Links tagged with 'phosphorylation'

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PhosPhAtDatabase Content

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The Arabidopsis Protein Phosphorylation Site Database (PhosPhAt 3.0) contains information on Arabidopsis phosphorylation sites which were identified by mass spectrometry in large scale experiments by different research groups. Specific information about the peptide properties, their annotated biological function as well as the experimental and analytical context is given. For a majority of peptides, the actual annotated mass spectrum is displayed in interactive manner.

This content is being maintained by Waltraud Schulze.

Phospho.ELMDatabase Content

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Database of experimentally verified phosphorylation sites in eukaryotic proteins. Annotations are done manually and database entries come from and are linked back to scientific literature. Phospho.ELM incorporates the data formerly found in PhosphoBase.

Phospho.ELMDatabase Content

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The Phospho.ELM resource is a relational database designed to store in vivo and in vitro phosphorylation data extracted from the scientific literature and phosphoproteomic analyses. The resource comprises serine, threonine and tyrosine non-redundant phosphorylation sites. New features include: structural disorder/order and accessibility information and a conservation score. Additionally, the conservation of the phosphosites can be visualized directly on the multiple sequence alignment used for the score calculation.

Phospho3D 2.0Database Content

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Phospho3D is a database of 3D structures of phosphorylation sites derived from Phospho.ELM. The database provides the results of a large-scale structural comparison of the 3D zones versus a representative dataset of structures, thus associating to each P-site a number of structurally similar sites. Phopsho3D has now many new features. Moreover, it features P3Dscan, a new functionality that allows the user to submit a protein structure and scan it against the 3D zones collected in Phospho3D.

This content is being maintained by azanzoni.

RegPhosDatabase Content

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RegPhos is a database for exploration of the phosphorylation network associated with an input of genes/proteins. Subcellular localization information is also included.

SCPSRMTool Content

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Cyclin-dependent kinase (CDK) consensus motifs are frequently clustered in CDK substrate proteins. Spatial clustering of phosphorylation site recognition motifs (SCPSRM) contains the scripts used to search for CDK clusters.

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