LiteFold/DisProt huggingface dataset:
Protein: DP01119 (UniProt P35222)
Region: residues 772	to 781
Annotation: disorder to order (Structural transition)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The high-resolution crystal structure of TIP-1 in complex with the C-terminal peptide of β-catenin provides molecular details for the recognition of β-catenin by TIP-1.
Cross-references: PDB:3DIW
ELM:LIG_PDZ_Class_1
Protein: DP01119 (UniProt P35222)
Region: residues 772	to 781
Annotation: protein binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The high-resolution crystal structure of TIP-1 in complex with the C-terminal peptide of β-catenin provides molecular details for the recognition of β-catenin by TIP-1.
Cross-references: PDB:3DIW
Protein: DP01119 (UniProt P35222)
Region: residues 19	to 44
Annotation: protein binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The 3.0 Å structure of a β-TrCP1-Skp1-β-catenin complex reveals the basis of substrate recognition by the β-TrCP1 WD40 domain.
Cross-references: PDB:1P22
Protein: DP01119 (UniProt P35222)
Region: residues 19	to 44
Annotation: disorder to order (Structural transition)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The 3.0 Å structure of a β-TrCP1-Skp1-β-catenin complex reveals the basis of substrate recognition by the β-TrCP1 WD40 domain.
Cross-references: PDB:1P22
Protein: DP01119 (UniProt P35222)
Region: residues 43	to 47
Annotation: phosphorylation display site (Disorder function)
Evidence: immunodetection assay evidence used in manual assertion
Supporting statements:
In this study, the phosphorylation of b-catenin at Ser45 was characterised using a phospho-specific antibody.
Protein: DP01119 (UniProt P35222)
Region: residues 17	to 21
Annotation: ubiquitination display site (Disorder function)
Evidence: enzymatic activity assay evidence used in manual assertion
Supporting statements:
These findings, together with the conservation of this lysine among β-catenin orthologs and paralogues (Table 1), suggest that Lys19 is a ubiquitination site of β-catenin in vivo.
Cross-references: PDB:1P22
Protein: DP01119 (UniProt P35222)
Region: residues 21	to 25
Annotation: glycosylation display site (Disorder function)
Evidence: immunodetection assay evidence used in manual assertion
Supporting statements:
Serine 23 of β-catenin was determined as a site for O-GlcNAc modification which regulated its subcellular distribution, its interactions with cellular partners and consequently its transcriptional activity.
Protein: DP01119 (UniProt P35222)
Region: residues 39	to 43
Annotation: phosphorylation display site (Disorder function)
Evidence: immunodetection assay evidence used in manual assertion
Supporting statements:
LiCl is a potent GSK-3 inhibitor (Stambolic et al. 1996, Hedgepeth et al. 1997) and indeed suppressed T41/S37/S33 but not S45 phosphorylation (Figure 2B).
Protein: DP01119 (UniProt P35222)
Region: residues 35	to 39
Annotation: phosphorylation display site (Disorder function)
Evidence: immunodetection assay evidence used in manual assertion
Supporting statements:
LiCl is a potent GSK-3 inhibitor (Stambolic et al. 1996, Hedgepeth et al. 1997) and indeed suppressed T41/S37/S33 but not S45 phosphorylation (Figure 2B).
Protein: DP01119 (UniProt P35222)
Region: residues 31	to 35
Annotation: phosphorylation display site (Disorder function)
Evidence: immunodetection assay evidence used in manual assertion
Supporting statements:
LiCl is a potent GSK-3 inhibitor (Stambolic et al. 1996, Hedgepeth et al. 1997) and indeed suppressed T41/S37/S33 but not S45 phosphorylation (Figure 2B).
Protein: DP01119 (UniProt P35222)
Region: residues 21	to 25
Annotation: phosphorylation display site (Disorder function)
Evidence: immunodetection assay evidence used in manual assertion
Supporting statements:
These data indicate that the S23 and S29 residues are indeed phosphorylated in vivo.
Protein: DP01119 (UniProt P35222)
Region: residues 27	to 31
Annotation: phosphorylation display site (Disorder function)
Evidence: immunodetection assay evidence used in manual assertion
Supporting statements:
These data indicate that the S23 and S29 residues are indeed phosphorylated in vivo.
