LiteFold/DisProt huggingface dataset:
Protein: DP03400 (UniProt Q9H4L7)
Region: residues 109	to 150
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The first, dCUE, corresponds to the tandem CUE domains spanning residues 144–295. The second, eCUE, corresponds to only the first CUE domain and the disordered region preceding it (residues 109–206).
The 13Cα, 13Cβ, 13Cʹ 1Hα, 1HN and 15N chemical shifts have been used to predict secondary structure propensities for dCUE and eCUE in solution using TALOS-N; these are plotted as a function of sequence. The predicted secondary structure shows the expected pattern of three α-helices in each CUE domain. Interestingly, a short β-strand is predicted in the otherwise disordered region preceding CUE1.
Annotation of region boundaries was done based on the information that the 1st CUE domain starts at residue 157 and based on Figure 2 a showing that the predicted helices of the domain only start after residue 150.
Cross-references: BMRB:27780
Protein: DP03400 (UniProt Q9H4L7)
Region: residues 200	to 250
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Secondary structure prediction of the SMARCAD1 sequence suggests that the N-terminal tandem CUE domains, termed CUE1 (residues 157–199) and CUE2 (residues 251–294), are each composed of a three helix bundle and are connected by a disordered linker rich in serines and charged amino acids (residues 200–250).
Moreover, the statistics for dCUE are reported for the individual functional domains, from which it is evident that the relatively poor overall assignment coverage stems from the flexible linker connecting the two CUE domains. This is mostly due to high sequence degeneracy and the lack of structural propensity in this region of the protein.
Lack of secondary structure for the linker region is also evident from Figure 2 a.
Cross-references: BMRB:27785
Protein: DP03400 (UniProt Q9H4L7)
Region: residues 200	to 250
Annotation: flexible linker (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Secondary structure prediction of the SMARCAD1 sequence suggests that the N-terminal tandem CUE domains, termed CUE1 (residues 157–199) and CUE2 (residues 251–294), are each composed of a three helix bundle and are connected by a disordered linker rich in serines and charged amino acids (residues 200–250).
Moreover, the statistics for dCUE are reported for the individual functional domains, from which it is evident that the relatively poor overall assignment coverage stems from the flexible linker connecting the two CUE domains. This is mostly due to high sequence degeneracy and the lack of structural propensity in this region of the protein.
No significant changes in chemical shift are observed in the 1H–15N HSQC for the residues of the CUE1 domain in the dCUE and eCUE constructs. This suggests that the N-terminal region, the linker, and the CUE2 domain do not make specific contacts with the CUE1 domain.
Cross-references: BMRB:27785
Protein: DP03401 (UniProt P18272)
Region: residues 600	to 645
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
 According to the RCI-S2 values provided by TALOS-N (Fig.2.c), the disordered (residues 600‒645) and ordered (residues 646‒739) regions are clearly differentiated.
A large fraction of the peaks of the presented HSQC spectrum show narrow peak dispersion and fall to the ppm range tipical for IDPs.
Cross-references: BMRB:27847
Protein: DP03401 (UniProt P18272)
Region: residues 25	to 62
Annotation: disorder (Structural state)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The first 37 residues at the N-terminus are unstructured.
In this publication the authors solved the crystal structure of the VP35 NPBP/ΔNPNTD complex. ΔNPNTD comprised the residues 25–457 of the Zaire ebolavirus (strain Mayinga-76) nucleoprotein.
Cross-references: PDB:4YPI
Protein: DP03401 (UniProt P18272)
Region: residues 38	to 240
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with high relative B-factor values used in manual assertion
Supporting statements:
All four ΔNPNTD molecules are present in the structure. However, the head lobes of molecules B and D show a high degree of disorder with corresponding high average and individual B-factors (Table S1 and Figure S3D). The B-factors indicate that the conformations of head lobes in symmetrically-equivalent copies of these molecules across the crystal lattice differ in their orientation by 1–2 Å. 
In this publication the authors solved the crystal structure of the VP35 NPBP/ΔNPNTD complex. ΔNPNTD comprised the residues 25–457 of the Zaire ebolavirus (strain Mayinga-76) nucleoprotein. They identified a head lobe spanning NP residues 38 to 240.
