LiteFold/DisProt huggingface dataset:
Protein: DP03739 (UniProt P24588)
Region: residues 300	to 427
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
AKAP5 is an IDP with a well-characterised PxIxIT SLiM that anchors Calcineurin.
The AKAP5c scaffold is highly disordered and monomeric
CD spectroscopy also showed AKAP5c to be predominantly disordered (Fig. 1d): the signature large negative ellipticity at 200 nm was dominant, and although there were indications of some secondary structure (as evidenced by the weak shoulder at 222 nm), this is likely to be transiently populated given the results from NMR.
Protein: DP03739 (UniProt P24588)
Region: residues 404	to 413
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Three distinct sections with pronounced dips in intensity were seen, 361QFLIS365, 390TLLIET395 and 404IQLSIEQLVN413, which we termed secondary sites 1, 2 and 3, respectively. Binding to these sites therefore does not depend on the presence of the PIAIIIT site.
Protein: DP03739 (UniProt P24588)
Region: residues 390	to 395
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Three distinct sections with pronounced dips in intensity were seen, 361QFLIS365, 390TLLIET395 and 404IQLSIEQLVN413, which we termed secondary sites 1, 2 and 3, respectively. Binding to these sites therefore does not depend on the presence of the PIAIIIT site.
Protein: DP03739 (UniProt P24588)
Region: residues 361	to 365
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Three distinct sections with pronounced dips in intensity were seen, 361QFLIS365, 390TLLIET395 and 404IQLSIEQLVN413, which we termed secondary sites 1, 2 and 3, respectively. Binding to these sites therefore does not depend on the presence of the PIAIIIT site.
Protein: DP03739 (UniProt P24588)
Region: residues 371	to 375
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
A small extra region of non-PIAIIIT interaction was apparent in AKAPILVF->SA in the absence of the secondary sites: 371VGVFA375, which contains three bulky hydrophobic residues but no isoleucine, and there were also weaker dips corresponding to regions containing just one or two hydrophobic residues: 378NGFED382, 386EQYET390, 398SLVKN402 and 424NLLQ427 (shown by asterisks in Fig. 5b). We hereon refer to these as ‘mini-SLiMs’ in order to differentiate them from the primary and secondary sites.
Protein: DP03739 (UniProt P24588)
Region: residues 337	to 343
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The Calcineurin anchoring site in AKAP5c is at 337PIAIIIT343, a near-consensus PxIxIT SLiM [19], [20], in which 338I takes the position of the consensus proline.
To investigate the involvement of more distal flanking regions, we titrated Calcineurin into 15N-labelled AKAP5c and followed binding by 15N HSQC (Fig. 2a). Many peaks showed a progressive decrease in intensity. At one molar equivalent, the reductions were significant, including those expected from residues 338IAIIIT343 (shown boxed).
Protein: DP03739 (UniProt P24588)
Region: residues 300	to 425
Annotation: protein binding (Molecular function)
Evidence: surface plasmon resonance evidence used in manual assertion
Supporting statements:
Nevertheless, the trend in apparent Kd is clear: AKAP5c binds Calcineurin about twice as tightly compared to AKAP5cILVF->SA, (Kd ∼0.3 vs 0.6 μM), and both PIAIIIT-containing AKAP constructs bind Calcineurin with at least ten-fold higher affinity than AKAP5cΔPIAIIIT, which has a Kd of ∼ 10 μM. Estimation of the total surface capacity for Calcineurin (Rmax) is also instructive as it gives information on the stoichiometry of binding under saturating conditions. From extrapolation of the binding curves, it appears that AKAP5c can accommodate significantly more Calcineurin than AKAP5cILVF->SA (62 vs 42 RU; Fig. 6d). The secondary sites appear to account for at least some of this ‘extra’ capacity, since Rmax for AKAP5cΔPIAIIIT is (very approximately) 12 RU.
