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
External IDs	OMIM: 615069 MGI: 2448432 HomoloGene: 134468 GeneCards: H4-16
Gene location (Human)
Chr.	Chromosome 12 (human)[1]
End	14,771,131 bp[1]
Gene ontology
Molecular function	• protein domain specific binding; • GO:0001948 protein binding; • protein heterodimerization activity; • DNA binding; • histone binding; • RNA binding;
Cellular component	• membrane; • chromosome; • protein complex; • nucleoplasm; • extracellular region; • nuclear chromosome; • nucleosome; • extracellular exosome; • cell nucleus; • nuclear chromosome, telomeric region; • extracellular matrix; • nuclear nucleosome; • macromolecular complex;
Biological process	• telomere organization; • cellular protein metabolic process; • positive regulation of gene expression, epigenetic; • protein heterotetramerization; • negative regulation of megakaryocyte differentiation; • CENP-A containing nucleosome assembly; • DNA replication-dependent nucleosome assembly; • chromatin silencing at rDNA; • negative regulation of gene expression, epigenetic; • DNA-templated transcription, initiation; • DNA replication-independent nucleosome assembly; • 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
	121504
	319158
	ENSG00000197837
	n/a
	P62805
	P62806
	NM_175054
	NM_175656
NP_001029249; NP_003486; NP_003531; NP_003535; NP_003537;
	NP_003539; NP_003536
NP_835515; NP_783587; NP_835582; NP_835499; NP_291074;
	NP_001182350; NP_783586; NP_783585; NP_835500; NP_835583; NP_783583; NP_783588; NP_694813
	Wikidata
View/Edit Human	View/Edit Mouse

Histone H4 is a protein that in humans is encoded by the HIST4H4 gene.[4]

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.[5]

References

GRCh38: Ensembl release 89: ENSG00000197837 - 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. 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.
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.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000197837 - Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[3] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid12408966-4] 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-5] "Entrez Gene: HIST4H4 histone cluster 4, H4".

HIST4H4

References

Further reading