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External resources - (No support from the ExPASy Team)SulfoSite is to computationally predict sulfation sites within given protein sequences. A representative set of 162 protein tyrosine sulfation sites from the Swiss-Port were used to analyze characteristics and to train and test in SulfoSite. Support Vector Machine (SVM) is applied for learning to each group of sequences and accessible surface area (ASA) value surrounding to the sulfation residues.
keywords: post-translational modification (PTM)
The SUMOplot??? Analysis Program predicts and scores sumoylation sites in your protein. The presence of this post-translational modification may help explain larger MWs than expected on SDS gels due to attachment of SUMO protein (11kDa) at multiple positions in your protein.
keywords: post-translational modification (PTM)
Protein sumoylation plays important roles in a variety of biological processes, such as transcriptional regulation, signaling transduction, cell cycle progression and differentiation. SUMOsp predicts sumoylation sites in proteins.
keywords: post-translational modification (PTM)
The SWISS-2DPAGE database assembles data on proteins identified on various 2-D PAGE and SDS-PAGE maps. Each SWISS-2DPAGE entry contains textual data on one protein, including mapping procedures, physiological and pathological information, experimental data and bibliographical references. In addition several 2-D PAGE and SDS-PAGE images are provided, showing the experimentally determined location of the protein, as well as a theoretical region where the protein might be found in the gel.
TermiNator predicts N-terminal methionine excision, N-terminal acetylation, N-terminal myristoylation and S-palmitoylation of either prokaryotic or eukaryotic proteins originating from organellar or nuclear genomes. It also relates the predicted N-terminus to protein half-life (5-220 hours) and relative translation efficiency (relative value 1-5) of eukaryotic proteins.
keywords: post-translational modification (PTM)
The UniProt Knowledgebase (UniProtKB) is the central hub for the collection of functional information on proteins with accurate, consistent and rich annotation. It consists of: UniProtKB/Swiss-Prot (manually-annotated records and curator-evaluated computational analysis) and UniProtKB/TrEMBL (computationally analyzed records awaiting manual annotation).
keywords: disease mutation, enzyme (catalytic activity), functional annotation, gene nomenclature, glycosylation, oligosaccharide (glycan, sugar), pathway, physico-chemical property, post-translational modification (PTM), protein data bank (PDB), protein domain, protein family, protein function, protein nomenclature, protein sequence analysis (primary structure), protein variation (variant), proteome database, quaternary structure, sequence alignment, sequence analysis, tertiary structure, transmembrane (trans-membrane)
UniProtKB/Swiss-Prot is the manually annotated component of UniProtKB. It contains manually-annotated (reviewed) records with information extracted from the literature and curator-evaluated computational analysis.
keywords: disease mutation, enzyme (catalytic activity), family database, functional annotation, gene nomenclature, glycosylation, influenza, pathway, physico-chemical property, post-translational modification (PTM), protein data bank (PDB), protein domain, protein family, protein function, protein nomenclature, protein sequence analysis (primary structure), protein variation (variant), quaternary structure, secondary structure, sequence alignment, sequence analysis, tertiary structure, topology prediction, transmembrane (trans-membrane)
The YinOYang WWW server produces neural network predictions for O-beta-GlcNAc attachment sites in eukaryotic protein sequences. This server can also use NetPhos, to mark possible phosphorylated sites and hence identify "Yin-Yang" sites.