LiteFold/DisProt huggingface dataset:
Protein: DP01502 (UniProt P33328)
Region: residues 1	to 91
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Snc2p appears to be unfolded as judged by CD spectroscopy and amide proton exchange experiments, in accord with previous reports for Snc2p homologs. Therefore, the SNARE regions that form binary and ternary complexes efficiently all seem, individually, to lack significant regular secondary structure.
Protein: DP01502 (UniProt P33328)
Region: residues 1	to 91
Annotation: disorder to order (Structural transition)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The addition of Snc2p to Sso1CT–Sec9CT binary complexes resulted in a further large increase in α-helix content, to a total value of greater than 85%. The high helix content of the ternary complex suggests strongly that Snc2p folds to adopt an α-helical structure upon binding to the binary t-SNARE complex and that one or both t-SNAREs also adopt additional helical structure.
Protein: DP01502 (UniProt P33328)
Region: residues 1	to 91
Annotation: protein binding (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The addition of Snc2p to Sso1CT–Sec9CT binary complexes resulted in a further large increase in α-helix content, to a total value of greater than 85%. The high helix content of the ternary complex suggests strongly that Snc2p folds to adopt an α-helical structure upon binding to the binary t-SNARE complex and that one or both t-SNAREs also adopt additional helical structure.
Protein: DP01502 (UniProt P33328)
Region: residues 1	to 91
Annotation: molecular adaptor activity (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Binary complexes form between the target membrane SNAREs Sso1p and Sec9p; these binary complexes can subsequently bind to the vesicle SNARE Snc2p to form ternary complexes.
Binary and ternary SNARE complex formation induces the folding of unstructured SNARE domains.
Ternary complexes form upon addition of the cytoplasmic domain of the post-Golgi v-SNARE Snc2p (Fig. 1c), as has been seen for the functionally redundant (and 83% identical) Snc1p.
Protein: DP01503 (UniProt P32867)
Region: residues 192	to 265
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Unlike Sso1p and Sso2p, which display CD spectra indicative of substantial (∼70%) α-helix content, Sso1CT and Sso2CT are largely unfolded. Therefore, the SNARE regions that form binary and ternary complexes efficiently all seem, individually, to lack significant regular secondary structure.
Protein: DP01503 (UniProt P32867)
Region: residues 192	to 265
Annotation: disorder to order (Structural transition)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
A dramatic acquisition of α-helical secondary structure accompanied the combination of Sso1CT and Sec9CT, with the final α-helix content of ∼60%. [...] The observed spectrum for Sso1CT–Sec9CT differs significantly from that anticipated for a non-interacting mixture, indicating that binary complex formation is coupled to significant folding of one or both of the largely-unstructured t-SNARE domains.
Protein: DP01503 (UniProt P32867)
Region: residues 192	to 265
Annotation: protein binding (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
A dramatic acquisition of α-helical secondary structure accompanied the combination of Sso1CT and Sec9CT, with the final α-helix content of ∼60%. [...] The observed spectrum for Sso1CT–Sec9CT differs significantly from that anticipated for a non-interacting mixture, indicating that binary complex formation is coupled to significant folding of one or both of the largely-unstructured t-SNARE domains.
Cross-references: PDB:3b5n
Protein: DP01504 (UniProt P39926)
Region: residues 196	to 269
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Unlike Sso1p and Sso2p, which display CD spectra indicative of substantial (∼70%) α-helix content, Sso1CT and Sso2CT are largely unfolded. Therefore, the SNARE regions that form binary and ternary complexes efficiently all seem, individually, to lack significant regular secondary structure.
Protein: DP01506 (UniProt P08263)
Region: residues 208	to 222
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The model included the full dimer with the exception of the C-terminal residues beyond Met208. The C-terminal helix has been omitted from the apo-structure due to the absence of any associated electron density.
