SLiMAn is a free access webserver devoted to analysis of interactomic results, to suggest interactions involving Short Linear Motif (SLiM) paired with structured domain within the submited list of putative interactants.
SLiMs are usually defined as short segments (< 25 residues) in a polypeptide harboring a signature recognized by a family of folded domains (e.g.: polyproline stretches and SH3 or WW domains).
From a simple list of proteins (Uniprot Acc/Ids), SLiMAn will process the data with 3 successive levels of analysis named:
SLiMAn-Pairings,
SLiMAn-Alignments
and
SLiMAn-Modeling.
Learn more about all the functionalities in the
documentation section
or in the user manual
and from the published research articles describing the first version
Reys & Labesse, Journal of Proteomic Research (2022)
and SLiMAn2 Reys et al, Nucleic Acids Research (2024).
A thorough description of the usage of SLiMAn2 is available in a coming issue of Method Mol. Biol., where an extensive application on the analysis of human tankyrase interactome is provided as an illustrative example.
A draft is available at:
https://www.researchsquare.com/article/rs-3973092/v1
This website is free and open to all users and there is no login requirement.
There are two main types of inputs:
:
)
FRAT2 Interactome (14 proteins)
Pragmin Interactome (62 proteins)
GIPC1 meta-interactome (96 proteins)
SLiMAn has its own structural database extracted from the PDB to provide templates for internal homology modeling (SLiMAn-Modeling procedure). This database contains a subset of PDB structures corresponding to complexes having a peptide containing an ELM motif in proximity to a Pfam domain.
The current database contains 5325 structures of protein-peptide complexes.
The database is accessible as is using this download link (244 Mo).
SLiMAn build : 2.6.08022023
DataBases last update : 2025-03-06 11:16:12
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