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, histone cluster 1 H3 family member c, H3C3
External IDs	OMIM: 602812 MGI: 2448355 HomoloGene: 134495 GeneCards: HIST1H3C
Gene location (Human) Chr. Chromosome 6 (human) Band 6p22.2 Start 26,045,411 bp End 26,045,821 bp
Gene location (Mouse) Chr. Chromosome 3 (mouse) Band 3|3 F2.1 Start 96,154,001 bp End 96,155,825 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in stomach colon lung kidney heart vagina ovary testicle Top expressed in secondary oocyte morula bone marrow uterus thymus duodenum liver islet of Langerhans blastocyst spermatocyte More reference expression data BioGPS n/a
Gene ontology Molecular function DNA binding histone binding protein binding protein heterodimerization activity cadherin binding nucleosomal DNA binding Cellular component membrane nucleoplasm chromosome extracellular region nuclear chromosome extracellular exosome nucleosome nucleus protein-containing complex Biological process telomere organization epigenetic maintenance of chromatin in transcription-competent conformation protein heterotetramerization blood coagulation DNA replication-dependent chromatin assembly rDNA heterochromatin assembly negative regulation of gene expression, epigenetic chromatin organization regulation of gene silencing by miRNA nucleosome assembly interleukin-7-mediated signaling pathway regulation of megakaryocyte differentiation regulation of hematopoietic stem cell differentiation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 8352 15077 Ensembl ENSG00000278272 ENSMUSG00000093769 UniProt P68431 P84228 RefSeq (mRNA) NM_003531 NM_178216 RefSeq (protein) NP_066298 NP_003520 NP_003525 NP_003527 NP_473386 NP_835734 NP_783584 NP_835510 NP_835587 NP_038576 NP_835511 NP_835512 Location (UCSC) Chr 6: 26.05 – 26.05 Mb Chr 3: 96.15 – 96.16 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Histone H3.1 is a protein that in humans is encoded by the HIST1H3C gene.

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, instead containing a palindromic termination element. This gene is found in the large histone gene cluster on chromosome 6.

Further reading

• Albig W, Doenecke D (1998). "The human histone gene cluster at the D6S105 locus". Human Genetics. 101 (3): 284–94. doi:10.1007/s004390050630. PMID 9439656. S2CID 38539096.
• El Kharroubi A, Piras G, Zensen R, Martin MA (1998). "Transcriptional activation of the integrated chromatin-associated human immunodeficiency virus type 1 promoter". Molecular and Cellular Biology. 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 to Cells. 5 (3): 221–33. doi:10.1046/j.1365-2443.2000.00319.x. PMID 10759893. S2CID 20198031.
• 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. S2CID 16057773.
• 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. Bibcode:2001Natur.410..116L. doi:10.1038/35065132. PMID 11242053. S2CID 4331863.
• 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. S2CID 10912876.
• 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. Bibcode:2002Natur.416..103N. doi:10.1038/nature722. PMID 11882902. S2CID 4423019.
• 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". Proceedings of the National Academy of Sciences of the United States of America. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. 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". Journal of Biological Chemistry. 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". The EMBO Journal. 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. Bibcode:2004Natur.430..578B. doi:10.1038/nature02766. PMID 15282608. S2CID 4392941.