Cross-references: PDB:1GSD
PDB:1GSE
PDB:1GSF
Protein: DP01506 (UniProt P08263)
Region: residues 208	to 222
Annotation: disorder to order (Structural transition)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
It would appear, that the presence of a hydrophobic substrate, or possibly just glutathione, stabilizes the helix. ... It seems that the environment around Phe220 (which includes Tyr9, a residue of some importance to the catalytic mechanism) is critical in determining whether the helix is ordered or not.
Protein: DP01506 (UniProt P08263)
Region: residues 208	to 222
Annotation: molecular function regulator (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
This helix, one edge of which is made up of hydrophobic residues, forms a lid over the H-site, providing a highly hydrophobic environment for the substrate, and has been shown to be important, though not essential, in catalysis.
Protein: DP01508 (UniProt Q15418)
Region: residues 683	to 735
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Already the narrow signal dispersion of the HSQC spectrum of the RSK1(683–735) peptide informed us about the disordered nature of this free RSK1 tail fragment.
Cross-references: PDB:5CSF
Protein: DP01508 (UniProt Q15418)
Region: residues 683	to 735
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Overlay of the HSQC spectra of the free and S100B complexed 15N-labeled RSK1(683–735) peptide. Addition of excess S100B resulted in changes in the spectrum. As changes were monitored from the 15N RSK1 peptide side (S100B protein was unlabeled), the consequence of complex formation would be observable as shifted and broadened peaks and also peaks broadened below the detection limit in the HSQC spectrum.
Cross-references: PDB:5CSF
Protein: DP01508 (UniProt Q15418)
Region: residues 683	to 735
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Deconvolution of the difference spectra by the program BeStSel reveals an ∼13-amino acid-long single helix in the bound state of RSK1(683–735), while the free peptide is completely disordered.
Cross-references: PDB:5CSF
Protein: DP01508 (UniProt Q15418)
Region: residues 683	to 735
Annotation: protein binding (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
An increase in the helical content of RSK1(683-735) upon complex formation can be observed in the CD spectra without major changes in the S100B structure itself.
Cross-references: PDB:5CSF
Protein: DP01508 (UniProt Q15418)
Region: residues 712	to 727
Annotation: protein binding (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
PepRSK1 contains a reverse D-­motif from a downstream MAP kinase-activated protein kinase (MAPKAP) that is a known ERK2 substrate. The bound peptides (e.g. pepRSK1) were not involved in crystal packing in the new cocrystals. For flexible linear motifs this is more favourable in order to capture them in their physiologically relevant binding geometry.
Cross-references: PDB:4h3p
Protein: DP01508 (UniProt Q15418)
Region: residues 730	to 735
Annotation: PDZ domain binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Upon complex formation with the PDZ domain, the core interaction motif (the last five residues) became invisible in the NMR spectrum as a result of signal broadening confirming their central role in complex formation (Fig. 7C,D).
Protein: DP01508 (UniProt Q15418)
Region: residues 730	to 735
Annotation: phosphorylation display site (Disorder function)
Evidence: heteronuclear single quantum coherence spectroscopy evidence used in manual assertion
Supporting statements:
Autophosphorylation, PDZ, and MAPK binding all target the 40‐residue‐long, disordered C‐terminal tail of RSK1
Ras‐ERK pathway activation influences RSK‐PDZ substrate interaction and activator MAP kinase binding by using an autoregulatory phosphoswitch located in the disordered RSK C‐terminal tail
Changes in the 1H-15N HSQC spectra of RSK1696–735 peptides confirmed that autophosphorylation by CTKD occurred only at Ser732 (Fig. 7A).
Cross-references: BMRB:27214
Protein: DP01508 (UniProt Q15418)
Region: residues 696	to 735
Annotation: disorder (Structural state)
Evidence: heteronuclear single quantum coherence spectroscopy evidence used in manual assertion
Supporting statements:
In the 15N-HSQC spectra of [15N] NCOA3 (1018–1088), the backbone amide resonances fall between 8.0 and 8.5 p.p.m. The lack of chemical shift dispersion reflect the intrinsic mobility of this region.
