MLK3 Products

Description

Mixed lineage kinase-3 (MLK-3) is a mitogen-activated kinase kinase kinase that mediates stress-activating protein kinase (SAPK)/c-Jun NH2-terminal kinase activation. MLK-3 and other MLK family kinases are characterized by the presence of multiple protein-protein interaction domains including a tandem leucine/isoleucine zipper (LZs) motif. Leucine zippers are known to mediate protein dimerization raising the possibility that the tandem leucine/isoleucine zippers may function as a dimerization motif of MLK-3 (1). MLK-3 has several interesting structural features including an SH3 domain in the absence of an SH2 domain, a region containing two leucine zippers with an adjacent carboxy-terminal basic region, and a proline rich region. (2). HPK1 has been found to phosphorylate MLK-3 activation loop in vitro, and Ser281 was found to be the major phosphorylation site, indicating that HPK1 also activates MLK-3 via phosphorylation of the kinase activation loop (3).

Bioinformatics

Entrez	26403 Mouse 309168 Rat 4296 Human
Uniprot	AAH64543 Human NP_002410 Human Q16584 Human
Product By Gene ID	4296
Alternate Names	EC 2.7.11 EC 2.7.11.25 MEKK11 mitogen-activated protein kinase kinase kinase 11 Mixed lineage kinase 3 MLK3MLK-3 PTK1protein-tyrosine kinase PTK1 SH3 domain-containing proline-rich kinase SPRKMGC17114 Src-homology 3 domain-containing proline-rich kinase

Research Areas for MLK3

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Protein Kinase