LiteFold/DisProt huggingface dataset:
Protein: DP01738 (UniProt P04271)
Region: residues 80	to 91
Annotation: protein binding (Molecular function)
Evidence: proton-based nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
Main interaction site for multiple S100B protein interactors.
Protein: DP01739 (UniProt P9WNR7)
Region: residues 456	to 478
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Authors said " Fifteen residues are missing at the C-terminal of the model due to the flexibility of the protein
sequence making interpretation impossible". I just annotated the region of missing electron density.
Cross-references: PDB:3X3N
Protein: DP01740 (UniProt P68688)
Region: residues 44	to 59
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Authors said about this region "Apparent structural  disorder, indicated by a large dispersion among the 20 conformers"
Cross-references: PDB:1EGO
Protein: DP01741 (UniProt Q6PHW0)
Region: residues 32	to 70
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Missing electron density
Cross-references: PDB:4TTB;PDB:4TTC
Protein: DP01741 (UniProt Q6PHW0)
Region: residues 161	to 178
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Authors said "However, electron density for residues 161–178 and 199–211 was not observed in the absence of bound I-Tyr. This is presumably due to disorder and/or dynamics of these regions. "
Cross-references: PDB:4TTB
Protein: DP01741 (UniProt Q6PHW0)
Region: residues 161	to 178
Annotation: disorder to order (Structural transition)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
About these regions, the authos claimed "However,
these regions were evident from a co-crystal containing I-Tyr. Under these conditions, a helix and loop surrounding the active site are stabilized. The helix in particular covers the active site and helps to sequester the I-TyrFMN complex from solvent"
Protein: DP01741 (UniProt Q6PHW0)
Region: residues 199	to 211
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Authors said "However, electron density for residues 161–178 and 199–211 was not observed in the absence of bound I-Tyr. This is presumably due to disorder and/or dynamics of these regions. "
Cross-references: PDB:4TTB
Protein: DP01741 (UniProt Q6PHW0)
Region: residues 199	to 211
Annotation: disorder to order (Structural transition)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
About these regions, the authos claimed "However,
these regions were evident from a co-crystal containing I-Tyr. Under these conditions, a helix and loop surrounding the active site are stabilized. The helix in particular covers the active site and helps to sequester the I-TyrFMN complex from solvent"
Protein: DP01742 (UniProt Q8NM20)
Region: residues 52	to 89
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The intrinsically flexible nature of the C-terminal segment (52–97) was confirmed by the observation of quite intense peaks in 2D [15N,1H]-HSQC, which reflect long T2-spin relaxation times arising from large scale and rapid motional modes superimposed onto the overall rotational tumbling.

The residues the authors are referring to corresponds to the 52-89 region of this Uniprot.
Cross-references: PDB:2JN6
BMRB:15086
Protein: DP01744 (UniProt Q07528)
Region: residues 1	to 160
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
CD spectra shows this region is disordered.
Protein: DP01744 (UniProt Q07528)
Region: residues 1	to 160
Annotation: disorder (Structural state)
Evidence: proton-based nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
The 1D 1H NMR spectra of Atg20[FR] (Fig. 2B, Right) also exhibits poor dispersion in the amide region, further confirming that the N terminus of Atg20 is disordered.
Protein: DP01744 (UniProt Q07528)
Region: residues 1	to 160
Annotation: protein binding (Molecular function)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
Atg20 was tagged on the N terminus with protein A (PA), and was used for affinity isolation of HA-tagged Atg11. We found that the Atg20 FR was required for efficient binding to Atg11 (Fig. 3A)
Protein: DP01744 (UniProt Q07528)
Region: residues 139	to 145
Annotation: phosphorylation display site (Disorder function)
Evidence: mass spectrometry evidence used in manual assertion
Supporting statements:
 Atg20 is phosphorylated on Ser139, Thr144, Ser145, Ser307, Ser342, Ser343, and Thr517, all of which are previously unreported phosphorylation sites mediated by unknown kinases. In addition to these sites, our MS analysis also detected phosphorylation on Ser45 and Ser49, which are targeted by Cdc28/Cdk1 (31), and on Ser363 and Thr365, sites recognized by casein kinase 2 (CK2) (32), in agreement with previous high-throughput studies.
