Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (436K) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (21)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Kawabata, T.
Right arrow Articles by Nishikawa, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kawabata, T.
Right arrow Articles by Nishikawa, K.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, Vol 27, Issue 1 355-357, Copyright © 1999 by Oxford University Press

ARTICLES

The Protein Mutant Database

T Kawabata, M Ota and K Nishikawa
Center for Information Biology, National Institute of Genetics, 1111 Yata, Mishima, Shizuoka 411-8540, Japan. takawaba@lab.nig.ac.jp

Currently the protein mutant database (PMD) contains over 81 000 mutants, including artificial as well as natural mutants of various proteins extracted from about 10 000 articles. We recently developed a powerful viewing and retrieving system (http://pmd.ddbj.nig.ac.jp), which is integrated with the sequence and tertiary structure databases. The system has the following features: (i) mutated sequences are displayed after being automatically generated from the information described in the entry together with the sequence data of wild-type proteins integrated. This is a convenient feature because it allows one to see the position of altered amino acids (shown in a different color) in the entire sequence of a wild-type protein; (ii) for those proteins whose 3D structures have been experimentally determined, a 3D structure is displayed to show mutation sites in a different color; (iii) a sequence homology search against PMD can be carried out with any query sequence; (iv) a summary of mutations of homologous sequences can be displayed, which shows all the mutations at a certain site of a protein, recorded throughout the PMD.
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Nucleic Acids ResHome page
B. Contreras-Moreira
3D-footprint: a database for the structural analysis of protein-DNA complexes
Nucleic Acids Res., September 18, 2009; (2009) gkp781v1.
[Abstract] [Full Text] [PDF]

Home page
 FASEB J.Home page
Y. Bromberg, J. Overton, C. Vaisse, R. L. Leibel, and B. Rost
In silico mutagenesis: a case study of the melanocortin 4 receptor
FASEB J, September 1, 2009; 23(9): 3059 - 3069.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
A. Pavelka, E. Chovancova, and J. Damborsky
HotSpot Wizard: a web server for identification of hot spots in protein engineering
Nucleic Acids Res., July 1, 2009; 37(suppl_2): W376 - W383.
[Abstract] [Full Text] [PDF]

Home page
 Brief BioinformHome page
R. Karchin
Next generation tools for the annotation of human SNPs
Brief Bioinform, January 1, 2009; 10(1): 35 - 52.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
M. M. Gromiha, Y. Yabuki, M. X. Suresh, A. M. Thangakani, M. Suwa, and K. Fukui
TMFunction: database for functional residues in membrane proteins
Nucleic Acids Res., January 1, 2009; 37(suppl_1): D201 - D204.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
M. Lonquety, Z. Lacroix, N. Papandreou, and J. Chomilier
SPROUTS: a database for the evaluation of protein stability upon point mutation
Nucleic Acids Res., January 1, 2009; 37(suppl_1): D374 - D379.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
H. Xi, J. Park, G. Ding, Y.-H. Lee, and Y. Li
SysPIMP: the web-based systematical platform for identifying human disease-related mutated sequences from mass spectrometry
Nucleic Acids Res., January 1, 2009; 37(suppl_1): D913 - D920.
[Abstract] [Full Text] [PDF]

Home page
 BioinformaticsHome page
Y. Bromberg, G. Yachdav, and B. Rost
SNAP predicts effect of mutations on protein function
Bioinformatics, October 15, 2008; 24(20): 2397 - 2398.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
Y. Bromberg and B. Rost
SNAP: predict effect of non-synonymous polymorphisms on function
Nucleic Acids Res., June 28, 2007; 35(11): 3823 - 3835.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
G. Lopez, A. Valencia, and M. Tress
FireDB--a database of functionally important residues from proteins of known structure
Nucleic Acids Res., January 12, 2007; 35(suppl_1): D219 - D223.
[Abstract] [Full Text] [PDF]

Home page
 Protein Eng Des SelHome page
M. R. Stam, E. G.J. Danchin, C. Rancurel, P. M. Coutinho, and B. Henrissat
Dividing the large glycoside hydrolase family 13 into subfamilies: towards improved functional annotations of {alpha}-amylase-related proteins
Protein Eng. Des. Sel., December 1, 2006; 19(12): 555 - 562.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
R. R. Gabdoulline, S. Ulbrich, S. Richter, and R. C. Wade
ProSAT2--Protein Structure Annotation Server.
Nucleic Acids Res., July 1, 2006; 34(Web Server issue): W79 - W83.
[Abstract] [Full Text] [PDF]

Home page
 GeneticsHome page
L. Y. Yampolsky and A. Stoltzfus
The Exchangeability of Amino Acids in Proteins
Genetics, August 1, 2005; 170(4): 1459 - 1472.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
D. Cotter, P. Guda, E. Fahy, and S. Subramaniam
MitoProteome: mitochondrial protein sequence database and annotation system
Nucleic Acids Res., January 1, 2004; 32(90001): D463 - 467.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
A. Schafferhans, J. E. W. Meyer, and S. I. O'Donoghue
The PSSH database of alignments between protein sequences and tertiary structures
Nucleic Acids Res., January 1, 2003; 31(1): 494 - 498.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
M. M. Gromiha, J. An, H. Kono, M. Oobatake, H. Uedaira, P. Prabakaran, and A. Sarai
ProTherm, version 2.0: thermodynamic database for proteins and mutants
Nucleic Acids Res., January 1, 2000; 28(1): 283 - 285.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.