BANF1 Antibody - #DF14424

Plays fundamental roles in nuclear assembly, chromatin organization, gene expression and gonad development. May potently compress chromatin structure and be involved in membrane recruitment and chromatin decondensation during nuclear assembly. Contains 2 non-specific dsDNA-binding sites which may promote DNA cross-bridging.

(Microbial infection) Exploited by retroviruses for inhibiting self-destructing autointegration of retroviral DNA, thereby promoting integration of viral DNA into the host chromosome. EMD and BAF are cooperative cofactors of HIV-1 infection. Association of EMD with the viral DNA requires the presence of BAF and viral integrase. The association of viral DNA with chromatin requires the presence of BAF and EMD.

(Microbial infection) In case of poxvirus infection, has an antiviral activity by blocking viral DNA replication.

Ser-4 is the major site of phosphorylation as compared to Thr-2 and Thr-3. Phosphorylation on Thr-2; Thr-3 and Ser-4 disrupts its ability to bind DNA and reduces its ability to bind LEM domain-containing proteins. Non phosphorylated BAF seems to enhance binding between EMD and LMNA. Dephosphorylated by protein phosphatase 2A (PP2A) following interaction with ANKLE2/LEM4 during mitotic exit, leading to mitotic nuclear envelope reassembly.

(Microbial infection) Phosphorylated at the N-terminus by vaccinia virus (VacV) B1 kinase, leading to BANF1 relocalization to the cytoplasm, loss of dimerization and impaired DNA binding activity. Hyperphosphorylation is linked to the loss of ability to suppress vaccinia virus replication.

Nucleus. Cytoplasm. Chromosome. Nucleus envelope.
Note: Significantly enriched at the nuclear inner membrane, diffusely throughout the nucleus during interphase and concentrated at the chromosomes during the M-phase. The phosphorylated form (by VRK1 or vaccinia virus B1 kinase) shows a cytoplasmic localization whereas the unphosphorylated form locates almost exclusively in the nucleus (PubMed:24600006, PubMed:16495336). May be included in HIV-1 virions via its interaction with viral GAG polyprotein.

Widely expressed. Expressed in colon, brain, heart, kidney, liver, lung, ovary, pancreas, placenta, prostate, skeletal muscle, small intestine, spleen and testis. Not detected in thymus and peripheral blood leukocytes.

Homodimer. Heterodimerizes with BAFL. Interacts with ANKLE2/LEM4, leading to decreased phosphorylation by VRK1 and promoting dephosphorylation by protein phosphatase 2A (PP2A). Binds non-specifically to double-stranded DNA, and is found as a hexamer or dodecamer upon DNA binding. Binds to LEM domain-containing nuclear proteins such as LEMD3/MAN1, TMPO/LAP2 and EMD (emerin). Interacts with ANKLE1 (via LEM domain); the interaction may favor BANF1 dimerization. Interacts with CRX and LMNA (lamin-A). Binds linker histone H1.1 and core histones H3.

(Microbial infection) Interacts with HIV-1 pre-integration complex in cytoplasm by binding to viral matrix protein and Gag polyprotein.

Has a helix-hairpin-helix (HhH) structural motif conserved among proteins that bind non-specifically to DNA.

LEM domain proteins bind centrally on the BAF dimer.

Belongs to the BAF family.