Protein: DP01744 (UniProt Q07528)
Region: residues 45	to 49
Annotation: phosphorylation display site (Disorder function)
Evidence: mass spectrometry evidence used in manual assertion
Supporting statements:
 Atg20 is phosphorylated on Ser139, Thr144, Ser145, Ser307, Ser342, Ser343, and Thr517, all of which are previously unreported phosphorylation sites mediated by unknown kinases. In addition to these sites, our MS analysis also detected phosphorylation on Ser45 and Ser49, which are targeted by Cdc28/Cdk1 (31), and on Ser363 and Thr365, sites recognized by casein kinase 2 (CK2) (32), in agreement with previous high-throughput studies.
Protein: DP01747 (UniProt P48788)
Region: residues 97	to 182
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The high intensity of the peaks corresponding to the C-terminal region of TnI, relative to the size of the troponin complex and the intensity of peaks from other regions of the protein, suggests that this is a very flexible region which moves independently from the rest of the complex.
Protein: DP01747 (UniProt P48788)
Region: residues 98	to 182
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Although the relaxation data clearly show that this region is flexible, one possibility to explain the presence of the plateau is the presence of some sort of nascent structure. A second possibility is that this profile is an intrinsic property of disordered regions in general. We found that similar results can be recognized in other IDRs attached to globular domains using 15N relaxation data.
Protein: DP01748 (UniProt P05556)
Region: residues 752	to 798
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The spectra  recorded  for  the b1wt peptide showed no distinct minima at 222 nm and a strong minimum at ~200 nm (Fig.8A ), indicating that the b1wt peptide contains little a-helix (~13% by  least-squared regression analysis).
Protein: DP01748 (UniProt P05556)
Region: residues 752	to 798
Annotation: protein binding (Molecular function)
Evidence: surface plasmon resonance evidence used in manual assertion
Supporting statements:
The integrin b1 cytoplasmic tails self-interact in a specific and dose-dependent manner as shown  by surface plasmon resonance analysis.
Protein: DP01748 (UniProt P05556)
Region: residues 784	to 798
Annotation: protein binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
We present cocrystal structures of KRIT1 with ICAP1 and ICAP1 with integrin β1 cytoplasmic tail to 2.54 and 3.0 Å resolution (the resolutions at which I/σI = 2 are 2.75 and 3.0 Å, respectively).
Cross-references: PDB:4DX9
Protein: DP01748 (UniProt P05556)
Region: residues 784	to 798
Annotation: disorder to order (Structural transition)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
We present co-crystal structures of KRIT1 with ICAP1 and ICAP1 with integrin β1 cytoplasmic tail to 2.54 Å and 3.0 Å resolution (the resolutions at which I/σI = 2 are 2.75 Å and 3.0 Å, respectively). 
Cross-references: PDB:4DX9
Protein: DP01748 (UniProt P05556)
Region: residues 752	to 795
Annotation: protein binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Here, we report the first structure of talin bound to an authentic full-length beta integrin tail.
Cross-references: PDB:3G9W
Protein: DP01748 (UniProt P05556)
Region: residues 792	to 796
Annotation: acetylation display site (Disorder function)
Evidence: mass spectrometry evidence used in manual assertion
Supporting statements:
We used high-resolution mass spectrometry to identify3600 lysine acetylation sites on 1750 proteins and quantified acetylation changes in responseto the deacetylase inhibitors suberoylanilide hydroxamic acid and MS-275.
Protein: DP01748 (UniProt P05556)
Region: residues 752	to 798
Annotation: protein binding (Molecular function)
Evidence: bait-prey hybrid interaction evidence used in manual assertion
Supporting statements:
We report here that the Arg kinase domain interacts directly with a lysine-rich membrane-proximal segment in the integrin β1 cytoplasmic tail, that Arg phosphorylates the membrane-proximal Tyr-783 in the β1 tail, and that the Arg Src homology domain then engages this phosphorylated region in the tail.
