LiteFold/DisProt huggingface dataset:
Protein: DP01668 (UniProt P12081)
Region: residues 1	to 52
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Well-defined electron density is present for most parts of the protein in all four chains of Hs-cHisRS except the N-terminal WHEP domains (52 residues). In addition, in all four chains, five residues at the C-termini, and between eight to twelve residues in two internal loops (Pro344 to Gly355; Glu401 to Glu402), are disordered. These loops are not directly involved in histidine or ATP binding.
Cross-references: PDB:4PHC
Protein: DP01669 (UniProt Q26680)
Region: residues 1	to 25
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The first 26 residues from the N-terminus exhibited random-coil amide chemical shifts with non-uniform intensities, indicating that the N-terminal region is indeed solvent-exposed and dynamically disordered. 

Cross-references: PDB:2LVV
Protein: DP01669 (UniProt Q26680)
Region: residues 206	to 218
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
C-terminal residues (206–218) also have chemical shifts consistent with a random coil.
Cross-references: PDB:2LVV
Protein: DP01670 (UniProt Q9I1X7)
Region: residues 1	to 31
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Inspection of the final NMR ensemble of 15 structures (see Table 1 for statistics) reveals a disordered N-terminus (1–31). This fact is also borne out by the extremely low 15N-{1H} NOE values (0.08 ± 0.21; see Figure 1) for this region. However, some degree of local ordering is seen encompassing residues Asp15–Thr19 (15N-{1H} NOE: 0.18 ± 0.01).
Cross-references: PDB:2LJ6
Protein: DP01671 (UniProt P71590)
Region: residues 1	to 32
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The N-terminal part of the protein from Met1 to Val32 is disordered and represented in gray.
Consistent with the absence of long-range NOEs, the 32 first residues adopt a random-coil conformation, with the exception of residues Ala22 to Phe27 that form a short dynamic helix, essentially defined by TALOS restraints.
Cross-references: PDB:2LC0
BMRB:17585
Protein: DP01671 (UniProt P71590)
Region: residues 133	to 429
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The others residues, corresponding to the 133–429 PG-rich peptidic segment, gave rise to the intense cross-peaks centered at 8.5 ppm in the proton dimension of the [1H,15N] HSQC spectrum of the full-length protein, thus strongly suggesting that this segment adopts a random-coil conformation.
Protein: DP01675 (UniProt O75928)
Region: residues 466	to 479
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
 Consistent with the previous finding (22), the SSS sequence of PIASX-P and all residues C-terminal to the SSS sequence do not show inter-residue NOEs. The resonances of these residues are very narrow and identical to those of the unbound peptide. The sharp resonances indicate that these residues are highly flexible, and their motions are not restricted by forming the peptide-SUMO complex.
Cross-references: PDB:2ASQ
Protein: DP01675 (UniProt O75928)
Region: residues 466	to 474
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The residues from the PIASX-P peptide that contact SUMO-1 include Val-2, Asp-3, Val-4, Ile-5, Leu-7, and Thr-8. Except for residue Asp-3, all of these residues have much broader NMR resonances in the complex than in the unbound peptide, indicating that complex formation has significantly restricted their motions.
Cross-references: PDB:2ASQ
Protein: DP01676 (UniProt O14686)
Region: residues 4210	to 4280
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
MLL4 4210–4280 has a more pronounced disorder tendency, as demonstrated by the IUPred profile and is devoid of any predicted ANCHOR binding sites (Figure 1E). Its sequence contains a significant portion of glutamines (Figure 1D), but it does not contain Q stretches longer than 4 residues. Far-UV CD measurements confirmed the disorder predictions,
Protein: DP01677 (UniProt P06454)
Region: residues 1	to 111
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
As shown in Figure 6A, the 1H NMR spectrum of prothymosin at pH 8.0 was characteristic of a highly denatured protein. The resonances were sharp (indicating a high degree of rapid local segmental motion), the amide proton resonances were weak in intensity (indicating little regular hydrogen bonding due to hydrogen exchange with bulk solvent), and the spectrum was poorly dispersed.
