LiteFold/DisProt huggingface dataset:
Protein: DP01555 (UniProt Q9EPU7)
Region: residues 4	to 91
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The loss of signals is consistent with KRAB(Ab) binding to the much larger KAP-1–RBCC protein. Given that the KRAB(Ab):KAP-1–RBCC complex is 1:3 molar ratio, the complex is a 180 kDa species. Here molecular tumbling is slow therefore the NMR signals are too broad to be readily detected. Therefore, the loss of observable peaks in the complex versus in the free spectra indicates that KRAB(Ab) was binding to KAP-1–RBCC.
Protein: DP01555 (UniProt Q9EPU7)
Region: residues 4	to 91
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The results of the proteolysis of the KRAB:KAP-1 complex, suggest that KRAB is well folded upon binding KAP-1. In addition, the spectrum of KRAB in complex with KAP-1–RBCC exhibits no heterogeneity, which would be expected if some chemical exchange processes were present.
Protein: DP01555 (UniProt Q9EPU7)
Region: residues 4	to 91
Annotation: disorder (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
the proteolysis of the free KRAB constructs, clearly indicates that any such structure is transient as it does not lead to protection from proteases.
Protein: DP01556 (UniProt Q96GC6)
Region: residues 4	to 77
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The HSQC spectra of ZNF274-KRAB(AB) shows that the majority of backbone amide resonances exhibit poor dispersion, indicating substantial regions of disordered structure. Most backbone resonances fall (> 95%) within the center of the spectrum (7.7 ppm to 8.5 ppm), some are broadened or missing indicating intermediate timescale motions. Minimal NOE cross-peaks and the 1D 1H spectra confirm the lack of structure.
Protein: DP01556 (UniProt Q96GC6)
Region: residues 4	to 77
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Transcriptional repression by the KRAB domains correlates with its binding to KAP-1 (KRAB associated protein 1), also referred to as TIF1β or KRIP-1. The KRAB domain binds directly with high affinity to the RBCC domain of KAP-1.
Protein: DP01556 (UniProt Q96GC6)
Region: residues 4	to 77
Annotation: disorder (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
Consistent with these studies, the proteolysis of the free KRAB constructs, clearly indicates that any such structure is transient as it does not lead to protection from proteases.
Protein: DP01556 (UniProt Q96GC6)
Region: residues 4	to 246
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
CD spectra of the ZNF274–KRAB(AB)-SCAN protein construct showed that it contains mostly random coil (56% ∼ 65%) with a small degree of helix (35% ∼ 39%) but little β sheet (0 ∼ 5%). These data suggest that the KRAB domain alone may not be highly structured.
Protein: DP01557 (UniProt P27682)
Region: residues 25	to 210
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The far-UV CD spectra of the 7B2  did not support the presence of secondary structures such as α helices or β strands. The characteristic negative peaks at 208 and 222 nm displayed by α helical proteins were not visible in 7B2 spectra. The α helical content was estimated as 29% for 27 kDa 7B2, while the β sheet content was 14%.
Protein: DP01557 (UniProt P27682)
Region: residues 25	to 210
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The 1H–15N HSQC spectrum displayed considerably smaller number of peaks than would be expected from a well-folded 186-residue protein. The chemical shift dispersion was extremely narrow, between 6.9 and 8.4 ppm, indicative of unfolded protein. This conclusion was strengthened by the natural abundance 13C–1H HSQC spectrum, where we observed far fewer peaks and poor chemical shift dispersion.
Protein: DP01557 (UniProt P27682)
Region: residues 25	to 210
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
7B2 is a small secretory protein that is known to be required for the productive maturation of the subtilisin-like endoprotease prohormone convertase 2 (proPC2). The motifs and domains required for the interaction between 7B2 and proPC2 are established.
Protein: DP01558 (UniProt Q9XTY3)
Region: residues 17	to 211
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The far-UV CD spectra of the 7B2 protein samples did not support the presence of typical secondary structures elements. The characteristic negative peaks at 208 and 222 nm displayed by α helical proteins were not visible in 7B2 spectra. Estimation of secondary structure content revealed that the 27 kDa C. elegans protein contained few structural elements, only 18% α helix and 26% β sheet content.
Protein: DP01558 (UniProt Q9XTY3)
Region: residues 17	to 211
Annotation: protein binding (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Despite the low level of overall sequence conservation, the physiological functions of the C. elegans protein with regard to help the maturation of prohormone convertase 2 (proPC2) within the secretory pathway appear to be similar to those of the vertebrate proteins.
Protein: DP01559 (UniProt Q04964)
Region: residues 1	to 104
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Sml1 is highly flexible in solution with no defined tertiary structure. Three regions exhibited a high degree of backbone order (S2 > 0.6); residues 4 to 14, 20 to 35, and 61 to 80. Regions 4-14 and 61-80 are alpha-helical, as shown by the positive secondary Cα chemical shifts. Overall, Sml1 is best characterized as a loosely folded protein in which the two main helices are oriented in an antiparallel fashion.
Protein: DP01559 (UniProt Q04964)
Region: residues 1	to 104
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The small spectral width of the amide signals of Sml1 clearly indicates that the protein is mainly unfolded. Secondary chemical shifts analysis suggests the presence of two helical regions in Sml1. SSP-analysis shows that the helix propensity in region 60-80 is very high. Interestingly, the region 33-45 has β-sheet propensity. The NOE values are all above 0 and the pattern is similar as for the relaxation rates.
Protein: DP01560 (UniProt Q9UMR2)
Region: residues 55	to 91
Annotation: disorder to order (Structural transition)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The section Asp55–Ser68 of the N-terminal extension, which was partly disordered in the RNA complex, folded into an -helix that occupied the central cleft between the two lobes.
Protein: DP01560 (UniProt Q9UMR2)
Region: residues 55	to 91
Annotation: protein binding (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The Asp55–Ser68 -helix makes a significant number of side chain interactions with both conserved domains.
Protein: DP01560 (UniProt Q9UMR2)
Region: residues 55	to 91
Annotation: self-inhibition (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The interactions of the cleft-inserted helix with the conserved domains and with the nucleotide attest to the specificity and selectivity of the positioning of the N-terminal extension and point to a potential regulatory mechanism for the intrinsic ATPase activity of DDX19.
Protein: DP01561 (UniProt P08235)
Region: residues 1	to 169
Annotation: disorder (Structural state)
Evidence: fluorescence evidence used in manual assertion
Supporting statements:
The tryptophan in MR-AF1a is essentially solvent exposed with a λmax of 351 nm, i.e. not significantly changed by urea-induced unfolding (Fig. 3A and Table 1).
Protein: DP01561 (UniProt P08235)
Region: residues 1	to 169
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The spectrum in buffer shows a strong minimum at around 197 nm, which is indicative of nonordered structure (Fig. 4A).
Protein: DP01561 (UniProt P08235)
Region: residues 247	to 385
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The far-UV spectra for MR-MD showed a similar trend with a more helical conformation adopted in the presence of TFE (Fig. 4B and Table 2).
Protein: DP01561 (UniProt P08235)
Region: residues 247	to 385
Annotation: disorder (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
Supplemental Fig. 1B shows that the MR-MD polypeptide is digested in a time-dependent manner, and this digestion is prevented in the presence of TMAO. This is consistent with induced folding of the MD and adoption of a more protease-resistant conformation.
Protein: DP01561 (UniProt P08235)
Region: residues 1	to 602
Annotation: disorder (Structural state)
Evidence: fluorescence evidence used in manual assertion
Supporting statements:
Fluorescence and far-UV spectroscopy analysis of the full-length MR-NTD revealed some composite structural properties seen with the isolated domains, but generally, the fluorescence emission for the solvent exposed tryptophan was dominant, and the polypeptide showed a propensity to form helical secondary structure in a hydrophobic environment (Tables 1 and 2 and Supplemental Fig. 2, A and B).
