LiteFold/DisProt huggingface dataset:
Protein: DP02558 (UniProt Q9NP70)
Region: residues 223	to 447
Annotation: disorder (Structural state)
Evidence: dynamic light scattering assay evidence used in manual assertion
Supporting statements:
The broadest peak (with a half‐width spanning interval of approximately 90 nm), corresponding to hrAMBN‐Cter, illustrates clearly the disordered nature of the C‐terminus and the huge spectrum of its structural forms.
Protein: DP02558 (UniProt Q9NP70)
Region: residues 62	to 98
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
no well defined elements of regular secondary structure were observed in the CD spectra of the synthetic peptide encompassing residues 36–72 (peptide 36–72) of AMBN
There is a shift in residue numbering due to the lack of signal peptide of 26 residues in the studied protein construct.
Protein: DP02558 (UniProt Q9NP70)
Region: residues 62	to 98
Annotation: disorder (Structural state)
Evidence: temperature-induced protein unfolding evidence used in manual assertion
Supporting statements:
In addition, thermal denaturation CD experiments with peptide 36–72 showed profiles characteristic for IDPs
There is a shift in residue numbering due to the lack of signal peptide of 26 residues in the studied protein construct.
Protein: DP02558 (UniProt Q9NP70)
Region: residues 62	to 98
Annotation: self-assembly (Disorder function)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
Electron microscopy revealed that the AMBN high molecular mass self-assemblies were flat ribbon-like supramolecular structures with an average width of 18 ± 4 nm and with a variable size, ranging from tens to hundreds of nanometers in length
This clearly shows that the segment encompassing residues 36–72 confers the self-assembly capacity of AMBN.
There is a shift in residue numbering due to the lack of signal peptide of 26 residues in the studied protein construct.
Here we observed that AMBN self-associates into ribbon-like supramolecular structures and that this self-assembly process is abolished by the deletion of the 37 residues long segment 36–72 located in the N-terminal portion of the molecule.
Protein: DP02558 (UniProt Q9NP70)
Region: residues 27	to 447
Annotation: disorder (Structural state)
Evidence: dynamic light scattering assay evidence used in manual assertion
Supporting statements:
The disordered character of all the studied molecules becomes apparent when compared with the DLS profile of BSA.
One of the studied molecules was full-length ameloblastin, so it is stated to be disordered. Figure 5 shows large difference between the DLS curves of the ameloblastin constructs and that of BSA. Also, Trhoughout the paper the authors emphasize that the disordered, acidic C-terminus has a stronger effect on the structure of the full protein than the slightly more ordered N-terminal half.
Protein: DP02558 (UniProt Q9NP70)
Region: residues 220	to 225
Annotation: limited proteolysis display site (Disorder function)
Evidence: combinatorial experimental and author inference evidence contained in single publication used in manual assertion
Supporting statements:
All analyses and modelling data were in agreement with earlier experimental  observations  that  tooth-specific  proteases (enamelysin and kallikrein) separate the basic N-terminus from the acidic C-terminal region of the AMBN molecule.
Protein: DP02558 (UniProt Q9NP70)
Region: residues 27	to 447
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The CD spectra of all three AMBN molecules at physiological temperature did not provide a clear signal of a dominant and well-profiled structure.
One of the three AMBN constructs studied was the full-lengh protein.
Protein: DP02559 (UniProt Q969R2)
Region: residues 1	to 184
Annotation: disorder (Structural state)
Evidence: chromatography evidence used in manual assertion
Supporting statements:
In all cases, we observed that N-ter had a large impact on protein size, increasing the Stoke’s radius by ∼0.5 to 1 nm for OSBP constructs (OSBP versus ΔN-OSBP, N-PH-FFAT versus PH-FFAT, N-PH-ΔCC-FFAT versus PH-ΔCC-FFAT) and by ∼1.3 nm for ORP4 constructs (N-PH-FFAT versus PH-FFAT) (Figure 1D). This increase was about 2-fold higher than what was expected from the slope of the calibration curve, which was established with folded globular standards.
