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PROSITE documentation PDOC50172

BRCT domain profile





Description

The breast cancer susceptibility gene contains at its C-terminus two copies of a conserved domain that was named BRCT for BRCA1 C-terminus. This domain of about 95 amino acids exists in a large number of proteins from prokaryotes to eukaryotes. BRCT domain-containing proteins are involved in multiple cellular responses, including cell cycle checkpoint control, DNA repair, and transcription regulation [1,2,3]. The BRCT domain is not limited to the C-termini of protein sequences and can be found in multiple copies or in a single copy as in RAP1 and TdT. Aside from a role as phospho-peptide modules, BRCT domains have been implicated in phosphorylation-independent protein interactions, DNA binding and poly(ADP-ribose) (PAR) binding [4,5].

The BRCT domain fold is comprised of a central 4-stranded β-sheet flanked by a single α-helix (α2) on one side and two α-helices (α1 and α3) on the opposite side (see <PDB:1CDZ>) [5,6].

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

  • Mammalian breast cancer type 1 susceptibility protein. It may regulate gene expression.
  • Human p53-binding protein 1.
  • Human poly(ADP-ribose) polymerase (PARP) (EC 2.4.2.30). It modifies various nuclear proteins by poly(ADP-rybosyl)ation.
  • Vertebrate DNA nucleotidylexotransferase (EC 2.7.7.31). It adds nucleotides at the junction (N region) of rearranged Ig heavy chain and T cell receptor gene segments during the maturation of B and T cells.
  • Mammalian DNA-repair protein XRCC1.
  • Human DNA ligase III (EC 6.5.1.1). It is involved in DNA strand-break repair.
  • Human DNA ligase IV (EC 6.5.1.1).
  • Drosophila germline transcription factor 1. A putative transcription factor active during oogenesis and embryogenesis.
  • Baker's yeast DNA ligase II (EC 6.5.1.1).
  • Baker's yeast RAD9 protein. It is essential for cell cycle arrest following DNA damage by X-irradiation or inactivation of DNA ligase.
  • Baker's yeast RAP1. It is involved in telomeric and HM loci silencing.
  • Escherichia coli DNA ligase (EC 6.5.1.2). It is essential for DNA replication and repair of damaged DNA.
  • Synechocystis sp. DNA ligase (EC 6.5.1.2). It is probably essential for DNA replication and repair of damaged DNA.

The profile we developed covers the entire BRCT domain.

Expert(s) to contact by email:

Hofmann K.

Last update:

December 2019 / Text revised.

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Technical section

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

BRCT, PS50172; BRCT domain profile  (MATRIX)


References

1AuthorsKoonin E.V. Altschul S.F. Bork P.
TitleBRCA1 protein products ... Functional motifs...
SourceNat. Genet. 13:266-268(1996).
PubMed ID8673121
DOI10.1038/ng0796-266

2AuthorsBork P. Hofmann K. Bucher P. Neuwald A.F. Altschul S.F. Koonin E.V.
TitleA superfamily of conserved domains in DNA damage-responsive cell cycle checkpoint proteins.
SourceFASEB J. 11:68-76(1997).
PubMed ID9034168

3AuthorsCallebaut I. Mornon J.-P.
TitleFrom BRCA1 to RAP1: a widespread BRCT module closely associated with DNA repair.
SourceFEBS Lett. 400:25-30(1997).
PubMed ID9000507

4AuthorsYu X. Chini C.C.S. He M. Mer G. Chen J.
TitleThe BRCT domain is a phospho-protein binding domain.
SourceScience 302:639-642(2003).
PubMed ID14576433
DOI10.1126/science.1088753

5AuthorsLeung C.C.Y. Glover J.N.M.
TitleBRCT domains: easy as one, two, three.
SourceCell. Cycle. 10:2461-2470(2011).
PubMed ID21734457
DOI10.4161/cc.10.15.16312

6AuthorsZhang X. Morera S. Bates P.A. Whitehead P.C. Coffer A.I. Hainbucher K. Nash R.A. Sternberg M.J. Lindahl T. Freemont P.S.
TitleStructure of an XRCC1 BRCT domain: a new protein-protein interaction module.
SourceEMBO J. 17:6404-6411(1998).
PubMed ID9799248
DOI10.1093/emboj/17.21.6404



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