Search results for P42336

Showing 26 results out of 26

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Results (26 results from a total of 26)

Identifier: R-HSA-74787
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PIK3CA: P42336
Identifier: R-HSA-1500691
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PIK3CA: P42336
The arginine residue at position 38 of PIK3CA (R38) is located at a contact site between the ABD and kinase domains of PIK3CA. Substitution of this arginine residue with cysteine in PIK3CA R38C mutant is likely to disrupt the interaction between the ABD domain and the kinase domain, causing a confomrational change of the kinase domain that leads to increased enzymatic activity (Huang et al. 2007).
Identifier: R-HSA-2395950
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PIK3CA: P42336
The arginine residue at position 38 of PIK3CA (R38) is located at a contact site between the ABD and kinase domains of PIK3CA. Substitution of this arginine residue with glycine in PIK3CA R38G mutant is likely to disrupt the interaction between the ABD domain and the kinase domain, causing a confomrational change of the kinase domain that leads to increased enzymatic activity (Huang et al. 2007).
Identifier: R-HSA-2395947
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PIK3CA: P42336
The arginine residue at position 38 of PIK3CA (R38) is located at a contact site between the ABD and kinase domains of PIK3CA. Substitution of this arginine residue with serine in PIK3CA R38S mutant is likely to disrupt the interaction between the ABD domain and the kinase domain, causing a confomrational change of the kinase domain that leads to increased enzymatic activity (Huang et al. 2007).
Identifier: R-HSA-1500718
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PIK3CA: P42336
The arginine residue at position 38 of PIK3CA (R38) is located at a contact site between the ABD and kinase domains of PIK3CA. Substitution of this arginine residue with histidine in PIK3CA R38H mutant is likely to disrupt the interaction between the ABD domain and the kinase domain, causing a confomrational change of the kinase domain that leads to increased enzymatic activity (Huang et al. 2007). PIK3CA R38H mutant shows reduced PIK3R1 binding and modestly increased catalytic activity (measured indirectly, via AKT1 phosphorylation) under serum starved conditions (Zhao et al. 2005).
Identifier: R-HSA-2328003
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PIK3CA: P42336
Based on structural and functional studies of PIK3CA E542K mutant (Miled et al. 2007), substitution of glutamic acid residue at position 542 of PIK3CA with glutamine is expected to disrupt inhibitory interaction between the helical domain of PIK3CA and the nSH2 domain of PIK3R1, resulting in constitutive activity of the PI3K complex containing PIK3CA E542Q mutant.
Identifier: R-HSA-1500695
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PIK3CA: P42336
Based on structural and functional studies of PIK3CA Q546K mutant (Miled et al. 2007), substitution of glutamine residue at position 546 of PIK3CA with proline is expected to disrupt inhibitory interaction between the helical domain of PIK3CA and the nSH2 domain of PIK3R1, resulting in constitutive activity of the PI3K complex containing PIK3CA Q546P mutant.
Identifier: R-HSA-2362373
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PIK3CA: P42336
Based on structural and functional studies of PIK3CA Q546K mutant (Miled et al. 2007), substitution of glutamine residue at position 546 of PIK3CA with arginine is expected to disrupt inhibitory interaction between the helical domain of PIK3CA and the nSH2 domain of PIK3R1, resulting in constitutive activity of the PI3K complex containing PIK3CA Q546R mutant.
Identifier: R-HSA-2362374
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PIK3CA: P42336
Based on structural and functional studies of PIK3CA Q546K mutant (Miled et al. 2007), substitution of glutamine residue at position 546 of PIK3CA with histidine is expected to disrupt inhibitory interaction between the helical domain of PIK3CA and the nSH2 domain of PIK3R1, resulting in constitutive activity of the PI3K complex containing PIK3CA Q546H mutant.
Identifier: R-HSA-1500709
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PIK3CA: P42336
Based on structural and functional studies of the PIK3CA E545K mutant (Miled et al. 2007, Huang et al. 2007, Zhao et al. 2005), the substitution of glutamic acid residue at position 545 of PIK3CA with glycine is expected to disrupt inhibitory interaction between the helical domain of PIK3CA and the nSH2 domain of PIK3R1 and result in the constitutive activity of the PI3K complex containing PIK3CA E545G mutant.
Identifier: R-HSA-2362375
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PIK3CA: P42336
Based on structural and functional studies of PIK3CA Q546L mutant (Miled et al. 2007), substitution of glutamine residue at position 546 of PIK3CA with leucine is expected to disrupt inhibitory interaction between the helical domain of PIK3CA and the nSH2 domain of PIK3R1, resulting in constitutive activity of the PI3K complex containing PIK3CA Q546L mutant.
Identifier: R-HSA-2328074
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PIK3CA: P42336
Based on structural and functional studies of PIK3CA E542K mutant (Miled et al. 2007), substitution of glutamic acid residue at position 542 of PIK3CA with valine is expected to disrupt inhibitory interaction between the helical domain of PIK3CA and the nSH2 domain of PIK3R1, resulting in constitutive activity of the PI3K complex containing PIK3CA E542V mutant.
Identifier: R-HSA-2362365
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PIK3CA: P42336
