LiteFold/DisProt huggingface dataset:
Protein: DP04178 (UniProt O14746)
Region: residues 418	to 443
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
The PDB shows this region lacks electron density, indicating it is disordered
Cross-references: PDB:7QXS
PDB:7QXB
PDB:7QXA
EMDB:14197 
EMDB:14196
Protein: DP04178 (UniProt O14746)
Region: residues 222	to 240
Annotation: protein import into nucleus (Biological process)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
To determine whether nuclear localization of hTERT is affected by different cellular backgrounds, several cell lines – including MCF7, H1299 and U2OS cells – were transfected with Flag–hTERT and various mutant constructs (Flag-7A, Flag-S227A and Flag-S227E, see Fig. 1A), and then subjected to immunofluorescence analyses using an antibody against Flag (supplementary material Fig. S1). The results indicated that both the bipartite NLS and Akt-mediated phosphorylation at S227 are required for efficient nuclear import of hTERT, suggesting that the mechanism of nuclear localization of hTERT is not cell-type specific.
Protein: DP04179 (UniProt P30519)
Region: residues 1	to 29
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The A molecule of heme-bound HO-2 was lacking electron density for Met1–Met28 and Thr243–Lys264. The B molecule of heme-bound HO-2 was missing density for Met1–Arg29 and Leu249–Lys264.
The PDB shows this region lacks electron density, indicating it is disordered
Cross-references: PDB:2RGZ
Protein: DP04179 (UniProt P30519)
Region: residues 249	to 264
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The A molecule of heme-bound HO-2 was lacking electron density for Met1–Met28 and Thr243–Lys264. The B molecule of heme-bound HO-2 was missing density for Met1–Arg29 and Leu249–Lys264.
The PDB shows this region lacks electron density, indicating it is disordered.
Cross-references: PDB:2RGZ
Protein: DP04179 (UniProt P30519)
Region: residues 1	to 29
Annotation: flexible N-terminal tail (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The A molecule of heme-bound HO-2 was lacking electron density for Met1–Met28 and Thr243–Lys264. The B molecule of heme-bound HO-2 was missing density for Met1–Arg29 and Leu249–Lys264.
The PDB structure shows the 1-29 region lacks electron density, indicating it's disordered.
Cross-references: PDB:2RGZ
Protein: DP04180 (UniProt O60232)
Region: residues 1	to 12
Annotation: disorder (Structural state)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
We were not able to model residues 1–12 and 78–111 in the electron density map and coincidentally, these regions correlate with the intrinsic disorder prediction plot of SSSCA1 and confirm that these residues likely are disordered in the protein crystal as well (Fig. 1a).
Cross-references: PDB:6HCZ
Protein: DP04180 (UniProt O60232)
Region: residues 78	to 111
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
We were not able to model residues 1–12 and 78–111 in the electron density map and coincidentally, these regions correlate with the intrinsic disorder prediction plot of SSSCA1 and confirm that these residues likely are disordered in the protein crystal as well (Fig. 1a).
Cross-references: PDB:6HCZ
Protein: DP04180 (UniProt O60232)
Region: residues 1	to 11
Annotation: flexible N-terminal tail (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
We were not able to model residues 1–12 and 78–111 in the electron density map and coincidentally, these regions correlate with the intrinsic disorder prediction plot of SSSCA1 and confirm that these residues likely are disordered in the protein crystal as well (Fig. 1a).
Protein: DP04182 (UniProt Q99453)
Region: residues 228	to 240
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
NMR secondary chemical shift analysis and chemical shift-derived S2 order parameters calculated by TALOS-N36 indicate that the polyAla tract particularly populates α-helical conformations, while the rest of the protein remains largely disordered (Fig. 1D).
Cross-references: PDB:8PUI
Protein: DP04182 (UniProt Q99453)
Region: residues 261	to 314
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
NMR secondary chemical shift analysis and chemical shift-derived S2 order parameters calculated by TALOS-N36 indicate that the polyAla tract particularly populates α-helical conformations, while the rest of the protein remains largely disordered (Fig. 1D).
