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Ex.: O00571, ddx3x (keyword), ATP-dependent RNA helicase DDX3X, PXD000680 or 3JRV

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PDB 
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Phospho-sites

Showing 2 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
109 PhosphoY PRIDE yes
131 PhosphoT UP, PRIDE Combined yes

3D structure is not available

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Phosphorylated amino acids are colored red on the inner ring.

The first amino acid of the protein sequence is colored darker on each ring.

Phospho peptides

Showing 4 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
109 95 113 15 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD000612 1 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
131 129 136 3 9
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD004252 6 Modulating the selectivity of affinity absorbents to multi-phosphopeptides by a novel competitive substitution strategy Homo sapiens (Human) PARTIAL 2016-08-03 cell culture -
PXD001060 11 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell -
PXD000836 5 HOPE-fixation of lung tissue allows retrospective proteome and phosphoproteome studies Homo sapiens (Human) PARTIAL 2014-05-22 lung -
PXD000612 1 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD003531 1 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
PXD001333 1 Anion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC Homo sapiens (Human) PARTIAL 2015-04-23 HeLa cell -
PXD006482 1 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney -
PXD005366 46 Robust, sensitive and automated phosphopeptide enrichment optimized for low sample amounts applied to primary hippocampal neurons Homo sapiens (Human),Rattus norvegicus (Rat) PARTIAL 2016-12-14 cell culture -
PXD000680 3 Stable isotope labeling of phosphoproteins for large-scale phosphorylation rate determination Homo sapiens (Human) COMPLETE 2014-04-15 HeLa cell,HEK-293 cell -
131 129 137 3 13
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD001060 100 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell -
PXD004252 16 Modulating the selectivity of affinity absorbents to multi-phosphopeptides by a novel competitive substitution strategy Homo sapiens (Human) PARTIAL 2016-08-03 cell culture -
PXD000474 3 Simulated phosphopeptide spectral library for confident site localization Homo sapiens (Human) PARTIAL 2015-03-17 HeLa cell -
PXD003531 46 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD004940 7 Performance of the Orbitrap Fusion Lumos Tribrid in single-shot analyses of human samples Homo sapiens (Human) PARTIAL 2017-03-09 HeLa cell -
PXD001333 6 Anion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC Homo sapiens (Human) PARTIAL 2015-04-23 HeLa cell -
PXD005366 63 Robust, sensitive and automated phosphopeptide enrichment optimized for low sample amounts applied to primary hippocampal neurons Homo sapiens (Human),Rattus norvegicus (Rat) PARTIAL 2016-12-14 cell culture -
PXD004452 11 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
PXD002394 26 Proteomic and phosphoproteomic analysis of cisplatin resistance in patient derived serous ovarian cancer Homo sapiens (Human) PARTIAL 2017-05-02 cell suspension culture -
PXD000680 27 Stable isotope labeling of phosphoproteins for large-scale phosphorylation rate determination Homo sapiens (Human) COMPLETE 2014-04-15 HeLa cell,HEK-293 cell -
PXD000836 9 HOPE-fixation of lung tissue allows retrospective proteome and phosphoproteome studies Homo sapiens (Human) PARTIAL 2014-05-22 lung -
PXD000612 71 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD001546 6 Reproducibility of label-free single-shot phosphoproteomics applied to CRC cell lines Homo sapiens (Human) PARTIAL 2015-04-15 cell culture
131 131 137 1 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD000836 1 HOPE-fixation of lung tissue allows retrospective proteome and phosphoproteome studies Homo sapiens (Human) PARTIAL 2014-05-22 lung
PXD000612 11 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -

