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dbPPT: Database of Phospho-sites in Plants

Last update: July 2th, 2014. As one of the most important and ubiquitous post-translational modifications (PTMs) in plants, the reversible phosphorylation catalyzed by protein kinases is involved in regulating a wide range of biological processes such as cellular metabolism, signal transduction and environmental response ( Ranjeva. S), which contains large-scale phosphorylation sites (p-sites) based on mass spectrometry across 20. Currently, dbPPT contains 82,175. P-sites in 31,012. 2014, 2014: bau121.

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dbPPT: Database of Phospho-sites in Plants | dbppt.biocuckoo.org Reviews

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Last update: July 2th, 2014. As one of the most important and ubiquitous post-translational modifications (PTMs) in plants, the reversible phosphorylation catalyzed by protein kinases is involved in regulating a wide range of biological processes such as cellular metabolism, signal transduction and environmental response ( Ranjeva. S), which contains large-scale phosphorylation sites (p-sites) based on mass spectrometry across 20. Currently, dbPPT contains 82,175. P-sites in 31,012. 2014, 2014: bau121.

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dbPPT: Database of Phospho-sites in Plants | dbppt.biocuckoo.org Reviews

https://dbppt.biocuckoo.org

Last update: July 2th, 2014. As one of the most important and ubiquitous post-translational modifications (PTMs) in plants, the reversible phosphorylation catalyzed by protein kinases is involved in regulating a wide range of biological processes such as cellular metabolism, signal transduction and environmental response ( Ranjeva. S), which contains large-scale phosphorylation sites (p-sites) based on mass spectrometry across 20. Currently, dbPPT contains 82,175. P-sites in 31,012. 2014, 2014: bau121.

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dbPPT: Database of Phospho-sites in Plants

http://www.dbppt.biocuckoo.org/faq.php

Last update: July 2th, 2014. 8251; Data Summary. 20,545 (70.70%). 6,517 (22.43%). 1,996 (6.87%). 2,861 (88.33%). 2,181 (80.24%). 2,491 (89.32%). 12,211 (82.31%). 2,283 (15.39%). Oryza sativa subsp. japonica. 7,048 (81.92%). 1,243 (14.45%). Physcomitrella patens subsp. patens. 1,363 (90.93%). 10,940 (80.56%). 2,327 (17.14%). 64,089 (77.99%). 14,632 (17.81%). 3,454 (4.20%). You can select one of these twenty species listed below to browse all known proteins with p-sites of corresponding species. The term f...

2

dbPPT: Database of Phospho-sites in Plants

http://www.dbppt.biocuckoo.org/browse.php

Last update: July 2th, 2014. DbPPT 1.0 ( d. Lants) is a comprehensive database which includes 71,397. P-sites in 27,807. Plant organisms. In this database, we not only manually collected experimental verified phosphorylation substrates and sites on plants, but also integrated the other two important phosphorylation databases of plants including PhosPhAt ( Durek. In total, the database of dbPPT 1.0 consists of 56,078. PS (phosphorylation serine), 12,495. PT (phosphorylation threonine), and 2,824.

3

dbPPT: Database of Phospho-sites in Plants

http://www.dbppt.biocuckoo.org/download.php

Last update: July 2th, 2014. Please submit the form to get the download link of the dataset, many thanks. Note: all the field are requied. dbPPT is ONLY freely available for academic research. For commercial usage, please contact us. British Indian Ocean Territory. Congo, the Democratic Republic of the. Heard and Mc Donald Islands. Hong Kong, China. Korea, Republic of. Lao People's Democratic Republic. Micronesia, Federated States of. Moldova, Republic of. Saint Kitts and Nevis. Sao Tome and Principe.

4

dbPPT: Database of Phospho-sites in Plants

http://www.dbppt.biocuckoo.org/advance.php

Last update: July 2th, 2014. 8251; dbPPT 1.0 database Online Service Options. Please input multiple keywords to find the related information (One keyword one line). Please input a PROTEIN. Only one sequence is permitted. Tr C8CBK4 C8CBK4 WHEAT SNF1-type serine-threonine protein kinase OS=Triticum aestivum GN=SnRK2.4 PE=2 SV=1 nMEKYEAVRDIGSGNFGVARLMRNRETRELVAVKCIERGHRIDENVYREIINHRSLRHPNIIRFKEVVLTPTNLMIVMEFAAGGELFERICDRGRFSEDEARYFFQQLICGVSYCHHMQICHRDLKLENVLLDGSAAPRLKICDFGYSKSSVLHSRPKSAVGTPAYIAPEVLSRREY...

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dbPPT: Database of Phospho-sites in Plants

http://www.dbppt.biocuckoo.org/index.php

Last update: July 2th, 2014. As one of the most important and ubiquitous post-translational modifications (PTMs) in plants, the reversible phosphorylation catalyzed by protein kinases is involved in regulating a wide range of biological processes such as cellular metabolism, signal transduction and environmental response ( Ranjeva. S), which contains large-scale phosphorylation sites (p-sites) based on mass spectrometry across 20. Currently, dbPPT contains 82,175. P-sites in 31,012. 2014, 2014: bau121.

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DbPTM 10th Year Anniversary. An Integrated Resource for Protein Post-Translational Modifications. Drug binding-associated PTM sites. The Statistics of PTMs. Move to the Statistics Page. Modified residue Glycosylation Lipidation Crosslink. Structural characterization of PTM substrate sites. The Benchmark dataset of PTMs. ex: O-Glycosylation. Reconstruct the PTM Regulatory Network. ex: O-Glycosylation. Welcome to dbPTM 10th Year Anniversary. Integrative Platform for PTM Analysis. Large-scale identification...

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dbPPT: Database of Phospho-sites in Plants

Last update: July 2th, 2014. As one of the most important and ubiquitous post-translational modifications (PTMs) in plants, the reversible phosphorylation catalyzed by protein kinases is involved in regulating a wide range of biological processes such as cellular metabolism, signal transduction and environmental response ( Ranjeva. S), which contains large-scale phosphorylation sites (p-sites) based on mass spectrometry across 20. Currently, dbPPT contains 82,175. P-sites in 31,012. 2014, 2014: bau121.

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