LiteFold/DisProt huggingface dataset:
Protein: DP01164 (UniProt Q13625)
Region: residues 693	to 752
Annotation: protein homodimerization activity (Molecular function)
Evidence: peptide array evidence used in manual assertion
Supporting statements:
ASPP2 Pro-bound peptides from the first Ank repeat (aa 931–961) and from the SH3 domain (aa 1083–1096) (Table 1 and Fig. 5, A, B, and D). Screening a second peptide array revealed that ASPP2 Ank-SH3 bound several peptides derived from ASPP2 Pro (Table 2 and Fig. 5, C and D). These peptides are located between residues 693 and 752 at the N-terminal region of the ASPP2 Pro domain, and between residues 893 and 912 at its C terminus.
Protein: DP01164 (UniProt Q13625)
Region: residues 893	to 912
Annotation: protein homodimerization activity (Molecular function)
Evidence: peptide array evidence used in manual assertion
Supporting statements:
ASPP2 Pro-bound peptides from the first Ank repeat (aa 931–961) and from the SH3 domain (aa 1083–1096) (Table 1 and Fig. 5, A, B, and D). Screening a second peptide array revealed that ASPP2 Ank-SH3 bound several peptides derived from ASPP2 Pro (Table 2 and Fig. 5, C and D). These peptides are located between residues 693 and 752 at the N-terminal region of the ASPP2 Pro domain, and between residues 893 and 912 at its C terminus.
Protein: DP01164 (UniProt Q13625)
Region: residues 693	to 918
Annotation: self-inhibition (Disorder function)
Evidence: fluorescence anisotropy evidence used in manual assertion
Supporting statements:
We used fluorescence anisotropy to test the affinity of ASPP2 Ank-SH3 and ASPP2 Pro-Ank-SH3 to this peptide. ASPP2 Ank-SH3 bound NFκB 303–332 with Kd = 0.27 μm, whereas ASPP2 Pro-Ank-SH3 bound this peptide with Kd = 1.2 μm, an order of magnitude weaker (Fig. 7A). This shows that the presence of the proline-rich domain inhibits the interaction of ASPP2 Ank-SH3 with the NFκB peptide.
In summary, our results show that the interaction between ASPP2 Pro and ASPP2 Ank-SH3 inhibits the intermolecular interaction of the latter with the NFκB peptide.
Protein: DP01164 (UniProt Q13625)
Region: residues 693	to 918
Annotation: self-inhibition (Disorder function)
Evidence: competitive binding evidence used in manual assertion
Supporting statements:
Next, we tested by competition fluorescence anisotropy whether NFκB 303–332 and the ASPP2 Pro-derived peptide ASPP2 723–737 compete on the same binding site in ASPP2 Ank-SH3. When unlabeled ASPP2 723–737 was added to a pre-formed complex of ASPP2 Ank-SH3 and fluorescently labeled NFκB 303–332 at IS = 50 mm, competition took place and the anisotropy decreased almost completely back to the initial values (Fig. 7B). The same trend was observed when the competition was performed in the opposite way: Unlabeled NFκB 303–332 displaced fluorescently labeled ASPP2 723–737 even quicker (Fig. 7C), because its affinity to ASPP2 Ank-SH3 was much tighter.
In summary, our results show that the interaction between ASPP2 Pro and ASPP2 Ank-SH3 inhibits the intermolecular interaction of the latter with the NFκB peptide.
Protein: DP01165 (UniProt Q9HAN9)
Region: residues 109	to 146
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Additionally, a stretch of
37 residues between helix C and strand d (from 109 to 146) is
also disordered in the crystal. This region contains the predicted
nuclear localization signal (NLS) sequence PGRKRKW
and two putative phosphorylation site serine residues (Ser-109
and Ser-136)
Cross-references: PDB:1KQN
Protein: DP01166 (UniProt O30916)
Region: residues 1	to 148
Annotation: disorder (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
This complex was subjected to further analysis by limited proteolysis. The chaperone SigE was resistant to digestion but SopB was quickly digested to a 40 KDa protease-resistant fragment (Fig. 1A). This resistant fragment was identified by N-terminal sequencing and mass spectroscopy. It starts at residue E149 and the last amino acid residue identified by trypsin digestion followed by mass spectroscopy was R476. This result suggests that the 150 first residues of SopB are accessible to protease and may contain the CBD of SopB and the 40 KDa C-terminal region is very stable and may correspond to the Inositol-phosphatase domain of the effector.
