HIST2H2AA3: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Histone H2A type 2-A''' is a [[protein]] that in humans is encoded by the ''HIST2H2AA3'' [[gene]].<ref name="pmid6326092">{{cite journal | vauthors = Marashi F, Prokopp K, Stein J, Stein G | title = Evidence for a human histone gene cluster containing H2B and H2A pseudogenes | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 81 | issue = 7 | pages = 1936–40 | date = April 1984 | pmid = 6326092 | pmc = 345411 | doi = 10.1073/pnas.81.7.1936 }}</ref><ref name="pmid8179821">{{cite journal | vauthors = Mannironi C, Orr A, Hatch C, Pilch D, Ivanova V, Bonner W | title = The relative expression of human histone H2A genes is similar in different types of proliferating cells | journal = DNA and Cell Biology | volume = 13 | issue = 2 | pages = 161–70 | date = February 1994 | pmid = 8179821 | pmc =  | doi = 10.1089/dna.1994.13.161 }}</ref><ref name="pmid15527963">{{cite journal | vauthors = Braastad CD, Hovhannisyan H, van Wijnen AJ, Stein JL, Stein GS | title = Functional characterization of a human histone gene cluster duplication | journal = Gene | volume = 342 | issue = 1 | pages = 35–40 | date = November 2004 | pmid = 15527963 | pmc = | doi = 10.1016/j.gene.2004.07.036 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: HIST2H2AA3 histone cluster 2, H2aa3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8337| access-date = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_HIST2H2AA3_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|2aro}}, {{PDB2|2cv5}}, {{PDB2|2f8n}}, {{PDB2|2fj7}}, {{PDB2|2hio}}, {{PDB2|2nzd}}
| Name = Histone cluster 2, H2aa3
| HGNCid = 4736
| Symbol = HIST2H2AA3
| AltSymbols =; H2A.2; H2A; H2A/O; H2A/q; H2AFO; H2a-615; HIST2H2AA; H2A/R
| OMIM = 142720
| ECnumber = 
| Homologene = 79484
| MGIid = 96097
| 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 = 8337
    | Hs_Ensembl = 
    | Hs_RefseqProtein = NP_003507
    | Hs_RefseqmRNA = NM_003516
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 
    | Hs_GenLoc_start = 
    | Hs_GenLoc_end = 
    | Hs_Uniprot = 
    | Mm_EntrezGene = 15267
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = NM_013549
    | Mm_RefseqProtein = NP_038577
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Histone cluster 2, H2aa3''', also known as '''HIST2H2AA3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HIST2H2AA3 histone cluster 2, H2aa3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8337| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
[[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 a histone cluster on [[chromosome 1]]. This gene is one of four histone genes in the cluster that are duplicated; this record represents the centromeric copy.<ref name="entrez">{{cite web | title = Entrez Gene: HIST2H2AA3 histone cluster 2, H2aa3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8337| access-date = }}</ref>
{{PBB_Summary
| section_title =
| summary_text = 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 a histone cluster on chromosome 1. This gene is one of four histone genes in the cluster that are duplicated; this record represents the centromeric copy.<ref name="entrez">{{cite web | title = Entrez Gene: HIST2H2AA3 histone cluster 2, H2aa3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8337| accessdate = }}</ref>
}}


