LiteFold/DisProt huggingface dataset:
Protein: DP01578 (UniProt P41969)
Region: residues 309	to 429
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Chemical shift analysis (Cα, Cβ) showed no stable secondary structure elements in unmodified or phosphorylated Elk-1 TAD (fig. S2B).
Cross-references: BMRB:26762
Protein: DP01578 (UniProt P41969)
Region: residues 335	to 339
Annotation: phosphorylation display site (Disorder function)
Evidence: immunodetection assay evidence used in manual assertion
Supporting statements:
To obtain atomic-resolution insights into phosphorylation of the Elk-1 TAD, we used nuclear magnetic resonance (NMR) spectroscopy (20) to monitor its modification by recombinant ERK2 in vitro (Fig. 1B; fig. S2A). Time-resolved NMR experiments revealed that each phosphorylation proceeded efficiently, but at markedly different rates. Phosphorylation of Thr369 and Ser384, which flank the central Phe–Trp (FW) motif implicated in Mediator interaction (18), occurred faster than modification of Thr364, Thr354 and Ser390, whereas residues Thr418, Ser423 and Thr337 were modified more slowly (Fig. 1C), which we confirmed by immunoblotting (Fig. 1D). 
Cross-references: BMRB:26786
Protein: DP01578 (UniProt P41969)
Region: residues 367	to 371
Annotation: phosphorylation display site (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
To obtain atomic-resolution insights into phosphorylation of the Elk-1 TAD, we used nuclear magnetic resonance (NMR) spectroscopy (20) to monitor its modification by recombinant ERK2 in vitro (Fig. 1B; fig. S2A). Time-resolved NMR experiments revealed that each phosphorylation proceeded efficiently, but at markedly different rates. Phosphorylation of Thr369 and Ser384, which flank the central Phe–Trp (FW) motif implicated in Mediator interaction (18), occurred faster than modification of Thr364, Thr354 and Ser390, whereas residues Thr418, Ser423 and Thr337 were modified more slowly (Fig. 1C), which we confirmed by immunoblotting (Fig. 1D). 
Cross-references: BMRB:26786
Protein: DP01578 (UniProt P41969)
Region: residues 382	to 386
Annotation: phosphorylation display site (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
To obtain atomic-resolution insights into phosphorylation of the Elk-1 TAD, we used nuclear magnetic resonance (NMR) spectroscopy (20) to monitor its modification by recombinant ERK2 in vitro (Fig. 1B; fig. S2A). Time-resolved NMR experiments revealed that each phosphorylation proceeded efficiently, but at markedly different rates. Phosphorylation of Thr369 and Ser384, which flank the central Phe–Trp (FW) motif implicated in Mediator interaction (18), occurred faster than modification of Thr364, Thr354 and Ser390, whereas residues Thr418, Ser423 and Thr337 were modified more slowly (Fig. 1C), which we confirmed by immunoblotting (Fig. 1D). 
Cross-references: BMRB:26786
Protein: DP01578 (UniProt P41969)
Region: residues 362	to 366
Annotation: phosphorylation display site (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
To obtain atomic-resolution insights into phosphorylation of the Elk-1 TAD, we used nuclear magnetic resonance (NMR) spectroscopy (20) to monitor its modification by recombinant ERK2 in vitro (Fig. 1B; fig. S2A). Time-resolved NMR experiments revealed that each phosphorylation proceeded efficiently, but at markedly different rates. Phosphorylation of Thr369 and Ser384, which flank the central Phe–Trp (FW) motif implicated in Mediator interaction (18), occurred faster than modification of Thr364, Thr354 and Ser390, whereas residues Thr418, Ser423 and Thr337 were modified more slowly (Fig. 1C), which we confirmed by immunoblotting (Fig. 1D). 
