HIST1H3F

Histone cluster 1, H3f

PDB rendering based on 1aoi.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes

1CS9, 1CT6, 1O9S, 1Q3L, 2B2T, 2B2U, 2B2V, 2B2W, 2C1J, 2C1N, 2CV5, 2KWJ, 2KWK, 2L75, 2LBM, 2M0O, 2OQ6, 2OT7, 2OX0, 2RI7, 2UXN, 2VPG, 3A1B, 3AFA, 3AVR, 3AYW, 3AZE, 3AZF, 3AZG, 3AZH, 3AZI, 3AZJ, 3AZK, 3AZL, 3AZM, 3AZN, 3B95, 3KMT, 3KQI, 3LQI, 3LQJ, 3O34, 3O35, 3O37, 3QJ6, 3RIG, 3RIY, 3SOU, 3SOW, 3U31, 3U3D, 3U4S, 3U5N, 3U5O, 3U5P, 3UEE, 3UEF, 3UIG, 3UII, 3UIK, 3V43, 3W96, 3W97, 3W98, 3W99, 3WA9, 3WAA, 3WKJ, 3ZG6, 3ZVY, 4A0J, 4A0N, 4A7J, 4BD3, 4C1Q, 4F4U, 4F56, 4FWF, 4HON, 4I51, 4L7X, 4LK9, 4LKA, 4LLB, 4LXL, 4N4H, 4UP0, 4UY4, 4Z0R

Identifiers

Symbols

HIST1H3F ; H3/i; H3FI

External IDs

OMIM: 602816 HomoloGene: 134472 GeneCards: HIST1H3F Gene

Gene ontology
Molecular function	• DNA binding • protein binding • histone binding • protein heterodimerization activity
Cellular component	• nuclear chromosome • nucleosome • nuclear nucleosome • extracellular region • nucleus • nucleoplasm • membrane • protein complex • extracellular exosome
Biological process	• chromatin silencing at rDNA • positive regulation of defense response to virus by host • chromatin organization • nucleosome assembly • DNA replication-dependent nucleosome assembly • small GTPase mediated signal transduction • blood coagulation • gene expression • DNA methylation on cytosine • regulation of gene expression, epigenetic • negative regulation of gene expression, epigenetic • protein heterotetramerization • regulation of gene silencing
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 6:
26.25 – 26.25 Mb

Chr 13:
21.78 – 21.78 Mb

PubMed search

Histone H3.1 is a protein that in humans is encoded by the HIST1H3F 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 the large histone gene cluster on chromosome 6p22-p21.3.^[3]

References

↑ Albig W, Kioschis P, Poustka A, Meergans K, Doenecke D (Apr 1997). "Human histone gene organization: nonregular arrangement within a large cluster". Genomics 40 (2): 314–22. doi:10.1006/geno.1996.4592. PMID 9119399.
↑ Marzluff WF, Gongidi P, Woods KR, Jin J, Maltais LJ (Oct 2002). "The human and mouse replication-dependent histone genes". Genomics 80 (5): 487–98. doi:10.1016/S0888-7543(02)96850-3. PMID 12408966.
1 2 "Entrez Gene: HIST1H3F histone cluster 1, H3f".

