protein
Barrier-to-autointegration factor
Gene
BANF1
Organism
Homo sapiens(9606)
Length
89 aa
Mass
10,059 Da
Barrier-to-autointegration factor (BAF, encoded by *BANF1*) is a small non-specific DNA-binding protein that plays critical roles in mitotic nuclear reassembly, chromatin organization, DNA damage response, and innate immunity (UniProt: O75531). Through its dual dsDNA-binding domains, BAF promotes DNA cross-bridging and transiently stabilizes chromatin architecture during cell division, while also restricting cytosolic DNA-sensing pathways by outcompeting cGAS for substrate binding (UniProt: O75531).
BAF is involved in multiple cellular stress responses, including interactions with PARP1 during oxidative damage and recognition of exogenous cytosolic dsDNA at endosome rupture (UniProt: O75531). A known disease association is Nestor-Guillermo progeria syndrome (MIM 614008), characterized by premature lipoatrophy and bone loss (UniProt: O75531).
In Alzheimer's disease, BAF is downregulated in post-mortem human brain tissue compared to age-matched controls, with a mean log2 fold-change of −0.125 (Chaparral AD proteomics). This reduction may contribute to altered nuclear organization and impaired DNA-damage responses observed in neurodegeneration, though the modest magnitude suggests context-dependent effects across subcellular compartments.
Generated from the curated entity record below. May contain errors — verify against source links.
Proteomics Evidence · AD
↓ Down in ADP3
-0.125
P2
not detected
S2
not detected
S3
not detected
Mean log₂FC across detected fractions: -0.125 (1 of 4 fractions detected)
Human post-mortem AD brain vs age-matched controls, TMT-labeled, 4 subcellular fractions (P2, P3, S2, S3), DDA proteomics.
Related Publications
Browse all →Tau molecular diversity contributes to clinical heterogeneity in Alzheimer's disease.
Dujardin Simon et al.Nature medicine2020PMID 32572268Deep Multilayer Brain Proteomics Identifies Molecular Networks in Alzheimer's Disease Progression.
Bai Bing et al.Neuron2020PMID 31926610A Multi-network Approach Identifies Protein-Specific Co-expression in Asymptomatic and Symptomatic Alzheimer's Disease.
Seyfried Nicholas T et al.Cell systems2017PMID 27989508Large-scale deep multi-layer analysis of Alzheimer's disease brain reveals strong proteomic disease-related changes not observed at the RNA level.
Johnson Erik C B et al.Nature neuroscience2022PMID 35115731Organization and regulation of gene transcription.
Cramer PatrickNature2019PMID 31462772
Function
Non-specific DNA-binding protein that plays key roles in mitotic nuclear reassembly, chromatin organization, DNA damage response, gene expression and intrinsic immunity against foreign DNA (PubMed:10908652, PubMed:11792822, PubMed:12163470, PubMed:18005698, PubMed:25991860, PubMed:28841419, PubMed:31796734, PubMed:32792394). Contains two non-specific double-stranded DNA (dsDNA)-binding sites which promote DNA cross-bridging (PubMed:9465049). Plays a key role in nuclear membrane reformation at the end of mitosis by driving formation of a single nucleus in a spindle-independent manner (PubMed:28841419). Transiently cross-bridges anaphase chromosomes via its ability to bridge distant DNA sites, leading to the formation of a dense chromatin network at the chromosome ensemble surface that limits membranes to the surface (PubMed:28841419). Also acts as a negative regulator of innate immune activation by restricting CGAS activity toward self-DNA upon acute loss of nuclear membrane integrity (PubMed:32792394). Outcompetes CGAS for DNA-binding, thereby preventing CGAS activation and subsequent damaging autoinflammatory responses (PubMed:32792394). Also involved in DNA damage response: interacts with PARP1 in response to oxidative stress, thereby inhibiting the ADP-ribosyltransferase activity of PARP1 (PubMed:31796734). Involved in the recognition of exogenous dsDNA in the cytosol: associates with exogenous dsDNA immediately after its appearance in the cytosol at endosome breakdown and is required to avoid autophagy (PubMed:25991860). In case of poxvirus infection, has an antiviral activity by blocking viral DNA replication (PubMed:18005698)
(Microbial infection) Exploited by retroviruses for inhibiting self-destructing autointegration of retroviral DNA, thereby promoting integration of viral DNA into the host chromosome (PubMed:11005805, PubMed:16680152, PubMed:9465049). EMD and BAF are cooperative cofactors of HIV-1 infection (PubMed:16680152). Association of EMD with the viral DNA requires the presence of BAF and viral integrase (PubMed:16680152). The association of viral DNA with chromatin requires the presence of BAF and EMD (PubMed:16680152)
Disease associations
Nestor-Guillermo progeria syndromeNGPS
An atypical progeroid syndrome characterized by normal development in the first years of life, later followed by the emergence of generalized lipoatrophy, severe osteoporosis, and marked osteolysis. The atrophic facial subcutaneous fat pad and the marked osteolysis of the maxilla and mandible result in a typical pseudosenile facial appearance with micrognathia, prominent subcutaneous venous patterning, a convex nasal ridge, and proptosis. Cognitive development is completely normal. Patients do not have cardiovascular dysfunction, atherosclerosis, or metabolic anomalies.
Sources
Last updated 5/8/2026, 6:25:38 AM