LiteFold/DisProt huggingface dataset:
Protein: DP02345 (UniProt Q92804)
Region: residues 323	to 354
Annotation: flexible linker (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Architecturally, TAF15 is composed of an intrinsically unstructured N-terminal QGSY rich activation domain which is retained in the oncogenic fusions and possesses trans-activating properties, followed by a central and the C-terminal region comprising the RNA recognition motif (RRM) and a (Cys)4 RanBP2 type Zinc finger (ZnF) with interspersed unstructured elements rich in arginine and glycine, known as RGG motifs. The RRM exhibits highest degree of sequence conservation among the members of the FET family.
15N-{1H} Het-NOE values, corresponding to an average of ~0.75 in the RRM and ZnF domains, and ~0.38 in the RGG linker, indicated the presence of highly dynamic linker between the structured RRM and the RanBP2 type ZnF domain in the multi-domain protein
Moreover, random coil index analysis (RCI) of the backbone32 revealed the absence of any secondary structural elements between E323-K354, which constitute the RGG motif.
conclusively establish the predominant role played by RRM in mediating RNA binding and negate any significant contributions toward RNA recognition by the RGG motifs and the RanBP2 type zinc finger
Very few residues in the RGG motif (E323-R326 and G342), and the RanBP2 type zinc finger domain (S355, F370-R372) exhibited CSPs above the averaged CSP + 1σ (Fig. 2C). The CSPs in E323-R326 region can be explained from its existence as an extension of the C-terminal region of the RRM, which may provide additional contributions in stabilizing the complex. Despite these additional contributions, N- or C-terminal extensions in an RRM have been rarely shown to provide specificity in recognition
Protein: DP02346 (UniProt Q9BTL3)
Region: residues 2	to 45
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The HSQC of the unbound RAM shows that the majority of backbone amide peaks lie within a narrow range of chemical shifts in the proton dimension (7.9-8.5 PPM). There are 3–5 peaks at lower 1H chemical shifts which may indicate some small region(s) of ordered structure. However, the signals broadened significantly in presence of RNMT, showing a wider range of chemical shifts. These data indicate that RAM 2–45 is likely to be flexible in solution, but stabilised by binding to RNMT.
Protein: DP02346 (UniProt Q9BTL3)
Region: residues 2	to 45
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The HSQC of the unbound RAM shows that the majority of backbone amide peaks lie within a narrow range of chemical shifts in the proton dimension (7.9-8.5 PPM). There are 3–5 peaks at lower 1H chemical shifts which may indicate some small region(s) of ordered structure. However, the signals broadened significantly in presence of RNMT, showing a wider range of chemical shifts. These data indicate that RAM 2–45 is likely to be flexible in solution, but stabilised by binding to RNMT.
RNMT - RAM interaction does not alter the RNMT core structure but stabilises RAM.
Cross-references: PDB:5E8J
Protein: DP02346 (UniProt Q9BTL3)
Region: residues 2	to 45
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
RAM 2–45 is likely to be flexible in solution, but stabilised by binding to RNMT.
RNMT - RAM interaction does not alter the RNMT core structure but stabilises RAM.
RAM binds to the RNMT surface distal to the active site, resulting in stabilisation of a series of RNMT structures including a lobe which co-evolved with RAM in vertebrates.
Cross-references: PDB:5E8J
Protein: DP02346 (UniProt Q9BTL3)
Region: residues 2	to 45
Annotation: molecular function activator activity (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
RAM binds to the RNMT surface distal to the active site, resulting in stabilisation of a series of RNMT structures including a lobe which co-evolved with RAM in vertebrates.
RNMT also has an activating subunit, RAM (RNMT-activating miniprotein)
Cross-references: PDB:5E8J
Protein: DP02348 (UniProt Q8N5F7)
Region: residues 1	to 328
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Tha Cryo-EM structure of the Human spliceosomal PM5 C* complex, shows this region is disordered.
