LiteFold/DisProt huggingface dataset:
Protein: DP01640 (UniProt Q13351)
Region: residues 27	to 31
Annotation: protein destabilization (Biological process)
Evidence: luciferase reporter gene assay evidence used in manual assertion
Supporting statements:
s expected, the RLuc/FLuc ratio of each construct was found to increase linearly as a function of the five different concentrations of EKLF expression vector tested (Figure 5A). Linear regression analysis of this data was used to calculate a slope indicative of the stability of each EKLF constructs. Under these assay conditions, the levels of the EKLF-RLuc protein were slightly more than 2-fold lower than both the ΔTAD-EKLF-RLuc and the F27S/L28S/W31S-EKLF proteins (Figure 5B). In addition, the levels of the ΔTAD-EKLF-RLuc and the F27S/L28S/W31S-EKLF proteins were very similar. These results are in agreement with earlier studies showing that the PEST1 region within the minimal TAD of EKLF plays a significant role in ubiquitin-mediated degradation of EKLF (Quadrini and Bieker, 2006) and further establishes that the UBI-interacting domain in EKLF plays an important role in regulating its steady-state levels.
The Minimal TAD of EKLF Functions as a “Degron” in Cells
Protein: DP01641 (UniProt Q07955)
Region: residues 196	to 215
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Residues from 107–120 and from 196–215 are disordered in the structure calculations, and increased mobility of this section is confirmed by 15N relaxation measurements (supplementary Fig S2 online).
Cross-references: PDB:2O3D
Protein: DP01641 (UniProt Q07955)
Region: residues 107	to 120
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Residues from 107–120 and from 196–215 are disordered in the structure calculations, and increased mobility of this section is confirmed by 15N relaxation measurements (supplementary Fig S2 online).
Cross-references: PDB:2O3D
Protein: DP01641 (UniProt Q07955)
Region: residues 196	to 248
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The two-dimensional 15N-1H heteronuclear single quantum coherence (HSQC) spectrum of SRSF1(RS) had a narrow chemical shift dispersion pointing to extensive structural disorder (Figure 1B).
 In addition, large NMR line-widths (Figure 1B) indicate the presence of conformational exchange occurring on the micro-to-millisecond timescale. Taken together, the NMR data demonstrate that SRSF1(RS) is disordered and highly dynamic.
Protein: DP01641 (UniProt Q07955)
Region: residues 196	to 248
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Phosphorylation strongly changed the 15N-1H HSQC spectrum (Figure 1B).
 Taken together, NMR spectroscopy revealed that phosphorylation of the RS dipeptides in SRSF1(RS) causes a switch from a disordered conformation to a partially rigidified structure.
NMR spectroscopy demonstrated a dramatic phosphorylation-induced change in the flexibility of the RS and RS1 domains of SRSF1 (Figures 1C, 2E, and 2F).
Protein: DP01641 (UniProt Q07955)
Region: residues 204	to 219
Annotation: phosphorylation display site (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Sequence-specific resonance assignment unambiguously identified phosphorylated serines in the RS repeat stretches comprising residues 204–219 and 242–247.
NMR resonance assignment revealed that serines from S207–S217 were phosphorylated to 100% (Figures 2B and 2D).
Protein: DP01641 (UniProt Q07955)
Region: residues 242	to 247
Annotation: phosphorylation display site (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Sequence-specific resonance assignment unambiguously identified phosphorylated serines in the RS repeat stretches comprising residues 204–219 and 242–247.
Protein: DP01642 (UniProt P06492)
Region: residues 350	to 394
Annotation: disorder (Structural state)
Evidence: small-angle X-ray scattering evidence used in manual assertion
Supporting statements:
Interestingly, these two regions correlate well with the space most likely taken up by N-terminal residues 1−48 which were not included in the conserved VP16 core structure, and an apparent disordered segment in the crystal (residues 350−394; the boundaries correspond to the termini of the orange helix and strand, respectively).
In the crystal structure, the peptide is disordered between the orange helix and orange strand (residues 350−394).
HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).
Protein: DP01642 (UniProt P06492)
Region: residues 403	to 490
Annotation: disorder (Structural state)
Evidence: small-angle X-ray scattering evidence used in manual assertion
Supporting statements:
In contrast, the area that the remaining C-terminal “domain” (residues 403−490) is anticipated to occupy (corresponding to the bottom part of the shapes in Figure 5) only shows a small spatial extension to the globular core; i.e., it would not be possible to accommodate all C-terminal residues within the envelope. It seems likely that these residues are responsible for the intensity increase (and indicative of random chainlike behavior) observed in the very low-angle scattering regime.
Thus, we conclude that the C-terminal activation domain is disordered and particularly nonglobular in its native solution state and does not contribute to the globular core but extends into the solvent.
HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).
Protein: DP01642 (UniProt P06492)
Region: residues 412	to 490
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The absence of secondary and tertiary structure in aqueous solution at 35 °C, which is implied by Figure 2, is confirmed by inspection of two-dimensional NOE (NOESY) and rotating-frame NOE (ROESY) spectra of SAD and LAD. Intraresidue and CaH,-NHm sequential NOEs are observed, characteristic of an extended polypeptide chain; however, no sequential NH-NH,+1 NOEs, which are indicative of helical
or nonhelical turns, are observed.
Protein: DP01642 (UniProt P06492)
Region: residues 412	to 490
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The (1H,15N)-HSQC spectrum of VP16ad shows a small dispersion of intense signals in the proton dimension (<1 ppm), indicative for a lack of secondary structure. 
HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).
Cross-references: BMRB:6099
Protein: DP01642 (UniProt P06492)
Region: residues 412	to 490
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
In both activation subdomains negative 1HN, 15N, and 1Hα as well as positive 13Cα and 13C‘ resonance shifts are observed, indicative for α-helix formation.
From these analysis, we can clearly observe the formation of α-helices in the 443−447 and 469−483 region (Figure 4), especially since we have to take into account that resonances have only been mapped until a 1:10 complex.
Nevertheless, the NOE patterns clearly indicate that VP16ad exhibits an α−helical propensity throughout the sequence, except for the proline-rich 453−464 region. Many NOE contacts, indicative for an α-helix, are observed for residues 429−450 and 465−488 in both subdomains.
HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).
Cross-references: PDB:2PHG
PDB:2PHE
Protein: DP01642 (UniProt P06492)
Region: residues 412	to 490
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The titration experiments show progressive changes of the amide 1H and 15N chemical shifts, indicative for fast exchange between the bound and free states on the NMR time scale.
HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).
Cross-references: PDB:2PHG
Protein: DP01642 (UniProt P06492)
Region: residues 452	to 490
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The limited dispersion of the backbone 15N and1HN chemical shifts in the HSQC spectrum of15N-labeled VP16C alone (Fig.1A) and the intermediate values (∼7 Hz) of 1HN-1HCα coupling constants (11) indicated that VP16C alone has negligible secondary structure (12).
The VP16 gene fragment used in this publication was chemically synthesized. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).
Protein: DP01642 (UniProt P06492)
Region: residues 452	to 490
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Titration of15N-labeled VP16C with unlabeled TAF1–140 resulted in progressive rather than bimodal changes of the backbone 15N and 1HN chemical shifts (Fig. 1A), thus indicating that VP16C interacts weakly with TAF1–140 and hence exchanges rapidly between the free and bound states on the NMR time scale (13).
The VP16 gene fragment used in this publication was chemically synthesized. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).
Protein: DP01642 (UniProt P06492)
Region: residues 452	to 490
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Significant chemical shift changes were observed only for the β protons of Asp472, Phe479, Leu483, and Asp486 (Fig.1C). These four residues lie within and adjacent to the region of VP16C that is suggested by backbone chemical shift perturbation to undergo an induced folding transition.
Titration of15N-labeled VP16C with unlabeled TAF1–140 resulted in progressive rather than bimodal changes of the backbone 15N and 1HN chemical shifts (Fig. 1A), thus indicating that VP16C interacts weakly with TAF1–140 and hence exchanges rapidly between the free and bound states on the NMR time scale (13).
