HIST2H4A
From Wikipedia, the free encyclopedia
| Histone cluster 2, H4a |

PDB rendering based on 1aoi. |
| Available structures |
| PDB |
2BQZ, 2CV5, 2RNY, 3A6N, 3AFA, 3CFS, 3CFV, 3F9W, 3F9X, 3F9Y, 3F9Z, 3NQJ, 3NQU |
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| Identifiers |
| Symbols |
HIST2H4A; FO108; H4; H4/n; H4F2; H4FN; HIST1H4A; HIST1H4B; HIST1H4C; HIST1H4D; HIST1H4E; HIST1H4F; HIST1H4H; HIST1H4I; HIST1H4J; HIST1H4K; HIST1H4L; HIST2H4; HIST2H4B; HIST4H4 |
| External IDs |
OMIM: 142750 MGI: 2448443 HomoloGene: 111038 GeneCards: HIST2H4A Gene |
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| Orthologs |
| Species |
Human |
Mouse |
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| Entrez |
8370 |
320332 |
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| Ensembl |
n/a |
n/a |
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| UniProt |
P62805 |
n/a |
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| RefSeq (mRNA) |
XM_001124639 |
NM_175652 |
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| RefSeq (protein) |
XP_001124639 |
NP_783583 |
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| Location (UCSC) |
n/a |
n/a |
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| PubMed search |
[1] |
[2] |
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Histone H4 is a protein that in humans is encoded by the HIST2H4A gene.[1][2][3][4]
Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. This structure consists of approximately 146 bp of DNA wrapped around a nucleosome, an 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 H4 family. Transcripts from this gene lack polyA tails; instead, they 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.[4]
[edit] References
- ^ Pauli U, Chrysogelos S, Stein G, Stein J, Nick H (Jul 1987). "Protein-DNA interactions in vivo upstream of a cell cycle-regulated human H4 histone gene". Science 236 (4806): 1308–11. doi:10.1126/science.3035717. PMID 3035717.
- ^ Sierra F, Stein G, Stein J (Dec 1983). "Structure and in vitro transcription of a human H4 histone gene". Nucleic Acids Res 11 (20): 7069–86. doi:10.1093/nar/11.20.7069. PMC 326439. PMID 6314274. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=326439.
- ^ Braastad CD, Hovhannisyan H, van Wijnen AJ, Stein JL, Stein GS (Nov 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: HIST2H4A histone cluster 2, H4a". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8370.
[edit] Further reading
- Green L, Van Antwerpen R, Stein J, et al. (1984). "A major human histone gene cluster on the long arm of chromosome 1". Science 226 (4676): 838–40. doi:10.1126/science.6494913. PMID 6494913.
- Pelicci G, Lanfrancone L, Salcini AE, et al. (1995). "Constitutive phosphorylation of Shc proteins in human tumors". Oncogene 11 (5): 899–907. PMID 7675449.
- Díaz-Jullien C, Pérez-Estévez A, Covelo G, Freire M (1996). "Prothymosin alpha binds histones in vitro and shows activity in nucleosome assembly assay". Biochim. Biophys. Acta 1296 (2): 219–27. doi:10.1016/0167-4838(96)00072-6. PMID 8814229.
- Rodriguez P, Munroe D, Prawitt D, et al. (1997). "Functional characterization of human nucleosome assembly protein-2 (NAP1L4) suggests a role as a histone chaperone". Genomics 44 (3): 253–65. doi:10.1006/geno.1997.4868. PMID 9325046.
- 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.
- 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.
- 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.
- Seo SB, McNamara P, Heo S, et al. (2001). "Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the set oncoprotein". Cell 104 (1): 119–30. doi:10.1016/S0092-8674(01)00196-9. PMID 11163245.
- 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.
- Andersen JS, Lyon CE, Fox AH, et al. (2002). "Directed proteomic analysis of the human nucleolus". Curr. Biol. 12 (1): 1–11. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298.
- Weinmann AS, Yan PS, Oberley MJ, et al. (2002). "Isolating human transcription factor targets by coupling chromatin immunoprecipitation and CpG island microarray analysis". Genes Dev. 16 (2): 235–44. doi:10.1101/gad.943102. PMC 155318. PMID 11799066. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=155318.
- Marzluff WF, Gongidi P, Woods KR, et al. (2003). "The human and mouse replication-dependent histone genes". Genomics 80 (5): 487–98. doi:10.1016/S0888-7543(02)96850-3. PMID 12408966.
- 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.
- Hovhannisyan H, Cho B, Mitra P, et al. (2003). "Maintenance of open chromatin and selective genomic occupancy at the cell cycle-regulated histone H4 promoter during differentiation of HL-60 promyelocytic leukemia cells". Mol. Cell. Biol. 23 (4): 1460–9. doi:10.1128/MCB.23.4.1460-1469.2003. PMC 141140. PMID 12556504. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=141140.
- 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=151047.
- Pivot-Pajot C, Caron C, Govin J, et al. (2003). "Acetylation-dependent chromatin reorganization by BRDT, a testis-specific bromodomain-containing protein". Mol. Cell. Biol. 23 (15): 5354–65. doi:10.1128/MCB.23.15.5354-5365.2003. PMC 165724. PMID 12861021. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=165724.
- Coleman MA, Miller KA, Beernink PT, et al. (2004). "Identification of chromatin-related protein interactions using protein microarrays". Proteomics 3 (11): 2101–7. doi:10.1002/pmic.200300593. PMID 14595808.
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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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1f66: 2.6 A CRYSTAL STRUCTURE OF A NUCLEOSOME CORE PARTICLE CONTAINING THE VARIANT HISTONE H2A.Z
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1hq3: CRYSTAL STRUCTURE OF THE HISTONE-CORE-OCTAMER IN KCL/PHOSPHATE
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1id3: CRYSTAL STRUCTURE OF THE YEAST NUCLEOSOME CORE PARTICLE REVEALS FUNDAMENTAL DIFFERENCES IN INTER-NUCLEOSOME INTERACTIONS
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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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1u35: Crystal structure of the nucleosome core particle containing the histone domain of macroH2A
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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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2hue: Structure of the H3-H4 chaperone Asf1 bound to histones H3 and H4
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2io5: Crystal structure of the CIA- histone H3-H4 complex
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2nzd: Nucleosome core particle containing 145 bp of DNA
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