Protein: DP01748 (UniProt P05556)
Region: residues 786	to 791
Annotation: phosphorylation display site (Disorder function)
Evidence: immunodetection assay evidence used in manual assertion
Supporting statements:
The amounts of integrin β1 and phosphorylated Thr-788/Thr-789 β1 were detected by immunoblotting in cells with or without SDF1-α activation.
Protein: DP01748 (UniProt P05556)
Region: residues 783	to 787
Annotation: phosphorylation display site (Disorder function)
Evidence: mutant phenotype evidence used in manual assertion
Supporting statements:
Preventing Ser-785 or Thr 788/789 phosphorylation reduced adhesion, suggesting that phosphorylation regulates adhesiveness.
Protein: DP01748 (UniProt P05556)
Region: residues 781	to 785
Annotation: phosphorylation display site (Disorder function)
Evidence: immunodetection assay evidence used in manual assertion
Supporting statements:
We report here that the Arg kinase domain interacts directly with a lysine-rich membrane-proximal segment in the integrin β1 cytoplasmic tail, that Arg phosphorylates the membrane-proximal Tyr-783 in the β1 tail, and that the Arg Src homology domain then engages this phosphorylated region in the tail.
Protein: DP01748 (UniProt P05556)
Region: residues 793	to 797
Annotation: phosphorylation display site (Disorder function)
Evidence: mutant phenotype evidence used in manual assertion
Supporting statements:
Focal adhesion kinase (FAK) tyrosine phosphorylation and activation were severely impaired in response to beta1-dependent adhesion in GD25-beta1A(Y783/795F) cells compared to that in wild-type GD25-beta1A or mutants in which only a single tyrosine was altered (beta1A(Y783F) or beta1A(Y795F)).
Protein: DP01748 (UniProt P05556)
Region: residues 752	to 798
Annotation: self-assembly (Disorder function)
Evidence: surface plasmon resonance evidence used in manual assertion
Supporting statements:
The integrin b1 cytoplasmic tails self-interact in a specific and dose-dependent manner as shown by surface plasmon resonance analysis.
Protein: DP01750 (UniProt P62877)
Region: residues 12	to 39
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The structure also shows that residues Gly-12–Val-39 at the N terminus of sRbx112–108 are disordered, as indicated from a lack of inter-residue or long distance NOEs and near zero or negative 15N{1H} heteronuclear NOEs (supplemental Fig. 1).
Taken together, these data suggest that residues Gly-12–Val-39 at the N terminus of sRbx112–108 in the absence of a bound cullin molecule are disordered.
Four residues (W27S, V30S, L32Q, and W33S) were mutated in order to improve the solubility.
Cross-references: PDB:2LGV
Protein: DP01750 (UniProt P62877)
Region: residues 12	to 39
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The structure shows that the N terminus of Rbx1/ROC1 undergoes a large structural rearrangement from a disordered conformation to a structured β-strand in the CRL complex.
Structures of Rbx1/ROC1 in complex with cullin proteins show that the N terminus of Rbx1/ROC1 forms an ordered 16-residue intermolecular β-sheet with the C-terminal domain of the cullin scaffold protein (Fig. 2C; Ref 7).
Combining these results, we suggest that the N terminus of Rbx1/ROC1 undergoes a dramatic disordered-to-ordered conformational transition that is induced by protein-protein interactions with CUL1 (Fig. 2, A and C).
Four residues (W27S, V30S, L32Q, and W33S) were mutated in order to improve the solubility.
Protein: DP01750 (UniProt P62877)
Region: residues 12	to 39
Annotation: disorder to order (Structural transition)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The 16-residue Rbx1 β strand, which contains a kink in the middle, makes β-sheet backbone hydrogen bonds with the S1, S2 and S3 strands of Cul1, and it participates in the formation of the α/β hydrophobic core. The conserved Phe 22 and Trp 27 of Rbx1 have a central role, making multiple van der Waals contacts to side chains from the WH-A, H25, S1, S2 and S3 of Cul1 (Fig. 3b). The Cul1 residues involved in these interactions are highly conserved in Cul1 orthologues and paralogues (Fig. 3b and see Supplementary Information), indicating that other combinations of cullin and Rbx family members will form a similar intermolecular β-sheet. After the Rbx1 β strand, a tryptophan-rich Rbx1 region (Trp 33–Ala 34–Trp 35) packs both with the α/β domain and the following RING domain, resulting in a continuous surface between the two.
