Ptpn11
Domain
The SH2 domains repress phosphatase activity. Binding of these domains to phosphotyrosine-containing proteins relieves this auto-inhibition, possibly by inducing a conformational change in the enzyme.
Function
Acts downstream of various receptor and cytoplasmic protein tyrosine kinases to participate in the signal transduction from the cell surface to the nucleus (PubMed:14967142). Positively regulates MAPK signal transduction pathway (By similarity). Dephosphorylates GAB1, ARHGAP35 and EGFR (By similarity). Dephosphorylates ROCK2 at 'Tyr-722' resulting in stimulation of its RhoA binding activity (By similarity). Dephosphorylates CDC73 (By similarity). Dephosphorylates SOX9 on tyrosine residues, leading to inactivate SOX9 and promote ossification (PubMed:29644115). Dephosphorylates tyrosine-phosphorylated NEDD9/CAS-L (By similarity).
Post-translational modifications
Phosphorylated on Tyr-542 and Tyr-580 upon receptor protein tyrosine kinase activation; which creates a binding site for GRB2 and other SH2-containing proteins. Phosphorylated upon activation of the receptor-type kinase FLT3. Phosphorylated by activated PDGFRB (By similarity). Phosphorylated upon activation of the receptor-type kinase PDGFRA.
Sequence Similarities
Belongs to the protein-tyrosine phosphatase family. Non-receptor class 2 subfamily.
Tissue Specificity
Highly expressed in brain, heart and kidney.
Cellular localization
- Cytoplasm
Alternative names
Tyrosine-protein phosphatase non-receptor type 11, Protein-tyrosine phosphatase SYP, SH-PTP2, SHP-2, Shp2, Ptpn11
Database links
swissprot:P35235 entrezGene:19247
Other research areas
- Immunology & Infectious Disease