Curated Information
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Curated Information Page
PubMed Id: 9804419 
Mayans O, et al. (1998) Structural basis for activation of the titin kinase domain during myofibrillogenesis. Nature 395, 863-9 9804419
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.
Click on the protein name to open the protein page, and on the RSD number to open the site page.
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Y32341-p - Titin (human)
Orthologous residues
Titin (human): Y32341‑p, Titin iso3 (human): Y24917‑p, Titin iso6 (human): , Titin (mouse): Y33203‑p, Titin iso3 (mouse): , Titin iso4 (mouse): Y31457‑p, Titin (rat): Y32191‑p, Titin iso2 (rat):
 Methods used to characterize site in vivo mutation of modification site, phospho-antibody
 Relevant cell lines - cell types - tissues:  C2C12 (myoblast)
 Comments:  The large size of titin (2993428 Da /26,926 a.a.) precluded transfecting whole gene. For these studies, only the kinase domain was studied. Tyr 24917 is refered to as tyr 170 in this paper. Like ERK2, Tyr 24917 is buried in the inhibited, unphosphorylated structure of titin kinase.
Downstream Regulation
 Effect of modification (function):  enzymatic activity, induced

S157-p - Telethonin (mouse)
Orthologous residues
Telethonin (human): S157‑p, Telethonin (mouse): S157‑p, Telethonin (rat): S157‑p
 Methods used to characterize site in vivo mass spectrometry
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Titin (human)
 Comments:  Telethonin was contained in extracts of C2C12 mouse skeletal muscle cells.

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