Cross-references: PDB:8PUI
Protein: DP04183 (UniProt Q9ZHD1)
Region: residues 1	to 21
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
The first 21 residues are highly flexible and did not show any inter-residue NOE correlations.
Cross-references: PDB:8C2Q
Protein: DP04184 (UniProt P68633)
Region: residues 38	to 67
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
The NMR structure of soluble tA28 revealed an α-β-α sandwich-like structural motif from residues 68–146, in which the β-strands are stabilized by multiple hydrogen bonds among strands sandwiched by two α-helices, whereas residues 38–67 were uncovered as a disordered domain.
Cross-references: PDB:8GQO
Protein: DP04185 (UniProt C1LGM4)
Region: residues 74	to 114
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
The backbone NH peaks of the well-structured region (residues 1–73) are highlighted in black, and the overlapped backbone NH peaks of the disordered region (residues 74–114) are highlighted in red, in the 2D 1H-15N HSQC spectrum (Supplementary Figure S2).
Cross-references: PDB:8FA3
Protein: DP04186 (UniProt C7G3K3)
Region: residues 22	to 55
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
LaIT2 adopts a β-KTx-like structure with an unfolded N-domain and folded C-domain.
Cross-references: PDB:7WKF
Protein: DP04187 (UniProt O25506)
Region: residues 55	to 94
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Like D‐conformation of Hup, the secondary structure
analysis of M‐conformation revealed that it exhibits stable
N‐terminal dimerization domain, whereas its C‐terminal
DNA binding domain was found to be partially disordered
as inferred by the significantly lower values of secondary
shifts (i.e., <±0.2 ppm, Figure 2c).
Another important observation made here is that the C‐terminal half (from Glu55 to Lys94) was found to be disordered in monomeric M‐conformation (as evident from Figures 2c and 5c).
Protein: DP04187 (UniProt O25506)
Region: residues 55	to 94
Annotation: order (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Contrary to this, the HNN‐based amide correlations were
not discerned for D‐conformation of Hup suggesting that
this conformation is structurally stable and with slow
molecular tumbling rate—possibly due to its dimeric state
in solution—rendering short T2 values for the amide spins.
The secondary structure analysis (Figure 2c) revealed that the D‐conformation of Hup at pH of 6.0 consists of (a) three α helical regions: Ile7‐Ala13 (α1), Lys19‐Ser38 (α2), and Lys84‐Glu92 (α3) and (b) five β strands: Glu41‐ Leu45 (β1), Gly49‐Gln56 (β2), Lys59‐Val63 (β3), Ser66‐ Glu73 (β4), and Arg76‐Gly83 (β5). 
Cross-references: BMRB:26942
Protein: DP04187 (UniProt O25506)
Region: residues 55	to 94
Annotation: order to disorder (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
An important observation revealed by variable temperature study (temperature varied from 285 to 312 K) is that the protein undergoes a local, but reversible conformational change between D and M states with amid point around 300 +/−5 K for dimerization domain and around 305 +/−5 K for DNA binding domain.
The phenomenon of dimer dissociation was further corroborated by increased number of amide cross peaks (54 in number)corresponding to M‐conformation at 310 K compared to 48 peaks discerned at 298 K.
In solution the protein dimerize and the region is structured. When the monomeric form is encouraged (i.e by increasing the temperature) is possible to note that the same region is disordered. In the dimeric (D) form the C-terminal is ordered, while in the monomer form (M) this region is disordered.
Cross-references: BMRB:26942
Protein: DP04188 (UniProt P49748)
Region: residues 486	to 518
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The electron density map is generally well ordered for the entire polypeptide chain with the exception of the first seven N-terminal amino acids and residues 446–478 (using the full-length mature VLCAD numbering scheme), which, therefore, were not included in the structural model.
However, the residues 446–478 are disordered in the VLCAD structure. Because of the proximity of residues both 445 and 479 to the surface (Fig. 4A), it is expected that the disordered residues also pack at the surface of the molecule. Fig. 4A shows a helix model built from residues 441–476, which include the disordered residues.
