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O75531 (BAF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Barrier-to-autointegration factor
Alternative name(s):
Breakpoint cluster region protein 1
Gene names
Name:BANF1
Synonyms:BAF, BCRG1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length89 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.9 Ref.17

Subunit structure

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. Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.22

Subcellular location

Nucleus. Cytoplasm. Chromosome. 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. Ref.16

Tissue specificity

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.

Domain

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.

Post-translational modification

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. Ref.14 Ref.16 Ref.22

Involvement in disease

Nestor-Guillermo progeria syndrome (NGPS) [MIM:614008]: An 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.26

Sequence similarities

Belongs to the BAF family.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 8989Barrier-to-autointegration factor
PRO_0000423190
Initiator methionine11Removed; alternate Ref.18
Chain2 – 8988Barrier-to-autointegration factor, N-terminally processed
PRO_0000221026

Amino acid modifications

Modified residue11N-acetylmethionine Ref.20
Modified residue21N-acetylthreonine; in Barrier-to-autointegration factor, N-terminally processed Ref.18
Modified residue21Phosphothreonine; by VRK1 and VRK2 Ref.16
Modified residue31Phosphothreonine; by VRK1 and VRK2 Ref.16
Modified residue41Phosphoserine; by VRK1 and VRK2 Ref.14 Ref.16

Natural variations

Natural variant121A → T in NGPS; shows a dramatic reduction in BANF1 protein levels indicating that the mutation impairs protein stability. Ref.26
VAR_065954

Experimental info

Mutagenesis41S → A: Complete loss of phosphorylation. Ref.14
Mutagenesis41S → E: Complete loss of phosphorylation and mislocalization of EMD in nucleus. Ref.14
Mutagenesis61K → A: Complete loss of LEMD3/MAN1 and histone H1/H3 binding. Ref.6 Ref.9 Ref.12 Ref.13
Mutagenesis61K → E: Complete loss of dsDNA and LEMD3/MAN1 binding. Ref.6 Ref.9 Ref.12 Ref.13
Mutagenesis81R → A: Enhances histone H1/H3 binding. Ref.12 Ref.13
Mutagenesis81R → E: Complete loss of LEMD3/MAN1 binding. Ref.12 Ref.13
Mutagenesis91D → A: Reduces binding to dsDNA, LEMD3/MAN1 and histone H1/H3. Ref.9 Ref.12 Ref.13
Mutagenesis141P → A: No effect on LEMD3/MAN1 and enhances histone H1/H3 binding. Ref.6 Ref.12 Ref.13
Mutagenesis181K → A: No effect on histone H1/H3 binding. Ref.6 Ref.13
Mutagenesis251G → E: Complete loss of dsDNA, EMD, histone H1/H3 and LEMD3/MAN1 binding. Ref.9 Ref.12 Ref.13
Mutagenesis251G → Q: Complete loss of EMD binding and reduces dsDNA binding. Ref.9 Ref.12 Ref.13
Mutagenesis261I → A: Reduces histone H1/H3 and LEMD3/MAN1 binding. Fails to promote HIV-1 genome integration. Ref.6 Ref.12 Ref.13
Mutagenesis261I → K: Fails to promote HIV-1 genome integration. Ref.6 Ref.12 Ref.13
Mutagenesis271G → E: Fails to bind dsDNA. Ref.9
Mutagenesis271G → Q: Reduces binding to dsDNA. Ref.9
Mutagenesis291V → A: No effect on histone H1/H3 binding. Ref.13
Mutagenesis321K → E: No effect on histone H1/H3 binding. Ref.13
Mutagenesis331K → E: No effect on histone H1/H3 binding. Ref.13
Mutagenesis371R → A: No effect on histone H1/H3 binding. Ref.12 Ref.13
Mutagenesis371R → E: Reduces LEMD3/MAN1 binding. Ref.12 Ref.13
Mutagenesis411K → A: No effect on histone H1/H3 and LEMD3/MAN1 binding. Ref.6 Ref.12 Ref.13
Mutagenesis411K → E: Reduces histone H1/H3 binding. Ref.6 Ref.12 Ref.13
Mutagenesis461L → E: Complete loss of dsDNA, histone H1/H3 and LEMD3/MAN1 binding. Ref.9 Ref.12 Ref.13
Mutagenesis471G → E: Complete loss of EMD, histone H1/h3 and LEMD3/MAN1 binding. Ref.9 Ref.12 Ref.13
Mutagenesis501L → A: Reduces LEMD3/MAN1 binding. No effect on Histone H1/H3 binding. Ref.6 Ref.12 Ref.13
Mutagenesis501L → K: Fails to promote HIV-1 genome integration. Ref.6 Ref.12 Ref.13
Mutagenesis511V → E: Complete loss of EMD, and histone H1/H3 binding. Reduces dsDNA and LEMD3/MAN1 binding. Ref.9 Ref.12 Ref.13
Mutagenesis531K → A: No effect on LEMD3/MAN1 binding. Enhances histone H1/H3 binding. Ref.6 Ref.9 Ref.12 Ref.13
Mutagenesis531K → E: Complete loss of EMD binding. Reduces LEMD3/MAN1 binding. Enhances histone H1/H3 binding. Ref.6 Ref.9 Ref.12 Ref.13
Mutagenesis541K → A: Reduces LEMD3/MAN1 binding. No effect on histone H1/H3 binding. Ref.6 Ref.9 Ref.12 Ref.13
Mutagenesis541K → E: Reduces binding to dsDNA. Ref.6 Ref.9 Ref.12 Ref.13
Mutagenesis601R → E: No effect on histone H1/H3 binding. Ref.13
Mutagenesis621W → A: Complete loss of LEMD3/MAN1 binding. Enhances histone H1/H3 binding. Ref.6 Ref.12 Ref.13
Mutagenesis641K → E: Enhances histone H1/H3 binding. Ref.13
Mutagenesis751R → E: Reduces binding to dsDNA. No effect on histone H1/H3 binding. Ref.9 Ref.13
Mutagenesis801C → A: No effect on histone H1/H3 and LEMD3/MAN1 binding. Ref.6 Ref.12 Ref.13
Mutagenesis821R → E: No effect on histone H1/H3 binding. Ref.13

