DNA binding; molecular function;
Cellular component	nucleosome; nucleus; chromosome; extracellular exosome; nucleoplasm;
Biological process	negative regulation of cell population proliferation; chromatin organization;
	Sources:Amigo / QuickGO
Orthologs
	8334
	665433
	ENSG00000180573
	ENSMUSG00000094248
	Q93077
C0HKE2; B2RVF0; C0HKE1; C0HKE3; C0HKE4;
	C0HKE5; C0HKE6; C0HKE7; C0HKE8; C0HKE9
	NM_003512
	NM_001177544
	NP_003503
NP_835496; NP_835495; NP_835494; NP_835491; NP_835489;
	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
	Wikidata
View/Edit Human	View/Edit Mouse

Histone H2A type 1-C is a protein that in humans is encoded by the HIST1H2AC gene.[5][6][7]

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. Transcripts from this gene lack polyA tails but instead contain a palindromic termination element. This gene is found in the large histone gene cluster on chromosome 6.[7]

Cancer

HIST1H2AC gene has been observed progressively downregulated in Human papillomavirus-positive neoplastic keratinocytes derived from uterine cervical preneoplastic lesions at different levels of malignancy.[8] For this reason, HIST1H2AC is likely to be associated with tumorigenesis and may be a potential prognostic marker for uterine cervical preneoplastic lesions progression.[8]

References

GRCh38: Ensembl release 89: ENSG00000180573 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000094248 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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.
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.
"Entrez Gene: HIST1H2AC histone cluster 1, H2ac".
Rotondo JC, Bosi S, Bassi C, Ferracin M, Lanza G, Gafà R, Magri E, Selvatici R, Torresani S, Marci R, Garutti P, Negrini M, Tognon M, Martini F (April 2015). "Gene expression changes in progression of cervical neoplasia revealed by microarray analysis of cervical neoplastic keratinocytes". J Cell Physiol. 230 (4): 802–812. doi:10.1002/jcp.24808. hdl:11392/2066612. PMID 25205602. S2CID 24986454.

Ruddy DA, Kronmal GS, Lee VK, et al. (1997). "A 1.1-Mb transcript map of the hereditary hemochromatosis locus". Genome Res. 7 (5): 441–56. doi:10.1101/gr.7.5.441. PMID 9149941.
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. S2CID 38539096.
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.
Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID 15635413. S2CID 4344740.
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.
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.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000180573 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000094248 - 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.

[pmid9119399-5] 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.

[pmid12408966-6] 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.

[entrez-7] "Entrez Gene: HIST1H2AC histone cluster 1, H2ac".

[Rotondo_2015-8] Rotondo JC, Bosi S, Bassi C, Ferracin M, Lanza G, Gafà R, Magri E, Selvatici R, Torresani S, Marci R, Garutti P, Negrini M, Tognon M, Martini F (April 2015). "Gene expression changes in progression of cervical neoplasia revealed by microarray analysis of cervical neoplastic keratinocytes". J Cell Physiol. 230 (4): 802–812. doi:10.1002/jcp.24808. hdl:11392/2066612. PMID 25205602. S2CID 24986454.

HIST1H2AC

Cancer

References

Further reading