Minimotif Miner, a tool for investigating protein function
In addition to large domains, many short motifs mediate functional post-translational modification of proteins as well as protein-protein interactions and protein trafficking functions. We have constructed a motif database comprising 312 unique motifs and a web-based tool for identifying motifs in proteins. Functional motifs predicted by MnM can be ranked by several approaches, and we validated these scores by analyzing thousands of confirmed examples and by confirming prediction of previously unidentified 14-3-3 motifs in EFF-1.
14-3-3 Proteins/chemistry; 14-3-3 Proteins/physiology; Amino Acid Motifs; Amino acid sequence; Animals; Caenorhabditis elegans; Caenorhabditis elegans Proteins/chemistry; Caenorhabditis elegans Proteins/physiology; Databases; Databases as Topic; Internet; Membrane Glycoproteins/chemistry; Membrane Glycoproteins/physiology; Minitof Miner; Molecular Sequence Data; Proteins/chemistry; Proteins/physiology; Sequence Alignment; Sequence alignment (Bioinformatics); Sequence Analysis; Protein/methods; Software
Computer Sciences | Genetics and Genomics | Life Sciences | Molecular Biology | Neurosciences | Structural Biology
del Campo, J. J.,
Shinn, J. H.,
Mohler, W. A.,
Maciejewski, M. W.,
Gryk, M. R.,
Schiller, S. R.,
Schiller, M. R.
Minimotif Miner, a tool for investigating protein function.
Nature Methods, 3(3),