Hiester KG, Santy LC (2013) The cytohesin coiled-coil domain interacts with threonine 276 to control membrane association. PLoS One 8, e82084 24303080

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.

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T276-p - cytohesin 2 (human) ▲

Modsite: LGGGRVKtWKRRWFI SwissProt Entrez-Gene Orthologous residues cytohesin 2 (human): T276‑p, cytohesin 2 (mouse): T276‑p, cytohesin 2 (rat): T276‑p Characterization Methods used to characterize site in vivo:  mutation of modification site, western blotting Relevant cell lines - cell types - tissues:  MDCK (epithelial) Cellular systems studied:  cell lines Species studied:  dog Enzymes shown to modify site in vitro:  Type Enzyme KINASE Akt1 (human) Downstream Regulation Effect of modification (function):  molecular association, regulation, protein conformation Effect of modification (process):  signaling pathway regulation Comments:  association with membranes, activation of Arf6

S392-p - cytohesin 2 (human) ▲
Modsite: AARKKRIsVKKKQEQ SwissProt Entrez-Gene Orthologous residues cytohesin 2 (human): S392‑p, cytohesin 2 (mouse): S392‑p, cytohesin 2 (rat): S392‑p Characterization Methods used to characterize site in vivo:  mutation of modification site, phosphopeptide mapping Relevant cell lines - cell types - tissues:  293 (epithelial) Cellular systems studied:  cell lines Species studied:  human