Protein: DP01677 (UniProt P06454)
Region: residues 1	to 111
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
As shown in Figure 6A, the 1H NMR spectrum of prothymosin at pH 8.0 was characteristic of a highly denatured protein. The resonances were sharp (indicating a high degree of rapid local segmental motion), the amide proton resonances were weak in intensity (indicating little regular hydrogen bonding due to hydrogen exchange with bulk solvent), and the spectrum was poorly dispersed. At pH 2.4 (Figure 6B), prothymosin still gave a spectrum characteristic of a denatured protein, although significant differences were observed as compared to pH 8.5. These differences included changes in the chemical shifts of some carbon-attached protons (which, being nonexchangeable, should not be dependent on the pH of the bulk solvent) and an increase in the line widths of some aliphatic resonances. These observations strongly suggest that a structural change had occurred, with the polypeptide becoming more compact and ordered.
Protein: DP01677 (UniProt P06454)
Region: residues 1	to 111
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
 1H,15N heteronuclear single quantum coherence (HSQC) spectra of the individual proteins exhibit low dispersion of the 1H chemical shifts, as expected for IDPs14,21-23 (Fig. 1e,f).
Protein: DP01677 (UniProt P06454)
Region: residues 1	to 111
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
ProTα acts as a linker histone chaperone by interacting with H1 and increasing its mobility in the nucleus. Here we show that ProTα and H1 bind to one another with very high affinity, but that both proteins fully retain their structural disorder.
Protein: DP01677 (UniProt P06454)
Region: residues 15	to 110
Annotation: calcium ion binding (Molecular function)
Evidence: small molecule detection assay evidence used in manual assertion
Supporting statements:
We found ProTα to interact with calcium at micromolar affinity (~70 μM; Figure 1H).
This is reflected in its affinity for calcium and a greater number of calcium binding sites, with ProTα interacting with ~10 calcium ions (Figure 1I), the same stoichiometry as was previously reported [44].
Given the high number, extensive spreading and overlapping ion binding regions in ProTα, the entire sequence could be annotated. Despite this fact, it is observable in figure 2 that the first 15 residues of the N-terminus do not follow chemical shift upon calcium binding. Therefore, they are excluded.
Protein: DP01677 (UniProt P06454)
Region: residues 15	to 110
Annotation: calcium ion binding (Molecular function)
Evidence: heteronuclear single quantum coherence spectroscopy evidence used in manual assertion
Supporting statements:
The NMR peaks from the highly acidic stretch overlap and addition of calcium led to large changes in chemical shifts, meaning that we could not follow all individual peaks and quantify their CSPs (regions indicated by red in Figure 1E).
Given the high number, extensive spreading and overlapping ion binding regions in ProTα, the entire sequence could be annotated. Despite this fact, it is observable in figure 2 that the first 15 residues of the N-terminus do not follow chemical shift upon calcium binding. Therefore, they are excluded.
Protein: DP01677 (UniProt P06454)
Region: residues 1	to 111
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The inset to Figure 2 shows that at pH 7.5 ProTα is characterized by a far-UV CD spectrum, which is typical of unfolded proteins, but at pH 2.5 a considerable rearrangement of the spectrum is observed.
Protein: DP01677 (UniProt P06454)
Region: residues 1	to 111
Annotation: disorder to order (Structural transition)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The inset to Figure 2 shows that at pH 7.5 ProTα is characterized by a far-UV CD spectrum, which is typical of unfolded proteins, but at pH 2.5 a considerable rearrangement of the spectrum is observed.
