LiteFold/DisProt huggingface dataset:
Protein: DP02812 (UniProt A6NI73)
Region: residues 147	to 157
Annotation: glycosylation display site (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Thus, this loop is more flexible than the equivalent region in the other LRC receptors. Since the predicted N-linked glycosylation site (Asn116) was located on the disordered AB loop in D2, the attached sugar moiety might be expected to be very mobile
Disordered residue 106-116 of the crystal structure corresponds to sequence residues 147-157, therefore the glycosylated residue is Asn157
Cross-references: PDB:2D3V
Protein: DP02815 (UniProt P62330)
Region: residues 34	to 56
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The crystal structure of Δ13Arf6-GDP reveals an unprecedented unfolding of the GTPase core β-strands, which is fully accounted for by small-angle X-ray scattering data in solution and by ab initio three-dimensional envelope calculation. NMR chemical shifts identify this structural disorder in Δ13Arf6-GDP, 
The structure of Δ13Arf6-GDP in the crystal and in solution was analyzed by the combination of structural and biophysical methods, revealing a partial unfolding of the switch 1 and interswitch regions unique to this small GTPase. 
Residues affected by structural changes extend from Lys34 in strand β1′, which corresponds to switch 1 in Arf-GDP structures, to Asn56 after strand β2 (interswitch) in the central β-sheet. The β1′–β2 region is essentially disordered in one Δ13Arf6-GDP subunit of the asymmetric unit, while in the other subunit, β1′–β2
strands β1′ and β2, which form switch 1 and part of the interswitch in Arf6-GDPFL, are relocated as far as 47 Å away from their original positions, yielding a flexible loop that protrudes from the small GTPase core
Cross-references: PDB:3N5C
Protein: DP02815 (UniProt P62330)
Region: residues 34	to 56
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The crystal structure of Δ13Arf6-GDP reveals an unprecedented unfolding of the GTPase core β-strands, which is fully accounted for by small-angle X-ray scattering data in solution and by ab initio three-dimensional envelope calculation. NMR chemical shifts identify this structural disorder in Δ13Arf6-GDP, 
The structure of Δ13Arf6-GDP in the crystal and in solution was analyzed by the combination of structural and biophysical methods, revealing a partial unfolding of the switch 1 and interswitch regions unique to this small GTPase. 
NMR: NMR chemical shifts provide a powerful means of detecting local disorder in proteins…It features a significant number of peaks that are too broad to be resolved individually, and a paucity of peaks in the ranges 8.5–10 ppm (1 H) and 123– 133 ppm (15N), which generally correspond to βsheet structures….fully consistent with the unfolding of β-strands and with the enrichment in flexible structures, as seen in the Δ13Arf6-GDP crystal
strands β1′ and β2, which form switch 1 and part of the interswitch in Arf6-GDPFL, are relocated as far as 47 Å away from their original positions, yielding a flexible loop that protrudes from the small GTPase core
Cross-references: PDB:3N5C
Protein: DP02815 (UniProt P62330)
Region: residues 34	to 56
Annotation: disorder (Structural state)
Evidence: small-angle X-ray scattering evidence used in manual assertion
Supporting statements:
The crystal structure of Δ13Arf6-GDP reveals an unprecedented unfolding of the GTPase core β-strands, which is fully accounted for by small-angle X-ray scattering data in solution and by ab initio three-dimensional envelope calculation. NMR chemical shifts identify this structural disorder in Δ13Arf6-GDP, 
The structure of Δ13Arf6-GDP in the crystal and in solution was analyzed by the combination of structural and biophysical methods, revealing a partial unfolding of the switch 1 and interswitch regions unique to this small GTPase. 
