Sequence of this protein is as follows: MVQKKPAELQ GFHRSFKGQN PFELAFSLDQ PDHGDSDFGL QCSARPDMPA SQPIDIPDAK KRGKKKKRGR ATDSFSGRFE DVYQLQEDVL GEGAHARVQT CINLITSQEY AVKIIEKQPG HIRSRVFREV EMLYQCQGHR NVLELIEFFE EEDRFYLVFE KMRGGSILSH IHKRRHFNEL EASVVVQDVA SALDFLHNKG IAHRDLKPEN ILCEHPNQVS PVKICDFDLG SGIKLNGDCS PISTPELLTP CGSAEYMAPE VVEAFSEEAS IYDKRCDLWS LGVILYILLS GYPPFVGRCG SDCGWDRGEA CPACQNMLFE SIQEGKYEFP DKDWAHISCA AKDLISKLLV RDAKQRLSAA QVLQHPWVQG CAPENTLPTP MVLQRWDSHF LLPPHPCRIH VRPGGLVRTV TVNE
MAP kinase-interacting kinase 1 (Mnk1) and Mnk2, members of the Ser/Thr protein kinase family, bind tightly to the growth factor-regulated MAP kinases, Erk1 and Erk2. Erk and p38 phosphorylate MNK1 and Mnk2, which stimulates their in vitro kinase activity toward a substrate, eukaryotic initiation factor-4E (eIF-4E). Overexpression of Mnk2 results in increased phosphorylation of endogenous eIF-4E, showing that it can act as an eIF-4E kinase in vivo. Mnk2 may play a role in the response to environmental stress and cytokines. This ubiquitiously expressed protein appears to regulate transcription by phosphorylating eIF-4E, thus increasing the affinity of this protein for the 7-methylguanosine-containing mRNA cap. Expression of active mutants of MNK1 and MNK2 in 293 cells diminishes cap-dependent translation relative to cap-independent translation in a transient reporter assay. Human Mnk2 is homologous to murine Mnk2 (approximately 94% identical) and human Mnk1 (71% identical). In vitro phosphorylation studies show that Mnk2 is a significantly better substrate than Mnk1 for extracellular signal-regulated kinase 2 (Erk2), p38MAPKalpha, and p38MAPKbeta. Mnk2 has also been shown to interact with the C-terminal regions of eIF-4G1 and eIF-4G2.
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Protein Aliases: G protein-coupled receptor kinase 7; MAP kinase signal-integrating kinase 2; MAP kinase-interacting serine/threonine-protein kinase 2; MAPK signal-integrating kinase 2
Gene Aliases: GPRK7; MKNK2; MNK2
UniProt ID: (Human) Q9HBH9
Entrez Gene ID: (Human) 2872