HIST1H2AC: Difference between revisions

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'''Histone H2A type 1-C''' is a [[protein]] that in humans is encoded by the ''HIST1H2AC'' [[gene]].<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: HIST1H2AC histone cluster 1, H2ac| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8334| accessdate = }}</ref>
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{{GNF_Protein_box
| image = PBB_Protein_HIST1H2AC_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, H2ac
| HGNCid = 4733
| Symbol = HIST1H2AC
| AltSymbols =; H2A/l; H2AFL; MGC99519; dJ221C16.4
| OMIM = 602794
| ECnumber =
| Homologene = 74477
| MGIid = 2448285
  | GeneAtlas_image1 = PBB_GE_HIST1H2AC_215071_s_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 = 8334
    | Hs_Ensembl = ENSG00000180573
    | Hs_RefseqProtein = NP_003503
    | Hs_RefseqmRNA = NM_003512
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 6
    | Hs_GenLoc_start = 26232352
    | Hs_GenLoc_end = 26247309
    | Hs_Uniprot = Q93077
    | Mm_EntrezGene = 319163
    | Mm_Ensembl = ENSMUSG00000060081
    | Mm_RefseqmRNA = NM_175658
    | Mm_RefseqProtein = NP_783589
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 13
    | Mm_GenLoc_start = 23941927
    | Mm_GenLoc_end = 23942316
    | Mm_Uniprot = 
  }}
}}
'''Histone cluster 1, H2ac''', also known as '''HIST1H2AC''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HIST1H2AC histone cluster 1, H2ac| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8334| 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. 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 the large histone gene cluster on chromosome 6.<ref name="entrez">{{cite web | title = Entrez Gene: HIST1H2AC histone cluster 1, H2ac| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8334| 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. Transcripts from this gene lack polyA tails but instead contain a palindromic termination element. This gene is found in the large histone gene cluster on chromosome 6.<ref name="entrez">{{cite web | title = Entrez Gene: HIST1H2AC histone cluster 1, H2ac| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8334| 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=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=Ruddy DA, Kronmal GS, Lee VK, etal |title=A 1.1-Mb transcript map of the hereditary hemochromatosis locus. |journal=Genome Res. |volume=7 |issue= 5 |pages= 441–56 |year= 1997 |pmid= 9149941 |doi=  10.1101/gr.7.5.441}}
*{{cite journal  | author=Ruddy DA, Kronmal GS, Lee VK, ''et al.'' |title=A 1.1-Mb transcript map of the hereditary hemochromatosis locus. |journal=Genome Res. |volume=7 |issue= 5 |pages= 441-56 |year= 1997 |pmid= 9149941 |doi=  }}
*{{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 }}
*{{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=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=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=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=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, 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=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=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=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=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=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=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=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=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=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=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=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=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=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=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=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 }}
*{{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 }}
*{{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   |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=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 }}
*{{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=8334}}
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Latest revision as of 13:38, 31 August 2017

VALUE_ERROR (nil)
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 1-C is a protein that in humans is encoded by the HIST1H2AC gene.[1][2][3]

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 the large histone gene cluster on chromosome 6.[3]

References

  1. ↑ 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.
  2. ↑ 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.
  3. ↑ 3.0 3.1 "Entrez Gene: HIST1H2AC histone cluster 1, H2ac".

Further reading



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