HIST1H4A

Histone H4 is a protein that in humans is encoded by the HIST1H4A gene.[4][5][6]

H4C1
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	H4C1, H4FA, histone cluster 1, H4a, histone cluster 1 H4 family member a, HIST1H4A, H4 clustered histone 1, H4C5, H4C4, H4C9, H4C12, H4-16, H4C3, H4C13, H4C11, H4C14, H4C15, H4C8, H4C6, H4C2
External IDs	OMIM: 602822 MGI: 2448423 HomoloGene: 134481 GeneCards: H4C1
Gene location (Human) Chr. Chromosome 6 (human)[1] Band 6p22.2 Start 26,021,679 bp[1] End 26,021,990 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 • 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
Species	Human	Mouse
Entrez	8359	319156
Ensembl	ENSG00000278637	n/a
UniProt	P62805	P62806
RefSeq (mRNA)	NM_003538	NM_175654
RefSeq (protein)	NP_003537 NP_003486 NP_003535 NP_003539 NP_003531 NP_003536	NP_783585 NP_783588 NP_835583 NP_783583 NP_835499 NP_835500 NP_291074 NP_783586 NP_694813 NP_835515 NP_783587 NP_835582 NP_001182350
Location (UCSC)	Chr 6: 26.02 – 26.02 Mb	n/a
PubMed search	[2]	[3]
Wikidata
View/Edit Human View/Edit Mouse

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.[6]

References

1. GRCh38: Ensembl release 89: ENSG00000278637 - 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.
4. 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.
5. 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.
6. "Entrez Gene: HIST1H4A histone cluster 1, H4a".

Further reading

• 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.
• 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. doi:10.1128/mcb.18.5.2535. PMC 110633. PMID 9566873.
• Lorain S, Quivy JP, Monier-Gavelle F, et al. (1998). "Core histones and HIRIP3, a novel histone-binding protein, directly interact with WD repeat protein HIRA". Mol. Cell. Biol. 18 (9): 5546–56. doi:10.1128/MCB.18.9.5546. PMC 109139. PMID 9710638.
• 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.
• Freire J, Covelo G, Sarandeses C, et al. (2001). "Identification of nuclear-import and cell-cycle regulatory proteins that bind to prothymosin alpha". Biochem. Cell Biol. 79 (2): 123–31. doi:10.1139/bcb-79-2-123. PMID 11310559.
• 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.
• 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.
• Yoon HG, Chan DW, Huang ZQ, et al. (2003). "Purification and functional characterization of the human N-CoR complex: the roles of HDAC3, TBL1 and TBLR1". EMBO J. 22 (6): 1336–46. 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): 6550–61. doi:10.1093/emboj/cdg631. PMC 291826. PMID 14657027.
• Phee H, Abraham RT, Weiss A (2005). "Dynamic recruitment of PAK1 to the immunological synapse is mediated by PIX independently of SLP-76 and Vav1". Nat. Immunol. 6 (6): 608–17. doi:10.1038/ni1199. PMID 15864311.