HIST1H4C

Histone cluster 1, H4c

PDB rendering based on 1aoi.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes

1ZKK, 2BQZ, 2CV5, 2IG0, 2KWN, 2KWO, 2LVM, 2QQS, 2RJE, 2RNY, 2RS9, 3A6N, 3AFA, 3AN2, 3AV1, 3AV2, 3AYW, 3AZE, 3AZF, 3AZG, 3AZH, 3AZI, 3AZJ, 3AZK, 3AZL, 3AZM, 3AZN, 3CFS, 3CFV, 3F9W, 3F9X, 3F9Y, 3F9Z, 3IJ1, 3JPX, 3NQJ, 3NQU, 3O36, 3QBY, 3QZS, 3QZT, 3QZV, 3R45, 3UVW, 3UVX, 3UVY, 3UW9, 3W96, 3W97, 3W98, 3W99, 3WA9, 3WAA, 3WKJ, 3WTP, 4GQB, 4H9N, 4H9O, 4H9P, 4H9Q, 4H9R, 4H9S, 4HGA, 4M38, 4N3W, 4N4F, 4QUT, 4QUU, 4QYD

Identifiers

Symbols

HIST1H4C ; H4/g; H4FG; dJ221C16.1

External IDs

OMIM: 602827 MGI: 2448420 HomoloGene: 134234 GeneCards: HIST1H4C Gene

Gene ontology
Molecular function	• DNA binding • protein binding • histone demethylase activity (H4-K20 specific) • histone binding • poly(A) RNA binding • protein heterodimerization activity
Cellular component	• nuclear chromosome • nucleosome • extracellular region • nucleus • nucleoplasm • membrane • protein complex • extracellular exosome
Biological process	• chromatin silencing at rDNA • mitotic cell cycle • telomere maintenance • chromatin organization • nucleosome assembly • DNA replication-dependent nucleosome assembly • DNA replication-independent nucleosome assembly • small GTPase mediated signal transduction • gene expression • DNA methylation on cytosine • CENP-A containing nucleosome assembly • histone H4-K20 demethylation • regulation of gene expression, epigenetic • negative regulation of megakaryocyte differentiation • negative regulation of gene expression, epigenetic • protein heterotetramerization
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 6:
26.1 – 26.1 Mb

Chr 3:
96.26 – 96.26 Mb

PubMed search

Histone H4 is a protein that in humans is encoded by the HIST1H4C gene.^[1]^[2]^[3]

Function

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 H4 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.^[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: HIST1H4C histone cluster 1, H4c".

Drabent B, Kardalinou E, Bode C, Doenecke D (1995). "Association of histone H4 genes with the mammalian testis-specific H1t histone gene". DNA Cell Biol. 14 (7): 591–7. doi:10.1089/dna.1995.14.591. PMID 7626218.
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.
Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F (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.
Deng L, Wang D, de la Fuente C, Wang L, Li H, Lee CG, Donnelly R, Wade JD, Lambert P, Kashanchi F (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.
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.
Dickinson LA, Burnett R, Melander C, Edelson BS, Arora PS, Dervan PB, Gottesfeld JM (2005). "Arresting cancer proliferation by small-molecule gene regulation". Chem. Biol. 11 (11): 1583–94. doi:10.1016/j.chembiol.2004.09.004. PMID 15556009.

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

1id3: CRYSTAL STRUCTURE OF THE YEAST NUCLEOSOME CORE PARTICLE REVEALS FUNDAMENTAL DIFFERENCES IN INTER-NUCLEOSOME INTERACTIONS

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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HIST1H4C

Function

References

Further reading