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Protein

Barrier-to-autointegration factor

Gene

Banf1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 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 nons-pecific dsDNA-binding sites which may promote DNA cross-bridging (By similarity).By similarity

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • protein homodimerization activity Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-RNO-2993913. Clearance of Nuclear Envelope Membranes from Chromatin.
R-RNO-2995383. Initiation of Nuclear Envelope Reformation.

Names & Taxonomyi

Protein namesi
Recommended name:
Barrier-to-autointegration factor
Alternative name(s):
LAP2-binding protein 1
Cleaved into the following chain:
Gene namesi
Name:Banf1
Synonyms:Baf, Bcrp1, L2bp1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi620662. Banf1.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm By similarity
  • Chromosome By similarity

  • 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 (By similarity).By similarity

GO - Cellular componenti

  • condensed chromosome Source: RGD
  • cytoplasm Source: UniProtKB-SubCell
  • extracellular exosome Source: Ensembl
  • nucleoplasm Source: Ensembl
  • nucleus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002210291 – 89Barrier-to-autointegration factorAdd BLAST89
Initiator methionineiRemoved; alternateBy similarity
ChainiPRO_00004231932 – 89Barrier-to-autointegration factor, N-terminally processedAdd BLAST88

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei2N-acetylthreonine; in Barrier-to-autointegration factor, N-terminally processedBy similarity1
Modified residuei2Phosphothreonine; by VRK1 and VRK2By similarity1
Modified residuei3Phosphothreonine; by VRK1 and VRK2By similarity1
Modified residuei4Phosphoserine; by VRK1 and VRK2By similarity1

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 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ9R1T1.
PRIDEiQ9R1T1.

PTM databases

iPTMnetiQ9R1T1.
PhosphoSitePlusiQ9R1T1.

Expressioni

Gene expression databases

BgeeiENSRNOG00000020460.
GenevisibleiQ9R1T1. RN.

Interactioni

Subunit structurei

Homodimer. Heterodimerizes with BAFL. 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.By similarity

GO - Molecular functioni

  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

MINTiMINT-4998435.
STRINGi10116.ENSRNOP00000027734.

Structurei

3D structure databases

ProteinModelPortaliQ9R1T1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

Has a helix-hairpin-helix (HhH) structural motif conserved among proteins that bind non-specifically to DNA.By similarity
LEM domain proteins bind centrally on the BAF dimer, whereas DNA binds to the left and right sides.By similarity

Sequence similaritiesi

Belongs to the BAF family.Curated

Phylogenomic databases

eggNOGiKOG4233. Eukaryota.
ENOG4111URU. LUCA.
GeneTreeiENSGT00390000018613.
HOGENOMiHOG000231927.
HOVERGENiHBG029345.
InParanoidiQ9R1T1.
OMAiELFQEWM.
OrthoDBiEOG091G109J.
PhylomeDBiQ9R1T1.
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.

Q9R1T1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTSQKHRDF VAEPMGEKPV GSLAGIGDAL GKRLEERGFD KAYVVLGQFL
60 70 80
VLKKDEDLFR EWLKDTCGAN AKQSRDCFGC LREWCDAFL
Length:89
Mass (Da):10,045
Last modified:May 1, 2000 - v1
Checksum:i9D9930BBDC92F4C7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB024333 mRNA. Translation: BAA83101.1.
BC084726 mRNA. Translation: AAH84726.1.
RefSeqiNP_446083.1. NM_053631.3.
XP_006230692.1. XM_006230630.3.
XP_006230693.1. XM_006230631.1.
UniGeneiRn.19921.

Genome annotation databases

EnsembliENSRNOT00000027734; ENSRNOP00000027734; ENSRNOG00000020460.
GeneIDi114087.
KEGGirno:114087.
UCSCiRGD:620662. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB024333 mRNA. Translation: BAA83101.1.
BC084726 mRNA. Translation: AAH84726.1.
RefSeqiNP_446083.1. NM_053631.3.
XP_006230692.1. XM_006230630.3.
XP_006230693.1. XM_006230631.1.
UniGeneiRn.19921.

3D structure databases

ProteinModelPortaliQ9R1T1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4998435.
STRINGi10116.ENSRNOP00000027734.

PTM databases

iPTMnetiQ9R1T1.
PhosphoSitePlusiQ9R1T1.

Proteomic databases

PaxDbiQ9R1T1.
PRIDEiQ9R1T1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000027734; ENSRNOP00000027734; ENSRNOG00000020460.
GeneIDi114087.
KEGGirno:114087.
UCSCiRGD:620662. rat.

Organism-specific databases

CTDi8815.
RGDi620662. Banf1.

Phylogenomic databases

eggNOGiKOG4233. Eukaryota.
ENOG4111URU. LUCA.
GeneTreeiENSGT00390000018613.
HOGENOMiHOG000231927.
HOVERGENiHBG029345.
InParanoidiQ9R1T1.
OMAiELFQEWM.
OrthoDBiEOG091G109J.
PhylomeDBiQ9R1T1.
TreeFamiTF315060.

Enzyme and pathway databases

ReactomeiR-RNO-2993913. Clearance of Nuclear Envelope Membranes from Chromatin.
R-RNO-2995383. Initiation of Nuclear Envelope Reformation.

Miscellaneous databases

PROiQ9R1T1.

Gene expression databases

BgeeiENSRNOG00000020460.
GenevisibleiQ9R1T1. RN.

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_RAT
AccessioniPrimary (citable) accession number: Q9R1T1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: May 1, 2000
Last modified: November 2, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.