PROSITE documentation PDOC51021
BAR domain profile


The BAR (Bin-Amphiphysin-Rvs) domain is about 200 amino acid long. This domain can be found alone or in association with other domains such as SH3 (see <PDOC50002>) and RhoGAP (see <PDOC50238>). BAR domain containing proteins are a unique class of adaptor proteins characterized by a common N-terminal fold termed the BAR domain. This set of adaptors, which includes the mammalian proteins amphiphysin and Bin1 and the yeast proteins Rvs167 and Rvs161, has been implicated in diverse cellular processes, including synaptic vesicle endocytosis, actin regulation, differentiation, cell survival, and tumorigenesis. Clearly there are two functions associated with the BAR domain, the sensing and/or induction of membrane curvature and the binding to a small GTPase [1,2].

The resolution of the N-terminus of amphiphysin has shown that the BAR domain forms a crescent-shaped dimer of a three-helix coiled-coil with a characteristic set of conserved hydrophobic, aromatic and hydrophilic amino acids (see <PDB:1URU>) [3,4]. More structural studies revealed that dimerization is a minimal function of BAR-domain-containning proteins. It was suggested that the V-shaped dimer is able to sense and/or induce membrane bending.

More, amphiphysin and endophilin contain a short sequence stretch adjacent to the N terminus of the BAR domain which is presumed to be essential for lipid-binding and tubule formation. This sequence at the N-terminal end was shown to form an amphipathic helix, thereby extending the helical backbone of the dimer at the tips. Together with the BAR domain, this sequence motif is termed N-BAR and can be found in a subgroup of the BAR-domain family including amphiphysin. This stretch is not covered by the developed profile.

Some proteins known to contain a BAR domain are listed below:

  • Animal amphiphysin proteins.
  • Yeast Rvs (amphiphysin-like) proteins.
  • Animal endophylin SH3-containing GRB2-like proteins.
  • Animal Bin Myc box dependent interacting proteins [2].
  • Animal nadrins.
  • Animal Tuba proteins [5].

The profile we developed covers the entire BAR domain.


This profile picks up the entire Bin-Amphiphysin-Rvs family. But recent papers, based on sequence and structural similarities have shown that a conserved region in more divergent families, like oligophrenin, centaurin β, sorting nexin, ICA69, pick1 or arfaptins, is related to the BAR domain [6,7,8]. These families are however too divergent to be detected by this profile.

Last update:

September 2004 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

BAR, PS51021; BAR domain profile  (MATRIX)


1AuthorsBalguerie A. Sivadon P. Bonneu M. Aigle M.
TitleRvs167p, the budding yeast homolog of amphiphysin, colocalizes with actin patches.
SourceJ. Cell Sci. 112:2529-2537(1999).
PubMed ID10393809

2AuthorsGe K. Prendergast G.C.
TitleBin2, a functionally nonredundant member of the BAR adaptor gene family.
SourceGenomics 67:210-220(2000).
PubMed ID10903846

3AuthorsZimmerberg J. McLaughlin S.
TitleMembrane curvature: how BAR domains bend bilayers.
SourceCurr. Biol. 14:R250-R252(2004).
PubMed ID15043839

4AuthorsMiele A.E. Watson P.J. Evans P.R. Traub L.M. Owen D.J.
TitleTwo distinct interaction motifs in amphiphysin bind two independent sites on the clathrin terminal domain beta-propeller.
SourceNat. Struct. Mol. Biol. 11:242-248(2004).
PubMed ID14981508

5AuthorsSalazar M.A. Kwiatkowski A.V. Pellegrini L. Cestra G. Butler M.H. Rossman K.L. Serna D.M. Sondek J. Gertler F.B. De Camilli P.
TitleTuba, a novel protein containing bin/amphiphysin/Rvs and Dbl homology domains, links dynamin to regulation of the actin cytoskeleton.
SourceJ. Biol. Chem. 278:49031-49043(2003).
PubMed ID14506234

6AuthorsHabermann B.
TitleThe BAR-domain family of proteins: a case of bending and binding?
SourceEMBO Rep. 5:250-255(2004).
PubMed ID14993925

7AuthorsPeter B.J. Kent H.M. Mills I.G. Vallis Y. Butler P.J.G. Evans P.R. McMahon H.T.
TitleBAR domains as sensors of membrane curvature: the amphiphysin BAR structure.
SourceScience 303:495-499(2004).
PubMed ID14645856

8AuthorsRichnau N. Fransson A. Farsad K. Aspenstroem P.
TitleRICH-1 has a BIN/Amphiphysin/Rvsp domain responsible for binding to membrane lipids and tubulation of liposomes.
SourceBiochem. Biophys. Res. Commun. 320:1034-1042(2004).
PubMed ID15240152

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