Protein: DP01119 (UniProt P35222)
Region: residues 47	to 51
Annotation: acetylation display site (Disorder function)
Evidence: immunodetection assay evidence used in manual assertion
Supporting statements:
In line with loss of SIRT1 repression, expression of wild type MCC but not MCC‐R506Q mutant resulted in β‐cat‐K49 deacetylation (Fig. 6c).
Protein: DP01119 (UniProt P35222)
Region: residues 62	to 66
Annotation: phosphorylation display site (Disorder function)
Evidence: immunodetection assay evidence used in manual assertion
Supporting statements:
PTK6 directly phosphorylates beta-catenin on Tyr64, Tyr142, Tyr331 and/or Tyr333, with the predominant site being Tyr64.
Protein: DP01119 (UniProt P35222)
Region: residues 772	to 781
Annotation: protein binding (Molecular function)
Evidence: isothermal titration calorimetry evidence used in manual assertion
Supporting statements:
ITC experimentsusing our present system show weak binding of Lin-7 to the C-terminal of β-catenin (SupplementaryData Fig. 5).
Protein: DP01119 (UniProt P35222)
Region: residues 683	to 781
Annotation: protein binding (Molecular function)
Evidence: bait-prey hybrid interaction evidence used in manual assertion
Supporting statements:
To test whether Fhit directly interacts with LEF-1 or β-catenin, in vitro pull-down experiments with purified recombinant fusion proteins were performed. In contrast to Hint1, Fhit directly associates with β-catenin.
Protein: DP01119 (UniProt P35222)
Region: residues 31	to 35
Annotation: regulation of protein ubiquitination (Biological process)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
We demonstrate that the mutants D32A and G34A exhibit no change in phosphorylation by GSK3β, but display reduced ubiquitination compared to wild-type and S33A mutant β-catenin.
D32A and G34A were greatly reduced compared to WT β-catenin in their degree of ubiquitination.
Since the phosphorylation status of D32A and G34A is normal, we concluded that alterations to the ubiquitination status of β-catenin are due to its interaction with the ubiquitin machinery and its function as a ubiquitin substrate.
Protein: DP01119 (UniProt P35222)
Region: residues 33	to 37
Annotation: phosphorylation display site (Disorder function)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
A greater than 50% reduction in phosphorylation was seen in the QUAD (S33AS37AT41AS45A) and S33AS37A mutants, as expected for partial serine/threonine mutants of β-catenin. Since there are multiple kinase sites that are substrates for GSK3β, no β-catenin mutants showed complete loss of phosphorylation similar to the α-catenin control. 
The double serine mutant S33S37A served as a negative control, since β-TrCP-mediated ubiquitination of β-catenin is phosphorylation dependent.
Protein: DP01119 (UniProt P35222)
Region: residues 32	to 37
Annotation: ubiquitin protein ligase binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The phosphoserine, aspartic acid, and hydrophobic residues of the destruction motif are recognized directly by contacts from β-TrCP1.
The destruction motif comprises the 32-37 region. 
These findings support the structure-based conclusion that Asp32, pSer33, pSer37, and Gly34 are critical for β-TrCP1-β-catenin binding and specificity, while Ile35, which makes fewer contacts, plays a smaller role.
Cross-references: PDB:1P22
ELM:deg_scf_trcp1_1
Protein: DP01119 (UniProt P35222)
Region: residues 30	to 40
Annotation: disorder to order (Structural transition)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Of the 26 β-catenin residues in the crystals, only an 11 residue segment (residues 30 to 40), centered on the doubly phosphorylated destruction motif (residues 32 to 37), is ordered in the structure.
Cross-references: PDB:1P22
Protein: DP01119 (UniProt P35222)
Region: residues 17	to 21
Annotation: ubiquitination display site (Disorder function)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
When the R7 mutant of ubiquitin is used, the SCFβ-TrCP1 monoubiquitinates the doubly phosphorylated β-catenin (lane 3) and IκBα (lane 6) peptides at comparable rates. The reaction is dependent on Lys19 in the β-catenin peptide (lane 5) and is specific for β-TrCP1 because Cul1-Rbx1 (lane 7) or SCFSkp2-Cks1 (lane 8) cannot substitute for SCFβ-TrCP1. 
