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Protocols

DisProt specifications

Information


Unique identifier OMICS_03616
Name DisProt
Alternative name Database of Protein Disorder
Restrictions to use None
Community driven Yes
Data access File download, Browse
User data submission Allowed
Version 7.0.3
Maintained Yes

Documentation


Publications for Database of Protein Disorder

DisProt citations

 (106)
library_books

Discovery of Cryoprotective Activity in Human Genome Derived Intrinsically Disordered Proteins

2018
Int J Mol Sci
PMCID: 5855623
PMID: 29385704
DOI: 10.3390/ijms19020401

[…] mino acid sequences of human and mouse orthologs share >99% identity. Sequence redundancy was removed using BLASTClust. Because our purpose was to find novel IDPs, we cross-referenced sequences using DisProt and removed those that were known to be disordered []. We cloned 35 out of 53 candidate genes using a standard PCR cloning technique and assessed them by our original thermostable membrane pro […]

library_books

Pi Pi contacts are an overlooked protein feature relevant to phase separation

2018
eLife
PMCID: 5847340
PMID: 29424691
DOI: 10.7554/eLife.31486.045

[…] order predictions were obtained using Disopred3.16 () (standard command line and Refseq database) and IUPRED-Long (; ) against the phase separation test and training sets, the PDB test set, the human Disprot set, and a random selection of 7397 sequences from the human proteome. To convert these into per-sequence scores for comparison to the PScore, we then used the optimized window averaging metho […]

library_books

Functional Analysis of Human Hub Proteins and Their Interactors Involved in the Intrinsic Disorder Enriched Interactions

2017
Int J Mol Sci
PMCID: 5751360
PMID: 29257115
DOI: 10.3390/ijms18122761

[…] ins), and three versions of ESpritz that were designed for three types of annotations of disordered residues: using crystal structures, nuclear magnetic resonance structures, and annotations from the DisProt database [,]. We implemented the consensus using the majority vote, where three or more out of the five methods must predict the disorder for a given residue to be predicted as disordered. Thi […]

library_books

Novel linear motif filtering protocol reveals the role of the LC8 dynein light chain in the Hippo pathway

2017
PLoS Comput Biol
PMCID: 5746249
PMID: 29240760
DOI: 10.1371/journal.pcbi.1005885

[…] ods for the filtering steps. The importance of this optimization can be best demonstrated through the example of disorder prediction methods. Several methods, such as DISOPRED3, PONDR VSL2 or ESpritz Disprot [–], that were tested in this work, perform better on specific datasets of ordered and disordered proteins [–]. Nevertheless, IUPred achieved the best results for this specific problem, suppor […]

library_books

Analysis of the interactome of Schistosoma mansoni histone deacetylase 8

2017
PLoS Negl Trop Dis
PMCID: 5722368
PMID: 29155817
DOI: 10.1371/journal.pntd.0006089

[…] larly, it is possible that HDACs bind directly to the MBD2 IDR, because the human HDAC interactome study reveals a specific interaction between MBD2 and HDAC1/2 []. The Database of Protein Disorders (DisProt, www.disprot.org) [] predicts an IDR domain located between the MBD and the C-terminal coiled-coil domains of SmMBD2, which may be involved in SmHDAC8 binding.Focusing on the biological proces […]

library_books

Random protein sequences can form defined secondary structures and are well tolerated in vivo

2017
Sci Rep
PMCID: 5684393
PMID: 29133927
DOI: 10.1038/s41598-017-15635-8

[…] ucted three control libraries of 100/109-residue protein fragments from (i) the TOP8000 dataset of structured proteins deposited in the PDB database, (ii) the Uniprot sequence database, and (iii) the DisProt database of IDPs–.The similarity of the random and the known proteins sequences was assessed by the BLAST method implemented in BLAST + 2.6.0 software package. The NCBI Protein Reference Seque […]

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DisProt institution(s)
Department of Biomedical Sciences, University of Padova, Padova, Italy; Institute of Biosciences and Medical Technology, University of Tampere, Finland; [etc]
DisProt funding source(s)
COST Action BM1405 NGP-net, ELIXIR-IIB (elixir-italy.org), ‘Lendület’ Grant from the Hungarian Academy of Sciences (LP2014-16), Hungarian Scientific Research Fund (OTKA K 108798), AIRC Research Fellowship, Spanish Ministerio de Educación Cultura i Deporte PhD Fellowship, Mexican National Council for Science and Technology (CONACYT) PhD Fellowship (215503), Grant [email protected] funded by Norte Portugal Regional Operational Programme (NORTE 2020), under the PORTUGAL 2020 Partnership Agreement, through the European Regional Development Fund (ERDF), Direction Générale des Armées and Aix-Marseille University PhD Fellowship, OTKA Grant (PD-OTKA 108772), French Ministry of National Education, Research and Technology PhD Fellowship, Ministry of Education, Science and Technological Development of the Republic of Serbia (173001, 173049), ICREA-Academia Award, Odysseus Grant from Research Foundation Flanders (FWO) (G.0029.12), AIRC IG Grant (17753, in part), Italian Ministry of Health (GR-2011-02347754, GR-2011-02346845), Swedish Research Council Grant (VR-NT 2012-5046)

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