HIST4H4

H4-16

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes

4H9O, 3WKJ, 3AYW, 3WA9, 5B0Z, 5AVB, 2CV5, 5AV5, 3AV2, 3WTP, 3AV1, 3AZK, 3X1V, 5AV8, 1F66, 4QUU, 3CFS, 4YYK, 4QUT, 3NQJ, 3A6N, 3W99, 5AVC, 2RS9, 3F9Z, 3QZT, 3QBY, 3W97, 4M38, 4YM6, 3CFV, 4HGA, 1EQZ, 2RJE, 3QZV, 1HQ3, 4H9P, 3AZL, 3AFA, 1TZY, 3UVY, 5CPK, 3JPX, 4U9W, 4N3W, 4YYJ, 4YYD, 4H9N, 4H9R, 3AZI, 4LD9, 3UVX, 3AZH, 5BNX, 4N4F, 1U35, 4YYG, 3O36, 2ARO, 5AV9, 4H9S, 3AZF, 3W98, 4GQB, 4H9Q, 5BNV, 3WAA, 3AZG, 3AZE, 2RNY, 1ZKK, 2QQS, 2LVM, 3X1T, 3AN2, 2KWO, 3QZS, 3F9W, 5FFW, 5CPJ, 3F9X, 3IJ1, 4YM5, 3AZJ, 4YY6, 3AZN, 2IG0, 4YYH, 4YYI, 5CPI, 3W96, 3R45, 2KWN, 3F9Y, 5AV6, 3AZM, 5BO0, 3X1S, 4QYD, 4KGC, 3UVW, 4YYN, 3X1U, 3UW9, 2F8N, 3NQU, 5B0Y, 4YYM, 5C3I, 4Z5T, 5B24, 5FA5, 4Z2M, 5E5A, 5FWE, 5B2I, 5B40, 5B2J, 5JA4, 5AY8, 4ZUX

Identifiers

Aliases

H4-16, H4/p, histone cluster 4, H4, histone cluster 4 H4, HIST4H4, H4 histone 16, H4C5, H4C4, H4C9, H4C12, H4C3, H4C13, H4C11, H4C1, H4C14, H4C15, H4C8, H4C6, H4C2, H4C16

External IDs

OMIM: 615069; MGI: 2448432; HomoloGene: 134468; GeneCards: H4-16; OMA:H4-16 - orthologs

Gene location (Human)

Chr.	Chromosome 12 (human)^[1]

Band	12p12.3	Start	14,767,999 bp^[1]
Band	12p12.3	End	14,771,131 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 13 (mouse)^[2]

Band	13\|13 A3.1	Start	22,224,806 bp^[2]
Band	13\|13 A3.1	End	22,225,532 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

bone marrow cells

Achilles tendon

epithelium of colon

tonsil

right uterine tube

prostate

testicle

sural nerve

body of pancreas

stomach

Top expressed in

muscle of thigh

granulocyte

blood

triceps brachii muscle

ventricular zone

sternocleidomastoid muscle

temporal muscle

quadriceps femoris muscle

soleus muscle

embryo

More reference expression data

BioGPS

n/a

Gene ontology
Molecular function	protein domain specific binding protein binding protein heterodimerization activity DNA binding histone binding RNA binding
Cellular component	membrane chromosome nucleoplasm extracellular region nuclear chromosome nucleosome extracellular exosome nucleus extracellular matrix protein-containing complex
Biological process	telomere organization epigenetic maintenance of chromatin in transcription-competent conformation protein heterotetramerization negative regulation of megakaryocyte differentiation CENP-A containing chromatin assembly DNA replication-dependent chromatin assembly rDNA heterochromatin assembly negative regulation of gene expression, epigenetic DNA-templated transcription, initiation double-strand break repair via nonhomologous end joining beta-catenin-TCF complex assembly telomere capping nucleosome assembly regulation of gene silencing by miRNA regulation of megakaryocyte differentiation regulation of hematopoietic stem cell differentiation
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


121504


319158

Ensembl


ENSG00000197837


ENSMUSG00000060639

UniProt


P62805


P62806

RefSeq (mRNA)


NM_175054


NM_175656

RefSeq (protein)

NP_003537 NP_003486 NP_003535 NP_003539 NP_003531
NP_003536

NP_291074 NP_783587 NP_783588 NP_835499 NP_835500
NP_001182350 NP_835515 NP_783585 NP_783586 NP_835582 NP_835583 NP_783583 NP_694813

Location (UCSC)

Chr 12: 14.77 – 14.77 Mb

Chr 13: 22.22 – 22.23 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Histone H4 is a protein that in humans is encoded by the HIST4H4 gene.^[5]

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.^[6]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000197837 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000060639 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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. Bibcode:1987Sci...236.1308P. 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. doi:10.1128/mcb.18.5.2535. 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. doi:10.1128/MCB.19.3.1673. 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 (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. S2CID 20145752.
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. Bibcode:2002PNAS...99.8707L. 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. Bibcode:2002PNAS...9916899M. 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. S2CID 25223336.
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. S2CID 23471253.
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