Basic Information
Name | Autophagy-related protein 9 (Cytoplasm to vacuole targeting protein 7) |
Uniprot ID | Q12142 |
Systematic gene name | YDL149W |
Standard gene name | ATG9 |
Gene names | ATG9 APG9 AUT9 CVT7 YDL149W D1560 |
Description from SGD | YDL149W ATG9 SGDID:S000002308, Chr IV from 184925-187918, Genome Release 64-3-1, Verified ORF, "Transmembrane protein involved in forming Cvt and autophagic vesicles; cycles between the phagophore assembly site (PAS) and other cytosolic punctate structures, not found in autophagosomes; may be involved in membrane delivery to the PAS" |
Protein length | 997 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MERDEYQLPN SHGKNTFLSR IFGLQSDEVN PSLNSQEMSN FPLPDIERGS
SLLHSTNDSR EDVDENDLRV PESDQGTSTE EEDEVDEEQV QAYAPQISDG
LDGDHQLNSV TSKENVLETE KSNLERLVEG STDDSVPKVG QLSSEEEEDN
EFINNDGFDD DTPLFQKSKI HEFSSKKSNT IEDGKRPLFF RHILQNNRPQ
RDTQKLFTSS NAIHHDKDKS ANNGPRNING NQKHGTKYFG SATQPRFTGS
PLNNTNRFTK LFPLRKPNLL SNISVLNNTP EDRINTLSVK ERALWKWANV
ENLDIFLQDV YNYYLGNGFY CIILEKILNI CTLLFVVFVS TYMGHCVDYS
KLPTSHRVSD IIIDKCYSNS ITGFTKFFLW MFYFFVILKI VQLYFDVQKL
SELQNFYKYL LNISDDELQT LPWQNVIQQL MYLKDQNAMT ANVVEVKAKN
RIDAHDVANR IMRRENYLIA LYNSDILNLS LPIPLFRTNV LTKTLEWNIN
LCVMGFVFNE SGFIKQSILK PSQREFTREE LQKRFMLAGF LNIILAPFLV
TYFVLLYFFR YFNEYKTSPG SIGARQYTPI AEWKFREYNE LYHIFKKRIS
LSTTLANKYV DQFPKEKTNL FLKFVSFICG SFVAILAFLT VFDPENFLNF
EITSDRSVIF YITILGAIWS VSRNTITQEY HVFDPEETLK ELYEYTHYLP
KEWEGRYHKE EIKLEFCKLY NLRIVILLRE LTSLMITPFV LWFSLPSSAG
RIVDFFRENS EYVDGLGYVC KYAMFNMKNI DGEDTHSMDE DSLTKKIAVN
GSHTLNSKRR SKFTAEDHSD KDLANNKMLQ SYVYFMDDYS NSENLTGKYQ
LPAKKGYPNN EGDSFLNNKY SWRKQFQPGQ KPELFRIGKH ALGPGHNISP
AIYSTRNPGK NWDNNNNGDD IKNGTNNATA KNDDNNGNND HEYVLTESFL
DSGAFPNHDV IDHNKMLNSN YNGNGILNKG GVLGLVKEYY KKSDVGR
SLLHSTNDSR EDVDENDLRV PESDQGTSTE EEDEVDEEQV QAYAPQISDG
LDGDHQLNSV TSKENVLETE KSNLERLVEG STDDSVPKVG QLSSEEEEDN
EFINNDGFDD DTPLFQKSKI HEFSSKKSNT IEDGKRPLFF RHILQNNRPQ
RDTQKLFTSS NAIHHDKDKS ANNGPRNING NQKHGTKYFG SATQPRFTGS
PLNNTNRFTK LFPLRKPNLL SNISVLNNTP EDRINTLSVK ERALWKWANV
ENLDIFLQDV YNYYLGNGFY CIILEKILNI CTLLFVVFVS TYMGHCVDYS
KLPTSHRVSD IIIDKCYSNS ITGFTKFFLW MFYFFVILKI VQLYFDVQKL
SELQNFYKYL LNISDDELQT LPWQNVIQQL MYLKDQNAMT ANVVEVKAKN
RIDAHDVANR IMRRENYLIA LYNSDILNLS LPIPLFRTNV LTKTLEWNIN
LCVMGFVFNE SGFIKQSILK PSQREFTREE LQKRFMLAGF LNIILAPFLV
TYFVLLYFFR YFNEYKTSPG SIGARQYTPI AEWKFREYNE LYHIFKKRIS
LSTTLANKYV DQFPKEKTNL FLKFVSFICG SFVAILAFLT VFDPENFLNF
EITSDRSVIF YITILGAIWS VSRNTITQEY HVFDPEETLK ELYEYTHYLP
KEWEGRYHKE EIKLEFCKLY NLRIVILLRE LTSLMITPFV LWFSLPSSAG
RIVDFFRENS EYVDGLGYVC KYAMFNMKNI DGEDTHSMDE DSLTKKIAVN
GSHTLNSKRR SKFTAEDHSD KDLANNKMLQ SYVYFMDDYS NSENLTGKYQ
LPAKKGYPNN EGDSFLNNKY SWRKQFQPGQ KPELFRIGKH ALGPGHNISP
AIYSTRNPGK NWDNNNNGDD IKNGTNNATA KNDDNNGNND HEYVLTESFL
DSGAFPNHDV IDHNKMLNSN YNGNGILNKG GVLGLVKEYY KKSDVGR
Legend
- X Phoshorylation
- X Ubiquitination
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[11, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[11, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[11, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[19, Phos] | Papinski, D., Schuschnig, M., Reiter, W., Wilhelm, L., Barnes, C.A., Maiolica, A., Hansmann, I., Pfaffenwimmer, T., Kijanska, M., Stoffel, I., Lee, S.S., Brezovich, A., Lou, J.H., Turk, B.E., Aebersold, R., Ammerer, G., Peter, M., Kraft, C. (2014). Early steps in autophagy depend on direct phosphorylation of Atg9 by the Atg1 kinase. Mol Cell 53: 471-483. (Publication) (All modifications) |
[26, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[59, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[59, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[59, Phos] | Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications) |
[59, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[111, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[111, Phos] | 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. (Publication) (All modifications) |
[111, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[112, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[112, Phos] | 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. (Publication) (All modifications) |
[112, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[119, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[119, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[121, Ubi] | 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. (Publication) (All modifications) |
