SPRED2

SPRED2 is a member of the Sprouty (see SPRY1; MIM 602465)/SPRED family of proteins that regulate growth factor-induced activation of the MAP kinase cascade (see MAPK1; MIM 176948) (Nonami et al., 2004 [PubMed 15465815]).[supplied by OMIM

sprouty-related, EVH1 domain containing 2

Negatively regulates Ras signaling pathways and downstream activation of MAP kinases (PubMed:15683364).
Inhibits fibroblast growth factor (FGF)-induced retinal lens fiber differentiation, probably by inhibiting FGF-mediated phosphorylation of ERK1/2 (By similarity).
Inhibits TGFB-induced epithelial-to-mesenchymal transition in lens epithelial cells (By similarity).

Biological Process negative regulation of epithelial to mesenchymal transitionISS:UniProtKB
Biological Process negative regulation of ERK1 and ERK2 cascadeISS:UniProtKB
Biological Process negative regulation of lens fiber cell differentiationISS:UniProtKB
Biological Process negative regulation of MAPK cascadeISS:UniProtKB
Biological Process negative regulation of peptidyl-threonine phosphorylationManual Assertion Based On ExperimentIMP:BHF-UCL
Biological Process negative regulation of transforming growth factor beta receptor signaling pathwayISS:UniProtKB
Biological Process positive regulation of DNA damage response, signal transduction by p53 class mediatorBy SimilarityISS:BHF-UCL
Biological Process regulation of protein deacetylationBy SimilarityISS:BHF-UCL

Cell membrane
Cytoplasmic vesicle, secretory vesicle membrane
Cytoplasm
Detected in the cytoplasm of the stratum spinosum cells, where it is associated with cytoplasmic vesicles that are supposed to be secretory granules.

Phosphorylated on serine and threonine residues (PubMed:15683364).
Phosphorylated on tyrosine. Phosphorylation of Tyr-228 and Tyr-231 are required for ubiquitination (PubMed:17094949).
Ubiquitinated; leading to degradation by the proteasome.