Search results for P60484

Showing 30 results out of 123

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Results (30 results from a total of 123)

Identifier: R-HSA-9659402
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PTEN: P60484
Identifier: R-HSA-9659145
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PTEN: P60484
Identifier: R-HSA-9659400
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PTEN: P60484
Identifier: R-HSA-9659406
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PTEN: P60484
Identifier: R-HSA-9659405
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PTEN: P60484
Identifier: R-HSA-9659148
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PTEN: P60484
Identifier: R-HSA-9659404
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PTEN: P60484
Identifier: R-HSA-9658931
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PTEN: P60484
Identifier: R-HSA-9659120
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PTEN: P60484
Identifier: R-HSA-9659312
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PTEN: P60484
Identifier: R-HSA-9659318
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PTEN: P60484
Identifier: R-HSA-9659189
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PTEN: P60484
Identifier: R-HSA-9659387
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PTEN: P60484
Identifier: R-HSA-9659130
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PTEN: P60484
Identifier: R-HSA-9659129
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PTEN: P60484
Identifier: R-HSA-9659193
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PTEN: P60484
Identifier: R-HSA-9659320
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PTEN: P60484
Identifier: R-HSA-9659390
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PTEN: P60484
Identifier: R-HSA-9659389
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PTEN: P60484
Identifier: R-HSA-9659196
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PTEN: P60484
Identifier: R-HSA-9658915
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PTEN: P60484
Identifier: R-HSA-9659360
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PTEN: P60484
Identifier: R-HSA-9659050
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PTEN: P60484
Identifier: R-HSA-9659305
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PTEN: P60484
Identifier: R-HSA-9659049
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PTEN: P60484
Identifier: R-HSA-9658920
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PTEN: P60484
Identifier: R-HSA-9658926
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PTEN: P60484
Identifier: R-HSA-9659117
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PTEN: P60484
Identifier: R-HSA-9659052
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PTEN: P60484
Identifier: R-HSA-2318465
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PTEN: 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).
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