==References==
== References ==
{{reflist|2}}
{{reflist}}
==Further reading==
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Allen BS, Stein JL, Stein GS, Ostrer H | title = Single-copy flanking sequences in human histone gene clusters map to chromosomes 1 and 6 | journal = Genomics | volume = 10 | issue = 2 | pages = 486–8 | date = June 1991 | pmid = 2071153 | doi = 10.1016/0888-7543(91)90337-E }}
| citations =
* {{cite journal | vauthors = Kaiser P, Mandl S, Schweiger M, Schneider R | title = Characterization of functionally independent domains in the human ubiquitin conjugating enzyme UbcH2 | journal = FEBS Letters | volume = 377 | issue = 2 | pages = 193–6 | date = December 1995 | pmid = 8543049 | doi = 10.1016/0014-5793(95)01323-7 }}
*{{cite journal | author=Allen BS, Stein JL, Stein GS, Ostrer H |title=Single-copy flanking sequences in human histone gene clusters map to chromosomes 1 and 6. |journal=Genomics |volume=10 |issue= 2 |pages= 486-8 |year= 1991 |pmid= 2071153 |doi= }}
* {{cite journal | vauthors = Wang ZF, Tisovec R, Debry RW, Frey MR, Matera AG, Marzluff WF | title = Characterization of the 55-kb mouse histone gene cluster on chromosome 3 | journal = Genome Research | volume = 6 | issue = 8 | pages = 702–14 | date = August 1996 | pmid = 8858345 | doi = 10.1101/gr.6.8.702 }}
*{{cite journal  | author=Marashi F, Prokopp K, Stein J, Stein G |title=Evidence for a human histone gene cluster containing H2B and H2A pseudogenes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=81 |issue= 7 |pages= 1936-40 |year= 1984 |pmid= 6326092 |doi=  }}
* {{cite journal | vauthors = Albig W, Doenecke D | title = The human histone gene cluster at the D6S105 locus | journal = Human Genetics | volume = 101 | issue = 3 | pages = 284–94 | date = December 1997 | pmid = 9439656 | doi = 10.1007/s004390050630 }}
*{{cite journal  | author=Mannironi C, Orr A, Hatch C, ''et al.'' |title=The relative expression of human histone H2A genes is similar in different types of proliferating cells. |journal=DNA Cell Biol. |volume=13 |issue= 2 |pages= 161-70 |year= 1994 |pmid= 8179821 |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 = Molecular and Cellular Biology | volume = 18 | issue = 5 | pages = 2535–44 | date = May 1998 | pmid = 9566873 | pmc = 110633 | doi = 10.1128/mcb.18.5.2535 }}
*{{cite journal | author=Kaiser P, Mandl S, Schweiger M, Schneider R |title=Characterization of functionally independent domains in the human ubiquitin conjugating enzyme UbcH2. |journal=FEBS Lett. |volume=377 |issue= 2 |pages= 193-6 |year= 1996 |pmid= 8543049 |doi= }}
* {{cite journal | vauthors = Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F | 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 | date = November 2000 | pmid = 11080476 | doi = 10.1006/viro.2000.0593 }}
*{{cite journal | author=Wang ZF, Tisovec R, Debry RW, ''et al.'' |title=Characterization of the 55-kb mouse histone gene cluster on chromosome 3. |journal=Genome Res. |volume=6 |issue= 8 |pages= 702-14 |year= 1997 |pmid= 8858345 |doi= }}
* {{cite journal | vauthors = Nemergut ME, Mizzen CA, Stukenberg T, Allis CD, Macara IG | title = Chromatin docking and exchange activity enhancement of RCC1 by histones H2A and H2B | journal = Science | volume = 292 | issue = 5521 | pages = 1540–3 | date = May 2001 | pmid = 11375490 | doi = 10.1126/science.292.5521.1540 }}
*{{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, Wang D, de la Fuente C, Wang L, Li H, Lee CG, Donnelly R, Wade JD, Lambert P, Kashanchi F | title = Enhancement of the p300 HAT activity by HIV-1 Tat on chromatin DNA | journal = Virology | volume = 289 | issue = 2 | pages = 312–26 | date = October 2001 | pmid = 11689053 | doi = 10.1006/viro.2001.1129 }}
*{{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 = 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 = November 2002 | pmid = 12408966 | doi = 10.1016/S0888-7543(02)96850-3 }}
*{{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 = 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 = The EMBO Journal | volume = 22 | issue = 24 | pages = 6550–61 | date = December 2003 | pmid = 14657027 | pmc = 291826 | doi = 10.1093/emboj/cdg631 }}
*{{cite journal | author=Venter JC, Adams MD, Myers EW, ''et al.'' |title=The sequence of the human genome. |journal=Science |volume=291 |issue= 5507 |pages= 1304-51 |year= 2001 |pmid= 11181995 |doi= 10.1126/science.1058040 }}
* {{cite journal | vauthors = Yusufzai TM, Tagami H, Nakatani Y, Felsenfeld G | title = CTCF tethers an insulator to subnuclear sites, suggesting shared insulator mechanisms across species | journal = Molecular Cell | volume = 13 | issue = 2 | pages = 291–8 | date = January 2004 | pmid = 14759373 | doi = 10.1016/S1097-2765(04)00029-2 }}
*{{cite journal  | author=Nemergut ME, Mizzen CA, Stukenberg T, ''et al.'' |title=Chromatin docking and exchange activity enhancement of RCC1 by histones H2A and H2B. |journal=Science |volume=292 |issue= 5521 |pages= 1540-3 |year= 2001 |pmid= 11375490 |doi= 10.1126/science.292.5521.1540 }}
* {{cite journal | vauthors = Zhang Y, Griffin K, Mondal N, Parvin JD | title = Phosphorylation of histone H2A inhibits transcription on chromatin templates | journal = The Journal of Biological Chemistry | volume = 279 | issue = 21 | pages = 21866–72 | date = May 2004 | pmid = 15010469 | doi = 10.1074/jbc.M400099200 }}
*{{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 = Aihara H, Nakagawa T, Yasui K, Ohta T, Hirose S, Dhomae N, Takio K, Kaneko M, Takeshima Y, Muramatsu M, Ito T | title = Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 during mitosis in the early Drosophila embryo | journal = Genes & Development | volume = 18 | issue = 8 | pages = 877–88 | date = April 2004 | pmid = 15078818 | pmc = 395847 | doi = 10.1101/gad.1184604 }}
*{{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 = Wang H, Wang L, Erdjument-Bromage H, Vidal M, Tempst P, Jones RS, Zhang Y | title = Role of histone H2A ubiquitination in Polycomb silencing | journal = Nature | volume = 431 | issue = 7010 | pages = 873–8 | date = October 2004 | pmid = 15386022 | doi = 10.1038/nature02985 }}
*{{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 | 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 | author=Yusufzai TM, Tagami H, Nakatani Y, Felsenfeld G |title=CTCF tethers an insulator to subnuclear sites, suggesting shared insulator mechanisms across species. |journal=Mol. Cell |volume=13 |issue= 2 |pages= 291-8 |year= 2004 |pmid= 14759373 |doi= }}
*{{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, 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, 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  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |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 }}
*{{cite journal  | author=Braastad CD, Hovhannisyan H, van Wijnen AJ, ''et al.'' |title=Functional characterization of a human histone gene cluster duplication. |journal=Gene |volume=342 |issue= 1 |pages= 35-40 |year= 2005 |pmid= 15527963 |doi= 10.1016/j.gene.2004.07.036 }}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=8337}}


