HIST2H3C
Histone H3.2 is a protein that in humans is encoded by the HIST2H3C gene.[1][2][3]
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 H3 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 telomeric copy.[3]
Interactions
HIST2H3C has been shown to interact with NCOA6.[4]
References
- ^ Marzluff WF, Gongidi P, Woods KR, Jin J, Maltais LJ (Oct 2002). "The human and mouse replication-dependent histone genes". Genomics 80 (5): 487–498. doi:10.1016/S0888-7543(02)96850-3. PMID 12408966.
- ^ Marashi F, Helms S, Shiels A, Silverstein S, Greenspan DS, Stein G, Stein J (Jul 1986). "Enhancer-facilitated expression of prokaryotic and eukaryotic genes using human histone gene 5' regulatory sequences". Biochem Cell Biol 64 (4): 277–289. doi:10.1139/o86-039. PMID 3013246.
- ^ a b "Entrez Gene: HIST2H3C histone cluster 2, H3c". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=126961.
- ^ Goo, Young-Hwa; Sohn Young Chang, Kim Dae-Hwan, Kim Seung-Whan, Kang Min-Jung, Jung Dong-Ju, Kwak Eunyee, Barlev Nickolai A, Berger Shelley L, Chow Vincent T, Roeder Robert G, Azorsa David O, Meltzer Paul S, Suh Pan-Gil, Song Eun Joo, Lee Kong-Joo, Lee Young Chul, Lee Jae Woon (Jan. 2003). "Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins". Mol. Cell. Biol. (United States) 23 (1): 140–149. doi:10.1128/MCB.23.1.140-149.2003. ISSN 0270-7306. PMC 140670. PMID 12482968. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=140670.
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): 838–840. doi:10.1126/science.6494913. PMID 6494913.
- Ohe Y, Iwai K (1982). "Human spleen histone H3. Isolation and amino acid sequence". J. Biochem. 90 (4): 1205–11. PMID 7309716.
- 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.
- Albig W, Doenecke D (1998). "The human histone gene cluster at the D6S105 locus". Hum. Genet. 101 (3): 284–294. 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.
- Ahn J, Gruen JR (1999). "The genomic organization of the histone clusters on human 6p21.3". Mamm. Genome 10 (7): 768–770. doi:10.1007/s003359901089. PMID 10384058.
- Goto H, Tomono Y, Ajiro K et al. (1999). "Identification of a novel phosphorylation site on histone H3 coupled with mitotic chromosome condensation". J. Biol. Chem. 274 (36): 25543–25549. doi:10.1074/jbc.274.36.25543. PMID 10464286.
- 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): 278–295. doi:10.1006/viro.2000.0593. PMID 11080476.
- Lachner M, O'Carroll D, Rea S et al. (2001). "Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins". Nature 410 (6824): 116–120. doi:10.1038/35065132. PMID 11242053.
- Shankaranarayanan P, Chaitidis P, Kühn H, Nigam S (2001). "Acetylation by histone acetyltransferase CREB-binding protein/p300 of STAT6 is required for transcriptional activation of the 15-lipoxygenase-1 gene". J. Biol. Chem. 276 (46): 42753–42760. doi:10.1074/jbc.M102626200. PMID 11509556.
- 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): 312–326. doi:10.1006/viro.2001.1129. PMID 11689053.
- Goto H, Yasui Y, Nigg EA, Inagaki M (2002). "Aurora-B phosphorylates Histone H3 at serine28 with regard to the mitotic chromosome condensation". Genes Cells 7 (1): 11–17. doi:10.1046/j.1356-9597.2001.00498.x. PMID 11856369.
- Ganesan S, Silver DP, Greenberg RA et al. (2002). "BRCA1 supports XIST RNA concentration on the inactive X chromosome". Cell 111 (3): 393–405. doi:10.1016/S0092-8674(02)01052-8. PMID 12419249.
- 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): 16899–16903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- Goo YH, Sohn YC, Kim DH et al. (2003). "Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins". Mol. Cell. Biol. 23 (1): 140–149. doi:10.1128/MCB.23.1.140-149.2003. PMC 140670. PMID 12482968. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=140670.
- Preuss U, Landsberg G, Scheidtmann KH (2003). "Novel mitosis-specific phosphorylation of histone H3 at Thr11 mediated by Dlk/ZIP kinase". Nucleic Acids Res. 31 (3): 878–885. doi:10.1093/nar/gkg176. PMC 149197. PMID 12560483. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=149197.
- 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): 1336–1346. doi:10.1093/emboj/cdg120. PMC 151047. PMID 12628926. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=151047.
- 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): 6550–6561. doi:10.1093/emboj/cdg631. PMC 291826. PMID 14657027. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=291826.
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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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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