HIST4H4

Histone cluster 4, H4

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, 4GQB, 4H9N, 4H9O, 4H9P, 4H9Q, 4H9R, 4H9S, 4HGA, 4M38, 4N3W, 4N4F

Identifiers

Symbols

HIST4H4 ; H4/p

External IDs

OMIM: 615069 MGI: 2448436 HomoloGene: 134468 ChEMBL: 5876 GeneCards: HIST4H4 Gene

Gene ontology
Molecular function	• DNA binding
Cellular component	• nucleosome • nucleus • chromosome
Biological process	• establishment and/or maintenance of chromatin architecture • nucleosome assembly • phosphoinositide-mediated signaling
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
149.8 – 149.81 Mb

Chr 13:
21.74 – 21.74 Mb

PubMed search

Histone H4 is a protein that in humans is encoded by the HIST4H4 gene.^[1]

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone 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 H4 family. Transcripts from this gene lack polyA tails; instead, they contain a palindromic termination element.^[2]

References

↑ Marzluff WF, Gongidi P, Woods KR, Jin J, Maltais LJ (Oct 2002). "The human and mouse replication-dependent histone genes". Genomics 80 (5): 487–98. doi:10.1016/S0888-7543(02)96850-3. PMID 12408966.
↑ "Entrez Gene: HIST4H4 histone cluster 4, H4".

Pauli U, Chrysogelos S, Stein G et al. (1987). "Protein-DNA interactions in vivo upstream of a cell cycle-regulated human H4 histone gene.". Science 236 (4806): 1308–11. doi:10.1126/science.3035717. PMID 3035717.
Borowski P, Heiland M, Oehlmann K et al. (1996). "Non-structural protein 3 of hepatitis C virus inhibits phosphorylation mediated by cAMP-dependent protein kinase.". Eur. J. Biochem. 237 (3): 611–8. doi:10.1111/j.1432-1033.1996.0611p.x. PMID 8647104.
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.
Zhang Y, Sun ZW, Iratni R et al. (1998). "SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex". Mol. Cell 1 (7): 1021–31. doi:10.1016/S1097-2765(00)80102-1. PMID 9651585.
Carrier F, Georgel PT, Pourquier P et al. (1999). "Gadd45, a p53-Responsive Stress Protein, Modifies DNA Accessibility on Damaged Chromatin". Mol. Cell. Biol. 19 (3): 1673–85. PMC 83961. PMID 10022855.
Buggy JJ, Sideris ML, Mak P et al. (2001). "Cloning and characterization of a novel human histone deacetylase, HDAC8". Biochem. J. 350 Pt 1 (Pt 1): 199–205. doi:10.1042/0264-6021:3500199. PMC 1221242. PMID 10926844.
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.
Chadwick BP, Willard HF (2001). "A Novel Chromatin Protein, Distantly Related to Histone H2a, Is Largely Excluded from the Inactive X Chromosome". J. Cell Biol. 152 (2): 375–84. doi:10.1083/jcb.152.2.375. PMC 2199617. PMID 11266453.
Kovalsky O, Lung FD, Roller PP, Fornace AJ (2001). "Oligomerization of human Gadd45a protein". J. Biol. Chem. 276 (42): 39330–9. doi:10.1074/jbc.M105115200. PMID 11498536.
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.
Lahn BT, Tang ZL, Zhou J et al. (2002). "Previously uncharacterized histone acetyltransferases implicated in mammalian spermatogenesis". Proc. Natl. Acad. Sci. U.S.A. 99 (13): 8707–12. doi:10.1073/pnas.082248899. PMC 124363. PMID 12072557.
Ono S, Oue N, Kuniyasu H et al. (2003). "Acetylated histone H4 is reduced in human gastric adenomas and carcinomas". J. Exp. Clin. Cancer Res. 21 (3): 377–82. PMID 12385581.
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.
Kzhyshkowska J, Rusch A, Wolf H, Dobner T (2003). "Regulation of transcription by the heterogeneous nuclear ribonucleoprotein E1B-AP5 is mediated by complex formation with the novel bromodomain-containing protein BRD7". Biochem. J. 371 (Pt 2): 385–93. doi:10.1042/BJ20021281. PMC 1223277. PMID 12489984.
Fujita K, Shimazaki N, Ohta Y et al. (2004). "Terminal deoxynucleotidyltransferase forms a ternary complex with a novel chromatin remodeling protein with 82 kDa and core histone". Genes Cells 8 (6): 559–71. doi:10.1046/j.1365-2443.2003.00656.x. PMID 12786946.
Shiio Y, Eisenman RN (2004). "Histone sumoylation is associated with transcriptional repression". Proc. Natl. Acad. Sci. U.S.A. 100 (23): 13225–30. doi:10.1073/pnas.1735528100. PMC 263760. PMID 14578449.
Coleman MA, Miller KA, Beernink PT et al. (2004). "Identification of chromatin-related protein interactions using protein microarrays". Proteomics 3 (11): 2101–7. doi:10.1002/pmic.200300593. PMID 14595808.
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.
Kanno T, Kanno Y, Siegel RM et al. (2004). "Selective recognition of acetylated histones by bromodomain proteins visualized in living cells". Mol. Cell 13 (1): 33–43. doi:10.1016/S1097-2765(03)00482-9. PMID 14731392.

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

HIST4H4

References

Further reading