Cross-references: PDB:1LDK
PDB:1LDJ
Protein: DP01750 (UniProt P62877)
Region: residues 12	to 39
Annotation: protein binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The 16-residue Rbx1 β strand, which contains a kink in the middle, makes β-sheet backbone hydrogen bonds with the S1, S2 and S3 strands of Cul1, and it participates in the formation of the α/β hydrophobic core. The conserved Phe 22 and Trp 27 of Rbx1 have a central role, making multiple van der Waals contacts to side chains from the WH-A, H25, S1, S2 and S3 of Cul1 (Fig. 3b). The Cul1 residues involved in these interactions are highly conserved in Cul1 orthologues and paralogues (Fig. 3b and see Supplementary Information), indicating that other combinations of cullin and Rbx family members will form a similar intermolecular β-sheet. After the Rbx1 β strand, a tryptophan-rich Rbx1 region (Trp 33–Ala 34–Trp 35) packs both with the α/β domain and the following RING domain, resulting in a continuous surface between the two.
Cross-references: PDB:1LDK
PDB:1LDJ
Protein: DP01750 (UniProt P62877)
Region: residues 12	to 39
Annotation: molecular adaptor activity (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
SCF complexes are the largest family of E3 ubiquitin–protein ligases and mediate the ubiquitination of diverse regulatory and signalling proteins.
Protein: DP01750 (UniProt P62877)
Region: residues 1	to 18
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB structure shows this region lacks electron density, indicating it is disordered.
Cross-references: PDB:1U6G
Protein: DP01751 (UniProt O43172)
Region: residues 1	to 169
Annotation: disorder (Structural state)
Evidence: analytical ultracentrifugation evidence used in manual assertion
Supporting statements:
Additionally, the large values for the frictional ratio are indicative of highly extended shape in solution, as would be expected from intrinsically disordered regions (IDRs), and this may skew the modeling of s-values, leading to larger than expected molecular mass.
Protein: DP01751 (UniProt O43172)
Region: residues 1	to 169
Annotation: molten globule (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
PRPF41–169, PRPF4106–169, and PRPF41–98 spectra have a classically ‘irregular’ shape, as evidenced by negative ellipticity values in the far UV.
When compared with a database containing CD spectra of folded and disordered proteins, PRPF41–169 and PRPF41–98 have ellipticity values at 200 and 222 nm that place them in a region where molten globule proteins cluster (Figure 4) [29,30].
Protein: DP01751 (UniProt O43172)
Region: residues 106	to 169
Annotation: protein binding (Molecular function)
Evidence: isothermal titration calorimetry evidence used in manual assertion
Supporting statements:
We found that PRPF41–169 bound to PPIH with a Kd value of 0.5 µM.
We identified very tight binding between PRPF4106–169 and PPIH. The value of Kd of 0.08 µM is significantly higher affinity than that reported for the PRPF4107–136 peptide, and six times tighter than binding to PRPF41–169 (Figure 2).
Protein: DP01751 (UniProt O43172)
Region: residues 106	to 169
Annotation: protein binding (Molecular function)
Evidence: surface plasmon resonance evidence used in manual assertion
Supporting statements:
PRPF41–169 interacted with PPIH with an affinity of 0.39 ± 0.04 µM, and PRPF4106–169 with an affinity of 0.08 ± 0.01 µM (Figure 3). These values are quite similar to those obtained by ITC (Figure 2). PRPF41–98 bound to PPIH with a modest Kd value of 10.84 ± 1.37 µM (Figure 3).