Protein: DP02559 (UniProt Q969R2)
Region: residues 1	to 184
Annotation: localization (Biological process)
Evidence: mutant phenotype evidence used in manual assertion
Supporting statements:
ORP4 PH-FFAT showed significantly higher Golgi partitioning than ORP4 N-PH-FFAT (Figure 2B). Thus, the N-ter of OSBP and ORP4 reduce the Golgi membrane partitioning of these proteins.
Protein: DP02561 (UniProt P60880)
Region: residues 83	to 141
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
In general, the SNAP25 loop region is disordered in solution.
Protein: DP02561 (UniProt P60880)
Region: residues 83	to 141
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion
Supporting statements:
The hydrogen-deuterium exchange experiment shows that the hydrogen exchange rate of the residues in the middle part (107–131) is too fast to be detected in both buffer and bicelle. The hydrogen exchange rate of Nterminal residues is barely slower than C-terminal residues in buffer
Protein: DP02561 (UniProt P60880)
Region: residues 83	to 110
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
We then expressed the SNAP25 loop region alone to simplify the spectra and acquired the 1H-15N HSQC in buffer and liposomes (Fig. 3 B). Assignments were made by using standard triple resonance experiments (Supplemental Fig. S10 B). In the membrane, many cross peaks from the N-terminal of loop region were broadened beyond detection. The crosspeaks intensity ratios of the SNAP25 loop in buffer and liposomes (Fig. 3 C) also show that the cross-peak intensity decrease caused by membrane binding is localized to the N-terminal of the SNAP25 loop, especially the cysteine rich domain. 
First, membrane binding induces a disorder-to-order conformational transition of the SNAP25 loop involving the formation of an a-helix.
Protein: DP02561 (UniProt P60880)
Region: residues 111	to 141
Annotation: phosphorylation display site (Disorder function)
Evidence: combinatorial experimental and author inference evidence contained in single publication used in manual assertion
Supporting statements:
In this process, phosphorylation of the threonine (T)138 in the C-terminal of the SNAP25 loop influences the electrostatic interaction with syx-1, which explains how phosphorylation T138 mediates SNARE-complex assembly.
Protein: DP02561 (UniProt P60880)
Region: residues 111	to 141
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
To determine whether the membrane-induced SNAP25 conformational change affects its interaction with syx-1, we acquired 1H-15N HSQC NMR spectra of uniformly enriched SNAP25 loop with or without unenriched syx-1 (1–264) in aqueous buffer and in liposomes (Fig. 6 A, B). Most of the spectrum is unchanged upon addition of syx-1 (1–264) in the buffer, but in liposomes, significant changes in signal intensities were observed in the C-terminal of the SNAP25 loop, and a number of resonances disappeared.
Second, the loop region mediates SNARE complex assembly through its interaction with the syx-1
Protein: DP02561 (UniProt P60880)
Region: residues 83	to 110
Annotation: lipid binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
We then expressed the SNAP25 loop region alone to simplify the spectra and acquired the 1H-15N HSQC in buffer and liposomes (Fig. 3 B). Assignments were made by using standard triple resonance experiments (Supplemental Fig. S10 B). In the membrane, many cross peaks from the N-terminal of loop region were broadened beyond detection. The crosspeaks intensity ratios of the SNAP25 loop in buffer and liposomes (Fig. 3 C) also show that the cross-peak intensity decrease caused by membrane binding is localized to the N-terminal of the SNAP25 loop, especially the cysteine rich domain.
First, membrane binding induces a disorder-to-order conformational transition of the SNAP25 loop involving the formation of an a-helix.
Protein: DP02562 (UniProt P10081)
Region: residues 223	to 233
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In these models, the distance from eIF4A residue 223 to residue 233 is  18 –20  Å,  which  can  be  accommodated  readily  by  the  linker polypeptide.
This structure and the intrinsic disorder of the carboxyl-terminal  domain  within  it  suggest  that,  in  solution,eIF4A can be a distended molecule and that the linker between domains  is  relatively  flexible  (although  it  does  not  have  an unusually  high  fraction  of  glycine,  alanine,  or  serine,  which  is characteristic  of  many  flexible  polypeptides).