Structures

Showing 21 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
1FS1 B X-ray 1.7999999523162842 2 A 1.0 109, 131
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
109 109 TYR H 1.0 49.902462005615234 0.0
131 131 THR C 1.0 68.75663757324219 4.0239129066467285
2E31 B X-ray 2.4000000953674316 2 A 1.0 109, 131
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
109 109 TYR H 1.0 61.185035705566406 0.0
131 131 THR C 1.0 67.48564147949219 0.0
5IBK A X-ray 2.5 3 B 1.0 109, 131
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
109 109 TYR H 1.0 85.54707336425781 0.0
131 131 THR C 1.0 74.55730438232422 7.514291763305664
5JH5 B X-ray 2.549999952316284 2 A 1.0 109, 131
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
109 109 TYR H 1.0 50.98560333251953 0.0
131 131 THR C 1.0 64.52420806884766 1.1713886260986328
3WSO B X-ray 2.5999999046325684 2 A 1.0 109, 131
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
109 109 TYR H 1.0 68.42545318603516 0.0
131 131 THR C 1.0 73.49897766113281 4.181310176849365
4I6J C X-ray 2.700000047683716 3 B 1.0 109, 131
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
109 109 TYR H 1.0 107.2928695678711 0.0
131 131 THR C 1.0 60.118431091308594 1.675497055053711
1FQV B X-ray 2.799999952316284 2 A 1.0 109, 131
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
109 109 TYR H 1.0 51.6210823059082 0.0
131 131 THR C 1.0 66.62252044677734 1.1720390319824219
5K35 B X-ray 2.8499999046325684 2 A 1.0 109, 131
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
109 109 TYR H 1.0 55.304325103759766 0.0
131 131 THR C 1.0 49.50154113769531 7.045603275299072
1FS2 B X-ray 2.9000000953674316 4 A 1.0 109, 131
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
109 109 TYR H 1.0 62.880496978759766 0.0
131 131 THR C 1.0 63.84138488769531 0.6592808961868286
2E32 B X-ray 3.5199999809265137 2 A 1.0 109, 131
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
109 109 TYR H 1.0 118.88421630859375 0.0
131 131 THR C 1.0 63.24467468261719 0.1566149741411209
2AST A X-ray 2.299999952316284 8 B 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
109 1109 TYR H 1.0 53.205326080322266 0.0
131 1131 THR C 1.0 62.771297454833984 1.8402884006500244
2OVR A X-ray 2.5 3 B 0.18112047
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
109 1109 TYR H 1.0 60.99923324584961 0.0
131 1131 THR C 1.0 27.700878143310547 1.965072512626648
2OVQ A X-ray 2.5999999046325684 12 B 0.30099675
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
109 1109 TYR H 1.0 62.09697341918945 0.0
131 1131 THR C 1.0 34.298831939697266 4.32564115524292
5V4B A X-ray 2.5999999046325684 12 B 0.26051405
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
109 1109 TYR H 1.0 57.27452087402344 0.0
131 1131 THR C 1.0 62.30768585205078 10.55254077911377
5VZU A X-ray 2.700000047683716 6 B 0.47738495
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
109 1109 TYR H 1.0 64.72846221923828 0.0
131 1131 THR C 1.0 59.62839126586914 0.5011969804763794
5VZT A X-ray 2.700000047683716 4 B 0.51097757
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
109 1109 TYR H 1.0 60.737388610839844 0.0
131 1131 THR C 1.0 65.679443359375 1.169030785560608
3L2O A X-ray 2.799999952316284 4 B 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
109 1109 TYR H 1.0 59.9923095703125 0.0
131 1131 THR C 1.0 79.7709732055664 12.54491138458252
2OVP A X-ray 2.9000000953674316 8 B 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
109 1109 TYR H 1.0 49.78413772583008 0.0
131 1131 THR C 1.0 37.62154769897461 2.3966314792633057
1P22 B X-ray 2.950000047683716 3 A 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
109 88 TYR C 1.0 70.1573715209961 0.0
131 110 THR C 1.0 42.42246627807617 4.943868160247803
2ASS A X-ray 3.0 6 B 0.9474077
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
109 1109 TYR H 1.0 56.58957290649414 0.0
131 1131 THR C 1.0 66.02790069580078 1.8428233861923218
1LDK D X-ray 3.0999999046325684 10 E 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
109 2109 TYR H 1.0 68.98542022705078 0.0
131 2131 THR C 1.0 83.24308013916016 6.794768333435059

Mutations

Showing 0 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease