LiteFold/DisProt huggingface dataset:
Protein: DP00707 (UniProt Q9UER7)
Region: residues 1	to 50
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
In addition to the linker between these domains, the ~50 N-terminal and ~340 C-terminal residues of DAXX are predicted to be unstructured. The intrinsic disorder of these regions was confirmed by NMR analysis of DAXX 1-144 (not shown) and mDAXX566-739.
Protein: DP00708 (UniProt O35613)
Region: residues 566	to 739
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
In addition to the linker between these domains, the ~50 N-terminal and ~340 C-terminal residues of DAXX are predicted to be unstructured. The intrinsic disorder of these regions was confirmed by NMR analysis of DAXX 1-144 (not shown) and mDAXX566-739.
Protein: DP00708 (UniProt O35613)
Region: residues 441	to 499
Annotation: disorder (Structural state)
Evidence: curator inference from database used in manual assertion
Supporting statements:
"This poly-E region is inferred by the curator to be disordered, based on MobiDB-Lite and according to experimental evidence demonstrating that poly-E repeats display random-coil-like conformation (PMID:16949547)"
Protein: DP00709 (UniProt Q9Y3M2)
Region: residues 1	to 63
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The fact that the majority of peaks observed in the 1H−15N HSQC of N-Cby can essentially overlay with the peaks observed in the spectrum of full-length Cby (except for residues 50−63) suggests that at least a large portion of the N-terminal part of the protein is disordered and may not interact significantly with the C-terminal segment (Figure ​2b).
Protein: DP00709 (UniProt Q9Y3M2)
Region: residues 1	to 63
Annotation: negative regulation of protein binding (Biological process)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The greater intensity losses observed in the TC-1 spectrum upon titration with C-Cby suggest that C-Cby binds TC-1 with a higher affinity than the full-length protein. This was confirmed by ITC experiments, which revealed that C-Cby binds to TC-1 with a Kd of ∼ 2 μM [Fig. 7(C), Supporting Information Fig. 3(A)].
Alternatively, the disordered N-terminus of Cby may inhibit the interaction by acting as an entropic bristle, that is, an unstructured region that impedes surrounding macromolecules via random, thermally driven motions.
Protein: DP00709 (UniProt Q9Y3M2)
Region: residues 1	to 63
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The disordered nature of N-Cby is also confirmed by CD spectropolarimetry. The CD spectrum of N-Cby (Figure 7b) displays a large and negative signal at 190 nm and negligible ellipticities at 208 and 222 nm, indicating that N-Cby is largely unstructured (48).
Protein: DP00709 (UniProt Q9Y3M2)
Region: residues 1	to 63
Annotation: negative regulation of protein binding (Biological process)
Evidence: isothermal titration calorimetry evidence used in manual assertion
Supporting statements:
The greater intensity losses observed in the TC-1 spectrum upon titration with C-Cby suggest that C-Cby binds TC-1 with a higher affinity than the full-length protein. This was confirmed by ITC experiments, which revealed that C-Cby binds to TC-1 with a Kd of ∼ 2 μM [Fig. 7(C), Supporting Information Fig. 3(A)].
Alternatively, the disordered N-terminus of Cby may inhibit the interaction by acting as an entropic bristle, that is, an unstructured region that impedes surrounding macromolecules via random, thermally driven motions.
Protein: DP00709 (UniProt Q9Y3M2)
Region: residues 102	to 126
Annotation: disorder (Structural state)
Evidence: protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion
Supporting statements:
Similarly, residues 102‐126, which make up the very C‐terminal end of Cby, exhibited extremely rapid deuterium uptake.
Protein: DP00709 (UniProt Q9Y3M2)
Region: residues 102	to 126
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The data indicate that the C‐terminal 20 residues are not structured and that the helical content of Cby is maintained upon deletion of this disordered extension. Notably, the CD spectrum of a synthetic construct comprising the C‐terminal 25 residues of Cby (CbyC25), shows that the C‐terminal extension is largely disordered but does have α‐helical propensity (deconvolution: 42% helical, 12% strand, and 46% turns/disordered) [Fig. ​4(C)].
Protein: DP00709 (UniProt Q9Y3M2)
Region: residues 102	to 126
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Notably, truncation of the C‐terminal extension of Cby does not induce significant chemical shift changes or intensity attenuation to the signals originating from the N‐terminal half, indicating that there are no long‐range interactions between the N‐ and C‐terminal disordered regions of Cby.
