Table S1.
Identification of phosphorylated residues and their quantification in the ABD of wild-type Mlph in vitro
| Modified amino acid | Localization probability | Phospho (STY) probabilities | Score | Occupancy, % |
| 400 | 0.708 | ISGSST(0.708)SSEDE | 183 | 18.1 |
| 401 | 0.949 | SGSSTS(0.949)SEDET | 208 | 37.1 |
| 416 | 0.999 | TFLGGS(0.999)PKVCT | 186 | 51.1 |
| 435 | 1.00 | ERNPRS(1.00)PGNPA | 128 | 60.9 |
| 443 | 0.386 | NPARPT(0.386)KSTDE | 51 | ND |
| 445 | 0.989 | ARPTKS(0.989)TDEEL | 122 | 18.9 |
| 446 | 0.988 | RPTKST(0.988)DEELS | 92 | 8.46 |
| 451 | 0.999 | TDEELS(0.999)EMEDR | 214 | 26.9 |
| 491 | 0.999 | LTVKPS(0.999)GKPRR | 145 | ND |
| 498 | 1.00 | KPRRKS(1.00)GIPIF | 150 | 99.7 |
| 517 | 1.00 | DRIPKT(1.00)PPADP | 137 | 22.2 |
| 537 | 0.999 | TTAVPS(0.999)LLRRK | 49 | ND |
| 544 | 0.999 | LRRKYS(0.999)PSSQG | 185 | 49.2 |
| 546 | 0.836 | RKYSPS(0.836)SQGVD | 126 | ND |
| 554 | 0.994 | GVDSGS(0.994)FDRKS | 143 | ND |
| 559 | 0.972 | SFDRKS(0.972)VYRGS | 100 | ND |
| 564 | 0.982 | SVYRGS(0.982)LTQRN | 89 | ND |
The residues found to be phosphorylated in proteomic analyses are highlighted in bold letters as in Fig. S1. The highly conserved residue S498 that also represents the strongest cAMP-dependent protein kinase consensus site was quantitatively phosphorylated in vitro. ND, not detected.