Curated Information
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Curated Information Page
PubMed Id: 16956385 
Yeh TY, et al. (2006) Regulatory dissociation of Tctex-1 light chain from dynein complex is essential for the apical delivery of rhodopsin. Traffic 7, 1495-502 16956385
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, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus®, click here.
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S82-p - DYNLT1 (human)
Orthologous residues
DYNLT1 (human): S82‑p, DYNLT1 (mouse): S82‑p, DYNLT1 (rat): S82‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site
 Relevant cell lines - cell types - tissues:  293 (epithelial), MDCK (epithelial)
 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
DNCLI1 (human) Disrupts co-immunoprecipitation, yeast two-hybrid
Rhodopsin (human) Induces co-immunoprecipitation
 Comments:  S82E and S82A mutants cause relocalization of rhodopsin; S82E mutant TCTEL1 is excluded, while S82A mutant protein is impaired in release, from dynein complexes


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