Cross-references: PDB:8C6J
EMDB:16452
Protein: DP02348 (UniProt Q8N5F7)
Region: residues 1	to 328
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
NKAP is a 415 residue protein implicated in T-cell development; it consists of highly charged repetitive sequences like Ser-Arg and poly-Lys and is expected to be intrinsically disordered through almost its entire length. However, residues 329-358 form a short helix that bridges the N- and C-terminal fragments of Slu7 bound to Prp8 and stabilizes the P complex.
The PDB structure is about the Human post-catalytic P complex spliceosome not of this protein in solution. 
Cross-references: PDB:6QDV
EMDB:4525
Protein: DP02348 (UniProt Q8N5F7)
Region: residues 359	to 415
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
NKAP is a 415 residue protein implicated in T-cell development; it consists of highly charged repetitive sequences like Ser-Arg and poly-Lys and is expected to be intrinsically disordered through almost its entire length. However, residues 329-358 form a short helix that bridges the N- and C-terminal fragments of Slu7 bound to Prp8 and stabilizes the P complex.
The PDB structure is about the Human post-catalytic P complex spliceosome not of this protein in solution.
Cross-references: PDB:6QDV
EMDB:4525
Protein: DP02348 (UniProt Q8N5F7)
Region: residues 1	to 328
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
Table S2 shows the region 329-358 is the only one with electron density capable of being modeled. Indicating the rest of the protein is disordered in the cryo-EM structure of human C* complex.
Cross-references: EMDB:32321
PDB:7W5B
Protein: DP02348 (UniProt Q8N5F7)
Region: residues 359	to 415
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
Table S2 shows the region 329-358 is the only one with electron density capable of being modeled. Indicating the rest of the protein is disordered in the cryo-EM structure of human C* complex.
Cross-references: EMDB:32321
PDB:7W5B
Protein: DP02349 (UniProt P51825)
Region: residues 738	to 760
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
1H-15N heteronuclear NOE experiments show that AF4 residues 761-775 are ordered in the complex whereas the remainder is flexible
The AF4-AF9 fusion included an N-terminal 6-his tag and TEV protease site, with the coding sequence for AF4 residues 738-779 directly fused to AF9 residues 490-568 in pET 32a
Cross-references: PDB:2LM0
Protein: DP02353 (UniProt P0DMV9)
Region: residues 229	to 306
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Here, we describe a new crystal form of the human Hsp70 ATPase domain. The refined structure of this new crystal form is compared with that previously reported (Sriram et al., 1997) and provides evidence for the flexibility of the IIB subdomain of the structure, which corresponds to residues 229-306 (Flaherty et al., 1990)
Protein: DP02357 (UniProt O14187)
Region: residues 1	to 46
Annotation: disorder (Structural state)
Evidence: microscopy evidence used in manual assertion
Supporting statements:
Except for the N-terminal 46 amino acids and the C-terminal Jab1/MPN domain, most of the Spp42 sequences have a well-defined EM density
Cross-references: PDB:3JB9
Protein: DP02357 (UniProt O14187)
Region: residues 2044	to 2363
Annotation: disorder (Structural state)
Evidence: microscopy evidence used in manual assertion
Supporting statements:
Except for the N-terminal 46 amino acids and the C-terminal Jab1/MPN domain, most of the Spp42 sequences have a well-defined EM density
The Jab1/MPN domain (residues 2044 to 2363) is disordered
The Jab1/MPN domain, responsible for binding the ATPase/helicase Brr2 (17, 18), is flexible and disordered in our structure.
Cross-references: PDB:3JB9
Protein: DP02359 (UniProt Q8IYB3)
Region: residues 300	to 350
Annotation: localization (Biological process)
Evidence: immunodetection assay evidence used in manual assertion
Supporting statements:
Dissecting the N-terminal domain further showed that SRm160300–350 was sufficient to target EGFP to the paraspeckle region adjacent to speckled domains
Amino acids 300–350 targeted SRm160 to sites on the nuclear matrix and peripheral to speckled domains. EGFP-SRm160300–350 was transiently expressed in HeLa cells. EGFP-SRm160300–350 (A) in fixed cells was concentrated in and around speckled domains (overlay, C) as visualized by the B1C8 antibody for SRm160 (B) but was also visible in nucleoli. (D) EGFP-SRm300300–350 remained bound after the removal of soluble proteins and chromatin in a nuclear matrix preparation.
amino acids 300–350, although necessary for targeting the SRm160 N terminus to speckled domains, were inefficient in anchoring the EGFP fusion protein to speckled domains.