Cross-references: BMRB:26786
Protein: DP01578 (UniProt P41969)
Region: residues 352	to 357
Annotation: phosphorylation display site (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
To obtain atomic-resolution insights into phosphorylation of the Elk-1 TAD, we used nuclear magnetic resonance (NMR) spectroscopy (20) to monitor its modification by recombinant ERK2 in vitro (Fig. 1B; fig. S2A). Time-resolved NMR experiments revealed that each phosphorylation proceeded efficiently, but at markedly different rates. Phosphorylation of Thr369 and Ser384, which flank the central Phe–Trp (FW) motif implicated in Mediator interaction (18), occurred faster than modification of Thr364, Thr354 and Ser390, whereas residues Thr418, Ser423 and Thr337 were modified more slowly (Fig. 1C), which we confirmed by immunoblotting (Fig. 1D). 
Cross-references: BMRB:26786
Protein: DP01578 (UniProt P41969)
Region: residues 388	to 392
Annotation: phosphorylation display site (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
To obtain atomic-resolution insights into phosphorylation of the Elk-1 TAD, we used nuclear magnetic resonance (NMR) spectroscopy (20) to monitor its modification by recombinant ERK2 in vitro (Fig. 1B; fig. S2A). Time-resolved NMR experiments revealed that each phosphorylation proceeded efficiently, but at markedly different rates. Phosphorylation of Thr369 and Ser384, which flank the central Phe–Trp (FW) motif implicated in Mediator interaction (18), occurred faster than modification of Thr364, Thr354 and Ser390, whereas residues Thr418, Ser423 and Thr337 were modified more slowly (Fig. 1C), which we confirmed by immunoblotting (Fig. 1D). 
Cross-references: BMRB:26786
Protein: DP01578 (UniProt P41969)
Region: residues 416	to 420
Annotation: phosphorylation display site (Disorder function)
Evidence: immunodetection assay evidence used in manual assertion
Supporting statements:
To obtain atomic-resolution insights into phosphorylation of the Elk-1 TAD, we used nuclear magnetic resonance (NMR) spectroscopy (20) to monitor its modification by recombinant ERK2 in vitro (Fig. 1B; fig. S2A). Time-resolved NMR experiments revealed that each phosphorylation proceeded efficiently, but at markedly different rates. Phosphorylation of Thr369 and Ser384, which flank the central Phe–Trp (FW) motif implicated in Mediator interaction (18), occurred faster than modification of Thr364, Thr354 and Ser390, whereas residues Thr418, Ser423 and Thr337 were modified more slowly (Fig. 1C), which we confirmed by immunoblotting (Fig. 1D). 
Cross-references: BMRB:26786
Protein: DP01578 (UniProt P41969)
Region: residues 421	to 425
Annotation: phosphorylation display site (Disorder function)
Evidence: immunodetection assay evidence used in manual assertion
Supporting statements:
To obtain atomic-resolution insights into phosphorylation of the Elk-1 TAD, we used nuclear magnetic resonance (NMR) spectroscopy (20) to monitor its modification by recombinant ERK2 in vitro (Fig. 1B; fig. S2A). Time-resolved NMR experiments revealed that each phosphorylation proceeded efficiently, but at markedly different rates. Phosphorylation of Thr369 and Ser384, which flank the central Phe–Trp (FW) motif implicated in Mediator interaction (18), occurred faster than modification of Thr364, Thr354 and Ser390, whereas residues Thr418, Ser423 and Thr337 were modified more slowly (Fig. 1C), which we confirmed by immunoblotting (Fig. 1D). 
Cross-references: BMRB:26786
Protein: DP01578 (UniProt P41969)
Region: residues 354	to 390
Annotation: transcription regulator activator activity (Molecular function)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
As expected, alanine substitutions of fast and/or intermediate sites, or of the FW motif, greatly diminished or abolished the ability of Elk-1 to activate TCF-SRF target gene transcription after TPA stimulation (Fig. 3A; fig. S4D). Surprisingly, however, mutation of the slow sites substantially enhanced Elk-1-mediated activation of TCF-SRF target genes (Fig. 3A).
The reconstituted TKO MEFs exhibited enhanced proliferation rates, which correlated with the ability of each mutant to promote transcriptional activation (Fig. 3C).
 Mutagenesis experiments showed that phosphorylation of fast and intermediate sites promoted Mediator interaction and transcriptional activation, whereas modification of slow sites counteracted both functions, thereby limiting Elk-1 output.
