HIST1H3F

Histone H3.1 is a protein that in humans is encoded by the HIST1H3F gene.

H3C7
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	H3C7, H3/i, H3FI, histone cluster 1, H3f, histone cluster 1 H3 family member f, H3 clustered histone 7, HIST1H3F, H3C4, H3C12, H3C2, H3C8, H3C10, H3C3, H3C6, H3C1, H3C11
External IDs	OMIM: 602816; MGI: 2448350; HomoloGene: 134472; GeneCards: H3C7; OMA:H3C7 - orthologs
Gene location (Human) Chr. Chromosome 6 (human) Band 6p22.2 Start 26,250,142 bp End 26,250,635 bp
Gene location (Mouse) Chr. Chromosome 13 (mouse) Band 13|13 A3.1 Start 21,967,130 bp End 21,967,540 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in bone marrow cells gonad epithelium of colon mucosa of transverse colon tonsil stromal cell of endometrium ventricular zone ganglionic eminence blood cervix Top expressed in genital tubercle embryo neural tube triceps brachii muscle blood vastus lateralis muscle embryo spermatocyte yolk sac temporal muscle 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 8968 319153 Ensembl ENSG00000277775 ENSMUSG00000101972 UniProt P68431 P68433 RefSeq (mRNA) NM_021018 NM_178207 RefSeq (protein) NP_066298 NP_003520 NP_003525 NP_003527 NP_835513 NP_835514 NP_659539 Location (UCSC) Chr 6: 26.25 – 26.25 Mb Chr 13: 21.97 – 21.97 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.
• 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.
• 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.
• Xiao B, Jing C, Wilson JR, et al. (2003). "Structure and catalytic mechanism of the human histone methyltransferase SET7/9" (PDF). Nature. 421 (6923): 652–6. Bibcode:2003Natur.421..652X. doi:10.1038/nature01378. PMID 12540855. S2CID 4423407.
• 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.
• 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.
• Couture JF, Collazo E, Hauk G, Trievel RC (2006). "Structural basis for the methylation site specificity of SET7/9". Nat. Struct. Mol. Biol. 13 (2): 140–6. doi:10.1038/nsmb1045. PMID 16415881. S2CID 38483056.
• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.