We have proposed that a region from residues 441 to 476 mediates membrane binding. This region is disordered in the crystal structure.
Cross-references: PDB:3B96
Protein: DP04189 (UniProt P29372)
Region: residues 131	to 141
Annotation: disorder (Structural state)
Evidence: crystallography evidence used in manual assertion
Supporting statements:
The residues that lack electron density in the low-affinity complex, and are thus considered disordered, include Glu131- Arg141 (loop 1), Gly263 -Lys273 (loop 2), and C terminal residues after Asp289 (loop 3) (Figure 3A,B).
Cross-references: PDB:3UBY
Protein: DP04189 (UniProt P29372)
Region: residues 263	to 273
Annotation: disorder (Structural state)
Evidence: crystallography evidence used in manual assertion
Supporting statements:
The residues that lack electron density in the low-affinity complex, and are thus considered disordered, include Glu131- Arg141 (loop 1), Gly263 -Lys273 (loop 2), and C terminal residues after Asp289 (loop 3) (Figure 3A,B).
Cross-references: PDB:3UBY
Protein: DP04189 (UniProt P29372)
Region: residues 263	to 273
Annotation: DNA binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Figure 1B shows amino acid side and main chains in this region, are involved in DNA binding in the higher-affinity DNA binding conformation. This interaction also leads to the gain of structure in this region.
Cross-references: PDB:3UBY
Protein: DP04189 (UniProt P29372)
Region: residues 131	to 141
Annotation: disorder to order (Structural transition)
Evidence: crystallography evidence used in manual assertion
Supporting statements:
Here, previously disordered loops are completely ordered to display the full potential of a continuous electrostatic surface for binding DNA; Tyr162 is fully inserted into the DNA, and a base lesion is bound tightly in the AAG active site.
After the release of the base-lesion contact, the active site and other loops of AAG would become partially disordered, decreasing the extent of order of the DNA 
 binding surface, ultimately leaving AAG in its lower-affinity, nonspecific searching state once again.
Cross-references: PDB:3UBY
Protein: DP04189 (UniProt P29372)
Region: residues 263	to 273
Annotation: disorder to order (Structural transition)
Evidence: crystallography evidence used in manual assertion
Supporting statements:
Here, previously disordered loops are completely ordered to display the full potential of a continuous electrostatic surface for binding DNA; Tyr162 is fully inserted into the DNA, and a base lesion is bound tightly in the AAG active site.
After the release of the base-lesion contact, the active site and other loops of AAG would become partially disordered, decreasing the extent of order of the DNA 
 binding surface, ultimately leaving AAG in its lower-affinity, nonspecific searching state once again.
Cross-references: PDB:3UBY
Protein: DP04189 (UniProt P29372)
Region: residues 131	to 141
Annotation: DNA binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Figure 1B shows amino acid side and main chains in this region, are involved in DNA binding in the higher-affinity DNA binding conformation. This interaction also leads to the gain of structure in this region.
Cross-references: PDB:3UBY
Protein: DP04190 (UniProt P03170)
Region: residues 4	to 15
Annotation: order (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
In micellar solution of deuterated sodium dodecyl sulfate, the viral TAP inhibitor adopts an ordered structure. There are two helical regions extending from residues 4 to 15 and from residues 22 to 32.
Cross-references: PDB:1QLO
Protein: DP04190 (UniProt P03170)
Region: residues 22	to 32
Annotation: order (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
In micellar solution of deuterated sodium dodecyl sulfate, the viral TAP inhibitor adopts an ordered structure. There are two helical regions extending from residues 4 to 15 and from residues 22 to 32.
Cross-references: PDB:1QLO
Protein: DP04190 (UniProt P03170)
Region: residues 1	to 53
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Surprisingly, the CD spectrum of ICP47(1-53) shows no characteristic of secondary structure in phosphate buffer (Figure 2A).
Protein: DP04190 (UniProt P03170)
Region: residues 1	to 88
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Surprisingly, the CD spectrum of ICP47(1−53) shows no characteristics of secondary structure in phosphate buffer (Figure 2a). The same result was obtained for full-length His-ICP47 (not shown).
