Banf1
entrez
114087
canonical
uniprot
Q9R1T1
canonical
ensembl
ENSRNOG00000020460
resolver
ensembl
ENSRNOG00055021151
resolver
ensembl
ENSRNOG00060025348
resolver
ensembl
ENSRNOG00065033671
resolver
ensp
ENSRNOP00000027734
resolver
ensp
ENSRNOP00055029351
resolver
ensp
ENSRNOP00060036420
resolver
ensp
ENSRNOP00065047623
resolver
enst
ENSRNOT00000027734
resolver
enst
ENSRNOT00055036139
resolver
enst
ENSRNOT00060043889
resolver
enst
ENSRNOT00065057838
resolver
genesymbol
Banf1
resolver
genesymbol_syn
Baf
resolver
genesymbol_syn
L2bp1
resolver
uniprot_entry
BAF_RAT
resolver
amino_acid_sequence
MTTSQKHRDFVAEPMGEKPVGSLAGIGDALGKRLEERGFDKAYVVLGQFLVLKKDEDLFREWLKDTCGANAKQSRDCFGCLREWCDAFL
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. Contains two non-specific double-stranded DNA (dsDNA)-binding sites which promote DNA cross-bridging. 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. 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. Also acts as a negative regulator of innate immune activation by restricting CGAS activity toward self-DNA upon acute loss of nuclear membrane integrity. Outcompetes CGAS for DNA-binding, thereby preventing CGAS activation and subsequent damaging autoinflammatory responses. Also involved in DNA damage response: interacts with PARP1 in response to oxidative stress, thereby inhibiting the ADP-ribosyltransferase activity of PARP1. 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. {ECO:0000250|UniProtKB:O75531}.
uniprot
proteins
mass_dalton
10045
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:0000250|UniProtKB:O75531}.
uniprot
proteins
protein_family
BAF family
uniprot
proteins
pubmed
10393804
uniprot
proteins
pubmed
15489334
uniprot
proteins
sequence_length
89
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75531}. Chromosome {ECO:0000250|UniProtKB:O75531}. Nucleus envelope {ECO:0000250|UniProtKB:O75531}. Cytoplasm {ECO:0000250|UniProtKB:O75531}. 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. {ECO:0000250|UniProtKB:O75531}.
uniprot
proteins