The Eukaryotic Linear Motif resource for
Functional Sites in Proteins
Functional site class:
BRCT phosphopeptide ligands
Functional site description:
BRCT domains are protein modules mainly found in Eukaryota. BRCT domains are present in proteins that are associated with DNA damage response. They recognize and bind specific phosphorylated serine (pS) sequences. This phospho-protein mediated interaction of the BRCT domain has a central role in cell-cycle check point and DNA repair functions.
ELMs with same func. site: LIG_BRCT_BRCA1_1  LIG_BRCT_BRCA1_2  LIG_BRCT_MDC1_1 
ELM Description:
The LIG_BRCT_BRCA1_2 motif binds with high affinity to the BRCT domain of BRCA1. The motif has the consensus sequence S..F.K and these residues are specially recognized by the binding pocket in the BRCT domains. The lower affinity motif lacks the lysine residue (S..F).
Pattern: .(S)..F.K
Pattern Probability: 0.0001169
Present in taxon: Eukaryota
Interaction Domain:
BRCT (PF00533) BRCA1 C Terminus (BRCT) domain (Stochiometry: 1 : 1)
PDB Structure: 1T29
o See 1 Instance for LIG_BRCT_BRCA1_2
o Abstract
BRCT domains were first identified in and named after the breast cancer susceptibility protein BRCA1 (Zhang,1999). They have alpha/beta structures that occur singly or as multiple repeats. BRCT domains are 80-100 amino acid in length and function as phosphopeptide ligands (Clapperton,2004). They are found in nuclear proteins that are typically associated with cell cycle checkpoint functions responsive to DNA damage (Glover,2004). An unusual feature of paired BRCT motifs is that the phosphopeptides bind across the domain-domain interface (Clapperton,2004). Available data when this entry was prepared suggest that BRCTs may bind exclusively to phosphoserine peptides. By contrast FHA domains, which are often found in a similar functional context, recognise phosphothreonine peptides (LIG_FHA_1). Many of the BRCT ligands are likely to be at pSQ motifs phosphorylated by the checkpoint kinases, ATM, ATR, DNA-PK (Glover,2004). BRCA1-binding motifs are S..F.K (high affinity) or S..F (lower affinity) (Clapperton,2004). Metazoa MDC1 binds histone H2AX C-terminal S..Y$ motifs (Lee,2005), which may be S..F$ in plants and S..L$ in Fungi, but experimental evidence has been lacking. Also, a poorly characterised motif binding the TopBP1 BRCT may match the pattern S.II but more data is needed (Liu,2003). Since consensus motifs have so far been defined for just a few BRCT domains, the range of different binding motif patterns could be quite large.

o 8 selected references:

o 5 GO-Terms:

o 1 Instance for LIG_BRCT_BRCA1_2
(click table headers for sorting; Notes column: =Number of Switches, =Number of Interactions)
Acc., Gene-, NameStartEndSubsequenceLogic#Ev.OrganismNotes
989 995 IVISRSTSPTFNKQTKRVSW TP 3 Homo sapiens (Human)
Please cite: ELM 2016-data update and new functionality of the eukaryotic linear motif resource. (PMID:26615199)

ELM data can be downloaded & distributed for non-commercial use according to the ELM Software License Agreement