Difference between revisions of "Phosphatase Subfamily PPIP5K"
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PPIP5K is conserved across [[Phosphatase_Glossary#Opisthokont|opisthokont]]. Human genome has three copies. | PPIP5K is conserved across [[Phosphatase_Glossary#Opisthokont|opisthokont]]. Human genome has three copies. | ||
+ | === Domain === | ||
+ | PPIP5K has two domains: N-terminal RimK/ATP-grasp domain which encodes its kinase activity, and C-terminal HP2 domain <cite>fridy07</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>. | ||
=== Functions === | === Functions === | ||
Human PPIP5K1 and PPIP5K2 mediates phosphorylation of InsP6 and 5-InsP7 to 1-InsP7 and InsP8, which are multifunctional signaling molecules that regulate diverse cellular activities <cite>fridy07, choi07</cite>. | Human PPIP5K1 and PPIP5K2 mediates phosphorylation of InsP6 and 5-InsP7 to 1-InsP7 and InsP8, which are multifunctional signaling molecules that regulate diverse cellular activities <cite>fridy07, choi07</cite>. |
Revision as of 03:43, 2 January 2015
Phosphatase Classification: Fold HP: Superfamily HP (histidine phosphatase): Family HP, branch 2: PPIP5K
Evolution
PPIP5K is conserved across opisthokont. Human genome has three copies.
Domain
PPIP5K has two domains: N-terminal RimK/ATP-grasp domain which encodes its kinase activity, and C-terminal HP2 domain [1]. 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 [2].
Functions
Human PPIP5K1 and PPIP5K2 mediates phosphorylation of InsP6 and 5-InsP7 to 1-InsP7 and InsP8, which are multifunctional signaling molecules that regulate diverse cellular activities [1, 3].