Protein: DP01561 (UniProt P08235)
Region: residues 1	to 602
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Supplemental Fig. 2, B. shows this peptide has a large negative ellipticity around 200 nm, typical of unstructured regions.
Protein: DP01561 (UniProt P08235)
Region: residues 1	to 602
Annotation: TBP-class protein binding (Molecular function)
Evidence: glutathione S-transferase pull-down assay evidence used in manual assertion
Supporting statements:
By contrast, the TBP was found to preferentially interact with the MR-AF1b domain, and full-length NTD, in the absence of TMAO (Fig. 5B).
Protein: DP01561 (UniProt P08235)
Region: residues 1	to 169
Annotation: TBP-class protein binding (Molecular function)
Evidence: glutathione S-transferase pull-down assay evidence used in manual assertion
Supporting statements:
No selective interactions were indentified for the MR-AF1a domain for any of the proteins tested, although some modest binding of TBP was seen in some experiments (Fig. 5).
Protein: DP01561 (UniProt P08235)
Region: residues 450	to 602
Annotation: TBP-class protein binding (Molecular function)
Evidence: glutathione S-transferase pull-down assay evidence used in manual assertion
Supporting statements:
By contrast, the TBP was found to preferentially interact with the MR-AF1b domain, and full-length NTD, in the absence of TMAO (Fig. 5B).
A similar analysis of the interaction of TBP with increasing amounts of GST alone or GST-MR-AF1b, but in the absence of TMAO, also resulted in saturable binding, and from the corresponding Eadie-Hofstee plot, a dissociation constant of 1.4 μm was calculated for this interaction (Fig. 7, A–C).
Protein: DP01561 (UniProt P08235)
Region: residues 247	to 385
Annotation: receptor transactivation (Biological process)
Evidence: luciferase reporter gene assay evidence used in manual assertion
Supporting statements:
To confirm the importance of regions within the NTD for transactivation, a construct was made containing the NTD-DBD with a FLAG tag and transfected into COS-1 cells together with a luciferase reporter gene driven by two glucocorticoid response elements (GREs). 
Deletion of the MD reduced the transcriptional activity of the NTD by 35%, whereas deleting AF1a or AF1b region resulted in a loss of greater than 97% of the activity of the full NTD (Fig. 2B). Importantly, the AF1b domain alone linked to the DBD retained 26% the activity of the MR-NTD-DBD polypeptide (Fig. 1B).
Protein: DP01561 (UniProt P08235)
Region: residues 1	to 169
Annotation: receptor transactivation (Biological process)
Evidence: luciferase reporter gene assay evidence used in manual assertion
Supporting statements:
To confirm the importance of regions within the NTD for transactivation, a construct was made containing the NTD-DBD with a FLAG tag and transfected into COS-1 cells together with a luciferase reporter gene driven by two glucocorticoid response elements (GREs). 
Deletion of the MD reduced the transcriptional activity of the NTD by 35%, whereas deleting AF1a or AF1b region resulted in a loss of greater than 97% of the activity of the full NTD (Fig. 2B). Importantly, the AF1b domain alone linked to the DBD retained 26% the activity of the MR-NTD-DBD polypeptide (Fig. 1B).
Protein: DP01561 (UniProt P08235)
Region: residues 450	to 602
Annotation: receptor transactivation (Biological process)
Evidence: luciferase reporter gene assay evidence used in manual assertion
Supporting statements:
To confirm the importance of regions within the NTD for transactivation, a construct was made containing the NTD-DBD with a FLAG tag and transfected into COS-1 cells together with a luciferase reporter gene driven by two glucocorticoid response elements (GREs). 
