Curated Information
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Curated Information Page
PubMed Id: 15105425 
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.
Sevilla A, Santos CR, Vega FM, Lazo PA (2004) Human vaccinia-related kinase 1 (VRK1) activates the ATF2 transcriptional activity by novel phosphorylation on Thr-73 and Ser-62 and cooperates with JNK. J Biol Chem 279, 27458-65 15105425
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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S62-p - ATF-2 (human)
Orthologous residues
ATF‑2 (human): S62‑p, ATF‑2 (mouse): S44‑p, ATF‑2 (rat): S44‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site, phosphopeptide mapping
 Relevant cell lines - cell types - tissues:  293T (epithelial), HeLa (cervical)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE VRK1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE VRK1 (human) mutation in upstream enzyme recognition motif, transfection of inactive enzyme, co-immunoprecipitation
Downstream Regulation
 Effect of modification (function):  activity, induced, protein stabilization
 Effect of modification (process):  transcription, induced

T69-p - ATF-2 (human)
Orthologous residues
ATF‑2 (human): T69‑p, ATF‑2 (mouse): T51‑p, ATF‑2 (rat): T51‑p

T71-p - ATF-2 (human)
Orthologous residues
ATF‑2 (human): T71‑p, ATF‑2 (mouse): T53‑p, ATF‑2 (rat): T53‑p

T73-p - ATF-2 (human)
Orthologous residues
ATF‑2 (human): T73‑p, ATF‑2 (mouse): T55‑p, ATF‑2 (rat): T55‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site, phosphopeptide mapping
 Relevant cell lines - cell types - tissues:  293T (epithelial), HeLa (cervical)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE VRK1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE VRK1 (human) mutation in upstream enzyme recognition motif, transfection of inactive enzyme, co-immunoprecipitation
Downstream Regulation
 Effect of modification (function):  activity, induced, protein stabilization
 Effect of modification (process):  transcription, induced


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