Using a series of FLAG- and enhanced GFP-conjugated deletion mutants we found two contiguous sequences that independently target SRm160 to nuclear matrix sites at splicing speckled domains: amino acids 300–350 and 351–688. Constructs containing amino acids 300–350 were also targeted to sites peripheral to speckled domains where most mRNA originate subsequent to splicing. Sequences from the N-terminal domain localized proteins to the nuclear lamina near sites where mRNA leaves the nucleus.
In this study we identified domains of SRm160 important for spatial targeting within the nucleus and for binding to the nuclear matrix.
The spatial targeting and nuclear matrix binding domains of SRm160.
Protein: DP02359 (UniProt Q8IYB3)
Region: residues 351	to 688
Annotation: localization (Biological process)
Evidence: immunodetection assay evidence used in manual assertion
Supporting statements:
We have identified the sequences within the splicing coactivator SRm160 that target it to the splicing factor-rich, speckled domains of the nucleus. These consist of two contiguous sequence domains of SRm160: amino acids 300–350 and 351–688. Both sequences are characterized by an unusual high content of arginine, proline, and serine: 88% for SRm160300–350 and 64% for SRm160351–688.
Using a series of FLAG- and enhanced GFP-conjugated deletion mutants we found two contiguous sequences that independently target SRm160 to nuclear matrix sites at splicing speckled domains: amino acids 300–350 and 351–688. 
In this study we identified domains of SRm160 important for spatial targeting within the nucleus and for binding to the nuclear matrix.
The spatial targeting and nuclear matrix binding domains of SRm160.
Protein: DP02359 (UniProt Q8IYB3)
Region: residues 151	to 377
Annotation: molecular condensate scaffold activity (Molecular function)
Evidence: combinatorial evidence used in manual assertion
Supporting statements:
To test whether this SRRM1 fragment undergoes RNA-dependent phase separation, we performed titration experiments with total HeLa cell RNA followed by microscopic analyses. At protein/RNA ratios of 0.25 and 0.5, formation of condensates was observed at protein concentrations of 2.5–30 μM SRRM1 (Figure ​7A and B). Also, in the inverse experiment, a titration of increasing amounts of RNA at a given SRRM1 concentration of 10 μM resulted in robust condensate formation (Figure  7C). These findings were cross-validated in centrifugation sedimentation experiments (Figure ​7D). In none of the experiments, condensate formation or sedimentation was observed in the absence of RNA, demonstrating that SRRM1 is capable of RNA-dependent phase separation as observed for Loc1p.
Protein: DP02360 (UniProt O14810)
Region: residues 74	to 83
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
We next co-crystallized SNAREΔ60 with a CPX fragment (scCPX) consisting of its central and accessory helices (residues 26–83) and containing three “superclamp” mutations (D27L, E34F, R37A) that increase its clamping efficiency both in vitro19 and in vivo38. The structure was determined at 3.5 Å resolution using the truncated SNARE complex as a search model in the molecular replacement method (Table 1), and CPX was modeled into difference electron density. The final model includes residues 190–250 of syntaxin1, 10–74 and 141–203 of SNAP25, 29–60 of VAMP2, and 26–73 of CPX
Cross-references: PDB:3RL0
PDB:3RK3
Protein: DP02361 (UniProt O95429)
Region: residues 357	to 376
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Chemical shift distribution and local flexibility of the construct. The upper panel shows the chemical shift distribution for Cα and Cβ as determined by Eq. 1. Positive values are indicators for α‐helical secondary structure. The lower panel shows the ratio of T 1/T 2 15N relaxation times as a measure for local flexibility. Lower values indicate higher flexibility.
The green box shows the N‐terminal unstructured region present in our construct
The N‐terminus G353–T376 of our construct is unstructured as indicated by the lower T 1/T 2 ratios measured from the relaxation rates (Fig. 2). Furthermore, these residues do not show any long‐range NOEs. This demonstrates that the N‐terminus of our construct does not belong to the BAG domain of SODD and its presence does not induce a shift of helix 1 to a position suggested by the original sequence alignment.
Cross-references: PDB:1M7K
Protein: DP02364 (UniProt Q9H6Z4-3)
Region: residues 31	to 45
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
N-terminally GST-tagged RanBP3 NLS (human, isoform 3, also known as RanBP3-b, residues 31–60; UniProt code, Q9H6Z4)
Residues 46–59 of RanBP3 bound to the major NLS-binding site in an extended conformation were identified unambiguously in the electron density map (Fig. 1A). The other residues of RanBP3 did not have defined electron density, indicating that these residues were disordered in the crystal.
Cross-references: PDB:5XZX
Protein: DP02365 (UniProt Q13464)
Region: residues 895	to 913
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
However, unlike our previous structure of the Rock SBD, residues 895–913 were disordered
Cross-references: PDB:5F5P
Protein: DP02368 (UniProt P29536)
Region: residues 299	to 313
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The structure of Lmod1ABS2, the strongest nucleator among the naturally occurring ABS2s analysed here , was determined at 1.54 Å resolution , and shows residues Ala-314 to Gln-486
Cross-references: PDB:4Z79
Protein: DP02369 (UniProt Q00780)
Region: residues 570	to 612
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues 613–743 of each crystallographically independent chain have clear and continuous density, whereas the N-terminal 42 residues and the His6 tag are invisible and presumed disordered.
Cross-references: PDB:1O91
Protein: DP02371 (UniProt O08583)
Region: residues 77	to 104
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The N-terminal tail consisting of residues Ser77 to Gly104 is highly disordered, as deduced from the secondary chemical shifts, the lack of medium-range and long-range NOEs and the {1H}-15N heteronuclear NOEs
It should also be noted that the N-terminal region of ALY77−182 which corresponds to residues 77−104 is flexible and without regular structure. This N-terminal “tail” contains several aliphatic and aromatic side chains that could also modulate interactions.
Although chemical shift dispersion of the majority of the backbone HN protons is good, overlap was observed for many of the loop regions as well as the N-terminal flexible region.
1H-15N-correlated NMR spectrum of ALY77−182 exhibits signals characteristic of a folded protein plus sharp overlapped resonances indicative of flexible regions
Cross-references: PDB:1NO8
Protein: DP02371 (UniProt O08583)
Region: residues 84	to 95
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Nevertheless, residues Asp84 to Phe95 exhibit some restriction of motion, as indicated by {1H}-15N heteronuclear NOEs in the range of 0.1−0.2.
Cross-references: PDB:1NO8
Protein: DP02371 (UniProt O08583)
Region: residues 77	to 182
Annotation: RNA folding chaperone (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
ALY itself exhibits RNA binding activity and may act as an RNA chaperone by modulating the formation of RNA−protein and RNA−RNA complexes
Cross-references: PDB:1NO8
Protein: DP02371 (UniProt O08583)
Region: residues 77	to 182
Annotation: molecular adaptor activity (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
ALY itself exhibits RNA binding activity and may act as an RNA chaperone by modulating the formation of RNA−protein and RNA−RNA complexes
Recently, it was reported that ALY is a component of the general mRNA export machinery
Cross-references: PDB:1NO8
Protein: DP02372 (UniProt Q88MI5)
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:
In GraT, on the other hand, the first 22 N-terminal residues together with the 6-His tag are located in an interstitial space and could not be traced due to lack of electron density.
