Motif Criteria Details:
Motif1:
[V/I]-[V/I]-[D/E]-[V/I/L]-[T/D/E]
Motif2:
[V/I]-[V/I]-[V/I/L]-[V/I/L]-[D/E]
Motif3:
[V/I/L/F/Y]-[V/I]-DLT
PolySUMO-binding proteins
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Motif4
Protein Sequences:
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Fasta format only
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*Polysumoylation is a crucial cellular response to stresses against genomic integrity or proteostasis. Like the small ubiquitin-like modifier (SUMO)-targeted ubiquitin ligase RNF4, proteins with clustered SUMO-interacting motifs (SIMs) can be important signal transducers downstream of polysumoylation. To identify novel polySUMO-binding proteins, we conducted a computational string search with a custom Python script. We found clustered SIMs in another RING domain protein Arkadia/RNF111. Detailed biochemical analysis of the Arkadia SIMs revealed that dominant SIMs in a SIM cluster often contain a pentameric VIDLT ((V/I/L/F/Y)(V/I)DLT) core sequence that is also found in the SIMs in PIAS family E3s and is likely the best-fitted structure for SUMO recognition. This idea led to the identification of additional novel SIM clusters in FLASH/CASP8AP2, C5orf25, and SOBP/JXC1. We suggest that the clustered SIMs in these proteins form distinct SUMO binding domains to recognize diverse forms of protein sumoylation.
(Sun & Hunter 2012
J Biol Chem.
Dec 7;287(50):42071-83)
Webpage developed by:
A.K.Garg 2013