Protein: DP04190 (UniProt P03170)
Region: residues 1	to 88
Annotation: disorder (Structural state)
Evidence: fluorescence evidence used in manual assertion
Supporting statements:
At 10 and 37 °C, the fluorescence emission has its maximum at 355 nm, indicating that the tryptophan is completely solvent exposed (Figure 5). While hydrophobic side chains are usually buried in folded domains, the fluorescence data give further evidence that ICP47 is highly dynamic and mainly unstructured in aqueous solution.
Protein: DP04190 (UniProt P03170)
Region: residues 1	to 13
Annotation: disorder to order (Structural transition)
Evidence: fluorescence evidence used in manual assertion
Supporting statements:
After addition of pure DMPC vesicles at 20 °C, the wavelength of the emission maximum remains constant and the fluorescence intensity increases slightly, reflecting only a very weak interaction of ICP47(1−53) with neutral changed phospholipids. By increasing the molar ratio of DMPG/DMPC vesicles, we observed drastic changes of the fluorescence emission. The emission maximum was shifted to 335 nm and the fluorescence intensity increased 2-fold. The changes of the secondary structure observed in different lipid charge densities are in very good agreement with the changes in tryptophan fluorescence.
However, in the presence of membrane mimetics, a drastic conformational change of ICP47 to a more α-helical structure was observed. This result is in line with secondary structure predictions, which propose two helices located within residues 3−13 and 35−43 (Figure 6a).
Therefore, we conclude that both predicted α-helices are formed under these conditions.
Protein: DP04190 (UniProt P03170)
Region: residues 1	to 13
Annotation: disorder to order (Structural transition)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
As summarized in Figure 3, lipid vesicles that contain negatively charged lipids, such as phosphatidic acid (PA), phosphatidylglycerol (PG), or phosphatidylserine (PS) (latter not shown), induce an α-helical conformation, whereas neutral or positively charged lipid vesicles, such as phosphatidylcholine (DMPC or POPC) or dihexadecyldimethylammonium bromide (DHDAB), hardly affect the secondary structure of ICP47(1−53). Therefore, we conclude that the viral TAP inhibitor adopts a more α-helical structure when bound to membranes and that negatively charged lipids induce membrane adsorption and conformational change.
However, in the presence of membrane mimetics, a drastic conformational change of ICP47 to a more α-helical structure was observed. This result is in line with secondary structure predictions, which propose two helices located within residues 3−13 and 35−43 (Figure 6a).
Therefore, we conclude that both predicted α-helices are formed under these conditions.
Protein: DP04190 (UniProt P03170)
Region: residues 1	to 53
Annotation: molecular sequestering activity (Molecular function)
Evidence: radioisotope assay evidence used in manual assertion
Supporting statements:
Using a TAP inhibition assay as previously described (Ahn et al., 1996), we compared the activity of this fragment with the full-length protein expressed in E. coli. As summarized in Figure 1, we found the truncated ICP47(1−53) to be fully active with respect to inhibition of peptide binding to human TAP.
Protein: DP04190 (UniProt P03170)
Region: residues 1	to 53
Annotation: TAP binding (Molecular function)
Evidence: protein binding evidence used in manual assertion
Supporting statements:
The binding constants of His-ICP47 and ICP47(1−53) for human TAP appear to be identical and were determined to be 50 and 60 nM, respectively. So we conclude that ICP47(1−53), lacking the redundant N-terminal fusion tag and the C-terminal domain, covers the active domain of the TAP inhibitor.
Protein: DP04190 (UniProt P03170)
Region: residues 1	to 53
Annotation: lipid binding (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
As summarized in Figure 3, lipid vesicles that contain negatively charged lipids, such as phosphatidic acid (PA), phosphatidylglycerol (PG), or phosphatidylserine (PS) (latter not shown), induce an α-helical conformation, whereas neutral or positively charged lipid vesicles, such as phosphatidylcholine (DMPC or POPC) or dihexadecyldimethylammonium bromide (DHDAB), hardly affect the secondary structure of ICP47(1−53). Therefore, we conclude that the viral TAP inhibitor adopts a more α-helical structure when bound to membranes and that negatively charged lipids induce membrane adsorption and conformational change.