The VP16 gene fragment used in this publication was chemically synthesized. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).
Protein: DP01642 (UniProt P06492)
Region: residues 452	to 490
Annotation: molecular function activator activity (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Titration of15N-labeled VP16C with unlabeled TAF1–140 resulted in progressive rather than bimodal changes of the backbone 15N and 1HN chemical shifts (Fig. 1A), thus indicating that VP16C interacts weakly with TAF1–140 and hence exchanges rapidly between the free and bound states on the NMR time scale (13).
The VP16 gene fragment used in this publication was chemically synthesized. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).
Protein: DP01642 (UniProt P06492)
Region: residues 456	to 490
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
NMR structural studies demonstrate that VP16C is disordered in the free state, and forms a 9-residue α-helix involving residues Asp472 to Thr480 in complex with Tfb1.
The VP16 gene fragment used in this publication was derived from the Human herpesvirus 1 KOS strain. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).
Protein: DP01642 (UniProt P06492)
Region: residues 456	to 490
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Addition of VP16C (VP16456−490) to 15N-labeled Tfb11−115 produced changes in 1H and 15N chemical shifts for several signals of Tfb11−115 in the 2D 1H−15N HSQC spectra (Figure 1).
The structure of the Tfb11−115/VP16C complex is well defined by the NMR data (Figure 2).
The VP16 gene fragment used in this publication was derived from the Human herpesvirus 1 KOS strain. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).
Cross-references: PDB:2K2U
Protein: DP01642 (UniProt P06492)
Region: residues 469	to 485
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
As anticipated, free VP16 469–485 exhibited very few NOEs; only sequential NOEs between CαH and NH protons [d α N(i,i+1) NOEs] were clearly observed, indicative of an extended random-coil structure (19).
The VP16 gene fragment used in this publication was chemically synthesized. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).
Protein: DP01642 (UniProt P06492)
Region: residues 469	to 485
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
In contrast, VP16469–485 in the presence of 0.1 mole equivalents of TAF1–140 showed numerous NOE cross-peaks, including a substantial number arising fromdNN(i,i+1),dαN(i,i), and dαβ(i,i+3) NOEs. The overall pattern of the NOE connectivities (Fig.3B) is characteristic of that observed for α-helical secondary structure, especially in the region from Asp472 to Leu483. Thus, residues 472 to 483 of VP16C, and perhaps even residues flanking this region, adopt an α-helical structure when bound to TAF1–140(20).
The VP16 gene fragment used in this publication was chemically synthesized. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).
Protein: DP01642 (UniProt P06492)
Region: residues 469	to 485
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
To determine the structure of VP16 469 – 485 bound to TAF1–140, we performed transferred nuclear Overhauser effect (TRNOE) experiments.
Thus, residues 472 to 483 of VP16C, and perhaps even residues flanking this region, adopt an α-helical structure when bound to TAF1–140(20).
The VP16 gene fragment used in this publication was chemically synthesized. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).
Protein: DP01642 (UniProt P06492)
Region: residues 469	to 485
Annotation: molecular function activator activity (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Thus, residues 472 to 483 of VP16C, and perhaps even residues flanking this region, adopt an α-helical structure when bound to TAF1–140(20).
The VP16 gene fragment used in this publication was chemically synthesized. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).
Protein: DP01642 (UniProt P06492)
Region: residues 475	to 484
Annotation: molecular function activator activity (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Sequential assignment of the HSQC cross-peaks (14) established that the backbone-perturbed residues are located within a region at the COOH-terminal end of VP16C that encompasses residues 475 to 484 (Fig. 1B).
The VP16 gene fragment used in this publication was chemically synthesized. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).
Protein: DP01642 (UniProt P06492)
Region: residues 475	to 484
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Sequential assignment of the HSQC cross-peaks (14) established that the backbone-perturbed residues are located within a region at the COOH-terminal end of VP16C that encompasses residues 475 to 484 (Fig. 1B).
