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PDE3B PDE3B PIK3CG PIK3CG PIK3R6 PIK3R6 PIK3CA PIK3CA PIK3R5 PIK3R5 GNB1 GNB1 PIK3R1 PIK3R1 PIK3R2 PIK3R2 PIK3R3 PIK3R3 GNG2 GNG2 PIK3CB PIK3CB
"PIK3R6" - Phosphoinositide 3-kinase regulatory subunit 6 in Homo sapiens
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
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gene co-occurrence
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textmining
co-expression
protein homology
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PIK3R6Phosphoinositide 3-kinase regulatory subunit 6; Regulatory subunit of the PI3K gamma complex. Acts as an adapter to drive activation of PIK3CG by beta-gamma G protein dimers. The PIK3CG-PIK3R6 heterodimer is much less sensitive to beta-gamma G protein dimers than PIK3CG-PIK3R5 and its membrane recruitment and beta-gamma G protein dimer-dependent activation requires HRAS bound to PIK3CG. Recruits of the PI3K gamma complex to a PDE3B-RAPGEF3 signaling complex involved in angiogenesis; signaling seems to involve RRAS (754 aa)    
Predicted Functional Partners:
PIK3CG
Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform; Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Links G-protein coupled receptor activation to PIP3 production. Involved in immune, inflammatory and allergic responses. Modulates [...] (1102 aa)
     
  0.972
PDE3B
cGMP-inhibited 3’,5’-cyclic phosphodiesterase B; Cyclic nucleotide phosphodiesterase with a dual- specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. May play a role in fat metabolism. Regulates cAMP binding of RAPGEF3. Through simultaneous binding to RAPGEF3 and PIK3R6 assembles a signaling complex in which the PI3K gamma complex is activated by RAPGEF3 and which is involved in angiogenesis; Phosphodiesterases (1112 aa)
       
  0.972
PIK3R5
Phosphoinositide 3-kinase regulatory subunit 5; Regulatory subunit of the PI3K gamma complex. Required for recruitment of the catalytic subunit to the plasma membrane via interaction with beta-gamma G protein dimers. Required for G protein-mediated activation of PIK3CG (By similarity) (880 aa)
     
0.966
PIK3CB
Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform; Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns (Phosphatidylinositol), PtdIns4P (Phosphatidylinositol 4- phosphate) and PtdIns(4,5)P2 (Phosphatidylinositol 4,5- bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Involved in the activation of AKT1 upon stimulatio [...] (1070 aa)
       
  0.962
GNG2
Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2; Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction (By similarity) (71 aa)
     
 
  0.962
PIK3R3
Phosphatidylinositol 3-kinase regulatory subunit gamma; Binds to activated (phosphorylated) protein-tyrosine kinases through its SH2 domain and regulates their kinase activity. During insulin stimulation, it also binds to IRS-1 (461 aa)
         
  0.956
GNB1
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1; Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction (340 aa)
         
  0.955
PIK3R2
Phosphatidylinositol 3-kinase regulatory subunit beta; Regulatory subunit of phosphoinositide-3-kinase (PI3K), a kinase that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5- trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Binds to activated (phosphorylated) protein-tyrosine kinases, through its SH2 domain, and acts as an adapter, mediating th [...] (728 aa)
         
  0.946
PIK3R1
Phosphatidylinositol 3-kinase regulatory subunit alpha; Binds to activated (phosphorylated) protein-Tyr kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Necessary for the insulin-stimulated increase in glucose uptake and glycogen synthesis in insulin-sensitive tissues. Plays an important role in signaling in response to FGFR1, FGFR2, FGFR3, FGFR4, KITLG/SCF, KIT, PDGFRA and PDGFRB. Likewise, plays a role in ITGB2 signaling. Modulates the cellular response to ER stress by promoting nuclear translocation [...] (724 aa)
         
  0.939
PIK3CA
Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform; Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns (Phosphatidylinositol), PtdIns4P (Phosphatidylinositol 4- phosphate) and PtdIns(4,5)P2 (Phosphatidylinositol 4,5- bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Participates in cellular signaling in response to [...] (1068 aa)
       
  0.936
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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