Based on structural and functional studies of the PIK3CA E545K mutant (Miled et al. 2007, Huang et al. 2007, Zhao et al. 2005), the substitution of glutamic acid residue at position 545 of PIK3CA with valine is expected to disrupt inhibitory interaction between the helical domain of PIK3CA and the nSH2 domain of PIK3R1 and result in the constitutive activity of the PI3K complex containing PIK3CA E545V mutant.
Identifier: R-HSA-2362383
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PIK3CA: P42336
Based on structural and functional studies of PIK3CA Q546K mutant (Miled et al. 2007), substitution of glutamine residue at position 546 of PIK3CA with glutamic acid is expected to disrupt inhibitory interaction between the helical domain of PIK3CA and the nSH2 domain of PIK3R1, resulting in constitutive activity of the PI3K complex containing PIK3CA Q546E mutant.
Identifier: R-HSA-2362362
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PIK3CA: P42336
Based on structural and functional studies of the PIK3CA E545K mutant (Miled et al. 2007, Huang et al. 2007, Zhao et al. 2005), the substitution of glutamic acid residue at position 545 of PIK3CA with glutamine is expected to disrupt inhibitory interaction between the helical domain of PIK3CA and the nSH2 domain of PIK3R1 and result in the constitutive activity of the PI3K complex containing PIK3CA E545Q mutant.
Identifier: R-HSA-1500706
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PIK3CA: P42336
Substitution of glutamic acid residue at position 545 of PIK3CA with lysine disrupts inhibitory interaction between the helical domain of PIK3CA and the nSH2 domain of PIK3R1. The PI3K complex containing PIK3CA E545K mutant is constitutively active under serum starved conditions (Miled et al. 2007, Huang et al. 2007, Zhao et al. 2005).
Identifier: R-HSA-2362355
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PIK3CA: P42336
Similar to PIK3CA E545K mutant (Miled et al. 2007, Huang et al. 2007, Zhao et al. 2005), PIK3CA E545A mutant is constitutively active in the absence of growth factors (Horn et al. 2008). The underlying mechanism for oncogenic activation is likely to be identical - the substitution of glutamic acid residue at position 545 of PIK3CA with alanine is expected to disrupt inhibitory interaction between the helical domain of PIK3CA and the nSH2 domain of PIK3R1.
Identifier: R-HSA-1500705
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PIK3CA: P42336
Substitution of glutamine residue at position 546 of PIK3CA with lysine disrupts inhibitory interaction between the helical domain of PIK3CA and the nSH2 domain of PIK3R1. The PI3K complex containing PIK3CA Q546K mutant is constitutively active (Miled et al. 2007).
Identifier: R-HSA-1500701
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PIK3CA: P42336
Substitution of glutamic acid residue at position 542 of PIK3CA with lysine disrupts inhibitory interaction between the helical domain of PIK3CA and the nSH2 domain of PIK3R1. The PI3K complex containing PIK3CA E542K mutant is constitutively active (Miled et al. 2007, Horn et al. 2008).
Identifier: R-HSA-1500720
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PIK3CA: P42336
Substitution of histidine residue with tyrosine at position 1047 in the kinase domain of PIK3CA is predicted, based on PIK3CA crystal structure, to change the conformation of the activation loop (Huang et al. 2007).
Identifier: R-HSA-2395932
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PIK3CA: P42336
Substitution of methionine residue with valine at position 1043 in the kinase domain of PIK3CA is predicted, based on PIK3CA crystal structure, to change the conformation of the activation loop (Huang et al. 2007).
Identifier: R-HSA-2395934
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PIK3CA: P42336
Substitution of methionine residue with threonine at position 1043 in the kinase domain of PIK3CA is predicted, based on PIK3CA crystal structure, to change the conformation of the activation loop (Huang et al. 2007).
Identifier: R-HSA-1500719
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PIK3CA: P42336
Substitution of methionine residue with isoleucine at position 1043 in the kinase domain of PIK3CA is predicted, based on PIK3CA crystal structure, to change the conformation of the activation loop (Huang et al. 2007). The PI3K complex containing PIK3CA M1043I mutant is constitutively active, but its activity may be additional boosted by binding of PIK3R1 regulatory subunit to phosphopeptides generated by activated receptor tyrosine kinases (Hon et al. 2011).
Identifier: R-HSA-1500716
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PIK3CA: P42336
Substitution of histidine residue with arginine at position 1047 in the kinase domain of PIK3CA is predicted, based on PIK3CA crystal structure, to change the conformation of the activation loop (Huang et al. 2007). The PI3K complex containing PIK3CA H1047R mutant is constitutively active, in the absence of growth factors (Zhao et al. 2005, Horn et al. 2008), but its activity may be additional boosted by binding of PIK3R1 regulatory subunit to phosphopeptides generated by activated receptor tyrosine kinases (Hon et al. 2011).
Identifier: R-HSA-1500714
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PIK3CA: P42336
Substitution of histidine residue with leucine at position 1047 in the kinase domain of PIK3CA is predicted, based on PIK3CA crystal structure, to change the conformation of the activation loop (Huang et al. 2007). The PI3K complex containing PIK3CA H1047L mutant is constitutively active, but its activity may be additional boosted by binding of PIK3R1 regulatory subunit to phosphopeptides generated by activated receptor tyrosine kinases (Hon et al. 2011).
Species: Homo sapiens
Curator: Bruce May
Designer: Cristoffer Sevilla
PIK3CA,B,G icon
Set of Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha, beta and gamma.
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