LiteFold/DisProt huggingface dataset:
Protein: DP01584 (UniProt P19880)
Region: residues 565	to 650
Annotation: molecular adaptor activity (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The active oxidized form, a nuclear export signal (NES) in the carboxy-terminal cysteine-rich domain is masked by disulphide- bond-mediated interactions with a conserved amino-terminal a-helix.
Protein: DP01588 (UniProt P52799)
Region: residues 253	to 300
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
a detailed NMR study on the structural and dynamic properties of the cytoplasmic domain of human ephrin B2. Our results reveal the following: (1) the N-terminal region of the cytoplasmic domain from residues 253 to 300 lacks the ability for structure formation and is particularly prone to aggregation
Protein: DP01588 (UniProt P52799)
Region: residues 323	to 333
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
the C-terminal functional subdomain from residues 301 to 333 assumes two distinctive structural elements with residues 301-322 adopting a well-packed hairpin structure followed by a flexible C-terminal tail.
Protein: DP01588 (UniProt P52799)
Region: residues 301	to 322
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
the unphosphorylated 22-residue motif adopts a well formed beta-hairpin structure in isolation from the ephrinB cytoplasmic subdomain. However, this beta-hairpin is radically abolished by tyrosine phosphorylation, regardless of the relative location and number of Tyr residues.
Protein: DP01588 (UniProt P52799)
Region: residues 301	to 322
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
the present study reveals that, as shown by circular dichroism and NMR, the unphosphorylated 22-residue motif adopts a well formed beta-hairpin structure in isolation from the ephrinB cytoplasmic subdomain. However, this beta-hairpin is radically abolished by tyrosine phosphorylation, regardless of the relative location and number of Tyr residues.
Protein: DP01588 (UniProt P52799)
Region: residues 301	to 322
Annotation: order to disorder (Structural transition)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
However, this beta-hairpin is radically abolished by tyrosine phosphorylation, regardless of the relative location and number of Tyr residues.
Protein: DP01589 (UniProt P9WJA9)
Region: residues 1	to 18
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The extreme N-terminal (residues 1 to 18) and C-terminal (residues 150 to 162) regions were not defined and have been omitted for clarity.
Protein: DP01589 (UniProt P9WJA9)
Region: residues 19	to 33
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Rather than acting to tether a disordered N-terminal region, phosphorylation of Thr22 appears to stabilize a preexisting but low-occupancy association of residues 21 to 30 with the FHA domain. Amino acid residues 21 to 33 adopted an extended conformation that encompassed a short region with helical propensity
Protein: DP01589 (UniProt P9WJA9)
Region: residues 19	to 33
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
We therefore propose that, rather than acting to tether a disordered N-terminal region, phosphorylation of Thr22 appears to sta- bilize a preexisting but low-occupancy association of residues 21 to 30 with the FHA domain.
Protein: DP01589 (UniProt P9WJA9)
Region: residues 19	to 33
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
hese data suggest a mechanism for the regulation of intermolecular interactions of Rv1827 through intramolecular binding of its N-terminal region to the FHA domain after phosphorylation at either Thr21 or Thr22 by PknG or PknB
Protein: DP01589 (UniProt P9WJA9)
Region: residues 19	to 33
Annotation: phosphorylation display site (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
these data suggest a mechanism for the regulation of intermolecular interactions of Rv1827 through intramolecular binding of its N-terminal region to the FHA domain after phosphorylation at either Thr21 or Thr22 by PknG or PknB,
Protein: DP01589 (UniProt P9WJA9)
Region: residues 19	to 33
Annotation: molecular function inhibitor activity (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Intramolecular interactions regulate the binding of Rv1827 to target enzymes
Protein: DP01589 (UniProt P9WJA9)
Region: residues 34	to 54
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Regions of high mobility were apparent at the N- and C-termini and at the region corresponding to amino acid residues 34 to 54
Protein: DP01589 (UniProt P9WJA9)
Region: residues 150	to 162
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The extreme N-terminal (residues 1 to 18) and C-terminal (residues 150 to 162) regions were not defined and have been omitted for clarity.