Cross-references: BMRB:27213
BMRB:27214
Protein: DP01508 (UniProt Q15418)
Region: residues 709	to 735
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
This region lacks electron density in the X-ray structure, indicating it is disordered.
Cross-references: PDB:3RNY
Protein: DP01508 (UniProt Q15418)
Region: residues 731	to 735
Annotation: phosphorylation display site (Disorder function)
Evidence: in vitro protein kinase assay evidence used in manual assertion
Supporting statements:
Here, Ser732 was the main phosphorylated site, but we could also detect both Thr733 and Thr734 phosphorylated peptides. These latter CTT autophosphorylation sites might be mutually exclusive because no double or triple phosphorylated peptides were observed.
Protein: DP01508 (UniProt Q15418)
Region: residues 577	to 588
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Some loop regions, including part of the ‘activation loop’, are missing in our structure owing to poor electron density (Supplementary Table S1).
Additionally to the missing regions 578-583 and 577-585 in chain A and B (respectively, shown in table S1), the deposited data in PDB shows the residues 586, 587 and 588 also lack electron coordinates, so they are  considered as part of the IDR.
Cross-references: PDB:3RNY
Protein: DP01508 (UniProt Q15418)
Region: residues 729	to 735
Annotation: PDZ domain binding (Molecular function)
Evidence: microscale thermophoresis evidence used in manual assertion
Supporting statements:
Therefore, microscale thermophoresis (MST) was used and a ~ 20 μm interaction was detected (Fig. 3B). With competitive titration experiments, we could also show that phosphorylation at the major C-terminal autophosphorylation site (Ser732) does not influence the steady-state-binding affinity of the CTT peptide (729–735) to the second PDZ domain of MAGI-1 (Fig. 3C).
Protein: DP01508 (UniProt Q15418)
Region: residues 730	to 735
Annotation: PDZ domain binding (Molecular function)
Evidence: microscale thermophoresis evidence used in manual assertion
Supporting statements:
As expected, the bound RSK1 peptide shows a canonical class I PDZ domain-binding mode (Fig. 5A) [29].
We also solved crystal structures with phosphorylated CTT peptides (pSer732) and captured the MAGI-1–pRSK1 (CTT) complex in two slightly different crystal forms (Fig. 5B).
In summary, the CTT phosphorylation at Ser732 is compatible with PDZ binding, while phosphorylation at Thr733 would very likely disrupt RSK1–PDZ (MAGI-1) binding due to steric hindrance within the binding pocket.
Cross-references: PDB:5N7G
PDB:5N7D
PDB:5N7F
Protein: DP01508 (UniProt Q15418)
Region: residues 725	to 729
Annotation: self-interaction (Disorder function)
Evidence: combinatorial experimental and curator inference evidence used in manual assertion
Supporting statements:
However, the endothermic nature of binding between the PDZ domain and the longer RSK1712–735 (or RSK1696–735) peptide suggests that some degree of disordered-to-order transition occurs in the CTT upon phosphorylation. 
In contrast, comparison of the measured ΔCp values of a longer peptide (RSK712–735) to that of the shorter RSK729–735 peptide and differences in this value caused by phosphorylation (Fig. 6B, table, rows 1–3) suggest that there are intramolecular interactions in the free phosphorylated form of the longer (RSK712–735) peptide, which are absent in the shorter phosphopeptide.
Conversely, based on the discrepancy between calculated and measured ΔCp values for the longer peptide, one can estimate the hydration of the intramolecularly shielded residues, which is 60–70 cal·mol−1·K−1 suggesting that it is a small intramolecular clamp, possibly involving residues N-terminal to Lys729.
In the case of the unphosphorylated peptide, such minor peaks can be assigned to Leu730 and Ser732, which are next to cis-Pro731. In contrast, a considerably longer minor fragment (between residues 728–735) became apparent in the NMR spectrum of the phosphorylated peptide (Fig. 7F). This region showed large beta propensity based on SCS values.
