HIST2H2AC

Protein-coding gene in the species Homo sapiens
H2AC20
Identifiers
AliasesH2AC20, H2A, H2A-GL101, H2A/q, H2AFQ, histone cluster 2, H2ac, histone cluster 2 H2A family member c, H2A clustered histone 20, HIST2H2AC
External IDsOMIM: 602797; MGI: 2448316; HomoloGene: 128596; GeneCards: H2AC20; OMA:H2AC20 - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for H2AC20
Genomic location for H2AC20
Band1q21.2Start149,886,918 bp[1]
End149,887,411 bp[1]
Gene location (Mouse)
Chromosome 3 (mouse)
Chr.Chromosome 3 (mouse)[2]
Chromosome 3 (mouse)
Genomic location for H2AC20
Genomic location for H2AC20
Band3|3 F2.1Start96,127,677 bp[2]
End96,128,196 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • Achilles tendon

  • bone marrow cells

  • epithelium of colon

  • corpus callosum

  • sural nerve

  • testicle

  • gonad

  • blood

  • tonsil

  • cervix
Top expressed in
  • uterus

  • genital tubercle

  • spermatocyte

  • embryo

  • embryo

  • tail of embryo

  • mesencephalon

  • yolk sac

  • bone marrow

  • muscle of thigh
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • protein heterodimerization activity
  • DNA binding
  • molecular function
Cellular component
  • nucleosome
  • nucleus
  • chromosome
  • extracellular exosome
Biological process
  • chromatin organization
  • biological process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

8338

319176

Ensembl

ENSG00000184260

ENSMUSG00000068855

UniProt

Q16777

Q64523

RefSeq (mRNA)

NM_003517

NM_175662

RefSeq (protein)

NP_003508

NP_783593

Location (UCSC)Chr 1: 149.89 – 149.89 MbChr 3: 96.13 – 96.13 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Histone H2A type 2-C is a protein that in humans is encoded by the HIST2H2AC gene.[5][6][7][8]

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.[8]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000184260 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000068855 – 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. ^ Collart D, Romain PL, Huebner K, Pockwinse S, Pilapil S, Cannizzaro LA, Lian JB, Croce CM, Stein JL, Stein GS (Jan 1993). "A human histone H2B.1 variant gene, located on chromosome 1, utilizes alternative 3' end processing". J Cell Biochem. 50 (4): 374–85. doi:10.1002/jcb.240500406. PMID 1469070. S2CID 7732783.
  6. ^ 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. S2CID 38539096.
  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. ^ a b "Entrez Gene: HIST2H2AC histone cluster 2, H2ac".

