HIST3H3

From Wikipedia, the free encyclopedia

Histone cluster 3, H3

PDB rendering based on 1aoi.

Available structures: 1aoi, 1eqz, 1f66, 1hio, 1hq3, 1kx3, 1kx4, 1kx5, 1m18, 1m19, 1m1a, 1p34, 1p3a, 1p3b, 1p3f, 1p3g, 1p3i, 1p3k, 1p3l, 1p3m, 1p3o, 1p3p, 1s32, 1tzy, 1u35, 1zbb, 1zla, 2aro, 2cv5, 2f8n, 2fj7, 2hio, 2hue, 2io5, 2nzd

Identifiers

Symbol(s)

HIST3H3; H3.4; H3/g; H3FT; H3t; MGC126886; MGC126888

External IDs

OMIM: 602820 HomoloGene: 86894

Gene ontology
Molecular Function:	• DNA binding
Cellular Component:	• nucleosome • nucleus • chromosome
Biological Process:	• nucleosome assembly • chromosome organization and biogenesis (sensu Eukaryota)

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_003493 (mRNA)
NP_003484 (protein)

XM_356549 (mRNA)
XP_356549 (protein)

Location

Chr 1: 226.68 - 226.68 Mb

n/a

Pubmed search

[1]

[2]

Histone cluster 3, H3, also known as HIST3H3, is a human gene.

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 H3 family. Transcripts from this gene lack polyA tails; instead, they contain a palindromic termination element. This gene is located separately from the other H3 genes that are in the histone gene cluster on chromosome 6p22-p21.3.^[1]

[edit] References

^ Entrez Gene: HIST3H3 histone cluster 3, H3.

[edit] Further reading

Govin J, Caron C, Rousseaux S, Khochbin S (2005). "Testis-specific histone H3 expression in somatic cells.". Trends Biochem. Sci. 30 (7): 357–9. doi:10.1016/j.tibs.2005.05.001. PMID 15922600.
Bernués J, Espel E, Querol E (1986). "Identification of the core-histone-binding domains of HMG1 and HMG2.". Biochim. Biophys. Acta 866 (4): 242–51. PMID 3697355.
Ishimi Y, Ichinose S, Omori A, et al. (1996). "Binding of human minichromosome maintenance proteins with histone H3.". J. Biol. Chem. 271 (39): 24115–22. PMID 8798650.
Albig W, Ebentheuer J, Klobeck G, et al. (1996). "A solitary human H3 histone gene on chromosome 1.". Hum. Genet. 97 (4): 486–91. PMID 8834248.
Mizzen CA, Yang XJ, Kokubo T, et al. (1997). "The TAF(II)250 subunit of TFIID has histone acetyltransferase activity.". Cell 87 (7): 1261–70. PMID 8980232.
Witt O, Albig W, Doenecke D (1997). "Testis-specific expression of a novel human H3 histone gene.". Exp. Cell Res. 229 (2): 301–6. doi:10.1006/excr.1996.0375. PMID 8986613.
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. 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. PMID 9566873.
Zhang Y, Sun ZW, Iratni R, et al. (1998). "SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex.". Mol. Cell 1 (7): 1021–31. PMID 9651585.
Lorain S, Quivy JP, Monier-Gavelle F, et al. (1998). "Core histones and HIRIP3, a novel histone-binding protein, directly interact with WD repeat protein HIRA.". Mol. Cell. Biol. 18 (9): 5546–56. PMID 9710638.
Becker W, Weber Y, Wetzel K, et al. (1998). "Sequence characteristics, subcellular localization, and substrate specificity of DYRK-related kinases, a novel family of dual specificity protein kinases.". J. Biol. Chem. 273 (40): 25893–902. PMID 9748265.
Carrier F, Georgel PT, Pourquier P, et al. (1999). "Gadd45, a p53-responsive stress protein, modifies DNA accessibility on damaged chromatin.". Mol. Cell. Biol. 19 (3): 1673–85. PMID 10022855.
Sassone-Corsi P, Mizzen CA, Cheung P, et al. (1999). "Requirement of Rsk-2 for epidermal growth factor-activated phosphorylation of histone H3.". Science 285 (5429): 886–91. PMID 10436156.
Thomson S, Clayton AL, Hazzalin CA, et al. (1999). "The nucleosomal response associated with immediate-early gene induction is mediated via alternative MAP kinase cascades: MSK1 as a potential histone H3/HMG-14 kinase.". EMBO J. 18 (17): 4779–93. doi:10.1093/emboj/18.17.4779. PMID 10469656.
Hsieh YJ, Kundu TK, Wang Z, et al. (1999). "The TFIIIC90 subunit of TFIIIC interacts with multiple components of the RNA polymerase III machinery and contains a histone-specific acetyltransferase activity.". Mol. Cell. Biol. 19 (11): 7697–704. PMID 10523658.
Cheung P, Tanner KG, Cheung WL, et al. (2000). "Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation.". Mol. Cell 5 (6): 905–15. PMID 10911985.
Buggy JJ, Sideris ML, Mak P, et al. (2001). "Cloning and characterization of a novel human histone deacetylase, HDAC8.". Biochem. J. 350 Pt 1: 199–205. PMID 10926844.
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. PMID 11163245.