Cross-references: PDB:4YPI
Protein: DP03402 (UniProt J9V8B5)
Region: residues 44	to 97
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The cytoplasmic tail residues are mostly disordered but an extended backbone conformation is adopted by the LC3 binding motif and the putative M1 interaction site has partial helical content with a small pH-dependence.
All measured heteronuclear NOEs were negative, indicating that the distal cytoplasmic tail was highly dynamic throughout. 
Backbone amide resonances for residues 44–64 were largely missing due to chemical exchange broadening.
The whole cytoplasmic tail of MP2 (residues 44-97) was found to be disordered based on heteronuclear NOEs. Within this longer region, residues 44-64 were also affected by chemical exchange broadening.
Cross-references: BMRB:50113
BMRB:50127
Protein: DP03402 (UniProt J9V8B5)
Region: residues 46	to 62
Annotation: lipid binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
A membrane proximal cytoplasmic region (residues ~ 46–97) contains a membrane-interacting amphipathic helix (APH; residues ~ 46–62) that is important in lipid raft targeting and virus scission.
HMQC spectra of the M2-APH-CT construct were acquired in the presence of 50 mM LMPC:LMPG micelles (4:1) or POPC:POPG liposomes (4:1; 17 mM total lipid) at pH 7.2. The detectable amides of the APH residues Gly58 and Gly62 were perturbed upon addition of the membrane mimetics. By contrast, none of the detectable resonances for residues outside of the APH were perturbed upon addition of either micelles or liposomes at pH 7.2 or pH 5.5, consistent with there being no interactions of the distal cytoplasmic tail with membranes.
Protein: DP03403 (UniProt Q8WXS3-1)
Region: residues 1	to 180
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Analysis of structural elements by the CSI web server (data not shown) resulted in an all-coil prediction. This supports the expectation based upon the appearance of the [1H, 15N]-HSQC spectrum which showed a reduced spectral dispersion of average chemical shifts implying flexibility typical for intrinsically disordered proteins.
Cross-references: BMRB:28084
Protein: DP03404 (UniProt P56211)
Region: residues 1	to 112
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The bioinformatical analyses were experimentally confirmed in 1H–15N 2D HSQC spectra of ARPPs, that is, the disordered nature of ARPPs manifests itself as low dispersion of chemical shift in the 1HN dimension, all amide proton resonances falling between 7.7 and 8.5 ppm.
In this paper, we have presented a nearly complete assignment of main-chain 1H, 13C, and 15N chemical shifts in two intrinsically disordered proteins, ARPP-16 and ARPP-19.
Cross-references: BMRB:27912
Protein: DP03404 (UniProt P56211)
Region: residues 1	to 112
Annotation: disorder (Structural state)
Evidence: heteronuclear single quantum coherence spectroscopy evidence used in manual assertion
Supporting statements:
The 2D 1H,15N heteronuclear single quantum coherence (HSQC) spectra of unbound ARPP1921,22 and FAM122ANterm confirmed that both are IDPs with multiple regions of amino acids with preferred α-helical propensities (using chemical shift index (CSI) analysis; Extended Data Fig. 3a–f).
Cross-references: BMRB:51881
Protein: DP03404 (UniProt P56211)
Region: residues 60	to 65
Annotation: phosphorylation display site (Disorder function)
Evidence: heteronuclear single quantum coherence spectroscopy evidence used in manual assertion
Supporting statements:
The 2D 1H,15N HSQC spectrum of thiophosphorylated ARPP19 identified two phosphorylated residues, Ser62, the established MASTL phosphorylation substrate, and Ser104, a serine that was previously identified as a protein kinase A (PKA) substrate, and also shows recognition site homology to the MASTL specificity sequence23. 
Cross-references: BMRB:51882
Protein: DP03404 (UniProt P56211)
Region: residues 102	to 106
Annotation: phosphorylation display site (Disorder function)
Evidence: heteronuclear single quantum coherence spectroscopy evidence used in manual assertion
Supporting statements:
The 2D 1H,15N HSQC spectrum of thiophosphorylated ARPP19 identified two phosphorylated residues, Ser62, the established MASTL phosphorylation substrate, and Ser104, a serine that was previously identified as a protein kinase A (PKA) substrate, and also shows recognition site homology to the MASTL specificity sequence23. 
