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The InterPro protein families database: the classification resource after 15 years.

Mitchell A, Chang HY, Daugherty L, Fraser M, Hunter S, Lopez R, McAa C, McMenamin C, Nuka G, Pesseat S, Sangrador-Vegas A, Scheremetjew M, Rato C, Yong SY, Bateman A, Punta M, Attwood TK, Sigrist CJ, Redaschi N, Rivoire C, Xenarios I, Kahn D, Guyot D, Bork P, Letunic I, Gough J, Oates M, Haft D, Huang H, Natale DA, Wu CH, Orengo C, Sillitoe I, Mi H, Thomas PD, Finn RD - Nucleic Acids Res. (2014)

Bottom Line: Here, we report on the status of InterPro as it enters its 15th year of operation, and give an overview of new developments with the database and its associated Web interfaces and software.We also discuss the challenges faced by the resource given the explosive growth in sequence data in recent years.InterPro (version 48.0) contains 36,766 member database signatures integrated into 26,238 InterPro entries, an increase of over 3993 entries (5081 signatures), since 2012.

View Article: PubMed Central - PubMed

Affiliation: European Molecular Biology Laboratory, European Bioinformatics Institute (EMBL-EBI), Wellcome Trust Genome Campus, Hinxton, Cambridge, CB10 1SD, UK.

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The InterPro Domain Architecture tool showing the results of searching with a VIT and 14-3-3 domain. Checking the ‘Order sensitivity’ option (A) means that domain order is taken into account in the results section (B). The domains can be reordered by dragging and dropping their graphical representations (C), or removed from the query by dragging them to the dustbin (D) or clicking on the [x] icon next to their name and accession (E). The InterPro accession string (F) summarizes the domain architecture composition.
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Figure 5: The InterPro Domain Architecture tool showing the results of searching with a VIT and 14-3-3 domain. Checking the ‘Order sensitivity’ option (A) means that domain order is taken into account in the results section (B). The domains can be reordered by dragging and dropping their graphical representations (C), or removed from the query by dragging them to the dustbin (D) or clicking on the [x] icon next to their name and accession (E). The InterPro accession string (F) summarizes the domain architecture composition.

Mentions: Once the required domains have been selected, pressing the ‘Apply’ button performs the appropriate query. The different domain architectures matching the query, along with the number of proteins matching each domain architecture, are displayed graphically (as shown in Figure 5). A cartoon version of the query is also generated, with domains represented as coloured squares that can be reordered or removed from the query by dragging and dropping, which automatically updates the search results.


The InterPro protein families database: the classification resource after 15 years.

Mitchell A, Chang HY, Daugherty L, Fraser M, Hunter S, Lopez R, McAa C, McMenamin C, Nuka G, Pesseat S, Sangrador-Vegas A, Scheremetjew M, Rato C, Yong SY, Bateman A, Punta M, Attwood TK, Sigrist CJ, Redaschi N, Rivoire C, Xenarios I, Kahn D, Guyot D, Bork P, Letunic I, Gough J, Oates M, Haft D, Huang H, Natale DA, Wu CH, Orengo C, Sillitoe I, Mi H, Thomas PD, Finn RD - Nucleic Acids Res. (2014)

The InterPro Domain Architecture tool showing the results of searching with a VIT and 14-3-3 domain. Checking the ‘Order sensitivity’ option (A) means that domain order is taken into account in the results section (B). The domains can be reordered by dragging and dropping their graphical representations (C), or removed from the query by dragging them to the dustbin (D) or clicking on the [x] icon next to their name and accession (E). The InterPro accession string (F) summarizes the domain architecture composition.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4383996&req=5

Figure 5: The InterPro Domain Architecture tool showing the results of searching with a VIT and 14-3-3 domain. Checking the ‘Order sensitivity’ option (A) means that domain order is taken into account in the results section (B). The domains can be reordered by dragging and dropping their graphical representations (C), or removed from the query by dragging them to the dustbin (D) or clicking on the [x] icon next to their name and accession (E). The InterPro accession string (F) summarizes the domain architecture composition.
Mentions: Once the required domains have been selected, pressing the ‘Apply’ button performs the appropriate query. The different domain architectures matching the query, along with the number of proteins matching each domain architecture, are displayed graphically (as shown in Figure 5). A cartoon version of the query is also generated, with domains represented as coloured squares that can be reordered or removed from the query by dragging and dropping, which automatically updates the search results.

Bottom Line: Here, we report on the status of InterPro as it enters its 15th year of operation, and give an overview of new developments with the database and its associated Web interfaces and software.We also discuss the challenges faced by the resource given the explosive growth in sequence data in recent years.InterPro (version 48.0) contains 36,766 member database signatures integrated into 26,238 InterPro entries, an increase of over 3993 entries (5081 signatures), since 2012.

View Article: PubMed Central - PubMed

Affiliation: European Molecular Biology Laboratory, European Bioinformatics Institute (EMBL-EBI), Wellcome Trust Genome Campus, Hinxton, Cambridge, CB10 1SD, UK.

Show MeSH