These findings, together with the conservation of this lysine among β-catenin orthologs and paralogues (Table 1), suggest that Lys19 is a ubiquitination site of β-catenin in vivo.
Protein: DP01120 (UniProt P24864)
Region: residues 360	to 373
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The N-terminal 14 residues, which contain the phosphorylated Ser372 (pSer372), and the C-terminal five residues are not visible in the electron density maps and are presumably disordered.
Cross-references: PDB:2OVQ
Protein: DP01121 (UniProt Q38825)
Region: residues 82	to 94
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
above the auxin-binding site, the highly coiled IAA7 peptide is docked to the upper part of the surface pocket
Cross-references: PDB:2P1Q
Protein: DP01121 (UniProt Q38825)
Region: residues 82	to 94
Annotation: protein binding (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
peptide adopts a highly coiled conformation and fills the TIR1 pocket with the central hydrophobic consensus motif
Protein: DP01122 (UniProt Q27934)
Region: residues 107	to 130
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
[degron DEG_SIAH_1] peptide used in the crystallization included residues 107–130. Thus, residues 108–113 and 125–130 were flexible and could not be modeled.
Protein: DP01122 (UniProt Q27934)
Region: residues 107	to 130
Annotation: protein binding (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
degron motif (PXAXVXP) (as defined by House et al., 2003) that do interact with Siah include Arg115 and Thr123
Protein: DP01123 (UniProt P43403)
Region: residues 258	to 302
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Two regions of the molecule appeared to be disordered and were not modeled. These were the N-terminal portion of the SH2-kinase linker (residues 258 to 302) and a portion of the activation loop of the kinase domain (residues 484 to 500).
Cross-references: PDB:4K2R
Protein: DP01123 (UniProt P43403)
Region: residues 484	to 500
Annotation: phosphorylation display site (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Tyr493 located in the disordered part of the ZAP70 activation loop is phosphorylated
Protein: DP01124 (UniProt Q9Y261)
Region: residues 240	to 258
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
"the electron density of wing 2 (residues 240–258) in the FOXA2-DBD/DBE2 structure could not be observed. This result suggested that wing 2 was flexible and disordered in the crystal."
Cross-references: PDB:5X07
Protein: DP01124 (UniProt Q9Y261)
Region: residues 240	to 258
Annotation: nucleic acid binding (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
"To test whether wing 2 contributes to FOXA2-DBD/DNA binding, we constructed a truncated fragment of FOXA2 without wing 2 and measured the DNA binding ability using ITC. The binding affinity of FOXA2 was reduced by ∼30-fold when the C-terminal wing 2 region was removed. These results suggested that wing 2 of FOXA2 was important for optimal DNA binding."
Protein: DP01127 (UniProt Q8VHK2)
Region: residues 603	to 1430
Annotation: disorder (Structural state)
Evidence: proton-based nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
The one-dimensional 1H-NMR spectra of the PRD-His fragments (prolin rich domains) also underscores a largely disordered conformational state. Chemical shifts show a poor dispersion, i.e. amide proton signals are clustered within a half-p.p.m. range centred at 8 p.p.m., whereas the methyl group protons are clustered at around 1 p.p.m. Such a limited dispersion and signal overlap in 1H chemical shifts are typical of IDPs.
Protein: DP01127 (UniProt Q8VHK2)
Region: residues 603	to 1430
Annotation: protein binding (Molecular function)
Evidence: proton-based nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
The molecular mechanism of the function of Caskins is not known at present. As a result of their large size, the capacity to bind multiple partners and the lack of catalytic domains, they probably fall into the class of scaffold proteins, which bind components of a signal transduction pathway simultaneously and ensure the speciﬁcity and efﬁciency of signal propagation. As the long regions of these proteins often lack any sequence similarity to other proteins and appear to lack folded structural domains, we anticipated that structural disorder may be a general feature of scaffold proteins. The ﬁrst and second proline-rich regions of Caskin1 (PRD1-GST and PRD2-GST were able to interact with the GFP-Abi2 protein.
Protein: DP01127 (UniProt Q8VHK2)
Region: residues 603	to 1430
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The CD spectrum of PRD-His shows a minimum at 202 nm, which is characteristic of a protein in a largely disordered conformation. The CD spectra of the separate PRDs also show characteristic minima around 200 nm, which underscores the unstructured nature of these regions.
