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Protein

Barrier-to-autointegration factor

Gene

BANF1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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. Exploited by retroviruses for inhibiting self-destructing autointegration of retroviral DNA, thereby promoting integration of viral DNA into the host chromosome. EMD and BAF are cooperative cofactors of HIV-1 infection. Association of EMD with the viral DNA requires the presence of BAF and viral integrase. The association of viral DNA with chromatin requires the presence of BAF and EMD.3 Publications

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW

GO - Biological processi

  1. DNA integration Source: Ensembl
  2. establishment of integrated proviral latency Source: Reactome
  3. mitotic cell cycle Source: Reactome
  4. mitotic nuclear envelope disassembly Source: Reactome
  5. mitotic nuclear envelope reassembly Source: Reactome
  6. response to virus Source: ProtInc
  7. viral process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_160242. Initiation of Nuclear Envelope Reformation.
REACT_160251. Clearance of Nuclear Envelope Membranes from Chromatin.
REACT_6866. Autointegration results in viral DNA circles.
REACT_6918. Integration of provirus.
REACT_7991. Vpr-mediated nuclear import of PICs.
REACT_8990. Integration of viral DNA into host genomic DNA.
REACT_9058. 2-LTR circle formation.
REACT_9406. APOBEC3G mediated resistance to HIV-1 infection.

Names & Taxonomyi

Protein namesi
Recommended name:
Barrier-to-autointegration factor
Alternative name(s):
Breakpoint cluster region protein 1
Cleaved into the following chain:
Gene namesi
Name:BANF1
Synonyms:BAF, BCRG1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:17397. BANF1.

Subcellular locationi

Nucleus 1 Publication. Cytoplasm 1 Publication. Chromosome 1 Publication
Note: Significantly enriched at the nuclear inner membrane, diffusely throughout the nucleus during interphase and concentrated at the chromosomes during the M-phase. May be included in HIV-1 virions via its interaction with viral GAG polyprotein. The phosphorylated form (by VRK1) shows a cytoplasmic localization.

GO - Cellular componenti

  1. chromosome Source: UniProtKB-SubCell
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: Reactome
  4. extracellular vesicular exosome Source: UniProtKB
  5. nucleoplasm Source: HPA
  6. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Nestor-Guillermo progeria syndrome (NGPS)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn atypical progeroid syndrome characterized by normal development in the first years of life, later followed by the emergence of generalized lipoatrophy, severe osteoporosis, and marked osteolysis. The atrophic facial subcutaneous fat pad and the marked osteolysis of the maxilla and mandible result in a typical pseudosenile facial appearance with micrognathia, prominent subcutaneous venous patterning, a convex nasal ridge, and proptosis. Cognitive development is completely normal. Patients do not have cardiovascular dysfunction, atherosclerosis, or metabolic anomalies.

See also OMIM:614008
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121A → T in NGPS; shows a dramatic reduction in BANF1 protein levels indicating that the mutation impairs protein stability. 1 Publication
VAR_065954

