H2AC21 References

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H2AC21

Identifiers

H2AC21, H2AB, histone cluster 2, H2ab, histone cluster 2 H2A family member b, H2A clustered histone 21, HIST2H2AB

External IDs

OMIM: 615014 MGI: 2448314 HomoloGene: 111318 GeneCards: H2AC21

Gene location ( Human)

Chr.	Chromosome 1 (human)^[1]

Band	1q21.2	Start	149,887,469 bp^[1]
Band	1q21.2	End	149,887,965 bp^[1]

Gene location ( Mouse)

Chr.	Chromosome 3 (mouse)^[2]

Band	3\|3 F2.1	Start	96,127,181 bp^[2]
Band	3\|3 F2.1	End	96,127,624 bp^[2]

RNA expression pattern

Human

Mouse (ortholog)

Top expressed in

Achilles tendon

bone marrow cells

corpus callosum

sural nerve

thymus

blood

urinary bladder

skeletal muscle tissue

cervix

monocyte

Top expressed in

spermatocyte

morula

uterus

urinary bladder

spermatid

adrenal gland

mesencephalon

testicle

yolk sac

neural tube

More reference expression data


More reference expression data

Gene ontology
Molecular function	DNA binding protein heterodimerization activity molecular function
Cellular component	nucleosome extracellular exosome nucleus chromosome
Biological process	chromatin organization biological process
Sources: Amigo / QuickGO

Species

Human

Mouse


317772


621893


ENSG00000184270


ENSMUSG00000063689


Q8IUE6


Q64522

RefSeq (mRNA)


NM_175065


NM_178213

RefSeq (protein)


NP_778235


NP_835585

Location (UCSC)

Chr 1: 149.89 – 149.89 Mb

Chr 3: 96.13 – 96.13 Mb

PubMed search

^[3]

^[4]

View/Edit Human

View/Edit Mouse

Histone H2A type 2-B is a protein that in humans is encoded by the HIST2H2AB gene.^[5]^[6]

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 contain a palindromic termination element.^[6]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000184270 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000063689 – 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.
^ 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.
^ ^a ^b "Entrez Gene: HIST2H2AB histone cluster 2, H2ab".

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.
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.
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.
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.
Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. Bibcode: 2006Natur.441..315G. doi: 10.1038/nature04727. PMID 16710414.

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
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
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

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