ERK 8 (phospho Thr175/Y177) rabbit pAb

Catalytic activity: ATP + a protein = ADP + a phosphoprotein. Domain: The N-terminal region (1-20) is the minimal region necessary for ubiquitination and further proteosomal degradation. Domain: The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases. enzyme regulation: Activated by threonine and tyrosine phosphorylation. Inhibited by dual specificity phosphatases, such as DUSP1. function: In vitro, phosphorylates MBP. PTM: Dually phosphorylated on Thr-175 and Tyr-177, which activates the enzyme. Autophosphorylated on threonine and tyrosine residues in vitro. PTM: Ubiquitinated. Ubiquitination may allow its tight kinase activity regulation and rapid turnover. May be ubiquitinated by a SCF E3 ligase. similarity: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily. similarity: Contains 1 protein kinase domain. subunit: Interacts with CSK/c-Src, ABL1, RET and TGFB1I1. tissue specificity: Widely expressed with a maximal expression in lung and kidney.