Cross-references: PDB:1FUU
PDB:1FUK
Protein: DP02562 (UniProt P10081)
Region: residues 223	to 233
Annotation: flexible linker (Disorder function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
In these models, the distance from eIF4A residue 223 to residue 233 is  18 –20  Å,  which  can  be  accommodated  readily  by  the  linker polypeptide.
This structure and the intrinsic disorder of the carboxyl-terminal  domain  within  it  suggest  that,  in  solution,eIF4A can be a distended molecule and that the linker between domains  is  relatively  flexible  (although  it  does  not  have  an unusually  high  fraction  of  glycine,  alanine,  or  serine,  which  is characteristic  of  many  flexible  polypeptides).
Cross-references: PDB:1FUU
PDB:1FUK
Protein: DP02564 (UniProt Q15717)
Region: residues 1	to 19
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The first 19 amino acids form an N-terminal intrinsically disordered region that extends from the canonical RRM fold. The disordered nature of the N-terminal segment is supported by the absence of NOE-derived distances within this region. In addition, chemical shift-based secondary structure propensity analysis revealed no preferential secondary structure propensity
Cross-references: PDB:5SZW
Protein: DP02567 (UniProt P01266)
Region: residues 610	to 620
Annotation: flexible linker (Disorder function)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
In the TG monomer, the globular NTD is connected to the core region via a linker (residues 610–620) that crosses the central dimer interface and is partially flexible
Cross-references: PDB:6SCJ
EMDB:EMD-10141
Protein: DP02567 (UniProt P01266)
Region: residues 610	to 620
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In the TG monomer, the globular NTD is connected to the core region via a linker (residues 610–620) that crosses the central dimer interface and is partially flexible
Protein: DP02567 (UniProt P01266)
Region: residues 1	to 23
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
The PDB shows that this region lacks electron density, indicating that it is disordered.
Cross-references: PDB:6SCJ
EMDB:EMD-10141
Protein: DP02567 (UniProt P01266)
Region: residues 388	to 407
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
The PDB shows that this region lacks electron density, indicating that it is disordered.
Cross-references: PDB:6SCJ
EMDB:EMD-10141
Protein: DP02567 (UniProt P01266)
Region: residues 511	to 546
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
The PDB shows that this region lacks electron density, indicating that it is disordered.
Cross-references: PDB:6SCJ
EMDB:EMD-10141
Protein: DP02567 (UniProt P01266)
Region: residues 830	to 847
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
The PDB shows that this region lacks electron density, indicating that it is disordered.
Cross-references: PDB:6SCJ
EMDB:EMD-10141
Protein: DP02567 (UniProt P01266)
Region: residues 1010	to 1020
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
The PDB shows that this region lacks electron density, indicating that it is disordered.
Cross-references: PDB:6SCJ
EMDB:EMD-10141
Protein: DP02567 (UniProt P01266)
Region: residues 1234	to 1243
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
The PDB shows that this region lacks electron density, indicating that it is disordered.
Cross-references: PDB:6SCJ
EMDB:EMD-10141
Protein: DP02567 (UniProt P01266)
Region: residues 1640	to 1657
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
The PDB shows that this region lacks electron density, indicating that it is disordered.
Cross-references: PDB:6SCJ
EMDB:EMD-10141
Protein: DP02567 (UniProt P01266)
Region: residues 1802	to 1814
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
The PDB shows that this region lacks electron density, indicating that it is disordered.
Cross-references: PDB:6SCJ
EMDB:EMD-10141
Protein: DP02567 (UniProt P01266)
Region: residues 2729	to 2768
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
The PDB shows that this region lacks electron density, indicating that it is disordered.
Cross-references: PDB:6SCJ
EMDB:EMD-10141
Protein: DP02568 (UniProt P04616)
Region: residues 66	to 116
Annotation: disorder (Structural state)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Although full-length Rev is present in the crystals (SDS–PAGE of a crystal showed unaltered Rev mobility, with contaminants at ∼5%) (Fig. S2), only residues 9 to 65—the N-terminal domain (NTD)—were found to be ordered (Fig. 1A).
