Basic Information
Name | ATP-dependent RNA helicase DBP2 (EC 3.6.4.13) (DEAD box protein 2) (p68-like protein) |
Uniprot ID | P24783 |
Systematic gene name | YNL112W |
Standard gene name | DBP2 |
Gene names | DBP2 YNL112W N1945 |
Description from SGD | YNL112W DBP2 SGDID:S000005056, Chr XIV from 413639-414911,415914-416281, Genome Release 64-3-1, Verified ORF, "ATP-dependent RNA helicase of the DEAD-box protein family; has strong preference for dsRNA; remodels RNA-protein complex (RNP) to facilitate efficient transcription termination ; required for assembly of Yra1p, Nab2p and Mex67p onto mRNA and formation of nuclear mRNP; involved in mRNA decay and rRNA processing; may be involved in suppression of transcription from cryptic initiation sites" |
Protein length | 546 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MTYGGRDQQY NKTNYKSRGG DFRGGRNSDR NSYNDRPQGG NYRGGFGGRS
NYNQPQELIK PNWDEELPKL PTFEKNFYVE HESVRDRSDS EIAQFRKENE
MTISGHDIPK PITTFDEAGF PDYVLNEVKA EGFDKPTGIQ CQGWPMALSG
RDMVGIAATG SGKTLSYCLP GIVHINAQPL LAPGDGPIVL VLAPTRELAV
QIQTECSKFG HSSRIRNTCV YGGVPKSQQI RDLSRGSEIV IATPGRLIDM
LEIGKTNLKR VTYLVLDEAD RMLDMGFEPQ IRKIVDQIRP DRQTLMWSAT
WPKEVKQLAA DYLNDPIQVQ VGSLELSASH NITQIVEVVS DFEKRDRLNK
YLETASQDNE YKTLIFASTK RMCDDITKYL REDGWPALAI HGDKDQRERD
WVLQEFRNGR SPIMVATDVA ARGIDVKGIN YVINYDMPGN IEDYVHRIGR
TGRAGATGTA ISFFTEQNKG LGAKLISIMR EANQNIPPEL LKYDRRSYGG
GHPRYGGGRG GRGGYGRRGG YGGGRGGYGG NRQRDGGWGN RGRSNY
NYNQPQELIK PNWDEELPKL PTFEKNFYVE HESVRDRSDS EIAQFRKENE
MTISGHDIPK PITTFDEAGF PDYVLNEVKA EGFDKPTGIQ CQGWPMALSG
RDMVGIAATG SGKTLSYCLP GIVHINAQPL LAPGDGPIVL VLAPTRELAV
QIQTECSKFG HSSRIRNTCV YGGVPKSQQI RDLSRGSEIV IATPGRLIDM
LEIGKTNLKR VTYLVLDEAD RMLDMGFEPQ IRKIVDQIRP DRQTLMWSAT
WPKEVKQLAA DYLNDPIQVQ VGSLELSASH NITQIVEVVS DFEKRDRLNK
YLETASQDNE YKTLIFASTK RMCDDITKYL REDGWPALAI HGDKDQRERD
WVLQEFRNGR SPIMVATDVA ARGIDVKGIN YVINYDMPGN IEDYVHRIGR
TGRAGATGTA ISFFTEQNKG LGAKLISIMR EANQNIPPEL LKYDRRSYGG
GHPRYGGGRG GRGGYGRRGG YGGGRGGYGG NRQRDGGWGN RGRSNY
Legend
- X K-acetylation
- X Monomethylation
- X Phoshorylation
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
Use imported representation
Loading structure from server... It may take a while.
If you believe something went wrong, please make sure PDB ID is correct.
Please also make sure that WebGL is enabled in your browser.
- Internet Explorer: sorry. IE doesn't support WebGL.
- Firefox (version 4 or later): try force enable WebGL.
- Chrome: try force enable WebGL.
- Safari: enable WebGL.
References
[12, K-acetyl] | Henriksen, P., Wagner, S. A., Weinert, B. T., et al. (2012). Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Molecular & Cellular Proteomics, 11(11), 1510-1522. (Publication) (All modifications) |
[18, Mono-CH3] | 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. (Publication) (All modifications) |
[43, Mono-CH3] | 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. (Publication) (All modifications) |
[88, 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) |
[88, 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) |
[88, 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) |
[88, 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) |
[88, 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) |
[88, 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) |
[88, 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) |
[88, 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) |
[88, Phos] | Soulard, A., Cremonesi, A., Moes, S., Schütz, F., Jenö, P., Hall, M.N. (2010). The rapamycin-sensitive phosphoproteome reveals that TOR controls protein kinase A toward some but not all substrates. Molecular Biology of the Cell 21(19): 3475-3486. (Publication) (All modifications) |
[88, Phos] | Rødkær, S.V., Pultz, D., Brusch, M., Bennetzen, M.V., Falkenby, L.G., Andersen, J.S., Færgeman, N.J. (2014). Quantitative proteomics identifies unanticipated regulators of nitrogen- and glucose starvation. Mol Biosyst 10: 2176-2188. (Publication) (All modifications) |
[88, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[90, 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) |
[90, 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) |
[90, Phos] | 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. (Publication) (All modifications) |
[90, 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) |
[90, 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) |
[90, 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) |
[90, 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) |
[90, 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) |
[90, 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) |
[90, Phos] | Soulard, A., Cremonesi, A., Moes, S., Schütz, F., Jenö, P., Hall, M.N. (2010). The rapamycin-sensitive phosphoproteome reveals that TOR controls protein kinase A toward some but not all substrates. Molecular Biology of the Cell 21(19): 3475-3486. (Publication) (All modifications) |
[90, 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) |
[90, Phos] | Rødkær, S.V., Pultz, D., Brusch, M., Bennetzen, M.V., Falkenby, L.G., Andersen, J.S., Færgeman, N.J. (2014). Quantitative proteomics identifies unanticipated regulators of nitrogen- and glucose starvation. Mol Biosyst 10: 2176-2188. (Publication) (All modifications) |
[90, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[113, 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) |
[113, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[114, 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) |
[114, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[123, 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) |
[123, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[227, 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) |
[234, 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) |
[237, 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) |
[237, 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) |
[243, 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) |
[283, K-acetyl] | Henriksen, P., Wagner, S. A., Weinert, B. T., et al. (2012). Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Molecular & Cellular Proteomics, 11(11), 1510-1522. (Publication) (All modifications) |
[356, 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) |
[356, 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) |
[363, 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) |
[363, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[368, 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) |
[368, 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) |
[368, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[369, 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) |
[369, 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) |
[369, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[411, 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) |
[417, 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) |
[497, 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) |
[497, 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) |
[497, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[509, Mono-CH3] | 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. (Publication) (All modifications) |
[512, Mono-CH3] | 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. (Publication) (All modifications) |
[518, Mono-CH3] | 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. (Publication) (All modifications) |
[525, Mono-CH3] | 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. (Publication) (All modifications) |