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{{Infobox_gene}}
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'''Histone H2A type 1-B/E''' is a [[protein]] that in humans is encoded by the ''HIST1H2AB'' [[gene]].<ref name="pmid9439656">{{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 |date=Feb 1998 | pmid = 9439656 | pmc =  | doi =10.1007/s004390050630  }}</ref><ref name="pmid9119399">{{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 | pmc = | doi = 10.1006/geno.1996.4592 }}</ref><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: HIST1H2AB histone cluster 1, H2ab| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8335| accessdate = }}</ref>
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{{GNF_Protein_box
| image = PBB_Protein_HIST1H2AB_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 1, H2ab
| HGNCid = 4734
| Symbol = HIST1H2AB
| AltSymbols =; H2A/m; H2AFM
| OMIM = 602795
| ECnumber =
| Homologene = 69326
| MGIid = 2448287
  | 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 = 8335
    | Hs_Ensembl =
    | Hs_RefseqProtein = NP_003504
    | Hs_RefseqmRNA = NM_003513
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr =
    | Hs_GenLoc_start =
    | Hs_GenLoc_end =
    | Hs_Uniprot =   
    | Mm_EntrezGene = 319164
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = NM_178189
    | Mm_RefseqProtein = NP_835496
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot =   
  }}
}}
'''Histone cluster 1, H2ab''', also known as '''HIST1H2AB''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HIST1H2AB histone cluster 1, H2ab| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8335| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = 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 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.<ref name="entrez">{{cite web | title = Entrez Gene: HIST1H2AB histone cluster 1, H2ab| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8335| accessdate = }}</ref>
| summary_text = 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 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.<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=Zhong R, Roeder RG, Heintz N |title=The primary structure and expression of four cloned human histone genes. |journal=Nucleic Acids Res. |volume=11 |issue= 21 |pages= 7409-25 |year= 1984 |pmid= 6647026 |doi=  }}
*{{cite journal  |vauthors=Zhong R, Roeder RG, Heintz N |title=The primary structure and expression of four cloned human histone genes. |journal=Nucleic Acids Res. |volume=11 |issue= 21 |pages= 7409–25 |year= 1984 |pmid= 6647026 |doi=  10.1093/nar/11.21.7409| pmc=326492 }}
*{{cite journal  | author=Albig W, Kioschis P, Poustka A, ''et al.'' |title=Human histone gene organization: nonregular arrangement within a large cluster. |journal=Genomics |volume=40 |issue= 2 |pages= 314-22 |year= 1997 |pmid= 9119399 |doi= 10.1006/geno.1996.4592 }}
*{{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=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=  }}
*{{cite journal   |vauthors=Deng L, de la Fuente C, Fu P, etal |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=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=Deng L, Wang D, de la Fuente C, etal |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, 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   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |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 }}
*{{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  |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=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=Citterio E, Papait R, Nicassio F, etal |title=Np95 is a histone-binding protein endowed with ubiquitin ligase activity. |journal=Mol. Cell. Biol. |volume=24 |issue= 6 |pages= 2526–35 |year= 2004 |pmid= 14993289 |doi= 10.1128/MCB.24.6.2526-2535.2004| pmc=355858 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |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 }}
*{{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=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=Aihara H, Nakagawa T, Yasui K, etal |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 }}
*{{cite journal | author=Citterio E, Papait R, Nicassio F, ''et al.'' |title=Np95 is a histone-binding protein endowed with ubiquitin ligase activity. |journal=Mol. Cell. Biol. |volume=24 |issue= 6 |pages= 2526-35 |year= 2004 |pmid= 14993289 |doi=  }}
*{{cite journal   |vauthors=Wang H, Wang L, Erdjument-Bromage H, etal |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  | 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   |vauthors=Andersen JS, Lam YW, Leung AK, etal |title=Nucleolar proteome dynamics. |journal=Nature |volume=433 |issue= 7021 |pages= 77–83 |year= 2005 |pmid= 15635413 |doi= 10.1038/nature03207 }}
*{{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  |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=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=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=Andersen JS, Lam YW, Leung AK, ''et al.'' |title=Nucleolar proteome dynamics. |journal=Nature |volume=433 |issue= 7021 |pages= 77-83 |year= 2005 |pmid= 15635413 |doi= 10.1038/nature03207 }}
*{{cite journal   |vauthors=Bergink S, Salomons FA, Hoogstraten D, etal |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 }}
*{{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  | 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, 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 }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=8335}}
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Latest revision as of 13:38, 31 August 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

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

Histone H2A type 1-B/E is a protein that in humans is encoded by the HIST1H2AB gene.[1][2][3][4]

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 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.[4]

References

  1. Albig W, Doenecke D (Feb 1998). "The human histone gene cluster at the D6S105 locus". Hum Genet. 101 (3): 284–94. doi:10.1007/s004390050630. PMID 9439656.
  2. Albig W, Kioschis P, Poustka A, Meergans K, Doenecke D (Apr 1997). "Human histone gene organization: nonregular arrangement within a large cluster". Genomics. 40 (2): 314–22. doi:10.1006/geno.1996.4592. PMID 9119399.
  3. 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.
  4. 4.0 4.1 "Entrez Gene: HIST1H2AB histone cluster 1, H2ab".

Further reading