Albig W, Kardalinou E, Drabent B, et al. (1991). "Isolation and characterization of two human H1 histone genes within clusters of core histone genes.". Genomics 10 (4): 940–8. doi:10.1016/0888-7543(91)90183-F. PMID 1916825.
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.
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.
Rea S, Eisenhaber F, O'Carroll D, et al. (2000). "Regulation of chromatin structure by site-specific histone H3 methyltransferases.". Nature 406 (6796): 593–9. doi:10.1038/35020506. PMID 10949293.
Hsu JY, Sun ZW, Li X, et al. (2000). "Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes.". Cell 102 (3): 279–91. doi:10.1016/S0092-8674(00)00034-9. PMID 10975519.
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.
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): 116–20. doi:10.1038/35065132. PMID 11242053.
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.
Yang L, Xia L, Wu DY, et al. (2002). "Molecular cloning of ESET, a novel histone H3-specific methyltransferase that interacts with ERG transcription factor.". Oncogene 21 (1): 148–52. doi:10.1038/sj.onc.1204998. PMID 11791185.
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): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Xiao B, Jing C, Wilson JR, et al. (2003). "Structure and catalytic mechanism of the human histone methyltransferase SET7/9.". Nature 421 (6923): 652–6. doi:10.1038/nature01378. PMID 12540855.
Koessler H, Doenecke D, Albig W (2003). "Aberrant expression pattern of replication-dependent histone h3 subtype genes in human tumor cell lines.". DNA Cell Biol. 22 (4): 233–41. doi:10.1089/104454903321908629. PMID 12823900.
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): 6550–61. doi:10.1093/emboj/cdg631. PMC 291826. PMID 14657027.
Couture JF, Collazo E, Hauk G, Trievel RC (2006). "Structural basis for the methylation site specificity of SET7/9.". Nat. Struct. Mol. Biol. 13 (2): 140–6. doi:10.1038/nsmb1045. PMID 16415881.
Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

PDB gallery

1aoi: COMPLEX BETWEEN NUCLEOSOME CORE PARTICLE (H3,H4,H2A,H2B) AND 146 BP LONG DNA FRAGMENT

1eqz: X-RAY STRUCTURE OF THE NUCLEOSOME CORE PARTICLE AT 2.5 A RESOLUTION

1f66: 2.6 A CRYSTAL STRUCTURE OF A NUCLEOSOME CORE PARTICLE CONTAINING THE VARIANT HISTONE H2A.Z

1hq3: CRYSTAL STRUCTURE OF THE HISTONE-CORE-OCTAMER IN KCL/PHOSPHATE

1kx3: X-Ray Structure of the Nucleosome Core Particle, NCP146, at 2.0 A Resolution

1kx4: X-Ray Structure of the Nucleosome Core Particle, NCP146b, at 2.6 A Resolution

1kx5: X-Ray Structure of the Nucleosome Core Particle, NCP147, at 1.9 A Resolution

1m18: LIGAND BINDING ALTERS THE STRUCTURE AND DYNAMICS OF NUCLEOSOMAL DNA

1m19: LIGAND BINDING ALTERS THE STRUCTURE AND DYNAMICS OF NUCLEOSOMAL DNA

1m1a: LIGAND BINDING ALTERS THE STRUCTURE AND DYNAMICS OF NUCLEOSOMAL DNA

1p34: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants

1p3a: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants

1p3b: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants

1p3f: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants

1p3g: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants

1p3i: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants

1p3k: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants

1p3l: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants

1p3m: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants

1p3o: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants

1p3p: Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants

1s32: Molecular Recognition of the Nucleosomal 'Supergroove'

1tzy: Crystal Structure of the Core-Histone Octamer to 1.90 Angstrom Resolution

1u35: Crystal structure of the nucleosome core particle containing the histone domain of macroH2A

1zbb: Structure of the 4_601_167 Tetranucleosome

1zla: X-ray Structure of a Kaposi's sarcoma herpesvirus LANA peptide bound to the nucleosomal core

2aro: Crystal Structure Of The Native Histone Octamer To 2.1 Angstrom Resolution, Crystalised In The Presence Of S-Nitrosoglutathione

2cv5: Crystal structure of human nucleosome core particle

2f8n: 2.9 Angstrom X-ray structure of hybrid macroH2A nucleosomes

2fj7: Crystal structure of Nucleosome Core Particle Containing a Poly (dA.dT) Sequence Element

2hio: HISTONE OCTAMER (CHICKEN), CHROMOSOMAL PROTEIN

2hue: Structure of the H3-H4 chaperone Asf1 bound to histones H3 and H4

2io5: Crystal structure of the CIA- histone H3-H4 complex

2nzd: Nucleosome core particle containing 145 bp of DNA

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HIST1H3F

References

Further reading