Search results for P60484

Showing 30 results out of 42

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Results (30 results from a total of 42)

Identifier: P60484-1
Species: Homo sapiens
Primary external reference: UniProt: P60484-1
Identifier: R-HSA-6807264
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: P60484
Identifier: R-HSA-6807247
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P60484
Identifier: R-HSA-8948777
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P60484
Identifier: R-HSA-6807280
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P60484
Identifier: R-HSA-8851009
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P60484
Identifier: R-HSA-8850936
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P60484
Identifier: R-HSA-8948798
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P60484
Identifier: R-HSA-8948841
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P60484
Identifier: R-HSA-8847980
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P60484
Identifier: R-HSA-2318571
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PTEN: P60484
Identifier: R-HSA-2318568
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P60484
Identifier: R-HSA-2318573
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P60484
Identifier: R-HSA-2318465
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P60484
PTEN missense mutation that results in the substitution of serine at position 170 with glyciine affects the phosphatase domain of PTEN. Serine residue S170 is involved in the formation of intedomain hydrogen bonds between the phosphatase domain and the membrane-binding C2 domain (Lee et al. 1999). PTEN S170G (Ser170Gly) mutant has not been studied directly but is assumed to have impaired phosphoinositide phosphatase activity similar to other S170 substitution mutants of PTEN (Han et al. 2000).
Identifier: R-HSA-2318455
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P60484
PTEN missense mutation that results in the substitution of serine at position 170 with isoleucine affects the phosphatase domain of PTEN. Serine residue S170 is involved in the formation of intedomain hydrogen bonds between the phosphatase domain and the membrane-binding C2 domain (Lee et al. 1999). PTEN S170I (Ser170Ile) mutant has not been studied directly but is assumed to have impaired phosphoinositide phosphatase activity similar to other S170 substitution mutants of PTEN (Han et al. 2000). PTEN S170I is found as a germline mutation in Cowden and Bannayan-Riley-Ruvalcaba familial cancer syndromes (Pilarski et al. 2011).
Identifier: R-HSA-2318503
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P60484
PTEN missense mutation that results in the substitution of glycine at position 129 with valine affects the conserved H-C-K/R-A-G-K-G-R sequence (corresponding to HCXXGXXR motif of protein tyrosine phosphatases) in the catalytic cleft of the PTEN phosphatase domain. PTEN G129V (Gly129Val) mutant has not been studied directly but is assumed to have impaired phosphoinositide phosphatase activity, similar to other G129 substitution mutants of PTEN (Han et al. 2000).
Identifier: R-HSA-2317461
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P60484
PTEN missense mutation that results in the substitution of cysteine at position 124 with phenylalanine affects the conserved H-C-K/R-A-G-K-G-R sequence (corresponding to HCXXGXXR motif of protein tyrosine phosphatases) in the catalytic cleft of the PTEN phosphatase domain. The cystein residue in this motif, corresponding to C124 of human PTEN, 'attacks' the phosphate group of a substrate and forms a thio-phosphate intermediate during dephosphorylation reaction (Guan and Dixon 1991, Barford et al. 1994, Lee et al. 1999). PTEN C124F (Cys124Phe) mutant has not been functionally studied but is assumed to have impaired phosphoinositide phosphatase activity similar to other C124 substitution mutants (Han et al. 2000, Koul et al. 2002).
Identifier: R-HSA-2317432
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P60484
PTEN missense mutation that results in the substitution of arginine at position 130 with proline affects the conserved H-C-K/R-A-G-K-G-R sequence (corresponding to HCXXGXXR motif of protein tyrosine phosphatases) in the catalytic cleft of the PTEN phosphatase domain. The arginine residue in this motif, corresponding to R130 of human PTEN, is essential for catalysis (Barford et al. 1994, Lee et al. 1999). PTEN R130P mutant has not been functionally studied but is assumed to have impaired phosphoinositide phosphatase activity, similar to other PTEN R130 substitution mutants (Han et al. 2000).
Identifier: R-HSA-2317464
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P60484
PTEN missense mutation that results in the substitution of cysteine at position 124 with tyrosine affects the conserved H-C-K/R-A-G-K-G-R sequence (corresponding to HCXXGXXR motif of protein tyrosine phosphatases) in the catalytic cleft of the PTEN phosphatase domain. The cystein residue in this motif, corresponding to C124 of human PTEN, 'attacks' the phosphate group of a substrate and forms a thio-phosphate intermediate during dephosphorylation reaction (Guan and Dixon 1991, Barford et al. 1994, Lee et al. 1999). PTEN C124Y (Cys124Tyr) mutant has not been functionally studied but is assumed to have impaired phosphoinositide phosphatase activity similar to other C124 substitution mutants (Han et al. 2000, Koul et al. 2002).
Identifier: R-HSA-2317379
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P60484
