Barrier to autointegration factor 1

Barrier-to-autointegration factor is a protein that in humans is encoded by the BANF1 gene.[5][6] It is a member of the barrier-to-autointegration factor family of proteins.

BANF1
Available structures
PDBOrtholog search: PDBe RCSB
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
Gene location (Human)
Chr.Chromosome 11 (human)[1]
Band11q13.1Start66,002,228 bp[1]
End66,004,149 bp[1]
RNA expression pattern
More reference expression data
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: 5.36 – 5.37 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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.[6] It also associates with the LEM Domain containing proteins LAP2, Emerin, and MAN1. The protein's DNA binding ability is modulated by ATP concentration.[7]

Interactions

Barrier to autointegration factor 1 has been shown to interact with Thymopoietin.[8]

Clinical relevance

Mutations in this gene have been shown to cause hereditary progeroid syndrome.[9]

gollark: See last paragraph.
gollark: ``` They're very gentle creatures, spending most of their lives flying lazy loops in the sky or draped decoratively over evergreen boughs and along eaves. Their green "garland" along their spine is modified dorsal fin, flexible, not stiff. Though they do eat normal small prey animals, the mainstay of their diet is mana absorbed through the green fins. They greatly prefer Life mana, but an abundance of any in a region will suffice. The berries are most often highly refined fire mana, and give gentle, comforting warmth to any who find one. They will gather in small groups in areas with higher than normal mana concentrations in the air, though they can be seen nearly anywhere. They appear to be oblivious to extremes of both hot and cold weather, though they're seen more often during the snowy months. It is believed that they actively convert excess mana to fire mana, which is then deliberately dropped in the form of their berries. If one finds a nest made by one of these dragons they will find a layer of the mana berries lining the bottom, presumably to keep the eggs warm while the parent is away. These dragons are believed to be the source of the practice of decorating homes and trees with garlands made of evergreen boughs and holly berries or cranberries.```The Wiki™.
gollark: Oh, wait, it makes sense.
gollark: ???
gollark: Hub: has lots of 2G SAltkins.Me: is kind of annoyed that they all say SAltkin swap.

See also
  • Retroviral integration

References
  1. GRCh38: Ensembl release 89: ENSG00000175334 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000024844 - Ensembl, 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. 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. 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. 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


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