Below is the list of all references used in our database. After clicking on the short reference name or the modification count, you will get a list of modifications imported from that particular source.
| Short name | Full reference | Modification count |
|---|---|---|
| Post-translational modifications: | ||
| Albuquerque et al. (2008) | Albuquerque, C.P., Smolka, M.B., Payne, S.H., Bafna, V., Eng, J., Zhou, H. (2008). A multidimensional chromatography technology for in-depth phosphoproteome analysis. Molecular and Cellular Proteomics 7(7):1389-1396. https://doi.org/10.1074/mcp.M700468-MCP200 Phosphoproteome of cells grown under standard conditions (YPD media) compared to cells exposed to DNA-damaging agent (0.05% methyl methanesulfonate) |
1649 |
| Alepuz et al. (2003) | Alepuz, P.M., de Nadal, E., Zapater, M., Ammerer, G., Posas, F. (2003). Osmostress-induced transcription by Hot1 depends on a Hog1-mediated recruitment of the RNA Pol II. EMBO J 22: 2433-2442. https://doi.org/10.1093/emboj/cdg243 Osmostress regulated trasncrition regulated by protein kinase Hog1 |
1 |
| Alexandru et al. (2001) | Alexandru, G., Uhlmann, F., Mechtler, K., Poupart, M.A., Nasmyth, K. (2001). Phosphorylation of the cohesin subunit Scc1 by Polo/Cdc5 kinase regulates sister chromatid separation in yeast. Cell 105: 459-472. https://doi.org/10.1016/s0092-8674(01)00362-2 Phoshorylation of the cohesin subunit Mdc1/Scc1 by Polo/Cdc5 protein kinase |
10 |
| Anders et al. (2020) | Anders, A., Ghosh, B., Glatter, T., Sourjik, V. (2020). Design of a MAPK signalling cascade balances energetic cost versus accuracy of information transmission. Nat Commun 11: 3494. https://doi.org/10.1038/s41467-020-17276-4 Analysis of phosphorylatio-dephosphorylation cyclin of MAP kinases |
1 |
| Annan et al. (2008) | Annan, R.B., Wu, C., Waller, D.D., Whiteway, M., Thomas, D.Y. (2008). Rho5p is involved in mediating the osmotic stress response in Saccharomyces cerevisiae, and its activity is regulated via Msi1p and Npr1p by phosphorylation and ubiquitination. Eukaryot Cell 7: 1441-1449. https://doi.org/10.1128/EC.00120-08 Osmotic stress-induced phosphorylation and ubiquitination of the small GTPase Rho5 |
2 |
| Anton et al. (2013) | Anton, F., Dittmar, G., Langer, T., Escobar-Henriques, M. (2013). Two deubiquitylases act on mitofusin and regulate mitochondrial fusion along independent pathways. Mol Cell 49: 487-498. https://doi.org/10.1016/j.molcel.2012.12.003 Ubiquitylation of the mitofusin Fzo1 |
2 |
| Aoki et al. (2011) | Aoki, Y., Kanki, T., Hirota, Y., Kurihara, Y., Saigusa, T., Uchiumi, T., Kang, D. (2011). Phosphorylation of Serine 114 on Atg32 mediates mitophagy. Mol Biol Cell 22: 3206-3217. https://doi.org/10.1091/mbc.E11-02-0145 Mapping phosphorylated sites on Atg32 protein |
2 |
| Back et al. (2019) | Back, S., Gorman, A.W., Vogel, C., Silva, G.M. (2019). Site-specific K63 ubiquitinomics provides insights into translation regulation under stress. Journal of Proteome Research 18(1): 309-318. https://doi.org/10.1021/acs.jproteome.8b00623 Ubiquitylated sites on proteins in cells exposed to oxidative stress |
379 |
| Bai et al. (2017) | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. https://doi.org/10.1016/j.funbio.2017.06.004 A database of phosphosites on fungal proteins [not curated since 2017] |