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi4 – 41S → A: Complete loss of phosphorylation. 1 Publication
Mutagenesisi4 – 41S → E: Complete loss of phosphorylation and mislocalization of EMD in nucleus. 1 Publication
Mutagenesisi6 – 61K → A: Complete loss of LEMD3/MAN1 and histone H1/H3 binding. 4 Publications
Mutagenesisi6 – 61K → E: Complete loss of dsDNA and LEMD3/MAN1 binding. 4 Publications
Mutagenesisi8 – 81R → A: Enhances histone H1/H3 binding. 2 Publications
Mutagenesisi8 – 81R → E: Complete loss of LEMD3/MAN1 binding. 2 Publications
Mutagenesisi9 – 91D → A: Reduces binding to dsDNA, LEMD3/MAN1 and histone H1/H3. 3 Publications
Mutagenesisi14 – 141P → A: No effect on LEMD3/MAN1 and enhances histone H1/H3 binding. 3 Publications
Mutagenesisi18 – 181K → A: No effect on histone H1/H3 binding. 2 Publications
Mutagenesisi25 – 251G → E: Complete loss of dsDNA, EMD, histone H1/H3 and LEMD3/MAN1 binding. 3 Publications
Mutagenesisi25 – 251G → Q: Complete loss of EMD binding and reduces dsDNA binding. 3 Publications
Mutagenesisi26 – 261I → A: Reduces histone H1/H3 and LEMD3/MAN1 binding. Fails to promote HIV-1 genome integration. 3 Publications
Mutagenesisi26 – 261I → K: Fails to promote HIV-1 genome integration. 3 Publications
Mutagenesisi27 – 271G → E: Fails to bind dsDNA. 1 Publication
Mutagenesisi27 – 271G → Q: Reduces binding to dsDNA. 1 Publication
Mutagenesisi29 – 291V → A: No effect on histone H1/H3 binding. 1 Publication
Mutagenesisi32 – 321K → E: No effect on histone H1/H3 binding. 1 Publication
Mutagenesisi33 – 331K → E: No effect on histone H1/H3 binding. 1 Publication
Mutagenesisi37 – 371R → A: No effect on histone H1/H3 binding. 2 Publications
Mutagenesisi37 – 371R → E: Reduces LEMD3/MAN1 binding. 2 Publications
Mutagenesisi41 – 411K → A: No effect on histone H1/H3 and LEMD3/MAN1 binding. 3 Publications
Mutagenesisi41 – 411K → E: Reduces histone H1/H3 binding. 3 Publications
Mutagenesisi46 – 461L → E: Complete loss of dsDNA, histone H1/H3 and LEMD3/MAN1 binding. 3 Publications
Mutagenesisi47 – 471G → E: Complete loss of EMD, histone H1/h3 and LEMD3/MAN1 binding. 3 Publications
Mutagenesisi50 – 501L → A: Reduces LEMD3/MAN1 binding. No effect on Histone H1/H3 binding. 3 Publications
Mutagenesisi50 – 501L → K: Fails to promote HIV-1 genome integration. 3 Publications
Mutagenesisi51 – 511V → E: Complete loss of EMD, and histone H1/H3 binding. Reduces dsDNA and LEMD3/MAN1 binding. 3 Publications
Mutagenesisi53 – 531K → A: No effect on LEMD3/MAN1 binding. Enhances histone H1/H3 binding. 4 Publications
Mutagenesisi53 – 531K → E: Complete loss of EMD binding. Reduces LEMD3/MAN1 binding. Enhances histone H1/H3 binding. 4 Publications
Mutagenesisi54 – 541K → A: Reduces LEMD3/MAN1 binding. No effect on histone H1/H3 binding. 4 Publications
Mutagenesisi54 – 541K → E: Reduces binding to dsDNA. 4 Publications
Mutagenesisi60 – 601R → E: No effect on histone H1/H3 binding. 1 Publication
Mutagenesisi62 – 621W → A: Complete loss of LEMD3/MAN1 binding. Enhances histone H1/H3 binding. 3 Publications
Mutagenesisi64 – 641K → E: Enhances histone H1/H3 binding. 1 Publication
Mutagenesisi75 – 751R → E: Reduces binding to dsDNA. No effect on histone H1/H3 binding. 2 Publications
Mutagenesisi80 – 801C → A: No effect on histone H1/H3 and LEMD3/MAN1 binding. 3 Publications
Mutagenesisi82 – 821R → E: No effect on histone H1/H3 binding. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi614008. phenotype.
Orphaneti280576. Nestor-Guillermo progeria syndrome.
PharmGKBiPA134903639.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8989Barrier-to-autointegration factorPRO_0000221026Add
BLAST
Initiator methioninei1 – 11Removed; alternate1 Publication
Chaini2 – 8988Barrier-to-autointegration factor, N-terminally processedPRO_0000423190Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei2 – 21N-acetylthreonine; in Barrier-to-autointegration factor, N-terminally processed1 Publication
Modified residuei2 – 21Phosphothreonine; by VRK1 and VRK21 Publication
Modified residuei3 – 31Phosphothreonine; by VRK1 and VRK21 Publication
Modified residuei4 – 41Phosphoserine; by VRK1 and VRK22 Publications

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.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO75531.
PaxDbiO75531.
PeptideAtlasiO75531.
PRIDEiO75531.

PTM databases

PhosphoSiteiO75531.

Expressioni

Tissue specificityi

Widely expressed. Expressed in colon, brain, heart, kidney, liver, lung, ovary, pancreas, placenta, prostate, skeletal muscle, small intestine, spleen and testis. Not detected in thymus and peripheral blood leukocytes.