Protein: DP01166 (UniProt O30916)
Region: residues 29	to 45
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
 The structure of the N-terminal domain of SopB (residues 29–181) in complex with Cdc42 has recently been solved [35]. Analysis of this structure shows no electronic density for residues from 29 to 45 and 171 to 181 suggesting that these fragments don't have a stable conformation in the complex.
Cross-references: PDB:4DID
Protein: DP01167 (UniProt P02730)
Region: residues 1	to 54
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues 1-54, 202-211, and 357-379 were not observed or were poorly defined by the electron density.
Protein: DP01168 (UniProt F9UST4)
Region: residues 126	to 147
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
A fragment (residues 126–147, including several highly conserved residues) is severely disordered, except for in chain B of an alternative substrate-free structure (PDB ID code 5UNM), where it folds into an extended loop
Protein: DP01169 (UniProt P24255)
Region: residues 1	to 105
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The σ54(106-269) peaks are well-dispersed and nearly all of them overlay with a peak in the σ54(1-269) spectrum. The extra peaks in the σ54(1-269) construct, which must correspond to the first 105 residues of E.c. σ54, are poorly dispersed and in the region of the spectrum that corresponds to unfolded residues. Other constructs of E.c. σ54 were also studied, including the full length protein (residues 1-477), the AID-linker-4 helix bundle σ54(1-186), the AID alone σ54(1-62), and a segment of the AID alone σ54(11-48). In all of these the pattern of poorly dispersed peaks associated with the AID, with 1H shifts between 8 and 9 ppm, occurs.
Protein: DP01169 (UniProt P24255)
Region: residues 1	to 105
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
A segment of the AID drives complex formation with the activator ATPase domain NtrC1C in its ATP state.
Protein: DP01169 (UniProt P24255)
Region: residues 1	to 105
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
We performed similar experiments with full length 15N-labeled E.coli σ54 and RNA polymerase. With excess core RNAP present most of the peaks corresponding to the AID and linker are broadened. The ~10 remaining peaks likely correspond to the N-terminal residues before the start of, and possibly including, the N-terminal helix of the AID. So the σ54 AID is an unstructured, intrinsically disordered domain in σ54 alone, with most of it becoming ordered when in complex with core polymerase.
Protein: DP01170 (UniProt O00268)
Region: residues 408	to 838
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
 The spectrum of TAF4N/C was also represented by a large minimum at 205 nm, suggesting that the molecule was largely disordered. However, a careful observation revealed that the negative minimum in the spectrum of TAF4N/C was broader and shallower than that of Sp1‐QB.
These results suggest that some part of TAF4N/C may adopt an α‐helical conformation. Nevertheless, the spectra of both proteins indicated that most of the molecule was largely disordered, consistent with NMR observations.
Protein: DP01170 (UniProt O00268)
Region: residues 408	to 838
Annotation: disorder (Structural state)
Evidence: small-angle X-ray scattering evidence used in manual assertion
Supporting statements:
On the other hand, the R g value of TAF4N/C was significantly smaller than that is expected for the urea‐denatured state of protein with 431 amino acid residues (∼70 Å).32 The result is consistent with that of CD spectrum, suggesting possible formation of α‐helical structure in some part of TAF4N/C.
None of the plot for Sp1‐QA, Sp1‐QB, and TAF4N/C showed any clear peaks, suggesting that these proteins are largely disordered.