Protein: DP00709 (UniProt Q9Y3M2)
Region: residues 1	to 63
Annotation: disorder (Structural state)
Evidence: protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion
Supporting statements:
Deuteration was quasi‐instantaneous for the N‐terminal half of Cby, that is, deuterium levels of >90% were observed already for the first experimental time point of 1 min.
Protein: DP00709 (UniProt Q9Y3M2)
Region: residues 1	to 66
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Deconvolution of the spectra using the DichroWeb software44 gives 30% helical, 21% strand, and 49% disordered/turn structure for the full‐length Cby and 41% helical, 17% strand, and 42% disordered/turn for CbyΔC20.
Next, we sought to characterize isolated C‐terminal half of Cby in the absence of the disordered N‐terminus. A CD spectrum reveals that C‐Cby (residues 67‐126) is largely helical [Fig. ​4(C)]. 
Circular dichroism spectra shows a large drop of the disordered percentage when the region 1-66 is deleted.
Protein: DP00712 (UniProt Q9UGL1)
Region: residues 115	to 129
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Perturbations to 1H–15N correlation spectra revealed that the flexible loop L1 of ARID was the main DNA-binding interface.
The flexible loop L1 makes a major contribution to the protein–DNA interaction.
Protein: DP00712 (UniProt Q9UGL1)
Region: residues 115	to 129
Annotation: nucleic acid binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Perturbations to 1H–15N correlation spectra revealed that the flexible loop L1 of ARID was the main DNA-binding interface.
The flexible loop L1 makes a major contribution to the protein–DNA interaction.
Protein: DP00712 (UniProt Q9UGL1)
Region: residues 188	to 199
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Like other ARIDs, the human JARID1B ARID domain also includes six helices (H1:E5-Q27, H2:L43-E53, H3:F56-K61, H4:W65-K71, H5:A79-R90, H6:L92-F100) and two loops (loop L1:G28-D42 and loop L2:M72-K78). 
When compared to the ARID domains of Mrf-2, Dri, and RBP2, we found that both SWI1 and JARID1B ARID have a shorter loop L2.
Protein: DP00712 (UniProt Q9UGL1)
Region: residues 119	to 128
Annotation: nucleic acid binding (Molecular function)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
An EMSA experiment showed that the ARID/BRIGHT domain could interact with DNA duplex d (5′-ATTGCACAGTA-3′), which is consistent with a previous study [18]. Moreover, the interaction could only be detected in low salt concentrations, below 50 mM NaCl (Fig. 1C). It can be proposed that the DNA-binding ability of the JARID1B ARID domain is salt-dependent, which is similar to other ARID studies.
Quantitative analysis of DNA binding was performed by fluorescence titration experiments. The equilibrium dissociation constants (Kd) of the different mutants were calculated (Table 1 and Fig. S2). Current experimental evidence has confirmed that the loop L1, especially R38 in loop L1, is an important region in DNA-binding activity. Other residues (K32, H35, and L41) close to R38 on Loop1 that resulted in relatively large chemical shift changes when mutated may participate in the interaction between protein and DNA.
Mutations of JARID1B ARID affect DNA binding in EMSA. Obvious weaker binding occurs using the mutants R38A and 4A (K32A, H35A, R38A, L41A).
The authors use a different numbering for the residues and (considering the UniProt sequence) are referring to the mutation R125A and the quadruple mutations K119A, H122A, R125A, L128A.
Protein: DP00712 (UniProt Q9UGL1)
Region: residues 1	to 27
Annotation: disorder (Structural state)
Evidence: protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion
Supporting statements:
The HDX data clearly show that the first 27 residues are disordered with corresponding fast HDX, whereas significantly slower HDX is observed in the following jmjN and ARID domain regions.
Protein: DP00712 (UniProt Q9UGL1)
Region: residues 198	to 311
Annotation: disorder (Structural state)
Evidence: protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion
Supporting statements:
The following region (residues 198–375) is characterized by fast HDX and two regions that lack HDX data. However, the PHD1 domain region is characterized by slow HDX, demonstrating the presence of higher-order structure.
Protein: DP00712 (UniProt Q9UGL1)
Region: residues 339	to 375
Annotation: disorder (Structural state)
Evidence: protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion
Supporting statements:
The following region (residues 198–375) is characterized by fast HDX and two regions that lack HDX data. However, the PHD1 domain region is characterized by slow HDX, demonstrating the presence of higher-order structure.
Protein: DP00712 (UniProt Q9UGL1)
Region: residues 430	to 453
Annotation: disorder (Structural state)
Evidence: protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion
Supporting statements:
In the jmjC domain, the segment containing res. 430–453 to seen to display very fast HDX. This agrees well with the KDM5B 1–753 crystal structure19, where the region 442–447 lacked electron density and was omitted from the model.
