DisProt 7.0: A major update of the database of disordered proteins

Damiano Piovesan; Francesco Tabaro; Ivan Mičetić; Marco Necci; Federica Quaglia; Christopher J. Oldfield; Maria Cristina Aspromonte; Norman E. Davey; Radoslav Davidović; Zsuzsanna Dosztányi; Arne Elofsson; Alessandra Gasparini; András Hatos; Andrey V. Kajava; Lajos Kalmar; Emanuela Leonardi; Tamas Lazar; Sandra Macedo-Ribeiro; Mauricio Macossay-Castillo; Attila Meszaros; Giovanni Minervini; Nikoletta Murvai; Jordi Pujols; Daniel B. Roche; Edoardo Salladini; Eva Schad; Antoine Schramm; Beata Szabo; Agnes Tantos; Fiorella Tonello; Konstantinos D. Tsirigos; Nevena Veljković; Salvador Ventura; Wim Vranken; Per Warholm; Vladimir N. Uversky; A. Keith Dunker; Sonia Longhi; Peter Tompa; Silvio C.E. Tosatto

doi:https://doi.org/10.1093/nar/gkw1056

DisProt 7.0: A major update of the database of disordered proteins

Damiano Piovesan, Francesco Tabaro, Ivan Mičetić, Marco Necci, Federica Quaglia, Christopher J. Oldfield, Maria Cristina Aspromonte, Norman E. Davey, Radoslav Davidović, Zsuzsanna Dosztányi, Arne Elofsson, Alessandra Gasparini, András Hatos, Andrey V. Kajava, Lajos Kalmar, Emanuela Leonardi, Tamas Lazar, Sandra Macedo-Ribeiro, Mauricio Macossay-Castillo, Attila MeszarosGiovanni Minervini, Nikoletta Murvai, Jordi Pujols, Daniel B. Roche, Edoardo Salladini, Eva Schad, Antoine Schramm, Beata Szabo, Agnes Tantos, Fiorella Tonello, Konstantinos D. Tsirigos, Nevena Veljković, Salvador Ventura, Wim Vranken, Per Warholm, Vladimir N. Uversky, A. Keith Dunker, Sonia Longhi, Peter Tompa, Silvio C.E. Tosatto

Research output: Contribution to journal › Article › Research › peer-review

122 Citations (Scopus)

Abstract

© The Author(s) 2016. The Database of Protein Disorder (DisProt, URL: www.disprot.org) has been significantly updated and upgraded since its last major renewal in 2007. The current release holds information on more than 800 entries of IDPs/IDRs, i.e. intrinsically disordered proteins or regions that exist and function without a well-defined three-dimensional structure. We have re-curated previous entries to purge DisProt from conflicting cases, and also upgraded the functional classification scheme to reflect continuous advance in the field in the past 10 years or so. We define IDPs as proteins that are disordered along their entire sequence, i.e. entirely lack structural elements, and IDRs as regions that are at least five consecutive residues without well-defined structure. We base our assessment of disorder strictly on experimental evidence, such as X-ray crystallography and nuclear magnetic resonance (primary techniques) and a broad range of other experimental approaches (secondary techniques). Confident and ambiguous annotations are highlighted separately. DisProt 7.0 presents classified knowledge regarding the experimental characterization and functional annotations of IDPs/IDRs, and is intended to provide an invaluable resource for the research community for a better understanding structural disorder and for developing better computational tools for studying disordered proteins.

Original language	English
Pages (from-to)	D219-D227
Journal	Nucleic Acids Research
Volume	45
Issue number	D1
DOIs	https://doi.org/10.1093/nar/gkw1056
Publication status	Published - 1 Jan 2017

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Piovesan, D., Tabaro, F., Mičetić, I., Necci, M., Quaglia, F., Oldfield, C. J., Aspromonte, M. C., Davey, N. E., Davidović, R., Dosztányi, Z., Elofsson, A., Gasparini, A., Hatos, A., Kajava, A. V., Kalmar, L., Leonardi, E., Lazar, T., Macedo-Ribeiro, S., Macossay-Castillo, M., ... Tosatto, S. C. E. (2017). DisProt 7.0: A major update of the database of disordered proteins. Nucleic Acids Research, 45(D1), D219-D227. https://doi.org/10.1093/nar/gkw1056

