HIST1H3C: Difference between revisions

Jump to navigation Jump to search
m (Bot: HTTP→HTTPS)
imported>Veryproicelandic
(added some links, removed that flag, cleaned up the syntax, stubbed it...)
 
Line 1: Line 1:
{{Infobox_gene}}
{{Infobox_gene}}
'''Histone H3.1''' is a [[protein]] that in humans is encoded by the ''HIST1H3C'' [[gene]].<ref name="pmid8227173">{{cite journal |vauthors=Kardalinou E, Eick S, Albig W, Doenecke D | title = Association of a human H1 histone gene with an H2A pseudogene and genes encoding H2B.1 and H3.1 histones | journal = J Cell Biochem | volume = 52 | issue = 4 | pages = 375–83 |date=Dec 1993 | pmid = 8227173 | pmc =  | doi = 10.1002/jcb.240520402 }}</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: HIST1H3C histone cluster 1, H3c| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8352| accessdate = }}</ref>
'''Histone H3.1''' is a [[protein]] that in [[human]]s is encoded by the ''HIST1H3C'' [[gene]].<ref name="pmid8227173">{{cite journal |vauthors=Kardalinou E, Eick S, Albig W, Doenecke D | title = Association of a human H1 histone gene with an H2A pseudogene and genes encoding H2B.1 and H3.1 histones | journal = [[Journal of Cellular Biochemistry]] | volume = 52 | issue = 4 | pages = 375–83 |date=Dec 1993 | pmid = 8227173 | pmc =  | doi = 10.1002/jcb.240520402 }}</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: HIST1H3C histone cluster 1, H3c| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8352| 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 H3 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: HIST1H3C histone cluster 1, H3c| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8352| accessdate = }}</ref>
| summary_text = [[Histone]]s are basic [[nuclear protein]]s that are responsible for the [[nucleosome]] structure of the [[chromosome|chromosomal]] fiber in [[eukaryote]]s. Two [[molecule]]s 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 [[intron]]less, and encodes a member of the [[histone H3]] family. Transcripts from this gene lack polyA tails, instead containing 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: HIST1H3C histone cluster 1, H3c| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8352| accessdate = }}</ref>
}}
}}


