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The UniProt database is an example of a protein sequence database. As of 2013 it contained over 40 million sequences and is growing at an exponential rate. [1] Historically, sequences were published in paper form, but as the number of sequences grew, this storage method became unsustainable.
Swiss-Prot has collected over 81 000 variants in roughly 13,000 human protein sequence records from peer-reviewed literature. It is unclear how many unique proteins types are present in the database. Signal transduction pathway databases
UniProtKB/Swiss-Prot is a manually annotated, non-redundant protein sequence database. It combines information extracted from scientific literature and biocurator-evaluated computational analysis. The aim of UniProtKB/Swiss-Prot is to provide all known relevant information about a particular protein.
Protein database maintains the text record for individual protein sequences, derived from many different resources such as NCBI Reference Sequence (RefSeq) project, GenBank, PDB, and UniProtKB/SWISS-Prot. Protein records are present in different formats including FASTA and XML and are linked to other NCBI resources. Protein provides the ...
In 2002, PIR – along with its international partners, the European Bioinformatics Institute and the Swiss Institute of Bioinformatics – were awarded a grant from NIH to create UniProt, a single worldwide database of protein sequence and function, by unifying the Protein Information Resource-Protein Sequence Database, Swiss-Prot, and TrEMBL ...
a protein databases that includes visuals of protein structure. Also, includes protein pathways and gene sequences including other tools. SCOP the Structural Classification of Proteins a detailed and comprehensive description of the structural and evolutionary relationships between all proteins whose structure is known. SWISS-MODEL Repository
The image above contains clickable links This diagram (which is interactive) of protein structure uses PCNA as an example. (Protein primary structure is the linear sequence of amino acids in a peptide or protein. [1] By convention, the primary structure of a protein is reported starting from the amino-terminal (N) end to the carboxyl-terminal ...
This approach uses protein sequence data and the chemical and physical interactions of the encoded amino acids to predict the 3-D structures of proteins with no homology to solved protein structures. One highly successful method for ab initio modeling is the Rosetta program, which divides the protein into short segments and arranges short ...