Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Barrier-to-autointegration factor

Gene

BANF1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. 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.3 Publications

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • enzyme binding Source: UniProtKB
  • LEM domain binding Source: UniProtKB
  • protein C-terminus binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein N-terminus binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000175334-MONOMER.
ReactomeiR-HSA-162592. Integration of provirus.
R-HSA-164843. 2-LTR circle formation.
R-HSA-175567. Integration of viral DNA into host genomic DNA.
R-HSA-177539. Autointegration results in viral DNA circles.
R-HSA-180689. APOBEC3G mediated resistance to HIV-1 infection.
R-HSA-180910. Vpr-mediated nuclear import of PICs.
R-HSA-2993913. Clearance of Nuclear Envelope Membranes from Chromatin.
R-HSA-2995383. Initiation of Nuclear Envelope Reformation.
SIGNORiO75531.

Names & Taxonomyi

Protein namesi
Recommended name:
Barrier-to-autointegration factor
Alternative name(s):
Breakpoint cluster region protein 1
Cleaved into the following chain:
Gene namesi
Name:BANF1
Synonyms:BAF, BCRG1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:17397. BANF1.

Subcellular locationi

  • Nucleus 1 Publication
  • Cytoplasm 1 Publication
  • Chromosome 1 Publication

  • Note: Significantly enriched at the nuclear inner membrane, diffusely throughout the nucleus during interphase and concentrated at the chromosomes during the M-phase. May be included in HIV-1 virions via its interaction with viral GAG polyprotein. The phosphorylated form (by VRK1) shows a cytoplasmic localization.

GO - Cellular componenti

  • condensed chromosome Source: Ensembl
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Nestor-Guillermo progeria syndrome (NGPS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:614008
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06595412A → T in NGPS; shows a dramatic reduction in BANF1 protein levels indicating that the mutation impairs protein stability. 1 PublicationCorresponds to variant rs387906871dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi4S → A: Complete loss of phosphorylation. 1 Publication1
Mutagenesisi4S → E: Complete loss of phosphorylation and mislocalization of EMD in nucleus. 1 Publication1
Mutagenesisi6K → A: Complete loss of LEMD3/MAN1 and histone H1/H3 binding. 4 Publications1
Mutagenesisi6K → E: Complete loss of dsDNA and LEMD3/MAN1 binding. 4 Publications1
Mutagenesisi8R → A: Enhances histone H1/H3 binding. 2 Publications1
Mutagenesisi8R → E: Complete loss of LEMD3/MAN1 binding. 2 Publications1
Mutagenesisi9D → A: Reduces binding to dsDNA, LEMD3/MAN1 and histone H1/H3. 3 Publications1