Cross-references: PDB:2X7L
Protein: DP02568 (UniProt P04616)
Region: residues 34	to 50
Annotation: disorder (Structural state)
Evidence: heteronuclear single quantum coherence spectroscopy evidence used in manual assertion
Supporting statements:
We further characterized the differences in IA and IIB binding modes using amide proton chemical shifts from 15N HSQC NMR spectra to monitor changes in the peptide-RNA interfaces. There is little peak dispersion of peptide resonances in the absence of RNA (Figure 5C), indicative of a largely unstructured molecule.
Protein used in this publication is from Human immunodeficiency virus type 1 group M subtype B (isolate HXB3). IDR has 100% identity to this Uniprot.
Protein: DP02568 (UniProt P04616)
Region: residues 34	to 50
Annotation: disorder to order (Structural transition)
Evidence: heteronuclear single quantum coherence spectroscopy evidence used in manual assertion
Supporting statements:
We further characterized the differences in IA and IIB binding modes using amide proton chemical shifts from 15N HSQC NMR spectra to monitor changes in the peptide-RNA interfaces. There is little peak dispersion of peptide resonances in the absence of RNA (Figure 5C), indicative of a largely unstructured molecule. However, we observe substantial amide peak dispersion in the presence of either IIB (red) or IA (blue) RNAs (Figure 5C), including the Hε protons of arginine side chains (Figure 5C inset). The overall upfield shifts observed in both 1H and 15N dimensions is consistent with stabilization of peptide α-helical structure upon binding (Wang and Jardetzky, 2002).
Protein used in this publication is from Human immunodeficiency virus type 1 group M subtype B (isolate HXB3). IDR has 100% identity to this Uniprot.
Protein: DP02568 (UniProt P04616)
Region: residues 34	to 50
Annotation: order (Structural state)
Evidence: heteronuclear single quantum coherence spectroscopy evidence used in manual assertion
Supporting statements:
The overall upfield shifts observed in both 1H and 15N dimensions is consistent with stabilization of peptide α-helical structure upon binding (Wang and Jardetzky, 2002).
Protein used in this publication is from Human immunodeficiency virus type 1 group M subtype B (isolate HXB3). IDR has 100% identity to this Uniprot.
Protein: DP02568 (UniProt P04616)
Region: residues 34	to 50
Annotation: RNA binding (Molecular function)
Evidence: heteronuclear single quantum coherence spectroscopy evidence used in manual assertion
Supporting statements:
Given, the purine-rich internal loop of IA, we asked if this amino acid also is essential for IA binding. Interestingly, mutation of Asn40 had no effect on IA binding. Conversely, mutation of Arg41, which does not affect IIB binding (Tan et al., 1993), showed a reproducible 2-fold decrease in IA affinity (Figure 5A). R38A and R46A mutants showed similar 2-fold reductions in IA affinity but had no effect on IIB, while R43A, R44A, and W45A mutants bound IA like the wild type peptide. Helical wheel projections clearly show that different surfaces of the helix are used to recognize IIB and IA RNAs (Figure 5B).
Protein used in this publication is from Human immunodeficiency virus type 1 group M subtype B (isolate HXB3). IDR has 100% identity to this Uniprot.
Protein: DP02568 (UniProt P04616)
Region: residues 34	to 50
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
CD spectra of the Rev ARM peptide in physiological buffer exhibited a minimum around 200 nm, typical of an unfolded state (Fig. 1 A).
Protein used in this publication is from Human immunodeficiency virus type 1 group M subtype B (isolate HXB3). IDR has 100% identity to this Uniprot.
Protein: DP02568 (UniProt P04616)
Region: residues 34	to 50
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
To obtain residue-specific information regarding the Rev ARM peptide, we recorded 1HN,15N-HSQC spectra (Fig. 2). In aqueous solution, the peptide shows little dispersion of the resonances (Fig. 2 B), indicative of an unfolded peptide and in accordance with the CD data.
Protein used in this publication is from Human immunodeficiency virus type 1 group M subtype B (isolate HXB3). IDR has 100% identity to this Uniprot.