Such far-UV CD spectral changes can be explained by the appearance of some α-helix in the protein at low pH ( 45, 46)
Protein: DP01677 (UniProt P06454)
Region: residues 1	to 111
Annotation: disorder to order (Structural transition)
Evidence: fluorescence anisotropy evidence used in manual assertion
Supporting statements:
 The inset to Figure 3 shows that in the case of ProTα a decrease in pH leads to considerable changes in ANS fluorescence (compare curves 1 and 2), reflecting the pH-induced transformation to the partially folded compact conformation. The formation of this intermediate is reflected in the pH dependence of the ANS fluorescence intensity (see Figure 3). The pH dependence of free ANS is also presented for comparison. It follows from Figure 3 that the transition from unfolded to partially folded conformation takes place between pH 5.5 and pH 3.5
Protein: DP01677 (UniProt P06454)
Region: residues 1	to 111
Annotation: disorder (Structural state)
Evidence: fluorescence anisotropy evidence used in manual assertion
Supporting statements:
 The inset to Figure 3 shows that in the case of ProTα a decrease in pH leads to considerable changes in ANS fluorescence (compare curves 1 and 2), reflecting the pH-induced transformation to the partially folded compact conformation. The formation of this intermediate is reflected in the pH dependence of the ANS fluorescence intensity (see Figure 3). The pH dependence of free ANS is also presented for comparison. It follows from Figure 3 that the transition from unfolded to partially folded conformation takes place between pH 5.5 and pH 3.5
Protein: DP01677 (UniProt P06454)
Region: residues 1	to 111
Annotation: disorder (Structural state)
Evidence: gel-filtration evidence used in manual assertion
Supporting statements:
The results of chromatographic analysis are presented in Table 2. It is evident that the hydrodynamic dimensions of ProTα at neutral pH are close to those measured in the presence of 8 M urea. The small difference between the two values is due to swelling of the unfolded polypeptide chain in a good solvent ( 20). Both values are virtually indistinguishable from RS, calculated for the completely unfolded protein with a molecular mass of 12.21 kDa.
Protein: DP01677 (UniProt P06454)
Region: residues 1	to 111
Annotation: disorder to order (Structural transition)
Evidence: gel-filtration evidence used in manual assertion
Supporting statements:
The results of chromatographic analysis are presented in Table 2. It is evident that the hydrodynamic dimensions of ProTα at neutral pH are close to those measured in the presence of 8 M urea. The small difference between the two values is due to swelling of the unfolded polypeptide chain in a good solvent ( 20). Both values are virtually indistinguishable from RS, calculated for the completely unfolded protein with a molecular mass of 12.21 kDa.
Table 2 shows that a decrease in pH leads to a pronounced decrease of the ProTα hydrodynamic dimension. It should be emphasized that the RS value determined for ProTα at pH 2.5 is still far from that expected for a globular protein of 12 kDa.
Protein: DP01677 (UniProt P06454)
Region: residues 1	to 111
Annotation: disorder to order (Structural transition)
Evidence: small-angle X-ray scattering evidence used in manual assertion
Supporting statements:
The profile of the Kratky plot at neutral pH is typical for a random coil conformation, whereas at pH 2.5 considerable change in the shape of the scattering curves is detected, reflecting the presence of more ordered conformation under such conditions.
Protein: DP01677 (UniProt P06454)
Region: residues 1	to 111
Annotation: disorder (Structural state)
Evidence: small-angle X-ray scattering evidence used in manual assertion
Supporting statements:
The profile of the Kratky plot at neutral pH is typical for a random coil conformation, whereas at pH 2.5 considerable change in the shape of the scattering curves is detected, reflecting the presence of more ordered conformation under such conditions.
Protein: DP01677 (UniProt P06454)
Region: residues 1	to 111
Annotation: disorder (Structural state)
Evidence: urea-induced protein unfolding evidence used in manual assertion
Supporting statements:
Figure 7 shows that the denaturant-induced unfolding of the ProTα acid state represents a very broad transition characterized by the absence of the sigmoid shape, typical of the unfolding of native and molten globule conformations ( 50, 51).
Protein: DP01677 (UniProt P06454)
Region: residues 1	to 111
Annotation: molten globule (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The CD spectra of unbound ProTα and H1 reflect the low secondary structure content of the individual IDPs, except for the small helix-turn-helix domain of H113,19,20 (Fig. 1c).
