{PDOC50172}
{PS50172; BRCT}
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* BRCT domain profile *
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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 beta-sheet flanked
by a  single  alpha-helix  (alpha2) on one side and two alpha-helices  (alpha1
and alpha3) 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.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Expert(s) to contact by email:
           Hofmann K.; Kay.Hofmann@memorec.com

-Last update: December 2019 / Text revised.

[ 1] Koonin E.V., Altschul S.F., Bork P.
     "BRCA1 protein products ... Functional motifs..."
     Nat. Genet. 13:266-268(1996).
     PubMed=8673121; DOI=10.1038/ng0796-266
[ 2] Bork P., Hofmann K., Bucher P., Neuwald A.F., Altschul S.F.,
     Koonin E.V.
     "A superfamily of conserved domains in DNA damage-responsive cell
     cycle checkpoint proteins."
     FASEB J. 11:68-76(1997).
     PubMed=9034168
[ 3] Callebaut I., Mornon J.-P.
     "From BRCA1 to RAP1: a widespread BRCT module closely associated with
     DNA repair."
     FEBS Lett. 400:25-30(1997).
     PubMed=9000507
[ 4] Yu X., Chini C.C.S., He M., Mer G., Chen J.
     "The BRCT domain is a phospho-protein binding domain."
     Science 302:639-642(2003).
     PubMed=14576433; DOI=10.1126/science.1088753
[ 5] Leung C.C.Y., Glover J.N.M.
     "BRCT domains: easy as one, two, three."
     Cell. Cycle. 10:2461-2470(2011).
     PubMed=21734457; DOI=10.4161/cc.10.15.16312
[ 6] Zhang 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.
     "Structure of an XRCC1 BRCT domain: a new protein-protein interaction
     module."
     EMBO J. 17:6404-6411(1998).
     PubMed=9799248; DOI=10.1093/emboj/17.21.6404

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