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Table 1 Highly phosphorylated proteins identified in RBC membrane ghosts

From: Proteomic analysis of ERK1/2-mediated human sickle red blood cell membrane protein phosphorylation

Protein description Gene name Unique phosphorylated peptides Unique phosphorylated residues
Ankyrin-1 ANK1 33 23
Glyophorin A GYPA 23 8
Alpha-adducin ADD1 22 18
Beta-adducin ADD2 18 11
Protein 4.1 EPB41 17 13
Dematin EPB49 16 13
Spectrin beta chain SPTB1 15 11
Band 3 anion transport protein SLC4A1 14 7
Uncharacterized protein LOC388588 YA047 7 5
GTPase-activating protein and VPS9 domain-containing protein 1 GAPVD1 5 5
Lipin-2 LPIN2 5 6
Serine/threonin-protein kinase WNK1 WNK1 5 6
  1. Twelve unique phosphoproteins were identified by at least five unique phosphopeptides. These included proteins of the ankyrin complex (ankyrin-1), the cytoskeleton network (spectrin β chain) and the junctional complex involved in binding integral membrane proteins to cytoskeletal proteins (α- and β-adducins, dematin, and protein 4.1), which affect RBC shape, flexibility and adhesion, or proteins that affect anion transport, protein trafficking and adhesion (band 3 and glycophorin A), G protein activation (GTPase activating protein), lipid biosynthesis (lipin 2) and serine/threonine phosphorylation (serine/threonine protein kinase).