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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).