Research Article

Application of Phosphoproteomics to Find Targets of Casein Kinase 1 in the Flagellum of Chlamydomonas

Table 1

Phosphoproteins identified in 137c [11] whose phosphopeptides or phosphorylation sites are missing in CKI-7-treated cells.

Flagellar central pair-associated protein; PF6
Hydin-like protein; HYD3
Inner dynein arm I1 intermediate chain; IC138
Intraflagellar transport protein IFT43
Outer dynein arm docking complex subunit 1a,b; ODA-DC1, ODA3
Radial spoke protein 17; RSP17
FAP59c; RecF/RecN/SMC N-terminal domain
FAP116a,d,e; microtubule-binding protein MIP-T3 domain
FAP190a,f; sterile alpha motif
FAP228; callose synthase-like protein; 1,3-beta-glucan synthase component
FAP230; ankyrin repeats; ion transport protein domain
FAP254; putative ankyrin-like protein
FAP288; EF hand
FAP1a,g
FAP93
FAP147
FAP184
FAP263

The function of depicted proteins is given as determined by NCBI BLASTp, along with their conserved domains.
aNot all previously identified peptides (listed in Table S1 in [11]) are present in the CKI-7-treated cells.
bVariants of peptide TISGADTPEEVLAYWEGLK with the phosphorylation sites Thr-345, Ser-347, and Thr-351 as well as variants of peptide ILGYTGSDVEEEEPESEEETEEEANKDDGVVDR with the phosphorylation sites Tyr-697 and Ser-709 are missing.
cPredicted functional domains are present only in the Vs3 model.
dVs2 model differs significantly from Vs3 model.
eThe phosphorylation site Ser-255 in peptide SASPGGEDPLNKSGSAAPK is missing.
fVariants of peptide STSSIGGGYSEPVGSDGEGSDAASAKPR with phosphorylation sites on Ser-370, Ser-375 and Ser-379 are missing.
gThe phosphorylation site Ser-55 in peptide SRGSFQEGQAMVR is missing.