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]
^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. PMID10393804.
Goldberg M, Harel A, Gruenbaum Y (2000). "The nuclear lamina: molecular organization and interaction with chromatin". Crit. Rev. Eukaryot. Gene Expr. 9 (3–4): 285–93. doi:10.1615/critreveukargeneexpr.v9.i3-4.130. PMID10651245.
Segura-Totten M, Wilson KL (2004). "BAF: roles in chromatin, nuclear structure and retrovirus integration". Trends Cell Biol. 14 (5): 261–6. doi:10.1016/j.tcb.2004.03.004. PMID15130582.
Van Maele B, Debyser Z (2005). "HIV-1 integration: an interplay between HIV-1 integrase, cellular and viral proteins". AIDS Reviews. 7 (1): 26–43. PMID15875659.
Van Maele B, Busschots K, Vandekerckhove L, et al. (2006). "Cellular co-factors of HIV-1 integration". Trends Biochem. Sci. 31 (2): 98–105. doi:10.1016/j.tibs.2005.12.002. PMID16403635.
Dear PH, Bankier AT, Piper MB (1998). "A high-resolution metric HAPPY map of human chromosome 14". Genomics. 48 (2): 232–41. doi:10.1006/geno.1997.5140. PMID9521877.
Lynch RA, Piper M, Bankier A, et al. (1999). "Genomic and functional map of the chromosome 14 t(12;14) breakpoint cluster region in uterine leiomyoma". Genomics. 52 (1): 17–26. doi:10.1006/geno.1998.5406. PMID9740667.
Cai M, Huang Y, Zheng R, et al. (1998). "Solution structure of the cellular factor BAF responsible for protecting retroviral DNA from autointegration". Nat. Struct. Biol. 5 (10): 903–9. doi:10.1038/2345. PMID9783751. S2CID857675.
Furukawa K (1999). "LAP2 binding protein 1 (L2BP1/BAF) is a candidate mediator of LAP2-chromatin interaction". J. Cell Sci. 112 (15): 2485–92. doi:10.1242/jcs.112.15.2485. PMID10393804.
Lee KK, Haraguchi T, Lee RS, et al. (2002). "Distinct functional domains in emerin bind lamin A and DNA-bridging protein BAF". J. Cell Sci. 114 (Pt 24): 4567–73. doi:10.1242/jcs.114.24.4567. PMID11792821.
Haraguchi T, Koujin T, Segura-Totten M, et al. (2002). "BAF is required for emerin assembly into the reforming nuclear envelope". J. Cell Sci. 114 (Pt 24): 4575–85. doi:10.1242/jcs.114.24.4575. PMID11792822.
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
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
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
2odg: Complex of barrier-to-autointegration factor and LEM-domain of emerin
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