LiteFold/DisProt huggingface dataset:
Protein: DP00011 (UniProt P0DMM9)
Region: residues 64	to 77
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The disordered residues cluster into several regions; the N and C termini (residues 1–7 and 294–295) and regions labelled I, II and III in Figure 1 corresponding to residues 64–77, 91–93 and 216–261, respectively.
Cross-references: PDB:1CJM
Protein: DP00011 (UniProt P0DMM9)
Region: residues 64	to 77
Annotation: flexible linker (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
An interesting feature of this structure is the loop region connecting helix α3 and strand β7. This loop is positioned close to the active site, but extends away from the core of the enzyme to interact with the active site region of another monomer of SULT1A3, related by crystallographic symmetry (Figure 3).
Cross-references: PDB:1CJM
Protein: DP00011 (UniProt P0DMM9)
Region: residues 216	to 261
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The disordered residues cluster into several regions; the N and C termini (residues 1–7 and 294–295) and regions labelled I, II and III in Figure 1 corresponding to residues 64–77, 91–93 and 216–261, respectively.
Cross-references: PDB:1CJM
Protein: DP00012 (UniProt P13569)
Region: residues 708	to 831
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Phosphorylated and nonphosphorylated R8 had similar CD spectra in the aqueous buffers (Fig. A), suggesting that phosphorylation did not induce a large structural change in R8.
Protein: DP00012 (UniProt P13569)
Region: residues 708	to 831
Annotation: phosphorylation display site (Disorder function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The data show that R8 (residues 708–831 of CFTR) is functional; it stimulated CFTR-ΔR/S660A channel activity. Surprisingly, R8 is predominantly unstructured, exhibiting a CD spectrum characteristic of random coil, both when phosphorylated and nonphosphorylated.
Protein: DP00012 (UniProt P13569)
Region: residues 654	to 838
Annotation: disorder (Structural state)
Evidence: proton-based nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
NMR 1H-15N correlation spectra for the nonphosphorylated R region and the highly phosphorylated R region (superimposed in Fig. 1b) show sharp peaks, with dispersion for backbone amide proton resonances limited to values between approximately 8 and 8.7 p.p.m. in the proton dimension. This limited dispersion is diagnostic of disorder (in contrast to a dispersion of ~7 to 10 p.p.m. for folded proteins) and reflects the rapid interconversion between heterogeneous conformations in disordered proteins, in which all nuclei experience similar average chemical environments
Cross-references: BMRB:15340
BMRB:15336
Protein: DP00012 (UniProt P13569)
Region: residues 654	to 838
Annotation: phosphorylation display site (Disorder function)
Evidence: proton-based nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
The R region is disordered independent of phosphorylation.
Protein: DP00012 (UniProt P13569)
Region: residues 708	to 831
Annotation: disorder (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
The tryptic patterns of phosphorylated and nonphosphorylated R8 (Fig. A) show that most of the protein is susceptible to trypsin.
Protein: DP00012 (UniProt P13569)
Region: residues 789	to 819
Annotation: 14-3-3 protein binding (Molecular function)
Evidence: fluorescence polarization evidence used in manual assertion
Supporting statements:
However, peptides not containing the pS768 binding motif also showed a stronger affinity for 14-3-3β than the singly phosphorylated peptides, especially CFTR_R8, which features pS795 and pS813.
LIG_14-3-3_CanoR_1 corresponds to the SLIM reported for the  792-797 region
Cross-references: ELM:LIG_14-3-3_CanoR_1
Protein: DP00012 (UniProt P13569)
Region: residues 762	to 801
Annotation: 14-3-3 protein binding (Molecular function)
Evidence: fluorescence polarization evidence used in manual assertion
Supporting statements:
The results showed that in all cases 14-3-3γ binds the strongest, followed by η, β, ζ, ε, τ, and σ, respectively (Fig. S1A). The results from this experiment also showed that CFTR_R7 and CFTR_R6 exhibit the strongest binding to all seven 14-3-3 isoforms.
The strongest binder in this assay was CFTR_R7, which features the pS768 and pS795 epitopes, followed by CFTR_R6, featuring pS753 and pS768.
