HIST1H3C

Histone cluster 1, H3c

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

HIST1H3C ; H3.1; H3/c; H3FC

External IDs

OMIM: 602812 MGI: 3647311 HomoloGene: 134495 GeneCards: HIST1H3C 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:
26.05 – 26.05 Mb

Chr 3:
96.25 – 96.25 Mb

PubMed search

Histone H3.1 is a protein that in humans is encoded by the HIST1H3C gene.^[1]^[2]^[3]^[4]

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 is intronless and encodes a member of the histone H3 family. Transcripts from this gene lack polyA tails but instead contain a palindromic termination element. This gene is found in the large histone gene cluster on chromosome 6.^[4]

References

↑ Kardalinou E, Eick S, Albig W, Doenecke D (Dec 1993). "Association of a human H1 histone gene with an H2A pseudogene and genes encoding H2B.1 and H3.1 histones". J Cell Biochem 52 (4): 375–83. doi:10.1002/jcb.240520402. PMID 8227173.
↑ 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: HIST1H3C histone cluster 1, H3c".

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.
Munakata T, Adachi N, Yokoyama N, et al. (2000). "A human homologue of yeast anti-silencing factor has histone chaperone activity.". Genes Cells 5 (3): 221–33. doi:10.1046/j.1365-2443.2000.00319.x. PMID 10759893.
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.
Nielsen PR, Nietlispach D, Mott HR, et al. (2002). "Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9.". Nature 416 (6876): 103–7. doi:10.1038/nature722. PMID 11882902.
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.
Umehara T, Horikoshi M (2003). "Transcription initiation factor IID-interactive histone chaperone CIA-II implicated in mammalian spermatogenesis.". J. Biol. Chem. 278 (37): 35660–7. doi:10.1074/jbc.M303549200. PMID 12842904.
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.
Black BE, Foltz DR, Chakravarthy S, et al. (2004). "Structural determinants for generating centromeric chromatin.". Nature 430 (6999): 578–82. doi:10.1038/nature02766. PMID 15282608.

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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HIST1H3C

References

Further reading