Protein: DP03739 (UniProt P24588)
Region: residues 337	to 343
Annotation: protein binding (Molecular function)
Evidence: isothermal titration calorimetry evidence used in manual assertion
Supporting statements:
Binding was also investigated by isothermal titration calorimetry (ITC). Titration of AKAP5c and AKAP5cILVF->SA into Calcineurin gave clear sigmoidal binding curves (Fig. 6e). Low heats prevented detection of binding to AKAP5cΔPIAIIIT (not shown), presumably due to insufficient binding at the attainable concentrations of free Calcineurin or small ΔH, or both.
Protein: DP03739 (UniProt P24588)
Region: residues 390	to 417
Annotation: calmodulin binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
However, on addition of Calmodulin, while no further changes to PIAIIIT were observed, some non-PIAIIIT peaks in the region 390-417 showed an additional loss in intensity over that induced by Calcineurin (Fig. 3b), and in addition, were observed to shift (Fig. 3c&d), indicative of a faster exchange regime and weaker binding than to Calcineurin. In order to establish whether these changes were Calcineurin-dependent, a further titration was performed in which Ca2+ and Calmodulin were added directly to AKAP5c in the absence of Calcineurin (Fig. 3c&d). A similar pattern of chemical shift changes was seen for 390-417, indicating that they result from direct binding to Calmodulin.
Protein: DP03740 (UniProt Q9C6B8)
Region: residues 289	to 451
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The measured spectra of PIN1 HL–1 (Figure 1C) reached the first minimum at 229 nm, followed by negative maxima at 220 nm. Later, up to 200 nm, the signal was only decreasing. When compared with the control measurement of poly–L–lysine, which at pH seven is completely unstructured (Figure 1B, black line), the spectral curves of PIN1 HL–1 and control do not overlap, indicating that the HL is not completely unstructured. What is more, the PIN1 HL–1 spectrum corresponds neither to the spectra of poly–L–Lys in the α–helical nor in the β-sheet state (Figure 1B, red and blue lines, respectively), pointing out that PIN1 HL–1 cannot be defined as completely structured either. Unfortunately, the CD cannot provide precise structural data, only a gross composition with the share of alpha, beta, and unstructured regions without determining their exact locations. Therefore, we decided to zoom in on particular areas testing shorter fragments also outside the HL–1 to get more complete coverage of the whole PIN1 HL.
Protein: DP03741 (UniProt P03300)
Region: residues 1457	to 1469
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
Negative heteronuclear NOE values are observed for contiguous regions at both the N- and C termini (Figure 3(b)), indicating that these regions are disordered in solution. Consistent with this observation, long range NOE's were observed only for residues 15–45 (Figure 3(c)).
Cross-references: PDB:1NG7
Protein: DP03741 (UniProt P03300)
Region: residues 1501	to 1515
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
Negative heteronuclear NOE values are observed for contiguous regions at both the N- and C termini (Figure 3(b)), indicating that these regions are disordered in solution. Consistent with this observation, long range NOE's were observed only for residues 15–45 (Figure 3(c)).
Cross-references: PDB:1NG7
Protein: DP03742 (UniProt P04584)
Region: residues 111	to 135
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
The 25 C-terminal residues appear to be disordered, based on the absence of significant amide-to-amide (i to i + 1 and i to i − 1) and amide–side-chain NOEs, as well as near-zero residual dipolar couplings (RDCs). 
Cross-references: PDB:2K4E
Protein: DP03743 (UniProt Q96QZ7)
Region: residues 555	to 580
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
Experimental evidence shows that this 25-residue tail tends slowly towards greater disorder in the unliganded domain, as expected for an unstructured polypeptide chain attached to a structured domain.
Cross-references: PDB:2KPL
PDB:2KPK
BMRB:16558 
BMRB:16559
Protein: DP03744 (UniProt Q9VVJ7)
Region: residues 150	to 178
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
Residues 62-70 (including an uncleaved N-terminal hexahistidine tag) and residues 150-178 of Sep15 are not shown because these regions are also flexible.
Cross-references: PDB:2A4H
Protein: DP03744 (UniProt Q9VVJ7)
Region: residues 17	to 61
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
By comparing the 1H,15N HSQC spectra of Sep15 with different construct boundaries, we determined that the N terminus of Sep15 (residues 17-61) was disordered. 
