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This database contains nearly 300 sequences known to bind calmodulin, published as of March 2003.  Homologous sequence searches were performed using WU-BLAST2 on the SWALL database (Non-Redundant Protein Sequence Database incorporating SWISSPROT, TREMBL, TREMBLNEW) with default search options.

View numerical averages of the sequences in the database

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Browse the Database by motif class:

Browse list of unclassified (undetermined/disputed) and putative (unproven) calmodulin binding domains (not included in the Database)

The sequences are divided into motifs based on the distance between key hydrophobic residues (e.g. Rhoads and Friedberg, 1997). Numerous structural analyses show that the key interaction occurs through bulky hydrophobic residues such as Phe, Trp, Ile, Leu, or Val.

The 1-14 motif refers to a group of sequences whose key bulky residues are spaced 12 residues apart. These sequences should be similar to the characterized binding motifs of smooth muscle and skeletal muscle myosin light chain kinase (smMLCK, skMLCK) in binding properties.

The 1-10 motif refers to a group of sequences whose key bulky residues are spaced 8 residues apart. They should theoretically be similar to Ca2+/calmodulin dependent kinase II (CaMKII) in binding properties.

The 1-16 motif refers to a group of sequences whose key bulky residues are spaced 14 residues apart. Currently, this motif is believed to be unique to Ca2+/calmodulin dependent protein kinase kinase (CaMKK).

The IQ motif refers to a group of sequences that share the IQ motif found in a number of mostly Ca2+-independent CaM binding proteins. IQ motifs have been characterized in several myosins and calcium channels, such as the L-type calcium channel (Zuhlke et al., 1999).

The others class contains sequences that do not conform to any of the above groups. This may be due to lack of detailed information describing the molecular interaction between calmodulin and target.

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