Curated Information
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Home > Curated Information Page > PubMed Id: 20573420
Wang C, et al. (2010) Plk1-mediated mitotic phosphorylation of PinX1 regulates its stability. Eur J Cell Biol 89, 748-56 20573420
This page summarizes selected information from the record referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2015, 43:D512-20). To learn more about the scope of PhosphoSitePlus®, click here.
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S110-p - PINX1 (human)
Modsite: SDKKEKKsFSLEEKs SwissProt Entrez-Gene
Orthologous residues
PINX1 (human): S110‑p, PINX1 (mouse): S110‑p, PINX1 (rat): S110‑p
Characterization
Methods used to characterize site in vivo electrophoretic mobility shift, immunoprecipitation, mass spectrometry (in vitro), mutation of modification site, western blotting
Relevant cell lines - cell types - tissues:  HEK293T (epithelial), HeLa (cervical)
Cellular systems studied:  cell lines
Species studied:  human
Comments:  multiple sites mutant (5A)
Enzymes shown to modify site in vitro
Type Enzyme
KINASE PLK1 (human)
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PLK1 (human) pharmacological inhibitor of upstream enzyme, co-immunoprecipitation, transfection of wild-type enzyme
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
nocodazole increase
GW_843682X nocodazole inhibit treatment-induced increase
Downstream Regulation
Effect of modification (function):  protein degradation, ubiquitination

S117-p - PINX1 (human)
Modsite: sFSLEEKsKISKNRV SwissProt Entrez-Gene
Orthologous residues
PINX1 (human): S117‑p, PINX1 (mouse): S117‑p, PINX1 (rat): S117‑p
Characterization
Methods used to characterize site in vivo electrophoretic mobility shift, immunoprecipitation, mass spectrometry (in vitro), mutation of modification site, western blotting
Relevant cell lines - cell types - tissues:  HEK293T (epithelial), HeLa (cervical)
Cellular systems studied:  cell lines
Species studied:  human
Comments:  multiple sites mutant (5A)
Enzymes shown to modify site in vitro
Type Enzyme
KINASE PLK1 (human)
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PLK1 (human) pharmacological inhibitor of upstream enzyme, co-immunoprecipitation, transfection of wild-type enzyme
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
nocodazole increase
GW_843682X nocodazole inhibit treatment-induced increase
Downstream Regulation
Effect of modification (function):  protein degradation, ubiquitination

T141-p - PINX1 (human)
Modsite: DLSSRSKtDLDCIFG SwissProt Entrez-Gene
Orthologous residues
PINX1 (human): T141‑p, PINX1 (mouse): T141‑p, PINX1 (rat): T141‑p
Characterization
Methods used to characterize site in vivo electrophoretic mobility shift, immunoprecipitation, mass spectrometry (in vitro), mutation of modification site, western blotting
Relevant cell lines - cell types - tissues:  HEK293T (epithelial), HeLa (cervical)
Cellular systems studied:  cell lines
Species studied:  human
Comments:  multiple sites mutant (5A)
Enzymes shown to modify site in vitro
Type Enzyme
KINASE PLK1 (human)
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PLK1 (human) pharmacological inhibitor of upstream enzyme, co-immunoprecipitation, transfection of wild-type enzyme
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
nocodazole increase
GW_843682X nocodazole inhibit treatment-induced increase
Downstream Regulation
Effect of modification (function):  protein degradation, ubiquitination

S226-p - PINX1 (human)
Modsite: ATGKDVEsyLQPkAK SwissProt Entrez-Gene
Orthologous residues
PINX1 (human): S226‑p, PINX1 (mouse): N232‑p, PINX1 (rat): N232‑p
Characterization
Methods used to characterize site in vivo electrophoretic mobility shift, immunoprecipitation, mass spectrometry (in vitro), mutation of modification site, western blotting
Relevant cell lines - cell types - tissues:  HEK293T (epithelial), HeLa (cervical)
Cellular systems studied:  cell lines
Species studied:  human
Comments:  multiple sites mutant (5A)
Enzymes shown to modify site in vitro
Type Enzyme
KINASE PLK1 (human)
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PLK1 (human) pharmacological inhibitor of upstream enzyme, co-immunoprecipitation, transfection of wild-type enzyme
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
nocodazole increase
GW_843682X nocodazole inhibit treatment-induced increase
Downstream Regulation
Effect of modification (function):  protein degradation, ubiquitination

T317-p - PINX1 (human)
Modsite: EDATLEEtLVKKKKK SwissProt Entrez-Gene
Orthologous residues
PINX1 (human): T317‑p, PINX1 (mouse): A321‑p, PINX1 (rat): A321‑p
Characterization
Methods used to characterize site in vivo electrophoretic mobility shift, immunoprecipitation, mass spectrometry (in vitro), mutation of modification site, western blotting
Relevant cell lines - cell types - tissues:  HEK293T (epithelial), HeLa (cervical)
Cellular systems studied:  cell lines
Species studied:  human
Comments:  multiple sites mutant (5A)
Enzymes shown to modify site in vitro
Type Enzyme
KINASE PLK1 (human)
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PLK1 (human) pharmacological inhibitor of upstream enzyme, co-immunoprecipitation, transfection of wild-type enzyme
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
nocodazole increase
GW_843682X nocodazole inhibit treatment-induced increase
Downstream Regulation
Effect of modification (function):  protein degradation, ubiquitination