HIST2H3C

Histone H3.2 is a protein that in humans is encoded by the HIST2H3C gene.^[4][5][6]

H3C14
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2IIJ, 2X4W, 2X4X, 2X4Y, 3AV1, 3DB3, 3MO8, 3R93, 4MZF, 4MZG, 4MZH, 4OUC, 5BO0, 2HIO, 5B0Z, 2ARO, 1EQZ, 1HQ3, 4KGC, 1TZY, 4UUZ, 2F8N, 5B0Y, 4LD9, 5B40, 5CIU
Identifiers
Aliases	H3C14, H3, H3.2, H3/M, H3F2, H3FM, H3FN, histone cluster 2, H3c, histone cluster 2 H3 family member c, HIST2H3C, H3 clustered histone 14, H3C15, H3C13
External IDs	OMIM: 142780; MGI: 3650546; HomoloGene: 134475; GeneCards: H3C14; OMA:H3C14 - orthologs
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1q21.2 Start 149,840,687 bp[1] End 149,841,208 bp[1]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in bone marrow cells epithelium of colon ganglionic eminence ventricular zone right uterine tube cerebellum cerebellar cortex cerebellar hemisphere right hemisphere of cerebellum gonad n/a More reference expression data BioGPS n/a
Gene ontology Molecular function protein heterodimerization activity DNA binding histone binding protein binding chromatin binding nucleosomal DNA binding Cellular component extracellular exosome extracellular region nucleoplasm chromosome nucleosome nucleus chromatin Biological process epigenetic maintenance of chromatin in transcription-competent conformation blood coagulation rDNA heterochromatin assembly nucleosome assembly negative regulation of gene expression, epigenetic negative regulation of transcription by RNA polymerase II chromatin organization regulation of gene silencing by miRNA interleukin-7-mediated signaling pathway regulation of megakaryocyte differentiation regulation of hematopoietic stem cell differentiation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 126961 625328 Ensembl ENSG00000203811 ENSMUSG00000082029 UniProt Q71DI3 P02301 RefSeq (mRNA) NM_021059 NM_001370931 RefSeq (protein) NP_066403 NP_001116847 XP_894986 Location (UCSC) Chr 1: 149.84 – 149.84 Mb n/a PubMed search [2] [3]
Wikidata
View/Edit Human View/Edit Mouse

Function

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 a histone cluster on chromosome 1. This gene is one of four histone genes in the cluster that are duplicated; this record represents the telomeric copy.^[6]

Interactions

HIST2H3C has been shown to interact with NCOA6.^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000203811 – 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. Marzluff WF, Gongidi P, Woods KR, Jin J, Maltais LJ (Oct 2002). "The human and mouse replication-dependent histone genes". Genomics. 80 (5): 487–498. doi:10.1016/S0888-7543(02)96850-3. PMID 12408966.
5. Marashi F, Helms S, Shiels A, Silverstein S, Greenspan DS, Stein G, Stein J (Jul 1986). "Enhancer-facilitated expression of prokaryotic and eukaryotic genes using human histone gene 5' regulatory sequences". Biochem Cell Biol. 64 (4): 277–289. doi:10.1139/o86-039. PMID 3013246.
6. "Entrez Gene: HIST2H3C histone cluster 2, H3c".
7. Goo YH, Sohn YC, Kim DH, Kim SW, Kang MJ, Jung DJ, Kwak E, Barlev NA, Berger SL, Chow VT, Roeder RG, Azorsa DO, Meltzer PS, Suh PG, Song EJ, Lee KJ, Lee YC, Lee JW (Jan 2003). "Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins". Mol. Cell. Biol. 23 (1): 140–149. doi:10.1128/MCB.23.1.140-149.2003. PMC 140670. PMID 12482968.

