The RESID database of protein modifications as a resource and annotation tool

被引:114
作者
Garavelli, JS [1 ]
机构
[1] EMBL Outstn, European Bioinformat Inst, Hinxton CB10 1SD, Cambs, England
关键词
bioinformatics; database annotation; protein cross-links; protein modifications;
D O I
10.1002/pmic.200300777
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The RESID Database of Protein Modifications is a comprehensive collection of annotations and structures for protein modifications and cross-links including pre-, co-, and post-translational modifications. The database provides: systematic and alternate names, atomic formulas and masses, enzymatic activities that generated the modifications, keywords, literature citations, Gene Ontology (GO) cross-references, protein sequence database feature table annotations, structure diagrams, and molecular models. This database is freely accessible on the Internet through resources provided by the European Bioinformatics Institute (http:H www.ebi.ac.uk/RESID), and by the National Cancer Institute-Frederick Advanced Biomedical Computing Center (http://www.ncifcrf.gov/RESID). Each RESID Database entry presents a chemically unique modification and shows how that modification is currently annotated in the protein sequence databases, Swiss-Prot and the Protein Information Resource (PIR). The RESID Database provides a table of corresponding equivalent feature annotations that is used in the UniProt project, an international effort to combine the resources of the Swiss-Prot, TrEMBL and PIR. As an annotation tool, the RESID Database is used in standardizing and enhancing modification descriptions in the feature tables of Swiss-Prot entries. As an Internet resource, the RESID Database assists researchers in high-throughput proteomics to search monoisotopic
引用
收藏
页码:1527 / 1533
页数:7
相关论文
共 21 条
[1]  
Apweiler R, 2004, NUCLEIC ACIDS RES, V32, pD115, DOI [10.1093/nar/gkw1099, 10.1093/nar/gkh131]
[2]  
Ashburner M, 2001, GENOME RES, V11, P1425
[3]   The SWISS-PROT protein knowledgebase and its supplement TrEMBL in 2003 [J].
Boeckmann, B ;
Bairoch, A ;
Apweiler, R ;
Blatter, MC ;
Estreicher, A ;
Gasteiger, E ;
Martin, MJ ;
Michoud, K ;
O'Donovan, C ;
Phan, I ;
Pilbout, S ;
Schneider, M .
NUCLEIC ACIDS RESEARCH, 2003, 31 (01) :365-370
[4]  
CORNISHBOWDEN A, 1984, EUR J BIOCHEM, V138, P9, DOI 10.1111/j.1432-1033.1984.tb07877.x
[5]   Bioinorganic motifs: towards functional classification of metalloproteins [J].
Degtyarenko, K .
BIOINFORMATICS, 2000, 16 (10) :851-864
[6]  
Degtyarenko Kirill, 2004, BMC Struct Biol, V4, P3, DOI 10.1186/1472-6807-4-3
[7]   The RESID Database of Protein Modifications: 2003 developments [J].
Garavelli, JS .
NUCLEIC ACIDS RESEARCH, 2003, 31 (01) :499-501
[8]  
GARAVELLI JS, 1993, PROTEIN SCI S1, V2, P133
[9]   Prediction of human protein function from post-translational modifications and localization features [J].
Jensen, LJ ;
Gupta, R ;
Blom, N ;
Devos, D ;
Tamames, J ;
Kesmir, C ;
Nielsen, H ;
Stærfeldt, HH ;
Rapacki, K ;
Workman, C ;
Andersen, CAF ;
Knudsen, S ;
Krogh, A ;
Valencia, A ;
Brunak, S .
JOURNAL OF MOLECULAR BIOLOGY, 2002, 319 (05) :1257-1265
[10]  
KOCH TH, 1984, METHOD ENZYMOL, V107, P563