Protein: DP00712 (UniProt Q9UGL1)
Region: residues 441	to 453
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with high relative B-factor values used in manual assertion
Supporting statements:
Residues 441-444 are missing in the crystal structure and nearby residues have a high relative B-factor values. This agrees with the fast HDX seen for residues 430-453 (pmid:30858420).
Cross-references: DisProt:DP00712r010
PDB:5FPU
Protein: DP00712 (UniProt Q9UGL1)
Region: residues 469	to 481
Annotation: disorder (Structural state)
Evidence: protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion
Supporting statements:
The region 469–481 also shows fast HDX. As seen in the crystal structure, in particular the region around H474 is suggested to be disordered.
Protein: DP00712 (UniProt Q9UGL1)
Region: residues 543	to 554
Annotation: disorder (Structural state)
Evidence: protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion
Supporting statements:
The fast exchange of the region 543–554 also agrees with the poorly defined electron density around residue 545 in the crystal structure.
Protein: DP00712 (UniProt Q9UGL1)
Region: residues 1078	to 1125
Annotation: disorder (Structural state)
Evidence: protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion
Supporting statements:
A weak coil-coil signature is also observed approximately 100 amino acids downstream of these 3 motifs, at residues 1056–1072. After this the region 1078–1125 displays fast HDX.
Protein: DP00712 (UniProt Q9UGL1)
Region: residues 1271	to 1344
Annotation: disorder (Structural state)
Evidence: protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion
Supporting statements:
Another predicted helical region 1228–1270, supported by the HDX data, is located immediately after the PHD2 domain, again followed by a long unstructured region 1271–1344 with fast HDX.
Protein: DP00712 (UniProt Q9UGL1)
Region: residues 1376	to 1450
Annotation: disorder (Structural state)
Evidence: protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion
Supporting statements:
This region is followed by another predicted helical region 1345–1365 with reduced HDX that in turn is followed by a region 1376–1450 with sparse HDX sequence coverage. Data for the only peptide from this region shows fast HDX demonstrating a disordered structure despite a predicted helicity.
Protein: DP00716 (UniProt P02545)
Region: residues 567	to 664
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
We here report the NMR 1H, 15N, 13CO, 13Cα and 13Cβ chemical shift assignment of the C-terminal region that is specific to prelamin A, from amino acid 567 to amino acid 664. We also report the NMR 1H, 15N, 13CO, 13Cα and 13Cβ chemical shift assignment of the C-terminal region of the progerin variant, from amino acid 567 to amino acid 614. Analysis of these chemical shift data confirms that both prelamin A and progerin C-terminal domains are largely disordered and identifies a common partially populated α-helix from amino acid 576 to amino acid 585.
Protein: DP00725 (UniProt P41851)
Region: residues 44	to 85
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The N-terminal part of the constructs, i.e. residues 44–85, which are just C-terminal of the predicted transmembrane region comprising residues 24–43, are disordered in the present structure.
Protein: DP00726 (UniProt Q5UPJ7)
Region: residues 150	to 166
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
This helix is followed by a variable loop disordered in TyrRSapm as well as in the M. jannaschii apo TyrRS structure 1U7D
Cross-references: PDB:2J5B
Protein: DP00726 (UniProt Q5UPJ7)
Region: residues 150	to 166
Annotation: protein binding (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The dimer interface should then appear more flexible than the rest of the molecule, leading to higher B-factor values. This region of the TyrRSapm structure is actually more agitated than its surroundings.
Cross-references: PDB:2J5B
Protein: DP00726 (UniProt Q5UPJ7)
Region: residues 150	to 166
Annotation: self-assembly (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Forcing the TyrRSapm dimer into the standard conformation would cost 1,000 Å2 of the buried surface area and greatly reduce its stability. Conversely, forcing the other (canonical) TyrRS dimer into the conformation observed for the TyrRSapm dimer would also be energetically unfavorable, again at a cost of about 1,000 Å2.
Cross-references: PDB:2J5B
Protein: DP00728 (UniProt P00760)
Region: residues 4	to 47
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
some 37% was crystallographically disordered (missing residues 16-41, 62-84, 110-120, 139-156, 1860190, 223-224). The presence within this disordered region of all the previously identified sites of proteolytic cleavage is evidence that the disorder represents the changes occurring in vivo.
Cross-references: PDB:1EZX
Protein: DP00728 (UniProt P00760)
Region: residues 4	to 47
Annotation: order to disorder (Structural transition)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
showing a loss of stability and an increase in proteolytic vulnerability of proteases in complexes with serpins.
