Title : A key role for the phosphorylation of Ser440 by the cyclic AMP-dependent protein kinase in regulating the activity of the Src homology 2 domain-containing Inositol 5'-phosphatase (SHIP1).

Pub. Date : 2010 Nov 5

PMID : 20810657






3 Functional Relationships(s)
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1 Using a combination of approaches, we identified the serine residue regulating SHIP1 activity. Serine inositol polyphosphate-5-phosphatase D Homo sapiens
2 After mass spectrometric identification of 17 serine and threonine residues on SHIP1 as being phosphorylated by PKA in vitro, studies with truncation mutants of SHIP1 narrowed the phosphorylation site to the catalytic region between residues 400 and 866. Serine inositol polyphosphate-5-phosphatase D Homo sapiens
3 These results suggest that activation of SHIP1 by PKA via phosphorylation on Ser(440) is an important regulatory event in hematopoietic cells. Serine inositol polyphosphate-5-phosphatase D Homo sapiens