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  Domain Name: STKc_MASTL
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase. Serine/Threonine Kinases (STKs), Microtubule-associated serine/threonine (MAST) kinase subfamily, MAST-like (MASTL) kinases, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. The human MASTL gene has also been labelled FLJ14813. A missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. To date, the function of MASTL is unknown.
No pairwise interactions are available for this conserved domain.

Total Mutations Found: 29
Total Disease Mutations Found: 10
This domain occurred 17 times on human genes (34 proteins).



  COFFIN-LOWRY SYNDROME
  COFFIN-LOWRY SYNDROME, MILD
  MENTAL RETARDATION, X-LINKED 19
  THROMBOCYTOPENIA 2


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Range on the Protein:  

   Protein ID            Protein Position

Domain Position:  


Feature Name:Total Found:
active site
ATP binding site
substrate binding site
activation loop (A-loop)
































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Please Cite: Peterson, T.A., Adadey, A., Santana-Cruz ,I., Sun, Y., Winder A, Kann, M.G., (2010) DMDM: Domain Mapping of Disease Mutations. Bioinformatics 26 (19), 2458-2459.

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