Home LiteratureArticle Details
PMID: 23203878 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

D²P²: database of disordered protein predictions.

Nucleic acids research ·Vol. 41 ·No. Database issue ·2013-01-00 ·Pages D508-16

Oates ME, Romero P, Ishida T, Ghalwash M, Mizianty MJ, Xue B, Dosztányi Z, Uversky VN, Obradovic Z, Kurgan L, Dunker AK, Gough J

Abstract

We present the Database of Disordered Protein Prediction (D(2)P(2)), available at http://d2p2.pro (including website source code). A battery of disorder predictors and their variants, VL-XT, VSL2b, PrDOS, PV2, Espritz and IUPred, were run on all protein sequences from 1765 complete proteomes (to be updated as more genomes are completed). Integrated with these results are all of the predicted (mostly structured) SCOP domains using the SUPERFAMILY predictor. These disorder/structure annotations together enable comparison of the disorder predictors with each other and examination of the overlap between disordered predictions and SCOP domains on a large scale. D(2)P(2) will increase our understanding of the interplay between disorder and structure, the genomic distribution of disorder, and its evolutionary history. The parsed data are made available in a unified format for download as flat files or SQL tables either by genome, by predictor, or for the complete set. An interactive website provides a graphical view of each protein annotated with the SCOP domains and disordered regions from all predictors overlaid (or shown as a consensus). There are statistics and tools for browsing and comparing genomes and their disorder within the context of their position on the tree of life.