LIG_14-3-3_CanoR_1 corresponds to the SLIM reported for the  766-770 region
Cross-references: ELM:LIG_14-3-3_CanoR_1
Protein: DP00012 (UniProt P13569)
Region: residues 747	to 774
Annotation: 14-3-3 protein binding (Molecular function)
Evidence: fluorescence polarization evidence used in manual assertion
Supporting statements:
The results showed that in all cases 14-3-3γ binds the strongest, followed by η, β, ζ, ε, τ, and σ, respectively (Fig. S1A). The results from this experiment also showed that CFTR_R7 and CFTR_R6 exhibit the strongest binding to all seven 14-3-3 isoforms.
LIG_14-3-3_CanoR_1 corresponds to the SLIM reported for the  751-755 region and 766-770 region.
Cross-references: ELM:LIG_14-3-3_CanoR_1
Protein: DP00012 (UniProt P13569)
Region: residues 747	to 774
Annotation: 14-3-3 protein binding (Molecular function)
Evidence: isothermal titration calorimetry evidence used in manual assertion
Supporting statements:
The binding affinities of CFTR_R6, CFTR_R7, and CFTR_R8 for 14-3-3β were 75.8, 24.0, and 370 µM, respectively (Fig. 2 C–E and Fig. S2 A–C).
LIG_14-3-3_CanoR_1 corresponds to the SLIM reported for the  751-755 region and 766-770 region.
Cross-references: ELM: LIG_14-3-3_CanoR_1
Protein: DP00012 (UniProt P13569)
Region: residues 762	to 801
Annotation: 14-3-3 protein binding (Molecular function)
Evidence: isothermal titration calorimetry evidence used in manual assertion
Supporting statements:
The binding affinities of CFTR_R6, CFTR_R7, and CFTR_R8 for 14-3-3β were 75.8, 24.0, and 370 µM, respectively (Fig. 2 C–E and Fig. S2 A–C).
LIG_14-3-3_CanoR_1 corresponds to the SLIM reported for the  766-770 region and 792-797 region.
Cross-references: ELM: LIG_14-3-3_CanoR_1
Protein: DP00012 (UniProt P13569)
Region: residues 789	to 819
Annotation: 14-3-3 protein binding (Molecular function)
Evidence: isothermal titration calorimetry evidence used in manual assertion
Supporting statements:
The binding affinities of CFTR_R6, CFTR_R7, and CFTR_R8 for 14-3-3β were 75.8, 24.0, and 370 µM, respectively (Fig. 2 C–E and Fig. S2 A–C).
LIG_14-3-3_CanoR_1 corresponds to the SLIM reported for the  792-797 region
Cross-references: ELM: LIG_14-3-3_CanoR_1
Protein: DP00012 (UniProt P13569)
Region: residues 766	to 770
Annotation: 14-3-3 protein binding (Molecular function)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
Although the coexpression with PKA resulted in only a partially phosphorylated R domain (a variation of three to nine phosphoryl groups was attached to the R domain; Dataset S1, W-AA), eliminating the serine at position 768 shows a significant decrease in binding affinity to 14-3-3β (56.5–125.9 µM) whereas the other positions (700 and 753) resulted in a smaller decrease (59.9 and 92.6 µM, respectively) (Fig. S3 D–H).
Protein: DP00012 (UniProt P13569)
Region: residues 766	to 770
Annotation: 14-3-3 protein binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Here, interpretable density was found for 11 of the 40 amino acid residues present in the CFTR_R7 peptide (R766–L770 and K793–P798) (Fig. S5B). The structure of 14-3-3γ–CFTR_R7 shows that, as for the CFTR_R6 structure, both phosphorylated binding motifs are simultaneously bound to the 14-3-3 dimer: pS768 is located in the binding groove of 14-3-3 protomer A, and pS795 is located in protomer B (Fig. S5A).
LIG_14-3-3_CanoR_1 corresponds to the SLIM reported for the 766-770 region.
Cross-references: PDB:5D3E
ELM:LIG_14-3-3_CanoR_1
Protein: DP00012 (UniProt P13569)
Region: residues 751	to 758
Annotation: 14-3-3 protein binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Interpretable density for 19 out of 28 amino acids of the CFTR_R6 peptide (R751–G758 and R764–T774) was found (Fig. 3 A and B). The protein structure shows that both phosphorylated binding motifs of the peptide are simultaneously bound to one 14-3-3 dimer.
