Curated Information
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Curated Information Page
PubMed Id: 11018042 
Sumi T, Matsumoto K, Nakamura T (2001) Specific activation of LIM kinase 2 via phosphorylation of threonine 505 by ROCK, a Rho-dependent protein kinase. J Biol Chem 276, 670-6 11018042
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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T505-p - LIMK2 (rat)
Orthologous residues
LIMK2 (human): T505‑p, LIMK2 iso2 (human): T484‑p, LIMK2 iso3 (human): T484‑p, LIMK2 (mouse): T505‑p, LIMK2 (rat): T505‑p
 Methods used to characterize site in vivo mutation of modification site, phosphoamino acid analysis
 Relevant cell lines - cell types - tissues:  COS (fibroblast), HeLa (cervical)
 Cellular systems studied:  cell lines
 Species studied:  human, monkey
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE ROCK1 (rat) genetic transfer of constitutively active upstream enzyme, inhibition of upstream enzyme
Downstream Regulation
 Effect of modification (function):  activity, induced
 Comments:  T505 phosphorylation is also essential for the induction of actin cytoskeletal changes.

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