Cross-references: PDB:2A4H
Protein: DP03745 (UniProt Q8VHC3)
Region: residues 25	to 34
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
Residues 25-34 and residues 121-145 (including an uncleaved C-terminal hexahistidine tag) of SelM are not shown because these regions are flexible. 
Cross-references: PDB:2A2P
Protein: DP03745 (UniProt Q8VHC3)
Region: residues 121	to 145
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
Residues 25-34 and residues 121-145 (including an uncleaved C-terminal hexahistidine tag) of SelM are not shown because these regions are flexible. 
Cross-references: PDB:2A2P
Protein: DP03748 (UniProt P75862)
Region: residues 169	to 180
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final model includes ZapC residues 2–168 (residues 169–180 were disordered) and 109 solvent molecules.
Only C-terminal residues 169–180 are disordered in the structure, consistent with the fact that although the ZapC C-terminal region is relatively conserved among enteric bacteria, this region shows significant diversity in both length and sequence among ZapC homologs in other bacteria (Fig. 1D).
Cross-references: PDB:5E1L
Protein: DP03749 (UniProt Q92871)
Region: residues 1	to 11
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Similar to the native PMM1 structure, the first 11 residues of the N-terminus and the last six residues of the C-terminus were disordered; the electron density for the remainder of the protein was clear and ordered.
Cross-references: PDB:6CFV
PDB:6CFS
PDB:6CFT
PDB:6CFR
PDB:6CFU
Protein: DP03751 (UniProt Q9XZT6)
Region: residues 221	to 250
Annotation: deoxynucleoside kinase activity (Molecular function)
Evidence: deletion mutation phenotypic evidence used in manual assertion
Supporting statements:
The C-terminal 20 amino acids were dispensable for phosphorylation of deoxyribonucleosides but necessary for full activity with purine ribonucleosides. Removal of the C-terminal 20 amino acids increased the specific activity 2-fold, but 99% of the activity was lost after removal of the C-terminal 30 amino acids.
In the present paper, we describe a cDNA from D. melanogaster with homology to the cDNA of mammalian TK2, dCK, and dGK but with a unique C-terminal amino acid sequence that appeared to be important for the catalytic activity.
Comparison of the specific activities (Table I) shows that rDm-dNKΔC30 had about 1% of the specific activity of rDm-dNK.
As compared with rDm-dNK, the relative activities of rDm-dNKΔC10 and rDm-dNKΔC20 with deoxyribonucleosides remained largely unchanged, whereas there was a substantial decrease in the phosphorylation of the purine ribonucleosides adenosine and guanosine, as well as of all dideoxyribonucleosides and AZT (Table III). 
The very C-terminal part of the enzyme, the terminal 10 amino acids, harboring a putative phosphorylation and nuclear localization signal, did not influence catalytic efficiency for thymidine but reduced the phosphorylation of purine-dideoxyribo- and ribonucleosides. C-terminal truncation of 20 amino acids changed the thymidine turnover unexpectedly toward higher rates. This suggests that the C-terminal domain of Dm-dNK has an inhibitory effect on phosphorylation of deoxyribonucleosides, although on the other hand promoting phosphorylation of other substrates, such as purine ribo- and dideoxyribonucleosides. The terminal 20 amino acids seemed to be essential for phosphorylation of purine ribonucleosides and dideoxyadenosine. Thus, this deletion reduced the broad substrate specificity (Table III). Deletion of 30 amino acids at the C terminus decreased the activity to about 1% of rDm-dNK, indicating the loss of a domain essential for catalysis.
Protein: DP03755 (UniProt A0A090N8E9)
Region: residues 735	to 751
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
However, the 17 C-terminal residues including most of the post-SET domain were not observed.
Cross-references: PDB:4MI0
Protein: DP03756 (UniProt P36888)
Region: residues 762	to 782
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows this region lacks electron density and is disordered.
Cross-references: PDB:1RJB
Protein: DP03756 (UniProt P36888)
Region: residues 948	to 958
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows this region lacks electron density and is disordered.
