Table 1. mRNP components differentially phosphorylated in kinase-dead mutants.
| Protein | Identified Phosphosite(s) a | KD/WT (normalized) b | Kinase-dead mutant |
|---|---|---|---|
| Dcp2p | S747/ S751/ S771/ S439 | 4.3/ 1.8/ 0.44/ 2.6 | kss1/ fus3/ ste20/ snf1 |
| Ded1p | S369 | 4.9 | ste20 |
| Dhh1p | S14 | 0.34 | elm1 |
| Eap1p | S30/ S282/ T391 | 0.31/ 0.12/ 0.28 | snf1 |
| Edc3p | S255 | 1.8 | fus3 |
| Hrp1p | S2, S3 | 2.7 | ste7 |
| Igo1p | S157 | 0.03/ 0.08 | snf1/ tpk2 |
| Ngr1p | S524 | 0.17 | snf1 |
| Pat1 | S255 | 4.5 | ste20 |
| Pbp1 | S106/ S436 | 0.32/ 2.9 | elm1/ kss1 |
| Sbp1 | T91 | 3.2/ 2.6/ 3.1/ 5.1/ 8.1 | snf1/ ste7/ ste11/ ste20/ tpk2 |
| Tif4632p | S74/ T355 | 1.8/ 2.6 | fus3/ elm1 |
| Xrn1p | S1510 | 2.9 | kss1 |
| Ygr250cp | S482, T486/ S501/ T653 | 4.7/ 7.2/ 4.2 | ste20/ snf1/ ste20 |
aResidues on distinct phosphopeptides are separated by slashes; residues on a single phosphopeptide are separated by commas. Phosphorylation sites were localized with p>0.75.
bRatio of phosphopeptide in kinase-dead mutant relative to wild-type normalized to protein level. All results exhibit a statistical significance of ≤0.05.