HIST1H2AE
HIST1H2AE
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Available structures |
PDB | Ortholog search: PDBe RCSB |
List of PDB id codes |
2CV5, 3A6N, 3AFA, 3AN2, 3AV1, 3AV2, 3AYW, 3AZE, 3AZF, 3AZG, 3AZH, 3AZI, 3AZJ, 3AZK, 3AZL, 3AZM, 3AZN, 3W96, 3W97, 3W98, 3W99, 3WKJ, 3WTP, 5CPJ, 5B0Z, 4YM5, 5AV9, 5AVB, 5AV5, 4YM6, 5CPI, 3X1V, 5AV6, 3X1S, 5AV8, 5CPK, 5AVC, 5B0Y, 4Z5T, 5B24, 2RVQ, 5B40, 5AY8, 5B2I, 5B2J
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Identifiers |
Aliases |
HIST1H2AE, H2A.1, H2A.2, H2A/a, H2AFA, histone cluster 1, H2ae |
External IDs |
MGI: 2448457 HomoloGene: 135791 GeneCards: HIST1H2AE
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Orthologs |
Species |
Human |
Mouse |
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Entrez |
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Ensembl |
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UniProt |
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RefSeq (mRNA) |
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RefSeq (protein) |
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Location (UCSC) |
Chr 6: 26.22 – 26.22 Mb |
Chr 13: 21.72 – 21.72 Mb |
PubMed search |
[1] |
[2]
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Wikidata |
Histone H2A type 1-B/E is a protein that in humans is encoded by the HIST1H2AE gene.[3][4][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 lack polyA tails; instead, they contain a palindromic termination element. This gene is found in the large histone gene cluster on chromosome 6p22-p21.3.[6]
References
- ↑ "Human PubMed Reference:".
- ↑ "Mouse PubMed Reference:".
- ↑ Albig W, Kioschis P, Poustka A, Meergans K, Doenecke D (Apr 1997). "Human histone gene organization: nonregular arrangement within a large cluster". Genomics. 40 (2): 314–22. doi:10.1006/geno.1996.4592. PMID 9119399.
- ↑ Albig W, Kardalinou E, Drabent B, Zimmer A, Doenecke D (Nov 1991). "Isolation and characterization of two human H1 histone genes within clusters of core histone genes". Genomics. 10 (4): 940–8. doi:10.1016/0888-7543(91)90183-F. PMID 1916825.
- ↑ 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.
- 1 2 "Entrez Gene: HIST1H2AE histone cluster 1, H2ae".
Further reading
- 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. 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.
- Galasinski SC, Louie DF, Gloor KK, et al. (2002). "Global regulation of post-translational modifications on core histones". J. Biol. Chem. 277 (4): 2579–88. doi:10.1074/jbc.M107894200. PMID 11709551.
- 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.
- Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6". Nature. 425 (6960): 805–11. doi:10.1038/nature02055. PMID 14574404.
- 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. doi:10.1038/nature02985. PMID 15386022.
- 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.
- 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.
- 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.
- Boyne MT, Pesavento JJ, Mizzen CA, Kelleher NL (2006). "Precise characterization of human histones in the H2A gene family by top down mass spectrometry". J. Proteome Res. 5 (2): 248–53. doi:10.1021/pr050269n. PMID 16457589.
PDB gallery |
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| 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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