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.
  • Kimura A, Horikoshi M (1999). "Tip60 acetylates six lysines of a specific class in core histones in vitro". Genes Cells. 3 (12): 789–800. doi:10.1046/j.1365-2443.1998.00229.x. PMID 10096020.
  • 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.
  • Lahn BT, Tang ZL, Zhou J, et al. (2002). "Previously uncharacterized histone acetyltransferases implicated in mammalian spermatogenesis". Proc. Natl. Acad. Sci. U.S.A. 99 (13): 8707–12. Bibcode:2002PNAS...99.8707L. doi:10.1073/pnas.082248899. PMC 124363. PMID 12072557.
  • 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.
  • Yoon HG, Chan DW, Huang ZQ, et al. (2003). "Purification and functional characterization of the human N-CoR complex: the roles of HDAC3, TBL1 and TBLR1". EMBO J. 22 (6): 1336–46. doi:10.1093/emboj/cdg120. PMC 151047. PMID 12628926.
  • Fujita K, Shimazaki N, Ohta Y, et al. (2004). "Terminal deoxynucleotidyltransferase forms a ternary complex with a novel chromatin remodeling protein with 82 kDa and core histone". Genes Cells. 8 (6): 559–71. doi:10.1046/j.1365-2443.2003.00656.x. PMID 12786946. S2CID 25223336.
  • 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.
  • Braastad CD, Hovhannisyan H, van Wijnen AJ, et al. (2005). "Functional characterization of a human histone gene cluster duplication". Gene. 342 (1): 35–40. doi:10.1016/j.gene.2004.07.036. PMID 15527963.
  • 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.
  • v
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  • 1aoi: COMPLEX BETWEEN NUCLEOSOME CORE PARTICLE (H3,H4,H2A,H2B) AND 146 BP LONG DNA FRAGMENT
    1aoi: COMPLEX BETWEEN NUCLEOSOME CORE PARTICLE (H3,H4,H2A,H2B) AND 146 BP LONG DNA FRAGMENT
  • 1eqz: X-RAY STRUCTURE OF THE NUCLEOSOME CORE PARTICLE AT 2.5 A RESOLUTION
    1eqz: X-RAY STRUCTURE OF THE NUCLEOSOME CORE PARTICLE AT 2.5 A RESOLUTION
  • 1hq3: CRYSTAL STRUCTURE OF THE HISTONE-CORE-OCTAMER IN KCL/PHOSPHATE
    1hq3: CRYSTAL STRUCTURE OF THE HISTONE-CORE-OCTAMER IN KCL/PHOSPHATE
  • 1kx3: X-Ray Structure of the Nucleosome Core Particle, NCP146, at 2.0 A Resolution
    1kx3: X-Ray Structure of the Nucleosome Core Particle, NCP146, at 2.0 A Resolution
  • 1kx4: X-Ray Structure of the Nucleosome Core Particle, NCP146b, at 2.6 A Resolution
    1kx4: X-Ray Structure of the Nucleosome Core Particle, NCP146b, at 2.6 A Resolution
  • 1kx5: X-Ray Structure of the Nucleosome Core Particle, NCP147, at 1.9 A Resolution
    1kx5: X-Ray Structure of the Nucleosome Core Particle, NCP147, at 1.9 A Resolution
  • 1m18: LIGAND BINDING ALTERS THE STRUCTURE AND DYNAMICS OF NUCLEOSOMAL DNA
    1m18: LIGAND BINDING ALTERS THE STRUCTURE AND DYNAMICS OF NUCLEOSOMAL DNA
  • 1m19: LIGAND BINDING ALTERS THE STRUCTURE AND DYNAMICS OF NUCLEOSOMAL DNA
    1m19: LIGAND BINDING ALTERS THE STRUCTURE AND DYNAMICS OF NUCLEOSOMAL DNA
  • 1m1a: LIGAND BINDING ALTERS THE STRUCTURE AND DYNAMICS OF NUCLEOSOMAL DNA
    1m1a: LIGAND BINDING ALTERS THE STRUCTURE AND DYNAMICS OF NUCLEOSOMAL DNA
  • 1p34: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
    1p34: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
  • 1p3a: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
    1p3a: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
  • 1p3b: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
    1p3b: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
  • 1p3f: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
    1p3f: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
  • 1p3g: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
    1p3g: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
  • 1p3i: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
    1p3i: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
  • 1p3k: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
    1p3k: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
  • 1p3l: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
    1p3l: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
  • 1p3m: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
    1p3m: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
  • 1p3o: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
    1p3o: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
  • 1p3p: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
    1p3p: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
  • 1s32: Molecular Recognition of the Nucleosomal 'Supergroove'
    1s32: Molecular Recognition of the Nucleosomal 'Supergroove'
  • 1tzy: Crystal Structure of the Core-Histone Octamer to 1.90 Angstrom Resolution
    1tzy: Crystal Structure of the Core-Histone Octamer to 1.90 Angstrom Resolution
  • 1zbb: Structure of the 4_601_167 Tetranucleosome
    1zbb: Structure of the 4_601_167 Tetranucleosome
  • 1zla: X-ray Structure of a Kaposi's sarcoma herpesvirus LANA peptide bound to the nucleosomal core
    1zla: X-ray Structure of a Kaposi's sarcoma herpesvirus LANA peptide bound to the nucleosomal core
  • 2aro: Crystal Structure Of The Native Histone Octamer To 2.1 Angstrom Resolution, Crystalised In The Presence Of S-Nitrosoglutathione
    2aro: Crystal Structure Of The Native Histone Octamer To 2.1 Angstrom Resolution, Crystalised In The Presence Of S-Nitrosoglutathione
  • 2cv5: Crystal structure of human nucleosome core particle
    2cv5: Crystal structure of human nucleosome core particle
  • 2f8n: 2.9 Angstrom X-ray structure of hybrid macroH2A nucleosomes
    2f8n: 2.9 Angstrom X-ray structure of hybrid macroH2A nucleosomes
  • 2fj7: Crystal structure of Nucleosome Core Particle Containing a Poly (dA.dT) Sequence Element
    2fj7: Crystal structure of Nucleosome Core Particle Containing a Poly (dA.dT) Sequence Element
  • 2hio: HISTONE OCTAMER (CHICKEN), CHROMOSOMAL PROTEIN
    2hio: HISTONE OCTAMER (CHICKEN), CHROMOSOMAL PROTEIN
  • 2nzd: Nucleosome core particle containing 145 bp of DNA
    2nzd: Nucleosome core particle containing 145 bp of DNA
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