8186 |
| Baro et al. (2018) | Baro, B., Játiva, S., Calabria, I., Vinaixa, J., Bech-Serra, J.J., de LaTorre, C., Rodrigues, J., Hernáez, M.L., Gil, C., Barceló-Batllori, S., Larsen, M.R., Queralt, E. (2018). SILAC-based phosphoproteomics reveals new PP2A-Cdc55-regulated processes in budding yeast. Gigascience 7: giy047. https://doi.org/10.1093/gigascience/giy047 Changes in phosphoproteome in Cdc55 deficient cells reveal substrates of PP2A important for mitotic exit |
8 |
| Barz et al. (2020) | Barz, S., Kriegenburg, F., Henning, A., Bhattacharya, A., Mancilla, H., Sánchez-Martín, P., Kraft, C. (2020). Atg1 kinase regulates autophagosome-vacuole fusion by controlling SNARE bundling. EMBO Rep 21: e51869. https://doi.org/10.15252/embr.202051869 Regulation of Ykt6 activity on autophagosomes via phosphorylation by the Atg1 kinase |
2 |
| Belanger et al. (2005) | Belanger, K.D., Gupta, A., MacDonald, K.M., Ott, C.M., Hodge, C.A., Cole, C.M., Davis, L.I. (2005). Nuclear pore complex function in Saccharomyces cerevisiae is influenced by glycosylation of the transmembrane nucleoporin Pom152p. Genetics 171: 935-947. https://doi.org/10.1534/genetics.104.036319 Glycosylation of nuclear pore complex proteins |
1 |
| Benzi et al. (2020) | Benzi, G., Camasses, A., Atsunori, Y., Katou, Y., Shirahige, K., Piatti, S. (2020). A common molecular mechanism underlies the role of Mps1 in chromosome biorientation and the spindle assembly checkpoint. EMBO Rep 21: e50257. https://doi.org/10.15252/embr.202050257 Hyperphosphorylation of AMP-activated protein kinase Snf1 on T210 under low glucose conditions |
1 |
| Bhagwat et al. (2021) | Bhagwat, N.R., Owens, S.N., Ito, M., Boinapalli, J.V,, Poa, P., Ditzel, A., Kopparapu, S., Mahalawat, M., Davies, O.R., Collins, S.R., Johnson, J.R., Krogan, N.J., Hunter, N. (2021). SUMO is a pervasive regulator of meiosis. Elife 10:e57720. https://doi.org/10.7554/eLife.57720 SUMO-modified meiotic proteome, sites co-midified by SUMO and phosphorylatio |
555 |
| Boeckstaens et al. (2015) | Boeckstaens, M., Merhi, A., Llinares, E., Van Vooren, P., Springael, J.Y., Wintjens, R., Marini, A.M. (2015). Identification of a novel regulatory mechanism of nutrient transport controlled by TORC1-Npr1-Amu1/Par32. PLoS Genet 11: e1005382. https://doi.org/10.1371/journal.pgen.1005382 Npr1-mediated phosphorylation of Par32 induced by exposure to rapamycin |
4 |
| Bontron et al. (2013) | Bontron, S., Jaquenoud, M., Vaga, S., Talarek, N., Bodenmiller, B., Aebersold, R., De Virgilio, C. (2013). Yeast endosulfines control entry into quiescence and chronological life span by inhibiting protein phosphatase 2A. Cell Rep 3: 16-22. https://doi.org/10.1016/j.celrep.2012.11.025 Targets of protein phosphatase PP2A Cdc55 |
2 |
| Brachmann et al. (2020) | Brachmann, C., Kaduhr, L., Jüdes, A., Ravichandran, K.E., West, J.D., Glatt, S., Schaffrath, R. (2020). Redox requirements for ubiquitin-like urmylation of Ahp1, a 2-Cys peroxiredoxin from yeast. Redox Biol 30: 101438. https://doi.org/10.1016/j.redox.2020.101438 Urmylation of the peroxiredoxin Ahp1 |
1 |