Protein: DP01578 (UniProt P41969)
Region: residues 335	to 339
Annotation: transcription regulator inhibitor activity (Molecular function)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
As expected, alanine substitutions of fast and/or intermediate sites, or of the FW motif, greatly diminished or abolished the ability of Elk-1 to activate TCF-SRF target gene transcription after TPA stimulation (Fig. 3A; fig. S4D). Surprisingly, however, mutation of the slow sites substantially enhanced Elk-1-mediated activation of TCF-SRF target genes (Fig. 3A).
The reconstituted TKO MEFs exhibited enhanced proliferation rates, which correlated with the ability of each mutant to promote transcriptional activation (Fig. 3C).
Protein: DP01578 (UniProt P41969)
Region: residues 418	to 423
Annotation: transcription regulator inhibitor activity (Molecular function)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
As expected, alanine substitutions of fast and/or intermediate sites, or of the FW motif, greatly diminished or abolished the ability of Elk-1 to activate TCF-SRF target gene transcription after TPA stimulation (Fig. 3A; fig. S4D). Surprisingly, however, mutation of the slow sites substantially enhanced Elk-1-mediated activation of TCF-SRF target genes (Fig. 3A).
The reconstituted TKO MEFs exhibited enhanced proliferation rates, which correlated with the ability of each mutant to promote transcriptional activation (Fig. 3C).
 Mutagenesis experiments showed that phosphorylation of fast and intermediate sites promoted Mediator interaction and transcriptional activation, whereas modification of slow sites counteracted both functions, thereby limiting Elk-1 output.
Protein: DP01578 (UniProt P41969)
Region: residues 418	to 423
Annotation: negative regulation of protein binding (Biological process)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
We prepared extracts of TKO cells expressing wildtype or mutant Elk-1 proteins and assessed Elk-1 assocation with Mediator by co-immunoprecipitation of the MED23, MED24 and MED16 subunits. Consistent with the transcription experiments, Elk-1–Mediator interaction was induced by TPA stimulation and dependent on the FW motif; it was abolished by alanine substitutions of fast and intermediate sites, and was increased in the slow-site Elk-1 mutant (Fig. 3D).
 Mutagenesis experiments showed that phosphorylation of fast and intermediate sites promoted Mediator interaction and transcriptional activation, whereas modification of slow sites counteracted both functions, thereby limiting Elk-1 output.
Protein: DP01578 (UniProt P41969)
Region: residues 335	to 339
Annotation: negative regulation of protein binding (Biological process)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
We prepared extracts of TKO cells expressing wildtype or mutant Elk-1 proteins and assessed Elk-1 assocation with Mediator by co-immunoprecipitation of the MED23, MED24 and MED16 subunits. Consistent with the transcription experiments, Elk-1–Mediator interaction was induced by TPA stimulation and dependent on the FW motif; it was abolished by alanine substitutions of fast and intermediate sites, and was increased in the slow-site Elk-1 mutant (Fig. 3D).
 Mutagenesis experiments showed that phosphorylation of fast and intermediate sites promoted Mediator interaction and transcriptional activation, whereas modification of slow sites counteracted both functions, thereby limiting Elk-1 output.
Protein: DP01578 (UniProt P41969)
Region: residues 335	to 339
Annotation: positive regulation of protein binding (Biological process)
Evidence: loss-of-function mutant phenotype evidence used in manual assertion
Supporting statements:
We prepared extracts of TKO cells expressing wildtype or mutant Elk-1 proteins and assessed Elk-1 assocation with Mediator by co-immunoprecipitation of the MED23, MED24 and MED16 subunits. Consistent with the transcription experiments, Elk-1–Mediator interaction was induced by TPA stimulation and dependent on the FW motif; it was abolished by alanine substitutions of fast and intermediate sites, and was increased in the slow-site Elk-1 mutant (Fig. 3D).
 Mutagenesis experiments showed that phosphorylation of fast and intermediate sites promoted Mediator interaction and transcriptional activation, whereas modification of slow sites counteracted both functions, thereby limiting Elk-1 output.