Protein: DP01127 (UniProt Q8VHK2)
Region: residues 603	to 1430
Annotation: disorder (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
PRD-His shows a greater sensitivity to proteolysis with a protease of wide substrate speciﬁcity, subtilisin, than does the globular control protein BSA; this provides an indication of its disordered conformation.
Protein: DP01127 (UniProt Q8VHK2)
Region: residues 603	to 1430
Annotation: disorder (Structural state)
Evidence: chromatography evidence used in manual assertion
Supporting statements:
Gel ﬁltration data also verify the disordered nature of the proline-rich region, as the apparent molecular mass (mapp) of PRD-His (334.5 kDa) is 3.9 times higher than the real value (85.9 kDa).
Protein: DP01128 (UniProt O43806)
Region: residues 25	to 93
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Before binding, p27 is at least partially disordered and folds upon binding its Cdk/cyclin targets.
Protein: DP01128 (UniProt O43806)
Region: residues 25	to 93
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Before binding, p27 is at least partially disordered and folds upon binding its Cdk/cyclin targets.
Protein: DP01128 (UniProt O43806)
Region: residues 25	to 93
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Before binding, p27 is at least partially disordered and folds upon binding its Cdk/cyclin targets.
Protein: DP01128 (UniProt O43806)
Region: residues 22	to 97
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
In the presence of macromolecular crowding agents, neither the intrinsically disordered C-terminal activation domain of c-Fos nor the kinase-inhibition domain of p27Kip1 undergoes any significant conformational change that is detected by changes in either circular dichroism or fluorescence spectra.
While intrinsically disordered at physiological temperatures, marginally stable helix is present in p27ID at 5 °C (Figure 2A).8 Addition of TFE to p27ID induced a marked change in the CD spectrum indicative of a large increase in helix content (Figure 2A). However addition of several crowding agents did not induce any significant change in the CD spectrum of p27ID above 212 nm that reflects formation of helical or strand secondary structure (Figure 2B).
A decrease in the intensity of the CD signal of p27ID at 204 nm was observed in the presence of the 37.5 and 77 kDa dextrans, and the fluorescence emission intensity of p27ID at 350 nm was reduced in the presence of 77 kDa dextran and Ficoll 70 (as observed for FosAD).
Protein: DP01128 (UniProt O43806)
Region: residues 22	to 97
Annotation: disorder (Structural state)
Evidence: intrinsic fluorescence-based protein conformation evidence
Supporting statements:
In the presence of macromolecular crowding agents, neither the intrinsically disordered C-terminal activation domain of c-Fos nor the kinase-inhibition domain of p27Kip1 undergoes any significant conformational change that is detected by changes in either circular dichroism or fluorescence spectra.
Crowding agents did not affect the p27ID fluorescence emission maximum of 350 nm (Figure 2C) or did not affect significantly the fluorescence spectrum of ANS in the presence of p27ID (data not shown).
A decrease in the intensity of the CD signal of p27ID at 204 nm was observed in the presence of the 37.5 and 77 kDa dextrans, and the fluorescence emission intensity of p27ID at 350 nm was reduced in the presence of 77 kDa dextran and Ficoll 70 (as observed for FosAD).
Protein: DP01128 (UniProt O43806)
Region: residues 1	to 158
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The CD spectrum of full-length human p27 is characteristic of an unfolded protein (Figure 3). The minimum at 200 nm is indicative of an unfolded conformation, and the weak negative shoulder at 222 nm suggests the absence of significant amounts of helix or β-strand. The helix content is estimated at 2 or 6% from [θ]222 or CDPro, respectively. The results indicate that full-length p27, while active as a Cdk inhibitor, is largely unfolded.
Protein: DP01128 (UniProt O43806)
Region: residues 22	to 97
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
We report here a study of the functional consequences of conformational preferences in the intrinsically disordered human p27 Cdk-inhibition domain. Rather than existing as a random coil, the p27 Cdk-inhibition domain exhibits a propensity to form preexisting helical structure that corresponds to the α-helix, but not the 310 helix, that forms upon binding cyclin A-Cdk2.
