HIST1H2AH

H2AC12
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2F8N
Identifiers
Aliases	H2AC12 , H2A/S, H2AFALii, H2AH, dJ86C11.1, histone cluster 1, H2ah, histone cluster 1 H2A family member h, HIST1H2AH, H2A clustered histone 12
External IDs	OMIM: 615013 MGI: 2448295 HomoloGene: 119667 GeneCards: H2AC12
Gene location (Human) Chr. Chromosome 6 (human) [1] Band 6p22.1 Start 27,147,106 bp [1] End 27,147,562 bp [1]
Gene location (Mouse) Chr. Chromosome 13 (mouse) [2] Band 13|13 A3.1 Start 22,219,334 bp [2] End 22,219,738 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in bone marrow cells Achilles tendon corpus callosum thymus sural nerve ganglionic eminence blood placenta lymph node urinary bladder Top expressed in uterus yolk sac spermatid bone marrow morula spermatocyte thymus mesencephalon spleen proximal tubule More reference expression data BioGPS n/a
Gene ontology Molecular function protein heterodimerization activity DNA binding molecular function Cellular component nucleosome extracellular exosome nucleus chromosome Biological process chromatin organization biological process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 85235 319168 Ensembl ENSG00000274997 ENSMUSG00000069302 UniProt Q96KK5 Q8CGP6 RefSeq (mRNA) NM_080596 NM_175659 RefSeq (protein) NP_542163 NP_783590 Location (UCSC) Chr 6: 27.15 – 27.15 Mb Chr 13: 22.22 – 22.22 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Histone H2A type 1-H is a protein that in humans is encoded by the HIST1H2AH gene. ^{[5] [6]}

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 tails but instead contain a palindromic termination element. This gene is found in the histone microcluster on chromosome 6p21.33. ^[6]

References

1. GRCh38: Ensembl release 89: ENSG00000274997 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000069302 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Marzluff WF, Gongidi P, Woods KR, Jin J, Maltais LJ (Oct 2002). "The human and mouse replication-dependent histone genes". Genomics. 80 (5): 487–98. doi:10.1016/S0888-7543(02)96850-3. PMID   12408966.
6. "Entrez Gene: HIST1H2AH histone cluster 1, H2ah".

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.
• 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.
• 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.
• 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.
• 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.
• Kimura H, Takizawa N, Allemand E, et al. (2006). "A novel histone exchange factor, protein phosphatase 2Cγ, mediates the exchange and dephosphorylation of H2A–H2B". J. Cell Biol. 175 (3): 389–400. doi:10.1083/jcb.200608001. PMC   2064517 . PMID   17074886.