Janczyk PŁ, et al. (2023) Aurora A phosphorylates Ndel1 to reduce the levels of Mad1 and NuMA at spindle poles. Mol Biol Cell 34, br1 36350697

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, 2015, 43:D512-20). To learn more about the scope of PhosphoSitePlus®, click here.

Information from this record has been curated, but not yet edited in PhosphoSitePlus® and may be incomplete.

Click on the protein name to open the protein page, and on the RSD number to open the site page.

Download

S285-p - NDEL1 (human) ▲

Modsite: kDQAsRKsYISGNVN SwissProt Entrez-Gene Orthologous residues NDEL1 (human): S285‑p, NDEL1 iso2 (human): S285‑p, NDEL1 iso3 (human): S285‑p, NDEL1 (mouse): S285‑p, NDEL1 (rat): S285‑p Characterization Methods used to characterize site in vivo:  [32P] ATP in vitro, immunoassay, mass spectrometry (in vitro), mutation of modification site, phospho-antibody Relevant cell lines - cell types - tissues:  E.coli (bacterial), HeLa (cervical) Cellular systems studied:  cell lines Species studied:  bacteria, frog, human Comments:  S3 cells Enzymes shown to modify site in vitro:  Type Enzyme KINASE AurA (human) KINASE AurB (human) Downstream Regulation Effect of modification (process):  cell cycle regulation, cytoskeletal reorganization