Overall, this NMR data indicated significant chemical shift changes for residues of the charged motif (Arg725, Arg726, Arg728, and Lys729). Pro731 undergoes cis-trans isomerization and the chemical shift differences for Lys729 and Arg728 are more prominent in the cis-Pro peptide, suggesting the existence of a more pronounced charge clamp specifically involving these latter two residues.
Here, the phosphorylation triggers a transient local fold that can result in slowed-down conformational kinetics [43]. Similar intramolecular charge clamps have already been shown in some cases [44-46]; however, the RSK1 CTT phosphoswitch appears to be the first clear case where it acts as a modulator on the assembly of a signaling complex.
Protein: DP01508 (UniProt Q15418)
Region: residues 725	to 732
Annotation: self-regulatory activity (Disorder function)
Evidence: combinatorial experimental and curator inference evidence used in manual assertion
Supporting statements:
Experimental evidence for the intramolecular charge clamp in phosphorylated CTT
Interestingly, ERK2-binding affinity to the RSK1 peptide decreased five-fold (from 0.2 μm to 1 μm) when the peptide was phosphorylated at Ser732 (Fig. 3D).
This intramolecular charge clamp would prevent the formation of a presumably transient interaction between the CTT and ERK2 and will lead to weakened binding [11].
Interestingly, phosphorylation of Ser732 participates in the formation of a charged clamp, which affects ERK–RSK binding.
Here, the phosphorylation triggers a transient local fold that can result in slowed-down conformational kinetics [43]. Similar intramolecular charge clamps have already been shown in some cases [44-46]; however, the RSK1 CTT phosphoswitch appears to be the first clear case where it acts as a modulator on the assembly of a signaling complex.
The observed independent localization trends of activated ERK and activated RSK (Fig. 11D) and the charge clamp-based dissociation promoting effect of RSK1 CTT (Fig. 10F) can synergistically contribute to the periodicity and the amplitude of macroscopically observed pERK dissociation patterns.
Protein: DP01508 (UniProt Q15418)
Region: residues 712	to 726
Annotation: mitogen-activated protein kinase binding (Molecular function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
PepRSK1 contains a reverse D-­motif from a downstream MAP kinase-activated protein kinase (MAPKAP) that is a known ERK2 substrate (RSK1; Garai et al., 2012
Cross-references: ELM:DOC_MAPK_gen_1
PDB:4H3P
Protein: DP01509 (UniProt P9WIP5)
Region: residues 56	to 71
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Aside from K62, amide cross peaks are absent from W56 to D71 suggesting that the C-terminal region is unstructured in solution.
Cross-references: PDB:2KHR
BMRB:16253
Protein: DP01509 (UniProt P9WIP5)
Region: residues 1	to 12
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Because both the N- and C-terminal regions are disordered, G1* - A12 and W56 - D71, respectively, most of these regions have been removed from the Figure for clarity.
Protein: DP01510 (UniProt O25010)
Region: residues 1	to 30
Annotation: disorder (Structural state)
Evidence: chromatography evidence used in manual assertion
Supporting statements:
In gel filtration experiments, the HP0222 migrated as a molecule with a molecular mass of approximately 35 kD, and the HP0222str migrated as a 13 kDa molecule. The larger‐than‐expected apparent size of HP0222 in the above experiments was the result of the 42‐residue‐long (12 residue His‐tag and the first 30 residues of HP0222) unstructured N‐terminal sequences.
Protein: DP01510 (UniProt O25010)
Region: residues 1	to 30
Annotation: disorder (Structural state)
Evidence: dynamic light scattering assay evidence used in manual assertion
Supporting statements:
Light scattering experiments on HP0222 indicated molecular size of approximately 40 kDa. The larger‐than‐expected apparent size of HP0222 in the above experiments was the result of the 42‐residue‐long (12 residue His‐tag and the first 30 residues of HP0222) unstructured N‐terminal sequences.
