Curated Information
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Home > Curated Information Page > PubMed Id: 15817481
Litjens SH, et al. (2005) Modeling and experimental validation of the binary complex of the plectin actin-binding domain and the first pair of fibronectin type III (FNIII) domains of the beta4 integrin. J Biol Chem 280, 22270-7 15817481
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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S1325-p - ITGB4 (human)
Modsite: tQPKRPMsIPIIPDI SwissProt Entrez-Gene
Orthologous residues
ITGB4 (human): S1325‑p, ITGB4 iso2 (human): S1325‑p, ITGB4 iso3 (human): S1325‑p, ITGB4 (mouse): S1327‑p, ITGB4 iso2 (mouse): S1327‑p, ITGB4 iso3 (mouse): S1327‑p, ITGB4 (rat): S1327‑p
Characterization
Methods used to characterize site in vivo mutation of modification site
Disease tissue studied:  PA-JEB
Relevant cell lines - cell types - tissues:  PA-JEB (keratinocyte)
Cellular systems studied:  cell lines
Species studied:  human
Downstream Regulation
Effect of modification (function):  molecular association, regulation
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
Plectin-1 (human) Induces intracellular localization microscopy-colocalization, pull-down assay