SAXS: The SAXS envelope of Arf6- GDPFL was essentially globular and superimposed very well with the crystal structure of Arf6-GDPFL (Fig. 3c). In contrast, the Δ13Arf6-GDP SAXS envelope displayed a large protrusion (Fig. 3d). Remarkably, the protrusion readily accommodated the partially unfolded β1′–β2 strands from the Δ13Arf6-GDP crystal structure (Fig. 3d), suggesting that a similar unfolding takes place in solution
strands β1′ and β2, which form switch 1 and part of the interswitch in Arf6-GDPFL, are relocated as far as 47 Å away from their original positions, yielding a flexible loop that protrudes from the small GTPase core
Cross-references: PDB:3N5C
Protein: DP02815 (UniProt P62330)
Region: residues 34	to 56
Annotation: disorder to order (Structural transition)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The crystal structure of Δ13Arf6-GDP reveals an unprecedented unfolding of the GTPase core β-strands, which is fully accounted for by small-angle X-ray scattering data in solution and by ab initio three-dimensional envelope calculation. NMR chemical shifts identify this structural disorder in Δ13Arf6-GDP, 
The structure of Δ13Arf6-GDP in the crystal and in solution was analyzed by the combination of structural and biophysical methods, revealing a partial unfolding of the switch 1 and interswitch regions unique to this small GTPase. 
Altogether, this is one of the largest conformational departures from the classical fold of a small GTPase....This indicates that the local disorder in Δ13Arf6- GDP is not an intrinsic property of Δ13Arf6, but is specific for its GDP-bound form


strands β1′ and β2, which form switch 1 and part of the interswitch in Arf6-GDPFL, are relocated as far as 47 Å away from their original positions, yielding a flexible loop that protrudes from the small GTPase core
Cross-references: PDB:3N5C
Protein: DP02815 (UniProt P62330)
Region: residues 34	to 56
Annotation: molecular function regulator (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The crystal structure of Δ13Arf6-GDP reveals an unprecedented unfolding of the GTPase core β-strands, which is fully accounted for by small-angle X-ray scattering data in solution and by ab initio three-dimensional envelope calculation. NMR chemical shifts identify this structural disorder in Δ13Arf6-GDP [...] Taken together, these experiments suggest an unfolding model for the nucleotide switch of Arf6 and shed new light on its biochemical differences with Arf1.
The structure of Δ13Arf6-GDP in the crystal and in solution was analyzed by the combination of structural and biophysical methods, revealing a partial unfolding of the switch 1 and interswitch regions unique to this small GTPase. 

Altogether, this is one of the largest conformational departures from the classical fold of a small GTPase [...] the 1 H–15N HSQC spectrum of Δ13Arf6-GTP is very well defined and is representative of a well-ordered conformation (Fig. 2, blue). This indicates that the local disorder in Δ13Arf6- GDP is not an intrinsic property of Δ13Arf6, but is specific for its GDP-bound form


Altogether, our results suggest that the GDP/GTP structural switch of Arf6 may follow a structural route different from that of Arf1. The interswitch toggle of Arf6 may proceed through a local unfolding of the interswitch, possibly via a GEFbound intermediate in which Arf6 resembles the Δ13Arf6-GDP structure (Fig. 5d)
The conformational switch is proposed to participate in the nucleotide exchange (GTP/GDP) function of Arf6
Cross-references: PDB:3N5C
Protein: DP02816 (UniProt P48740-3)
Region: residues 364	to 380
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The 17 C-terminal residues that are unique to MAP-1 are disordered in the crystal.
Protein: DP02817 (UniProt Q64373)
Region: residues 28	to 81
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
When Bcl-xl F105A (form II) and Bcl-xl F105A (form I) were superposed for 142 Ca (except for Ser28 to Ile81), the overlay, with an RMSD of 0.43 Å, suggested that they were very similar overall


During the course of determining the three-dimensional structure of Bcl-xl, a large region of Bcl-xl was found to be unstructured in the wild type and Y101A and F105A mutant forms, as determined by previous NMR and X-ray crystallographic techniques [3–6,9]. 
