Abstract
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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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14-3-3 Proteins / chemistry
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14-3-3 Proteins / physiology
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Amino Acid Motifs*
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Amino Acid Sequence
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Animals
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Caenorhabditis elegans Proteins / chemistry
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Caenorhabditis elegans Proteins / physiology
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Databases as Topic
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Internet
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Membrane Glycoproteins / chemistry
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Membrane Glycoproteins / physiology
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Molecular Sequence Data
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Proteins / chemistry
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Proteins / physiology*
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Sequence Alignment
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Sequence Analysis, Protein / methods*
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Software*
Substances
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14-3-3 Proteins
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Caenorhabditis elegans Proteins
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EFF-1 protein, C elegans
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Membrane Glycoproteins
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Proteins