| Breitkreutz et al. (2010) | Breitkreutz, A., Choi, H., Sharom, J.R., Boucher, L., Neduva, V., Larsen, B., Lin, Z.Y., Breitkreutz, B.J., Stark, C., Liu, G., Ahn, J., Dewar-Darch, D., Reguly, T., Tang, X., Almeida, R., Qin, Z.S., Pawson, T., Gingras, A.C., Nesvizhskii, A.I., Tyers, M. (2010). A global protein kinase and phosphatase interaction network in yeast. Science 328: 1043-1046. https://doi.org/10.1126/science.1176495 Proteomic analysis of complexes containing protein kinases and phosphatases |
68 |
| Brito et al. (2019) | Brito, A.S., Soto, Diaz, S., Van Vooren, P., Godard, P., Marini, A.M., Boeckstaens, M. (2019). Pib2-dependent feedback control of the TORC1 signaling network by the Npr1 kinase. iScience 20: 415-433. https://doi.org/10.1016/j.isci.2019.09.025 Pib2-dependent inhibition of TORC1 mediated by protein kinase Npr1 |
2 |
| Busso et al. (2015) | Busso, C., Ferreira-Júnior, J.R., Paulela, J.A., Bleicher, L., Demasi, M., Barros, M.H. (2015). Coq7p relevant residues for protein activity and stability. Biochimie 119: 92-102. https://doi.org/10.1016/j.biochi.2015.10.016 Identification of phosphorylated residues on the Cat5/Coq7 protein |
1 |
| Caesar et al. (2006) | Caesar, R., Warringer, J., Blomberg, A. (2006). Physiological importance and identification of novel targets for the N-terminal acetyltransferase NatB. Eukaryot Cell 5: 368-378. https://doi.org/10.1128/EC.5.2.368-378.2006 Targets of the N-terminal acetyltransferase |
1 |
| Cao et al. (2014) | Cao, L., Yu, L., Guo, Z., Shen, A., Guo, Y., Liang, X. (2014). N-Glycosylation site analysis of proteins from Saccharomyces cerevisiae by using hydrophilic interaction liquid chromatography-based enrichment, parallel deglycosylation, and mass spectrometry. J Proteome Res 13: 1485-1493. https://doi.org/10.1021/pr401049e Profiling of N-glycosylated sites on cellular proteins proteins |
22 |
| Caslavska-Zempel et al. (2016) | Caslavka Zempel, K.E., Vashisht, A.A., Barshop, W.D., Wohlschlegel, J.A., Clarke, S.G. (2016). Determining the mitochondrial methyl proteome in Saccharomyces cerevisiae using heavy methyl SILAC. Journal of Proteome Research 15(12): 4436-4451. https://doi.org/10.1021/acs.jproteome.6b00521 Methylproteome of cell grown under respiratory conditions |
17 |
| Chandel et al. (2016) | Chandel, A., Das, K.K., Bachhawat, A.K. (2016). Glutathione depletion activates the yeast vacuolar transient receptor potential channel, Yvc1p, by reversible glutathionylation of specific cysteines. Mol Biol Cell 27: 3913-3925. https://doi.org/10.1091/mbc.E16-05-0281 Glutathionylated sites on the protein Yvc1p |
3 |
| Chang and Huh (2018) | Chang, Y., Huh, W.K. (2018). Ksp1-dependent phosphorylation of eIF4G modulates post-transcriptional regulation of specific mRNAs under glucose deprivation conditions. Nucleic Acids Res 46: 3047-3060. https://doi.org/10.1093/nar/gky097 Phosprylation status of mRNA binding proteins under glucose deprivation |
33 |
| Chee and Haase (2010) | Chee, M.K., Haase, S.B. (2010). B-cyclin/CDKs regulate mitotic spindle assembly by phosphorylating kinesins-5 in budding yeast. PLoS Genet 6: e1000935. https://doi.org/10.1371/journal.pgen.1000935 Clb/Cdc28-depemdent phosphorylation of kinesin-5 motors Kip1 and Cin8 |
4 |
| Chen et al. (2010) | Chen, S.H., Albuquerque, C.P., Liang, J., Suhandynata, R.T., Zhou, H. (2010). A proteome-wide analysis of kinase-substrate network in the DNA damage response. J Biol Chem 285: 12803-12812. https://doi.org/10.1074/jbc.M110.106989 Targets of DNA damage response protein kinases Mec1/Tel1, Rad53, and Dun1 |