This and previous structures show that the region 28-81 is disordered with missing electron density
Cross-references: PDB:3IHC
Protein: DP02817 (UniProt Q64373)
Region: residues 28	to 81
Annotation: molecular recognition display site (Disorder function)
Evidence: immunodetection assay evidence used in manual assertion
Supporting statements:
The rate of nonenzymatic deamidation of two asparagines in the antiapoptotic protein Bcl-xL is accelerated by this increase in pH. Deamidation of these asparagines is a signal for the degradation of Bcl-xL, which is a component of the apoptotic response to DNA damage […]we present evidence that deamidation of human Bcl-xL is intramolecularly catalyzed in a manner that is dependent upon these histidines. Further, we present evidence that these histidines act as a pH-sensitive switch that enhances the effect of the increase in pH on the rate of Bcl-xL deamidation
We have previously demonstrated that the antiapoptotic Bcl-2 family member Bcl-xL undergoes deamidation at Asn 52 and Asn 66 when susceptible tumor cells are treated with DNAdamaging antineoplastic agents [...] We now report that human Bcl-xL contains histidines in close proximity to each of its two deamidation sites and that such histidines are conserved throughout the Bcl-xL p
Indeed, we show here that deamidation of human Bcl-xL is intramolecularly catalyzed in a manner that involves these highly conserved histidines and that treatment of susceptible tumor cells with DNA-damaging agents increases the catalytic activity.

Additionally, we consistently found that total Bcl-xL(H58A/H71A) is markedly increased relative to total wild-type Bcl-xL in cisplatin-treated cells (Fig. 5A). Finally, we found that Bcl-xL(H58A/H71A) is deamidated at a slower rate than wild-type Bcl-xL in cells treated with cycloheximide (Fig. 5B)
All residues that are deamidated (N52 and N66) as well as the catalytic histidines (H58 and H71) are within the IDP region
Protein: DP02818 (UniProt Q07157)
Region: residues 589	to 627
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The previous structures of the SG domains of ZO proteins revealed flexibility between the SH3 and GUK domains (that is, the structure of each individual domain is rather rigid, but the relative domain-domain conformation is variable).
The U5 region is a variable surface loop sequence near the C-terminal part of the SH3 domain. It is present in the PSG construct but did not show any traceable electron density.
Cross-references: PDB:3TSZ
PDB:3TSW
Protein: DP02818 (UniProt Q07157)
Region: residues 589	to 627
Annotation: flexible linker (Disorder function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The previous structures of the SG domains of ZO proteins revealed flexibility between the SH3 and GUK domains (that is, the structure of each individual domain is rather rigid, but the relative domain-domain conformation is variable).
The U5 region is a variable surface loop sequence near the C-terminal part of the SH3 domain. It is present in the PSG construct but did not show any traceable electron density.
Cross-references: PDB:3TSZ
PDB:3TSW
Protein: DP02818 (UniProt Q07157)
Region: residues 675	to 687
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Final built models comprised the following residues: PSG 417–587, 629–674, and 688–803. Residue Lys629 was modeled as an alanine (residues: 588–628 (U5) and 675–687 were lacking unambiguous electron density); PSG+JAM-A 421–588, 628–684, and 687–802 (residues: 417–420, 589–627 (U5), 685, 686, and 803 were lacking unambiguous electron density); PDZ3 420–512 (residues: 417–419 and 513–516 were lacking unambiguous electron density).
Cross-references: PDB:3TSW
Protein: DP02818 (UniProt Q07157)
Region: residues 265	to 420
Annotation: disorder (Structural state)
Evidence: author statement used in manual assertion
Supporting statements:
All 4 TJP1 variants are predicted to be deleterious and affect highly conserved amino acids, either at the GUK (guanylate kinase)–like domain (p.(Y669C)) or at the disordered region of the protein between the PDZ2 and PDZ3 domains (p.(R265W), p.(S329L), and p.(D360V)).
Since the PDZ2 domain comprises the 186-264 region, and the PDZ3 domain comprises the 421-502 region, the authors are referring to the 265-420 region as disordered.
Protein: DP02818 (UniProt Q07157)
Region: residues 795	to 1631
Annotation: disorder (Structural state)
Evidence: author statement used in manual assertion
Supporting statements:
ZO-1/2 harbors three consecutive PSD-95/Discs large/and ZO-1 (PDZ) domains at the N-terminus of the protein. They follow a Src homology domain, the guanylate kinase (GUK) domain, and a long intrinsically disordered region that contains the actin-binding site (Figure 1c).
In the Figure 1c the authors shows the IDR spans between the GUK domain (606-794) and the ZU5 domain (1632-1748).
Protein: DP02819 (UniProt Q62420)
Region: residues 1	to 26
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues 1–26 are disordered at the N termini, which both point in the direction of the distal ends of the crescent-shaped dimer.