Protein: DP01170 (UniProt O00268)
Region: residues 408	to 838
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
All resonance peaks were poorly dispersed along the 1H chemical shift axis and appeared within the range of 8.5 and 7.5 ppm, indicating that the protein had neither secondary nor tertiary structures that were stabilized by regular hydrogen bonds and the rigid packing of side chains (Fig. ​(Fig.2).2). This result suggests that the central region of TAF4, which contains all the Q‐domains, is intrinsically disordered under physiological conditions.
Protein: DP01170 (UniProt O00268)
Region: residues 408	to 838
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
We found that it was possible to classify the residues of Sp1‐QB into two groups: one independent of the concentrations of TAF4N/C and the other showing a significant decrease in intensity. The results for several representative residues are shown in Figure ​Figure3(D).3(D). These plots corresponded well among residues belonging to the same group, suggesting that the interaction between Sp1‐QB and TAF4N/C is consistent to the two‐state binding model.
Protein: DP01170 (UniProt O00268)
Region: residues 408	to 838
Annotation: protein binding (Molecular function)
Evidence: surface plasmon resonance evidence used in manual assertion
Supporting statements:
The fit converged well, and single association and dissociation rate constants were estimated to be 4.40 ± 0.08 M−1 s−1 and (3.03 ± 0.06) × 10−4 s−1, respectively. The equilibrium association constant between Sp1‐QB and TAF4N/C was estimated to be (1.45 ± 0.04) × 104 M−1 from these association and dissociation rate constants. These results suggest a significant interaction between Sp1‐QB and TAF4N/C.
Protein: DP01171 (UniProt P42768)
Region: residues 201	to 268
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
SDS-polyacrylamide gel electrophoresis analysis of the purified fragments (Fig. 1B) and mass spectroscopy show that the WASP fragments of 4 kDa (residues 221–257), 7 kDa (201–268), and 13 kDa (201–321) molecular mass, termed W4, W7, and W13, respectively, can be isolated as soluble non-GST fusion proteins without degradation and in reasonable quantities.
It can be seen from Fig. 5D that the spectra of W4 and W7 in the <210 nm range resemble those expected for a random coil conformation.
Protein: DP01171 (UniProt P42768)
Region: residues 201	to 268
Annotation: protein binding (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The CRIB/GBD motif of WASP mediated binding to Cdc42.
Protein: DP01171 (UniProt P42768)
Region: residues 201	to 268
Annotation: disorder to order (Structural transition)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The binding of Cdc42 induces a structural rearrangement of residues in the GBD/CRIB motif, or alternatively, the Wiskott Aldrich syndrome protein fragments have an ensemble of conformations, one of which is stabilized by Cdc42 binding.
Protein: DP01171 (UniProt P42768)
Region: residues 201	to 268
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Short and medium range NOEs were analyzed to characterize the secondary structure of W7. Surprisingly, considering the tight binding of W7 to Cdc42, amino acid regions in the N-terminal part of W7 including the GBD/CRIB motif itself do not show any obvious secondary structure. Only the region from Trp-252 to Asp-264 shows NOEs typical of an α-helical conformation.
Protein: DP01172 (UniProt O43516)
Region: residues 2	to 101
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The CD curve of WIP-N (res2-101) exhibits a minimum at 195 nm and a weak shoulder at 220 nm, characteristic features of an unstructured protein.
Protein: DP01172 (UniProt O43516)
Region: residues 2	to 101
Annotation: protein binding (Molecular function)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
WIP interacts with actin through its N‐terminal domain that contains two canonical actin binding motifs (ABMs).
Protein: DP01172 (UniProt O43516)
Region: residues 2	to 101
Annotation: disorder to order (Structural transition)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
For the ABM the disordered to folded transition involves a gain of stabilizing interactions with actin at the price of a decrease in its entropy; by partially mirroring the future bound state the ABM can limit this entropic loss and increase its binding affinity.