Cross-references: BMRB:51882
Protein: DP03404 (UniProt P56211)
Region: residues 20	to 112
Annotation: protein phosphatase 2A binding (Molecular function)
Evidence: heteronuclear single quantum coherence spectroscopy evidence used in manual assertion
Supporting statements:
For ARPP19, around 90 N/HN cross-peaks (residues 20–112) showed reduced intensities.
Protein: DP03404 (UniProt P56211)
Region: residues 20	to 75
Annotation: protein phosphatase 2A binding (Molecular function)
Evidence: heteronuclear single quantum coherence spectroscopy evidence used in manual assertion
Supporting statements:
To identify which residues of ARPP19 and FAM122A bind B55, we repeated the NMR experiments using B55 loopless (B55LL), a variant that lacks the PP2Aa binding loop (amino acids 126–164 are replaced with NG; Extended Data Fig. 1a) and is thus unable to bind PP2Aa. Overlaying the 2D 1H,15N HSQC spectra of ARPP19 and tpS62tpS104ARPP19 with and without B55LL showed that the identity and number of N/HN cross-peaks with reduced intensities are similar, but not identical, to those observed with PP2A:B55 (Fig. 1f,g and Extended Data Fig. 5a,b). Specifically, the peaks corresponding to residues 20–75 and 105–112 show significant reductions in intensities, whereas ARPP19 residues 75–104 show little or no intensity loss with B55LL. This shows that two distinct ARPP19 domains—20–75 and 105–112—bind B55.
Protein: DP03404 (UniProt P56211)
Region: residues 105	to 112
Annotation: protein phosphatase 2A binding (Molecular function)
Evidence: heteronuclear single quantum coherence spectroscopy evidence used in manual assertion
Supporting statements:
To identify which residues of ARPP19 and FAM122A bind B55, we repeated the NMR experiments using B55 loopless (B55LL), a variant that lacks the PP2Aa binding loop (amino acids 126–164 are replaced with NG; Extended Data Fig. 1a) and is thus unable to bind PP2Aa. Overlaying the 2D 1H,15N HSQC spectra of ARPP19 and tpS62tpS104ARPP19 with and without B55LL showed that the identity and number of N/HN cross-peaks with reduced intensities are similar, but not identical, to those observed with PP2A:B55 (Fig. 1f,g and Extended Data Fig. 5a,b). Specifically, the peaks corresponding to residues 20–75 and 105–112 show significant reductions in intensities, whereas ARPP19 residues 75–104 show little or no intensity loss with B55LL. This shows that two distinct ARPP19 domains—20–75 and 105–112—bind B55.
Protein: DP03404 (UniProt P56211)
Region: residues 42	to 75
Annotation: protein phosphatase 2A binding (Molecular function)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
The remaining unaccounted density corresponds to tpARPP19 or FAM122A (tpARPP19 residues 42–75 and 86–112; FAM122A residues 81–111). tpARPP19 binds exclusively to B55 and PP2Ac using helices connected by extended yet ordered loops (helices are pre-populated in free ARPP19; Extended Data Fig. 3a,c,i).
Cross-references: PDB:8TTB
EMDB:41604
Protein: DP03404 (UniProt P56211)
Region: residues 86	to 112
Annotation: protein phosphatase 2A binding (Molecular function)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
The remaining unaccounted density corresponds to tpARPP19 or FAM122A (tpARPP19 residues 42–75 and 86–112; FAM122A residues 81–111). tpARPP19 binds exclusively to B55 and PP2Ac using helices connected by extended yet ordered loops (helices are pre-populated in free ARPP19; Extended Data Fig. 3a,c,i).
Cross-references: PDB:8TTB
EMDB:41604
Protein: DP03404 (UniProt P56211)
Region: residues 86	to 112
Annotation: disorder to order (Structural transition)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
tpARPP19 binds exclusively to B55 and PP2Ac using helices connected by extended yet ordered loops (helices are pre-populated in free ARPP19; Extended Data Fig. 3a,c,i).
Cross-references: PDB:8TTB
EMDB:41604
Protein: DP03404 (UniProt P56211)
Region: residues 86	to 112
Annotation: order (Structural state)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
tpARPP19 binds exclusively to B55 and PP2Ac using helices connected by extended yet ordered loops (helices are pre-populated in free ARPP19; Extended Data Fig. 3a,c,i).