Protein: DP01511 (UniProt P32917)
Region: residues 149	to 238
Annotation: molten globule (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
 First, we measured a two-dimensional (2D) 1H-15N heteronuclear correlation (HSQC) spectrum of scSte5 RH2 in the same standard conditions as in the DSC experiments above. The broad signals, indicating exchange between several conformations and the small chemical shift dispersion (Figure 2 a), are typical for a molten globule.
Protein: DP01511 (UniProt P32917)
Region: residues 149	to 238
Annotation: molten globule to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Binding was monitored by [1H,15N]-HSQC NMR spectroscopy, both with and without the addition of G protein subunits β/γ. Upon interaction with the binding partners, scSte5 RH2 underwent a dramatic conformational rearrangement (Figure S5). The resonances became more dispersed and narrower in linewidth. These changes provide evidence that, upon interaction with the Ste4/Ste18 heterodimer, the active form of scSte5 RH2 escapes the molten globule state at least partially and adopts a better-defined and less-dynamic structure.
Protein: DP01511 (UniProt P32917)
Region: residues 149	to 238
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Binding was monitored by [1H,15N]-HSQC NMR spectroscopy, both with and without the addition of G protein subunits β/γ. Upon interaction with the binding partners, scSte5 RH2 underwent a dramatic conformational rearrangement (Figure S5). The resonances became more dispersed and narrower in linewidth. These changes provide evidence that, upon interaction with the Ste4/Ste18 heterodimer, the active form of scSte5 RH2 escapes the molten globule state at least partially and adopts a better-defined and less-dynamic structure.
Protein: DP01511 (UniProt P32917)
Region: residues 149	to 238
Annotation: molten globule (Structural state)
Evidence: heat capacity-based evidence used in manual assertion
Supporting statements:
Thus, the diffuse non-cooperative nature of the scSte5 RH2 melting transition indicates a heterogeneous ensemble of conformations that are characteristic for a molten globule state, which has been previously observed in other domains.
Protein: DP01512 (UniProt P03050)
Region: residues 1	to 53
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
At pH 2, 20 °C, and a protein concentration of 64 µ , Arc is unfolded by the following criteria: (i) the circular dichroism spectrum shows very little secondary structure and increased random coil content compared with native Arc (Figure 1A); (ii) the fluorescence spectrum of the single tryptophan at position 14 is red shifted and shows reduced intensity compared to native Arc (Figure IB); and (iii) the protein behaves as a monomer in sedimentation equilibrium experiments (av Mw 5560), whereas native Arc is a dimer (av Afw 12 346) (Figure 1C).
Protein: DP01512 (UniProt P03050)
Region: residues 1	to 53
Annotation: protein binding (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
In the structure of the globular Arc dimer, each monomer is interwound with the other, forming a single folded domain with a conventional hydrophobic core.
Cross-references: PDB:1ARQ
Protein: DP01512 (UniProt P03050)
Region: residues 1	to 53
Annotation: disorder to order (Structural transition)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
In the structure of the globular Arc dimer, each monomer is interwound with the other, forming a single folded domain with a conventional hydrophobic core.
Protein: DP01512 (UniProt P03050)
Region: residues 1	to 53
Annotation: disorder (Structural state)
Evidence: fluorescence evidence used in manual assertion
Supporting statements:
At pH 2, 20 °C, and a protein concentration of 64 µ , Arc is unfolded by the following criteria: (i) the circular dichroism spectrum shows very little secondary structure and increased random coil content compared with native Arc (Figure 1A); (ii) the fluorescence spectrum of the single tryptophan at position 14 is red shifted and shows reduced intensity compared to native Arc (Figure IB); and (iii) the protein behaves as a monomer in sedimentation equilibrium experiments (av Mw 5560), whereas native Arc is a dimer (av Afw 12 346) (Figure 1C).
Protein: DP01513 (UniProt P53378)
Region: residues 439	to 473
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
We performed a combination of NMR experiments and computer simulations to investigate the structural and dynamical consequences of introducing negative charge at a site in the gamma-tubulin CT(439-473)  that is phosphorylated in vivo. The results derived from the two techniques were remarkably similar. Both showed that the WT gamma-CT is largely unstructured.