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{{Infobox_gene}}
{{PBB_Controls
'''Barrier-to-autointegration factor''' is a [[protein]] that in humans is encoded by the ''BANF1'' [[gene]].<ref name="pmid9465049">{{cite journal | vauthors = Lee MS, Craigie R | title = A previously unidentified host protein protects retroviral DNA from autointegration | journal = Proc Natl Acad Sci U S A | volume = 95 | issue = 4 | pages = 1528–33 |date=Mar 1998 | pmid = 9465049 | pmc = 19075 | doi =10.1073/pnas.95.4.1528  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: BANF1 barrier to autointegration factor 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8815| accessdate = }}</ref> It is a member of the [[barrier-to-autointegration factor]] family of proteins.
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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_BANF1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ci4.
| PDB = {{PDB2|1ci4}}, {{PDB2|1qck}}, {{PDB2|2bzf}}, {{PDB2|2ezx}}, {{PDB2|2ezy}}, {{PDB2|2ezz}}, {{PDB2|2odg}}
| Name = Barrier to autointegration factor 1
| HGNCid = 17397
| Symbol = BANF1
| AltSymbols =; BAF; BCRP1; D14S1460; MGC111161
| OMIM = 603811
| ECnumber = 
| Homologene = 2866
| MGIid = 1346330
| GeneAtlas_image1 = PBB_GE_BANF1_210125_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005694 |text = chromosome}}
| Process = {{GNF_GO|id=GO:0009615 |text = response to virus}} {{GNF_GO|id=GO:0015074 |text = DNA integration}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 8815
    | Hs_Ensembl = ENSG00000175334
    | Hs_RefseqProtein = NP_003851
    | Hs_RefseqmRNA = NM_003860
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 65526126
    | Hs_GenLoc_end = 65528192
    | Hs_Uniprot = O75531
    | Mm_EntrezGene = 23825
    | Mm_Ensembl = ENSMUSG00000024844
    | Mm_RefseqmRNA = NM_001038231
    | Mm_RefseqProtein = NP_001033320
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 19
    | Mm_GenLoc_start = 5364641
    | Mm_GenLoc_end = 5366651
    | Mm_Uniprot = O54962
  }}
}}
'''Barrier to autointegration factor 1''', also known as '''BANF1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: BANF1 barrier to autointegration factor 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8815| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The protein encoded by this gene was identified by its ability to protect [[retrovirus]]es from intramolecular integration and therefore promote intermolecular integration into the host cell genome. The endogenous function of the protein is unknown. The protein forms a homodimer which localizes to the nucleus and is specifically associated with chromosomes during [[mitosis]]. This protein binds to DNA in a non-specific manner and studies in rodents suggest that it also binds to [[thymopoietin|lamina-associated polypeptide 2]], a component of the [[nuclear lamina]].<ref name="entrez" /> It also associates with the LEM Domain containing proteins [[ERBB2IP|LAP2]], [[Emerin]], and [[MAN1]].
{{PBB_Summary
 
| section_title =
== Interactions ==
| summary_text = The protein encoded by this gene was identified by its ability to protect retroviruses from intramolecular integration and therefore promote intermolecular integration into the host cell genome. The endogenous function of the protein is unknown. The protein forms a homodimer which localizes to the nucleus and is specifically associated with chromosomes during mitosis. This protein binds to DNA in a non-specific manner and studies in rodents suggest that it also binds to lamina-associated polypeptide 2, a component of the nuclear lamina.<ref name="entrez">{{cite web | title = Entrez Gene: BANF1 barrier to autointegration factor 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8815| accessdate = }}</ref>
 
}}
Barrier to autointegration factor 1 has been shown to [[Protein-protein interaction|interact]] with [[Thymopoietin]].<ref name="pmid10393804">{{cite journal | author = Furukawa K | title = LAP2 binding protein 1 (L2BP1/BAF) is a candidate mediator of LAP2-chromatin interaction | journal = J. Cell Sci. | volume = 112 | issue = Pt 15| pages = 2485–92 |date=August 1999 | pmid = 10393804 | doi = }}</ref>
 