Piovesan, Damiano ; Tabaro, Francesco ; Mičetić, Ivan ; Necci, Marco ; Quaglia, Federica ; Oldfield, Christopher J. ; Aspromonte, Maria Cristina ; Davey, Norman E. ; Davidović, Radoslav ; Dosztányi, Zsuzsanna ; Elofsson, Arne ; Gasparini, Alessandra ; Hatos, András ; Kajava, Andrey V. ; Kalmar, Lajos ; Leonardi, Emanuela ; Lazar, Tamas ; Macedo-Ribeiro, Sandra ; Macossay-Castillo, Mauricio ; Meszaros, Attila ; Minervini, Giovanni ; Murvai, Nikoletta ; Pujols, Jordi ; Roche, Daniel B. ; Salladini, Edoardo ; Schad, Eva ; Schramm, Antoine ; Szabo, Beata ; Tantos, Agnes ; Tonello, Fiorella ; Tsirigos, Konstantinos D. ; Veljković, Nevena ; Ventura, Salvador ; Vranken, Wim ; Warholm, Per ; Uversky, Vladimir N. ; Dunker, A. Keith ; Longhi, Sonia ; Tompa, Peter ; Tosatto, Silvio C.E. / DisProt 7.0: A major update of the database of disordered proteins. In: Nucleic Acids Research. 2017 ; Vol. 45, No. D1. pp. D219-D227.

@article{1c239a47f8df4394970806b5882f3155,

title = "DisProt 7.0: A major update of the database of disordered proteins",

abstract = "{\textcopyright} The Author(s) 2016. The Database of Protein Disorder (DisProt, URL: www.disprot.org) has been significantly updated and upgraded since its last major renewal in 2007. The current release holds information on more than 800 entries of IDPs/IDRs, i.e. intrinsically disordered proteins or regions that exist and function without a well-defined three-dimensional structure. We have re-curated previous entries to purge DisProt from conflicting cases, and also upgraded the functional classification scheme to reflect continuous advance in the field in the past 10 years or so. We define IDPs as proteins that are disordered along their entire sequence, i.e. entirely lack structural elements, and IDRs as regions that are at least five consecutive residues without well-defined structure. We base our assessment of disorder strictly on experimental evidence, such as X-ray crystallography and nuclear magnetic resonance (primary techniques) and a broad range of other experimental approaches (secondary techniques). Confident and ambiguous annotations are highlighted separately. DisProt 7.0 presents classified knowledge regarding the experimental characterization and functional annotations of IDPs/IDRs, and is intended to provide an invaluable resource for the research community for a better understanding structural disorder and for developing better computational tools for studying disordered proteins.",

author = "Damiano Piovesan and Francesco Tabaro and Ivan Mi{\v c}eti{\'c} and Marco Necci and Federica Quaglia and Oldfield, {Christopher J.} and Aspromonte, {Maria Cristina} and Davey, {Norman E.} and Radoslav Davidovi{\'c} and Zsuzsanna Doszt{\'a}nyi and Arne Elofsson and Alessandra Gasparini and Andr{\'a}s Hatos and Kajava, {Andrey V.} and Lajos Kalmar and Emanuela Leonardi and Tamas Lazar and Sandra Macedo-Ribeiro and Mauricio Macossay-Castillo and Attila Meszaros and Giovanni Minervini and Nikoletta Murvai and Jordi Pujols and Roche, {Daniel B.} and Edoardo Salladini and Eva Schad and Antoine Schramm and Beata Szabo and Agnes Tantos and Fiorella Tonello and Tsirigos, {Konstantinos D.} and Nevena Veljkovi{\'c} and Salvador Ventura and Wim Vranken and Per Warholm and Uversky, {Vladimir N.} and Dunker, {A. Keith} and Sonia Longhi and Peter Tompa and Tosatto, {Silvio C.E.}",

year = "2017",

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doi = "https://doi.org/10.1093/nar/gkw1056",

language = "English",

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pages = "D219--D227",

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Piovesan, D, Tabaro, F, Mičetić, I, Necci, M, Quaglia, F, Oldfield, CJ, Aspromonte, MC, Davey, NE, Davidović, R, Dosztányi, Z, Elofsson, A, Gasparini, A, Hatos, A, Kajava, AV, Kalmar, L, Leonardi, E, Lazar, T, Macedo-Ribeiro, S, Macossay-Castillo, M, Meszaros, A, Minervini, G, Murvai, N, Pujols, J, Roche, DB, Salladini, E, Schad, E, Schramm, A, Szabo, B, Tantos, A, Tonello, F, Tsirigos, KD, Veljković, N, Ventura, S, Vranken, W, Warholm, P, Uversky, VN, Dunker, AK, Longhi, S, Tompa, P & Tosatto, SCE 2017, 'DisProt 7.0: A major update of the database of disordered proteins', Nucleic Acids Research, vol. 45, no. D1, pp. D219-D227. https://doi.org/10.1093/nar/gkw1056

DisProt 7.0: A major update of the database of disordered proteins. / Piovesan, Damiano; Tabaro, Francesco; Mičetić, Ivan; Necci, Marco; Quaglia, Federica; Oldfield, Christopher J.; Aspromonte, Maria Cristina; Davey, Norman E.; Davidović, Radoslav; Dosztányi, Zsuzsanna; Elofsson, Arne; Gasparini, Alessandra; Hatos, András; Kajava, Andrey V.; Kalmar, Lajos; Leonardi, Emanuela; Lazar, Tamas; Macedo-Ribeiro, Sandra; Macossay-Castillo, Mauricio; Meszaros, Attila; Minervini, Giovanni; Murvai, Nikoletta; Pujols, Jordi; Roche, Daniel B.; Salladini, Edoardo; Schad, Eva; Schramm, Antoine; Szabo, Beata; Tantos, Agnes; Tonello, Fiorella; Tsirigos, Konstantinos D.; Veljković, Nevena; Ventura, Salvador; Vranken, Wim; Warholm, Per; Uversky, Vladimir N.; Dunker, A. Keith; Longhi, Sonia; Tompa, Peter; Tosatto, Silvio C.E.