Cross-references: PDB:1ZWW
Protein: DP02819 (UniProt Q62420)
Region: residues 67	to 86
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues 67–86 (in the second protomer, residues 70–84) are disordered in the structure and they could extend either sideward or perpendicularly to the concave surface.
Cross-references: PDB:1ZWW
Protein: DP02819 (UniProt Q62420)
Region: residues 67	to 86
Annotation: molecular function regulator (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Here, we present the 2.3 A crystal structure of the endophilin-A1 BAR domain, which has been suggested to function in inducing and sensing membrane curvature at the site of endocytosis.
The endophilin-1A BAR domain thus constitutes a new variant of a BAR domain, and it may link endophilin-1A BAR function to calcium regulation of endocytosis.
Cross-references: PDB:1ZWW
Protein: DP02820 (UniProt Q62264)
Region: residues 77	to 104
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The model spans residues 8–149, although residues 46–48 and 77–104 are poorly ordered and were not placed in the electron density.
Cross-references: PDB:3ONT
Protein: DP02820 (UniProt Q62264)
Region: residues 1	to 150
Annotation: protein binding (Molecular function)
Evidence: co-immunoprecipitation evidence used in manual assertion
Supporting statements:
Interaction of S14 and MIG12 in Cultured Cells.
Protein: DP02820 (UniProt Q62264)
Region: residues 1	to 150
Annotation: molecular function inhibitor activity (Molecular function)
Evidence: sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion
Supporting statements:
The structure of S14 suggests a mechanism whereby heterodimer formation with MIG12 attenuates the ability of MIG12 to activate ACC.
S14 Knockdown Increases ACC Polymerization and Activity in Vivo.
Increasing S14 levels resulted in reduced ACC polymerization (Fig. 5A) and less MIG12 incorporation into ACC polymers
Cross-references: PDB:3ONT
Protein: DP02822 (UniProt Q8IVH8)
Region: residues 315	to 380
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The density for the compound was clearly distinct, as was in general the backbone density for residues between 13 and 314 (the site of Clostripain cleavage in solution), but the residues that follow were disordered.
Cross-references: PDB:5J5T
Protein: DP02822 (UniProt Q8IVH8)
Region: residues 315	to 380
Annotation: phosphorylation display site (Disorder function)
Evidence: chromatography evidence used in manual assertion
Supporting statements:
Phosphomapping of the isolated protein band (MS Bioworks) demonstrated that several sites were phosphorylated, namely: Thr38, Thr145, Thr164, Ser170, Thr227, Ser280, Thr327, Ser329, Thr332, and Tyr379. Because GLK is a Ser/Thr kinase, we reasoned that the Tyr379 phosphorylation must have been the result of another kinase acting on GLK as a substrate. The phosphorylation at Ser170 is likely due to autophosphorylation.
Cross-references: PDB:5J5T
Protein: DP02822 (UniProt Q8IVH8)
Region: residues 315	to 380
Annotation: flexible linker (Disorder function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The disordered region is localized between the kinase domain and the CNH domain
Cross-references: PDB:5J5T
Protein: DP02823 (UniProt Q9UKY0)
Region: residues 24	to 51
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The NMR structure of the recombinant human doppel protein, hDpl(24-152), contains a flexibly disordered "tail" comprising residues 24-51, and a globular domain extending from residues 52 to 149 for which a detailed structure was obtained.
The structure of hDpl(24–152) (Figure 1) contains a well defined globular domain and a flexibly disordered tail of residues 24–50, as is seen readily from the relative intensities of the 15N{1H}-NOEs (Supplementary Material, Figure S2a).
When compared to the remainder of the globular domain, there is a low propensity of medium-range and long-range NOE constraints in this region (Supplementary Material, Figure S2b), but the observation of positive 15N{1H}-NOEs for all amide moieties that were assigned in this region indicates that there is static disorder rather than increased intramolecular mobility.
Cross-references: PDB:1LG4
Protein: DP02824 (UniProt Q14019)
Region: residues 132	to 142
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final model fits the electron density map very well with good geometry. The model includes 131 residues of CLP (of a total of 142 residues).
