Curated Information
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Curated Information Page
PubMed Id: 14667408 
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.
Kunitoku N, et al. (2003) CENP-A phosphorylation by Aurora-A in prophase is required for enrichment of Aurora-B at inner centromeres and for kinetochore function. Dev Cell 5, 853-64 14667408
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S7-p - CENPA (human)
Orthologous residues
CENPA (human): S7‑p, CENPA (mouse): , CENPA (rat):
Characterization
 Methods used to characterize site in vivo microscopy-colocalization with upstream kinase, mutation of modification site, phospho-antibody, western blotting
 Relevant cell lines - cell types - tissues:  HeLa (cervical)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE AurA (human)
Downstream Regulation
 Effect of modification (function):  molecular association, regulation
 Effect of modification (process):  cell cycle regulation, chromatin organization, altered
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
AurA (human) Induces molecular association, regulation cell cycle regulation, chromatin organization, altered in vitro, co-immunoprecipitation
 Comments:  S7A mutation causes defective kinetochore function and mislocalization of Aurora B.


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