Cross-references: PDB:8TTB
EMDB:41604
Protein: DP03404 (UniProt P56211)
Region: residues 42	to 75
Annotation: order (Structural state)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
tpARPP19 binds exclusively to B55 and PP2Ac using helices connected by extended yet ordered loops (helices are pre-populated in free ARPP19; Extended Data Fig. 3a,c,i).
Cross-references: PDB:8TTB
EMDB:41604
Protein: DP03404 (UniProt P56211)
Region: residues 42	to 75
Annotation: disorder to order (Structural transition)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
tpARPP19 binds exclusively to B55 and PP2Ac using helices connected by extended yet ordered loops (helices are pre-populated in free ARPP19; Extended Data Fig. 3a,c,i).
Cross-references: PDB:8TTB
EMDB:41604
Protein: DP03404 (UniProt P56211)
Region: residues 1	to 41
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The lack of electron density shows this region is disordered.
The density for these residues is present but amorphous, suggesting that α2 remains somewhat mobile in the B55 bound state (a fuzzy interaction24,31,32).
Cross-references: PDB:8TTB
EMDB:41604
Protein: DP03404 (UniProt P56211)
Region: residues 76	to 85
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The lack of electron density shows this region is disordered.
ARPP19 residues 76QLPTAAPD83 remain mobile when bound to PP2A:B55.
Cross-references: PDB:8TTB
EMDB:41604
Protein: DP03404 (UniProt P56211)
Region: residues 25	to 41
Annotation: protein phosphatase 2A binding (Molecular function)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
ARPP19 residues 25–41 include helix α2 (25–34) and bind the cleft between B55 loops L4/5 (L4/5 refers to the loop connecting β-propellers 4 and 5) and between L5/6 (B55 adopts a WD40 fold composed of 7 β-propellers connected by 7 loops). The density for these residues is present but amorphous, suggesting that α2 remains somewhat mobile in the B55 bound state (a fuzzy interaction24,31,32).
Cross-references: PDB:8TTB
EMDB:41604
Protein: DP03404 (UniProt P56211)
Region: residues 32	to 41
Annotation: protein phosphatase 2A binding (Molecular function)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
To test α2 binding to PP2A:B55 in cells, we generated YFP–ARPP19 variants in which either five amino acids (5-Ala, 32AAAAA36 or 37AAAAA41) or one amino acid (32–41) were changed to alanine (or A34G) and then tested their ability to pull down PP2A:B55 from cells (Fig. 3b and Extended Data Fig. 9e,f). Although only a single point variant exhibited reduced B55 and PP2Ac binding (Y36A), both 5-Ala variants of YFP–ARPP19—32–36 and 37–41—were unable to pull down B55.
Protein: DP03404 (UniProt P56211)
Region: residues 47	to 56
Annotation: protein phosphatase 2A binding (Molecular function)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
To test whether these ARPP19 residues contribute to B55 binding in cells, we generated 5-Ala and single point variants for the ARPP19 α2–α3 loop and helix α3 and tested their ability to pull down PP2A:B55 from cells. Although B55 binding to the 42AAAAA46 variant was unchanged, the 47AAAAA51 and 52AAAAA56 variants could not pull down B55 (Fig. 3b). Multiple single alanine mutations for ARPP19 residues 47–56 also exhibited reductions in B55 and PP2Ac binding, particularly L53A and R52A (less than 25% compared with wild type), R50A and F48A (around 50% compared with wild type) and L49A and K55A (approximately 75% compared with wild type) (Fig. 3e and Extended Data Fig. 9g).
Protein: DP03404 (UniProt P56211)
Region: residues 57	to 76
Annotation: protein phosphatase 2A binding (Molecular function)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
Consistent with the structure, pull-down experiments using YFP–ARPP19 5-Ala variants, in which the kink and helix α4 residues are mutated to alanine (57AAAAA61, 62AAAAA66, 67AAAAA71 and 72AAAAA76), weaken B55 binding, albeit not to the same extent as 5-Ala variants of α2 or α3 (Fig. 3b).
