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ENZYME

ENZYME entry: EC 2.7.11.37

Accepted Name
MAST-subfamily kinase
Alternative Name(s)
microtubule-associated serine/threonine-protein kinase
Reaction catalysed
  • L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+)
  • L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H(+)
Comment(s)
  • MAST (Microtubule Associated Serine/Threonine) kinases are eukaryotic-wide kinases with roles in microtubule function, PTEN regulation and a variety of neuronal functions.
  • They are found in most eukaryotes, though lost from most fungi and ciliates.
  • MAST kinases associate with their substrates via their PDZ domains.
  • Substrates include EC 3.1.3.67 in human and nematodes, and Dlic (Dynein light intermediate chain) in Drosophila. The latter is phosphorylated on Ser(401).
Cross-references
BRENDA2.7.11.37
EC2PDB2.7.11.37
ExplorEnz2.7.11.37
PRIAM enzyme-specific profiles2.7.11.37
KEGG Ligand Database for Enzyme Nomenclature2.7.11.37
IUBMB Enzyme Nomenclature2.7.11.37
IntEnz2.7.11.37
MEDLINEFind literature relating to 2.7.11.37
MetaCyc2.7.11.37
Rhea expert-curated reactions2.7.11.37

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.7.11.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.7.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.-.-.-