Primary Information | |
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BoMiProt ID | Bomi2503 |
Protein Name | Protein phosphatase 1B |
Organism | Bos taurus |
Uniprot ID | O62830 |
Milk Fraction | Exosome |
Ref Sequence ID | NP_776855.1 |
Aminoacid Length | 484 |
Molecular Weight | 53431 |
FASTA Sequence | Download |
Gene Name | PPM1B |
Gene ID | 281995 |
Protein Existence Status | Reviewed: Experimental evidence at transcript level |
Secondary Information | |
Protein Function | serine/threonine phosphatase that regulates diverse, essential cellular processes such as cell cycle progression, protein synthesis, muscle contraction, carbohydrate metabolism, transcription and neuronal signaling; |
Linking IDs | Bomi71 |
Bibliography | 1. Maynes, J. T., Bateman, K. S., Cherney, M. M., Das, A. K., Luu, H. A., Holmes, C. F., & James, M. N. (2001). Crystal structure of the tumor-promoter okadaic acid bound to protein phosphatase-1. The Journal of Biological Chemistry, 276(47), 44078–44082. https://doi.org/10.1074/jbc.M107656200. 2. Ragusa, M. J., Dancheck, B., Critton, D. A., Nairn, A. C., Page, R., & Peti, W. (2010). Spinophilin directs protein phosphatase 1 specificity by blocking substrate binding sites. Nature Structural & Molecular Biology, 17(4), 459–464. https://doi.org/10.1038/nsmb.1786. 3. Kelker, M. S., Page, R., & Peti, W. (2009). Crystal Structures of Protein Phosphatase-1 Bound to Nodularin-R and Tautomycin: A Novel Scaffold for Structure-based Drug Design of Serine/Threonine Phosphatase Inhibitors. Journal of Molecular Biology, 385(1), 11–21. https://doi.org/10.1016/j.jmb.2008.10.053. 4. Dancheck, B., Ragusa, M. J., Allaire, M., Nairn, A. C., Page, R., & Peti, W. (2011). Molecular investigations of the structure and function of the protein phosphatase 1-spinophilin-inhibitor 2 heterotrimeric complex. Biochemistry, 50(7), 1238–1246. https://doi.org/10.1021/bi101774g. 5. Hou, J., An, X., Song, Y., Cao, B., Yang, H., Zhang, Z., … Li, Y. (2017). Detection and comparison of microRNAs in the caprine mammary gland tissues of colostrum and common milk stages. BMC Genetics, 18(1), 38. https://doi.org/10.1186/s12863-017-0498-2. 6. Favre, B., Turowski, P., & Hemmings, B. A. (1997). Differential inhibition and posttranslational modification of protein phosphatase 1 and 2A in MCF7 cells treated with calyculin-A, okadaic acid, and tautomycin. The Journal of Biological Chemistry, 272(21), 13856–13863. https://doi.org/10.1074/jbc.272.21.13856. |
Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | |
Predicted Disorder Regions | 1-19,319-330,377-397,428-484 |
DisProt Annotation | |
TM Helix Prediction | No TM helices |