BANF1
entrez
8815
canonical
uniprot
O75531
canonical
ensembl
ENSG00000175334
resolver
ensp
ENSP00000310275
resolver
ensp
ENSP00000416128
resolver
ensp
ENSP00000432867
resolver
ensp
ENSP00000433760
resolver
ensp
ENSP00000564373
resolver
ensp
ENSP00000564374
resolver
ensp
ENSP00000564375
resolver
ensp
ENSP00000564376
resolver
ensp
ENSP00000564377
resolver
ensp
ENSP00000564378
resolver
ensp
ENSP00000564379
resolver
ensp
ENSP00000564380
resolver
ensp
ENSP00000605856
resolver
ensp
ENSP00000605857
resolver
ensp
ENSP00000605858
resolver
ensp
ENSP00000605859
resolver
ensp
ENSP00000605860
resolver
ensp
ENSP00000605863
resolver
ensp
ENSP00000605864
resolver
ensp
ENSP00000605865
resolver
ensp
ENSP00000605866
resolver
ensp
ENSP00000611484
resolver
ensp
ENSP00000611485
resolver
enst
ENST00000312175
resolver
enst
ENST00000445560
resolver
enst
ENST00000527348
resolver
enst
ENST00000533166
resolver
enst
ENST00000894314
resolver
enst
ENST00000894315
resolver
enst
ENST00000894316
resolver
enst
ENST00000894317
resolver
enst
ENST00000894318
resolver
enst
ENST00000894319
resolver
enst
ENST00000894320
resolver
enst
ENST00000894321
resolver
enst
ENST00000935797
resolver
enst
ENST00000935798
resolver
enst
ENST00000935799
resolver
enst
ENST00000935800
resolver
enst
ENST00000935801
resolver
enst
ENST00000935804
resolver
enst
ENST00000935805
resolver
enst
ENST00000935806
resolver
enst
ENST00000935807
resolver
enst
ENST00000941425
resolver
enst
ENST00000941426
resolver
genesymbol
BANF1
resolver
genesymbol_syn
BAF
resolver
genesymbol_syn
BCRG1
resolver
hgnc
HGNC:17397
resolver
uniprot
O60558
resolver
uniprot
Q6FGG7
resolver
uniprot_entry
BAF_HUMAN
resolver
uniprot_sec
O60558
resolver
uniprot_sec
Q6FGG7
resolver
amino_acid_sequence
MTTSQKHRDFVAEPMGEKPVGSLAGIGEVLGKKLEERGFDKAYVVLGQFLVLKKDEDLFREWLKDTCGANAKQSRDCFGCLREWCDAFL
uniprot
proteins
disease_involvement
DISEASE: Nestor-Guillermo progeria syndrome (NGPS) [MIM:614008]: 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. {ECO:0000269|PubMed:21549337}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
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). {ECO:0000269|PubMed:10908652, ECO:0000269|PubMed:11792822, ECO:0000269|PubMed:12163470, ECO:0000269|PubMed:18005698, ECO:0000269|PubMed:25991860, ECO:0000269|PubMed:28841419, ECO:0000269|PubMed:31796734, ECO:0000269|PubMed:32792394, ECO:0000269|PubMed:9465049}.; FUNCTION: (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). {ECO:0000269|PubMed:11005805, ECO:0000269|PubMed:16680152, ECO:0000269|PubMed:9465049}.
uniprot
proteins
mass_dalton
10059
uniprot
proteins
mutagenesis
MUTAGEN 2..4; /note="TTS->AAA: 95% nuclear localization. Loss of BAF phosphorylation and ability to suppress vaccinia virus DNA replication."; /evidence="ECO:0000269|PubMed:16495336, ECO:0000269|PubMed:24600006"; MUTAGEN 2..4; /note="TTS->DDD: 85% cytoplasmic localization."; /evidence="ECO:0000269|PubMed:24600006"; MUTAGEN 2..3; /note="TT->AA: No effect on the initial rate of phosphorylation but a second slow phase of phosphorylation is absent."; /evidence="ECO:0000269|PubMed:16495336"; MUTAGEN 4; /note="S->A: Delayed phosphorylation with a 10-fold decrease in the initial phosphorylation rate. 71% loss of binding to lamin A."; /evidence="ECO:0000269|PubMed:16371512, ECO:0000269|PubMed:16495336"; MUTAGEN 4; /note="S->D: 75% cytoplasmic localization."; /evidence="ECO:0000269|PubMed:24600006"; MUTAGEN 4; /note="S->E: Complete loss of phosphorylation and mislocalization of EMD in nucleus."; /evidence="ECO:0000269|PubMed:16371512"; MUTAGEN 6; /note="K->A: Complete loss of LEMD3/MAN1 and histone H1/H3 binding."; /evidence="ECO:0000269|PubMed:11005805, ECO:0000269|PubMed:12163470, ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"; MUTAGEN 6; /note="K->E: Complete loss of dsDNA and LEMD3/MAN1 binding."; /evidence="ECO:0000269|PubMed:11005805, ECO:0000269|PubMed:12163470, ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"; MUTAGEN 8; /note="R->A: Enhances histone H1/H3 binding."; /evidence="ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"; MUTAGEN 8; /note="R->E: Complete loss of LEMD3/MAN1 binding."; /evidence="ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"; MUTAGEN 