Curated Information
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Home > Curated Information Page > PubMed Id: 15831457
Ihara M, Yamamoto H, Kikuchi A (2005) SUMO-1 modification of PIASy, an E3 ligase, is necessary for PIASy-dependent activation of Tcf-4. Mol Cell Biol 25, 3506-18 15831457
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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K35-sm - PIAS4 (human)
Modsite: GRSkSGLkHELVTRA SwissProt Entrez-Gene
Orthologous residues
PIAS4 (human): K35‑sm, PIAS4 (mouse): K35‑sm
Methods used to characterize site in vivo electrophoretic mobility shift, immunoprecipitation, modification-specific antibody, mutation of modification site, western blotting
Disease tissue studied:  cervical cancer, cervical adenocarcinoma
Relevant cell lines - cell types - tissues:  293 (epithelial), COS (fibroblast), HeLa S3 (cervical)
Cellular systems studied:  cell lines
Species studied:  green monkey, human
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
DESUMOYLASE SENP2 (human) siRNA inhibition of enzyme
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
siRNA increase SENP2 siRNA
Downstream Regulation
Effect of modification (function):  intracellular localization, molecular association, regulation, sumoylation
Effect of modification (process):  transcription, induced
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
PML (human) Disrupts microscopy-colocalization
Comments:  induces sumoylation of Tcf-4