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Literature summary extracted from

  • Edwin, F.; Anderson, K.; Patel, T.B.
    HECT domain-containing E3 ubiquitin ligase Nedd4 interacts with and ubiquitinates Sprouty2 (2010), J. Biol. Chem., 285, 255-264.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.26 Homo sapiens P46934
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-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.26 S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [Spry2]-L-lysine Spry2 is a regulator of receptor tyrosine kinase signaling in development and disease Homo sapiens [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[Spry2]-L-lysine isoform Nedd4 polyubiquitinates Spry2 via Lys48 on ubiquitin and decreases its stability. The Spry2/Nedd4 association involves theWW domains of Nedd4 and requires phosphorylation of the Mnk2 kinase sites, Ser112 and Ser121, on Spry2. The phospho-Ser112/121 region on Spry2 that binds WW domains of Nedd4 is a non-canonical WW domain binding region that does not contain Pro residues after phospho-Ser ?

Synonyms

EC Number Synonyms Comment Organism
2.3.2.26 Nedd4
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 Homo sapiens

General Information

EC Number General Information Comment Organism
2.3.2.26 physiological function silencing of endogenous isoform Nedd4 increases the cellular substrate Spry2 content and attenuates fibroblast growth factor-elicited ERK1/2. Mnk2 kinase silencing decreases Spry2-Nedd4 interactions and also augments the ability of Spry2 to inhibit fibroblast growth factor signaling Homo sapiens