N-terminal residues (3–0) are extended straight from β1 while C-terminal residues after Lys 131 cannot be defined by the electron density map.
The flexible C-terminal tail for CLP is 11 residues in length, while those for actophorin and yeast cofilin are 3 and 5, respectively.
Cross-references: PDB:1VFQ
Protein: DP02824 (UniProt Q14019)
Region: residues 132	to 142
Annotation: molecular adaptor activity (Molecular function)
Evidence: combinatorial experimental and author inference evidence contained in single publication used in manual assertion
Supporting statements:
LP also has a long flexible C terminus composed of 11 residues: AGGANYDAQTE. The first four residues form a hinge region, while the last seven make a good combination for molecular recognition. This flexible C terminus is sited not far from the region containing α1–β2, α4–β5 and β4–β5 loops. As a consequence, the flexible C terminus of CLP may be used to bind F-actin and/or other proteins.
Its long flexible C-terminal arm may help CLP binding other molecules.
In the CLP–F-actin contact surface, besides the complementary morphology of the two polymers, their flexible C-terminal tails could assist the CLP polymer to bind to F-actin.
Cross-references: PDB:1VFQ
Protein: DP02825 (UniProt P31153)
Region: residues 116	to 126
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The structure of (PPNP-bound) MATα2 has a disordered gating loop, providing direct evidence against the idea that it provides the energy for the opening of the gate.
The two ordered sites contain SAMe, PPNP, Mg2+, and K+, whereas the disordered sites contain only an ethylene glycol molecule as a result of the cryoprotection. The structure of (PPNP-bound) MATα2 has a disordered gating loop, and a comparison of the PPNP-bound, MAT(α2)4(βV2)2, and SAMe+ADO+MET+PPNP structures shows that the gate is open when active site is occupied by PPNP.
Cross-references: PDB:5A19
Protein: DP02825 (UniProt P31153)
Region: residues 116	to 126
Annotation: entropic chain (Disorder function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The structure of (PPNP-bound) MATα2 has a disordered gating loop, providing direct evidence against the idea that it provides the energy for the opening of the gate.
The two ordered sites contain SAMe, PPNP, Mg2+, and K+, whereas the disordered sites contain only an ethylene glycol molecule as a result of the cryoprotection. The structure of (PPNP-bound) MATα2 has a disordered gating loop, and a comparison of the PPNP-bound, MAT(α2)4(βV2)2, and SAMe+ADO+MET+PPNP structures shows that the gate is open when active site is occupied by PPNP.
The active site gating loop gains order and closes upon substrate binding.
Cross-references: PDB:5A19
Protein: DP02825 (UniProt P31153)
Region: residues 116	to 126
Annotation: small molecule binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The structure of (PPNP-bound) MATα2 has a disordered gating loop, providing direct evidence against the idea that it provides the energy for the opening of the gate.
The two ordered sites contain SAMe, PPNP, Mg2+, and K+, whereas the disordered sites contain only an ethylene glycol molecule as a result of the cryoprotection. The structure of (PPNP-bound) MATα2 has a disordered gating loop, and a comparison of the PPNP-bound, MAT(α2)4(βV2)2, and SAMe+ADO+MET+PPNP structures shows that the gate is open when active site is occupied by PPNP.
Cross-references: PDB:5A19
Protein: DP02825 (UniProt P31153)
Region: residues 116	to 126
Annotation: disorder to order (Structural transition)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The structure of (PPNP-bound) MATα2 has a disordered gating loop, providing direct evidence against the idea that it provides the energy for the opening of the gate.
The two ordered sites contain SAMe, PPNP, Mg2+, and K+, whereas the disordered sites contain only an ethylene glycol molecule as a result of the cryoprotection. The structure of (PPNP-bound) MATα2 has a disordered gating loop, and a comparison of the PPNP-bound, MAT(α2)4(βV2)2, and SAMe+ADO+MET+PPNP structures shows that the gate is open when active site is occupied by PPNP.
It has been suggested that when the active site is occupied, the loop is closed like a gate, but when the active site is empty, the loop becomes invisible in the structure, presumably resulting from an open dynamic gate.
The active site gating loop gains order and closes upon substrate binding.
Cross-references: PDB:5A19
PDB:5A1G
PDB:5A1I