The CD spectra of p27ID in kinase-assay buffer at 30 and 60 °C are also characteristic of an unfolded protein (Figure 5). The minimum at 204 nm is indicative of an unfolded conformation, and the weak negative shoulder at 222 nm suggests the absence of significant amounts of helix or β-strand.
Protein: DP01128 (UniProt O43806)
Region: residues 22	to 97
Annotation: disorder (Structural state)
Evidence: proton-based nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
The NMR properties of p27ID at 30 °C are characteristic of an unfolded protein. 1H chemical-shift ranges were obtained from DQF COSY (pH 4.4) or TOCSY−HSQC (pH 7.0) spectra using gradients for solvent suppression. The Hα and HN chemical shifts at pH 4.4 span 3.9−4.6 and 7.8−8.6 ppm, respectively, and at pH 7.0 span 4.05−4.59 and 7.77−8.58 ppm, respectively (data not shown). These chemical-shift ranges are typical of those observed in unfolded proteins ( 28). The amide 1H−15N NOE is negative (approximately −1 to −3.9) for each of 64 resolved mainchain amide cross-peaks at pH 4.4 (from an expected total of 70; data not shown), indicating that the p27ID main chain is highly flexible with motion on a time scale characteristic of unfolded proteins ( 29, 30).
Protein: DP01128 (UniProt O43806)
Region: residues 22	to 97
Annotation: protein binding (Molecular function)
Evidence: enzyme inhibition evidence used in manual assertion
Supporting statements:
p27ID binds cyclin A-Cdk2 with a Kd of 8 ± 2 nM at 30 °C (Figure 9).
Figure 9 Kd determinations from cyclin A-Cdk2 inhibition assays (50 nM cyclin A-Cdk2, 25 mM HEPES, 50 mM NaCl, and 5 mM MgCl2, pH 7.5, 30 °C).
Protein: DP01129 (UniProt P12296)
Region: residues 1	to 19
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
The majority of LM0P was random coil, interspersed with four short helical segments (Figs. 1 and 2 A and B). As defined by TALOS+ algorithms (17), the α1 and α2 segments (aa 23–26 and 29–31) spanned the COOH-half of the zinc finger. The α3 and α4 motifs, in the hinge region (aa 45–49) and near the COOH tail (aa 63–66), were less well defined.
The sequence of LM is 4 aa longer at the N-terminal.
Cross-references: PDB:2MMH
PDB:2MMI
PDB:2MML
PDB:2MMK
Protein: DP01129 (UniProt P12296)
Region: residues 27	to 41
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
The majority of LM0P was random coil, interspersed with four short helical segments (Figs. 1 and 2 A and B). As defined by TALOS+ algorithms (17), the α1 and α2 segments (aa 23–26 and 29–31) spanned the COOH-half of the zinc finger. The α3 and α4 motifs, in the hinge region (aa 45–49) and near the COOH tail (aa 63–66), were less well defined.
The sequence of LM is 4 aa longer at the N-terminal.
Cross-references: PDB:2MMH
PDB:2MMI
PDB:2MML
PDB:2MMK
Protein: DP01129 (UniProt P12296)
Region: residues 45	to 59
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
The majority of LM0P was random coil, interspersed with four short helical segments (Figs. 1 and 2 A and B). As defined by TALOS+ algorithms (17), the α1 and α2 segments (aa 23–26 and 29–31) spanned the COOH-half of the zinc finger. The α3 and α4 motifs, in the hinge region (aa 45–49) and near the COOH tail (aa 63–66), were less well defined.
The sequence of LM is 4 aa longer at the N-terminal.
Cross-references: PDB:2MMH
PDB:2MMI
PDB:2MML
PDB:2MMK
Protein: DP01129 (UniProt P12296)
Region: residues 1	to 19
Annotation: entropic chain (Disorder function)
Evidence: nuclear magnetic resonance evidence used in manual assertion
Supporting statements:
Surprisingly, when one or two phosphates were added, the overall proteins still configured largely as random coil (Fig. 1 and Fig. S6 B–D).
The remainder of each protein is random coil.
The figure 1 shows the secondary when the protein is without PTMs, phosphorilated or binding protein Ran. The secondary structure along the sequence is shown and the rest of the protein is random coil.
Cross-references: PDB:2MMH
PDB:2MMI
PDB:2MML
PDB:2MMK