Gene expression databases

BgeeiO75531.
CleanExiHS_BANF1.
ExpressionAtlasiO75531. baseline.
GenevestigatoriO75531.

Organism-specific databases

HPAiCAB032896.
HPA039242.

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. Interacts with HIV-1 pre-integration complex in cytoplasm by binding to viral matrix protein and Gag polyprotein.7 Publications

Protein-protein interaction databases

BioGridi114342. 58 interactions.
DIPiDIP-50395N.
IntActiO75531. 2 interactions.
MINTiMINT-5002289.
STRINGi9606.ENSP00000310275.

Structurei

Secondary structure

1
89
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 117Combined sources
Helixi20 – 223Combined sources
Helixi28 – 369Combined sources
Helixi42 – 5110Combined sources
Turni52 – 543Combined sources
Helixi56 – 6712Combined sources
Helixi71 – 8818Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CI4X-ray1.90A/B1-89[»]
1QCKNMR-A/B1-89[»]
2BZFX-ray2.87A1-89[»]
2EZXNMR-A/B1-89[»]
2EZYNMR-A/B1-89[»]
2EZZNMR-A/B1-89[»]
2ODGNMR-A/B1-89[»]
SMRiO75531. Positions 1-89.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75531.

Family & Domainsi

Domaini

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, whereas DNA binds to the left and right sides.

Sequence similaritiesi

Belongs to the BAF family.Curated

Phylogenomic databases

eggNOGiNOG251829.
GeneTreeiENSGT00390000018613.
HOVERGENiHBG029345.
InParanoidiO75531.
OMAiHRNFVAE.
OrthoDBiEOG7HHWVW.
PhylomeDBiO75531.
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.

O75531-1 [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:October 31, 1998 - v1
Checksum:i9A2180A2D284F5D0
GO

Sequence cautioni

The sequence AAC08964.1 differs from that shown. Reason: Frameshift at position 87. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121A → T in NGPS; shows a dramatic reduction in BANF1 protein levels indicating that the mutation impairs protein stability. 1 Publication
VAR_065954

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF070447 mRNA. Translation: AAC23575.1.
AF044773 mRNA. Translation: AAC08964.1. Frameshift.
AF068235 mRNA. Translation: AAD15901.1.
CR542140 mRNA. Translation: CAG46937.1.
BC005942 mRNA. Translation: AAH05942.1.
BC107702 mRNA. Translation: AAI07703.1.
CCDSiCCDS8125.1.
RefSeqiNP_001137457.1. NM_001143985.1.
NP_003851.1. NM_003860.3.
UniGeneiHs.433759.

Genome annotation databases

EnsembliENST00000312175; ENSP00000310275; ENSG00000175334.
ENST00000445560; ENSP00000416128; ENSG00000175334.
ENST00000527348; ENSP00000432867; ENSG00000175334.
ENST00000533166; ENSP00000433760; ENSG00000175334.
GeneIDi8815.
KEGGihsa:8815.
UCSCiuc001ogo.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF070447 mRNA. Translation: AAC23575.1.
AF044773 mRNA. Translation: AAC08964.1. Frameshift.
AF068235 mRNA. Translation: AAD15901.1.
CR542140 mRNA. Translation: CAG46937.1.
BC005942 mRNA. Translation: AAH05942.1.
BC107702 mRNA. Translation: AAI07703.1.
CCDSiCCDS8125.1.
RefSeqiNP_001137457.1. NM_001143985.1.
NP_003851.1. NM_003860.3.
UniGeneiHs.433759.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CI4X-ray1.90A/B1-89[»]
1QCKNMR-A/B1-89[»]
2BZFX-ray2.87A1-89[»]
2EZXNMR-A/B1-89[»]
2EZYNMR-A/B1-89[»]
2EZZNMR-A/B1-89[»]
2ODGNMR-A/B1-89[»]
SMRiO75531. Positions 1-89.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114342. 58 interactions.
DIPiDIP-50395N.
IntActiO75531. 2 interactions.
MINTiMINT-5002289.
STRINGi9606.ENSP00000310275.

PTM databases

PhosphoSiteiO75531.