Protein: DP01172 (UniProt O43516)
Region: residues 2	to 65
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
One- and two-bond J(15N,13Cα) couplings were acquired for WIP residues 2-65 at various temperatures, and in denaturing and crowding environments. Under native conditions fitted J-couplings identified in the WIP conformational ensemble a propensity for extended conformation at residues 16-23 and 45-60, and a helical tendency at residues 28-42. These findings are consistent with a previous study of the based upon chemical shift and RDC data and confirm that the WIP2-65 conformational ensemble is biased towards the structure assumed by this fragment in its actin-bound form.
Protein: DP01172 (UniProt O43516)
Region: residues 2	to 101
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The comparison between the 2D 1H‐15N heteronuclear single quantum coherence (HSQC) spectrum and the 2D in‐phase anti‐phase (IPAP) 13C‐15N (CON) spectrum of WIP-N further corroborates our identification of WIP-N as a disordered domain. The CON spectrum displays significantly advantageous spectral dispersion which is characteristic of disordered proteins. As expected, secondary chemical shifts in WIP-N are generally small, in the ±0.5 p.p.m. range. However, they are revealing in that they identify structural tendencies in the disordered state of WIP-N or regions for which the multi‐conformational average differs from random coil. In both prediction methods residues 30–42 exhibit a helical propensity, and residues 45–62 demonstrate a β‐strand propensity. Furthermore, a third region with β‐strand structural propensity, albeit lower than that of residues 45–62, is clearly revealed for residues 17–25. The ensemble‐based analysis of RDCs confirms our previous results, finding that in WIPN the multi‐conformational average for the N‐terminal ABM exhibits the characteristic helix‐β‐strand motif, and that it is preceded by an additional segment with β‐strand structural propensity. In addition, it shows that the ABM does not exhibit tertiary structure or even partial long‐range order and should be considered as an array of independent structural elements.
Protein: DP01172 (UniProt O43516)
Region: residues 407	to 503
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion
Supporting statements:
Regions that were most protected from solvent exchange, exhibiting negligible recovery after 20 ms, included residues 440–468, spanning the rigid VCR domain, and residues 475–479, both consistent with structural elements delineated by chemical-shift data. Low protection factors identified increased flexibility in two regions of WIPC, residues 470–474 and 481–490, which exhibited recovery rates of 5–10% and 10–25%, respectively.
Protein: DP01172 (UniProt O43516)
Region: residues 407	to 503
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The transiently structured regions are connected by unstructured linker segments, as could be deduced from minimal secondary structure, low transverse relaxation and hetNOE rates, minimal IRCS values, and exposure to solvent exchange.
Protein: DP01172 (UniProt O43516)
Region: residues 407	to 503
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
WASp-interacting protein (WIP) acts as the cellular chaperone of WASp, conveys WASp to areas of active actin assembly after antigen-receptor and chemokine receptor signaling (3,4), and stabilizes WASp by shielding it from cellular degradation systems. The C-terminal segment of WIP contains the verprolin conserved region (VCR; residues 444–478) that is capable of binding the N-terminal EVH1 domain of WASp.
Protein: DP01172 (UniProt O43516)
Region: residues 407	to 503
Annotation: protein folding chaperone (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
WASp-interacting protein (WIP) acts as the cellular chaperone of WASp, conveys WASp to areas of active actin assembly after antigen-receptor and chemokine receptor signaling (3,4), and stabilizes WASp by shielding it from cellular degradation systems. The C-terminal segment of WIP is capable of binding  and chaperoning the N-terminal EVH1 domain of WASp.
Protein: DP01172 (UniProt O43516)
Region: residues 407	to 503
Annotation: phosphorylation display site (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
One such region of interest is the phosphorylation site of residues 484–492, whose flexibility is consistent with its need to be sufficiently exposed to allow access to the phosphorylating enzyme PKCθ.
Protein: DP01172 (UniProt O43516)
Region: residues 407	to 503
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Thus, contributing to the formation of the WIP/WASp complex are preformed motifs at residues 462–465 and 474–478, and a third motif (residues 457–461) whose structure is formed only in the presence of WASp.