MeSH Terms
Databases, Protein Genome Internet Protein Conformation Protein Structure, Tertiary Proteins/chemistry,genetics Sequence Analysis, Protein
Chemicals
Proteins
Authors & Affiliations
12 authors, click to expand affiliations / ORCID
Oates Matt E
Department of Computer Science, University of Bristol, Bristol BS8 1UB, UK. Matt.Oates@bristol.ac.uk
Romero Pedro
Ishida Takashi
Ghalwash Mohamed
Mizianty Marcin J
Xue Bin
Dosztányi Zsuzsanna
Uversky Vladimir N
Obradovic Zoran
Kurgan Lukasz
Dunker A Keith
Gough Julian
References (41)
41 references, click to expand
  1. SCOP: a structural classification of proteins database for the investigation of sequences and structures.
    J Mol Biol. 1995 Apr 7;247(4):536-40 PMID: 7723011
  2. MOBI: a web server to define and visualize structural mobility in NMR protein ensembles.
    Bioinformatics. 2010 Nov 15;26(22):2916-7 PMID: 20861031
  3. Predicting Protein Disorder for N-, C-, and Internal Regions.
    Genome Inform Ser Workshop Genome Inform. 1999;10:30-40 PMID: 11072340
  4. PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse.
    Nucleic Acids Res. 2012 Jan;40(Database issue):D261-70 PMID: 22135298
  5. The RCSB Protein Data Bank: redesigned web site and web services.
    Nucleic Acids Res. 2011 Jan;39(Database issue):D392-401 PMID: 21036868
  6. PHD--an automatic mail server for protein secondary structure prediction.
    Comput Appl Biosci. 1994 Feb;10(1):53-60 PMID: 8193956
  7. The importance of intrinsic disorder for protein phosphorylation.
    Nucleic Acids Res. 2004 Feb 11;32(3):1037-49 PMID: 14960716
  8. On the complementarity of the consensus-based disorder prediction.
    Pac Symp Biocomput. 2012;:176-87 PMID: 22174273
  9. Assignment of homology to genome sequences using a library of hidden Markov models that represent all proteins of known structure.
    J Mol Biol. 2001 Nov 2;313(4):903-19 PMID: 11697912
  10. SUPERFAMILY 1.75 including a domain-centric gene ontology method.
    Nucleic Acids Res. 2011 Jan;39(Database issue):D427-34 PMID: 21062816
  11. Why are "natively unfolded" proteins unstructured under physiologic conditions?
    Proteins. 2000 Nov 15;41(3):415-27 PMID: 11025552
  12. Binary classification of protein molecules into intrinsically disordered and ordered segments.
    BMC Struct Biol. 2011 Jun 22;11:29 PMID: 21693062
  13. IDEAL: Intrinsically Disordered proteins with Extensive Annotations and Literature.
    Nucleic Acids Res. 2012 Jan;40(Database issue):D507-11 PMID: 22067451
  14. Development of an accurate classification system of proteins into structured and unstructured regions that uncovers novel structural domains: its application to human transcription factors.
    BMC Struct Biol. 2009 Apr 30;9:26 PMID: 19402914
  15. Uncertainty analysis in protein disorder prediction.
    Mol Biosyst. 2012 Jan;8(1):381-91 PMID: 22101336
  16. Conservation of intrinsic disorder in protein domains and families: I. A database of conserved predicted disordered regions.
    J Proteome Res. 2006 Apr;5(4):879-87 PMID: 16602695
  17. Protein secondary structure prediction based on position-specific scoring matrices.
    J Mol Biol. 1999 Sep 17;292(2):195-202 PMID: 10493868
  18. PrDOS: prediction of disordered protein regions from amino acid sequence.
    Nucleic Acids Res. 2007 Jul;35(Web Server issue):W460-4 PMID: 17567614
  19. Intrinsically unstructured proteins and their functions.
    Nat Rev Mol Cell Biol. 2005 Mar;6(3):197-208 PMID: 15738986
  20. Tissue-specific alternative splicing remodels protein-protein interaction networks.
    Mol Cell. 2012 Jun 29;46(6):884-92 PMID: 22749401
  21. A bimodal distribution of two distinct categories of intrinsically disordered structures with separate functions in FG nucleoporins.
    Mol Cell Proteomics. 2010 Oct;9(10):2205-24 PMID: 20368288
  22. Evaluation of disorder predictions in CASP9.
    Proteins. 2011;79 Suppl 10:107-18 PMID: 21928402
  23. Prediction and functional analysis of native disorder in proteins from the three kingdoms of life.
    J Mol Biol. 2004 Mar 26;337(3):635-45 PMID: 15019783
  24. Conservation of intrinsic disorder in protein domains and families: II. functions of conserved disorder.
    J Proteome Res. 2006 Apr;5(4):888-98 PMID: 16602696
  25. PONDR-FIT: a meta-predictor of intrinsically disordered amino acids.
    Biochim Biophys Acta. 2010 Apr;1804(4):996-1010 PMID: 20100603
  26. Micelle-induced folding of spinach thylakoid soluble phosphoprotein of 9 kDa and its functional implications.
    Biochemistry. 2006 Dec 26;45(51):15633-43 PMID: 17176085
  27. Prediction of protein binding regions in disordered proteins.
    PLoS Comput Biol. 2009 May;5(5):e1000376 PMID: 19412530
  28. Function and structure of inherently disordered proteins.
    Curr Opin Struct Biol. 2008 Dec;18(6):756-64 PMID: 18952168
  29. Sequence complexity of disordered protein.
    Proteins. 2001 Jan 1;42(1):38-48 PMID: 11093259
  30. Predicting intrinsic disorder in proteins: an overview.
    Cell Res. 2009 Aug;19(8):929-49 PMID: 19597536
  31. Sequence context-specific profiles for homology searching.
    Proc Natl Acad Sci U S A. 2009 Mar 10;106(10):3770-5 PMID: 19234132
  32. MobiDB: a comprehensive database of intrinsic protein disorder annotations.
    Bioinformatics. 2012 Aug 1;28(15):2080-1 PMID: 22661649
  33. The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins.
    J Mol Biol. 2005 Apr 8;347(4):827-39 PMID: 15769473
  34. DisProt: the Database of Disordered Proteins.
    Nucleic Acids Res. 2007 Jan;35(Database issue):D786-93 PMID: 17145717
  35. SCOP database in 2004: refinements integrate structure and sequence family data.
    Nucleic Acids Res. 2004 Jan 1;32(Database issue):D226-9 PMID: 14681400
  36. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs.
    Nucleic Acids Res. 1997 Sep 1;25(17):3389-402 PMID: 9254694
  37. Length-dependent prediction of protein intrinsic disorder.
    BMC Bioinformatics. 2006 Apr 17;7:208 PMID: 16618368
  38. Comprehensive comparative assessment of in-silico predictors of disordered regions.
    Curr Protein Pept Sci. 2012 Feb;13(1):6-18 PMID: 22044149
  39. ESpritz: accurate and fast prediction of protein disorder.
    Bioinformatics. 2012 Feb 15;28(4):503-9 PMID: 22190692
  40. Natively unfolded proteins: a point where biology waits for physics.
    Protein Sci. 2002 Apr;11(4):739-56 PMID: 11910019
  41. MetaDisorder: a meta-server for the prediction of intrinsic disorder in proteins.
    BMC Bioinformatics. 2012 May 24;13:111 PMID: 22624656
Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
1362-4962
Published
2013-01-00
Epub
2012-00-29
Pages
D508-16
Language
English
Region
England
NLM ID
0411011
PMCID
PMC3531159
Subset
IM
Grants
Biotechnology and Biological Sciences Research Council · BB/G022771/1 · United Kingdom
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com