Difference between revisions of "Phosphatase Subfamily PPIP5K"
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PPIP5K has two domains: N-terminal RimK/ATP-grasp domain, and C-terminal HP2 domain <cite>fridy07</cite>. The RimK is the active kinase domain <cite>fridy07, choi07</cite>. | PPIP5K has two domains: N-terminal RimK/ATP-grasp domain, and C-terminal HP2 domain <cite>fridy07</cite>. The RimK is the active kinase domain <cite>fridy07, choi07</cite>. | ||
| − | Unlike other members of HP2 family which are protein or non-protein phosphatases, the HP2 domain of PPIP5K is not catalytically active. Instead, this HP2 domain is specialized for binding PtdIns(3,4,5)P3, as a partial PH (pleckstrin homology) consensus sequence is spliced into this HP2 domain <cite> | + | Unlike other members of HP2 family which are protein or non-protein phosphatases, the HP2 domain of PPIP5K is not catalytically active. Instead, this HP2 domain is specialized for binding PtdIns(3,4,5)P3, as a partial PH (pleckstrin homology) consensus sequence is spliced into this HP2 domain <cite>gokhale11</cite>. |
=== Catalytic activity and functions === | === Catalytic activity and functions === | ||
Revision as of 03:41, 7 January 2015
Phosphatase Classification: Fold HP: Superfamily HP (histidine phosphatase): Family HP, branch 2: PPIP5K
PPIP5K is a phosphoinositol kinase that also has a pseudophosphatase domain which bind to PtdIns(3,4,5)P3. PPIP5K converts InsP6 and 5-InsP7 to 1-InsP7 and InsP8.
Evolution
PPIP5K is found in most eukaryotes. Most vertebrates have at least two copies, while invertebrates usually have one.
Domain
PPIP5K has two domains: N-terminal RimK/ATP-grasp domain, and C-terminal HP2 domain [1]. The RimK is the active kinase domain [1, 2].
Unlike other members of HP2 family which are protein or non-protein phosphatases, the HP2 domain of PPIP5K is not catalytically active. Instead, this HP2 domain is specialized for binding PtdIns(3,4,5)P3, as a partial PH (pleckstrin homology) consensus sequence is spliced into this HP2 domain [3].
Catalytic activity and functions
References
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