Protein: DP01590 (UniProt Q92945)
Region: residues 130	to 218
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
igh-sensitivity SOFAST 15N-1H HMQC spectra28 were recorded on samples from the two HPLC peaks (Fig. 4a): the two spectra clearly show that the nonphosphorylated protein is folded, whereas the phosphorylated protein is essentially unfolded.
Cross-references: PDB:2OPU
Protein: DP01590 (UniProt Q92945)
Region: residues 130	to 218
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
igh-sensitivity SOFAST 15N-1H HMQC spectra28 were recorded on samples from the two HPLC peaks (Fig. 4a): the two spectra clearly show that the nonphosphorylated protein is folded, whereas the phosphorylated protein is essentially unfolded.
Protein: DP01590 (UniProt Q92945)
Region: residues 130	to 218
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
We confirmed the folding state of phospho-KH1 by recording CD spectra at different temperatures
Protein: DP01590 (UniProt Q92945)
Region: residues 130	to 218
Annotation: disorder to order (Structural transition)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
igh-sensitivity SOFAST 15N-1H HMQC spectra28 were recorded on samples from the two HPLC peaks (Fig. 4a): the two spectra clearly show that the nonphosphorylated protein is folded, whereas the phosphorylated protein is essentially unfolded.
Protein: DP01590 (UniProt Q92945)
Region: residues 130	to 218
Annotation: protein folding chaperone (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Our data indicate that phosphorylation of KH1 unfolds the domain and creates a site for 14-3-3ζ binding.
Protein: DP01591 (UniProt P18212)
Region: residues 170	to 186
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Fig 1 shows part of the final 1.6-Å-resolution 2Fo – Fc electron-density map. The electron densities of the N-terminal portion (residues 10–15) and two loop regions (residues 91–107 and 138–140) were not seen in the model because of disorder. 
Loop region 91-107 corresponds to 170-186 region in Uniprot.
Cross-references: PDB:1V2B
Protein: DP01592 (UniProt Q8VHC5)
Region: residues 100	to 120
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The first 20 residues from the amino-terminus (residues 100–120), residues 177–178 (EF2 loop), and residues 192–195 (domain linker) all exhibited weak NMR signals with random coil chemical shifts, indicative of structural disorder in these regions.
Protein: DP01593 (UniProt P21374)
Region: residues 97	to 235
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The authors could not solve the structure for this region in the Cryo-EM experiment, probably due to poor electron density  expected for a disordered region.
Protein: DP01593 (UniProt P21374)
Region: residues 96	to 235
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The authors could not solve the structure for this region in the Cryo-EM experiment, probably due to poor electron density  expected for a disordered region.
Protein: DP01594 (UniProt Q80ZV0)
Region: residues 103	to 145
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The authors could not solve the structure for this region in the X-ray experiment, probably due to poor electron density expected for a disordered region
Protein: DP01594 (UniProt Q80ZV0)
Region: residues 107	to 122
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The authors could not solve the structure for this region in the X-ray experiment, probably due to poor electron density expected for a disordered region
Protein: DP01594 (UniProt Q80ZV0)
Region: residues 182	to 202
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The authors could not solve the structure for this region in the X-ray experiment, probably due to poor electron density expected for a disordered region
Protein: DP01594 (UniProt Q80ZV0)
Region: residues 283	to 308
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The authors could not solve the structure for this region in the X-ray experiment, probably due to poor electron density expected for a disordered region
Protein: DP01594 (UniProt Q80ZV0)
Region: residues 182	to 266
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The authors could not solve the structure for this region in the X-ray experiment, probably due to poor electron density expected for a disordered region
Protein: DP01599 (UniProt P47142)
Region: residues 55	to 71
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Following strand β1, there is a β-hairpin encompassing residues 50–74 with residues 55–71 not visible. Given that there are no unambiguous experimental sequence markers in this region (no Met and no Cys residues), there is some uncertainty of the sequence register in the 50–79 region of Vps25 WHA. The region from 55 to 74 represents an insertion in the yeast Vps25 relative to other species, so that the 50–74 β-hairpin may be unique to S. cerevisiae.
Protein: DP01599 (UniProt P47142)
Region: residues 56	to 70
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Vps25 is the most flexible of the three subunits. Flexible internal loops between residues 56–70, 110–115, 146–149 and 162–164, as well as the C-terminal ten residues, could not be visualized in electron density.