Mutagenesisi14P → A: No effect on LEMD3/MAN1 and enhances histone H1/H3 binding. 3 Publications1
Mutagenesisi18K → A: No effect on histone H1/H3 binding. 2 Publications1
Mutagenesisi25G → E: Complete loss of dsDNA, EMD, histone H1/H3 and LEMD3/MAN1 binding. 3 Publications1
Mutagenesisi25G → Q: Complete loss of EMD binding and reduces dsDNA binding. 3 Publications1
Mutagenesisi26I → A: Reduces histone H1/H3 and LEMD3/MAN1 binding. Fails to promote HIV-1 genome integration. 3 Publications1
Mutagenesisi26I → K: Fails to promote HIV-1 genome integration. 3 Publications1
Mutagenesisi27G → E: Fails to bind dsDNA. 1 Publication1
Mutagenesisi27G → Q: Reduces binding to dsDNA. 1 Publication1
Mutagenesisi29V → A: No effect on histone H1/H3 binding. 1 Publication1
Mutagenesisi32K → E: No effect on histone H1/H3 binding. 1 Publication1
Mutagenesisi33K → E: No effect on histone H1/H3 binding. 1 Publication1
Mutagenesisi37R → A: No effect on histone H1/H3 binding. 2 Publications1
Mutagenesisi37R → E: Reduces LEMD3/MAN1 binding. 2 Publications1
Mutagenesisi41K → A: No effect on histone H1/H3 and LEMD3/MAN1 binding. 3 Publications1
Mutagenesisi41K → E: Reduces histone H1/H3 binding. 3 Publications1
Mutagenesisi46L → E: Complete loss of dsDNA, histone H1/H3 and LEMD3/MAN1 binding. 3 Publications1
Mutagenesisi47G → E: Complete loss of EMD, histone H1/h3 and LEMD3/MAN1 binding. 3 Publications1
Mutagenesisi50L → A: Reduces LEMD3/MAN1 binding. No effect on Histone H1/H3 binding. 3 Publications1
Mutagenesisi50L → K: Fails to promote HIV-1 genome integration. 3 Publications1
Mutagenesisi51V → E: Complete loss of EMD, and histone H1/H3 binding. Reduces dsDNA and LEMD3/MAN1 binding. 3 Publications1
Mutagenesisi53K → A: No effect on LEMD3/MAN1 binding. Enhances histone H1/H3 binding. 4 Publications1
Mutagenesisi53K → E: Complete loss of EMD binding. Reduces LEMD3/MAN1 binding. Enhances histone H1/H3 binding. 4 Publications1
Mutagenesisi54K → A: Reduces LEMD3/MAN1 binding. No effect on histone H1/H3 binding. 4 Publications1
Mutagenesisi54K → E: Reduces binding to dsDNA. 4 Publications1
Mutagenesisi60R → E: No effect on histone H1/H3 binding. 1 Publication1
Mutagenesisi62W → A: Complete loss of LEMD3/MAN1 binding. Enhances histone H1/H3 binding. 3 Publications1
Mutagenesisi64K → E: Enhances histone H1/H3 binding. 1 Publication1
Mutagenesisi75R → E: Reduces binding to dsDNA. No effect on histone H1/H3 binding. 2 Publications1
Mutagenesisi80C → A: No effect on histone H1/H3 and LEMD3/MAN1 binding. 3 Publications1
Mutagenesisi82R → E: No effect on histone H1/H3 binding. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi8815.
MalaCardsiBANF1.
MIMi614008. phenotype.
OpenTargetsiENSG00000175334.
Orphaneti280576. Nestor-Guillermo progeria syndrome.
PharmGKBiPA134903639.

