Table 1.
Phosphorylation sites and functional annotation for selected phosphoproteins found in common between two or more of the four phosphoproteomic data sets compared in Figures 1B,C.
| Phosphorylation sitesA | |||||
|---|---|---|---|---|---|
| Protein | Bhaskara | Umezawa | Xue | Wang | Description |
|
Increased phosphopeptide abundance under stress or ABA treatment | |||||
| AT1G76810 | S537 (2.5)B | S696 | S696 | T219 | Translation initiation factor 2 (eIF-2) family |
| S604 (DOWN) | |||||
| AT5G38640 | S69 (2.7)B | S69 | N.R.C | S69 | NagB/RpiA/CoA transferase-like, Translation initiation factor elF-2B related |
| S108 (2.5) | S70 | ||||
| S127 (16.5)B | |||||
| AT4G39680 | S292 (1.5) | S415 | N.R. | S144 | SAP-domain nucleic acid binding protein |
| T417 | S319 | ||||
| T421 | S324 | ||||
| S436 | |||||
| S439 | |||||
| AT5G42950D | S1541 (8.6) | S1285 | S1520 | S1472 (Down) | GYF-domain, Essential for Potexvirus accumulation 1, EXA1 |
| AT1G18210 | S88 (1.8) | S54 | S54 | N.R. | Calcium-binding EF-hand family |
| S88 | |||||
| AT2G21230E | S300 (1.7) | S174 | S174 | N.R. | bZIP30 |
| S176 | S176 | ||||
| Decreased phosphopeptide abundance under stress or ABA treatment | |||||
| AT3G05900 | S426 (-2.2) B | S500 | S373 | S482 | Neurofilament protein-related |
| S456 (-1.6) | S455 | ||||
| S456 | |||||
| S500 | |||||
| AT2G37340 | S211 (-1.8) | S202 | N.R. | N.R. | Serine/Arginine-rich protein splicing factor RSZ33 |
| S219 (-1.8) | S204 | ||||
| S239 (-2.4) | S211 | ||||
| S245 (-3.5) | S219 | ||||
| AT5G40450 | S679 (-3.3)B | N.R. | S2802 | N.R. | Regulator of vacuole bulb biogenesis1, RBB1 |
| S2732 (-1.8) | |||||
| S2831 (-2.3)B | |||||
| S2834 (-2.5) | |||||
| AT4G25880 | S30 (-2.1) | N.R. | S154 | N.R. | Pumilio (APUM) regulator of mRNA stability and translation |
Phosphoproteins listed here are indicated by red numbers in Figures 1B,C. APhosphorylation site data were obtained from Supplementary Dataset S4 of Bhaskara et al., (2017), Supplementary Table S3 of Umezawa et al. (2013), Supplementary Tables S6, S7 of Xue et al. (2013), and Supplementary Tables S4, S5 of Wang et al. (2013). For several of the proteins listed here, additional phosphorylation sites were identified in one or more of these studies (and can be found in additional supplemental material from those studies) but either did meet their criteria for altered phosphopeptide abundance or were detected but not quantified and are thus not listed here. For Bhaskara et al. (2017) phosphorylation sites having either fold change greater than 1.5 and P ≥ 0.05 or fold change greater than 2 regardless of P-value are listed. For some of the proteins with up-regulated phosphopeptides in Bhaskara et al. (2017), phosphopeptides having the opposite regulation were also found in other studies and this is indicated by notation of “DOWN” in parentheses. BThis difference in phosphopeptide abundance was not significant at P ≥ 0.05. CN.R. = Not Reported. No phosphopeptide from this protein was reported to be altered in abundance by stress or ABA treatment. DPhosphopeptide abundance of AT5G42950 with phosphorylation at S39 (Kline et al., 2010) or S749 (Stecker et al., 2014) was also found to be increased by 5 min treatment with 50 μM ABA. EPhosphopeptide abundance of bZIP30 (AT2G21230) with phosphorylation at S176 was also found to be increased by 5 min treatment with 50 μM ABA in Kline et al. (2010) and Minkoff et al. (2015) and found to be increased by NaCl and mannitol (confirmed by SRM assay) in Stecker et al. (2014) Note that the supplemental Data of Minkoff et al. (2015) also includes comparison of their ABA affected phosphorylation sites to those identified in Umezawa et al. (2013) and Wang et al. (2013).