HIST3H3

H3-4
Available structures PDB Human UniProt search: PDBe RCSB List of PDB id codes 2V1D, 2YBP, 2YBS, 3A6N, 3T6R, 4V2W
Identifiers
Aliases	H3-4, H3.4, H3/g, H3FT, H3t, histone cluster 3, H3, histone cluster 3 H3, HIST3H3, H3.4 histone
External IDs	OMIM: 602820; HomoloGene: 133212; GeneCards: H3-4; OMA:H3-4 - orthologs
Gene location (Human) Chr. Chromosome 1 (human) Band 1q42.13 Start 228,424,845 bp End 228,425,360 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in testicle right testis left testis right coronary artery granulocyte ectocervix canal of the cervix mucosa of transverse colon right uterine tube right ovary n/a More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein heterodimerization activity DNA binding histone binding protein binding nucleosomal DNA binding Cellular component nucleosome extracellular exosome nucleus chromosome nucleoplasm Biological process negative regulation of protein oligomerization nucleosome assembly protein heterotetramerization double-strand break repair via nonhomologous end joining telomere capping Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 8290 n/a Ensembl ENSG00000168148 ENSG00000285435 n/a UniProt Q16695 n/a RefSeq (mRNA) NM_003493 n/a RefSeq (protein) NP_003484 n/a Location (UCSC) Chr 1: 228.42 – 228.43 Mb n/a PubMed search n/a
Wikidata
View/Edit Human

Histone H3.1t is a protein that in humans is encoded by the HIST3H3 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.

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. doi:10.1016/0167-4781(86)90049-7. 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. doi:10.1074/jbc.271.39.24115. PMID 8798650.
• 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. doi:10.1016/S0092-8674(00)81821-8. PMID 8980232. S2CID 18409257.
• 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. doi:10.1007/s004390050630. PMID 9439656. S2CID 38539096.
• 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.
• 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. doi:10.1016/S1097-2765(00)80102-1. 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. doi:10.1128/MCB.18.9.5546. PMC 109139. 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. doi:10.1074/jbc.273.40.25893. 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. doi:10.1128/MCB.19.3.1673. PMC 83961. 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. doi:10.1126/science.285.5429.886. 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. PMC 1171550. 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. doi:10.1128/mcb.19.11.7697. PMC 84812. 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. doi:10.1016/S1097-2765(00)80256-7. PMID 10911985.
• Buggy JJ, Sideris ML, Mak P, et al. (2001). "Cloning and characterization of a novel human histone deacetylase, HDAC8". Biochem. J. 350 (1): 199–205. doi:10.1042/0264-6021:3500199. PMC 1221242. 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. doi:10.1016/S0092-8674(01)00196-9. PMID 11163245. S2CID 11144887.