Polymorphism and mutation databases

BioMutaiBANF1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004231901 – 89Barrier-to-autointegration factorAdd BLAST89
Initiator methionineiRemoved; alternateCombined sources
ChainiPRO_00002210262 – 89Barrier-to-autointegration factor, N-terminally processedAdd BLAST88

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei2N-acetylthreonine; in Barrier-to-autointegration factor, N-terminally processedCombined sources1
Modified residuei2Phosphothreonine; by VRK1 and VRK21 Publication1
Modified residuei3Phosphothreonine; by VRK1 and VRK21 Publication1
Modified residuei4Phosphoserine; by VRK1 and VRK22 Publications1

Post-translational modificationi

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.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO75531.
MaxQBiO75531.
PaxDbiO75531.
PeptideAtlasiO75531.
PRIDEiO75531.
TopDownProteomicsiO75531.

PTM databases

iPTMnetiO75531.
PhosphoSitePlusiO75531.
SwissPalmiO75531.

Expressioni

Tissue specificityi

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.

Gene expression databases

BgeeiENSG00000175334.
CleanExiHS_BANF1.
ExpressionAtlasiO75531. baseline and differential.
GenevisibleiO75531. HS.

Organism-specific databases

HPAiCAB032896.
HPA039242.

Interactioni

Subunit structurei

Homodimer (PubMed:16337940, PubMed:22399800). Heterodimerizes with BAFL (PubMed:16337940). Interacts with ANKLE2/LEM4, leading to decreased phosphorylation by VRK1 and promoting dephosphorylation by protein phosphatase 2A (PP2A) (PubMed:22770216). 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) (PubMed:11792822, PubMed:15681850). Interacts with ANKLE1 (via LEM domain); the interaction may favor BANF1 dimerization (PubMed:22399800). Interacts with CRX and LMNA (lamin-A). Binds linker histone H1.1 and core histones H3 (PubMed:16203725). Interacts with HIV-1 pre-integration complex in cytoplasm by binding to viral matrix protein and Gag polyprotein (PubMed:12663813, PubMed:14645565).8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EMDP504023EBI-1055977,EBI-489887

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • LEM domain binding Source: UniProtKB
  • protein C-terminus binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein N-terminus binding Source: UniProtKB

Protein-protein interaction databases

BioGridi114342. 71 interactors.
DIPiDIP-50395N.
IntActiO75531. 15 interactors.
MINTiMINT-5002289.
STRINGi9606.ENSP00000310275.

Structurei

Secondary structure

189
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 11Combined sources7
Helixi20 – 22Combined sources3
Helixi28 – 36Combined sources9
Helixi42 – 51Combined sources10
Turni52 – 54Combined sources3
Helixi56 – 67Combined sources12
Helixi71 – 88Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CI4X-ray1.90A/B1-89[»]
1QCKNMR-A/B1-89[»]
2BZFX-ray2.87A1-89[»]
2EZXNMR-A/B1-89[»]
2EZYNMR-A/B1-89[»]
2EZZNMR-A/B1-89[»]
2ODGNMR-A/B1-89[»]
ProteinModelPortaliO75531.
SMRiO75531.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75531.

Family & Domainsi

Domaini

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, whereas DNA binds to the left and right sides.

Sequence similaritiesi

Belongs to the BAF family.Curated

Phylogenomic databases

eggNOGiKOG4233. Eukaryota.
ENOG4111URU. LUCA.
GeneTreeiENSGT00390000018613.
HOVERGENiHBG029345.
InParanoidiO75531.
OMAiELFQEWM.
OrthoDBiEOG091G109J.
PhylomeDBiO75531.
TreeFamiTF315060.

Family and domain databases

Gene3Di1.10.150.40. 1 hit.
InterProiIPR004122. BAF_prot.
[Graphical view]
PANTHERiPTHR12912. PTHR12912. 1 hit.
PfamiPF02961. BAF. 1 hit.
[Graphical view]
ProDomiPD019964. PD019964. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM01023. BAF. 1 hit.
[Graphical view]
SUPFAMiSSF47798. SSF47798. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O75531-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTSQKHRDF VAEPMGEKPV GSLAGIGEVL GKKLEERGFD KAYVVLGQFL
60 70 80
VLKKDEDLFR EWLKDTCGAN AKQSRDCFGC LREWCDAFL
Length:89
Mass (Da):10,059
Last modified:November 1, 1998 - v1
Checksum:i9A2180A2D284F5D0
GO

Sequence cautioni

The sequence AAC08964 differs from that shown. Reason: Frameshift at position 87.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06595412A → T in NGPS; shows a dramatic reduction in BANF1 protein levels indicating that the mutation impairs protein stability. 1 PublicationCorresponds to variant rs387906871dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF070447 mRNA. Translation: AAC23575.1.
AF044773 mRNA. Translation: AAC08964.1. Frameshift.
AF068235 mRNA. Translation: AAD15901.1.
CR542140 mRNA. Translation: CAG46937.1.
BC005942 mRNA. Translation: AAH05942.1.
BC107702 mRNA. Translation: AAI07703.1.
CCDSiCCDS8125.1.
RefSeqiNP_001137457.1. NM_001143985.1.
NP_003851.1. NM_003860.3.
XP_016874003.1. XM_017018514.1.
XP_016874004.1. XM_017018515.1.
UniGeneiHs.433759.