 LIG_14-3-3_CanoR_1 corresponds to the SLIM reported for the  751-755 region.
Cross-references: PDB:5D2D
ELM:LIG_14-3-3_CanoR_1
Protein: DP00012 (UniProt P13569)
Region: residues 698	to 702
Annotation: 14-3-3 protein binding (Molecular function)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
Although the coexpression with PKA resulted in only a partially phosphorylated R domain (a variation of three to nine phosphoryl groups was attached to the R domain; Dataset S1, W-AA), eliminating the serine at position 768 shows a significant decrease in binding affinity to 14-3-3β (56.5–125.9 µM) whereas the other positions (700 and 753) resulted in a smaller decrease (59.9 and 92.6 µM, respectively) (Fig. S3 D–H).
Protein: DP00012 (UniProt P13569)
Region: residues 751	to 755
Annotation: 14-3-3 protein binding (Molecular function)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
Although the coexpression with PKA resulted in only a partially phosphorylated R domain (a variation of three to nine phosphoryl groups was attached to the R domain; Dataset S1, W-AA), eliminating the serine at position 768 shows a significant decrease in binding affinity to 14-3-3β (56.5–125.9 µM) whereas the other positions (700 and 753) resulted in a smaller decrease (59.9 and 92.6 µM, respectively) (Fig. S3 D–H).
Protein: DP00012 (UniProt P13569)
Region: residues 764	to 774
Annotation: 14-3-3 protein binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Interpretable density for 19 out of 28 amino acids of the CFTR_R6 peptide (R751–G758 and R764–T774) was found (Fig. 3 A and B). The protein structure shows that both phosphorylated binding motifs of the peptide are simultaneously bound to one 14-3-3 dimer.
LIG_14-3-3_CanoR_1 corresponds to the SLIM reported for the 766-770 region.
Cross-references: ELM:LIG_14-3-3_CanoR_1
PDB:5D2D
Protein: DP00012 (UniProt P13569)
Region: residues 793	to 798
Annotation: 14-3-3 protein binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Here, interpretable density was found for 11 of the 40 amino acid residues present in the CFTR_R7 peptide (R766–L770 and K793–P798) (Fig. S5B). The structure of 14-3-3γ–CFTR_R7 shows that, as for the CFTR_R6 structure, both phosphorylated binding motifs are simultaneously bound to the 14-3-3 dimer: pS768 is located in the binding groove of 14-3-3 protomer A, and pS795 is located in protomer B (Fig. S5A).
LIG_14-3-3_CanoR_1 corresponds to the SLIM reported for the 792-797 region.
Cross-references: ELM:LIG_14-3-3_CanoR_1
PDB:5D3E
Protein: DP00013 (UniProt P0DN86)
Region: residues 132	to 165
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final electron density map allows a tracing of the α-subunit from residues 5 to 89 and the β-subunit from 2 to 111. The residue β111 is open to a large 50 A diameter solvent channel and it is assumed that the remaining 34 C-terminal residues adopt a random conformation and are therefore not visible in the map.
The IDR characterized in the publication and spanning the C-terminal residues corresponds to region 132-165 of the amino acid sequence, since the natural precursor form of the protein contains a signal peptide (1-20) that is cleaved in the mature secreted protein.
Cross-references: PDB:1HRP
Protein: DP00013 (UniProt P0DN86)
Region: residues 132	to 165
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The carboxy-terminal peptide of the beta-subunit, which is rich in O-linked sugars, is disordered.
The carboxyl terminus of the β-subunit projects into a solvent expanse and there is no defined electron density for the last 34 residues.
Cross-references: PDB:1HCN
Protein: DP00013 (UniProt P0DN86)
Region: residues 133	to 165
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In this model, part of the β-subunit (112B–145B) is not visible in the electron density map, as is the case with most of the N-linked sugar residues.
The IDR characterized in the publication and spanning the C-terminal residues corresponds to region 133-165 of the amino acid sequence, since the natural precursor form of the protein contains a signal peptide (1-20) that is cleaved in the mature secreted protein.
