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Protein

Barrier-to-autointegration factor

Gene

Banf1

Organism
Mus musculus (Mouse)
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 non-specific dsDNA-binding sites which may promote DNA cross-bridging (By similarity).By similarity

GO - Molecular functioni

  • DNA binding Source: MGI

GO - Biological processi

  • DNA integration Source: MGI
  • establishment of integrated proviral latency Source: MGI
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Barrier-to-autointegration factor
Alternative name(s):
Breakpoint cluster region protein 1
LAP2-binding protein 1
Cleaved into the following chain:
Gene namesi
Name:Banf1
Synonyms:Baf, Bcrp1, L2bp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1346330. 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

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8989Barrier-to-autointegration factorPRO_0000221027Add
BLAST
Initiator methionineiRemoved; alternateBy similarity
Chaini2 – 8988Barrier-to-autointegration factor, N-terminally processedPRO_0000423191Add
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

EPDiO54962.
MaxQBiO54962.
PaxDbiO54962.
PRIDEiO54962.
TopDownProteomicsiO54962.

PTM databases

iPTMnetiO54962.
PhosphoSiteiO54962.

Expressioni

Gene expression databases

BgeeiO54962.
CleanExiMM_BANF1.
GenevisibleiO54962. MM.

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

IntActiO54962. 4 interactions.
MINTiMINT-4089048.
STRINGi10090.ENSMUSP00000025762.

Structurei

3D structure databases

ProteinModelPortaliO54962.
SMRiO54962. 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.
HOGENOMiHOG000231927.
HOVERGENiHBG029345.
InParanoidiO54962.
OMAiELFQEWM.
OrthoDBiEOG7HHWVW.
PhylomeDBiO54962.
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.

O54962-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTSQKHRDF VAEPMGEKPV GSLAGIGDVL SKRLEERGFD KAYVVLGQFL
60 70 80
VLKKDEDLFR EWLKDTCGAN AKQSRDCFGC LREWCDAFL
Length:89
Mass (Da):10,103
Last modified:June 1, 1998 - v1
Checksum:i828924AFCB91E0D0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF037080 mRNA. Translation: AAC40032.1.
AB025349 mRNA. Translation: BAA83102.1.
AK003025 mRNA. Translation: BAB22518.1.
AK004212 mRNA. Translation: BAB23223.1.
AK010257 mRNA. Translation: BAB26800.1.
AK011079 mRNA. Translation: BAB27383.1.
AK011100 mRNA. Translation: BAB27397.1.
AK012588 mRNA. Translation: BAB28337.1.
AK088896 mRNA. Translation: BAC40639.1.
BC003709 mRNA. Translation: AAH03709.1.
CCDSiCCDS29458.1.
RefSeqiNP_001033320.1. NM_001038231.2.
NP_001273537.1. NM_001286608.1.
NP_035923.1. NM_011793.3.
XP_011246930.1. XM_011248628.1.
UniGeneiMm.358649.

Genome annotation databases

EnsembliENSMUST00000025762; ENSMUSP00000025762; ENSMUSG00000024844.
ENSMUST00000170010; ENSMUSP00000126202; ENSMUSG00000024844.
GeneIDi23825.
KEGGimmu:23825.
UCSCiuc008gcr.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF037080 mRNA. Translation: AAC40032.1.
AB025349 mRNA. Translation: BAA83102.1.
AK003025 mRNA. Translation: BAB22518.1.
AK004212 mRNA. Translation: BAB23223.1.
AK010257 mRNA. Translation: BAB26800.1.
AK011079 mRNA. Translation: BAB27383.1.
AK011100 mRNA. Translation: BAB27397.1.
AK012588 mRNA. Translation: BAB28337.1.
AK088896 mRNA. Translation: BAC40639.1.
BC003709 mRNA. Translation: AAH03709.1.
CCDSiCCDS29458.1.
RefSeqiNP_001033320.1. NM_001038231.2.
NP_001273537.1. NM_001286608.1.
NP_035923.1. NM_011793.3.
XP_011246930.1. XM_011248628.1.
UniGeneiMm.358649.

3D structure databases

ProteinModelPortaliO54962.
SMRiO54962. Positions 1-89.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO54962. 4 interactions.
MINTiMINT-4089048.
STRINGi10090.ENSMUSP00000025762.

PTM databases

iPTMnetiO54962.
PhosphoSiteiO54962.

Proteomic databases

EPDiO54962.
MaxQBiO54962.
PaxDbiO54962.
PRIDEiO54962.
TopDownProteomicsiO54962.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025762; ENSMUSP00000025762; ENSMUSG00000024844.
ENSMUST00000170010; ENSMUSP00000126202; ENSMUSG00000024844.
GeneIDi23825.
KEGGimmu:23825.
UCSCiuc008gcr.2. mouse.

Organism-specific databases

CTDi8815.
MGIiMGI:1346330. Banf1.

Phylogenomic databases

eggNOGiKOG4233. Eukaryota.
ENOG4111URU. LUCA.
GeneTreeiENSGT00390000018613.
HOGENOMiHOG000231927.
HOVERGENiHBG029345.
InParanoidiO54962.
OMAiELFQEWM.
OrthoDBiEOG7HHWVW.
PhylomeDBiO54962.
TreeFamiTF315060.

Enzyme and pathway databases

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

Miscellaneous databases

PROiO54962.
SOURCEiSearch...

Gene expression databases

BgeeiO54962.
CleanExiMM_BANF1.
GenevisibleiO54962. MM.

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. "A previously unidentified host protein protects retroviral DNA from autointegration."
    Lee M.S., Craigie R.
    Proc. Natl. Acad. Sci. U.S.A. 95:1528-1533(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "LAP2 binding protein 1 (L2BP1/BAF) is a candidate mediator of LAP2-chromatin interaction."
    Furukawa K.
    J. Cell Sci. 112:2485-2492(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH TMPO.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Liver and Thymus.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Heart, Lung and Testis.

Entry informationi

Entry nameiBAF_MOUSE
AccessioniPrimary (citable) accession number: O54962
Secondary accession number(s): Q542E6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: June 1, 1998
Last modified: June 8, 2016
This is version 116 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.