Proteomic databases

MaxQBiO75531.
PaxDbiO75531.
PeptideAtlasiO75531.
PRIDEiO75531.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000312175; ENSP00000310275; ENSG00000175334.
ENST00000445560; ENSP00000416128; ENSG00000175334.
ENST00000527348; ENSP00000432867; ENSG00000175334.
ENST00000533166; ENSP00000433760; ENSG00000175334.
GeneIDi8815.
KEGGihsa:8815.
UCSCiuc001ogo.3. human.

Organism-specific databases

CTDi8815.
GeneCardsiGC11P065769.
HGNCiHGNC:17397. BANF1.
HPAiCAB032896.
HPA039242.
MIMi603811. gene.
614008. phenotype.
neXtProtiNX_O75531.
Orphaneti280576. Nestor-Guillermo progeria syndrome.
PharmGKBiPA134903639.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG251829.
GeneTreeiENSGT00390000018613.
HOVERGENiHBG029345.
InParanoidiO75531.
OMAiHRNFVAE.
OrthoDBiEOG7HHWVW.
PhylomeDBiO75531.
TreeFamiTF315060.

Enzyme and pathway databases

ReactomeiREACT_160242. Initiation of Nuclear Envelope Reformation.
REACT_160251. Clearance of Nuclear Envelope Membranes from Chromatin.
REACT_6866. Autointegration results in viral DNA circles.
REACT_6918. Integration of provirus.
REACT_7991. Vpr-mediated nuclear import of PICs.
REACT_8990. Integration of viral DNA into host genomic DNA.
REACT_9058. 2-LTR circle formation.
REACT_9406. APOBEC3G mediated resistance to HIV-1 infection.

Miscellaneous databases

EvolutionaryTraceiO75531.
GeneWikiiBarrier_to_autointegration_factor_1.
GenomeRNAii8815.
NextBioi33066.
PROiO75531.
SOURCEiSearch...

Gene expression databases

BgeeiO75531.
CleanExiHS_BANF1.
ExpressionAtlasiO75531. baseline.
GenevestigatoriO75531.

