loading...| Preferred Name |
PPA2A dephosphorylates SPRY2 |
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| Definitions |
has a Stoichiometric coefficient of 2 Reviewed: Gotoh, N, 2011-08-26 Authored: Rothfels, K, 2011-08-15 In unstimulated cells, SPRY2 has been shown to be phosphorylated on multiple serine and threonine residues. In these cells, SPRY2 exists in a complex with the regulatory and catalytic subunits (A and C, respectively) of the serine/threonine phosphatase PP2A. After stimulation with FGF, the catalytic activity of PP2A increases and the phosphatase dephophorylates SPRY at serine 112 and serine 115. This is thought to promote changes in tertiary structure that promote GRB2 binding and phosphorylation of Y55 and Y227. |
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http://purl.obolibrary.org/obo/HINO_0009027 |
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| comment |
has a Stoichiometric coefficient of 2 Reviewed: Gotoh, N, 2011-08-26 Authored: Rothfels, K, 2011-08-15 In unstimulated cells, SPRY2 has been shown to be phosphorylated on multiple serine and threonine residues. In these cells, SPRY2 exists in a complex with the regulatory and catalytic subunits (A and C, respectively) of the serine/threonine phosphatase PP2A. After stimulation with FGF, the catalytic activity of PP2A increases and the phosphatase dephophorylates SPRY at serine 112 and serine 115. This is thought to promote changes in tertiary structure that promote GRB2 binding and phosphorylation of Y55 and Y227. |
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| definition source |
Reactome, http://www.reactome.org Pubmed17255109 |
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PPA2A dephosphorylates SPRY2 |
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| prefixIRI |
HINO:0009027 |
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| prefLabel |
PPA2A dephosphorylates SPRY2 |
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| seeAlso |
ReactomeREACT_111094 Reactome Database ID Release 431295632 |
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