Protein: DP01599 (UniProt P47142)
Region: residues 56	to 72
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
It lacks canonical helix 2, which instead folds into a large disordered loop followed by strands 3 and 4 that connects to helix 2 (at the corresponding position of canonical helix 3).
The final model lacks two to five flexible loops (molecule mol A, residues 56–72, 114–115, 156–157; mol B, residues 53–73, 157–158; mol C, residues 57–72, 155–158; mol D, residues 19–21, 55–73, 107–120, 156–160, 185–186).
Cross-references: PDB:1XB4
Protein: DP01600 (UniProt Q93KQ4)
Region: residues 51	to 81
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues 51-81 of the YscM2(33-81) polypeptide are disordered in the crystal and only the side chains in the α-helical segment could be assigned with confidence.
Cross-references: PDB:1TTW
Protein: DP01601 (UniProt P26599)
Region: residues 409	to 425
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
This loop (residues 409–425) appears to be very mobile and is unstructured apart from a single helical turn close to the start of β5. In our construct the linker makes no observable contact with the rest of the protein; however, it is positioned above the RNA binding surface and may play a role in RNA recognition (see below).
Cross-references: PDB:1QM9
Protein: DP01601 (UniProt P26599)
Region: residues 431	to 454
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
PTB-34 has a tandem domain structure in which the RRMs are tethered by a linker peptide of 25 residues in length. While the conformations of the secondary structural elements within RRMs 3 and 4 are well defined, the inter-domain linker region of PTB-34 was mostly unassigned (Conte et al., 1999).
Cross-references: PDB:1QM9
Protein: DP01601 (UniProt P26599)
Region: residues 431	to 454
Annotation: flexible linker (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
In our present analysis of the NMR structure of PTB-34, the extent of flexibility of the inter-domain linker is particularly striking (Figure 3): there are no inter-domain contacts whatsoever and the two RRM domains appear to tumble independently, the long linker region making no fixed contacts with the rest of the protein, presumably due to disorder.
Cross-references: PDB:1QM9
Protein: DP01601 (UniProt P26599)
Region: residues 143	to 184
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Assignments could not be made for the majority of residues within the extensive inter-domain linker sequence (residues 143–184 approximately) and also at the N- and C-termini. 15N-relaxation data confirm that these regions are highly flexible (data not shown) and are likely to be unstructured.
Cross-references: BMRB:5409
Protein: DP01601 (UniProt P26599)
Region: residues 143	to 184
Annotation: flexible linker (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Assignments could not be made for the majority of residues within the extensive inter-domain linker sequence (residues 143–184 approximately) and also at the N- and C-termini. 15N-relaxation data confirm that these regions are highly flexible (data not shown) and are likely to be unstructured.
Protein: DP01602 (UniProt Q86WV6)
Region: residues 342	to 379
Annotation: disorder (Structural state)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
pSTING adopts an extended random coil structure spanning two patches of positively charged residues and a large hydrophobic groove between them (Fig. S2 A and B).
Cross-references: PDB:5JEJ
Protein: DP01602 (UniProt Q86WV6)
Region: residues 359	to 379
Annotation: protein binding (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The pLxIS motif interacts with IRF-3 through electrostatic interactions, hydrogen bonds, and hydrophobic interactions. A cluster of positively charged residues, Arg285, His288, His290, and Lys313, interacts with pSer366 of pSTING through electrostatic interactions (Fig. 1B and Fig. S2B). Residues pSer366, Ile365, and Leu363 form three backbone hydrogen bonds with IRF-3.
Cross-references: PDB:5JEJ
Protein: DP01602 (UniProt Q86WV6)
Region: residues 358	to 379
Annotation: phosphorylation display site (Disorder function)
Evidence: mass spectrometry evidence used in manual assertion
Supporting statements:
To determine how the phosphorylated STING mediates the recruitment of IRF-3, we expressed small ubiquitin-related modifier (SUMO) fusions of the human STING CTD (residues 155–379) and C-terminal tail (CTT) (residues 342–379) and phosphorylated them in vitro with TBK1.
The phosphorylation sites were identified by MS analysis of the pSTING CTT.
Figure S1 shows the phosphorylated residues are Ser358, Ser366, Thr376 and Ser379.
