HIST2H3C

Histone cluster 2, H3c

PDB rendering based on 1aoi.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
2IIJ, 2X4W, 2X4X, 2X4Y, 3AV1, 3DB3, 3MO8, 3QO2, 3R93, 4MZF, 4MZG, 4MZH, 4OUC

Identifiers

Symbols

HIST2H3C ; H3; H3.2; H3/M; H3F2; H3FM; H3FN

External IDs

OMIM: 142780 MGI: 2448355 HomoloGene: 134475 GeneCards: HIST2H3C Gene

Gene ontology
Molecular function	• DNA binding
Cellular component	• nucleosome • nucleus • chromosome
Biological process	• nucleosome assembly • chromosome organization and biogenesis (sensu Eukaryota)
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
149.78 – 149.79 Mb

Chr 1:
180.8 – 180.81 Mb

PubMed search

Histone H3.2 is a protein that in humans is encoded by the HIST2H3C gene.^[1]^[2]^[3]

Function

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 a histone cluster on chromosome 1. This gene is one of four histone genes in the cluster that are duplicated; this record represents the telomeric copy.^[3]

Interactions

HIST2H3C has been shown to interact with NCOA6.^[4]

References

↑ Marzluff WF, Gongidi P, Woods KR, Jin J, Maltais LJ (Oct 2002). "The human and mouse replication-dependent histone genes". Genomics 80 (5): 487–498. doi:10.1016/S0888-7543(02)96850-3. PMID 12408966.
↑ Marashi F, Helms S, Shiels A, Silverstein S, Greenspan DS, Stein G et al. (Jul 1986). "Enhancer-facilitated expression of prokaryotic and eukaryotic genes using human histone gene 5' regulatory sequences". Biochem Cell Biol 64 (4): 277–289. doi:10.1139/o86-039. PMID 3013246.
↑ 3.0 3.1 "Entrez Gene: HIST2H3C histone cluster 2, H3c".
↑ Goo YH, Sohn YC, Kim DH, Kim SW, Kang MJ, Jung DJ et al. (Jan 2003). "Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins". Mol. Cell. Biol. 23 (1): 140–149. doi:10.1128/MCB.23.1.140-149.2003. PMC 140670. PMID 12482968.

Green L, Van Antwerpen R, Stein J, Stein G, Tripputi P, Emanuel B et al. (1984). "A major human histone gene cluster on the long arm of chromosome 1". Science 226 (4676): 838–840. doi:10.1126/science.6494913. PMID 6494913.
Ohe Y, Iwai K (1982). "Human spleen histone H3. Isolation and amino acid sequence". J. Biochem. 90 (4): 1205–11. PMID 7309716.
Díaz-Jullien C, Pérez-Estévez A, Covelo G, Freire M (1996). "Prothymosin alpha binds histones in vitro and shows activity in nucleosome assembly assay". Biochim. Biophys. Acta 1296 (2): 219–27. doi:10.1016/0167-4838(96)00072-6. PMID 8814229. Vancouver style error (help)
Albig W, Doenecke D (1998). "The human histone gene cluster at the D6S105 locus". Hum. Genet. 101 (3): 284–294. 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.
Ahn J, Gruen JR (1999). "The genomic organization of the histone clusters on human 6p21.3". Mamm. Genome 10 (7): 768–770. doi:10.1007/s003359901089. PMID 10384058.
Goto H, Tomono Y, Ajiro K, Kosako H, Fujita M, Sakurai M et al. (1999). "Identification of a novel phosphorylation site on histone H3 coupled with mitotic chromosome condensation". J. Biol. Chem. 274 (36): 25543–25549. doi:10.1074/jbc.274.36.25543. PMID 10464286.
Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD 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): 278–295. doi:10.1006/viro.2000.0593. PMID 11080476.
Lachner M, O'Carroll D, Rea S, Mechtler K, Jenuwein T (2001). "Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins". Nature 410 (6824): 116–120. doi:10.1038/35065132. PMID 11242053.
Shankaranarayanan P, Chaitidis P, Kühn H, Nigam S (2001). "Acetylation by histone acetyltransferase CREB-binding protein/p300 of STAT6 is required for transcriptional activation of the 15-lipoxygenase-1 gene". J. Biol. Chem. 276 (46): 42753–42760. doi:10.1074/jbc.M102626200. PMID 11509556. Vancouver style error (help)
Deng L, Wang D, de la Fuente C, Wang L, Li H, Lee CG et al. (2001). "Enhancement of the p300 HAT activity by HIV-1 Tat on chromatin DNA". Virology 289 (2): 312–326. doi:10.1006/viro.2001.1129. PMID 11689053.
Goto H, Yasui Y, Nigg EA, Inagaki M (2002). "Aurora-B phosphorylates Histone H3 at serine28 with regard to the mitotic chromosome condensation". Genes Cells 7 (1): 11–17. doi:10.1046/j.1356-9597.2001.00498.x. PMID 11856369.
Ganesan S, Silver DP, Greenberg RA, Avni D, Drapkin R, Miron A et al. (2002). "BRCA1 supports XIST RNA concentration on the inactive X chromosome". Cell 111 (3): 393–405. doi:10.1016/S0092-8674(02)01052-8. PMID 12419249.
Goo YH, Sohn YC, Kim DH, Kim SW, Kang MJ, Jung DJ et al. (2003). "Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins". Mol. Cell. Biol. 23 (1): 140–149. doi:10.1128/MCB.23.1.140-149.2003. PMC 140670. PMID 12482968.
Preuss U, Landsberg G, Scheidtmann KH (2003). "Novel mitosis-specific phosphorylation of histone H3 at Thr11 mediated by Dlk/ZIP kinase". Nucleic Acids Res. 31 (3): 878–885. doi:10.1093/nar/gkg176. PMC 149197. PMID 12560483.
Yoon HG, Chan DW, Huang ZQ, Li J, Fondell JD, Qin J et al. (2003). "Purification and functional characterization of the human N-CoR complex: the roles of HDAC3, TBL1 and TBLR1". EMBO J. 22 (6): 1336–1346. doi:10.1093/emboj/cdg120. PMC 151047. PMID 12628926.
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): 6550–6561. doi:10.1093/emboj/cdg631. PMC 291826. PMID 14657027.

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

HIST2H3C

Function

Interactions

References

Further reading