##gff-version 3 O75531 UniProtKB Chain 1 89 . . . ID=PRO_0000423190;Note=Barrier-to-autointegration factor O75531 UniProtKB Initiator methionine 1 1 . . . Note=Removed%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19413330;Dbxref=PMID:19413330 O75531 UniProtKB Chain 2 89 . . . ID=PRO_0000221026;Note=Barrier-to-autointegration factor%2C N-terminally processed O75531 UniProtKB Domain 20 35 . . . Note=HhH;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10924106;Dbxref=PMID:10924106 O75531 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:20068231;Dbxref=PMID:20068231 O75531 UniProtKB Modified residue 2 2 . . . Note=(Microbial infection) Phosphothreonine%3B by viral VacV B1 kinase;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16495336;Dbxref=PMID:16495336 O75531 UniProtKB Modified residue 2 2 . . . Note=N-acetylthreonine%3B in Barrier-to-autointegration factor%2C N-terminally processed;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19413330;Dbxref=PMID:19413330 O75531 UniProtKB Modified residue 2 2 . . . Note=Phosphothreonine%3B by VRK1 and VRK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16495336;Dbxref=PMID:16495336 O75531 UniProtKB Modified residue 3 3 . . . Note=(Microbial infection) Phosphothreonine%3B by viral VacV B1 kinase;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16495336;Dbxref=PMID:16495336 O75531 UniProtKB Modified residue 3 3 . . . Note=Phosphothreonine%3B by VRK1 and VRK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16495336;Dbxref=PMID:16495336 O75531 UniProtKB Modified residue 4 4 . . . Note=Phosphoserine%3B by viral VacV B1 kinase%2C VRK1 and VRK2;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16371512,ECO:0000269|PubMed:16495336;Dbxref=PMID:16371512,PMID:16495336 O75531 UniProtKB Natural variant 12 12 . . . ID=VAR_065954;Note=In NGPS%3B shows a dramatic reduction in BANF1 protein levels indicating that the mutation impairs protein stability. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21549337;Dbxref=dbSNP:rs387906871,PMID:21549337 O75531 UniProtKB Mutagenesis 2 4 . . . Note=95%25 nuclear localization. Loss of BAF phosphorylation and ability to suppress vaccinia virus DNA replication. TTS->AAA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16495336,ECO:0000269|PubMed:24600006;Dbxref=PMID:16495336,PMID:24600006 O75531 UniProtKB Mutagenesis 2 4 . . . Note=85%25 cytoplasmic localization. TTS->DDD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24600006;Dbxref=PMID:24600006 O75531 UniProtKB Mutagenesis 2 3 . . . Note=No effect on the initial rate of phosphorylation but a second slow phase of phosphorylation is absent. TT->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16495336;Dbxref=PMID:16495336 O75531 UniProtKB Mutagenesis 4 4 . . . Note=Delayed phosphorylation with a 10-fold decrease in the initial phosphorylation rate. 71%25 loss of binding to lamin A. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16371512,ECO:0000269|PubMed:16495336;Dbxref=PMID:16371512,PMID:16495336 O75531 UniProtKB Mutagenesis 4 4 . . . Note=75%25 cytoplasmic localization. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24600006;Dbxref=PMID:24600006 O75531 UniProtKB Mutagenesis 4 4 . . . Note=Complete loss of phosphorylation and mislocalization of EMD in nucleus. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16371512;Dbxref=PMID:16371512 O75531 UniProtKB Mutagenesis 6 6 . . . Note=Complete loss of LEMD3/MAN1 and histone H1/H3 binding. K->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11005805,ECO:0000269|PubMed:12163470,ECO:0000269|PubMed:15681850,ECO:0000269|PubMed:16203725;Dbxref=PMID:11005805,PMID:12163470,PMID:15681850,PMID:16203725 O75531 UniProtKB Mutagenesis 6 6 . . . Note=Complete loss of dsDNA and LEMD3/MAN1 binding. K->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11005805,ECO:0000269|PubMed:12163470,ECO:0000269|PubMed:15681850,ECO:0000269|PubMed:16203725;Dbxref=PMID:11005805,PMID:12163470,PMID:15681850,PMID:16203725 O75531 UniProtKB Mutagenesis 8 8 . . . Note=Enhances histone H1/H3 binding. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15681850,ECO:0000269|PubMed:16203725;Dbxref=PMID:15681850,PMID:16203725 O75531 UniProtKB Mutagenesis 8 8 . . . Note=Complete loss of LEMD3/MAN1 binding. R->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15681850,ECO:0000269|PubMed:16203725;Dbxref=PMID:15681850,PMID:16203725 O75531 UniProtKB Mutagenesis 9 9 . . . Note=Reduces binding to dsDNA%2C LEMD3/MAN1 and histone H1/H3. Reduced interaction with PARP1. D->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12163470,ECO:0000269|PubMed:15681850,ECO:0000269|PubMed:16203725,ECO:0000269|PubMed:31796734;Dbxref=PMID:12163470,PMID:15681850,PMID:16203725,PMID:31796734 O75531 UniProtKB Mutagenesis 14 14 . . . Note=No effect on LEMD3/MAN1 and enhances histone H1/H3 binding. P->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11005805,ECO:0000269|PubMed:15681850,ECO:0000269|PubMed:16203725;Dbxref=PMID:11005805,PMID:15681850,PMID:16203725 O75531 UniProtKB Mutagenesis 18 18 . . . Note=No effect on histone H1/H3 binding. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11005805,ECO:0000269|PubMed:16203725;Dbxref=PMID:11005805,PMID:16203725 O75531 UniProtKB Mutagenesis 25 25 . . . Note=Complete loss of dsDNA%2C EMD%2C histone H1/H3 and LEMD3/MAN1 binding. G->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12163470,ECO:0000269|PubMed:15681850,ECO:0000269|PubMed:16203725;Dbxref=PMID:12163470,PMID:15681850,PMID:16203725 O75531 UniProtKB Mutagenesis 25 25 . . . Note=Complete loss of EMD binding and reduces dsDNA binding. G->Q;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12163470,ECO:0000269|PubMed:15681850,ECO:0000269|PubMed:16203725;Dbxref=PMID:12163470,PMID:15681850,PMID:16203725 O75531 UniProtKB Mutagenesis 26 26 . . . Note=Reduces histone H1/H3 and LEMD3/MAN1 binding. Fails to promote HIV-1 genome integration. I->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11005805,ECO:0000269|PubMed:15681850,ECO:0000269|PubMed:16203725;Dbxref=PMID:11005805,PMID:15681850,PMID:16203725 O75531 UniProtKB Mutagenesis 26 26 . . . Note=Fails to promote HIV-1 genome integration. I->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11005805,ECO:0000269|PubMed:15681850,ECO:0000269|PubMed:16203725;Dbxref=PMID:11005805,PMID:15681850,PMID:16203725 O75531 UniProtKB Mutagenesis 27 27 . . . Note=Fails to bind dsDNA. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12163470;Dbxref=PMID:12163470 O75531 UniProtKB Mutagenesis 27 27 . . . Note=Reduces binding to dsDNA. G->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12163470;Dbxref=PMID:12163470 O75531 UniProtKB Mutagenesis 29 29 . . . Note=No effect on histone H1/H3 binding. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16203725;Dbxref=PMID:16203725 O75531 UniProtKB Mutagenesis 32 32 . . . Note=No effect on histone H1/H3 binding. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16203725;Dbxref=PMID:16203725 O75531 UniProtKB Mutagenesis 33 33 . . . Note=No effect on histone H1/H3 binding. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16203725;Dbxref=PMID:16203725 O75531 UniProtKB Mutagenesis 37 37 . . . Note=No effect on histone H1/H3 binding. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15681850,ECO:0000269|PubMed:16203725;Dbxref=PMID:15681850,PMID:16203725 O75531 UniProtKB Mutagenesis 37 37 . . . Note=Reduces LEMD3/MAN1 binding. R->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15681850,ECO:0000269|PubMed:16203725;Dbxref=PMID:15681850,PMID:16203725 O75531 UniProtKB Mutagenesis 41 41 . . . Note=No effect on histone H1/H3 and LEMD3/MAN1 binding. K->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11005805,ECO:0000269|PubMed:15681850,ECO:0000269|PubMed:16203725;Dbxref=PMID:11005805,PMID:15681850,PMID:16203725 O75531 UniProtKB Mutagenesis 41 41 . . . Note=Reduces histone H1/H3 binding. K->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11005805,ECO:0000269|PubMed:15681850,ECO:0000269|PubMed:16203725;Dbxref=PMID:11005805,PMID:15681850,PMID:16203725 O75531 UniProtKB Mutagenesis 46 46 . . . Note=Complete loss of dsDNA%2C histone H1/H3 and LEMD3/MAN1 binding. L->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12163470,ECO:0000269|PubMed:15681850,ECO:0000269|PubMed:16203725;Dbxref=PMID:12163470,PMID:15681850,PMID:16203725 O75531 UniProtKB Mutagenesis 47 47 . . . Note=Abolishes homodimerization%2C 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%2C leading to innate immune activation. Complete loss of EMD%2C histone H1/H3 and LEMD3/MAN1 binding. G->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12163470,ECO:0000269|PubMed:15681850,ECO:0000269|PubMed:16203725,ECO:0000269|PubMed:28841419,ECO:0000269|PubMed:32792394;Dbxref=PMID:12163470,PMID:15681850,PMID:16203725,PMID:28841419,PMID:32792394 