Protein: DP03404 (UniProt P56211)
Region: residues 76	to 112
Annotation: protein phosphatase inhibitor activity (Molecular function)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
Similarly, comparing the half-maximal inhibitory concentrations (IC50) of ARPP19 and a C-terminal deletion (ARPP19–75) with and without thiophosphorylation shows that the interaction of the C terminus with B55 is essential for the potent inhibition of PP2A:B55 (Fig. 3l and Extended Data Table 1), as the C-terminal deletion variants either do not inhibit (non-phosphorylated ARPP19 versus ARPP1919–75) or become a more than 50-fold weaker inhibitor (tpARPP19 versus tpARPP1919–75).
Protein: DP03404 (UniProt P56211)
Region: residues 1	to 112
Annotation: protein phosphatase inhibitor activity (Molecular function)
Evidence: fluorescence evidence used in manual assertion
Supporting statements:
We quantified PP2A:B55 inhibition by ARPP19, thiophosphorylated ARPP19 (full-length (amino acids 1–112) and phosphorylated with ATPγS using MASTL kinase) and FAM122A (N-terminal domain (amino acids 1–124) (FAM122ANterm)) (Fig. 1b). Whereas PP2A:B55 was only moderately inhibited by ARPP19, it was strongly inhibited by both thiophosphorylated ARPP19 and FAM122ANterm (Extended Data Table 1 and Extended Data Fig. 2a), with thiophosphorylated ARPP19 inhibiting PP2A:B55 around 250-fold more potently than FAM122A.
Protein: DP03404 (UniProt P56211)
Region: residues 20	to 112
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
For ARPP19, around 90 N/HN cross-peaks (residues 20–112) showed reduced intensities.
Protein: DP03405 (UniProt P56211-2)
Region: residues 1	to 96
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The bioinformatical analyses were experimentally confirmed in 1H–15N 2D HSQC spectra of ARPPs, that is, the disordered nature of ARPPs manifests itself as low dispersion of chemical shift in the 1HN dimension, all amide proton resonances falling between 7.7 and 8.5 ppm.
In this paper, we have presented a nearly complete assignment of main-chain 1H, 13C, and 15N chemical shifts in two intrinsically disordered proteins, ARPP-16 and ARPP-19.
Cross-references: BMRB:27911
Protein: DP03406 (UniProt P0A7G2)
Region: residues 101	to 133
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Order parameters, S2, derived by comparing CSI versus RCI values, indicate an increased flexibility for the 33 C-terminal residues of RbfA.
Cross-references: BMRB:27857
Protein: DP03406 (UniProt P0A7G2)
Region: residues 109	to 133
Annotation: disorder (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
Limited  tryptic  proteolysis  of purified   full-length   RbfA   revealed   preferential cleavage   at   residue   Arg108,   indicating   that   the C-terminal  25  residue  sequence  is  susceptible  to digestion by protease and possibly flexible.
Protein: DP03406 (UniProt P0A7G2)
Region: residues 109	to 133
Annotation: disorder (Structural state)
Evidence: cleavage assay evidence used in manual assertion
Supporting statements:
A  limited  trypsin  proteolysis  revealed  that  RbfA indeed  contained  an  easily  degradable  portion and   a   relatively   compact   region   resistant   to moderate  proteolysis .  The  molecular mass of the trypsin-resistant fragment was determined   to   be   12,143 Da   by   mass   spectroscopy, which  corresponds  to  an  RbfA  fragment  with  its C-terminal 25 residues truncated. 
The limited proteolysis data suggest that RbfA may have a C-terminal extension that is poorly  structured at least when the protein exists free from ribosomes.
Protein: DP03406 (UniProt P0A7G2)
Region: residues 109	to 133
Annotation: protein binding (Molecular function)
Evidence: qualitative western immunoblotting evidence used in manual assertion
Supporting statements:
In order to test whether the C-terminal regions of RbfA share a similar function, we studied the cellular localization of RbfAD25 by sucrose density-gradient centrifugation   followed by Western blotting. In cells expressing exogenous full-length RbfA, although the majority of the protein existed in soluble fractions, a significant amount co-fractionated with 30 S ribosomal subunits. In contrast, the truncated protein existed exclusively in the soluble fractions,  indicating that the C-terminal region of RbfA is required for its stable binding to 30 S subunits.