Curated Information
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Home > Curated Information Page > PubMed Id: 17018294
Roscic A, et al. (2006) Phosphorylation-dependent control of Pc2 SUMO E3 ligase activity by its substrate protein HIPK2. Mol Cell 24, 77-89 17018294
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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K494-sm - CBX4 (human)
Modsite: PPSSLQVkPEtPASA SwissProt Entrez-Gene
Orthologous residues
CBX4 (human): K494‑sm, CBX4 iso3 (human): K224‑sm, CBX4 (mouse): K490‑sm, CBX4 (rat): K420‑sm
Characterization
Methods used to characterize site in vivo electrophoretic mobility shift, mutation of modification site
Disease tissue studied:  bone cancer
Relevant cell lines - cell types - tissues:  HEK293T (epithelial), U2OS (bone cell)
Cellular systems studied:  cell lines
Species studied:  human
Upstream Regulation
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
adriamycin increase
SB203580 decrease

T497-p - CBX4 (human)
Modsite: SLQVkPEtPASAAVA SwissProt Entrez-Gene
Orthologous residues
CBX4 (human): T497‑p, CBX4 iso3 (human): T227‑p, CBX4 (mouse): A493‑p, CBX4 (rat): A423‑p
Characterization
Methods used to characterize site in vivo electrophoretic mobility shift, mutation of modification site
Disease tissue studied:  bone cancer
Relevant cell lines - cell types - tissues:  HEK293T (epithelial), U2OS (bone cell)
Cellular systems studied:  cell lines
Species studied:  human
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE HIPK2 (human) microscopy-colocalization, transfection of wild-type enzyme, electrophoretic mobility shift, transfection of inactive enzyme, co-immunoprecipitation
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
adriamycin increase
SB203580 decrease
Downstream Regulation
Effect of modification (function):  enzymatic activity, induced, intracellular localization, sumoylation
Comments:  increases CBX4 activity as a SUMO E3 ligase and sumoylation of HIPK2

K32-sm - HIPK2 (human)
Modsite: FCSVKKLkIEPSSNW SwissProt Entrez-Gene
Orthologous residues
HIPK2 (human): K32‑sm, HIPK2 (mouse): K32‑sm, HIPK2 (rat): K32‑sm
Characterization
Methods used to characterize site in vivo electrophoretic mobility shift, mutation of modification site
Disease tissue studied:  bone cancer
Relevant cell lines - cell types - tissues:  HEK293T (epithelial), U2OS (bone cell)
Cellular systems studied:  cell lines
Species studied:  human
Enzymes shown to modify site in vitro
Type Enzyme
SUMO LIGASE CBX4 (human)
SUMO LIGASE UBC9 (human)
SUMO LIGASE UBLE1A (human)
SUMO LIGASE SAE2 (human)
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
SUMO LIGASE CBX4 (human) transfection of wild-type enzyme, co-immunoprecipitation
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
adriamycin increase
PIAS4 (human) no change compared to control
SB203580 no change compared to control
Downstream Regulation
Effect of modification (function):  enzymatic activity, induced, intracellular localization, phosphorylation
Effect of modification (process):  transcription, inhibited
Comments:  K32A (aka K25A) mutant increases phosphorylation of CBX4