Protein: DP04190 (UniProt P03170)
Region: residues 1	to 53
Annotation: lipid binding (Molecular function)
Evidence: fluorescence evidence used in manual assertion
Supporting statements:
After addition of pure DMPC vesicles at 20 °C, the wavelength of the emission maximum remains constant and the fluorescence intensity increases slightly, reflecting only a very weak interaction of ICP47(1−53) with neutral changed phospholipids. By increasing the molar ratio of DMPG/DMPC vesicles, we observed drastic changes of the fluorescence emission. The emission maximum was shifted to 335 nm and the fluorescence intensity increased 2-fold. The changes of the secondary structure observed in different lipid charge densities are in very good agreement with the changes in tryptophan fluorescence.
Protein: DP04190 (UniProt P03170)
Region: residues 2	to 34
Annotation: negative regulation of transporter activity (Biological process)
Evidence: in vitro assay evidence used in manual assertion
Supporting statements:
ICP47(2−34) Blocks Peptide Binding to and Peptide Transport by TAP. The activity of the synthetic ICP47(2−34) was analyzed by an in vitro peptide transport assay based on specific N-glycosylation in microsomes. As shown in Figure 1A, ICP47(2−34) completely blocks TAP-specific peptide translocation of radiolabeled reporter peptides into microsomes.
Protein: DP04190 (UniProt P03170)
Region: residues 2	to 34
Annotation: TAP binding (Molecular function)
Evidence: in vitro assay evidence used in manual assertion
Supporting statements:
Moreover, we quantified the binding affinity of ICP47(2−34) to TAP and its ability to inhibit peptide binding by competition assays (Figure 1B). An affinity binding constant of Kd = 100 ± 14 nM was determined, which is in good agreement with the affinity constant for the full-length ICP47 ( 7, 8).
Protein: DP04190 (UniProt P03170)
Region: residues 2	to 34
Annotation: molecular sequestering activity (Molecular function)
Evidence: in vitro assay evidence used in manual assertion
Supporting statements:
Moreover, we quantified the binding affinity of ICP47(2−34) to TAP and its ability to inhibit peptide binding by competition assays (Figure 1B). An affinity binding constant of Kd = 100 ± 14 nM was determined, which is in good agreement with the affinity constant for the full-length ICP47 ( 7, 8).
Protein: DP04190 (UniProt P03170)
Region: residues 2	to 34
Annotation: phospholipid binding (Molecular function)
Evidence: in vitro assay evidence used in manual assertion
Supporting statements:
Microsomes prepared from noninfected insect cells were incubated with an increasing amount of radiolabeled ICP47(2−34) and washed, and the membrane-associated inhibitor was quantified. As shown in Figure 2 the polypeptide binds in a dose-dependent manner to microsomes, revealing an affinity constant Kd = 34 ± 9 μM. ICP47(2−34) shows a 350−400 times weaker affinity to microsomal membranes without than with human TAP.
Additionally, the membrane association explains the biphasic binding characteristics of ICP47 to TAP-containing microsomes (data not shown).
Protein: DP04190 (UniProt P03170)
Region: residues 4	to 15
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The structure calculation shows that the conformation of the peptide bound to SDS consists of two major helices extending from residues 4 to 15 and from 22 to 32 (Figure 7).
Cross-references: PDB:1QLO
Protein: DP04190 (UniProt P03170)
Region: residues 22	to 32
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The structure calculation shows that the conformation of the peptide bound to SDS consists of two major helices extending from residues 4 to 15 and from 22 to 32 (Figure 7).
Cross-references: PDB:1QLO
Protein: DP04191 (UniProt Q99P72)
Region: residues 1025	to 1090
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
We determined that the small amount of secondary structure evident in the CD spectrum is transient and not involved in a stable fold based on the following NMR data.