Protein: DP01578 (UniProt P41969)
Region: residues 309	to 429
Annotation: mediator complex binding (Molecular function)
Evidence: glutathione S-transferase pull-down assay evidence used in manual assertion
Supporting statements:
We obtained similar results when we used glutathione S-transferase (GST)-Elk-1 TAD proteins to recover Mediator proteins from unstimulated NIH3T3 cell extracts (Fig. 3E). In this assay, ERK2 phosphorylation time-course experiments showed that Mediator recovery by the wildtype Elk-1 TAD was most efficient prior to modifications of the slow sites (fig. S5, A and B). Taken together, these data show that according to the sites involved, ERK2 phosphorylation promotes or inhibits transcriptional activation by Elk-1, which reflects alterations in Elk-1–Mediator interactions.
Protein: DP01579 (UniProt P34233)
Region: residues 420	to 500
Annotation: disorder (Structural state)
Evidence: heteronuclear single quantum coherence spectroscopy evidence used in manual assertion
Supporting statements:
 The HSQC spectra show poor chemical shift dispersions and sharp line widths for both sequences.
Cross-references: BMRB:26719
Protein: DP01579 (UniProt P34233)
Region: residues 424	to 429
Annotation: phosphorylation display site (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The 10-fold phosphorylated version of Ash1 (referred to hereafter as pAsh1) was generated via overnight incubation of Ash1 with Cyclin A/Cdk2 (Figure S3).
Phosphorylation resulted in a downfield shift of 1H resonances and upfield shift of 15N resonances, especially for phosphorylated residues.
Cross-references: BMRB:26720
Protein: DP01579 (UniProt P34233)
Region: residues 420	to 500
Annotation: disorder (Structural state)
Evidence: small-angle X-ray scattering evidence used in manual assertion
Supporting statements:
SAXS data for unphosphorylated Ash1420–500 (referred to hereafter as Ash1) were collected to probe the global conformational preferences of this IDR.
Experimental SAXS data indicates disordered nature of Ash1 and pAsh1
Protein: DP01579 (UniProt P34233)
Region: residues 440	to 445
Annotation: phosphorylation display site (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The 10-fold phosphorylated version of Ash1 (referred to hereafter as pAsh1) was generated via overnight incubation of Ash1 with Cyclin A/Cdk2 (Figure S3).
Phosphorylation resulted in a downfield shift of 1H resonances and upfield shift of 15N resonances, especially for phosphorylated residues.
Cross-references: BMRB:26720
Protein: DP01579 (UniProt P34233)
Region: residues 450	to 455
Annotation: phosphorylation display site (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The 10-fold phosphorylated version of Ash1 (referred to hereafter as pAsh1) was generated via overnight incubation of Ash1 with Cyclin A/Cdk2 (Figure S3).
Phosphorylation resulted in a downfield shift of 1H resonances and upfield shift of 15N resonances, especially for phosphorylated residues.
Cross-references: BMRB:26720
Protein: DP01579 (UniProt P34233)
Region: residues 465	to 469
Annotation: phosphorylation display site (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The 10-fold phosphorylated version of Ash1 (referred to hereafter as pAsh1) was generated via overnight incubation of Ash1 with Cyclin A/Cdk2 (Figure S3).
Phosphorylation resulted in a downfield shift of 1H resonances and upfield shift of 15N resonances, especially for phosphorylated residues.
Cross-references: BMRB:26720
Protein: DP01579 (UniProt P34233)
Region: residues 488	to 492
Annotation: phosphorylation display site (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The 10-fold phosphorylated version of Ash1 (referred to hereafter as pAsh1) was generated via overnight incubation of Ash1 with Cyclin A/Cdk2 (Figure S3).
Phosphorylation resulted in a downfield shift of 1H resonances and upfield shift of 15N resonances, especially for phosphorylated residues.
Cross-references: BMRB:26720
Protein: DP01580 (UniProt P06239)
Region: residues 69	to 86
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion
Supporting statements:
HX MS of unbound Lck SH3 shows that Lck SH3 undergoes local unfolding with a half-life of ;10 sec. This unfolding rate is in stark contrast to that observed for Hck SH3 (;17 min). Regions that undergo local unfolding are shown in red (residues 44–61) and blue (residues 16–33).
