HIST1H3F: Difference between revisions

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{{Infobox_gene}}
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'''Histone H3.1''' is a [[protein]] that in humans is encoded by the ''HIST1H3F'' [[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: HIST1H3F histone cluster 1, H3f| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8968| accessdate = }}</ref>
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{{GNF_Protein_box
| image = PBB_Protein_HIST1H3F_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1aoi.
| PDB = {{PDB2|1aoi}}, {{PDB2|1eqz}}, {{PDB2|1f66}}, {{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|1u35}}, {{PDB2|1zbb}}, {{PDB2|1zla}}, {{PDB2|2aro}}, {{PDB2|2cv5}}, {{PDB2|2f8n}}, {{PDB2|2fj7}}, {{PDB2|2hio}}, {{PDB2|2hue}}, {{PDB2|2io5}}, {{PDB2|2nzd}}
| Name = Histone cluster 1, H3f
| HGNCid = 4773
| Symbol = HIST1H3F
| AltSymbols =; H3/i; H3FI
| OMIM = 602816
| ECnumber =
| Homologene = 88505
| MGIid =
  | Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0005515 |text = protein 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 = 8968
    | Hs_Ensembl = 
    | Hs_RefseqProtein = NP_066298
    | Hs_RefseqmRNA = NM_021018
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 
    | Hs_GenLoc_start = 
    | Hs_GenLoc_end = 
    | Hs_Uniprot = 
    | Mm_EntrezGene = 625328
    | Mm_Ensembl =  
    | Mm_RefseqmRNA = XM_889893
    | Mm_RefseqProtein = XP_894986
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Histone cluster 1, H3f''', also known as '''HIST1H3F''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HIST1H3F histone cluster 1, H3f| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8968| 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 H3 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: HIST1H3F histone cluster 1, H3f| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8968| accessdate = }}</ref>
| summary_text = [[Histone]]s 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 ([[Histone H2A|H2A]], [[Histone H2B|H2B]], [[Histone H3|H3]], and [[Histone H4|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 [[intron]]less and encodes a member of the histone H3 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 6]]p22-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=Albig W, Kardalinou E, Drabent B, ''et al.'' |title=Isolation and characterization of two human H1 histone genes within clusters of core histone genes. |journal=Genomics |volume=10 |issue= 4 |pages= 940-8 |year= 1991 |pmid= 1916825 |doi=  }}
*{{cite journal   |vauthors=Albig W, Kardalinou E, Drabent B, etal |title=Isolation and characterization of two human H1 histone genes within clusters of core histone genes. |journal=Genomics |volume=10 |issue= 4 |pages= 940–8 |year= 1991 |pmid= 1916825 |doi=10.1016/0888-7543(91)90183-F  }}
*{{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=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=Rea S, Eisenhaber F, O'Carroll D, etal |title=Regulation of chromatin structure by site-specific histone H3 methyltransferases. |journal=Nature |volume=406 |issue= 6796 |pages= 593–9 |year= 2000 |pmid= 10949293 |doi= 10.1038/35020506 }}
*{{cite journal | author=Rea S, Eisenhaber F, O'Carroll D, ''et al.'' |title=Regulation of chromatin structure by site-specific histone H3 methyltransferases. |journal=Nature |volume=406 |issue= 6796 |pages= 593-9 |year= 2000 |pmid= 10949293 |doi= 10.1038/35020506 }}
*{{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 | author=Hsu JY, Sun ZW, Li X, ''et al.'' |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=  }}
*{{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=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 | author=Lachner M, O'Carroll D, Rea S, ''et al.'' |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=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=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 | author=Yang L, Xia L, Wu DY, ''et al.'' |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=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=Xiao B, Jing C, Wilson JR, etal |title=Structure and catalytic mechanism of the human histone methyltransferase SET7/9. |journal=Nature |volume=421 |issue= 6923 |pages= 652–6 |year= 2003 |pmid= 12540855 |doi= 10.1038/nature01378 }}
*{{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=Koessler H, Doenecke D, Albig W |title=Aberrant expression pattern of replication-dependent histone h3 subtype genes in human tumor cell lines. |journal=DNA Cell Biol. |volume=22 |issue= 4 |pages= 233–41 |year= 2003 |pmid= 12823900 |doi= 10.1089/104454903321908629 }}
*{{cite journal | author=Xiao B, Jing C, Wilson JR, ''et al.'' |title=Structure and catalytic mechanism of the human histone methyltransferase SET7/9. |journal=Nature |volume=421 |issue= 6923 |pages= 652-6 |year= 2003 |pmid= 12540855 |doi= 10.1038/nature01378 }}
*{{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=Koessler H, Doenecke D, Albig W |title=Aberrant expression pattern of replication-dependent histone h3 subtype genes in human tumor cell lines. |journal=DNA Cell Biol. |volume=22 |issue= 4 |pages= 233-41 |year= 2003 |pmid= 12823900 |doi= 10.1089/104454903321908629 }}
*{{cite journal  |vauthors=Couture JF, Collazo E, Hauk G, Trievel RC |title=Structural basis for the methylation site specificity of SET7/9. |journal=Nat. Struct. Mol. Biol. |volume=13 |issue= 2 |pages= 140–6 |year= 2006 |pmid= 16415881 |doi= 10.1038/nsmb1045 }}
*{{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=Ewing RM, Chu P, Elisma F, etal |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue=  1|pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 | pmc=1847948 }}
*{{cite journal  | author=Couture JF, Collazo E, Hauk G, Trievel RC |title=Structural basis for the methylation site specificity of SET7/9. |journal=Nat. Struct. Mol. Biol. |volume=13 |issue= 2 |pages= 140-6 |year= 2006 |pmid= 16415881 |doi= 10.1038/nsmb1045 }}
*{{cite journal | author=Ewing RM, Chu P, Elisma F, ''et al.'' |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue=  |pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 }}
}}
}}
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{{refend}}
{{PDB Gallery|geneid=8968}}
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Latest revision as of 13:41, 31 August 2017

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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 H3.1 is a protein that in humans is encoded by the HIST1H3F gene.[1][2][3]

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 H3 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.[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: HIST1H3F histone cluster 1, H3f".

Further reading



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