Protein: DP02568 (UniProt P04616)
Region: residues 34	to 50
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Fig. 5 B shows that the [1HN],15N hetNOE values for Rev ARM in aqueous solution at pH 7.4 average 0.47 for residues T34–R50, consistent with a disordered peptide. In contrast, the hetNOEs of the Rev ARM peptide in complex with RRE StemIIB average 0.83 for residues T34–R50, and in 50% TFE average 0.77 for residues T34–R50. These higher hetNOE values indicate higher backbone rigidity and are typical of a well-ordered secondary structure.
RRE StemIIB it's the RNA binding Rev ARM.
Protein used in this publication is from Human immunodeficiency virus type 1 group M subtype B (isolate HXB3). IDR has 100% identity to this Uniprot.
Protein: DP02568 (UniProt P04616)
Region: residues 34	to 50
Annotation: order (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
In contrast, the hetNOEs of the Rev ARM peptide in complex with RRE StemIIB average 0.83 for residues T34–R50, and in 50% TFE average 0.77 for residues T34–R50. These higher hetNOE values indicate higher backbone rigidity and are typical of a well-ordered secondary structure.
RRE StemIIB it's the RNA binding Rev ARM.
Protein used in this publication is from Human immunodeficiency virus type 1 group M subtype B (isolate HXB3). IDR has 100% identity to this Uniprot.
Protein: DP02568 (UniProt P04616)
Region: residues 34	to 50
Annotation: RNA binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Fig. 5 B shows that the [1HN],15N hetNOE values for Rev ARM in aqueous solution at pH 7.4 average 0.47 for residues T34–R50, consistent with a disordered peptide. In contrast, the hetNOEs of the Rev ARM peptide in complex with RRE StemIIB average 0.83 for residues T34–R50, and in 50% TFE average 0.77 for residues T34–R50. These higher hetNOE values indicate higher backbone rigidity and are typical of a well-ordered secondary structure." Curator statement "RRE StemIIB it's the RNA binding Rev ARM.
RRE StemIIB it's the RNA binding Rev ARM.
Protein used in this publication is from Human immunodeficiency virus type 1 group M subtype B (isolate HXB3). IDR has 100% identity to this Uniprot.
Protein: DP02568 (UniProt P04616)
Region: residues 35	to 50
Annotation: protein export from nucleus (Biological process)
Evidence: green fluorescent protein fusion protein localization evidence used in manual assertion
Supporting statements:
Rev–GFP showed typical predominantly nuclear localization (>80% of fluorescence) (Fig. 2A). In contrast, RevM5–GFP fluorescence was apparent mainly in the cytoplasm, with less than 22% of total fluorescence in the nucleus (Fig. 2A).
RevM5 has a mutation in this IDR.
Protein: DP02568 (UniProt P04616)
Region: residues 76	to 80
Annotation: protein export from nucleus (Biological process)
Evidence: green fluorescent protein fusion protein localization evidence used in manual assertion
Supporting statements:
Analysis of the nuclear translocation activity of NES mutant peptides demonstrated that peptides with PAAAA instead of PPLER were defective in both nuclear import (Fig. 8A) and export (Fig. 9), indicating involvement of this sequence in a bidirectional transport activity of the Rev–NES.
Protein: DP02568 (UniProt P04616)
Region: residues 35	to 46
Annotation: RNA binding (Molecular function)
Evidence: electrophoretic mobility shift assay evidence used in manual assertion
Supporting statements:
As shown in a gel mobility shift assay (Figure 2), the addition of Rev normally leads to formation of multimeric complexes with 35S-labelled RRE.
Protein: DP02568 (UniProt P04616)
Region: residues 35	to 46
Annotation: protein binding (Molecular function)
Evidence: gel electrophoresis evidence used in manual assertion
Supporting statements:
The experiment demonstrates the specificity of the Rev-importin-β interaction, as importin-β did not bind to the GST-Rev NLS mutant, or to GST protein. This was an unexpected finding, and identifies Rev as the first protein known to contain an NLS specific for the 97 kDa importin-β receptor, and not importin-α.