Line 15: Line 17:
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{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  |vauthors=Albig W, Doenecke D |title=The human histone gene cluster at the D6S105 locus. |journal=[[Human Genetics (journal)|Human Genetics]] |volume=101 |issue= 3 |pages= 284–94 |year= 1998 |pmid= 9439656 |doi=10.1007/s004390050630  }}
*{{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  |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 |year= 1998 |pmid= 9566873 |doi=  10.1128/mcb.18.5.2535| pmc=110633  }}
*{{cite journal  |vauthors=Munakata T, Adachi N, Yokoyama N, etal |title=A human homologue of yeast anti-silencing factor has histone chaperone activity. |journal=Genes Cells |volume=5 |issue= 3 |pages= 221–33 |year= 2000 |pmid= 10759893 |doi=10.1046/j.1365-2443.2000.00319.x  }}
*{{cite journal  |vauthors=Munakata T, Adachi N, Yokoyama N, etal |title=A human homologue of yeast anti-silencing factor has histone chaperone activity. |journal=[[Genes to Cells]] |volume=5 |issue= 3 |pages= 221–33 |year= 2000 |pmid= 10759893 |doi=10.1046/j.1365-2443.2000.00319.x  }}
*{{cite journal  |vauthors=Hsu JY, Sun ZW, Li X, etal |title=Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes. |journal=Cell |volume=102 |issue= 3 |pages= 279–91 |year= 2000 |pmid= 10975519 |doi=10.1016/S0092-8674(00)00034-9  }}
*{{cite journal  |vauthors=Hsu JY, Sun ZW, Li X, etal |title=Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes. |journal=[[Cell (journal)|Cell]] |volume=102 |issue= 3 |pages= 279–91 |year= 2000 |pmid= 10975519 |doi=10.1016/S0092-8674(00)00034-9  }}
*{{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  |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 (journal)|Virology]] |volume=277 |issue= 2 |pages= 278–95 |year= 2001 |pmid= 11080476 |doi= 10.1006/viro.2000.0593 }}
*{{cite journal  |vauthors=Lachner M, O'Carroll D, Rea S, etal |title=Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. |journal=Nature |volume=410 |issue= 6824 |pages= 116–20 |year= 2001 |pmid= 11242053 |doi= 10.1038/35065132 }}
*{{cite journal  |vauthors=Lachner M, O'Carroll D, Rea S, etal |title=Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. |journal=[[Nature (journal)|Nature]] |volume=410 |issue= 6824 |pages= 116–20 |year= 2001 |pmid= 11242053 |doi= 10.1038/35065132 }}
*{{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  |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  |vauthors=Yang L, Xia L, Wu DY, etal |title=Molecular cloning of ESET, a novel histone H3-specific methyltransferase that interacts with ERG transcription factor. |journal=Oncogene |volume=21 |issue= 1 |pages= 148–52 |year= 2002 |pmid= 11791185 |doi= 10.1038/sj.onc.1204998 }}
*{{cite journal  |vauthors=Yang L, Xia L, Wu DY, etal |title=Molecular cloning of ESET, a novel histone H3-specific methyltransferase that interacts with ERG transcription factor. |journal=[[Oncogene (journal)|Oncogene]] |volume=21 |issue= 1 |pages= 148–52 |year= 2002 |pmid= 11791185 |doi= 10.1038/sj.onc.1204998 }}
*{{cite journal  |vauthors=Nielsen PR, Nietlispach D, Mott HR, etal |title=Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9. |journal=Nature |volume=416 |issue= 6876 |pages= 103–7 |year= 2002 |pmid= 11882902 |doi= 10.1038/nature722 }}
*{{cite journal  |vauthors=Nielsen PR, Nietlispach D, Mott HR, etal |title=Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9. |journal=Nature |volume=416 |issue= 6876 |pages= 103–7 |year= 2002 |pmid= 11882902 |doi= 10.1038/nature722 }}
*{{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  |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=[[Proceedings of the National Academy of Sciences of the United States of America]] |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 }}
*{{cite journal  |vauthors=Umehara T, Horikoshi M |title=Transcription initiation factor IID-interactive histone chaperone CIA-II implicated in mammalian spermatogenesis. |journal=J. Biol. Chem. |volume=278 |issue= 37 |pages= 35660–7 |year= 2003 |pmid= 12842904 |doi= 10.1074/jbc.M303549200 }}
*{{cite journal  |vauthors=Umehara T, Horikoshi M |title=Transcription initiation factor IID-interactive histone chaperone CIA-II implicated in mammalian spermatogenesis. |journal=[[Journal of Biological Chemistry]] |volume=278 |issue= 37 |pages= 35660–7 |year= 2003 |pmid= 12842904 |doi= 10.1074/jbc.M303549200 }}
*{{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  |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 |year= 2004 |pmid= 14657027 |doi= 10.1093/emboj/cdg631  | pmc=291826 }}
*{{cite journal  |vauthors=Black BE, Foltz DR, Chakravarthy S, etal |title=Structural determinants for generating centromeric chromatin. |journal=Nature |volume=430 |issue= 6999 |pages= 578–82 |year= 2004 |pmid= 15282608 |doi= 10.1038/nature02766 }}
*{{cite journal  |vauthors=Black BE, Foltz DR, Chakravarthy S, etal |title=Structural determinants for generating centromeric chromatin. |journal=Nature |volume=430 |issue= 6999 |pages= 578–82 |year= 2004 |pmid= 15282608 |doi= 10.1038/nature02766 }}
}}
}}
Line 43: Line 45:


{{protein-stub}}
{{protein-stub}}
{{gene-6-stub}}

Latest revision as of 07:58, 23 December 2018

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 H3.1 is a protein that in humans is encoded by the HIST1H3C 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 H3 family. Transcripts from this gene lack polyA tails, instead containing a palindromic termination element. This gene is found in the large histone gene cluster on chromosome 6.[4]

References

  1. Kardalinou E, Eick S, Albig W, Doenecke D (Dec 1993). "Association of a human H1 histone gene with an H2A pseudogene and genes encoding H2B.1 and H3.1 histones". Journal of Cellular Biochemistry. 52 (4): 375–83. doi:10.1002/jcb.240520402. PMID 8227173.
  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: HIST1H3C histone cluster 1, H3c".

Further reading