Protein: DP01677 (UniProt P06454)
Region: residues 1	to 111
Annotation: histone binding (Molecular function)
Evidence: fluorescence resonance energy transfer evidence used in manual assertion
Supporting statements:
The dominant contribution to the interaction with ProTα stems from the unstructured C-terminal part of H1, which alone binds with picomolar affinity. The N-terminal half and the isolated globular domain of H1 also bind ProTα, but with much lower affinity (Fig. 2b). At least four isolated globular domains can bind to ProTα at the same time, with modest chemical shift changes (Extended Data Fig. 1), suggesting the absence of a specific binding interface.
Protein: DP01700 (UniProt P02549)
Region: residues 1	to 20
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
We have determined the solution NMR structure of a recombinant peptide that consists of the first 156 residues of erythroid α-spectrin. The first 20 residues preceding the first helix (helix C′) are in a disordered conformation.
Cross-references: PDB:1OWA
Protein: DP01704 (UniProt P62318)
Region: residues 82	to 126
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The Sm protein D2 contains a particularly long N-terminal extension whereas B, D1 and D3 have long C-terminal extensions.
Cross-references: PDB:3CW1
Protein: DP01705 (UniProt Q07666)
Region: residues 136	to 156
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The 20 C-terminal amino acids (residues 136–156) do not exhibit any secondary structure. 15N R1 and R2 relaxation rates as well as {1H}-15N heteronuclear NOE data show that the C terminus is highly flexible, whereas the loop connecting the two helices has a slightly increased flexibility when compared with the helical segments (Fig. 2).
Cross-references: BMRB:16969
Protein: DP01705 (UniProt Q07666)
Region: residues 365	to 378
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
We used the 55 residue fragment Sam68-YY for crystallization, but only residues 379–389 (Sam68-2) are visible in our electron density map (Figure S1B).
Cross-references: PDB:3QHE
Protein: DP01705 (UniProt Q07666)
Region: residues 390	to 419
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
We used the 55 residue fragment Sam68-YY for crystallization, but only residues 379–389 (Sam68-2) are visible in our electron density map (Figure S1B).
Cross-references: PDB:3QHE
Protein: DP01705 (UniProt Q07666)
Region: residues 1	to 96
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The N-terminal (residues 1–96) and C-terminal (residues 267–368) regions of Sam68 were expressed in E. coli in the presence of [15N]ammonium chloride and [13C]glucose before purification. The NMR spectra show that these regions are intrinsically disordered and 72% and 65% of the non-proline residue backbone resonances for the N- and C-terminal regions, respectively, could be unambiguously assigned (Figure 1B, C).
Cross-references: BMRB:51359
Protein: DP01705 (UniProt Q07666)
Region: residues 267	to 368
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The N-terminal (residues 1–96) and C-terminal (residues 267–368) regions of Sam68 were expressed in E. coli in the presence of [15N]ammonium chloride and [13C]glucose before purification. The NMR spectra show that these regions are intrinsically disordered and 72% and 65% of the non-proline residue backbone resonances for the N- and C-terminal regions, respectively, could be unambiguously assigned (Figure 1B, C).
Cross-references: BMRB:51360
Protein: DP01705 (UniProt Q07666)
Region: residues 30	to 35
Annotation: phosphorylation display site (Disorder function)
Evidence: in vitro protein kinase assay evidence used in manual assertion
Supporting statements:
During the experiment, the resonance peaks of T33 and T317 shifted downfield in both 1H and 15N dimensions, a typical signature of serine or threonine phosphorylation (36) (Figure 2A, B). Resonances corresponding to other threonine and serine residues were not affected by the addition of Cdk1/cyclin B, indicating that only T33 and T317 were phosphorylated by Cdk1 in vitro. Incubation of the N-terminus with Cdk1 induced CSPs of residues surrounding T33 (notably H27, S29, R31, Q32, R35 and Q36) (Figure 2C), suggesting a possible conformational change upon T33 phosphorylation.
