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HIST1H2AE

{{Short description|Protein-coding gene in the species Homo sapiens}}

{{Infobox_gene}}

Histone H2A type 1-B/E is a protein that in humans is encoded by the HIST1H2AE gene.{{cite journal |vauthors=Albig W, Kioschis P, Poustka A, Meergans K, Doenecke D | title = Human histone gene organization: nonregular arrangement within a large cluster | journal = Genomics | volume = 40 | issue = 2 | pages = 314–22 |date=Apr 1997 | pmid = 9119399 | doi = 10.1006/geno.1996.4592 }}{{cite journal |vauthors=Albig W, Kardalinou E, Drabent B, Zimmer A, Doenecke D | title = Isolation and characterization of two human H1 histone genes within clusters of core histone genes | journal = Genomics | volume = 10 | issue = 4 | pages = 940–8 |date=Nov 1991 | pmid = 1916825 | doi =10.1016/0888-7543(91)90183-F }}{{cite journal |vauthors=Marzluff WF, Gongidi P, Woods KR, Jin J, Maltais LJ | title = The human and mouse replication-dependent histone genes | journal = Genomics | volume = 80 | issue = 5 | pages = 487–98 |date=Oct 2002 | pmid = 12408966 | doi =10.1016/S0888-7543(02)96850-3 }}{{cite web | title = Entrez Gene: HIST1H2AE histone cluster 1, H2ae| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3012}}

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone 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 H2A 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.

