HIST1H3C

HIST1H3C
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3WKJ, 3B95, 2C1J, 3AYW, 3WA9, 3U4S, 5AVB, 2CV5, 5AV5, 3U31, 2UXN, 3AZK, 2C1N, 5C11, 3QO2, 3X1V, 5C13, 4A0J, 4U68, 5AV8, 4LLB, 3U5O, 1O9S, 4FT2, 4HON, 3W99, 3ZVY, 4Z0R, 5AVC, 1CT6, 1Q3L, 3O37, 3W97, 3SOW, 3KMT, 4YM6, 4A7J, 3UEE, 2KWK, 4F4U, 3UEF, 3UIG, 4BD3, 3AZL, 4QBR, 4F56, 3AFA, 4LKA, 5CPK, 5FFV, 3V43, 5CH1, 3U5P, 3AZI, 3U5N, 3AZH, 3UIK, 4QBQ, 1U35, 4UY4, 2OT7, 5AV9, 2B2W, 3U3D, 3AZF, 3W98, 4I51, 4X3K, 4FWF, 2B2T, 2B2V, 4A0N, 2KWJ, 3WAA, 3QJ6, 5DAH, 3AZG, 3AZE, 3X1T, 3RIY, 2L75, 3A1B, 2VPG, 4QBS, 3O35, 5CPJ, 3ZG6, 4YM5, 3AZJ, 2RI7, 3AZN, 3AVR, 5CPI, 2LBM, 3W96, 3O34, 2M0O, 4L7X, 5CH2, 5AV6, 3AZM, 4UP0, 3X1S, 2OX0, 3UII, 3SOU, 4N4H, 4TN7, 1CS9, 3X1U, 4LXL, 2B2U, 2OQ6, 3RIG, 5C3I, 4YHP, 5B24, 5D6Y, 4YHZ, 4Z2M, 5HJD, 5HJC, 5HJB, 5B2I, 5HYN, 5FB0, 5FB1, 5IQL, 5B2J, 5JIN
Identifiers
Aliases	HIST1H3C, H3.1, H3/c, H3FC, histone cluster 1, H3c
External IDs	MGI: 2448355 HomoloGene: 134495 GeneCards: HIST1H3C
Gene ontology Molecular function • DNA binding • histone binding • protein binding • protein heterodimerization activity • cadherin binding involved in cell-cell adhesion Cellular component • nuclear nucleosome • membrane • nucleoplasm • protein complex • chromosome • extracellular region • nuclear chromosome • nucleosome • extracellular exosome • nucleus • nuclear chromosome, telomeric region • cell-cell adherens junction Biological process • telomere organization • cellular protein metabolic process • positive regulation of gene expression, epigenetic • nucleosome assembly • protein heterotetramerization • blood coagulation • DNA replication-dependent nucleosome assembly • regulation of gene silencing • chromatin silencing at rDNA • negative regulation of gene expression, epigenetic • gene silencing by RNA • xenophagy • positive regulation of defense response to virus by host • cell-cell adhesion Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	8352	15077
Ensembl	ENSG00000278272	ENSMUSG00000093769
UniProt	P68431	Q71DI3
RefSeq (mRNA)	NM_003531	NM_178216
RefSeq (protein)	NP_003520.1 NP_003521.2 NP_003522.1 NP_003523.1 NP_003524.1 NP_003525.1 NP_003526.1 NP_003527.1 NP_003528.1 NP_066298.1	NP_001005464.1 NP_001116847.1 NP_066403.2
Location (UCSC)	Chr 6: 26.05 – 26.05 Mb	Chr 3: 96.25 – 96.25 Mb
PubMed search	[1]	[2]
Wikidata

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Histone H3.1 is a protein that in humans is encoded by the HIST1H3C gene.^[3][4][5][6]

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 H3 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. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Kardalinou E, Eick S, Albig W, Doenecke D (Dec 1993). "Association of a human H1 histone gene with an H2A pseudogene and genes encoding H2B.1 and H3.1 histones". J Cell Biochem. 52 (4): 375–83. doi:10.1002/jcb.240520402. PMID 8227173.
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: HIST1H3C histone cluster 1, H3c".

Further reading

• 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.
• Munakata T, Adachi N, Yokoyama N, et al. (2000). "A human homologue of yeast anti-silencing factor has histone chaperone activity.". Genes Cells. 5 (3): 221–33. doi:10.1046/j.1365-2443.2000.00319.x. PMID 10759893.
• Hsu JY, Sun ZW, Li X, et al. (2000). "Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes.". Cell. 102 (3): 279–91. doi:10.1016/S0092-8674(00)00034-9. PMID 10975519.
• 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.
• Lachner M, O'Carroll D, Rea S, et al. (2001). "Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins.". Nature. 410 (6824): 116–20. doi:10.1038/35065132. PMID 11242053.
• 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.
• Yang L, Xia L, Wu DY, et al. (2002). "Molecular cloning of ESET, a novel histone H3-specific methyltransferase that interacts with ERG transcription factor.". Oncogene. 21 (1): 148–52. doi:10.1038/sj.onc.1204998. PMID 11791185.
• Nielsen PR, Nietlispach D, Mott HR, et al. (2002). "Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9.". Nature. 416 (6876): 103–7. doi:10.1038/nature722. PMID 11882902.
• 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.
• Umehara T, Horikoshi M (2003). "Transcription initiation factor IID-interactive histone chaperone CIA-II implicated in mammalian spermatogenesis.". J. Biol. Chem. 278 (37): 35660–7. doi:10.1074/jbc.M303549200. PMID 12842904.
• 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.
• Black BE, Foltz DR, Chakravarthy S, et al. (2004). "Structural determinants for generating centromeric chromatin.". Nature. 430 (6999): 578–82. doi:10.1038/nature02766. PMID 15282608.