Protein: DP01705 (UniProt Q07666)
Region: residues 316	to 320
Annotation: phosphorylation display site (Disorder function)
Evidence: in vitro protein kinase assay evidence used in manual assertion
Supporting statements:
During the experiment, the resonance peaks of T33 and T317 shifted downfield in both 1H and 15N dimensions, a typical signature of serine or threonine phosphorylation (36) (Figure 2A, B). Resonances corresponding to other threonine and serine residues were not affected by the addition of Cdk1/cyclin B, indicating that only T33 and T317 were phosphorylated by Cdk1 in vitro.
Protein: DP01705 (UniProt Q07666)
Region: residues 17	to 21
Annotation: phosphorylation display site (Disorder function)
Evidence: in vivo protein kinase assay evidence used in manual assertion
Supporting statements:
In terms of serine and threonine (S/T) phosphorylation, we observed phosphorylation of either S18 or S20 (S18/S20) and of either T33 or S35 (T33/S35) in HEK293T cells; and of either S18 or S20 and of either T33 or S35 and S113 in HCT116 cells (Table 1).
S18/S20 phosphorylation was observed in all stages of the cell cycle.
Protein: DP01705 (UniProt Q07666)
Region: residues 32	to 36
Annotation: phosphorylation display site (Disorder function)
Evidence: in vivo protein kinase assay evidence used in manual assertion
Supporting statements:
In terms of serine and threonine (S/T) phosphorylation, we observed phosphorylation of either S18 or S20 (S18/S20) and of either T33 or S35 (T33/S35) in HEK293T cells; and of either S18 or S20 and of either T33 or S35 and S113 in HCT116 cells (Table 1).
Protein: DP01705 (UniProt Q07666)
Region: residues 56	to 60
Annotation: phosphorylation display site (Disorder function)
Evidence: in vivo protein kinase assay evidence used in manual assertion
Supporting statements:
Additionally, S58 and S70 were phosphorylated during G1. These two specific phosphorylation events could be mediated by Erk1 as previously suggested (7). Interestingly, we identified T33 and T317 phosphorylation in mitosis.
Protein: DP01705 (UniProt Q07666)
Region: residues 58	to 72
Annotation: phosphorylation display site (Disorder function)
Evidence: in vivo protein kinase assay evidence used in manual assertion
Supporting statements:
Additionally, S58 and S70 were phosphorylated during G1. These two specific phosphorylation events could be mediated by Erk1 as previously suggested (7). Interestingly, we identified T33 and T317 phosphorylation in mitosis.
Protein: DP01705 (UniProt Q07666)
Region: residues 316	to 320
Annotation: phosphorylation display site (Disorder function)
Evidence: in vivo protein kinase assay evidence used in manual assertion
Supporting statements:
Additionally, S58 and S70 were phosphorylated during G1. These two specific phosphorylation events could be mediated by Erk1 as previously suggested (7). Interestingly, we identified T33 and T317 phosphorylation in mitosis.
Protein: DP01705 (UniProt Q07666)
Region: residues 10	to 61
Annotation: RNA binding (Molecular function)
Evidence: heteronuclear single quantum coherence spectroscopy evidence used in manual assertion
Supporting statements:
Increasing the G8.5 molar ratio with the Sam68 N- and C-termini induced chemical shift perturbations, consistent with the formation of a complex between these regions and the RNA (Figure 3B, C). These results demonstrate that the Sam68 N- and C-terminal regions can bind RNA independently of the rest of the protein. Analysis of the titration data suggests that both domains bind the G.8 RNA with dissociation constants in the low micromolar range (1–10 μM for the N-terminus and 30–70 μM for the C-terminus) (Supplementary Figure S2), very similar to the affinity of the STAR domain for the same RNA sequence (18).
Analysis of the chemical shift mapping shows that RNA binding affects most residues of the N- and C-termini, in particular residues 10–61 for the N-terminus and 281–338 for the C-terminus (Figure 3D, E).
 In that case, the addition of the RNA induces only minor chemical shift perturbation, suggesting that the N- and C-terminal regions of Sam68 bind specifically to the G8.5 RNA.
G8.5 is a RNA that contains the UAAA motif and was previously identified as a high affinity Sam68 binder by SELEX.