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KinMutBase: a registry of disease-causing mutations in protein kinase domains.

Ortutay, Csaba; Väliaho, Jouni; Stenberg, Kaj and Vihinen, Mauno LU (2005) In Human Mutation 25(5). p.435-442
Abstract
A large number of disease-causing mutations have been identified from several protein kinases. KinMutBase is a comprehensive knowledge base for human disease-related mutations in protein kinase domains (http://bioinf.uta.fi/KinMutBase/). The latest version contains 582 different mutations for 1,790 cases in 1,322 families. KinMutBase entries are described on the DNA, mRNA, and protein level. Numbers for affected patients and families are also provided. KinMutBase has extensive amount of links and cross-references to literature, other databases, and information sources. There are numerous interactive pages about sequences, structures, mutation statistics, and diseases. Detailed statistical study was done on frequencies of different types of... (More)
A large number of disease-causing mutations have been identified from several protein kinases. KinMutBase is a comprehensive knowledge base for human disease-related mutations in protein kinase domains (http://bioinf.uta.fi/KinMutBase/). The latest version contains 582 different mutations for 1,790 cases in 1,322 families. KinMutBase entries are described on the DNA, mRNA, and protein level. Numbers for affected patients and families are also provided. KinMutBase has extensive amount of links and cross-references to literature, other databases, and information sources. There are numerous interactive pages about sequences, structures, mutation statistics, and diseases. Detailed statistical study was done on frequencies of different types of mutations both on the DNA and protein level in serine/threonine kinase (PSK) and tyrosine kinase (PTK). Three-dimensional structures indicate clustering of disease-related mutations mainly to conserved subdomains, and substrate and coligand binding amino acids, although mutations appear throughout the sequences. CpG containing codons, especially for arginine, constitute the majority of mutational hotspots. There are certain clear differences in mutation patterns and types between PSKs and PTKs. (Less)
Please use this url to cite or link to this publication:
author
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Protein Kinases: chemistry, Protein Kinases: genetics
in
Human Mutation
volume
25
issue
5
pages
435 - 442
publisher
John Wiley & Sons
external identifiers
  • pmid:15832311
  • scopus:18744407884
ISSN
1059-7794
DOI
10.1002/humu.20166
language
English
LU publication?
no
id
7c36f36d-8c8a-49e9-a55a-95988af40538 (old id 3635421)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/15832311?dopt=Abstract
date added to LUP
2013-06-12 16:15:00
date last changed
2017-08-27 05:47:52
@article{7c36f36d-8c8a-49e9-a55a-95988af40538,
  abstract     = {A large number of disease-causing mutations have been identified from several protein kinases. KinMutBase is a comprehensive knowledge base for human disease-related mutations in protein kinase domains (http://bioinf.uta.fi/KinMutBase/). The latest version contains 582 different mutations for 1,790 cases in 1,322 families. KinMutBase entries are described on the DNA, mRNA, and protein level. Numbers for affected patients and families are also provided. KinMutBase has extensive amount of links and cross-references to literature, other databases, and information sources. There are numerous interactive pages about sequences, structures, mutation statistics, and diseases. Detailed statistical study was done on frequencies of different types of mutations both on the DNA and protein level in serine/threonine kinase (PSK) and tyrosine kinase (PTK). Three-dimensional structures indicate clustering of disease-related mutations mainly to conserved subdomains, and substrate and coligand binding amino acids, although mutations appear throughout the sequences. CpG containing codons, especially for arginine, constitute the majority of mutational hotspots. There are certain clear differences in mutation patterns and types between PSKs and PTKs.},
  author       = {Ortutay, Csaba and Väliaho, Jouni and Stenberg, Kaj and Vihinen, Mauno},
  issn         = {1059-7794},
  keyword      = {Protein Kinases: chemistry,Protein Kinases: genetics},
  language     = {eng},
  number       = {5},
  pages        = {435--442},
  publisher    = {John Wiley & Sons},
  series       = {Human Mutation},
  title        = {KinMutBase: a registry of disease-causing mutations in protein kinase domains.},
  url          = {http://dx.doi.org/10.1002/humu.20166},
  volume       = {25},
  year         = {2005},
}