Deletion of the MD reduced the transcriptional activity of the NTD by 35%, whereas deleting AF1a or AF1b region resulted in a loss of greater than 97% of the activity of the full NTD (Fig. 2B). Importantly, the AF1b domain alone linked to the DBD retained 26% the activity of the MR-NTD-DBD polypeptide (Fig. 1B).
Protein: DP01561 (UniProt P08235)
Region: residues 465	to 471
Annotation: receptor transactivation (Biological process)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
Mutating two serine residues and a leucine at positions 468, 469, and 470 (M5) (Fig. 8A) was predicted to disrupt local β-structure and increase α-helix. Mutating these residues or the leucine alone at 469 (M8) (Fig. 8A) impaired transactivation activity in the context of MR-NTD-DBD (Fig. 8B).
Protein: DP01562 (UniProt Q9Z1X4)
Region: residues 55	to 86
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues in the N- and C-termini and several loops (residues 1–5, 55–86, 341–353 and 375–380 of NF90 and 362–390 of
NF45) could not be modeled due to poor electron density in these regions that made a clear interpretation of the map difficult.
Protein: DP01562 (UniProt Q9Z1X4)
Region: residues 341	to 353
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues in the N- and C-termini and several loops (residues 1–5, 55–86, 341–353 and 375–380 of NF90 and 362–390 of
NF45) could not be modeled due to poor electron density in these regions that made a clear interpretation of the map difficult.
Protein: DP01562 (UniProt Q9Z1X4)
Region: residues 468	to 518
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The linker region connecting the two domains (residues 468–518) is not visible, consistent with the prediction that this region is natively disordered.
Protein: DP01563 (UniProt Q9CXY6)
Region: residues 362	to 390
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues in the N- and C-termini and several loops (residues 1–5, 55–86, 341–353 and 375–380 of NF90 and 362–390 of NF45) could not be modelled due to poor electron density in these regions that made a clear interpretation of the map difficult.
Cross-references: PDB:4AT7
Protein: DP01564 (UniProt Q12905)
Region: residues 362	to 390
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Structural studies were carried out with mouse NF90 and NF45. Mouse and human NF90 show 95% sequence identity while mouse and human NF45 are identical at the protein level.
Residues in the N- and C-termini and several loops (residues 1–5, 55–86, 341–353 and 375–380 of NF90 and 362–390 of NF45) could not be modelled due to poor electron density in these regions that made a clear interpretation of the map difficult.
Cross-references: PDB:4AT7
Protein: DP01565 (UniProt Q9GSG7)
Region: residues 1	to 112
Annotation: disorder (Structural state)
Evidence: sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion
Supporting statements:
Due to their unusual amino acid composition, IDPs bind less SDS molecules and move more slowly in gel than globular proteins. aaUsp-NTD (residues 1-112) exhibits such properties. The apparent molecular mass of aaUsp-NTD calculated on the basis of SDS-PAGE electrophoretical mobility was 14 kDa, whereas the theoretical molecular mass was 12.718 kDa.
Protein: DP01565 (UniProt Q9GSG7)
Region: residues 1	to 112
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The spectrum exhibits features of spectra typical of IDPs, because it has a deep minimum at 200 nm, which is characteristic for a random coil and it has a slight negative band at 222 nm, which is typical for ordered secondary structures. CD spectra in the presence of varying concentrations of GdmCl also imply that aaUsp-NTD is a highly unfolded protein with a residual secondary structure.
Protein: DP01565 (UniProt Q9GSG7)
Region: residues 1	to 112
Annotation: disorder (Structural state)
Evidence: chromatography evidence used in manual assertion
Supporting statements:
aaUsp-NTD's theoretical molecular mass is 12.718 kDa. The Ve of purified aaUsp-NTD corresponds to a pro-
tein with an apparent molecular mass equal to 24.7 kDa and RS equal to 22.7 Å (1 Å = 0.1 nm). This indicates 
that aaUsp-NTD may have an expanded conformation such as IDPs do.
