H3F3A

H3 histone, family 3A, also known as H3F3A, is a human gene.

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summary_text = 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 contains introns and its mRNA is polyadenylated, unlike most histone genes. The protein encoded is a replication-independent member of the histone H3 family.cite web | title = Entrez Gene: H3F3A H3 histone, family 3A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3020| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Zhang Y, Reinberg D |title=Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tails. |journal=Genes Dev. |volume=15 |issue= 18 |pages= 2343–60 |year= 2001 |pmid= 11562345 |doi= 10.1101/gad.927301
*cite journal | author=Wells D, Kedes L |title=Structure of a human histone cDNA: evidence that basally expressed histone genes have intervening sequences and encode polyadenylylated mRNAs. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 9 |pages= 2834–8 |year= 1985 |pmid= 2859593 |doi=
*cite journal | author=Wells D, Hoffman D, Kedes L |title=Unusual structure, evolutionary conservation of non-coding sequences and numerous pseudogenes characterize the human H3.3 histone multigene family. |journal=Nucleic Acids Res. |volume=15 |issue= 7 |pages= 2871–89 |year= 1987 |pmid= 3031613 |doi=
*cite journal | author=Ohe Y, Iwai K |title=Human spleen histone H3. Isolation and amino acid sequence. |journal=J. Biochem. |volume=90 |issue= 4 |pages= 1205–11 |year= 1982 |pmid= 7309716 |doi=
*cite journal | author=Kato S, Sekine S, Oh SW, "et al." |title=Construction of a human full-length cDNA bank. |journal=Gene |volume=150 |issue= 2 |pages= 243–50 |year= 1995 |pmid= 7821789 |doi=
*cite journal | author=Albig W, Bramlage B, Gruber K, "et al." |title=The human replacement histone H3.3B gene (H3F3B). |journal=Genomics |volume=30 |issue= 2 |pages= 264–72 |year= 1996 |pmid= 8586426 |doi= 10.1006/geno.1995.9878
*cite journal | author=Palaparti A, Baratz A, Stifani S |title=The Groucho/transducin-like enhancer of split transcriptional repressors interact with the genetically defined amino-terminal silencing domain of histone H3. |journal=J. Biol. Chem. |volume=272 |issue= 42 |pages= 26604–10 |year= 1997 |pmid= 9334241 |doi=
*cite journal | author=Lin X, Wells DE |title=Localization of the human H3F3A histone gene to 1q41, outside of the normal histone gene clusters. |journal=Genomics |volume=46 |issue= 3 |pages= 526–8 |year= 1998 |pmid= 9441765 |doi= 10.1006/geno.1997.5037
*cite journal | author=El Kharroubi A, Piras G, Zensen R, Martin MA |title=Transcriptional activation of the integrated chromatin-associated human immunodeficiency virus type 1 promoter. |journal=Mol. Cell. Biol. |volume=18 |issue= 5 |pages= 2535–44 |year= 1998 |pmid= 9566873 |doi=
*cite journal | author=Goto H, Tomono Y, Ajiro K, "et al." |title=Identification of a novel phosphorylation site on histone H3 coupled with mitotic chromosome condensation. |journal=J. Biol. Chem. |volume=274 |issue= 36 |pages= 25543–9 |year= 1999 |pmid= 10464286 |doi=
*cite journal | author=Lo WS, Trievel RC, Rojas JR, "et al." |title=Phosphorylation of serine 10 in histone H3 is functionally linked in vitro and in vivo to Gcn5-mediated acetylation at lysine 14. |journal=Mol. Cell |volume=5 |issue= 6 |pages= 917–26 |year= 2000 |pmid= 10911986 |doi=
*cite journal | author=Deng L, de la Fuente C, Fu P, "et al." |title=Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. |journal=Virology |volume=277 |issue= 2 |pages= 278–95 |year= 2001 |pmid= 11080476 |doi= 10.1006/viro.2000.0593
*cite journal | author=Lachner M, O'Carroll D, Rea S, "et al." |title=Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. |journal=Nature |volume=410 |issue= 6824 |pages= 116–20 |year= 2001 |pmid= 11242053 |doi= 10.1038/35065132
*cite journal | author=Zhong S, Zhang Y, Jansen C, "et al." |title=MAP kinases mediate UVB-induced phosphorylation of histone H3 at serine 28. |journal=J. Biol. Chem. |volume=276 |issue= 16 |pages= 12932–7 |year= 2001 |pmid= 11278789 |doi= 10.1074/jbc.M010931200
*cite journal | author=Suzuki H, Fukunishi Y, Kagawa I, "et al." |title=Protein-protein interaction panel using mouse full-length cDNAs. |journal=Genome Res. |volume=11 |issue= 10 |pages= 1758–65 |year= 2001 |pmid= 11591653 |doi= 10.1101/gr.180101
*cite journal | author=Deng L, Wang D, de la Fuente C, "et al." |title=Enhancement of the p300 HAT activity by HIV-1 Tat on chromatin DNA. |journal=Virology |volume=289 |issue= 2 |pages= 312–26 |year= 2001 |pmid= 11689053 |doi= 10.1006/viro.2001.1129
*cite journal | author=Bauer UM, Daujat S, Nielsen SJ, "et al." |title=Methylation at arginine 17 of histone H3 is linked to gene activation. |journal=EMBO Rep. |volume=3 |issue= 1 |pages= 39–44 |year= 2002 |pmid= 11751582 |doi= 10.1093/embo-reports/kvf013
*cite journal | author=Zegerman P, Canas B, Pappin D, Kouzarides T |title=Histone H3 lysine 4 methylation disrupts binding of nucleosome remodeling and deacetylase (NuRD) repressor complex. |journal=J. Biol. Chem. |volume=277 |issue= 14 |pages= 11621–4 |year= 2002 |pmid= 11850414 |doi= 10.1074/jbc.C200045200
*cite journal | author=Goto H, Yasui Y, Nigg EA, Inagaki M |title=Aurora-B phosphorylates Histone H3 at serine28 with regard to the mitotic chromosome condensation. |journal=Genes Cells |volume=7 |issue= 1 |pages= 11–7 |year= 2002 |pmid= 11856369 |doi=

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