In: Nucleic Acids Research, Vol. 45, No. D1, 01.01.2017, p. D219-D227.

Research output: Contribution to journal › Article › Research › peer-review

TY - JOUR

T1 - DisProt 7.0: A major update of the database of disordered proteins

AU - Piovesan, Damiano

AU - Tabaro, Francesco

AU - Mičetić, Ivan

AU - Necci, Marco

AU - Quaglia, Federica

AU - Oldfield, Christopher J.

AU - Aspromonte, Maria Cristina

AU - Davey, Norman E.

AU - Davidović, Radoslav

AU - Dosztányi, Zsuzsanna

AU - Elofsson, Arne

AU - Gasparini, Alessandra

AU - Hatos, András

AU - Kajava, Andrey V.

AU - Kalmar, Lajos

AU - Leonardi, Emanuela

AU - Lazar, Tamas

AU - Macedo-Ribeiro, Sandra

AU - Macossay-Castillo, Mauricio

AU - Meszaros, Attila

AU - Minervini, Giovanni

AU - Murvai, Nikoletta

AU - Pujols, Jordi

AU - Roche, Daniel B.

AU - Salladini, Edoardo

AU - Schad, Eva

AU - Schramm, Antoine

AU - Szabo, Beata

AU - Tantos, Agnes

AU - Tonello, Fiorella

AU - Tsirigos, Konstantinos D.

AU - Veljković, Nevena

AU - Ventura, Salvador

AU - Vranken, Wim

AU - Warholm, Per

AU - Uversky, Vladimir N.

AU - Dunker, A. Keith

AU - Longhi, Sonia

AU - Tompa, Peter

AU - Tosatto, Silvio C.E.

PY - 2017/1/1

Y1 - 2017/1/1

N2 - © The Author(s) 2016. The Database of Protein Disorder (DisProt, URL: www.disprot.org) has been significantly updated and upgraded since its last major renewal in 2007. The current release holds information on more than 800 entries of IDPs/IDRs, i.e. intrinsically disordered proteins or regions that exist and function without a well-defined three-dimensional structure. We have re-curated previous entries to purge DisProt from conflicting cases, and also upgraded the functional classification scheme to reflect continuous advance in the field in the past 10 years or so. We define IDPs as proteins that are disordered along their entire sequence, i.e. entirely lack structural elements, and IDRs as regions that are at least five consecutive residues without well-defined structure. We base our assessment of disorder strictly on experimental evidence, such as X-ray crystallography and nuclear magnetic resonance (primary techniques) and a broad range of other experimental approaches (secondary techniques). Confident and ambiguous annotations are highlighted separately. DisProt 7.0 presents classified knowledge regarding the experimental characterization and functional annotations of IDPs/IDRs, and is intended to provide an invaluable resource for the research community for a better understanding structural disorder and for developing better computational tools for studying disordered proteins.

AB - © The Author(s) 2016. The Database of Protein Disorder (DisProt, URL: www.disprot.org) has been significantly updated and upgraded since its last major renewal in 2007. The current release holds information on more than 800 entries of IDPs/IDRs, i.e. intrinsically disordered proteins or regions that exist and function without a well-defined three-dimensional structure. We have re-curated previous entries to purge DisProt from conflicting cases, and also upgraded the functional classification scheme to reflect continuous advance in the field in the past 10 years or so. We define IDPs as proteins that are disordered along their entire sequence, i.e. entirely lack structural elements, and IDRs as regions that are at least five consecutive residues without well-defined structure. We base our assessment of disorder strictly on experimental evidence, such as X-ray crystallography and nuclear magnetic resonance (primary techniques) and a broad range of other experimental approaches (secondary techniques). Confident and ambiguous annotations are highlighted separately. DisProt 7.0 presents classified knowledge regarding the experimental characterization and functional annotations of IDPs/IDRs, and is intended to provide an invaluable resource for the research community for a better understanding structural disorder and for developing better computational tools for studying disordered proteins.

UR - https://ddd.uab.cat/record/186042

U2 - https://doi.org/10.1093/nar/gkw1056

DO - https://doi.org/10.1093/nar/gkw1056

M3 - Article

VL - 45

SP - D219-D227

IS - D1

ER -