[122, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[122, Phos] | 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. (Publication) (All modifications) |
[122, Phos] | 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. (Publication) (All modifications) |
[131, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[131, Phos] | Vlastaridis P, Kyriakidou P, Chaliotis A, et al (2017) Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes. GigaScience 6:1–11. (Publication) (All modifications) |
[131, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[131, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[132, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[132, Phos] | Vlastaridis P, Kyriakidou P, Chaliotis A, et al (2017) Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes. GigaScience 6:1–11. (Publication) (All modifications) |
[132, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[132, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[135, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[135, Phos] | Vlastaridis P, Kyriakidou P, Chaliotis A, et al (2017) Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes. GigaScience 6:1–11. (Publication) (All modifications) |
[135, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[135, Phos] | Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications) |
[135, Phos] | 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. (Publication) (All modifications) |
[135, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[143, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[143, Phos] | Vlastaridis P, Kyriakidou P, Chaliotis A, et al (2017) Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes. GigaScience 6:1–11. (Publication) (All modifications) |
[143, Phos] | Studer RA, Rodriguez-Mias RA, Haas KM, et al (2016) Evolution of protein phosphorylation across 18 fungal species. Science 354:229–232. (Publication) (All modifications) |
[143, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[143, Phos] | Holt, L.J., Tuch, B.B., Villén, J., Johnson, A.D., Gygi, S.P., Morgan, D.O. (2009). Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution. Science 325(5948): 1682-1686. (Publication) (All modifications) |
[143, Phos] | Swaney, D.L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N.J., Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications) |
[143, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[144, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[144, Phos] | Vlastaridis P, Kyriakidou P, Chaliotis A, et al (2017) Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes. GigaScience 6:1–11. (Publication) (All modifications) |
[144, Phos] | Studer RA, Rodriguez-Mias RA, Haas KM, et al (2016) Evolution of protein phosphorylation across 18 fungal species. Science 354:229–232. (Publication) (All modifications) |
[144, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[144, Phos] | Holt, L.J., Tuch, B.B., Villén, J., Johnson, A.D., Gygi, S.P., Morgan, D.O. (2009). Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution. Science 325(5948): 1682-1686. (Publication) (All modifications) |
[144, Phos] | Swaney, D.L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N.J., Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications) |
[144, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[236, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[236, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[250, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[250, Phos] | Vlastaridis P, Kyriakidou P, Chaliotis A, et al (2017) Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes. GigaScience 6:1–11. (Publication) (All modifications) |
[250, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[250, Phos] | Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications) |
[250, Phos] | MacGilvray, M.E., Shishkova, E., Place, M., Wagner, E.R., Coon, J.J., Gasch, A.P. (2020). Phosphoproteome response to dithiothreitol reveals unique versus shared features of Saccharomyces cerevisiae stress responses. Journal of Proteome Research 19(8): 3405-3417. (Publication) (All modifications) |
