HIST1H2AK

H2AC15
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4QYL, 5KGF
Identifiers
Aliases	H2AC15, H2A/d, H2AFD, histone cluster 1, H2ak, histone cluster 1 H2A family member k, HIST1H2AK, H2A clustered histone 15, H2AC11, H2AC14, H2AC17, H2AC16, H2AC13, H2A.1
External IDs	OMIM: 602788; MGI: 2448287; HomoloGene: 134305; GeneCards: H2AC15; OMA:H2AC15 - orthologs
Gene location (Human) Chr. Chromosome 6 (human) Band 6p22.1 Start 27,837,880 bp End 27,838,375 bp
Gene location (Mouse) Chr. Chromosome 13 (mouse) Band 13|13 A3.1 Start 23,865,450 bp End 23,867,931 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in testicle trachea vastus lateralis muscle thalamus spinal ganglia epithelium of bronchus paraflocculus of cerebellum middle frontal gyrus frontal pole bone marrow cells Top expressed in granulocyte bone marrow uterus embryo yolk sac secondary oocyte primary oocyte zygote lens quadriceps femoris muscle More reference expression data BioGPS n/a
Gene ontology Molecular function enzyme binding DNA binding protein binding protein heterodimerization activity Cellular component nucleosome extracellular exosome nucleus chromosome Biological process chromatin organization biological process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 8330 319164 Ensembl ENSG00000275221 ENSMUSG00000069270 UniProt P0C0S8 C0HKE2 B2RVF0 C0HKE1 C0HKE3 C0HKE4 C0HKE5 C0HKE6 C0HKE7 C0HKE8 C0HKE9 RefSeq (mRNA) NM_003510 NM_178189 RefSeq (protein) NP_066408 NP_003505 NP_835496 NP_835495 NP_835494 NP_835491 NP_835489 NP_783591 NP_835493 NP_835496 NP_835489 NP_835495 NP_835494 NP_835491 NP_835492 NP_783591 NP_001171015 NP_835489 NP_001171015 NP_835496 NP_835491 NP_835493 NP_835494 NP_835495 NP_835492 NP_783591 NP_835494 NP_835489 NP_835495 NP_835491 NP_835492 NP_783591 NP_001171015 NP_835493 NP_835496 NP_835495 NP_835489 NP_835494 NP_835491 NP_835492 NP_783591 NP_001171015 NP_835493 NP_835496 NP_835492 NP_835491 NP_835489 NP_835495 NP_835494 NP_783591 NP_001171015 NP_835493 NP_835496 NP_835491 NP_835489 NP_835495 NP_835494 NP_835492 NP_783591 NP_001171015 NP_835493 NP_835496 NP_783591 NP_835489 NP_835495 NP_835494 NP_835491 NP_835492 NP_001171015 NP_835493 NP_835496 NP_783591 NP_835489 NP_835495 NP_835494 NP_835491 NP_835492 NP_001171015 NP_835493 NP_835496 Location (UCSC) Chr 6: 27.84 – 27.84 Mb Chr 13: 23.87 – 23.87 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Histone H2A type 1 is a protein that in humans is encoded by the HIST1H2AK 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 H2A family. Transcripts from this gene lack polyA tails but instead contain a palindromic termination element. This gene is found in the small histone gene cluster on chromosome 6p22-p21.3.

Further reading

• 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.
• Albig W, Trappe R, Kardalinou E, et al. (1999). "The human H2A and H2B histone gene complement". Biol. Chem. 380 (1): 7–18. doi:10.1515/BC.1999.002. PMID 10064132. S2CID 12807248.
• 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.
• 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.
• 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.
• Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6". Nature. 425 (6960): 805–11. Bibcode:2003Natur.425..805M. doi:10.1038/nature02055. PMID 14574404.
• 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.
• Zhang Y, Griffin K, Mondal N, Parvin JD (2004). "Phosphorylation of histone H2A inhibits transcription on chromatin templates". J. Biol. Chem. 279 (21): 21866–72. doi:10.1074/jbc.M400099200. PMID 15010469.
• Aihara H, Nakagawa T, Yasui K, et al. (2004). "Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 during mitosis in the early Drosophila embryo". Genes Dev. 18 (8): 877–88. doi:10.1101/gad.1184604. PMC 395847. PMID 15078818.
• Wang H, Wang L, Erdjument-Bromage H, et al. (2004). "Role of histone H2A ubiquitination in Polycomb silencing". Nature. 431 (7010): 873–8. Bibcode:2004Natur.431..873W. doi:10.1038/nature02985. PMID 15386022. S2CID 4344378.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID 15635413. S2CID 4344740.
• Hagiwara T, Hidaka Y, Yamada M (2005). "Deimination of histone H2A and H4 at arginine 3 in HL-60 granulocytes". Biochemistry. 44 (15): 5827–34. doi:10.1021/bi047505c. PMID 15823041.
• Bonenfant D, Coulot M, Towbin H, et al. (2006). "Characterization of histone H2A and H2B variants and their post-translational modifications by mass spectrometry". Mol. Cell. Proteomics. 5 (3): 541–52. doi:10.1074/mcp.M500288-MCP200. PMID 16319397.
• Cao R, Tsukada Y, Zhang Y (2006). "Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing". Mol. Cell. 20 (6): 845–54. doi:10.1016/j.molcel.2005.12.002. PMID 16359901.
• Boyne MT, Pesavento JJ, Mizzen CA, Kelleher NL (2006). "Precise characterization of human histones in the H2A gene family by top down mass spectrometry". J. Proteome Res. 5 (2): 248–53. doi:10.1021/pr050269n. PMID 16457589.
• Bergink S, Salomons FA, Hoogstraten D, et al. (2006). "DNA damage triggers nucleotide excision repair-dependent monoubiquitylation of histone H2A". Genes Dev. 20 (10): 1343–52. doi:10.1101/gad.373706. PMC 1472908. PMID 16702407.