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{{Underlinked|date=March 2014}}
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'''Histone H2A type 2-B''' is a [[protein]] that in humans is encoded by the ''HIST2H2AB'' [[gene]].<ref name="pmid12408966">{{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 | pmc =  | doi =10.1016/S0888-7543(02)96850-3 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: HIST2H2AB histone cluster 2, H2ab| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=317772| accessdate = }}</ref>
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| image = PBB_Protein_HIST2H2AB_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1aoi.
| PDB = {{PDB2|1aoi}}, {{PDB2|1eqz}}, {{PDB2|1hio}}, {{PDB2|1hq3}}, {{PDB2|1kx3}}, {{PDB2|1kx4}}, {{PDB2|1kx5}}, {{PDB2|1m18}}, {{PDB2|1m19}}, {{PDB2|1m1a}}, {{PDB2|1p34}}, {{PDB2|1p3a}}, {{PDB2|1p3b}}, {{PDB2|1p3f}}, {{PDB2|1p3g}}, {{PDB2|1p3i}}, {{PDB2|1p3k}}, {{PDB2|1p3l}}, {{PDB2|1p3m}}, {{PDB2|1p3o}}, {{PDB2|1p3p}}, {{PDB2|1s32}}, {{PDB2|1tzy}}, {{PDB2|1zbb}}, {{PDB2|1zla}}, {{PDB2|2aro}}, {{PDB2|2cv5}}, {{PDB2|2f8n}}, {{PDB2|2fj7}}, {{PDB2|2hio}}, {{PDB2|2nzd}}
| Name = Histone cluster 2, H2ab
| HGNCid = 20508
| Symbol = HIST2H2AB
| AltSymbols =;
| OMIM =
| ECnumber =
| Homologene = 82162
| MGIid = 2448314
  | GeneAtlas_image1 = PBB_GE_HIST2H2AB_gnf1h07838_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}}
| Component = {{GNF_GO|id=GO:0000786 |text = nucleosome}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005694 |text = chromosome}}
| Process = {{GNF_GO|id=GO:0006334 |text = nucleosome assembly}} {{GNF_GO|id=GO:0007001 |text = chromosome organization and biogenesis (sensu Eukaryota)}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 317772
    | Hs_Ensembl = ENSG00000184270
    | Hs_RefseqProtein = NP_778235
    | Hs_RefseqmRNA = NM_175065
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 148125698
    | Hs_GenLoc_end = 148126090
    | Hs_Uniprot = Q8IUE6
    | Mm_EntrezGene = 621893
    | Mm_Ensembl = ENSMUSG00000063689
    | Mm_RefseqmRNA = XM_886305
    | Mm_RefseqProtein = XP_891398
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 3
    | Mm_GenLoc_start = 96305321
    | Mm_GenLoc_end = 96305713
    | Mm_Uniprot = Q64522
  }}
}}
'''Histone cluster 2, H2ab''', also known as '''HIST2H2AB''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HIST2H2AB histone cluster 2, H2ab| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=317772| accessdate = }}</ref>


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| section_title =  
| section_title =  
| summary_text = 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 contain a palindromic termination element.<ref name="entrez">{{cite web | title = Entrez Gene: HIST2H2AB histone cluster 2, H2ab| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=317772| accessdate = }}</ref>
| summary_text = 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 contain a palindromic termination element.<ref name="entrez" />
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=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=  }}
*{{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, de la Fuente C, Fu P, ''et al.'' |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 }}
*{{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-format=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 }}
*{{cite journal  | author=Deng L, Wang D, de la Fuente C, ''et al.'' |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 }}
*{{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-format=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 }}
*{{cite journal  | author=Chen A, Kleiman FE, Manley JL, ''et al.'' |title=Autoubiquitination of the BRCA1*BARD1 RING ubiquitin ligase. |journal=J. Biol. Chem. |volume=277 |issue= 24 |pages= 22085-92 |year= 2002 |pmid= 11927591 |doi= 10.1074/jbc.M201252200 }}
*{{cite journal  | author=Chen A |title=Autoubiquitination of the BRCA1*BARD1 RING ubiquitin ligase |journal=J. Biol. Chem. |volume=277 |issue= 24 |pages= 22085–92 |year= 2002 |pmid= 11927591 |doi= 10.1074/jbc.M201252200  |name-list-format=vanc| author2=Kleiman FE  | author3=Manley JL  | display-authors=3  | last4=Ouchi  | first4=T  | last5=Pan  | first5=ZQ }}
*{{cite journal | author=Marzluff WF, Gongidi P, Woods KR, ''et al.'' |title=The human and mouse replication-dependent histone genes. |journal=Genomics |volume=80 |issue= 5 |pages= 487-98 |year= 2003 |pmid= 12408966 |doi= }}
*{{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  | author=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 }}
*{{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 }}
*{{cite journal  | author=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 }}
*{{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-format=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=Aihara H, Nakagawa T, Yasui K, ''et al.'' |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 }}
*{{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-format=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 }}
*{{cite journal  | author=Wang H, Wang L, Erdjument-Bromage H, ''et al.'' |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 }}
*{{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=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  |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 }}
*{{cite journal  | author=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 }}
*{{cite journal  | author=Bergink S |title=DNA damage triggers nucleotide excision repair-dependent monoubiquitylation of histone H2A |journal=Genes Dev. |volume=20 |issue= 10 |pages= 1343–52 |year= 2006 |pmid= 16702407 |doi= 10.1101/gad.373706 | pmc=1472908  |name-list-format=vanc| author2=Salomons FA  | author3=Hoogstraten D  | display-authors=3  | last4=Groothuis  | first4=TA  | last5=De Waard  | first5=H  | last6=Wu  | first6=J  | last7=Yuan  | first7=L  | last8=Citterio  | first8=E  | last9=Houtsmuller  | first9=AB }}
*{{cite journal  | author=Bergink S, Salomons FA, Hoogstraten D, ''et al.'' |title=DNA damage triggers nucleotide excision repair-dependent monoubiquitylation of histone H2A. |journal=Genes Dev. |volume=20 |issue= 10 |pages= 1343-52 |year= 2006 |pmid= 16702407 |doi= 10.1101/gad.373706 }}
*{{cite journal  | author=Gregory SG |title=The DNA sequence and biological annotation of human chromosome 1 |journal=Nature |volume=441 |issue= 7091 |pages= 315–21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 |name-list-format=vanc| author2=Barlow KF  | author3=McLay KE  | display-authors=3  | last4=Kaul  | first4=R.  | last5=Swarbreck  | first5=D.  | last6=Dunham  | first6=A.  | last7=Scott  | first7=C. E.  | last8=Howe  | first8=K. L.  | last9=Woodfine  | first9=K. }}
*{{cite journal  | author=Gregory SG, Barlow KF, McLay KE, ''et al.'' |title=The DNA sequence and biological annotation of human chromosome 1. |journal=Nature |volume=441 |issue= 7091 |pages= 315-21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=317772}}
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Latest revision as of 13:42, 31 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Histone H2A type 2-B is a protein that in humans is encoded by the HIST2H2AB gene.[1][2]

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 contain a palindromic termination element.[2]

References

  1. ↑ 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.
  2. ↑ 2.0 2.1 "Entrez Gene: HIST2H2AB histone cluster 2, H2ab".

Further reading



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