21 |
| Chen et al. (2018a) | Chen, Y.C., Jiang, P.H., Chen, H.M., Chen, C.H., Wang, Y.T., Chen, Y.J., Yu, C.J., Teng, S.C. (2018a). Glucose intake hampers PKA-regulated HSP90 chaperone activity. Elife 7: e39925. https://doi.org/10.7554/eLife.39925 Phosphoproteome of calorie-restricted cells (0.5% glucoce) |
239 |
| Chen et al. (2018b) | Chen, X., Yang, X., Shen, Y., Hou, J., Bao, X. (2018b). Screening phosphorylation site mutations in yeast acetyl-CoA carboxylase using malonyl-CoA sensor to improve malonyl-CoA-derived product. Front Microbiol 9: 47. https://doi.org/10.3389/fmicb.2018.00047 Phosphosites on acetyl-CoA carboxylase Acc1p |
13 |
| Chen et al. (2021) | Chen, Z., Malia, P.C., Hatakeyama, R., Nicastro, R., Hu, Z., Péli-Gulli, M.P., Gao, J., Nishimura, T., Eskes, E., Stefan, C.J., Winderickx, J., Dengjel, J., De Virgilio, C., Ungermann, C. (2021). TORC1 determines Fab1 lipid kinase function at signaling endosomes and vacuoles. Curr Biol 31: 297-309.e8 https://doi.org/10.1016/j.cub.2020.10.026 Phosphorylation of the lipid kinase Fab1 by TORC1 protein kinase |
5 |
| Chernova et al. (2020) | Chernova, T.A., Yang, Z., Karpova, T.S., Shanks, J.R., Shcherbik, N., Wilkinson, K.D., Chernoff, Y.O. (2020). Aggregation and Prion-Inducing Properties of the G-Protein Gamma Subunit Ste18 are Regulated by Membrane Association. Int J Mol Sci 21: 5038. https://doi.org/10.3390/ijms21145038 Ubiquitylation of the gamm subunit of G-protein Ste18 |
1 |
| Chun et al. (2019) | Chun, Y., Joo, Y.J., Suh, H., Batot, G., Hill, C.P., Formosa, T., Buratowski, S. (2019). Selective Kinase Inhibition Shows That Bur1 (Cdk9) Phosphorylates the Rpb1 Linker In Vivo. Mol Cell Biol 39: e00602-18. https://doi.org/10.1128/MCB.00602-18 The largets subunit of RNA polymerase II (Rpo21/Rpb1) is phosphorylated by protein kinase Sgv1/Bur1. |
2 |
| Clotet et al. (2006) | Clotet, J., Escoté, X., Adrover, M.A., Yaakov, G., Garí, E., Aldea, M., de Nadal, E., Posas, F. (2006). Phosphorylation of Hsl1 by Hog1 leads to a G2 arrest essential for cell survival at high osmolarity. EMBO J 25: 2338-2346. https://doi.org/10.1038/sj.emboj.7601095 Phosphorylation of protein kinase Hsl1 by Hog1 kinase |
1 |
| Couttas et al. (2012) | Couttas, T.A., Raftery, M.J., Padula, M.P., Herbert, B.R., Wilkins, M.R. (2012). Methylation of translation-associated proteins in Saccharomyces cerevisiae: Identification of methylated lysines and their methyltransferases. Proteomics 12: 960-972. https://doi.org/10.1002/pmic.201100570 Methylation of translation-associated proteins |
4 |
| Crutchley et al. (2009) | Crutchley, J., King, K.M., Keaton, M.A., Szkotnicki, L., Orlando, D.A., Zyla, T.R., Bardes, E.S., Lew, D.J. (2009). Molecular dissection of the checkpoint kinase Hsl1p. Mol Biol Cell 20: 1926-1936. https://doi.org/10.1091/mbc.e08-08-0848 Phosphorylation of kinase domain of protein kinase Hsl1 |
1 |
| DeMille et al. (2019) | DeMille, D., Pape, J.A., Bikman, B.T., Ghassemian, M., Grose, J.H. (2019). The regulation of Cbf1 by PAS Kinase is a pivotal control point for lipogenesis vs. respiration in Saccharomyces cerevisiae. G3 (Bethesda) 9: 33-46. https://doi.org/10.1534/g3.118.200663 Phosphorylation of centromere-binding factor 1 (Cbp1) by protein kinase Psk1 |