Secondary structure

.............. 89
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O75531 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 9A2180A2D284F5D0

FASTA8910,059
        10         20         30         40         50         60 
MTTSQKHRDF VAEPMGEKPV GSLAGIGEVL GKKLEERGFD KAYVVLGQFL VLKKDEDLFR 

        70         80 
EWLKDTCGAN AKQSRDCFGC LREWCDAFL 

« Hide

References

« Hide 'large scale' references
[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]"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(1998) [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 (MAY-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 (JUN-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(2004) [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(2000) [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(2000) [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(2001) [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(2002) [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(2003) [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(2003) [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(2005) [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(2005) [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(2006) [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(2006) [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(2006) [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(2006) [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(2009) [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(2009) [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(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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(2012) [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(2004) [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(1998) [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(2000) [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(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT NGPS THR-12.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001137457.1. NM_001143985.1.
NP_003851.1. NM_003860.3.
UniGeneHs.433759.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalO75531.
SMRO75531. Positions 1-89.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114342. 58 interactions.
DIPDIP-50395N.
IntActO75531. 2 interactions.
MINTMINT-5002289.
STRING9606.ENSP00000310275.

PTM databases

PhosphoSiteO75531.

Proteomic databases

PaxDbO75531.
PeptideAtlasO75531.
PRIDEO75531.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000312175; ENSP00000310275; ENSG00000175334.
ENST00000445560; ENSP00000416128; ENSG00000175334.
ENST00000527348; ENSP00000432867; ENSG00000175334.
ENST00000533166; ENSP00000433760; ENSG00000175334.
GeneID8815.
KEGGhsa:8815.
UCSCuc001ogo.3. human.

Organism-specific databases

CTD8815.
GeneCardsGC11P065769.
HGNCHGNC:17397. BANF1.
HPACAB032896.
MIM603811. gene.
614008. phenotype.
neXtProtNX_O75531.
Orphanet280576. Nestor-Guillermo progeria syndrome.
PharmGKBPA134903639.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG251829.
HOVERGENHBG029345.
InParanoidO75531.
OMADWCEEFL.
OrthoDBEOG7HHWVW.
PhylomeDBO75531.
TreeFamTF315060.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpressO75531.
BgeeO75531.
CleanExHS_BANF1.
GenevestigatorO75531.

Family and domain databases

Gene3D1.10.150.40. 1 hit.
InterProIPR004122. BAF_prot.
[Graphical view]
PANTHERPTHR12912. PTHR12912. 1 hit.
PfamPF02961. BAF. 1 hit.
[Graphical view]
ProDomPD019964. PD019964. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM01023. BAF. 1 hit.
[Graphical view]
SUPFAMSSF47798. SSF47798. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceO75531.
GeneWikiBarrier_to_autointegration_factor_1.
GenomeRNAi8815.
NextBio33066.
PROO75531.
SOURCESearch...

Entry information

Entry nameBAF_HUMAN
AccessionPrimary (citable) accession number: O75531
Secondary accession number(s): O60558, Q6FGG7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM