Histone H3.1

Histone H3.1 is a protein in humans that is encoded by the H3C1 gene.

H3C1
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	H3C1, H3/A, H3FA, histone cluster 1, H3a, histone cluster 1 H3 family member a, HIST1H3A, H3 clustered histone 1, H3C4, H3C7, H3C12, H3C2, H3C8, H3C10, H3C3, H3C6, H3C11
External IDs	OMIM: 602810 MGI: 2448322 HomoloGene: 134332 GeneCards: H3C1
Gene location (Human) Chr. Chromosome 6 (human) Band 6p22.2 Start 26,020,451 bp End 26,020,958 bp
Gene location (Mouse) Chr. Chromosome 13 (mouse) Band 13|13 A3.1 Start 23,759,937 bp End 23,761,185 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in bone marrow cells Achilles tendon monocyte thymus islet of Langerhans blood gastric mucosa right coronary artery corpus callosum cervix Top expressed in maxillary prominence medial ganglionic eminence quadriceps femoris muscle primitive streak blood left colon vastus lateralis muscle triceps brachii muscle skeletal muscle tissue autopod region 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 8350 319149 Ensembl ENSG00000275714 ENSMUSG00000099583 UniProt P68431 P84228 RefSeq (mRNA) NM_003529 NM_178204 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: 26.02 – 26.02 Mb Chr 13: 23.76 – 23.76 Mb PubMed search
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. This structure consists of approximately 146 bp of DNA wrapped around a nucleosome, an 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 H3 family. Transcripts from this gene lack polyA tails; instead, they contain a palindromic termination element. This gene is found in the large histone gene cluster on chromosome 6p22-p21.3.

Further reading

• Albig W, Kardalinou E, Drabent B, et al. (1991). "Isolation and characterization of two human H1 histone genes within clusters of core histone genes". Genomics. 10 (4): 940–8. doi:10.1016/0888-7543(91)90183-F. PMID 1916825.
• 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. 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". Mol. Cell. Biol. 18 (5): 2535–44. doi:10.1128/mcb.18.5.2535. PMC 110633. PMID 9566873.
• Ahn J, Gruen JR (1999). "The genomic organization of the histone clusters on human 6p21.3". Mamm. Genome. 10 (7): 768–70. doi:10.1007/s003359901089. PMID 10384058. S2CID 28275496.
• Rea S, Eisenhaber F, O'Carroll D, et al. (2000). "Regulation of chromatin structure by site-specific histone H3 methyltransferases". Nature. 406 (6796): 593–9. Bibcode:2000Natur.406..593R. doi:10.1038/35020506. PMID 10949293. S2CID 205008015.
• 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". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Koessler H, Doenecke D, Albig W (2003). "Aberrant expression pattern of replication-dependent histone h3 subtype genes in human tumor cell lines". DNA Cell Biol. 22 (4): 233–41. doi:10.1089/104454903321908629. PMID 12823900.
• 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.
• Citterio E, Papait R, Nicassio F, et al. (2004). "Np95 is a histone-binding protein endowed with ubiquitin ligase activity". Mol. Cell. Biol. 24 (6): 2526–35. doi:10.1128/MCB.24.6.2526-2535.2004. PMC 355858. PMID 14993289.