1 |
| Deng et al. (2009) | Deng, C., Xiong, X., Krutchinsky, A.N. (2009). Unifying fluorescence microscopy and mass spectrometry for studying protein complexes in cells. Mol Cell Proteomics 8: 1413-1423. https://doi.org/10.1074/mcp.M800397-MCP200 Phosphosites on eisosomal protein complexes purified from cells grown in a complex media and upon cell cycle release |
4 |
| Dey et al. (2019) | Dey, P., Su, W.M., Mirheydari, M., Han, G.S., Carman, G.M. (2019). Protein kinase C mediates the phosphorylation of the Nem1-Spo7 protein phosphatase complex in yeast. J Biol Chem 294: 15997-16009. https://doi.org/10.1074/jbc.RA119.010592 Protein kinase C - dependent phosphorylation of the Nem1–Spo7 complex |
1 |
| Dohlman et al. (1993) | Dohlman, H.G., Goldsmith, P., Spiegel, A.M., Thorner, J. (1993). Pheromone action regulates G-protein alpha-subunit myristoylation in the yeast Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 90: 9688-9692. https://doi.org/10.1073/pnas.90.20.9688 Myristoylated sites on the alpha subunit of G protein Gpa1 |
1 |
| Dokládal et al. (2021) | Dokládal, L., Stumpe, M., Hu, Z., Jaquenoud, M., Dengjel, J., De Virgilio, C. (2021). Phosphoproteomic responses of TORC1 target kinases reveal discrete and convergent mechanisms that orchestrate the quiescence program in yeast. Cell Rep 37: 110149. https://doi.org/10.1016/j.celrep.2021.110149 Rapamycin-sensitive phosphoproteome |
85 |
| Dubots et al. (2014) | Dubots, E., Cottier, S., Péli-Gulli, M.P., Jaquenoud, M., Bontron, S., Schneiter, R., De Virgilio, C. (2014). TORC1 regulates Pah1 phosphatidate phosphatase activity via the Nem1/Spo7 protein phosphatase complex. PLoS One 9: e104194. https://doi.org/10.1371/journal.pone.0104194 TORC1 - dependent phosphorylation of the Nem1–Spo7 complex |
2 |
| Eraso et al. (2006) | Eraso, P., Mazón, M.J., Portillo, F. (2006). Yeast protein kinase Ptk2 localizes at the plasma membrane and phosphorylates in vitro the C-terminal peptide of the H+-ATPase. Biochim Biophys Acta 1758: 164-170. https://doi.org/10.1016/j.bbamem.2006.01.010 Glucose-induced phosphorylation of plasma membrane H+-ATPase (Pma1) |
1 |
| Fang et al. (2014) | Fang, N.N., Chan, G.T., Zhu, M., Comyn, S.A., Persaud, A., Deshaies, R.J., Rotin, D., Gsponer, J., Mayor, T. (2014). Rsp5/Nedd4 is the main ubiquitin ligase that targets cytosolic misfolded proteins following heat stress. Nature Cell Biology 16(12): 1227-1237. https://doi.org/10.1038/ncb3054 Heat stress induced PTMs (ubiqitylation, carbamoylation, Met oxidation) |
106 |
| Feng et al. (2016) | Feng, Y., Backues, S.K., Baba, M., Heo, J.M., Harper, J.W., Klionsky, D.J. (2016). Phosphorylation of Atg9 regulates movement to the phagophore assembly site and the rate of autophagosome formation. Autophagy 12: 648-658. https://doi.org/10.1080/15548627.2016.1157237 Phosphorylation sites on Atg9 protein |
1 |
| Fernández-García (2012) | Fernández-García, P., Peláez, R., Herrero, P., Moreno, F. (2012). Phosphorylation of yeast hexokinase 2 regulates its nucleocytoplasmic shuttling. J Biol Chem 287: 42151-42164. https://doi.org/10.1074/jbc.M112.401679 Nucleo-cytoplasmic shuffling of hexokinase 2 (Hxk2) is regulated by phosphorylation |
