HIST2H2AC: Difference between revisions

Jump to navigation Jump to search
VisualWikitext
m (Robot: Automated text replacement (-{{WikiDoc Cardiology Network Infobox}} +, -<references /> +{{reflist|2}}, -{{reflist}} +{{reflist|2}}))
 
imported>Jmertel23
m (added wikilinks and removed "underlinked" tag)
 
(One intermediate revision by one other user not shown)
Line 1: Line 1:
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Histone H2A type 2-C''' is a [[protein]] that in humans is encoded by the ''HIST2H2AC'' [[gene]].<ref name="pmid1469070">{{cite journal |vauthors=Collart D, Romain PL, Huebner K, Pockwinse S, Pilapil S, Cannizzaro LA, Lian JB, Croce CM, Stein JL, Stein GS | title = A human histone H2B.1 variant gene, located on chromosome 1, utilizes alternative 3' end processing | journal = J Cell Biochem | volume = 50 | issue = 4 | pages = 374–85 |date=Jan 1993 | pmid = 1469070 | pmc =  | doi = 10.1002/jcb.240500406 }}</ref><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="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"/>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
 
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_HIST2H2AC_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, H2ac
| HGNCid = 4738
| Symbol = HIST2H2AC
| AltSymbols =; H2A; H2A/q; H2A-GL101; H2AFQ; MGC74460
| OMIM = 602797
| ECnumber =
| Homologene = 68327
| MGIid = 2448316
  | GeneAtlas_image1 = PBB_GE_HIST2H2AC_218280_x_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 = 8338
    | Hs_Ensembl = ENSG00000184260
    | Hs_RefseqProtein = NP_003508
    | Hs_RefseqmRNA = NM_003517
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 148125149
    | Hs_GenLoc_end = 148125585
    | Hs_Uniprot = Q16777
    | Mm_EntrezGene = 319176
    | Mm_Ensembl = ENSMUSG00000068855
    | Mm_RefseqmRNA = NM_175662
    | Mm_RefseqProtein = NP_783593
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 3
    | Mm_GenLoc_start = 96305860
    | Mm_GenLoc_end = 96306249
    | Mm_Uniprot = Q149V4
  }}
}}
'''Histone cluster 2, H2ac''', also known as '''HIST2H2AC''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HIST2H2AC histone cluster 2, H2ac| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8338| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{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. 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.<ref name="entrez">{{cite web | title = Entrez Gene: HIST2H2AC histone cluster 2, H2ac| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8338| accessdate = }}</ref>
| 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.<ref name="entrez">{{cite web | title = Entrez Gene: HIST2H2AC histone cluster 2, H2ac| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8338| accessdate = }}</ref>
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Collart D, Romain PL, Huebner K, ''et al.'' |title=A human histone H2B.1 variant gene, located on chromosome 1, utilizes alternative 3' end processing. |journal=J. Cell. Biochem. |volume=50 |issue= 4 |pages= 374-85 |year= 1993 |pmid= 1469070 |doi= 10.1002/jcb.240500406 }}
*{{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=Kimura A, Horikoshi M |title=Tip60 acetylates six lysines of a specific class in core histones in vitro |journal=Genes Cells |volume=3 |issue= 12 |pages= 789–800 |year= 1999 |pmid= 10096020 |doi=10.1046/j.1365-2443.1998.00229.x }}
*{{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, 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=Kimura A, Horikoshi M |title=Tip60 acetylates six lysines of a specific class in core histones in vitro. |journal=Genes Cells |volume=3 |issue= 12 |pages= 789-800 |year= 1999 |pmid= 10096020 |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=Chen A, Kleiman FE, Manley JL, etal |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=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=Lahn BT, Tang ZL, Zhou J, etal |title=Previously uncharacterized histone acetyltransferases implicated in mammalian spermatogenesis |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 13 |pages= 8707–12 |year= 2002 |pmid= 12072557 |doi= 10.1073/pnas.082248899  | pmc=124363 }}
*{{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   |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=Lahn BT, Tang ZL, Zhou J, ''et al.'' |title=Previously uncharacterized histone acetyltransferases implicated in mammalian spermatogenesis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 13 |pages= 8707-12 |year= 2002 |pmid= 12072557 |doi= 10.1073/pnas.082248899 }}
*{{cite journal   |vauthors=Yoon HG, Chan DW, Huang ZQ, etal |title=Purification and functional characterization of the human N-CoR complex: the roles of HDAC3, TBL1 and TBLR1 |journal=EMBO J. |volume=22 |issue= 6 |pages= 1336–46 |year= 2003 |pmid= 12628926 |doi= 10.1093/emboj/cdg120 | pmc=151047 }}
*{{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=Fujita K, Shimazaki N, Ohta Y, etal |title=Terminal deoxynucleotidyltransferase forms a ternary complex with a novel chromatin remodeling protein with 82 kDa and core histone |journal=Genes Cells |volume=8 |issue= 6 |pages= 559–71 |year= 2004 |pmid= 12786946 |doi=10.1046/j.1365-2443.2003.00656.x }}
*{{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=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=Yoon HG, Chan DW, Huang ZQ, ''et al.'' |title=Purification and functional characterization of the human N-CoR complex: the roles of HDAC3, TBL1 and TBLR1. |journal=EMBO J. |volume=22 |issue= 6 |pages= 1336-46 |year= 2003 |pmid= 12628926 |doi= 10.1093/emboj/cdg120 }}
*{{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=Fujita K, Shimazaki N, Ohta Y, ''et al.'' |title=Terminal deoxynucleotidyltransferase forms a ternary complex with a novel chromatin remodeling protein with 82 kDa and core histone. |journal=Genes Cells |volume=8 |issue= 6 |pages= 559-71 |year= 2004 |pmid= 12786946 |doi=  }}
*{{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=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=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=Gerhard DS, Wagner L, Feingold EA, etal |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 }}
*{{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=Braastad CD, Hovhannisyan H, van Wijnen AJ, etal |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 }}
*{{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=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   |vauthors=Bonenfant D, Coulot M, Towbin H, etal |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 }}
*{{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 }}
*{{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=Bonenfant D, Coulot M, Towbin H, ''et al.'' |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 }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=8338}}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


{{protein-stub}}
{{gene-1-stub}}
{{WikiDoc Sources}}

Latest revision as of 19:50, 22 February 2018

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

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 2-C is a protein that in humans is encoded by the HIST2H2AC gene.[1][2][3][4]

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.[4]

References

  1. ↑ Collart D, Romain PL, Huebner K, Pockwinse S, Pilapil S, Cannizzaro LA, Lian JB, Croce CM, Stein JL, Stein GS (Jan 1993). "A human histone H2B.1 variant gene, located on chromosome 1, utilizes alternative 3' end processing". J Cell Biochem. 50 (4): 374–85. doi:10.1002/jcb.240500406. PMID 1469070.
  2. ↑ 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.
  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: HIST2H2AC histone cluster 2, H2ac".

Further reading



Retrieved from "https://www.wikidoc.org/index.php?title=HIST2H2AC&oldid=1530599"