Cross-references: PDB:1RJB
Protein: DP03758 (UniProt Q96ST2)
Region: residues 352	to 548
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
(e) 2D 15N/1H HSQC NMR spectra obtained for IWS1352–548. The unstructured character of IWS1352–548 is illustrated by the poor dispersion of amide signals.
The unstructured character of the fragment was verified experimentally using CD spectroscopy, DSF and 1D 1H and 2D 15N/1H HSQC NMR spectra (Fig. 5e, Supplementary Figs 2 and 4c,d).
Protein: DP03758 (UniProt Q96ST2)
Region: residues 352	to 548
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The unstructured character of the fragment was verified experimentally using CD spectroscopy, DSF and 1D 1H and 2D 15N/1H HSQC NMR spectra (Fig. 5e, Supplementary Figs 2 and 4c,d).
Protein: DP03758 (UniProt Q96ST2)
Region: residues 352	to 548
Annotation: protein binding (Molecular function)
Evidence: multiplex bead-based immunoassay evidence used in manual assertion
Supporting statements:
IWS1 interacts exclusively with LEDGF/p75 constructs containing the IBD. Recombinant GST-LEDGF/p75, GST-LEDGF/p75325–530, GST-IBD, GST-PWWP or GST-LEDGF/p52 were titrated against 20 nM His-IWS1 in AlphaScreen.
Protein: DP03758 (UniProt Q96ST2)
Region: residues 352	to 548
Annotation: protein binding (Molecular function)
Evidence: isothermal titration calorimetry evidence used in manual assertion
Supporting statements:
Under optimal conditions (25 mM Tris-HCl, pH 8.5, 150 mM NaCl, 0.05% BME), the IBD-IWS1352–548 complex could readily be isolated using analytical SEC (Supplementary Fig. 4d), and the affinity of the interaction was determined using ITC (Fig. 5f). We calculated a Kd value of 6.7±2.0 μM and a 1:1 binding stoichiometry (N=0.96).
Protein: DP03758 (UniProt Q96ST2)
Region: residues 352	to 548
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
We followed the formation of the IBD-IWS1352–548 complexes via chemical shift perturbations of the IBD backbone signals (1H, 15N, 13C′; Fig. 5g) in the 3D HNCO spectra, analogous to our experiments with JPO21–130 and PogZ1117–1410. The specific changes induced by IWS1352–548 were localized to residues K360–D369, K402–V408, I412 and M413 of the IBD and overlap with those found for JPO2, PogZ and MLL1 (Fig. 5h). Overall, these experiments unambiguously confirm a novel IBM-mediated interaction between IWS1 and the LEDGF/p75 IBD.
Protein: DP03759 (UniProt P25454)
Region: residues 329	to 344
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
This region lacks electron density in PDB, indicating it is disordered.
Cross-references: PDB:1SZP
Protein: DP03759 (UniProt P25454)
Region: residues 1	to 77
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The yeast-specific N-terminal extension (residues 1–79), which is present in our protein but disordered within the crystal, and which was deleted in order to obtain crystals of I345T, likewise does not affect the structure of the DNA-free, nucleotide-free Rad51 filament.
The PDB shows that the disordered region is 1-77.
Protein: DP03759 (UniProt P25454)
Region: residues 328	to 347
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows this region lacks electron density, indicating it is disordered.
Protein: DP03760 (UniProt P26332)
Region: residues 385	to 400
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Outside the structured core, no long range distance restraints were observed for residues from Glu-359 to Ala-374 or from Glu-417 to Ser-433. The heteronuclear NOE values for these residues were less than 0.1 (Fig. 4), indicating that they are disordered in solution.
The authors are not considering the signal peptide, therefore the disordered region they mention corresponds to residues 385-400 and 443-459 of the Uniprot.
Cross-references: PDB:1XU6
Protein: DP03760 (UniProt P26332)
Region: residues 443	to 459
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Outside the structured core, no long range distance restraints were observed for residues from Glu-359 to Ala-374 or from Glu-417 to Ser-433. The heteronuclear NOE values for these residues were less than 0.1 (Fig. 4), indicating that they are disordered in solution.