9; /note="D->A: Reduces binding to dsDNA, LEMD3/MAN1 and histone H1/H3. Reduced interaction with PARP1."; /evidence="ECO:0000269|PubMed:12163470, ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725, ECO:0000269|PubMed:31796734"; MUTAGEN 14; /note="P->A: No effect on LEMD3/MAN1 and enhances histone H1/H3 binding."; /evidence="ECO:0000269|PubMed:11005805, ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"; MUTAGEN 18; /note="K->A: No effect on histone H1/H3 binding."; /evidence="ECO:0000269|PubMed:11005805, ECO:0000269|PubMed:16203725"; MUTAGEN 25; /note="G->E: Complete loss of dsDNA, EMD, histone H1/H3 and LEMD3/MAN1 binding."; /evidence="ECO:0000269|PubMed:12163470, ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"; MUTAGEN 25; /note="G->Q: Complete loss of EMD binding and reduces dsDNA binding."; /evidence="ECO:0000269|PubMed:12163470, ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"; MUTAGEN 26; /note="I->A: Reduces histone H1/H3 and LEMD3/MAN1 binding. Fails to promote HIV-1 genome integration."; /evidence="ECO:0000269|PubMed:11005805, ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"; MUTAGEN 26; /note="I->K: Fails to promote HIV-1 genome integration."; /evidence="ECO:0000269|PubMed:11005805, ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"; MUTAGEN 27; /note="G->E: Fails to bind dsDNA."; /evidence="ECO:0000269|PubMed:12163470"; MUTAGEN 27; /note="G->Q: Reduces binding to dsDNA."; /evidence="ECO:0000269|PubMed:12163470"; MUTAGEN 29; /note="V->A: No effect on histone H1/H3 binding."; /evidence="ECO:0000269|PubMed:16203725"; MUTAGEN 32; /note="K->E: No effect on histone H1/H3 binding."; /evidence="ECO:0000269|PubMed:16203725"; MUTAGEN 33; /note="K->E: No effect on histone H1/H3 binding."; /evidence="ECO:0000269|PubMed:16203725"; MUTAGEN 37; /note="R->A: No effect on histone H1/H3 binding."; /evidence="ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"; MUTAGEN 37; /note="R->E: Reduces LEMD3/MAN1 binding."; /evidence="ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"; MUTAGEN 41; /note="K->A: No effect on histone H1/H3 and LEMD3/MAN1 binding."; /evidence="ECO:0000269|PubMed:11005805, ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"; MUTAGEN 41; /note="K->E: Reduces histone H1/H3 binding."; /evidence="ECO:0000269|PubMed:11005805, ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"; MUTAGEN 46; /note="L->E: Complete loss of dsDNA, histone H1/H3 and LEMD3/MAN1 binding."; /evidence="ECO:0000269|PubMed:12163470, ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"; MUTAGEN 47; /note="G->E: Abolishes homodimerization, preventing ability to cross-bridge DNA. Abolished ability to mediate nuclear membrane reformation at the end of mitosis. Abolished ability to outcompete CGAS for DNA-binding, leading to innate immune activation. Complete loss of EMD, histone H1/H3 and LEMD3/MAN1 binding."; /evidence="ECO:0000269|PubMed:12163470, ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725, ECO:0000269|PubMed:28841419, ECO:0000269|PubMed:32792394"; MUTAGEN 50; /note="L->A: Reduces LEMD3/MAN1 binding. No effect on Histone H1/H3 binding."; /evidence="ECO:0000269|PubMed:11005805, ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"; MUTAGEN 50; /note="L->K: Fails to promote HIV-1 genome integration."; /evidence="ECO:0000269|PubMed:11005805, ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"; MUTAGEN 51; /note="V->E: Complete loss of EMD, and histone H1/H3 binding. Reduces dsDNA and LEMD3/MAN1 binding."; /evidence="ECO:0000269|PubMed:12163470, ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"; MUTAGEN 53; /note="K->A: No effect on LEMD3/MAN1 binding. Enhances histone H1/H3 binding."; /evidence="ECO:0000269|PubMed:11005805, ECO:0000269|PubMed:12163470, ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"; MUTAGEN 53; /note="K->E: Complete loss of EMD binding. Reduces LEMD3/MAN1 binding. Enhances histone H1/H3 binding."; /evidence="ECO:0000269|PubMed:11005805, ECO:0000269|PubMed:12163470, ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"; MUTAGEN 54; /note="K->A: Reduces LEMD3/MAN1 binding. No effect on histone H1/H3 binding."; /evidence="ECO:0000269|PubMed:11005805, ECO:0000269|PubMed:12163470, ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"; MUTAGEN 54; /note="K->E: Reduces binding to dsDNA."; /evidence="ECO:0000269|PubMed:11005805, ECO:0000269|PubMed:12163470, ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"; MUTAGEN 58; /note="L->R: Abolishes interaction with LEM domain-containing proteins without affecting homodimerization and DNA-binding. Does not affect its involvement in nuclear membrane reformation at the end of mitosis. Does not affect ability to outcompete CGAS for DNA-binding."; /evidence="ECO:0000269|PubMed:28841419, ECO:0000269|PubMed:32792394"; MUTAGEN 60; /note="R->E: No effect on histone H1/H3 binding."; /evidence="ECO:0000269|PubMed:16203725"; MUTAGEN 62; /note="W->A: Complete loss of LEMD3/MAN1 binding. Enhances histone H1/H3 binding."; /evidence="ECO:0000269|PubMed:11005805, ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"; MUTAGEN 64; /note="K->E: Enhances histone H1/H3 binding."; /evidence="ECO:0000269|PubMed:16203725"; MUTAGEN 75; /note="R->E: Reduces binding to dsDNA. No effect on histone H1/H3 binding."; /evidence="ECO:0000269|PubMed:12163470, ECO:0000269|PubMed:16203725"; MUTAGEN 80; /note="C->A: No effect on histone H1/H3 and LEMD3/MAN1 binding."; /evidence="ECO:0000269|PubMed:11005805, ECO:0000269|PubMed:15681850, ECO:0000269|PubMed:16203725"; MUTAGEN 82; /note="R->E: No effect on histone H1/H3 binding."; /evidence="ECO:0000269|PubMed:16203725
uniprot
proteins
post_translational_modification
PTM: 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. {ECO:0000269|PubMed:16371512, ECO:0000269|PubMed:16495336, ECO:0000269|PubMed:22770216}.; PTM: (Microbial infection) Phosphorylated by poxvirus B1 kinase (VPK1) on serine and threonine residues, leading to BANF1 relocalization to the cytoplasm, loss of dimerization and impaired DNA binding activity. {ECO:0000269|PubMed:18005698, ECO:0000269|PubMed:24600006}.; PTM: (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 (PubMed:16495336, PubMed:24600006). Hyperphosphorylation is linked to the loss of ability to suppress vaccinia virus replication (PubMed:24600006). {ECO:0000269|PubMed:16495336, ECO:0000269|PubMed:24600006}.
uniprot
proteins
protein_family
BAF family
uniprot
proteins
pubmed
10908652
uniprot
proteins
pubmed
10924106
uniprot
proteins
pubmed
11005805
uniprot
proteins
pubmed
11792822
uniprot
proteins
pubmed
12163470
uniprot
proteins
pubmed
12663813
uniprot
proteins
pubmed
14645565
uniprot
proteins
pubmed
15130582
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15681850
uniprot
proteins
pubmed
16203725
uniprot
proteins
pubmed
16337940
uniprot
proteins
pubmed
16371512
uniprot
proteins
pubmed
16495336
uniprot
proteins
pubmed
16680152
uniprot
proteins
pubmed
18005698
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21549337
uniprot
proteins
pubmed
22399800
uniprot
proteins
pubmed
22770216
uniprot
proteins
pubmed
24600006
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
25991860
uniprot
proteins
pubmed
28841419
uniprot
proteins
pubmed
31796734
uniprot
proteins
pubmed
32494070
uniprot
proteins
pubmed
32792394
uniprot
proteins
pubmed
9465049
uniprot
proteins
pubmed
9740667
uniprot
proteins
pubmed
9783751
uniprot
proteins
sequence_length
89
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16495336, ECO:0000269|PubMed:18005698, ECO:0000269|PubMed:24600006}. Chromosome {ECO:0000269|PubMed:16495336, ECO:0000269|PubMed:28841419, ECO:0000269|PubMed:31796734, ECO:0000269|PubMed:32792394}. Nucleus envelope {ECO:0000269|PubMed:24600006}. Cytoplasm {ECO:0000269|PubMed:16495336, ECO:0000269|PubMed:18005698, ECO:0000269|PubMed:24600006}. Note=Significantly enriched at the nuclear inner membrane, diffusely throughout the nucleus during interphase and concentrated at the chromosomes during the M-phase (PubMed:16495336, PubMed:24600006). The phosphorylated form (by VRK1) shows a cytoplasmic localization whereas the unphosphorylated form locates almost exclusively in the nucleus (PubMed:16495336, PubMed:24600006). May be included in HIV-1 virions via its interaction with viral GAG polyprotein (PubMed:14645565). {ECO:0000269|PubMed:14645565, ECO:0000269|PubMed:16495336, ECO:0000269|PubMed:24600006}.
uniprot
proteins