== Clinical relevance ==
 
Mutations in this gene have been shown to cause hereditary [[progeroid syndrome]].<ref name="pmid21549337">{{cite journal | vauthors = Puente XS, Quesada V, Osorio FG, Cabanillas R, Cadiñanos J, Fraile JM, Ordóñez GR, Puente DA, Gutiérrez-Fernández A, Fanjul-Fernández M, Lévy N, Freije JM, López-Otín C | title = Exome sequencing and functional analysis identifies BANF1 mutation as the cause of a hereditary progeroid syndrome | journal = Am. J. Hum. Genet. | volume = 88 | issue = 5 | pages = 650–6 |date=May 2011 | pmid = 21549337 | pmc = 3146734 | doi = 10.1016/j.ajhg.2011.04.010 }}</ref>


==See also==
==See also==
*[[retroviral integration]]
*[[retroviral integration]]
==References==
==References==
{{reflist|2}}
{{reflist}}


==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal  | vauthors=Goldberg M, Harel A, Gruenbaum Y |title=The nuclear lamina: molecular organization and interaction with chromatin |journal=Crit. Rev. Eukaryot. Gene Expr. |volume=9 |issue= 3–4 |pages= 285–93 |year= 2000 |pmid= 10651245 |doi=  10.1615/critreveukargeneexpr.v9.i3-4.130}}
| citations =
*{{cite journal  | vauthors=Segura-Totten M, Wilson KL |title=BAF: roles in chromatin, nuclear structure and retrovirus integration |journal=Trends Cell Biol. |volume=14 |issue= 5 |pages= 261–6 |year= 2004 |pmid= 15130582 |doi= 10.1016/j.tcb.2004.03.004 }}
*{{cite journal  | author=Goldberg M, Harel A, Gruenbaum Y |title=The nuclear lamina: molecular organization and interaction with chromatin. |journal=Crit. Rev. Eukaryot. Gene Expr. |volume=9 |issue= 3-4 |pages= 285-93 |year= 2000 |pmid= 10651245 |doi=  }}
*{{cite journal  | vauthors=Van Maele B, Debyser Z |title=HIV-1 integration: an interplay between HIV-1 integrase, cellular and viral proteins |journal=AIDS reviews |volume=7 |issue= 1 |pages= 26–43 |year= 2005 |pmid= 15875659 |doi=  }}
*{{cite journal  | author=Segura-Totten M, Wilson KL |title=BAF: roles in chromatin, nuclear structure and retrovirus integration. |journal=Trends Cell Biol. |volume=14 |issue= 5 |pages= 261-6 |year= 2004 |pmid= 15130582 |doi= 10.1016/j.tcb.2004.03.004 }}
*{{cite journal  | vauthors=Van Maele B, Busschots K, Vandekerckhove L |title=Cellular co-factors of HIV-1 integration |journal=Trends Biochem. Sci. |volume=31 |issue= 2 |pages= 98–105 |year= 2006 |pmid= 16403635 |doi= 10.1016/j.tibs.2005.12.002 |display-authors=etal}}
*{{cite journal  | author=Van Maele B, Debyser Z |title=HIV-1 integration: an interplay between HIV-1 integrase, cellular and viral proteins. |journal=AIDS reviews |volume=7 |issue= 1 |pages= 26-43 |year= 2005 |pmid= 15875659 |doi=  }}
*{{cite journal  | vauthors=Lee MS, Craigie R |title=Protection of retroviral DNA from autointegration: involvement of a cellular factor |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 21 |pages= 9823–7 |year= 1994 |pmid= 7937898 |doi=10.1073/pnas.91.21.9823  | pmc=44909  }}
*{{cite journal  | author=Van Maele B, Busschots K, Vandekerckhove L, ''et al.'' |title=Cellular co-factors of HIV-1 integration. |journal=Trends Biochem. Sci. |volume=31 |issue= 2 |pages= 98-105 |year= 2006 |pmid= 16403635 |doi= 10.1016/j.tibs.2005.12.002 }}
*{{cite journal  | vauthors=Dear PH, Bankier AT, Piper MB |title=A high-resolution metric HAPPY map of human chromosome 14 |journal=Genomics |volume=48 |issue= 2 |pages= 232–41 |year= 1998 |pmid= 9521877 |doi= 10.1006/geno.1997.5140 }}
*{{cite journal  | author=Lee MS, Craigie R |title=Protection of retroviral DNA from autointegration: involvement of a cellular factor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 21 |pages= 9823-7 |year= 1994 |pmid= 7937898 |doi= }}
