HIST2H2BE

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Histone cluster 2, H2be
File:PBB Protein HIST2H2BE image.jpg
PDB rendering based on 1aoi.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols HIST2H2BE ; H2B.1; GL105; H2B; H2B/q; H2BFQ; MGC129733; MGC129734
External IDs Template:OMIM5 Template:MGI HomoloGene88682
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Histone cluster 2, H2be, also known as HIST2H2BE, is a human gene.[1]

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. This gene encodes a member of the histone H2B family, and generates two transcripts through the use of the conserved stem-loop termination motif, and the polyA addition motif.[1]

References

  1. 1.0 1.1 "Entrez Gene: HIST2H2BE histone cluster 2, H2be".

Further reading

  • Collart D, Romain PL, Huebner K; et al. (1993). "A human histone H2B.1 variant gene, located on chromosome 1, utilizes alternative 3' end processing". J. Cell. Biochem. 50 (4): 374–85. doi:10.1002/jcb.240500406. PMID 1469070.
  • Collart D, Ramsey-Ewing A, Bortell R; et al. (1991). "Isolation and characterization of a cDNA from a human histone H2B gene which is reciprocally expressed in relation to replication-dependent H2B histone genes during HL60 cell differentiation". Biochemistry. 30 (6): 1610–7. PMID 1993178.
  • Jackson S, Brooks W, Jackson V (1994). "Dynamics of the interactions of histones H2A,H2B and H3,H4 with torsionally stressed DNA". Biochemistry. 33 (18): 5392–403. PMID 8180162.
  • Frohm M, Gunne H, Bergman AC; et al. (1996). "Biochemical and antibacterial analysis of human wound and blister fluid". Eur. J. Biochem. 237 (1): 86–92. PMID 8620898.
  • 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.
  • 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.
  • Khan IU, Wallin R, Gupta RS, Kammer GM (1998). "Protein kinase A-catalyzed phosphorylation of heat shock protein 60 chaperone regulates its attachment to histone 2B in the T lymphocyte plasma membrane". Proc. Natl. Acad. Sci. U.S.A. 95 (18): 10425–30. PMID 9724719.
  • 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.
  • Allen MP, Zeng C, Schneider K; et al. (1999). "Growth arrest-specific gene 6 (Gas6)/adhesion related kinase (Ark) signaling promotes gonadotropin-releasing hormone neuronal survival via extracellular signal-regulated kinase (ERK) and Akt". Mol. Endocrinol. 13 (2): 191–201. PMID 9973250.
  • Piredda L, Farrace MG, Lo Bello M; et al. (1999). "Identification of 'tissue' transglutaminase binding proteins in neural cells committed to apoptosis". FASEB J. 13 (2): 355–64. PMID 9973324.
  • 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.
  • Kawasaki H, Schiltz L, Chiu R; et al. (2000). "ATF-2 has intrinsic histone acetyltransferase activity which is modulated by phosphorylation". Nature. 405 (6783): 195–200. doi:10.1038/35012097. PMID 10821277.
  • 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.
  • Baake M, Doenecke D, Albig W (2001). "Characterisation of nuclear localisation signals of the four human core histones". J. Cell. Biochem. 81 (2): 333–46. PMID 11241673.
  • Chadwick BP, Willard HF (2001). "A novel chromatin protein, distantly related to histone H2A, is largely excluded from the inactive X chromosome". J. Cell Biol. 152 (2): 375–84. PMID 11266453.
  • Freire J, Covelo G, Sarandeses C; et al. (2001). "Identification of nuclear-import and cell-cycle regulatory proteins that bind to prothymosin alpha". Biochem. Cell Biol. 79 (2): 123–31. PMID 11310559.
  • Nemergut ME, Mizzen CA, Stukenberg T; et al. (2001). "Chromatin docking and exchange activity enhancement of RCC1 by histones H2A and H2B". Science. 292 (5521): 1540–3. doi:10.1126/science.292.5521.1540. PMID 11375490.
  • 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.

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