From Wikipedia, the free encyclopedia
Protein-coding gene in the species Homo sapiens
H2AC18
Identifiers
Aliases
H2AC18 , H2A, H2A.2, H2A/O, H2A/q, H2AFO, H2a-615, HIST2H2AA, histone cluster 2, H2aa3, histone cluster 2 H2A family member a3, HIST2H2AA3, H2A clustered histone 18, H2AC19External IDs
OMIM :
142720
MGI :
2448283
HomoloGene :
116071
GeneCards :
H2AC18
Wikidata
Histone H2A type 2-A is a
protein that in humans is encoded by the HIST2H2AA3
gene .
[5]
[6]
[7]
[8]
Function
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 a histone cluster on
chromosome 1 . This gene is one of four histone genes in the cluster that are duplicated; this record represents the centromeric copy.
[8]
References
^
a b c
GRCh38: Ensembl release 89: ENSG00000288825 –
Ensembl , May 2017
^
a b c
GRCm38: Ensembl release 89: ENSMUSG00000063954 –
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 .
^ Marashi F, Prokopp K, Stein J, Stein G (April 1984).
"Evidence for a human histone gene cluster containing H2B and H2A pseudogenes" . Proceedings of the National Academy of Sciences of the United States of America . 81 (7): 1936–40.
Bibcode :
1984PNAS...81.1936M .
doi :
10.1073/pnas.81.7.1936 .
PMC
345411 .
PMID
6326092 .
^ Mannironi C, Orr A, Hatch C, Pilch D, Ivanova V, Bonner W (February 1994).
"The relative expression of human histone H2A genes is similar in different types of proliferating cells" . DNA and Cell Biology . 13 (2): 161–70.
doi :
10.1089/dna.1994.13.161 .
PMID
8179821 .
^ Braastad CD, Hovhannisyan H, van Wijnen AJ, Stein JL, Stein GS (November 2004). "Functional characterization of a human histone gene cluster duplication". Gene . 342 (1): 35–40.
doi :
10.1016/j.gene.2004.07.036 .
PMID
15527963 . ^
a b
"Entrez Gene: HIST2H2AA3 histone cluster 2, H2aa3" .
Further reading
Allen BS, Stein JL, Stein GS, Ostrer H (June 1991). "Single-copy flanking sequences in human histone gene clusters map to chromosomes 1 and 6". Genomics . 10 (2): 486–8.
doi :
10.1016/0888-7543(91)90337-E .
PMID
2071153 . Kaiser P, Mandl S, Schweiger M, Schneider R (December 1995).
"Characterization of functionally independent domains in the human ubiquitin conjugating enzyme UbcH2" . FEBS Letters . 377 (2): 193–6.
doi :
10.1016/0014-5793(95)01323-7 .
PMID
8543049 . Wang ZF, Tisovec R, Debry RW, Frey MR, Matera AG, Marzluff WF (August 1996).
"Characterization of the 55-kb mouse histone gene cluster on chromosome 3" . Genome Research . 6 (8): 702–14.
doi :
10.1101/gr.6.8.702 .
PMID
8858345 . Albig W, Doenecke D (December 1997). "The human histone gene cluster at the D6S105 locus". Human Genetics . 101 (3): 284–94.
doi :
10.1007/s004390050630 .
PMID
9439656 .
S2CID
38539096 . El Kharroubi A, Piras G, Zensen R, Martin MA (May 1998).
"Transcriptional activation of the integrated chromatin-associated human immunodeficiency virus type 1 promoter" . Molecular and Cellular Biology . 18 (5): 2535–44.
doi :
10.1128/mcb.18.5.2535 .
PMC
110633 .
PMID
9566873 . Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F (November 2000).
"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 . Nemergut ME, Mizzen CA, Stukenberg T, Allis CD, Macara IG (May 2001). "Chromatin docking and exchange activity enhancement of RCC1 by histones H2A and H2B". Science . 292 (5521): 1540–3.
Bibcode :
2001Sci...292.1540N .
doi :
10.1126/science.292.5521.1540 .
PMID
11375490 . Deng L, Wang D, de la Fuente C, Wang L, Li H, Lee CG, Donnelly R, Wade JD, Lambert P, Kashanchi F (October 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 . Marzluff WF, Gongidi P, Woods KR, Jin J, Maltais LJ (November 2002). "The human and mouse replication-dependent histone genes". Genomics . 80 (5): 487–98.
doi :
10.1016/S0888-7543(02)96850-3 .
PMID
12408966 . Lusic M, Marcello A, Cereseto A, Giacca M (December 2003).
"Regulation of HIV-1 gene expression by histone acetylation and factor recruitment at the LTR promoter" . The EMBO Journal . 22 (24): 6550–61.
doi :
10.1093/emboj/cdg631 .
PMC
291826 .
PMID
14657027 . Yusufzai TM, Tagami H, Nakatani Y, Felsenfeld G (January 2004).
"CTCF tethers an insulator to subnuclear sites, suggesting shared insulator mechanisms across species" . Molecular Cell . 13 (2): 291–8.
doi :
10.1016/S1097-2765(04)00029-2 .
PMID
14759373 . Zhang Y, Griffin K, Mondal N, Parvin JD (May 2004).
"Phosphorylation of histone H2A inhibits transcription on chromatin templates" . The Journal of Biological Chemistry . 279 (21): 21866–72.
doi :
10.1074/jbc.M400099200 .
PMID
15010469 . Aihara H, Nakagawa T, Yasui K, Ohta T, Hirose S, Dhomae N, Takio K, Kaneko M, Takeshima Y, Muramatsu M, Ito T (April 2004).
"Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 during mitosis in the early Drosophila embryo" . Genes & Development . 18 (8): 877–88.
doi :
10.1101/gad.1184604 .
PMC
395847 .
PMID
15078818 . Wang H, Wang L, Erdjument-Bromage H, Vidal M, Tempst P, Jones RS, Zhang Y (October 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 .
PDB gallery
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
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
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
1m18 : 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
1p34 : 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
1p3f : 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
1p3k : 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
1p3o : 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'
1tzy : Crystal Structure of the Core-Histone Octamer to 1.90 Angstrom Resolution
1zbb : Structure of the 4_601_167 Tetranucleosome
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
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
2hio : HISTONE OCTAMER (CHICKEN), CHROMOSOMAL PROTEIN
2nzd : Nucleosome core particle containing 145 bp of DNA