Protein: DP01565 (UniProt Q9GSG7)
Region: residues 1	to 112
Annotation: disorder (Structural state)
Evidence: analytical ultracentrifugation evidence used in manual assertion
Supporting statements:
Analysis of the data obtained suggests that aaUsp-NTD eluted as a monomer (eluted as a distinct, symmetric peak corresponding to a monomer and the Ve value was independent of the sample concentration). Additionally, the frictional ratio was fitted to 1.8, indicating that aaUsp-NTD is an asymmetric protein with an RS of 28.1 Å.
Protein: DP01567 (UniProt B9UCQ5)
Region: residues 1	to 58
Annotation: disorder (Structural state)
Evidence: protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion
Supporting statements:
The results showed that the highest rate of exchange, approximately 80%, was observed for the peptides covering the NTD (residues 1-58), which is consistent with the results of the bioinformatic analyses, indicating that this region is disordered.
Protein: DP01569 (UniProt P34021-2)
Region: residues 2	to 226
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
EcRA-NTD spectra is reminiscent of spectra typical of proteins containing numerous disordered regions, because it displays a deep minimum around 200 nm. However, EcRA-NTD is not fully random coil-like, as it has a content of the residual secondary structure, which can be destroyed by GdmCl denaturation.
Protein: DP01569 (UniProt P34021-2)
Region: residues 2	to 226
Annotation: disorder (Structural state)
Evidence: chromatography evidence used in manual assertion
Supporting statements:
Stokes radius determined on the basis of gel filtration was substantially bigger, 36.6 +/-1.5 A for EcRA-NTD than the theoretical Stokes radius.
Protein: DP01569 (UniProt P34021-2)
Region: residues 2	to 226
Annotation: disorder (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
The protein was extensively degraded, however the peptide bonds were not accessible at random. There are nineteen potential trypsin cleavage sites within the EcRA-NTD sequence, yet only nine main proteolysis products were revealed through electrophoretic gels.
Protein: DP01570 (UniProt P12931)
Region: residues 1	to 84
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The low chemical shift dispersion in the HSQC spectrum is consistent with an unfolded domain. The measured chemical shifts of HN, NH, Cα, Cβ, and C′ have been compared with random-coil values corrected for local sequence effects. The observed deviations are small, as expected for an unfolded protein. N–HN RDCs measured for USrc are predominantly negative as for unfolded proteins.
Protein: DP01570 (UniProt P12931)
Region: residues 1	to 84
Annotation: phosphorylation display site (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The phosphorylation of c-SRC Ser17 by PKA (cAMP-dependent protein kinase) is a well-characterized process.
Protein: DP01571 (UniProt Q88QP8)
Region: residues 40	to 62
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The switch I loop of EF-Tuputida (residues 40–62) is disordered.
Protein: DP01572 (UniProt P0C0Y1)
Region: residues 1	to 11
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Is possible that the N-terminus (A1-L11) becomes structured in the presence of the LH1 R subunit and RC components (...). In addition, the lack of charged amino acids (L6-L11) suggests the N-terminus should be buried, and this may also occur in the presence of the LH1 R subunit and the RC.
The long T1 and T2 values for the N-terminus are typical of disordered polypeptides.
Protein: DP01574 (UniProt C6KSX0)
Region: residues 84	to 116
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Four regions of disorder are present in the Pf12short structure, all localized to surface loops projecting away from the core domain (dotted lines in Fig. 3A and 4A). In D1, a 33-residue region between Glu-83 and Ile-117 connecting β4 and β6 could not be modeled
Cross-references: PDB:2YMO
Protein: DP01574 (UniProt C6KSX0)
Region: residues 143	to 157
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
a 15-residue loop between Lys-142 (β7) and Asp-158 (β8) was disordered
Cross-references: PDB:2YMO