*{{cite journal  | vauthors=Lynch RA, Piper M, Bankier A |title=Genomic and functional map of the chromosome 14 t(12;14) breakpoint cluster region in uterine leiomyoma |journal=Genomics |volume=52 |issue= 1 |pages= 17–26 |year= 1999 |pmid= 9740667 |doi= 10.1006/geno.1998.5406 |display-authors=etal}}
*{{cite journal  | author=Lee MS, Craigie R |title=A previously unidentified host protein protects retroviral DNA from autointegration. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 4 |pages= 1528-33 |year= 1998 |pmid= 9465049 |doi= }}
*{{cite journal  | vauthors=Cai M, Huang Y, Zheng R |title=Solution structure of the cellular factor BAF responsible for protecting retroviral DNA from autointegration |journal=Nat. Struct. Biol. |volume=5 |issue= 10 |pages= 903–9 |year= 1998 |pmid= 9783751 |doi= 10.1038/2345 |display-authors=etal}}
*{{cite journal  | author=Dear PH, Bankier AT, Piper MB |title=A high-resolution metric HAPPY map of human chromosome 14. |journal=Genomics |volume=48 |issue= 2 |pages= 232-41 |year= 1998 |pmid= 9521877 |doi= 10.1006/geno.1997.5140 }}
*{{cite journal  | author=Furukawa K |title=LAP2 binding protein 1 (L2BP1/BAF) is a candidate mediator of LAP2-chromatin interaction |journal=J. Cell Sci. |volume=112 |issue= 15|pages= 2485–92 |year= 1999 |pmid= 10393804 |doi= }}
*{{cite journal  | author=Lynch RA, Piper M, Bankier A, ''et al.'' |title=Genomic and functional map of the chromosome 14 t(12;14) breakpoint cluster region in uterine leiomyoma. |journal=Genomics |volume=52 |issue= 1 |pages= 17-26 |year= 1999 |pmid= 9740667 |doi= 10.1006/geno.1998.5406 }}
*{{cite journal  | vauthors=Zheng R, Ghirlando R, Lee MS |title=Barrier-to-autointegration factor (BAF) bridges DNA in a discrete, higher-order nucleoprotein complex |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 16 |pages= 8997–9002 |year= 2000 |pmid= 10908652 |doi= 10.1073/pnas.150240197 | pmc=16810 |display-authors=etal}}
*{{cite journal  | author=Cai M, Huang Y, Zheng R, ''et al.'' |title=Solution structure of the cellular factor BAF responsible for protecting retroviral DNA from autointegration. |journal=Nat. Struct. Biol. |volume=5 |issue= 10 |pages= 903-9 |year= 1998 |pmid= 9783751 |doi= 10.1038/2345 }}
*{{cite journal  | vauthors=Umland TC, Wei SQ, Craigie R, Davies DR |title=Structural basis of DNA bridging by barrier-to-autointegration factor |journal=Biochemistry |volume=39 |issue= 31 |pages= 9130–8 |year= 2000 |pmid= 10924106 |doi=10.1021/bi000572w  }}
*{{cite journal  | author=Furukawa K |title=LAP2 binding protein 1 (L2BP1/BAF) is a candidate mediator of LAP2-chromatin interaction. |journal=J. Cell. Sci. |volume=112 ( Pt 15) |issue= |pages= 2485-92 |year= 1999 |pmid= 10393804 |doi=  }}
*{{cite journal  | vauthors=Harris D, Engelman A |title=Both the structure and DNA binding function of the barrier-to-autointegration factor contribute to reconstitution of HIV type 1 integration in vitro |journal=J. Biol. Chem. |volume=275 |issue= 50 |pages= 39671–7 |year= 2001 |pmid= 11005805 |doi= 10.1074/jbc.M002626200 }}
*{{cite journal  | author=Zheng R, Ghirlando R, Lee MS, ''et al.'' |title=Barrier-to-autointegration factor (BAF) bridges DNA in a discrete, higher-order nucleoprotein complex. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 16 |pages= 8997-9002 |year= 2000 |pmid= 10908652 |doi= 10.1073/pnas.150240197 }}
*{{cite journal  | vauthors=Lee KK, Haraguchi T, Lee RS |title=Distinct functional domains in emerin bind lamin A and DNA-bridging protein BAF |journal=J. Cell Sci. |volume=114 |issue= Pt 24 |pages= 4567–73 |year= 2002 |pmid= 11792821 |doi= |display-authors=etal}}
*{{cite journal  | author=Umland TC, Wei SQ, Craigie R, Davies DR |title=Structural basis of DNA bridging by barrier-to-autointegration factor. |journal=Biochemistry |volume=39 |issue= 31 |pages= 9130-8 |year= 2000 |pmid= 10924106 |doi= }}
*{{cite journal  | vauthors=Haraguchi T, Koujin T, Segura-Totten M |title=BAF is required for emerin assembly into the reforming nuclear envelope |journal=J. Cell Sci. |volume=114 |issue= Pt 24 |pages= 4575–85 |year= 2002 |pmid= 11792822 |doi=  |display-authors=etal}}
*{{cite journal  | author=Harris D, Engelman A |title=Both the structure and DNA binding function of the barrier-to-autointegration factor contribute to reconstitution of HIV type 1 integration in vitro. |journal=J. Biol. Chem. |volume=275 |issue= 50 |pages= 39671-7 |year= 2001 |pmid= 11005805 |doi= 10.1074/jbc.M002626200 }}
*{{cite journal  | vauthors=Segura-Totten M, Kowalski AK, Craigie R, Wilson KL |title=Barrier-to-autointegration factor: major roles in chromatin decondensation and nuclear assembly |journal=J. Cell Biol. |volume=158 |issue= 3 |pages= 475–85 |year= 2002 |pmid= 12163470 |doi= 10.1083/jcb.200202019 | pmc=2173821 }}
*{{cite journal  | author=Lee KK, Haraguchi T, Lee RS, ''et al.'' |title=Distinct functional domains in emerin bind lamin A and DNA-bridging protein BAF. |journal=J. Cell. Sci. |volume=114 |issue= Pt 24 |pages= 4567-73 |year= 2002 |pmid= 11792821 |doi=  }}
*{{cite journal  | vauthors=Strausberg RL, Feingold EA, Grouse LH |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 |display-authors=etal}}
*{{cite journal  | author=Haraguchi T, Koujin T, Segura-Totten M, ''et al.'' |title=BAF is required for emerin assembly into the reforming nuclear envelope. |journal=J. Cell. Sci. |volume=114 |issue= Pt 24 |pages= 4575-85 |year= 2002 |pmid= 11792822 |doi=  }}
*{{cite journal  | vauthors=Holaska JM, Lee KK, Kowalski AK, Wilson KL |title=Transcriptional repressor germ cell-less (GCL) and barrier to autointegration factor (BAF) compete for binding to emerin in vitro |journal=J. Biol. Chem. |volume=278 |issue= 9 |pages= 6969–75 |year= 2003 |pmid= 12493765 |doi= 10.1074/jbc.M208811200 }}
*{{cite journal  | author=Segura-Totten M, Kowalski AK, Craigie R, Wilson KL |title=Barrier-to-autointegration factor: major roles in chromatin decondensation and nuclear assembly. |journal=J. Cell Biol. |volume=158 |issue= 3 |pages= 475-85 |year= 2002 |pmid= 12163470 |doi= 10.1083/jcb.200202019 }}
*{{cite journal  | vauthors=Lin CW, Engelman A |title=The Barrier-to-Autointegration Factor Is a Component of Functional Human Immunodeficiency Virus Type 1 Preintegration Complexes |journal=J. Virol. |volume=77 |issue= 8 |pages= 5030–6 |year= 2003 |pmid= 12663813 |doi=10.1128/JVI.77.8.5030-5036.2003  | pmc=152146 }}
*{{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=Holaska JM, Lee KK, Kowalski AK, Wilson KL |title=Transcriptional repressor germ cell-less (GCL) and barrier to autointegration factor (BAF) compete for binding to emerin in vitro. |journal=J. Biol. Chem. |volume=278 |issue= 9 |pages= 6969-75 |year= 2003 |pmid= 12493765 |doi= 10.1074/jbc.M208811200 }}
*{{cite journal  | author=Lin CW, Engelman A |title=The barrier-to-autointegration factor is a component of functional human immunodeficiency virus type 1 preintegration complexes. |journal=J. Virol. |volume=77 |issue= 8 |pages= 5030-6 |year= 2003 |pmid= 12663813 |doi=  }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
==External links==
{{WikiDoc Sources}}
* {{UCSC gene info|BANF1}}
 
{{PDB Gallery|geneid=8815}}
 
 
{{gene-11-stub}}

Latest revision as of 19:25, 8 November 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

Barrier-to-autointegration factor is a protein that in humans is encoded by the BANF1 gene.[1][2] It is a member of the barrier-to-autointegration factor family of proteins.

Function

The protein encoded by this gene was identified by its ability to protect retroviruses from intramolecular integration and therefore promote intermolecular integration into the host cell genome. The endogenous function of the protein is unknown. The protein forms a homodimer which localizes to the nucleus and is specifically associated with chromosomes during mitosis. This protein binds to DNA in a non-specific manner and studies in rodents suggest that it also binds to lamina-associated polypeptide 2, a component of the nuclear lamina.[2] It also associates with the LEM Domain containing proteins LAP2, Emerin, and MAN1.

Interactions

Barrier to autointegration factor 1 has been shown to interact with Thymopoietin.[3]

Clinical relevance

Mutations in this gene have been shown to cause hereditary progeroid syndrome.[4]

See also

References

  1. ↑ Lee MS, Craigie R (Mar 1998). "A previously unidentified host protein protects retroviral DNA from autointegration". Proc Natl Acad Sci U S A. 95 (4): 1528–33. doi:10.1073/pnas.95.4.1528. PMC 19075. PMID 9465049.
  2. ↑ 2.0 2.1 "Entrez Gene: BANF1 barrier to autointegration factor 1".
  3. ↑ Furukawa K (August 1999). "LAP2 binding protein 1 (L2BP1/BAF) is a candidate mediator of LAP2-chromatin interaction". J. Cell Sci. 112 (Pt 15): 2485–92. PMID 10393804.
  4. ↑ Puente XS, Quesada V, Osorio FG, Cabanillas R, Cadiñanos J, Fraile JM, Ordóñez GR, Puente DA, Gutiérrez-Fernández A, Fanjul-Fernández M, Lévy N, Freije JM, López-Otín C (May 2011). "Exome sequencing and functional analysis identifies BANF1 mutation as the cause of a hereditary progeroid syndrome". Am. J. Hum. Genet. 88 (5): 650–6. doi:10.1016/j.ajhg.2011.04.010. PMC 3146734. PMID 21549337.

Further reading

External links


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