O75531 UniProtKB Mutagenesis 50 50 . . . Note=Reduces LEMD3/MAN1 binding. No effect on Histone H1/H3 binding. L->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11005805,ECO:0000269|PubMed:15681850,ECO:0000269|PubMed:16203725;Dbxref=PMID:11005805,PMID:15681850,PMID:16203725 O75531 UniProtKB Mutagenesis 50 50 . . . Note=Fails to promote HIV-1 genome integration. L->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11005805,ECO:0000269|PubMed:15681850,ECO:0000269|PubMed:16203725;Dbxref=PMID:11005805,PMID:15681850,PMID:16203725 O75531 UniProtKB Mutagenesis 51 51 . . . Note=Complete loss of EMD%2C and histone H1/H3 binding. Reduces dsDNA and LEMD3/MAN1 binding. V->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12163470,ECO:0000269|PubMed:15681850,ECO:0000269|PubMed:16203725;Dbxref=PMID:12163470,PMID:15681850,PMID:16203725 O75531 UniProtKB Mutagenesis 53 53 . . . Note=No effect on LEMD3/MAN1 binding. Enhances histone H1/H3 binding. K->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11005805,ECO:0000269|PubMed:12163470,ECO:0000269|PubMed:15681850,ECO:0000269|PubMed:16203725;Dbxref=PMID:11005805,PMID:12163470,PMID:15681850,PMID:16203725 O75531 UniProtKB Mutagenesis 53 53 . . . Note=Complete loss of EMD binding. Reduces LEMD3/MAN1 binding. Enhances histone H1/H3 binding. K->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11005805,ECO:0000269|PubMed:12163470,ECO:0000269|PubMed:15681850,ECO:0000269|PubMed:16203725;Dbxref=PMID:11005805,PMID:12163470,PMID:15681850,PMID:16203725 O75531 UniProtKB Mutagenesis 54 54 . . . Note=Reduces LEMD3/MAN1 binding. No effect on histone H1/H3 binding. K->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11005805,ECO:0000269|PubMed:12163470,ECO:0000269|PubMed:15681850,ECO:0000269|PubMed:16203725;Dbxref=PMID:11005805,PMID:12163470,PMID:15681850,PMID:16203725 O75531 UniProtKB Mutagenesis 54 54 . . . Note=Reduces binding to dsDNA. K->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11005805,ECO:0000269|PubMed:12163470,ECO:0000269|PubMed:15681850,ECO:0000269|PubMed:16203725;Dbxref=PMID:11005805,PMID:12163470,PMID:15681850,PMID:16203725 O75531 UniProtKB Mutagenesis 58 58 . . . Note=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. L->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:28841419,ECO:0000269|PubMed:32792394;Dbxref=PMID:28841419,PMID:32792394 O75531 UniProtKB Mutagenesis 60 60 . . . Note=No effect on histone H1/H3 binding. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16203725;Dbxref=PMID:16203725 O75531 UniProtKB Mutagenesis 62 62 . . . Note=Complete loss of LEMD3/MAN1 binding. Enhances histone H1/H3 binding. W->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11005805,ECO:0000269|PubMed:15681850,ECO:0000269|PubMed:16203725;Dbxref=PMID:11005805,PMID:15681850,PMID:16203725 O75531 UniProtKB Mutagenesis 64 64 . . . Note=Enhances histone H1/H3 binding. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16203725;Dbxref=PMID:16203725 O75531 UniProtKB Mutagenesis 75 75 . . . Note=Reduces binding to dsDNA. No effect on histone H1/H3 binding. R->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12163470,ECO:0000269|PubMed:16203725;Dbxref=PMID:12163470,PMID:16203725 O75531 UniProtKB Mutagenesis 80 80 . . . Note=No effect on histone H1/H3 and LEMD3/MAN1 binding. C->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11005805,ECO:0000269|PubMed:15681850,ECO:0000269|PubMed:16203725;Dbxref=PMID:11005805,PMID:15681850,PMID:16203725 O75531 UniProtKB Mutagenesis 82 82 . . . Note=No effect on histone H1/H3 binding. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16203725;Dbxref=PMID:16203725 O75531 UniProtKB Helix 3 11 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NDY O75531 UniProtKB Helix 20 22 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NDY O75531 UniProtKB Helix 28 36 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NDY O75531 UniProtKB Helix 42 51 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NDY O75531 UniProtKB Turn 52 54 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NDY O75531 UniProtKB Helix 56 67 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NDY O75531 UniProtKB Helix 71 88 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NDY