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Phospho3D 2.0: a database of 3D protein phosphorylation sites

Is a database of three-dimensional structures of phosphorylation sites which stores information retrieved from the Phospho.ELM. Database and which is enriched with structural information and annotations at the residue level. The database also collects the results of a large-scale structural comparison procedure providing clues for the identification of new putative phosphorylation sites. The complete dataset of 3D phosphorylation sites, as well as non-redundant subsets, are available on request.

http://www.phospho3d.org/

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Phospho3D 2.0: a database of 3D protein phosphorylation sites | phospho3d.org Reviews
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Is a database of three-dimensional structures of phosphorylation sites which stores information retrieved from the Phospho.ELM. Database and which is enriched with structural information and annotations at the residue level. The database also collects the results of a large-scale structural comparison procedure providing clues for the identification of new putative phosphorylation sites. The complete dataset of 3D phosphorylation sites, as well as non-redundant subsets, are available on request.
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2 documentation
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Phospho3D 2.0: a database of 3D protein phosphorylation sites | phospho3d.org Reviews

https://phospho3d.org

Is a database of three-dimensional structures of phosphorylation sites which stores information retrieved from the Phospho.ELM. Database and which is enriched with structural information and annotations at the residue level. The database also collects the results of a large-scale structural comparison procedure providing clues for the identification of new putative phosphorylation sites. The complete dataset of 3D phosphorylation sites, as well as non-redundant subsets, are available on request.

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phospho3d.org phospho3d.org
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Phospho3D

http://www.phospho3d.org/documentation.py

How to query phospho3D. Notice on MS data. Data and annotation sources. The phosphorylation of specific protein residues is a crucial event in the regulation of several cellular processes, acting on activation, deactivation or recognition of the target protein. A great deal of eukaryotic cell proteins (30 up to 50% of the total) undergo this post-translational modification. The structural basis and the determinants of phosphorylation specificity are often unclear. And that might be independent of the res...

2

Phospho3D

http://www.phospho3d.org/stats.py

Statistics on instances associated to kinase families. Mapped Phospho.ELM instances. Total number of instances on structure. Total number of instances on structure per residue type. 2240 S, 987 T, 2160 Y. Number of instances for which the kinase (or kinase family) responsible for the phosphorylation is known.

3

Phospho3D

http://www.phospho3d.org/links.py

Links Contacts and Download. Links to related resources. RCSB PDB - Protein Data Bank. Phosphorylation sites prediction tools.

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gps.biocuckoo.org gps.biocuckoo.org

GPS 3.0 - Kinase-specific Phosphorylation Site Prediction

http://gps.biocuckoo.org/links.php

Last update: Sep. 10th, 2014. Computational resources of protein phosphorylation :. Last updated: Dec 17, 2014. We apologized that the computational studies without any web links of databases or tools will not be included in this compendium, since it's not easy for experimentalists to use studies directly. We are grateful for users feedback. Please inform Dr. Yu Xue. To add, remove or update one or multiple web links below. 2 Prediction of non-specific or organism-specific phosphorylation sites. PhosphoN...

biocuckoo.org biocuckoo.org

The CUCKOO Workgroup

http://www.biocuckoo.org/link.php

Last update: Dec. 19th, 2014. The compendium of computational resources for protein PTMs. Protein post-translational modifications, also called as covalent modifications, play important role in all kinds of biological processes and pathways. To date, there were more than 350 types of PTMs discovered ( DeltaMass. Mann and Jensen, 2003. Walsh and Jefferis, 2006. We roughly classified the computational tools into two groups based on their PTMs types, including Attachment of chemical groups. C Detecting pote...

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Phospho3D 2.0: a database of 3D protein phosphorylation sites

Is a database of three-dimensional structures of phosphorylation sites which stores information retrieved from the Phospho.ELM. Database and which is enriched with structural information and annotations at the residue level. The database also collects the results of a large-scale structural comparison procedure providing clues for the identification of new putative phosphorylation sites. The complete dataset of 3D phosphorylation sites, as well as non-redundant subsets, are available on request.

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