The N-terminus of GraT is intrinsically disordered
Cross-references: PDB:6F8S
Protein: DP02372 (UniProt Q88MI5)
Region: residues 1	to 22
Annotation: molecular function activator activity (Molecular function)
Evidence: mutant phenotype evidence used in manual assertion
Supporting statements:
GraT induction results in a distinct cleavage pattern on lpp mRNA, which is not detected in non-induced samples (Fig. 6, source data are provided as a Source Data file). Most of the observed cut sites are located between the 2nd and 3rd nucleotides of codons with adenine in the 2nd position. The only exception is the 10th cleavage (Fig. 6), which is found between two codons but still following an A nucleotide. Strong codon dependence suggests that, like other HigB family toxins, GraT acts as a ribosome-dependent mRNase. Given that induction of Δ22GraT did not result in mRNA cleavage (Fig. 6), the N-terminal disordered region is necessary for GraT mRNAse activity.
Protein: DP02372 (UniProt Q88MI5)
Region: residues 1	to 22
Annotation: entropic chain (Disorder function)
Evidence: combinatorial experimental and author inference evidence contained in single publication used in manual assertion
Supporting statements:
On the other hand, this disordered stretch is more likely to work as an entropic barrier that sterically impedes the formation of the GraT2A2-DNA complex.
Cross-references: PDB:6F8S
Protein: DP02372 (UniProt Q88MI5)
Region: residues 1	to 22
Annotation: entropic chain (Disorder function)
Evidence: electrophoretic mobility shift assay evidence used in manual assertion
Supporting statements:
EMSAs using different (GraT2A2 or Δ22GraT2A2):operator molar ratios further confirm that in contrast to the wild-type GraT2A2, the Δ22GraT2A2 complex readily binds the graTA operator (Fig. 7c, d). These experiments suggest that the intrinsically disordered N-terminus of GraT is directly responsible for impairment of operator binding, likely via steric hindrance.
Protein: DP02372 (UniProt Q88MI5)
Region: residues 1	to 22
Annotation: entropic chain (Disorder function)
Evidence: beta galactosidase functional complementation evidence used in manual assertion
Supporting statements:
β-Galactosidase measurements show that while GraA alone represses the graTA promoter activity, the expression of the GraTA complex leads to full derepression of the promoter (Fig. 8a, source data are provided as a Source Data file). Expression of the Δ22GraTA with N-terminally truncated GraT again represses the promoter (Fig. 8a), which is in good accordance with strong binding of Δ22GraT2A2 to the operator (Fig. 7).
Protein: DP02373 (UniProt Q92837)
Region: residues 1	to 198
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
missing residues in the PDB
Cross-references: PDB:5OY4
Protein: DP02373 (UniProt Q92837)
Region: residues 224	to 279
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
missing residues in the PDB
Cross-references: PDB:5OY4
Protein: DP02373 (UniProt Q92837)
Region: residues 188	to 226
Annotation: molecular function inhibitor activity (Molecular function)
Evidence: sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion
Supporting statements:
we demonstrate that FRATtide (a peptide corresponding to residues 188–226 of FRAT1) binds to GSK3 and prevents GSK3 from interacting with Axin.
Demonstrated also in PMID:19802005, a short peptide (FRATtide) comprising amino-acids 188–226 from human FRAT1 is sufficient to inhibit GSK3
Protein: DP02375 (UniProt Q96T58)
Region: residues 3470	to 3494
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
No electron density was observed for the 25 N-terminal residues (amino acids 3470-3494) and three residues (amino acids 3542-3544) in a loop region. SDS-PAGE analysis of dissolved crystals showed that the crystals contain the full-length fragment, suggesting that these regions are disordered (data not shown).
Cross-references: PDB:1OW1
Protein: DP02376 (UniProt Q4ACU6)
Region: residues 588	to 600
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Superposition of the eight molecules per asymmetric unit of Shank3 PDZ showed that they diverge structurally mainly in the more or less defined loop (disordered loop region between residues 588‐600 for all molecules) connecting strands βB and βC as well as in the location of their N‐ and C‐termini
The dashed line indicates a disordered loop (residues 588–600)
Cross-references: PDB:3O5N