Protein: DP00728 (UniProt P00760)
Region: residues 4	to 47
Annotation: protein binding (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
we purifed the complex from a reaction mixture containing an excess of a1-antitrypsin over trypsin
Cross-references: imex:IM-14510-4
Protein: DP00728 (UniProt P00760)
Region: residues 115	to 125
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
some 37% was crystallographically disordered (missing residues 16-41, 62-84, 110-120, 139-156, 1860190, 223-224). The presence within this disordered region of all the previously identified sites of proteolytic cleavage is evidence that the disorder represents the changes occurring in vivo.
Cross-references: PDB:1EZX
Protein: DP00728 (UniProt P00760)
Region: residues 115	to 125
Annotation: order to disorder (Structural transition)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
showing a loss of stability and an increase in proteolytic vulnerability of proteases in complexes with serpins.
Protein: DP00728 (UniProt P00760)
Region: residues 115	to 125
Annotation: protein binding (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
we purifed the complex from a reaction mixture containing an excess of a1-antitrypsin over trypsin
Cross-references: imex:IM-14510-4
Protein: DP00728 (UniProt P00760)
Region: residues 68	to 89
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
some 37% was crystallographically disordered (missing residues 16-41, 62-84, 110-120, 139-156, 1860190, 223-224). The presence within this disordered region of all the previously identified sites of proteolytic cleavage is evidence that the disorder represents the changes occurring in vivo.
Cross-references: PDB:1EZX
Protein: DP00728 (UniProt P00760)
Region: residues 68	to 89
Annotation: order to disorder (Structural transition)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
showing a loss of stability and an increase in proteolytic vulnerability of proteases in complexes with serpins.
Protein: DP00728 (UniProt P00760)
Region: residues 68	to 89
Annotation: protein binding (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
we purifed the complex from a reaction mixture containing an excess of a1-antitrypsin over trypsin
Cross-references: imex:IM-14510-4
Protein: DP00728 (UniProt P00760)
Region: residues 142	to 159
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
some 37% was crystallographically disordered (missing residues 16-41, 62-84, 110-120, 139-156, 1860190, 223-224). The presence within this disordered region of all the previously identified sites of proteolytic cleavage is evidence that the disorder represents the changes occurring in vivo.
Cross-references: PDB:1EZX
Protein: DP00728 (UniProt P00760)
Region: residues 142	to 159
Annotation: order to disorder (Structural transition)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
showing a loss of stability and an increase in proteolytic vulnerability of proteases in complexes with serpins.
Protein: DP00728 (UniProt P00760)
Region: residues 142	to 159
Annotation: protein binding (Molecular function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
we purifed the complex from a reaction mixture containing an excess of a1-antitrypsin over trypsin
Cross-references: imex:IM-14510-4
Protein: DP00732 (UniProt Q00496)
Region: residues 235	to 245
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final model is complete, except for residues 234-244 and the 10 C-terminal residues in both molecules because of weak electron density, indicating that the region may be disordered.
In the mutant (b), the active site is partly covered by the loop 234-244 (top left of the figure), which is missing in the wild type.
Cross-references: PDB:1T3A
Protein: DP00732 (UniProt Q00496)
Region: residues 413	to 422
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final model is complete, except for residues 234-244 and the 10 C-terminal residues in both molecules because of weak electron density, indicating that the region may be disordered.
Cross-references: PDB:1T3A
Protein: DP00736 (UniProt Q9UKV8)
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:
Grey letters indicate disordered loops not observed in the Ago2 crystal structure.
Cross-references: PDB:4OLA
PDB:4OLB
Protein: DP00736 (UniProt Q9UKV8)
Region: residues 1	to 22
Annotation: flexible N-terminal tail (Disorder function)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The authors do not specify about the disordered region (1-22), but these residues are missing in the strucutre.
Cross-references: PDB:4OLA
PDB:4OLB
Protein: DP00736 (UniProt Q9UKV8)
Region: residues 818	to 838
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Grey letters indicate disordered loops not observed in the Ago2 crystal structure.
Cross-references: PDB:4OLA
PDB:4OLB
Protein: DP00736 (UniProt Q9UKV8)
Region: residues 820	to 837
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB evidence shows this region lacks electron density, indicating it is disordered.
Cross-references: PDB:5JS2
PDB:5JS1
Protein: DP00736 (UniProt Q9UKV8)
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 PDB evidence shows this region lacks electron density, indicating it is disordered.
Cross-references: PDB:5JS2
PDB:5JS1