Protein: DP01602 (UniProt Q86WV6)
Region: residues 344	to 379
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Electron density for the C-terminal end of the protein, AA344-379, positioned at the end of helix α9 was missing, suggesting that this part of the protein is flexible and probably swings around the tip of helix α9 protruding out of the concave cavity of the sheet.
Cross-references: PDB:4EF4
PDB:4EF5
Protein: DP01602 (UniProt Q86WV6)
Region: residues 344	to 379
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Both the final refined STINGCTD model in the apo and c-di-GMP–bound forms contains all the residues of STINGCTD except the two segments containing residues 149–150 and 344–379, which have no clear electron density and are presumed to be disordered in solution.
Cross-references: PDB:4F5W
PDB:4F5Y
Protein: DP01602 (UniProt Q86WV6)
Region: residues 342	to 379
Annotation: protein binding (Molecular function)
Evidence: surface plasmon resonance evidence used in manual assertion
Supporting statements:
Surface plasmon resonance (SPR) binding studies show that IRF-3 binds only to the pSTING CTD or CTT (Fig. S1 A and C). The affinity of the pSTING CTD for IRF-3 (Kd ∼48 μM) (Fig. S1B) is comparable to that of the pSTING CTT (Kd ∼43 μM) (Fig. S1D). These results show that STING binds to IRF-3 via its C-terminal pLxIS motif upon phosphorylation.
Protein: DP01602 (UniProt Q86WV6)
Region: residues 358	to 366
Annotation: protein binding (Molecular function)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
To identify the phosphorylation site of STING that is essential for IRF-3 recruitment, we mutated each of the four potential phosphorylated residues (Fig. S1E) to alanine and conducted IFN-β luciferase reporter assays in HEK293T cells, which do not express STING (28). As shown in Fig. 1C, the S366A mutation abolishes IFN-β reporter activation, consistent with previous studies (23). In addition, the S358A mutation partially impairs IFN-β reporter activation (Fig. 1C). However, the T376A and S379A mutations do not affect IFN-β reporter activation (Fig. 1C).
The L363A and I365A mutations individually or in combination strongly abolish IFN-β reporter activation (Fig. 1D). In contrast, the E362A and L364A mutations have only minor effects on STING-mediated signaling (Fig. 1D). The P361A mutation upstream of the pLxIS motif also dramatically reduces IFN-β reporter activation (Fig. 1D).
Protein: DP01604 (UniProt Q12483)
Region: residues 1	to 22
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The N-terminal region (that encompasses residues 1 to 22 preceding the helix 1) showed to be disordered in the crystal structure.
Protein: DP01604 (UniProt Q12483)
Region: residues 1	to 22
Annotation: lipid binding (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The N-terminal region of Vps22 (...) is particularly rich in basic residues (30% inhuman Vps22) (...). Consistent with this, we observe weak but reproducible binding of the N-terminal helical domain of Vps22 (residues 1–90) to brain-derived liposomes (data not shown), suggesting that Vps22 might contribute to membrane binding of ESCRT II.
Protein: DP01604 (UniProt Q12483)
Region: residues 1	to 19
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Vps22 consists of a single N-terminal coiled coil followed by two winged-helix (WH) domains (Supplementary Fig. 1a). All but the first 19 residues are ordered.
Protein: DP01605 (UniProt P19339)
Region: residues 244	to 253
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The loop connecting the β2 and β3 strands of the Sxl RBD1 (β2/β3 loop) consists of ten amino acid residues (R158 to G167), and is as long as that of the Sxl RBD2 (R244 to G253), whereas the corresponding loop of the U1A RBD1 is composed of only six amino acid residues (R48 to G53).
Protein: DP01605 (UniProt P19339)
Region: residues 201	to 211
Annotation: disorder (Structural state)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Characteristic of a poorly ordered region, the electron density for the 10-residue interdomain linker was weak and discontinuous in maps calculated with the multiwavelength anomalous diffraction data.
From the C terminus of RRM1, the second-closest RRM2 N terminus is 28.8 Å away, a distance that two residues could not possibly bridge. Weak electron density and the high B-factors of the interdomain linker imply significant flexibility in this region.
Cross-references: PDB:3SXL