O54962 · BAF_MOUSE
- ProteinBarrier-to-autointegration factor
- GeneBanf1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids
- Protein existenceEvidence at protein level
- Annotation score5/5
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 (By similarity).
Contains two non-specific double-stranded DNA (dsDNA)-binding sites which promote DNA cross-bridging (By similarity).
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 (By similarity).
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 (By similarity).
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:32156810).
Outcompetes CGAS for DNA-binding, thereby preventing CGAS activation and subsequent damaging autoinflammatory responses (By similarity).
Also involved in DNA damage response: interacts with PARP1 in response to oxidative stress, thereby inhibiting the ADP-ribosyltransferase activity of PARP1 (By similarity).
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 (By similarity).
Contains two non-specific double-stranded DNA (dsDNA)-binding sites which promote DNA cross-bridging (By similarity).
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 (By similarity).
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 (By similarity).
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:32156810).
Outcompetes CGAS for DNA-binding, thereby preventing CGAS activation and subsequent damaging autoinflammatory responses (By similarity).
Also involved in DNA damage response: interacts with PARP1 in response to oxidative stress, thereby inhibiting the ADP-ribosyltransferase activity of PARP1 (By similarity).
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 (By similarity).
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chromatin | |
Cellular Component | condensed chromosome | |
Cellular Component | cytosol | |
Cellular Component | nuclear envelope | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | DNA binding | |
Molecular Function | double-stranded DNA binding | |
Molecular Function | identical protein binding | |
Molecular Function | protein homodimerization activity | |
Biological Process | chromatin organization | |
Biological Process | chromosome organization | |
Biological Process | DNA integration | |
Biological Process | establishment of integrated proviral latency | |
Biological Process | mitotic nuclear membrane reassembly | |
Biological Process | negative regulation of cGAS/STING signaling pathway | |
Biological Process | negative regulation of innate immune response | |
Biological Process | negative regulation of protein ADP-ribosylation | |
Biological Process | negative regulation of type I interferon production | |
Biological Process | negative regulation of viral genome replication | |
Biological Process | response to oxidative stress |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBarrier-to-autointegration factor
- Alternative names
- Cleaved into 1 chains
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionO54962
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
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) shows a cytoplasmic localization whereas the unphosphorylated form locates almost exclusively in the nucleus. May be included in HIV-1 virions via its interaction with viral GAG polyprotein.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed; alternate | ||||
Sequence: M | ||||||
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000423191 | 1-89 | Barrier-to-autointegration factor | |||
Sequence: MTTSQKHRDFVAEPMGEKPVGSLAGIGDVLSKRLEERGFDKAYVVLGQFLVLKKDEDLFREWLKDTCGANAKQSRDCFGCLREWCDAFL | ||||||
Modified residue | 2 | N-acetylthreonine; in Barrier-to-autointegration factor, N-terminally processed | ||||
Sequence: T | ||||||
Modified residue | 2 | Phosphothreonine; by VRK1 and VRK2 | ||||
Sequence: T | ||||||
Chain | PRO_0000221027 | 2-89 | Barrier-to-autointegration factor, N-terminally processed | |||
Sequence: TTSQKHRDFVAEPMGEKPVGSLAGIGDVLSKRLEERGFDKAYVVLGQFLVLKKDEDLFREWLKDTCGANAKQSRDCFGCLREWCDAFL | ||||||
Modified residue | 3 | Phosphothreonine; by VRK1 and VRK2 | ||||
Sequence: T | ||||||
Modified residue | 4 | Phosphoserine; by VRK1 and VRK2 | ||||
Sequence: S |
Post-translational modification
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.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Homodimer. Heterodimerizes with BANF2. 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. Interacts with LEMD2 (via LEM domain). Interacts with PARP1; interaction takes place in response to oxidative DNA damage.
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 20-35 | HhH | ||||
Sequence: VGSLAGIGDVLSKRLE |
Domain
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.
Sequence similarities
Belongs to the BAF family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length89
- Mass (Da)10,103
- Last updated1998-06-01 v1
- Checksum828924AFCB91E0D0
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF037080 EMBL· GenBank· DDBJ | AAC40032.1 EMBL· GenBank· DDBJ | mRNA | ||
AB025349 EMBL· GenBank· DDBJ | BAA83102.1 EMBL· GenBank· DDBJ | mRNA | ||
AK003025 EMBL· GenBank· DDBJ | BAB22518.1 EMBL· GenBank· DDBJ | mRNA | ||
AK004212 EMBL· GenBank· DDBJ | BAB23223.1 EMBL· GenBank· DDBJ | mRNA | ||
AK010257 EMBL· GenBank· DDBJ | BAB26800.1 EMBL· GenBank· DDBJ | mRNA | ||
AK011079 EMBL· GenBank· DDBJ | BAB27383.1 EMBL· GenBank· DDBJ | mRNA | ||
AK011100 EMBL· GenBank· DDBJ | BAB27397.1 EMBL· GenBank· DDBJ | mRNA | ||
AK012588 EMBL· GenBank· DDBJ | BAB28337.1 EMBL· GenBank· DDBJ | mRNA | ||
AK088896 EMBL· GenBank· DDBJ | BAC40639.1 EMBL· GenBank· DDBJ | mRNA | ||
BC003709 EMBL· GenBank· DDBJ | AAH03709.1 EMBL· GenBank· DDBJ | mRNA |