The authors are not considering the signal peptide, therefore the disordered region they mention corresponds to residues 385-400 and 443-459 of the Uniprot.
Cross-references: PDB:1XU6
Protein: DP03761 (UniProt Q9GU80)
Region: residues 187	to 211
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The CD spectra of peptides 1 and 2 show minima between 195 and 200 nm (Fig. 3), which is characteristic of statistical coils [[28], [29], [30]].
The Protein kinase A regulatory subunit peptides used in this publication were derived from the Trypanosoma brucei brucei (strain 927/4 GUTat10.1) (Uniprot Q385V6) which is 100% identical to this Uniprot.
Protein: DP03761 (UniProt Q9GU80)
Region: residues 198	to 223
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The CD spectra of peptides 1 and 2 show minima between 195 and 200 nm (Fig. 3), which is characteristic of statistical coils [[28], [29], [30]].
The Protein kinase A regulatory subunit peptides used in this publication were derived from the Trypanosoma brucei brucei (strain 927/4 GUTat10.1) (Uniprot Q385V6) which is 100% identical to this Uniprot.
Protein: DP03761 (UniProt Q9GU80)
Region: residues 187	to 211
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The amide 1H region (7.6–9.0 ppm) of the 1H NMR spectra in water at pH 5.1 and 5 °C shows little dispersion (Sup. Fig. 3A), suggesting that this peptide does not adopt a stable secondary structure in these conditions.
 Moreover, taking the 1HN signal of S4 at 8.6 ppm in water as a local reference for peptide 1, the lack of change in the chemical shifts suggests that the presence of the DPC micelles does not alter the chemical environment of peptide 1 (Sup. Fig. 6).
The Protein kinase A regulatory subunit peptides used in this publication were derived from the Trypanosoma brucei brucei (strain 927/4 GUTat10.1) (Uniprot Q385V6) which is 100% identical to this Uniprot.
Cross-references: BMRB:50627
Protein: DP03761 (UniProt Q9GU80)
Region: residues 198	to 223
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Next, we recorded 1D and 2D NMR spectra on peptide 2. The 1D 1H NMR spectrum in aqueous solution at pH 5.0, 5 °C shows little dispersion in the amide 1H region (8.50–8.75 ppm) (Sup. Fig. 3B), suggesting that peptide 2, like peptide 1, does not adopt a stable secondary structure.
The 1D 1H NMR spectrum of peptide 2 recorded in the presence of DPC micelles also reveals poor signal dispersion in the amide region, as shown in Sup. Fig. 5B. Interestingly, the presence of DPC micelles shifts all the 1HN resonances to higher field, including the signals of the glycines. This is shown in Sup. Fig. 8 which uses the 1HN signal of S21 at 8.24 ppm as a local reference. The analysis of the 1Hα, 13Cα and 13Cβ conformational chemical shifts, displayed in Fig. 5B and Table 1, indicates that peptide 2 partially adopts a helical conformation. The helical population is 22% considering the whole peptide and reaches 53% for the segment spanning residues P16 to Y22 (Table 1).
The Protein kinase A regulatory subunit peptides used in this publication were derived from the Trypanosoma brucei brucei (strain 927/4 GUTat10.1) (Uniprot Q385V6) which is 100% identical to this Uniprot.
Cross-references: BMRB:50630
BMRB:50631
Protein: DP03764 (UniProt A4HN55)
Region: residues 1	to 29
Annotation: disorder (Structural state)
Evidence: electron microscopy evidence used in manual assertion
Supporting statements:
The electron microscopy evidence of the proteasome 20S subunit complexed with a imidazo[1,2-a]pyrimidine shows this region lacks electron density, indicating it is disordered.
Cross-references: PDB:6QM7
Protein: DP03765 (UniProt A0A109NYM0)
Region: residues 1	to 10
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In the crystal structure, no electron density was found for the initial ten residues (Met1–Glu10) at the N-terminus, which were omitted from the structure.
Cross-references: PDB:6L6O