SPR confirms bipartite binding between PRPF4 and PPIH
Protein: DP01751 (UniProt O43172)
Region: residues 1	to 98
Annotation: protein binding (Molecular function)
Evidence: surface plasmon resonance evidence used in manual assertion
Supporting statements:
PRPF41–169 interacted with PPIH with an affinity of 0.39 ± 0.04 µM, and PRPF4106–169 with an affinity of 0.08 ± 0.01 µM (Figure 3). These values are quite similar to those obtained by ITC (Figure 2). PRPF41–98 bound to PPIH with a modest Kd value of 10.84 ± 1.37 µM (Figure 3).
SPR confirms bipartite binding between PRPF4 and PPIH
Protein: DP01751 (UniProt O43172)
Region: residues 1	to 169
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
15N-1H HSQC spectroscopy exhibited a lack of dispersion along the proton axis, and only a limited number of peaks were visible in the spectra — hallmarks of an unfolded protein or IDR (Supplementary Figure S3).
Protein: DP01751 (UniProt O43172)
Region: residues 106	to 169
Annotation: protein binding (Molecular function)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
When PRPF41–169 F122A was used as an analyte, there was more than a 10-fold reduction in binding affinity to PPIH (15.6 compared with 0.38 µM). The binding of PRPF4106–169 F122A to wild-type PPIH was also weakened, by ~7-fold (0.63 compared with 0.08 µM). These results confirm the contribution of F122 to high-affinity interaction, although it is not enough to disrupt either complex entirely (Figure 7).
These results indicate that the W133A mutation in PPIH is perturbing an interaction with the PRPF41–98 region, and F122A weakens the interaction with the PRPF4106–169 region, but total disruption of the complex is not achieved until both mutations are used.
Protein: DP01751 (UniProt O43172)
Region: residues 107	to 137
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
We recorded circular dichroism (CD) spectra of the U4/U6-60K peptide (10−5 M) at 25 °C and 4 °C in physiological salt solution. Not surprisingly and in contrast to CypH, the peptide largely adopts a random coil conformation (data not shown).
Protein: DP01751 (UniProt O43172)
Region: residues 107	to 137
Annotation: order (Structural state)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The U4/U6-60K protein fragment folds into two α-helices (α1: Val107-Ala113; α2: Pro125-Ile135; numbering is according to the full-length U4/U6-60K protein) connected by an extended loop (Leu114-Gly124; Figure 1(C)).
Therefore, the entropic cost of folding upon interaction with CypH is made up by the binding energy, suggesting that the complex observed herein is strong and specific.
Cross-references: PDB:1MZW
Protein: DP01751 (UniProt O43172)
Region: residues 107	to 137
Annotation: disorder to order (Structural transition)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The U4/U6-60K protein fragment folds into two α-helices (α1: Val107-Ala113; α2: Pro125-Ile135; numbering is according to the full-length U4/U6-60K protein) connected by an extended loop (Leu114-Gly124; Figure 1(C)).
Therefore, the entropic cost of folding upon interaction with CypH is made up by the binding energy, suggesting that the complex observed herein is strong and specific.
Cross-references: PDB:1MZW
Protein: DP01751 (UniProt O43172)
Region: residues 107	to 137
Annotation: protein binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Binding of the U4/U6-60K peptide to a pre-shaped site on CypH
Therefore, the entropic cost of folding upon interaction with CypH is made up by the binding energy, suggesting that the complex observed herein is strong and specific.
Cross-references: PDB:1MZW
Protein: DP01752 (UniProt Q60598)
Region: residues 83	to 324
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The repeat region of cortactin is intrinsically disordered in solution
Using circular dichroism (CD) we find that in solution the cortactin repeats resemble a coil-like intrinsically disordered protein. Small-angle X-ray scattering (SAXS) also indicates that the cortactin repeats are intrinsically unfolded, and the experimentally observed radius of gyration (R g) is coincidental to that calculated by the program Flexible-Meccano for an unfolded peptide of this length.
Circular dichroism suggests a coil-like intrinsically disordered structure for the cortactin repeats
 In contrast, CD spectra of the cortactinCR had a minimum negative signal at 202 nm indicating the presence of mostly random coil, consistent with natively unfolded protein.