[250, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[274, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[279, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[657, Phos] | Papinski, D., Schuschnig, M., Reiter, W., Wilhelm, L., Barnes, C.A., Maiolica, A., Hansmann, I., Pfaffenwimmer, T., Kijanska, M., Stoffel, I., Lee, S.S., Brezovich, A., Lou, J.H., Turk, B.E., Aebersold, R., Ammerer, G., Peter, M., Kraft, C. (2014). Early steps in autophagy depend on direct phosphorylation of Atg9 by the Atg1 kinase. Mol Cell 53: 471-483. (Publication) (All modifications) |
[785, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[785, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[787, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[787, Phos] | Vlastaridis P, Kyriakidou P, Chaliotis A, et al (2017) Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes. GigaScience 6:1–11. (Publication) (All modifications) |
[787, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[787, Phos] | MacGilvray, M.E., Shishkova, E., Place, M., Wagner, E.R., Coon, J.J., Gasch, A.P. (2020). Phosphoproteome response to dithiothreitol reveals unique versus shared features of Saccharomyces cerevisiae stress responses. Journal of Proteome Research 19(8): 3405-3417. (Publication) (All modifications) |
[787, Phos] | Holt, L.J., Tuch, B.B., Villén, J., Johnson, A.D., Gygi, S.P., Morgan, D.O. (2009). Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution. Science 325(5948): 1682-1686. (Publication) (All modifications) |
[787, Phos] | 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. (Publication) (All modifications) |
[787, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[802, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[802, Phos] | Swaney, D.L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N.J., Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications) |
[802, Phos] | 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. (Publication) (All modifications) |
[802, Phos] | Papinski, D., Schuschnig, M., Reiter, W., Wilhelm, L., Barnes, C.A., Maiolica, A., Hansmann, I., Pfaffenwimmer, T., Kijanska, M., Stoffel, I., Lee, S.S., Brezovich, A., Lou, J.H., Turk, B.E., Aebersold, R., Ammerer, G., Peter, M., Kraft, C. (2014). Early steps in autophagy depend on direct phosphorylation of Atg9 by the Atg1 kinase. Mol Cell 53: 471-483. (Publication) (All modifications) |
[802, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[804, Phos] | Papinski, D., Schuschnig, M., Reiter, W., Wilhelm, L., Barnes, C.A., Maiolica, A., Hansmann, I., Pfaffenwimmer, T., Kijanska, M., Stoffel, I., Lee, S.S., Brezovich, A., Lou, J.H., Turk, B.E., Aebersold, R., Ammerer, G., Peter, M., Kraft, C. (2014). Early steps in autophagy depend on direct phosphorylation of Atg9 by the Atg1 kinase. Mol Cell 53: 471-483. (Publication) (All modifications) |
[819, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[831, Phos] | Papinski, D., Schuschnig, M., Reiter, W., Wilhelm, L., Barnes, C.A., Maiolica, A., Hansmann, I., Pfaffenwimmer, T., Kijanska, M., Stoffel, I., Lee, S.S., Brezovich, A., Lou, J.H., Turk, B.E., Aebersold, R., Ammerer, G., Peter, M., Kraft, C. (2014). Early steps in autophagy depend on direct phosphorylation of Atg9 by the Atg1 kinase. Mol Cell 53: 471-483. (Publication) (All modifications) |
[842, Phos] | Papinski, D., Schuschnig, M., Reiter, W., Wilhelm, L., Barnes, C.A., Maiolica, A., Hansmann, I., Pfaffenwimmer, T., Kijanska, M., Stoffel, I., Lee, S.S., Brezovich, A., Lou, J.H., Turk, B.E., Aebersold, R., Ammerer, G., Peter, M., Kraft, C. (2014). Early steps in autophagy depend on direct phosphorylation of Atg9 by the Atg1 kinase. Mol Cell 53: 471-483. (Publication) (All modifications) |
[864, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[864, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[948, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[948, Phos] | Papinski, D., Schuschnig, M., Reiter, W., Wilhelm, L., Barnes, C.A., Maiolica, A., Hansmann, I., Pfaffenwimmer, T., Kijanska, M., Stoffel, I., Lee, S.S., Brezovich, A., Lou, J.H., Turk, B.E., Aebersold, R., Ammerer, G., Peter, M., Kraft, C. (2014). Early steps in autophagy depend on direct phosphorylation of Atg9 by the Atg1 kinase. Mol Cell 53: 471-483. (Publication) (All modifications) |
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[971, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |