Curated Information
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Home > Curated Information Page > PubMed Id: 15766567
Gresko E, Möller A, Roscic A, Schmitz ML (2005) Covalent modification of human homeodomain interacting protein kinase 2 by SUMO-1 at lysine 25 affects its stability. Biochem Biophys Res Commun 329, 1293-9 15766567
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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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, western blotting
Relevant cell lines - cell types - tissues:  HEK293T (epithelial)
Cellular systems studied:  cell lines
Species studied:  human
Enzymes shown to modify site in vitro
Type Enzyme
SUMO LIGASE UBC9 (human)
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
SUMO LIGASE UBC9 (human) transfection of wild-type enzyme
Downstream Regulation
Effect of modification (function):  protein degradation