Further reading

• Green L, Van Antwerpen R, Stein J, Stein G, Tripputi P, Emanuel B, Selden J, Croce C (1984). "A major human histone gene cluster on the long arm of chromosome 1". Science. 226 (4676): 838–840. Bibcode:1984Sci...226..838G. doi:10.1126/science.6494913. PMID 6494913.
• Ohe Y, Iwai K (1982). "Human spleen histone H3. Isolation and amino acid sequence". J. Biochem. 90 (4): 1205–11. doi:10.1093/oxfordjournals.jbchem.a133573. PMID 7309716.
• Díaz-Jullien C, Pérez-Estévez A, Covelo G, Freire M (1996). "Prothymosin alpha binds histones in vitro and shows activity in nucleosome assembly assay". Biochim. Biophys. Acta. 1296 (2): 219–27. doi:10.1016/0167-4838(96)00072-6. PMID 8814229.
• Albig W, Doenecke D (1998). "The human histone gene cluster at the D6S105 locus". Hum. Genet. 101 (3): 284–294. 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): 768–770. doi:10.1007/s003359901089. PMID 10384058. S2CID 28275496.
• Goto H, Tomono Y, Ajiro K, Kosako H, Fujita M, Sakurai M, Okawa K, Iwamatsu A, Okigaki T, Takahashi T, Inagaki M (1999). "Identification of a novel phosphorylation site on histone H3 coupled with mitotic chromosome condensation". J. Biol. Chem. 274 (36): 25543–25549. doi:10.1074/jbc.274.36.25543. PMID 10464286.
• Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F (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): 278–295. doi:10.1006/viro.2000.0593. PMID 11080476.
• Lachner M, O'Carroll D, Rea S, Mechtler K, Jenuwein T (2001). "Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins". Nature. 410 (6824): 116–120. doi:10.1038/35065132. PMID 11242053. S2CID 4331863.
• Shankaranarayanan P, Chaitidis P, Kühn H, Nigam S (2001). "Acetylation by histone acetyltransferase CREB-binding protein/p300 of STAT6 is required for transcriptional activation of the 15-lipoxygenase-1 gene". J. Biol. Chem. 276 (46): 42753–42760. doi:10.1074/jbc.M102626200. PMID 11509556.
• Deng L, Wang D, de la Fuente C, Wang L, Li H, Lee CG, Donnelly R, Wade JD, Lambert P, Kashanchi F (2001). "Enhancement of the p300 HAT activity by HIV-1 Tat on chromatin DNA". Virology. 289 (2): 312–326. doi:10.1006/viro.2001.1129. PMID 11689053.
• Goto H, Yasui Y, Nigg EA, Inagaki M (2002). "Aurora-B phosphorylates Histone H3 at serine28 with regard to the mitotic chromosome condensation". Genes Cells. 7 (1): 11–17. doi:10.1046/j.1356-9597.2001.00498.x. PMID 11856369. S2CID 23717416.
• Ganesan S, Silver DP, Greenberg RA, Avni D, Drapkin R, Miron A, Mok SC, Randrianarison V, Brodie S, Salstrom J, Rasmussen TP, Klimke A, Marrese C, Marahrens Y, Deng CX, Feunteun J, Livingston DM (2002). "BRCA1 supports XIST RNA concentration on the inactive X chromosome". Cell. 111 (3): 393–405. doi:10.1016/S0092-8674(02)01052-8. PMID 12419249. S2CID 372211.
• Goo YH, Sohn YC, Kim DH, Kim SW, Kang MJ, Jung DJ, Kwak E, Barlev NA, Berger SL, Chow VT, Roeder RG, Azorsa DO, Meltzer PS, Suh PG, Song EJ, Lee KJ, Lee YC, Lee JW (2003). "Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins". Mol. Cell. Biol. 23 (1): 140–149. doi:10.1128/MCB.23.1.140-149.2003. PMC 140670. PMID 12482968.
• Preuss U, Landsberg G, Scheidtmann KH (2003). "Novel mitosis-specific phosphorylation of histone H3 at Thr11 mediated by Dlk/ZIP kinase". Nucleic Acids Res. 31 (3): 878–885. doi:10.1093/nar/gkg176. PMC 149197. PMID 12560483.
• Yoon HG, Chan DW, Huang ZQ, Li J, Fondell JD, Qin J, Wong J (2003). "Purification and functional characterization of the human N-CoR complex: the roles of HDAC3, TBL1 and TBLR1". EMBO J. 22 (6): 1336–1346. 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): 6550–6561. doi:10.1093/emboj/cdg631. PMC 291826. PMID 14657027.

External links

• Overview of all the structural information available in the PDB for UniProt: Q71DI3 (Histone H3.2) at the PDBe-KB.