Cross-references: PDB:1QFW
Protein: DP00013 (UniProt P0DN86)
Region: residues 143	to 165
Annotation: glycosylation display site (Disorder function)
Evidence: mass spectrometry evidence used in manual assertion
Supporting statements:
The N52 and N78 from the α-subunit and N13 and N30 from the β-subunit are N-glycosylated, whereas S121, S127, S132, and S138 from the β-subunit are attached with O-glycans [31–33, 39].
All four previously-reported O-glycosylation sites, S121, S127, S132, and S138, are within this peptide sequence.
Only S127, S132, and S138 within this peptide sequence are known O-glycosylation sites, suggesting there is at least one novel O-glycosylation site present in this peptide.
The mentioned glycosylation sites correspond to Ser141, Ser147, Ser152, Ser158.
Protein: DP00015 (UniProt P61926)
Region: residues 1	to 76
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
There is a deep minimum in this spectrum near 200 nm characteristic of a protein with a large proportion of random coil structure (29).
This result is in good agreement with the FTIR spectra. Thus both CD and FTIR support the conclusion that PKI contains a large proportion of random coil structure. The combined percentages of random coil and turn structures indicated by CD for this protein are unusually large.
Protein: DP00015 (UniProt P61926)
Region: residues 1	to 76
Annotation: disorder (Structural state)
Evidence: Fourier-transform infrared spectroscopy evidence used in manual assertion
Supporting statements:
In the amide I' region the PKI spectrum shows a single broad peak whose maximum occurs at 1645 cm-1, the characteristic frequency assigned to random coil structure, indicating that this might be the dominant secondary structure in the protein.
However, it is clear from the maximum in the spectrum at 1645 cm-1 that a significant portion of the structure of PKI is likely to be random coil in nature. One possible caveat to the interpretation of the FTIR data is that distorted helix structures have been observed to give rise to peaks as low as 1645 cm-1
This result is in good agreement with the FTIR spectra. Thus both CD and FTIR support the conclusion that PKI contains a large proportion of random coil structure. The combined percentages of random coil and turn structures indicated by CD for this protein are unusually large.
Protein: DP00015 (UniProt P61926)
Region: residues 1	to 76
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
PKIα is an intrinsically disordered protein with transient secondary and short-lived tertiary interactions
Far-UV circular dichroism (CD) spectrum of PKIα acquired at 25°C in native condition showing the typical CD profile for IDPs, with a minimum around 208 nm
Altogether, the CD and NMR data reveal that in absence of a binding partner PKIα samples transient secondary structures encompassing the HAR and NES motifs with short-lived tertiary conformations.
Protein: DP00015 (UniProt P61926)
Region: residues 1	to 76
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
PKIα is an intrinsically disordered protein with transient secondary and short-lived tertiary interactions
[1H,15N]-Heteronuclear single quantum correlation (HSQC) spectrum of PKIα free form with resonance assignment. The protein fingerprint features a poor resonance dispersion clustered around eight ppm in the 1H dimension, typical of intrinsically disordered proteins
Altogether, the CD and NMR data reveal that in absence of a binding partner PKIα samples transient secondary structures encompassing the HAR and NES motifs with short-lived tertiary conformations.
Cross-references: BMRB:50238
Protein: DP00015 (UniProt P61926)
Region: residues 1	to 76
Annotation: disorder (Structural state)
Evidence: small-angle X-ray scattering evidence used in manual assertion
Supporting statements:
These profiles show the typical signatures of intrinsically disordered proteins, with the Kratky plot featuring a plateau at high q values as well as the absence of a bell-shaped curve (Figure 7C, bottom panel). In addition, the P(r) curve shows that PKIα adopts a highly extended conformational ensemble, with an abnormally large Dmax (~110 Å) and Rg (~30 Å) values for a protein of its size, both parameters are indicative of an extended, intrinsically disordered protein (Kikhney and Svergun, 2015; Figure 8D). In fact, the back-calculated SAXS profiles from the RAM-generated ensembles are in excellent agreement with the experimental SAXS scattering profiles (χ = 0.86 for q < 0.2) (Figure 7C). In the bound state, the HAR motif of PKIα is more ordered and adopts a more stable helical conformation; whereas the NES motif is considerably more dynamic and adopts a transient helical conformation (Figure 7E).
Protein: DP00015 (UniProt P61926)
Region: residues 1	to 14
Annotation: pre-molten globule to molten globule (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
PKA-C recognizes and binds extended PKIα conformations, rigidifying the PSS region and increasing the helicity of the HAR and NES motifs.
