Curated Information
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Home > Curated Information Page > PubMed Id: 8360143
Hogervorst F, Kuikman I, Noteboom E, Sonnenberg A (1993) The role of phosphorylation in activation of the alpha 6A beta 1 laminin receptor. J Biol Chem 268, 18427-30 8360143
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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S1004-p - ITGA6 iso2 (human)
Modsite: VRVTVFPsKTVAQYS SwissProt Entrez-Gene
Orthologous residues
ITGA6 (human): S1043‑p, ITGA6 iso2 (human): S1004‑p, ITGA6 iso6 (human): S1043‑p, ITGA6 (mouse): S1004‑p, ITGA6 iso2 (mouse): S1004‑p, ITGA6 (rat): S905‑p
Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site
Relevant cell lines - cell types - tissues:  K562 (erythroid)
Cellular systems studied:  cell lines
Species studied:  human
Upstream Regulation
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
phorbol_ester increase S1043 phosphorylation appears to reduce the affinity of the integrin alpha-6 receptor for its ligand, laminin, although PMA treatment results in both increased receptor phosphorylation and ligand affinity.