The VP16 gene fragment used in this publication was chemically synthesized. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).
Protein: DP01642 (UniProt P06492)
Region: residues 475	to 484
Annotation: protein binding (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Sequential assignment of the HSQC cross-peaks (14) established that the backbone-perturbed residues are located within a region at the COOH-terminal end of VP16C that encompasses residues 475 to 484 (Fig. 1B).
The VP16 gene fragment used in this publication was chemically synthesized. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).
Protein: DP01642 (UniProt P06492)
Region: residues 412	to 456
Annotation: protein binding (Molecular function)
Evidence: isothermal titration calorimetry evidence used in manual assertion
Supporting statements:
By this method, VP16C bound to Tfb1 with an apparent Kd of 360 ± 40 nM and VP16N bound to Tfb1 with an apparent Kd of 1000 ± 100 nM (Table 1). These results suggested that both subdomains of the VP16TAD were capable of interacting with Tfb1, and the Kd obtained for the Tfb1/VP16C complex is very similar to the Kd observed between Tfb1 and the p53TAD2 (390 nM).
The VP16 gene fragment used in this publication was derived from the Human herpesvirus 1 KOS strain. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).
Protein: DP01642 (UniProt P06492)
Region: residues 456	to 490
Annotation: protein binding (Molecular function)
Evidence: isothermal titration calorimetry evidence used in manual assertion
Supporting statements:
By this method, VP16C bound to Tfb1 with an apparent Kd of 360 ± 40 nM and VP16N bound to Tfb1 with an apparent Kd of 1000 ± 100 nM (Table 1). These results suggested that both subdomains of the VP16TAD were capable of interacting with Tfb1, and the Kd obtained for the Tfb1/VP16C complex is very similar to the Kd observed between Tfb1 and the p53TAD2 (390 nM).
The VP16 gene fragment used in this publication was derived from the Human herpesvirus 1 KOS strain. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).
Protein: DP01642 (UniProt P06492)
Region: residues 456	to 490
Annotation: molecular function activator activity (Molecular function)
Evidence: isothermal titration calorimetry evidence used in manual assertion
Supporting statements:
By this method, VP16C bound to Tfb1 with an apparent Kd of 360 ± 40 nM and VP16N bound to Tfb1 with an apparent Kd of 1000 ± 100 nM (Table 1). These results suggested that both subdomains of the VP16TAD were capable of interacting with Tfb1, and the Kd obtained for the Tfb1/VP16C complex is very similar to the Kd observed between Tfb1 and the p53TAD2 (390 nM).
The VP16 gene fragment used in this publication was derived from the Human herpesvirus 1 KOS strain. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).
Protein: DP01642 (UniProt P06492)
Region: residues 456	to 490
Annotation: molecular function activator activity (Molecular function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Addition of VP16C (VP16456−490) to 15N-labeled Tfb11−115 produced changes in 1H and 15N chemical shifts for several signals of Tfb11−115 in the 2D 1H−15N HSQC spectra (Figure 1).
The structure of the Tfb11−115/VP16C complex is well defined by the NMR data (Figure 2).
The VP16 gene fragment used in this publication was derived from the Human herpesvirus 1 KOS strain. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).
Cross-references: PDB:2K2U
Protein: DP01642 (UniProt P06492)
Region: residues 412	to 456
Annotation: molecular function activator activity (Molecular function)
Evidence: isothermal titration calorimetry evidence used in manual assertion
Supporting statements:
By this method, VP16C bound to Tfb1 with an apparent Kd of 360 ± 40 nM and VP16N bound to Tfb1 with an apparent Kd of 1000 ± 100 nM (Table 1). These results suggested that both subdomains of the VP16TAD were capable of interacting with Tfb1, and the Kd obtained for the Tfb1/VP16C complex is very similar to the Kd observed between Tfb1 and the p53TAD2 (390 nM).
The VP16 gene fragment used in this publication was derived from the Human herpesvirus 1 KOS strain. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).