Database Commons
Database Commons

a catalog of worldwide biological databases

Database Profile

CaM

General information

URL: http://calcium.uhnres.utoronto.ca/ctdb
Full name: Calmodulin target database
Description: The intracellular calcium sensor protein calmodulin (CaM) interacts with a large number of proteins to regulate their biological functions in response to calcium stimulus. This molecular recognition process is diverse in its mechanism, but can be grouped into several classes based on structural and sequence information.
Year founded: 2000
Last update:
Version:
Accessibility:
Accessible
Country/Region: Canada

Classification & Tag

Data type:
Data object:
Database category:
Major species:
NA
Keywords:

Contact information

University/Institution: University of Toronto
Address: Division of Molecular and Structural Biology, Ontario Cancer Institute and Department of Medical Biophysics, University of Toronto, 610 University Avenue, Toronto, Ontario M5G 2M9, Canada
City:
Province/State:
Country/Region: Canada
Contact name (PI/Team): MitsuhikoIkura
Contact email (PI/Helpdesk): mikura@uhnres.utoronto.ca

Publications

12836676
Calmodulin target database. [PMID: 12836676]
Yap KL, Kim J, Truong K, Sherman M, Yuan T, Ikura M.

The intracellular calcium sensor protein calmodulin (CaM) interacts with a large number of proteins to regulate their biological functions in response to calcium stimulus. This molecular recognition process is diverse in its mechanism, but can be grouped into several classes based on structural and sequence information. We have developed a web-based database (http://calcium.uhnres.utoronto.ca/ctdb) for this family of proteins containing CaM binding sites or, as we propose to call it herein, CaM recruitment signaling (CRS) motifs. At present the CRS motif found in approximately 180 protein sequences in the databases can be divided into four subclasses, each subclass representing a distinct structural mode of molecular recognition involving CaM. The database can predict a putative CRS location within a given protein sequence, identify the subclass to which it may belong, and structural and biophysical parameters such as hydrophobicity, hydrophobic moment, and propensity for alpha-helix formation.

J Struct Funct Genomics. 2000:1(1) | 429 Citations (from Europe PMC, 2025-12-20)

Ranking

All databases:
894/6895 (87.049%)
Expression:
160/1347 (88.196%)
894
Total Rank
414
Citations
16.56
z-index

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Record metadata

Created on: 2018-02-08
Curated by:
Zhaohua Li [2018-03-04]
Zhaohua Li [2018-02-24]
Pei Wang [2018-02-08]