1 |
| Ficcaro et al. (2002) | Ficarro, S.B., McCleland, M.L., Stukenberg, P.T., Burke, D.J., Ross, M.M., Shabanowitz, J., Hunt, D.F., White, F.M. (2002). Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae. Nat Biotechnol 20: 301-305. https://doi.org/10.1038/nbt0302-301 Phosphoproteome of cells grown in a complex (YPD) medium |
111 |
| Folz et al. (2019) | Folz, H., Niño, C.A., Taranum, S., Caesar, S., Latta, L., Waharte, F., Salamero, J., Schlenstedt, G., Dargemont, C. (2019). SUMOylation of the nuclear pore complex basket is involved in sensing cellular stresses. J Cell Sci 132: jcs224279. https://doi.org/10.1242/jcs.224279 SUMO-modified sites on the nucleoporin component Nup2 |
2 |
| Foyn et al. (2013) | Foyn, H., van Damme, P., Støve, S.I., Glomnes, N., Evjenth, N., Gevaert, K., Arnesen, T. (2013). Protein N-terminal acetyltransferases act as N-terminal propionyltransferases in vitro and in vivo. Mol Cell Proteomics 12: 42-54. https://doi.org/10.1074/mcp.M112.019299 Propionylation catalyzed by N-terminal acetyltransferases |
4 |
| Frankovsky et al. (2021a) | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. https://doi.org/10.1016/j.mito.2020.12.016 Metaanalysis of the yeast phosphoproteome as of January 2021 |
9174 |
| Frankovsky et al. (2021b) | Frankovsky, J., Keresztesová, B., Bellová, J., et al. (2021). The yeast mitochondrial succinylome: Implications for regulation of mitochondrial nucleoids. Journal of Biological Chemistry, 297(4): 101155. https://doi.org/10.1016/j.jbc.2021.101155 Mitochondrial succinylome in cells grown on nonfermentable carbon source |
1904 |
| Gao et al. (2020) | Gao, J., Kurre, R., Rose, J., Walter, S., Fröhlich, F., Piehler, J., Reggiori, F., Ungermann, C. (2020). Function of the SNARE Ykt6 on autophagosomes requires the Dsl1 complex and the Atg1 kinase complex. EMBO Rep 21: e50733. https://doi.org/10.15252/embr.202050733 Regulation of Ykt6 activity on autophagosomes via phosphorylation by the Atg1 kinase |
3 |
| Gartner et al. (1992) | Gartner, A., Nasmyth, K., Ammerer, G. (1992). Signal transduction in Saccharomyces cerevisiae requires tyrosine and threonine phosphorylation of FUS3 and KSS1. Genes Dev 6: 1280-1292. https://doi.org/10.1101/gad.6.7.1280 Pheromone-induced phoisphorylation of protein kinases Fus2 and Kss1 |
2 |
| Gey et al. (2014) | Gey, U., Czupalla, C., Hoflack, B., Krause, U., Rödel, G. (2014). Proteomic analysis reveals a novel function of the kinase Sat4p in Saccharomyces cerevisiae mitochondria. PLoS One 9: e103956. https://doi.org/10.1371/journal.pone.0103956 The lipoylation status on Lat1p, Kgd2p and Gcv3p is affected by the protein kinase Sat4 |
3 |
| Ghosh et al. (2021) | Ghosh, C., Uppala, J.K., Sathe, L., Hammond, C.I., Anshu, A., Pokkuluri, P.R., Turk, B.E., Dey, M. (2021). Phosphorylation of Pal2 by the protein kinases Kin1 and Kin2 modulates HAC1 mRNA splicing in the unfolded protein response in yeast. Sci Signal 14: eaaz4401. https://doi.org/10.1126/scisignal.aaz4401 Phosphorylation of endocytic adaptor protein Pal1 by protein kinases Kin1 and Kin2 |
1 |