Genome annotation databases

EnsembliENST00000312175; ENSP00000310275; ENSG00000175334.
ENST00000445560; ENSP00000416128; ENSG00000175334.
ENST00000527348; ENSP00000432867; ENSG00000175334.
ENST00000533166; ENSP00000433760; ENSG00000175334.
GeneIDi8815.
KEGGihsa:8815.
UCSCiuc001ogo.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF070447 mRNA. Translation: AAC23575.1.
AF044773 mRNA. Translation: AAC08964.1. Frameshift.
AF068235 mRNA. Translation: AAD15901.1.
CR542140 mRNA. Translation: CAG46937.1.
BC005942 mRNA. Translation: AAH05942.1.
BC107702 mRNA. Translation: AAI07703.1.
CCDSiCCDS8125.1.
RefSeqiNP_001137457.1. NM_001143985.1.
NP_003851.1. NM_003860.3.
XP_016874003.1. XM_017018514.1.
XP_016874004.1. XM_017018515.1.
UniGeneiHs.433759.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CI4X-ray1.90A/B1-89[»]
1QCKNMR-A/B1-89[»]
2BZFX-ray2.87A1-89[»]
2EZXNMR-A/B1-89[»]
2EZYNMR-A/B1-89[»]
2EZZNMR-A/B1-89[»]
2ODGNMR-A/B1-89[»]
ProteinModelPortaliO75531.
SMRiO75531.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114342. 71 interactors.
DIPiDIP-50395N.
IntActiO75531. 15 interactors.
MINTiMINT-5002289.
STRINGi9606.ENSP00000310275.

PTM databases

iPTMnetiO75531.
PhosphoSitePlusiO75531.
SwissPalmiO75531.

Polymorphism and mutation databases

BioMutaiBANF1.

Proteomic databases

EPDiO75531.
MaxQBiO75531.
PaxDbiO75531.
PeptideAtlasiO75531.
PRIDEiO75531.
TopDownProteomicsiO75531.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000312175; ENSP00000310275; ENSG00000175334.
ENST00000445560; ENSP00000416128; ENSG00000175334.
ENST00000527348; ENSP00000432867; ENSG00000175334.
ENST00000533166; ENSP00000433760; ENSG00000175334.
GeneIDi8815.
KEGGihsa:8815.
UCSCiuc001ogo.4. human.

Organism-specific databases

CTDi8815.
DisGeNETi8815.
GeneCardsiBANF1.
HGNCiHGNC:17397. BANF1.
HPAiCAB032896.
HPA039242.
MalaCardsiBANF1.
MIMi603811. gene.
614008. phenotype.
neXtProtiNX_O75531.
OpenTargetsiENSG00000175334.
Orphaneti280576. Nestor-Guillermo progeria syndrome.
PharmGKBiPA134903639.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4233. Eukaryota.
ENOG4111URU. LUCA.
GeneTreeiENSGT00390000018613.
HOVERGENiHBG029345.
InParanoidiO75531.
OMAiELFQEWM.
OrthoDBiEOG091G109J.
PhylomeDBiO75531.
TreeFamiTF315060.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000175334-MONOMER.
ReactomeiR-HSA-162592. Integration of provirus.
R-HSA-164843. 2-LTR circle formation.
R-HSA-175567. Integration of viral DNA into host genomic DNA.
R-HSA-177539. Autointegration results in viral DNA circles.
R-HSA-180689. APOBEC3G mediated resistance to HIV-1 infection.
R-HSA-180910. Vpr-mediated nuclear import of PICs.
R-HSA-2993913. Clearance of Nuclear Envelope Membranes from Chromatin.
R-HSA-2995383. Initiation of Nuclear Envelope Reformation.
SIGNORiO75531.

Miscellaneous databases

EvolutionaryTraceiO75531.
GeneWikiiBarrier_to_autointegration_factor_1.
GenomeRNAii8815.
PROiO75531.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000175334.
CleanExiHS_BANF1.
ExpressionAtlasiO75531. baseline and differential.
GenevisibleiO75531. HS.

Family and domain databases

Gene3Di1.10.150.40. 1 hit.
InterProiIPR004122. BAF_prot.
[Graphical view]
PANTHERiPTHR12912. PTHR12912. 1 hit.
PfamiPF02961. BAF. 1 hit.
[Graphical view]
ProDomiPD019964. PD019964. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM01023. BAF. 1 hit.
[Graphical view]
SUPFAMiSSF47798. SSF47798. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiBAF_HUMAN
AccessioniPrimary (citable) accession number: O75531
Secondary accession number(s): O60558, Q6FGG7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: November 30, 2016
This is version 160 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.