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Barrier to autointegration factor 1

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(Redirected from BANF1) Protein-coding gene in the species Homo sapiens
BANF1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1QCK, 2ODG, 1CI4, 2BZF, 2EZY, 2EZZ, 2EZX

Identifiers
AliasesBANF1, BAF, BCRP1, D14S1460, NGPS, Barrier to autointegration factor 1, BAF nuclear assembly factor 1
External IDsOMIM: 603811; MGI: 1346330; HomoloGene: 2866; GeneCards: BANF1; OMA:BANF1 - orthologs
Gene location (Human)
Chromosome 11 (human)
Chr.Chromosome 11 (human)
Chromosome 11 (human)Genomic location for BANF1Genomic location for BANF1
Band11q13.1Start66,002,228 bp
End66,004,149 bp
Gene location (Mouse)
Chromosome 19 (mouse)
Chr.Chromosome 19 (mouse)
Chromosome 19 (mouse)Genomic location for BANF1Genomic location for BANF1
Band19|19 AStart5,414,666 bp
End5,417,196 bp
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • ganglionic eminence

  • ventricular zone

  • right uterine tube

  • muscle of thigh

  • apex of heart

  • gastrocnemius muscle

  • ascending aorta

  • body of uterus

  • Descending thoracic aorta

  • right coronary artery
Top expressed in
  • somite

  • embryo

  • medial ganglionic eminence

  • mandibular prominence

  • maxillary prominence

  • epiblast

  • embryo

  • thymus

  • fetal liver hematopoietic progenitor cell

  • hand
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

8815

23825

Ensembl

ENSG00000175334

ENSMUSG00000024844

UniProt

O75531

O54962

RefSeq (mRNA)

NM_003860
NM_001143985

NM_001038231
NM_001286608
NM_011793

RefSeq (protein)

NP_001137457
NP_003851

NP_001033320
NP_001273537
NP_035923

Location (UCSC)Chr 11: 66 – 66 MbChr 19: 5.41 – 5.42 Mb
PubMed search
Wikidata
View/Edit HumanView/Edit Mouse

Barrier-to-autointegration factor is a protein that in humans is encoded by the BANF1 gene. 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. It also associates with the LEM Domain containing proteins LAP2, Emerin, and MAN1. The protein's DNA binding ability is modulated by ATP concentration.

Interactions

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

Clinical relevance

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

See also

References

  1. ^ GRCh38: Ensembl release 89: ENSG00000175334Ensembl, May 2017
  2. ^ GRCm38: Ensembl release 89: ENSMUSG00000024844Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. 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. Bibcode:1998PNAS...95.1528L. doi:10.1073/pnas.95.4.1528. PMC 19075. PMID 9465049.
  6. ^ "Entrez Gene: BANF1 barrier to autointegration factor 1".
  7. Sridharan S, Kurzawa N, Werner T, Günthner I, Helm D, Huber W, Bantscheff M, Savitski MM (March 2019). "Proteome-wide solubility and thermal stability profiling reveals distinct regulatory roles for ATP". Nature Communications. 10 (1): 1155. Bibcode:2019NatCo..10.1155S. doi:10.1038/s41467-019-09107-y. PMC 6411743. PMID 30858367.
  8. 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. doi:10.1242/jcs.112.15.2485. PMID 10393804.
  9. 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

PDB gallery
  • 1ci4: THE CRYSTAL STRUCTURE OF HUMAN BARRIER-TO-AUTOINTEGRATION FACTOR (BAF) 1ci4: THE CRYSTAL STRUCTURE OF HUMAN BARRIER-TO-AUTOINTEGRATION FACTOR (BAF)
  • 1qck: SOLUTION STRUCTURE OF HUMAN BARRIER-TO-AUTOINTEGRATION FACTOR BAF, NMR, REGULARIZED MEAN STRUCTURE PLUS 20 INDIVIDUAL SIMULATED ANNEALING STRUCTURES 1qck: SOLUTION STRUCTURE OF HUMAN BARRIER-TO-AUTOINTEGRATION FACTOR BAF, NMR, REGULARIZED MEAN STRUCTURE PLUS 20 INDIVIDUAL SIMULATED ANNEALING STRUCTURES
  • 2bzf: STRUCTURAL BASIS FOR DNA BRIDGING BY BARRIER-TO-AUTOINTEGRATION FACTOR (BAF) 2bzf: STRUCTURAL BASIS FOR DNA BRIDGING BY BARRIER-TO-AUTOINTEGRATION FACTOR (BAF)
  • 2ezx: SOLUTION STRUCTURE OF HUMAN BARRIER-TO-AUTOINTEGRATION FACTOR BAF, NMR, REGULARIZED MEAN STRUCTURE 2ezx: SOLUTION STRUCTURE OF HUMAN BARRIER-TO-AUTOINTEGRATION FACTOR BAF, NMR, REGULARIZED MEAN STRUCTURE
  • 2ezy: SOLUTION STRUCTURE OF HUMAN BARRIER-TO-AUTOINTEGRATION FACTOR BAF, NMR, ENSEMBLE OF 20 SIMULATED ANNEALING STRUCTURES 2ezy: SOLUTION STRUCTURE OF HUMAN BARRIER-TO-AUTOINTEGRATION FACTOR BAF, NMR, ENSEMBLE OF 20 SIMULATED ANNEALING STRUCTURES
  • 2ezz: SOLUTION STRUCTURE OF HUMAN BARRIER-TO-AUTOINTEGRATION FACTOR BAF NMR, ENSEMBLE OF 20 SIMULATED ANNEALING STRUCTURES 2ezz: SOLUTION STRUCTURE OF HUMAN BARRIER-TO-AUTOINTEGRATION FACTOR BAF NMR, ENSEMBLE OF 20 SIMULATED ANNEALING STRUCTURES
  • 2odg: Complex of barrier-to-autointegration factor and LEM-domain of emerin 2odg: Complex of barrier-to-autointegration factor and LEM-domain of emerin


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