| Goldstein et al. (2017) | Goldstein, A., Siegler, N., Goldman, D., Judah, H., Valk, E., Kõivomägi, M., Loog, M., Gheber, L. (2017). Three Cdk1 sites in the kinesin-5 Cin8 catalytic domain coordinate motor localization and activity during anaphase. Cell. Mol. Life Sci. 74: 3395-3412. https://doi.org/10.1007/s00018-017-2523-z Cdk1-dependent phosphorylation of kinesin-5 Cin8 |
3 |
| Gonzáles-Rubio et al. (2021) | González-Rubio, G., Sellers-Moya, Á., Martín, H., Molina, M. (2021). Differential Role of Threonine and Tyrosine Phosphorylation in the Activation and Activity of the Yeast MAPK Slt2. Int J Mol Sci 22: 1110. https://doi.org/10.3390/ijms22031110 Dynamics of phosphorylation of the MAP kinase Slt2 |
2 |
| Griffiths et al. (2009) | Griffiths, L.M., Swartzlander, D., Meadows, K.L,, Wilkinson, K.D., Corbett, A.H., Doetsch, P.W. (2009). Dynamic compartmentalization of base excision repair proteins in response to nuclear and mitochondrial oxidative stress. Mol Cell Biol 29(3):794-807 https://doi.org/10.1128/MCB.01357-08 SUMO-modified sites on the DNA N-glycosylase Ntg1 |
1 |
| Grosshans et al. (2006) | Grosshans, B.L., Grötsch, H., Mukhopadhyay, D., Fernández, I.M., Pfannstiel, J., Idrissi, F.Z., Lechner, J., Riezman, H., Geli, M.I. (2006). TEDS site phosphorylation of the yeast myosins I is required for ligand-induced but not for constitutive endocytosis of the G protein-coupled receptor Ste2p. J Biol Chem 281: 11104-11114. https://doi.org/10.1074/jbc.M508933200 Phosphorylation of the myosins Myo3p and Myo5p and its role in endocytosis |
1 |
| Gruhler et al. (2005) | Gruhler, A., Olsen, J.V., Mohammed, S., Mortensen, P., Faergeman, N.J., Mann, M., Jensen, O.N. (2005). Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway. Mol Cell Proteomics 4: 310-327. https://doi.org/10.1074/mcp.M400219-MCP200 Pheromone-induced changes in phosphoproteome |
26 |
| Guo et al. (2017a) | Guo X, Niemi NM, Coon JJ, Pagliarini DJ (2017a) Integrative proteomics and biochemical analyses define Ptc6p as the Saccharomyces cerevisiae pyruvate dehydrogenase phosphatase. J Biol Chem 292:11751–11759. https://doi.org/10.1074/jbc.M117.787341 Phosphoproteome in wild-type cells compared to mutants lacking PTC5, PTC6 and PTC7 encoding mitochondrial protein phosphatases |
742 |
| Guo et al. (2017b) | Guo X, Niemi NM, Hutchins PD, et al (2017b) Ptc7p dephosphorylates select mitochondrial proteins to enhance metabolic function. Cell Reports 18:307–313. https://doi.org/10.1016/j.celrep.2016.12.049 Phosphoproteome in wild-type cells compared to mutants lacking PTC7 encoding mitochondrial protein phosphatase Ptc7 |
178 |
| Hamey et al. (2021) | Hamey, J.J., Nguyen, A., Wilkins, M.R. (2021). Discovery of arginine methylation, phosphorylation, and their co-occurrence in condensate-associated proteins in Saccharomyces cerevisiae. J Proteome Res 20: 2420-2434. https://doi.org/10.1021/acs.jproteome.0c00927 Arginine methylation, phosphorylation, and their co-occurrence in condensate-associated proteins |
6 |
| Heidinger-Pauli et al. (2008) | Heidinger-Pauli, J.M., Unal, E., Guacci, V., Koshland, D. (2008). The kleisin subunit of cohesin dictates damage-induced cohesion. Mol Cell 31: 47-56. https://doi.org/10.1016/j.molcel.2008.06.005 Regulation of alpha-kleisin subunit of the cohesin complex Mcd1/Scc1 by phosphorylation and acetylation |
3 |
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