PTEN missense mutation that results in the substitution of cysteine at position 124 with serine affects the conserved H-C-K/R-A-G-K-G-R sequence (corresponding to HCXXGXXR motif of protein tyrosine phosphatases) in the catalytic cleft of the PTEN phosphatase domain. The cystein residue in this motif, corresponding to C124 of human PTEN, 'attacks' the phosphate group of a substrate and forms a thio-phosphate intermediate during dephosphorylation reaction (Guan and Dixon 1991, Barford et al. 1994, Lee et al. 1999). PTEN C124S (Cys124Ser) mutant shows markedly decreased phosphoinositide phosphatase activity (Koul et al. 2002).
Identifier: R-HSA-2317473
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P60484
PTEN missense mutation that results in the substitution of arginine at position 173 with histidine affects the phosphatase domain of PTEN. Arginine residue R173 is involved in the formation of intedomain hydrogen bonds between the phosphatase domain and the membrane-binding C2 domain (Lee et al. 1999). PTEN R173H (Arg173His) mutant shows markedly decreased phosphoinositide phosphatase activity (Han et al. 2000).
Identifier: R-HSA-2317478
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P60484
PTEN missense mutation that results in the substitution of arginine at position 173 with cysteine affects the phosphatase domain of PTEN. Arginine residue R173 is involved in the formation of intedomain hydrogen bonds between the phosphatase domain and the membrane-binding C2 domain (Lee et al. 1999). PTEN R173C (Arg173Cys) mutant shows markedly decreased phosphoinositide phosphatase activity (Han et al. 2000).
Identifier: R-HSA-2318437
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P60484
PTEN missense mutation that results in the substitution of serine at position 170 with arginine affects the phosphatase domain of PTEN. Serine residue S170 is involved in the formation of intedomain hydrogen bonds between the phosphatase domain and the membrane-binding C2 domain (Lee et al. 1999). PTEN S170R (Ser170Arg) mutant shows markedly decreased phosphoinositide phosphatase activity (Han et al. 2000). PTEN S170R is found as a germline mutation in Bannayan-Riley-Ruvalcaba familial cancer syndrome (Marsh et al. 1997).
Identifier: R-HSA-2318469
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P60484
PTEN missense mutation that results in the substitution of histidine at position 123 with tyrosine affects the conserved H-C-K/R-A-G-K-G-R sequence (corresponding to HCXXGXXR motif of protein tyrosine phosphatases) in the catalytic cleft of the PTEN phosphatase domain. Replacement of the histidine residue in this motif, corresponding to H123 of human PTEN, with tyrosine results in a markedly decreased phosphoinositide phosphatase activity (Lee et al. 1999).
Identifier: R-HSA-2318501
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P60484
PTEN missense mutation that results in the substitution of glycine at position 129 with arginine affects the conserved H-C-K/R-A-G-K-G-R sequence (corresponding to HCXXGXXR motif of protein tyrosine phosphatases) in the catalytic cleft of the PTEN phosphatase domain. PTEN G129R (Gly129Arg) mutant shows markedly decreased phosphoinositide phosphatase activity (Han et al. 2000).
Identifier: R-HSA-2318565
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P60484
PTEN missense mutation that results in the substitution of histidine at position 93 with glutamine affects the conserved WPD loop of the phosphatase domain of PTEN. PTEN H93Q (His93Gln) mutant shows markedly decreased phosphoinositide phosphatase activity (Rodriguez-Escudero et al. 2011).
Identifier: R-HSA-2317416
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P60484
PTEN missense mutation that results in the substitution of arginine at position 130 with glutamine affects the conserved H-C-K/R-A-G-K-G-R sequence (corresponding to HCXXGXXR motif of protein tyrosine phosphatases) in the catalytic cleft of the PTEN phosphatase domain. The arginine residue in this motif, corresponding to R130 of human PTEN, is essential for catalysis (Barford et al. 1994, Lee et al. 1999). PTEN R130Q (Arg130Gln) mutant shows markedly decreased phosphoinositide phosphatase activity (Han et al. 2000). PTEN R130Q substitution is frequently found in endometrial cancer (Konopka et al. 2007).
Identifier: R-HSA-2317480
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P60484
PTEN missense mutation that results in the substitution of arginine at position 173 with proline affects the phosphatase domain of PTEN. Arginine residue R173 is involved in the formation of intedomain hydrogen bonds between the phosphatase domain and the membrane-binding C2 domain (Lee et al. 1999).PTEN R173P (Arg173Pro) mutant shows markedly decreased phosphoinositide phosphatase activity (Han et al. 2000).
Identifier: R-HSA-2318408
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P60484
PTEN missense mutation that results in the substitution of serine at position 170 with asparagine affects the phosphatase domain of PTEN. Serine residue S170 is involved in the formation of intedomain hydrogen bonds between the phosphatase domain and the membrane-binding C2 domain (Lee et al. 1999).PTEN S170N (Ser170Asn) mutant shows markedly decreased phosphoinositide phosphatase activity (Han et al. 2000).
Identifier: R-HSA-2318509
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P60484
PTEN missense mutation that results in the substitution of glycine at position 129 with glutamic acid affects the conserved H-C-K/R-A-G-K-G-R sequence (corresponding to HCXXGXXR motif of protein tyrosine phosphatases) in the catalytic cleft of the PTEN phosphatase domain. PTEN G129E (Gly129Glu) mutant shows markedly decreased phosphoinositide phosphatase activity (Han et al. 2000).