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(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Genomic and functional map of the chromosome 14 t(12;14) breakpoint cluster region in uterine leiomyoma."
    Lynch R.A., Piper M., Bankier A., Bhugra B., Surti U., Liu J., Buckler A., Dear P.H., Menon A.G.
    Genomics 52:17-26(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Uterus.
  3. "Human BAF homolog gene."
    Zhang J., Liu T., Ye M., Zhang Q., Fu G., Zhou J., Wu J., Shen Y., Yu M., Chen S., Mao M., Chen Z.
    Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  6. "Both the structure and DNA binding function of the barrier-to-autointegration factor contribute to reconstitution of HIV type 1 integration in vitro."
    Harris D., Engelman A.
    J. Biol. Chem. 275:39671-39677(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HIV-1 INTEGRATION, MUTAGENESIS OF LYS-6; PRO-14; LYS-18; ILE-26; LYS-41; LEU-50; LYS-53; LYS-54; TRP-62 AND CYS-80.
  7. "Barrier-to-autointegration factor (BAF) bridges DNA in a discrete, higher-order nucleoprotein complex."
    Zheng R., Ghirlando R., Lee M.S., Mizuuchi K., Krause M., Craigie R.
    Proc. Natl. Acad. Sci. U.S.A. 97:8997-9002(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MULTIMERIZATION.
  8. "BAF is required for emerin assembly into the reforming nuclear envelope."
    Haraguchi T., Koujin T., Segura-Totten M., Lee K.K., Matsuoka Y., Yoneda Y., Wilson K.L., Hiraoka Y.
    J. Cell Sci. 114:4575-4585(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EMD.
  9. "Barrier-to-autointegration factor: major roles in chromatin decondensation and nuclear assembly."
    Segura-Totten M., Kowalski A.K., Craigie R., Wilson K.L.
    J. Cell Biol. 158:475-485(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF LYS-6; ASP-9; GLY-25; GLY-27; LEU-46; GLY-47; VAL-51; LYS-53; LYS-54 AND ARG-75.
  10. "The barrier-to-autointegration factor is a component of functional human immunodeficiency virus type 1 preintegration complexes."
    Lin C.W., Engelman A.
    J. Virol. 77:5030-5036(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 PRE-INTEGRATION COMPLEX.
  11. "Barrier-to-autointegration factor BAF binds p55 Gag and matrix and is a host component of human immunodeficiency virus type 1 virions."
    Mansharamani M., Graham D.R., Monie D., Lee K.K., Hildreth J.E., Siliciano R.F., Wilson K.L.
    J. Virol. 77:13084-13092(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 MATRIX PROTEIN.
  12. "Direct binding of nuclear membrane protein MAN1 to emerin in vitro and two modes of binding to barrier-to-autointegration factor."
    Mansharamani M., Wilson K.L.
    J. Biol. Chem. 280:13863-13870(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LEMD3/MAN1, MUTAGENESIS OF LYS-6; ARG-8; ASP-9; PRO-14; GLY-25; ILE-26; ARG-37; LYS-41; LEU-46; GLY-47; LEU-50; VAL-51; LYS-53; LYS-54; TRP-62 AND CYS-80.
  13. "Binding of barrier to autointegration factor (BAF) to histone H3 and selected linker histones including H1.1."
    de Oca R.M., Lee K.K., Wilson K.L.
    J. Biol. Chem. 280:42252-42262(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HISTONE H1/H3, MUTAGENESIS OF LYS-6; ARG-8; ASP-9; PRO-14; LYS-18; GLY-25; ILE-26; VAL-29; LYS-32; LYS-33; ARG-37; LYS-41; LEU-46; GLY-47; LEU-50; VAL-51; LYS-53; LYS-54; ARG-60; TRP-62; LYS-64; ARG-75; CYS-80 AND ARG-82.
  14. "Barrier-to-autointegration factor phosphorylation on Ser-4 regulates emerin binding to lamin A in vitro and emerin localization in vivo."
    Bengtsson L., Wilson K.L.
    Mol. Biol. Cell 17:1154-1163(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-4, MUTAGENESIS OF SER-4.
  15. "Barrier-to-autointegration factor-like (BAF-L): a proposed regulator of BAF."
    Tifft K.E., Segura-Totten M., Lee K.K., Wilson K.L.
    Exp. Cell Res. 312:478-487(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BAFL.
  16. "The vaccinia-related kinases phosphorylate the N' terminus of BAF, regulating its interaction with DNA and its retention in the nucleus."
    Nichols R.J., Wiebe M.S., Traktman P.
    Mol. Biol. Cell 17:2451-2464(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-2; THR-3 AND SER-4, SUBCELLULAR LOCATION.
  17. "The inner-nuclear-envelope protein emerin regulates HIV-1 infectivity."
    Jacque J.-M., Stevenson M.
    Nature 441:641-645(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  19. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "Coordination of kinase and phosphatase activities by Lem4 enables nuclear envelope reassembly during mitosis."
    Asencio C., Davidson I.F., Santarella-Mellwig R., Ly-Hartig T.B., Mall M., Wallenfang M.R., Mattaj I.W., Gorjanacz M.
    Cell 150:122-135(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, DEPHOSPHORYLATION, INTERACTION WITH ANKLE2.
  23. "BAF: roles in chromatin, nuclear structure and retrovirus integration."
    Segura-Totten M., Wilson K.L.
    Trends Cell Biol. 14:261-266(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  24. "Solution structure of the cellular factor BAF responsible for protecting retroviral DNA from autointegration."
    Cai M., Huang Y., Zheng R., Wei S.Q., Ghirlando R., Lee M.S., Craigie R., Gronenborn A.M., Clore G.M.
    Nat. Struct. Biol. 5:903-909(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  25. "Structural basis of DNA bridging by barrier-to-autointegration factor."
    Umland T.C., Wei S.-Q., Craigie R., Davies D.R.
    Biochemistry 39:9130-9138(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF HOMODIMER.
  26. "Exome sequencing and functional analysis identifies BANF1 mutation as the cause of a hereditary progeroid syndrome."
    Puente X.S., Quesada V., Osorio F.G., Cabanillas R., Cadinanos J., Fraile J.M., Ordonez G.R., Puente D.A., Gutierrez-Fernandez A., Fanjul-Fernandez M., Levy N., Freije J.M., Lopez-Otin C.
    Am. J. Hum. Genet. 88:650-656(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT NGPS THR-12.

Entry informationi

Entry nameiBAF_HUMAN
AccessioniPrimary (citable) accession number: O75531
Secondary accession number(s): O60558, Q6FGG7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 14, 1999
Last sequence update: October 31, 1998
Last modified: March 31, 2015
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.