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Protein

Barrier-to-autointegration factor

Gene

BANF1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Barrier-to-autointegration factor
Cleaved into the following chain:
Gene namesi
Name:BANF1
Synonyms:BAF
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 29

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

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8989Barrier-to-autointegration factorPRO_0000221025Add
BLAST
Initiator methionineiRemoved; alternateBy similarity
Chaini2 – 8988Barrier-to-autointegration factor, N-terminally processedPRO_0000423189Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei2 – 21N-acetylthreonine; in Barrier-to-autointegration factor, N-terminally processedBy similarity
Modified residuei2 – 21Phosphothreonine; by VRK1 and VRK2By similarity
Modified residuei3 – 31Phosphothreonine; by VRK1 and VRK2By similarity
Modified residuei4 – 41Phosphoserine; by VRK1 and VRK2By similarity

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

PaxDbiP61283.
PRIDEiP61283.

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 CRX and LMNA (lamin-A). Binds linker histone H1.1 and core histones H3 with in vitro affinities of 500-900 and 100-200 nM (By similarity).By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000042612.

Structurei

3D structure databases

ProteinModelPortaliP61283.
SMRiP61283. Positions 1-89.
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.
HOVERGENiHBG029345.
InParanoidiP61283.
OMAiELFQEWM.
OrthoDBiEOG7HHWVW.
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.

P61283-1 [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:May 10, 2004 - v1
Checksum:i9A2180A2D284F5D0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF529228 mRNA. Translation: AAQ09227.1.
BT020975 mRNA. Translation: AAX08992.1.
RefSeqiNP_892033.1. NM_182988.3.
UniGeneiBt.103867.

Genome annotation databases

EnsembliENSBTAT00000045202; ENSBTAP00000042612; ENSBTAG00000031875.
GeneIDi360196.
KEGGibta:360196.
bta:785958.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF529228 mRNA. Translation: AAQ09227.1.
BT020975 mRNA. Translation: AAX08992.1.
RefSeqiNP_892033.1. NM_182988.3.
UniGeneiBt.103867.

3D structure databases

ProteinModelPortaliP61283.
SMRiP61283. Positions 1-89.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000042612.

Proteomic databases

PaxDbiP61283.
PRIDEiP61283.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000045202; ENSBTAP00000042612; ENSBTAG00000031875.
GeneIDi360196.
KEGGibta:360196.
bta:785958.

Organism-specific databases

CTDi8815.

Phylogenomic databases

eggNOGiKOG4233. Eukaryota.
ENOG4111URU. LUCA.
GeneTreeiENSGT00390000018613.
HOVERGENiHBG029345.
InParanoidiP61283.
OMAiELFQEWM.
OrthoDBiEOG7HHWVW.
TreeFamiTF315060.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi20812796.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Barrier-to-autointegration factor (Baf) interacts with cone-rod homeobox (Crx) and represses its transactivation function."
    Wang X., Xu S., Rivolta C., Li L.Y., Peng G.-H., Swain P.K., Sung C.-H., Swaroop A., Berson E.L., Dryja T.P., Chen S.
    Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Entry informationi

Entry nameiBAF_BOVIN
AccessioniPrimary (citable) accession number: P61283
Secondary accession number(s): Q5E9E5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: May 11, 2016
This is version 92 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, 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.