Abstract
The effects of tyrosine phosphorylation are manifested and regulated through protein domains that bind to specific phosphotyrosine motifs. STYX is a unique modular domain found within proteins implicated in mediating the effects of tyrosine phosphorylation in vivo. Individual STYX domains are not catalytically active; however, they resemble protein tyrosine phosphatase (PTP) domains and, like PTPs, contain core sequences that recognize phosphorylated substrates. Thus, the STYX domain adds to the repertoire of modular domains that can mediate intracellular signaling in response to protein phosphorylation.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Amino Acid Sequence
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Animals
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Autoantigens
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Binding Sites
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Carrier Proteins / chemistry
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Carrier Proteins / metabolism
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Databases, Factual
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Fungal Proteins / chemistry
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Fungal Proteins / metabolism
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Intracellular Signaling Peptides and Proteins*
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Membrane Proteins / chemistry
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Membrane Proteins / metabolism
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Molecular Sequence Data
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Mutation
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Phosphorylation
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Protein Tyrosine Phosphatases / chemistry
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Protein Tyrosine Phosphatases / genetics
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Protein Tyrosine Phosphatases / metabolism*
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Protein-Tyrosine Kinases / chemistry
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Protein-Tyrosine Kinases / metabolism
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Proteins / chemistry*
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Proteins / genetics
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Proteins / metabolism*
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Receptor-Like Protein Tyrosine Phosphatases, Class 8
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Sequence Homology, Amino Acid
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Viral Proteins / chemistry
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Viral Proteins / metabolism
Substances
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Autoantigens
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Carrier Proteins
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Fungal Proteins
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Intracellular Signaling Peptides and Proteins
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Membrane Proteins
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Proteins
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SBF1 protein, human
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Viral Proteins
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Protein-Tyrosine Kinases
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PTPRN protein, human
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Protein Tyrosine Phosphatases
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Receptor-Like Protein Tyrosine Phosphatases, Class 8