References

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Further reading

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  • {{cite journal | author=Rodriguez P |title=Functional characterization of human nucleosome assembly protein-2 (NAP1L4) suggests a role as a histone chaperone |journal=Genomics |volume=44 |issue= 3 |pages= 253–65 |year= 1997 |pmid= 9325046 |doi= 10.1006/geno.1997.4868 |name-list-style=vanc| author2=Munroe D | author3=Prawitt D | display-authors=3 | last4=Chu | first4=LL | last5=Bric | first5=E | last6=Kim | first6=J | last7=Reid | first7=LH | last8=Davies | first8=C | last9=Nakagama | first9=H }}
  • {{cite journal |vauthors=Albig W, Doenecke D |title=The human histone gene cluster at the D6S105 locus |journal=Hum. Genet. |volume=101 |issue= 3 |pages= 284–94 |year= 1998 |pmid= 9439656 |doi=10.1007/s004390050630 |s2cid=38539096 }}
  • {{cite journal |vauthors=El Kharroubi A, Piras G, Zensen R, Martin MA |title=Transcriptional Activation of the Integrated Chromatin-Associated Human Immunodeficiency Virus Type 1 Promoter |journal=Mol. Cell. Biol. |volume=18 |issue= 5 |pages= 2535–44 |year= 1998 |pmid= 9566873 |doi= 10.1128/mcb.18.5.2535| pmc=110633 }}
  • {{cite journal | author=Deng L |title=Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones |journal=Virology |volume=277 |issue= 2 |pages= 278–95 |year= 2001 |pmid= 11080476 |doi= 10.1006/viro.2000.0593 |name-list-style=vanc| author2=de la Fuente C | author3=Fu P | display-authors=3 | last4=Wang | first4=L | last5=Donnelly | first5=R | last6=Wade | first6=JD | last7=Lambert | first7=P | last8=Li | first8=H | last9=Lee | first9=CG | doi-access=free }}
  • {{cite journal | author=Deng L |title=Enhancement of the p300 HAT activity by HIV-1 Tat on chromatin DNA |journal=Virology |volume=289 |issue= 2 |pages= 312–26 |year= 2001 |pmid= 11689053 |doi= 10.1006/viro.2001.1129 |name-list-style=vanc| author2=Wang D | author3=de la Fuente C | display-authors=3 | last4=Wang | first4=L | last5=Li | first5=H | last6=Lee | first6=CG | last7=Donnelly | first7=R | last8=Wade | first8=JD | last9=Lambert | first9=P | doi-access=free }}
  • {{cite journal | author=Galasinski SC |title=Global regulation of post-translational modifications on core histones |journal=J. Biol. Chem. |volume=277 |issue= 4 |pages= 2579–88 |year= 2002 |pmid= 11709551 |doi= 10.1074/jbc.M107894200 |name-list-style=vanc| author2=Louie DF | author3=Gloor KK | display-authors=3 | last4=Resing | first4=KA | last5=Ahn | first5=NG |doi-access=free }}
  • {{cite journal | author=Strausberg RL |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |name-list-style=vanc| author2=Feingold EA | author3=Grouse LH | display-authors=3 | last4=Derge | first4=JG | last5=Klausner | first5=RD | last6=Collins | first6=FS | last7=Wagner | first7=L | last8=Shenmen | first8=CM | last9=Schuler | first9=GD |bibcode=2002PNAS...9916899M |doi-access=free }}
  • {{cite journal | author=Mungall AJ |title=The DNA sequence and analysis of human chromosome 6 |journal=Nature |volume=425 |issue= 6960 |pages= 805–11 |year= 2003 |pmid= 14574404 |doi= 10.1038/nature02055 |name-list-style=vanc| author2=Palmer SA | author3=Sims SK | display-authors=3 | last4=Edwards | first4=C. A. | last5=Ashurst | first5=J. L. | last6=Wilming | first6=L. | last7=Jones | first7=M. C. | last8=Horton | first8=R. | last9=Hunt | first9=S. E. | doi-access=free }}
  • {{cite journal |vauthors=Lusic M, Marcello A, Cereseto A, Giacca M |title=Regulation of HIV-1 gene expression by histone acetylation and factor recruitment at the LTR promoter |journal=EMBO J. |volume=22 |issue= 24 |pages= 6550–61 |year= 2004 |pmid= 14657027 |doi= 10.1093/emboj/cdg631 | pmc=291826 }}
  • {{cite journal |vauthors=Zhang Y, Griffin K, Mondal N, Parvin JD |title=Phosphorylation of histone H2A inhibits transcription on chromatin templates |journal=J. Biol. Chem. |volume=279 |issue= 21 |pages= 21866–72 |year= 2004 |pmid= 15010469 |doi= 10.1074/jbc.M400099200 |doi-access= free }}
  • {{cite journal | author=Aihara H |title=Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 during mitosis in the early Drosophila embryo |journal=Genes Dev. |volume=18 |issue= 8 |pages= 877–88 |year= 2004 |pmid= 15078818 |doi= 10.1101/gad.1184604 | pmc=395847 |name-list-style=vanc| author2=Nakagawa T | author3=Yasui K | display-authors=3 | last4=Ohta | first4=T | last5=Hirose | first5=S | last6=Dhomae | first6=N | last7=Takio | first7=K | last8=Kaneko | first8=M | last9=Takeshima | first9=Y }}
  • {{cite journal | author=Wang H |title=Role of histone H2A ubiquitination in Polycomb silencing |journal=Nature |volume=431 |issue= 7010 |pages= 873–8 |year= 2004 |pmid= 15386022 |doi= 10.1038/nature02985 |name-list-style=vanc| author2=Wang L | author3=Erdjument-Bromage H | display-authors=3 | last4=Vidal | first4=Miguel | last5=Tempst | first5=Paul | last6=Jones | first6=Richard S. | last7=Zhang | first7=Yi |bibcode=2004Natur.431..873W |s2cid=4344378 }}
  • {{cite journal | author=Gerhard DS |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 |name-list-style=vanc| author2=Wagner L | author3=Feingold EA | display-authors=3 | last4=Shenmen | first4=CM | last5=Grouse | first5=LH | last6=Schuler | first6=G | last7=Klein | first7=SL | last8=Old | first8=S | last9=Rasooly | first9=R }}
  • {{cite journal |vauthors=Hagiwara T, Hidaka Y, Yamada M |title=Deimination of histone H2A and H4 at arginine 3 in HL-60 granulocytes |journal=Biochemistry |volume=44 |issue= 15 |pages= 5827–34 |year= 2005 |pmid= 15823041 |doi= 10.1021/bi047505c }}
  • {{cite journal | author=Bonenfant D |title=Characterization of histone H2A and H2B variants and their post-translational modifications by mass spectrometry |journal=Mol. Cell. Proteomics |volume=5 |issue= 3 |pages= 541–52 |year= 2006 |pmid= 16319397 |doi= 10.1074/mcp.M500288-MCP200 |name-list-style=vanc| author2=Coulot M | author3=Towbin H | display-authors=3 | last4=Schindler | first4=P | last5=Van Oostrum | first5=J |doi-access=free }}
  • {{cite journal |vauthors=Cao R, Tsukada Y, Zhang Y |title=Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing |journal=Mol. Cell |volume=20 |issue= 6 |pages= 845–54 |year= 2006 |pmid= 16359901 |doi= 10.1016/j.molcel.2005.12.002 |doi-access= free }}
  • {{cite journal |vauthors=Boyne MT, Pesavento JJ, Mizzen CA, Kelleher NL |title=Precise characterization of human histones in the H2A gene family by top down mass spectrometry |journal=J. Proteome Res. |volume=5 |issue= 2 |pages= 248–53 |year= 2006 |pmid= 16457589 |doi= 10.1021/pr050269n }}

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