H2AFJ
H2A histone family, member J |
PDB rendering based on 1aoi. |
Available structures |
PDB |
1aoi, 1eqz, 1hio, 1hq3, 1kx3, 1kx4, 1kx5, 1m18, 1m19, 1m1a, 1p34, 1p3a, 1p3b, 1p3f, 1p3g, 1p3i, 1p3k, 1p3l, 1p3m, 1p3o, 1p3p, 1s32, 1tzy, 1zbb, 1zla, 2aro, 2cv5, 2f8n, 2fj7, 2hio, 2nzd |
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Identifiers |
Symbols |
H2AFJ; FLJ10903; FLJ52230; H2AJ; MGC921 |
External IDs |
MGI: 3606192 HomoloGene: 111025 GeneCards: H2AFJ Gene |
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Orthologs |
Species |
Human |
Mouse |
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Entrez |
55766 |
232440 |
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Ensembl |
ENSG00000246705 |
ENSMUSG00000060032 |
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UniProt |
Q9BTM1 |
Q8R1M2 |
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RefSeq (mRNA) |
NM_177925.2 |
NM_177688.4 |
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RefSeq (protein) |
NP_060737 |
NP_808356.1 |
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Location (UCSC) |
Chr 12:
14.93 – 14.93 Mb |
Chr 6:
136.76 – 136.76 Mb |
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PubMed search |
[1] |
[2] |
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Histone H2A.J is a protein that in humans is encoded by the H2AFJ gene.[1]
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 located on chromosome 12 and encodes a variant H2A histone. The protein is divergent at the C-terminus compared to the consensus H2A histone family member.[1]
References
Further reading
- Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1356129.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=291826.
- 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- 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.
- Chadwick BP, Willard HF (2001). "Histone H2A variants and the inactive X chromosome: identification of a second macroH2A variant.". Hum. Mol. Genet. 10 (10): 1101–13. doi:10.1093/hmg/10.10.1101. PMID 11331621.
- 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.
- 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. PMC 110633. PMID 9566873. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=110633.
PDB gallery
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1aoi: COMPLEX BETWEEN NUCLEOSOME CORE PARTICLE (H3,H4,H2A,H2B) AND 146 BP LONG DNA FRAGMENT
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1eqz: X-RAY STRUCTURE OF THE NUCLEOSOME CORE PARTICLE AT 2.5 A RESOLUTION
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1hq3: CRYSTAL STRUCTURE OF THE HISTONE-CORE-OCTAMER IN KCL/PHOSPHATE
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1kx3: X-Ray Structure of the Nucleosome Core Particle, NCP146, at 2.0 A Resolution
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1kx4: X-Ray Structure of the Nucleosome Core Particle, NCP146b, at 2.6 A Resolution
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1kx5: X-Ray Structure of the Nucleosome Core Particle, NCP147, at 1.9 A Resolution
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1m18: LIGAND BINDING ALTERS THE STRUCTURE AND DYNAMICS OF NUCLEOSOMAL DNA
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1m19: LIGAND BINDING ALTERS THE STRUCTURE AND DYNAMICS OF NUCLEOSOMAL DNA
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1m1a: LIGAND BINDING ALTERS THE STRUCTURE AND DYNAMICS OF NUCLEOSOMAL DNA
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1p34: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
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1p3a: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
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1p3b: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
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1p3f: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
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1p3g: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
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1p3i: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
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1p3k: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
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1p3l: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
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1p3m: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
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1p3o: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
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1p3p: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
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1s32: Molecular Recognition of the Nucleosomal 'Supergroove'
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1tzy: Crystal Structure of the Core-Histone Octamer to 1.90 Angstrom Resolution
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1zbb: Structure of the 4_601_167 Tetranucleosome
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1zla: X-ray Structure of a Kaposi's sarcoma herpesvirus LANA peptide bound to the nucleosomal core
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2aro: Crystal Structure Of The Native Histone Octamer To 2.1 Angstrom Resolution, Crystalised In The Presence Of S-Nitrosoglutathione
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2cv5: Crystal structure of human nucleosome core particle
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2f8n: 2.9 Angstrom X-ray structure of hybrid macroH2A nucleosomes
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2fj7: Crystal structure of Nucleosome Core Particle Containing a Poly (dA.dT) Sequence Element
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2hio: HISTONE OCTAMER (CHICKEN), CHROMOSOMAL PROTEIN
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2nzd: Nucleosome core particle containing 145 bp of DNA
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