Curated Information
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Curated Information Page
PubMed Id: 18257391 
This page summarizes selected information from the article 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.
Park JM, Intine RV, Maraia RJ (2007) Mouse and human La proteins differ in kinase substrate activity and activation mechanism for tRNA processing. Gene Expr 14, 71-81 18257391
Only sites from this record are displayed on this page. Click on the protein name to open the protein page, and on the RSD number to open the site page. For the complete dataset, click the download button, on the right.
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S366-p - SSB (human)
Orthologous residues
SSB (human): S366‑p, SSB (mouse): , SSB (rat):
Characterization
 Methods used to characterize site in vivo mutation of modification site
 Relevant cell lines - cell types - tissues:  yeast cell
 Cellular systems studied:  primary cells
 Species studied:  yeast
 Comments:  S. pombe
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE CK2A1 (human)
Downstream Regulation
 Effect of modification (function):  activity, induced

S199-p - SSB (mouse)
Orthologous residues
SSB (human): N199‑p, SSB (mouse): S199‑p, SSB (rat): S199‑p
Characterization
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE PKACA (human)
KINASE PKG1 (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
RNA Induces EMSA


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