{{protein-stub}}
{{protein-stub}}
{{WikiDoc Sources}}

Latest revision as of 02:47, 11 June 2018

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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-A is a protein that in humans is encoded by the HIST2H2AA3 gene.[1][2][3][4]

Function

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 a histone cluster on chromosome 1. This gene is one of four histone genes in the cluster that are duplicated; this record represents the centromeric copy.[4]

References

  1. ↑ Marashi F, Prokopp K, Stein J, Stein G (April 1984). "Evidence for a human histone gene cluster containing H2B and H2A pseudogenes". Proceedings of the National Academy of Sciences of the United States of America. 81 (7): 1936–40. doi:10.1073/pnas.81.7.1936. PMC 345411. PMID 6326092.
  2. ↑ Mannironi C, Orr A, Hatch C, Pilch D, Ivanova V, Bonner W (February 1994). "The relative expression of human histone H2A genes is similar in different types of proliferating cells". DNA and Cell Biology. 13 (2): 161–70. doi:10.1089/dna.1994.13.161. PMID 8179821.
  3. ↑ Braastad CD, Hovhannisyan H, van Wijnen AJ, Stein JL, Stein GS (November 2004). "Functional characterization of a human histone gene cluster duplication". Gene. 342 (1): 35–40. doi:10.1016/j.gene.2004.07.036. PMID 15527963.
  4. ↑ 4.0 4.1 "Entrez Gene: HIST2H2AA3 histone cluster 2, H2aa3".

Further reading


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