Protein: DP01580 (UniProt P06239)
Region: residues 69	to 86
Annotation: order to disorder (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion
Supporting statements:
HX MS of unbound Lck SH3 shows that Lck SH3 undergoes local unfolding with a half-life of ;10 sec. This unfolding rate is in stark contrast to that observed for Hck SH3 (;17 min). Regions that undergo local unfolding are shown in red (residues 44–61) and blue (residues 16–33).
Protein: DP01580 (UniProt P06239)
Region: residues 97	to 114
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion
Supporting statements:
HX MS of unbound Lck SH3 shows that Lck SH3 undergoes local unfolding with a half-life of ;10 sec. This unfolding rate is in stark contrast to that observed for Hck SH3 (;17 min). Regions that undergo local unfolding are shown in red (residues 44–61) and blue (residues 16–33).
Protein: DP01580 (UniProt P06239)
Region: residues 97	to 114
Annotation: order to disorder (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion
Supporting statements:
HX MS of unbound Lck SH3 shows that Lck SH3 undergoes local unfolding with a half-life of ;10 sec. This unfolding rate is in stark contrast to that observed for Hck SH3 (;17 min). Regions that undergo local unfolding are shown in red (residues 44–61) and blue (residues 16–33).
Protein: DP01581 (UniProt Q8NQJ3)
Region: residues 1	to 40
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
NMR experiments revealed that the N-terminal part of the unphosphorylated OdhI protein is fully disordered (Met1-Glu40).
Cross-references: PDB:2KB4
Protein: DP01581 (UniProt Q8NQJ3)
Region: residues 1	to 40
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
pT15 - an important number of intense peaks centered around 8.5 ppm in the 1H dimension of the HSQC recorded on OdhI and attributed to mobile unfolded residues disappeared in the HSQC spectrum recorded on pOdhI. This suggests the structuring of a large part of the N-terminal residues upon phosphorylation. PDB:  2KB3 2KB4
Protein: DP01581 (UniProt Q8NQJ3)
Region: residues 1	to 40
Annotation: phosphorylation display site (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
the phosphorylation results in the folding of 26 amino acids from the N-terminal, but only seven of them, centered on pThr15, are in contact with the FHA core domain according to our NMR data.
Protein: DP01582 (UniProt Q868N5)
Region: residues 358	to 392
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
NMR and circular dichroism (CD) evidence assign different conformational propensities to polyserine peptides from the honeybee and the jewel wasp Nasonia vitripennis; the former is extended and disordered and the latter more compact and helical.
Cross-references: PDB:2LIC
Protein: DP01582 (UniProt Q868N5)
Region: residues 358	to 392
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
The UV spectra of the peptides show considerable differences, suggesting a random coil for AmVg(358–392).
Protein: DP01582 (UniProt Q868N5)
Region: residues 336	to 385
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
AmVg (336–385) retains its random values and lack of NOEs indicative of any fixed structure, a result also supported by the CD spectrum
Protein: DP01582 (UniProt Q868N5)
Region: residues 336	to 385
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
AmVg (336–385) retains its random values and lack of NOEs indicative of any fixed structure, a result also supported by the CD spectrum
Protein: DP01584 (UniProt P19880)
Region: residues 300	to 322
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Upon reduction of the disulphide bonds, Yap1 undergoes a change to an unstructured conformation
Cross-references: PDB:1SSE
Protein: DP01584 (UniProt P19880)
Region: residues 300	to 322
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The active oxidized form, a nuclear export signal (NES) in the carboxy-terminal cysteine-rich domain is masked by disulphide- bond-mediated interactions with a conserved amino-terminal a-helix. Upon reduction of the disulphide bonds, Yap1 undergoes a change to an unstructured conformation
Protein: DP01584 (UniProt P19880)
Region: residues 565	to 650
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
Upon reduction of the disulphide bonds, Yap1 undergoes a change to an unstructured conformation.
Cross-references: PDB:1SSE
Protein: DP01584 (UniProt P19880)
Region: residues 565	to 650
Annotation: disorder to order (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The active oxidized form, a nuclear export signal (NES) in the carboxy-terminal cysteine-rich domain is masked by disulphide- bond-mediated interactions with a conserved amino-terminal a-helix. Upon reduction of the disulphide bonds, Yap1 undergoes a change to an unstructured conformation.