true2008-11-252024-01-24116SPRE2_RATIdentification of cDNA encoding rat Spred-2.Saitoh A.Hirasawa N.Ohuchi K.2003-10EMBL/GenBank/DDBJNUCLEOTIDE SEQUENCE [MRNA]Tesk1 interacts with Spry2 to abrogate its inhibition of ERK phosphorylation downstream of receptor tyrosine kinase signaling.Chandramouli S.Yu C.Y.Yusoff P.Lao D.H.Leong H.F.Mizuno K.Guy G.R.doi:10.1074/jbc.m7054572002008J. Biol. Chem.2831679-1691INTERACTION WITH TESK1Negative regulation of TGFbeta-induced lens epithelial to mesenchymal transition (EMT) by RTK antagonists.Zhao G.Wojciechowski M.C.Jee S.Boros J.McAvoy J.W.Lovicu F.J.doi:10.1016/j.exer.2015.01.0012015Exp. Eye Res.1329-16TISSUE SPECIFICITYratSpred2EukaryotaRegulation of RAS by GAPsFGFRL1 modulation of FGFR1 signalingExpressed in frontal cortex and 18 other cell types or tissuesbaseline and differentialEVH1_SPRED-likePleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)KBDPH-like_dom_sfSPRE_EVH1SproutyWH1/EVH1_domSPROUTY-RELATED, EVH1 DOMAIN-CONTAINING PROTEIN 2SPROUTY-RELATED, EVH1 DOMAIN-CONTAINING PROTEIN FAMILY MEMBERSproutyWH1WH1PH domain-likeKBDSPRWH1Sprouty-related, EVH1 domain-containing protein 2Spred-2Spred2Negatively regulates Ras signaling pathways and downstream activation of MAP kinases. Recruits and translocates NF1 to the cell membrane, thereby enabling NF1-dependent hydrolysis of active GTP-bound Ras to inactive GDP-bound Ras (By similarity). 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).Homodimer and heterodimer (By similarity). Able to interact with SPRED1 to form heterodimers (By similarity). Interacts with RAS (By similarity). May interact with ZDHHC13 (via ANK repeats) and ZDHHC17 (via ANK repeats) (By similarity). Interacts with TESK1 (PubMed:17974561). Interacts with NF1 (By similarity).Detected in the cytoplasm of the stratum spinosum cells, where it is associated with cytoplasmic vesicles that are supposed to be secretory granules.Expressed in the eye, with higher expression in lens epithelium than in lens fiber cells at postnatal day 15.Phosphorylated on serine and threonine residues. Phosphorylated on tyrosine. Phosphorylation of Tyr-224 and Tyr-227 are required for ubiquitination.Ubiquitinated; leading to degradation by the proteasome.Sprouty-related, EVH1 domain-containing protein 2468051410WH15122KBD197252SPR300408Disordered127171Disordered274294Polar residues145Phosphotyrosine224Phosphotyrosine2272005-11-22146805c098ce0d28753729bdb2582dd9e281efMTEETHPDDDSYIVRVKAVVMTRDDSSGGWFPQEGGGISRVGVCKVMHPEGNGRSGFLIHGERQKDKLVVLECYVRKDLVYTKANPTFHHWKVDNRKFGLTFQSPADARAFDRGVRKAIEDLIEGSTTSSSTIHNEAELGDDDVFTTATDSSSNSSQKREPNTRTISSPTSCEHRRIYTLDPYPMDLYHPDQRLPRSYPQVTFPEDDEEIVRINPREKIWMTGYEDYRHAPVRGKYLDSTEDADSYVRFAKGEVPKHEYTYPYVDSSDFGFGEDPKGNVIKTQPPRAKSRRRKENGERSRCVYCRDMFNHEENRRGHCQDAPDAVRTCIRRVSCMWCADSMLYHCMSDPEGDYTDPCSCDTSDEKFCLRWMALIALSFLAPCMCCYLPLRACHHCGVMCRCCGGKHKAAAtruetruetruetruetruetruetruetruetrue