Chemical shift index (CSI) for Cα and Cβ of free (red) and bound (blue) PKIα. The PSS motif becomes more rigid upon interaction with PKA-C. The HAR and the NES adopt a transient α-helical conformation, which is enhanced upon binding the kinase.
However, the HAR and PSS resonances display significant chemical shift changes (Figure 3A,B,E), suggesting that these regions of PKI undergo drastic structural rearrangements upon binding the kinase.
high affinity region (HAR, residues 1–14) of PKIα.
Protein: DP00015 (UniProt P61926)
Region: residues 15	to 24
Annotation: disorder to molten globule (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
PKA-C recognizes and binds extended PKIα conformations, rigidifying the PSS region and increasing the helicity of the HAR and NES motifs.
Chemical shift index (CSI) for Cα and Cβ of free (red) and bound (blue) PKIα. The PSS motif becomes more rigid upon interaction with PKA-C. The HAR and the NES adopt a transient α-helical conformation, which is enhanced upon binding the kinase.
However, the HAR and PSS resonances display significant chemical shift changes (Figure 3A,B,E), suggesting that these regions of PKI undergo drastic structural rearrangements upon binding the kinase.
pseudo-substrate recognition sequence (PSS, residues 15–24) of PKIα.
Protein: DP00015 (UniProt P61926)
Region: residues 38	to 47
Annotation: pre-molten globule to molten globule (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
PKA-C recognizes and binds extended PKIα conformations, rigidifying the PSS region and increasing the helicity of the HAR and NES motifs.
Chemical shift index (CSI) for Cα and Cβ of free (red) and bound (blue) PKIα. The PSS motif becomes more rigid upon interaction with PKA-C. The HAR and the NES adopt a transient α-helical conformation, which is enhanced upon binding the kinase.
nuclear export signal (NES, residues 38–47) of PKIα.
Protein: DP00015 (UniProt P61926)
Region: residues 48	to 75
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Although the C-terminal tail of PKIα interacts transiently with the kinase’s C-lobe, it remains essentially disordered facilitating the recruitment by the CRM1/RanGTP complex for nuclear export.
The C-terminal tail of PKIα interacts transiently with PKA-C.
The formation of the PKA-C/ATPγN/PKIα (ternary) complex is also reflected by the differences of longitudinal and transverse relaxation rates (ΔR1 and ΔR2) for both the HAR and PSS motifs upon forming the complex, which define a local rigidification of the PKIα backbone upon binding PKA-C, with the C-terminal portion (residues 47–75) remaining essentially unstructured (Figure 4B,C).
Region corresponding to the C-terminal tail of PKIα.
Cross-references: BMRB:50243
Protein: DP00015 (UniProt P61926)
Region: residues 48	to 75
Annotation: molecular adaptor activity (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Although the C-terminal tail of PKIα interacts transiently with the kinase’s C-lobe, it remains essentially disordered facilitating the recruitment by the CRM1/RanGTP complex for nuclear export.
The formation of the PKA-C/ATPγN/PKIα (ternary) complex is also reflected by the differences of longitudinal and transverse relaxation rates (ΔR1 and ΔR2) for both the HAR and PSS motifs upon forming the complex, which define a local rigidification of the PKIα backbone upon binding PKA-C, with the C-terminal portion (residues 47–75) remaining essentially unstructured (Figure 4B,C).
Region corresponding to the C-terminal tail of PKIα.
Protein: DP00015 (UniProt P61926)
Region: residues 1	to 14
Annotation: molecular adaptor activity (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Although the C-terminal tail of PKIα interacts transiently with the kinase’s C-lobe, it remains essentially disordered facilitating the recruitment by the CRM1/RanGTP complex for nuclear export.
The formation of the PKA-C/ATPγN/PKIα (ternary) complex is also reflected by the differences of longitudinal and transverse relaxation rates (ΔR1 and ΔR2) for both the HAR and PSS motifs upon forming the complex, which define a local rigidification of the PKIα backbone upon binding PKA-C, with the C-terminal portion (residues 47–75) remaining essentially unstructured (Figure 4B,C).
Region corresponding to the HAR motif of PKIα.