Protein: DP01173 (UniProt Q15726)
Region: residues 20	to 138
Annotation: disorder (Structural state)
Evidence: chromatography evidence used in manual assertion
Supporting statements:
The protein eluted from the SEC column at a volume corresponding to an apparent molar mass of 28 kDa. The mass derived from MALS data is 11.7 kDa, however, demonstrating that Kiss1 is monomeric. These inconsistent results indicate that Kiss1 is either folded with an elongated shape, or flexible and disordered.
Protein: DP01173 (UniProt Q15726)
Region: residues 20	to 138
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The low dispersion of the backbone 1HN chemical shifts observed in the HSQC spectrum indicates that KISS1 is largely disordered and flexible under native conditions. Analysis of chemical shift deviations and 15N T2 relaxation times does not provide clear evidence for any conformational preference, suggesting that KISS1 behaves as a random coil polypeptide.
Protein: DP01173 (UniProt Q15726)
Region: residues 20	to 138
Annotation: limited proteolysis display site (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
After secretion KISS is processed by the furin endoprotease. This enzyme recognizes dibasic cleavage sites on the amino acid sequence and, after the action of carboxypeptidases and peptidyl-glycine-α-amidating monooxygenase (PAM), generates a fragment of 54 residues known as Kisspeptin54 (KISS1 residues 68–121). Kisspeptin54 can be further cleaved into smaller 14, 13 and 10 residue fragments, or kisspeptins, which are ligands of the seven-transmembrane helix G protein-coupled receptor GPR54, also named KISS1R.
Protein: DP01173 (UniProt Q15726)
Region: residues 20	to 138
Annotation: phosphorylation display site (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Phosphorylated at residue Y110.
Protein: DP01173 (UniProt Q15726)
Region: residues 20	to 138
Annotation: molecular recognition display site (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
C-terminal amidation by peptidyl-glycine-α-amidating monooxygenase.
Protein: DP01173 (UniProt Q15726)
Region: residues 20	to 138
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
KISS1 and its fragments interact with KISS1R, their GPCR receptor.
Protein: DP01173 (UniProt Q15726)
Region: residues 20	to 138
Annotation: disorder (Structural state)
Evidence: temperature-induced protein unfolding evidence used in manual assertion
Supporting statements:
The thermal denaturation curve of Kiss1 followed by the changes in the CD signal at 222 nm does not show any cooperative folding-unfolding transition, indicating that KISS1 lacks a defined tertiary structure.
Protein: DP01173 (UniProt Q15726)
Region: residues 20	to 138
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The far-UV CD spectrum of Kiss1 shows a minimum at 198 nm and a shoulder at 226 nm, consistent with a predominantly random-coil protein with little secondary structure.
Protein: DP01173 (UniProt Q15726)
Region: residues 20	to 138
Annotation: disorder (Structural state)
Evidence: small-angle X-ray scattering evidence used in manual assertion
Supporting statements:
The Kratky representation is typical for a disordered protein, with a monotonic increase of I(s)s2 with the momentum transfer s. An analysis of the smallest angle data by Guinier’s approach for a momentum transfer range s·Rg < 1.3 (where Rg is the radius of gyration) indicates that KISS1 has an average radius of gyration of 34.7 ± 0.5 Å. This value is slightly larger than expected for an IDP of 120 residues (RgRC = 30.1 Å), suggesting that KISS1 could transiently adopt more extended structures.
Protein: DP01174 (UniProt O43474)
Region: residues 1	to 130
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The narrow chemical shift dispersion in the 1H dimension of the 1H-15N HSQC spectrum, suggests that the KLF41–130 fragment is intrinsically disordered. Analysis using the secondary structure propensity (SSP) algorithm (Marsh et al. 2006) indicates that most of KLF41–130 is disordered, however there are two continuous regions with >20% helical propensity spanning residues Asn42-Met51 and Asp104-His115 (Fig. 2). 
Cross-references: BMRB:26953