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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 9 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
292 PhosphoY UP, PRIDE Combined yes
499 PhosphoS UP, PRIDE Combined yes
525 PhosphoS UP Similarity
604 PhosphoY UP Similarity
821 PhosphoS PRIDE yes
827 PhosphoY PRIDE yes
884 PhosphoS UP, PRIDE Combined yes
1054 PhosphoY UP Experimental
1055 PhosphoY PRIDE 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 6 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
292 282 294 11 8
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD001060 3 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell -
PXD000612 5 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD001565 7 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain
PXD003531 4 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD005366 12 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 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
PXD003198 7 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line -
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 -
499 491 501 9 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD006482 1 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney
821 819 829 3 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD006482 1 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney
827 824 829 4 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD000680 1 Stable isotope labeling of phosphoproteins for large-scale phosphorylation rate determination Homo sapiens (Human) COMPLETE 2014-04-15 HeLa cell,HEK-293 cell
884 869 894 16 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD004452 2 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
1055 1047 1056 9 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD000612 3 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
4OLI A X-ray 2.799999952316284 Monomer [2TT]A:1201 0.05320041 604, 821, 827, 1054, 1055
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
604 604 TYR E 0.92 41.92269515991211 0.0
821 821 SER H 0.75 82.41299438476562 0.0
827 827 TYR H 1.0 11.306523323059082 0.0
1054 1054 TYR C 1.0 66.56206512451172 0.0
1055 1055 TYR E 1.0 61.49540328979492 0.0
4WOV A X-ray 1.7999999523162842 2 [SO4]A:903 0.1932013 604, 821, 827
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
604 604 TYR E 0.92 41.39735412597656 0.0
821 821 SER H 0.75 80.32223510742188 0.0
827 827 TYR H 1.0 9.358377456665039 0.0
5C03 A X-ray 1.899999976158142 Monomer [AGS]A:901 0.05358033 604, 821, 827
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
604 604 TYR E 0.92 43.51566696166992 0.0
821 821 SER H 0.75 75.62882232666016 0.0
827 827 TYR H 1.0 8.957417488098145 0.0
5TKD A X-ray 1.9199999570846558 2 [SO4]B:903 0.15650633 604, 821, 827
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
604 604 TYR E 0.92 41.033836364746094 0.0
821 821 SER H 0.75 59.29008102416992 0.0
827 827 TYR H 1.0 4.069413661956787 0.0
4PO6 A X-ray 1.9900000095367432 2 B 0.73643094 292, 499, 525
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
292 292 TYR C 0.76 140.7373504638672 0.0
499 499 SER E 0.26 33.65248489379883 0.0
525 525 SER C 1.0 11.873419761657715 0.0
3ZON A X-ray 2.1500000953674316 Monomer [IK1]A:1871 0.1 604, 821, 827
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
604 604 TYR E 0.92 42.74519348144531 0.0
821 821 SER H 0.75 75.87771606445312 0.0
827 827 TYR H 1.0 10.529536247253418 0.0
5C01 A X-ray 2.1500000953674316 Monomer A 0.0 604, 821, 827
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
604 604 TYR E 0.92 45.32762145996094 0.0
821 821 SER H 0.75 74.1484603881836 0.0
827 827 TYR H 1.0 9.265350341796875 0.0
3NZ0 A X-ray 2.0 Monomer [IZA]A:1 0.1 1054, 1055
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1054 1054 TYR E 1.0 58.74595260620117 0.0
1055 1055 TYR E 1.0 42.542823791503906 0.0
4GIH A X-ray 2.0 Monomer [0X5]A:1201 0.1 1054, 1055
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1054 1054 TYR E 1.0 54.076900482177734 0.0
1055 1055 TYR E 1.0 46.52033615112305 0.0
4GVJ A X-ray 2.0299999713897705 Monomer [ADP]A:1201 0.023046872 1054, 1055
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1054 1054 TYR E 1.0 64.8194808959961 0.0
1055 1055 TYR E 1.0 61.10911560058594 0.0
4GFO A X-ray 2.299999952316284 2 [SO4]A:1202 0.3663715 1054, 1055
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1054 1054 TYR E 1.0 62.937347412109375 0.0
1055 1055 TYR E 1.0 28.412521362304688 0.0
4GII A X-ray 2.309999942779541 Monomer [0X6]A:1201 0.1 1054, 1055
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1054 1054 TYR E 1.0 56.8414192199707 0.0
1055 1055 TYR E 1.0 50.28837203979492 0.0
4GJ2 A X-ray 2.4000000953674316 Monomer [0XH]A:1201 0.1 1054, 1055
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1054 1054 TYR E 1.0 47.097450256347656 0.0
1055 1055 TYR E 1.0 64.61409759521484 0.0
5WAL A X-ray 2.450000047683716 Monomer [9ZS]A:1201 0.1 1054, 1055
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1054 1054 TYR E 1.0 58.17570114135742 0.0
1055 1055 TYR E 1.0 32.497440338134766 0.0
3NYX A X-ray 2.5 Monomer [TZ1]A:1 0.06306857 1054, 1055
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1054 1054 TYR E 1.0 48.034767150878906 0.0
1055 1055 TYR E 1.0 22.955854415893555 0.0
4GJ3 A X-ray 2.5 Monomer [0XP]A:1201 0.1 1054, 1055
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1054 1054 TYR E 1.0 49.77875518798828 0.0
1055 1055 TYR E 1.0 38.23719787597656 0.0
5F1Z A X-ray 2.6500000953674316 Monomer [5U3]A:1200 0.1 1054, 1055
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1054 1054 TYR E 1.0 56.35619354248047 0.0
1055 1055 TYR E 1.0 61.833168029785156 0.0
5F20 A X-ray 2.9100000858306885 Monomer A 0.0 1054, 1055
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1054 1054 TYR C 1.0 85.5615463256836 0.0
1055 1055 TYR C 1.0 69.0101318359375 0.0
3LXP A X-ray 1.649999976158142 Monomer [IZA]A:1183 0.1 1055
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1055 1055 TYR E 1.0 54.56800842285156 0.0
4PY1 A X-ray 2.1600000858306885 Monomer [2YK]A:1201 0.1 1055
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1055 1055 TYR E 1.0 50.454551696777344 0.0
3LXN A X-ray 2.5 Monomer A 0.0 1055
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1055 1055 TYR E 1.0 57.315345764160156 0.0

Mutations

Showing 14 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
4 R H Polymorphism
81 A V Polymorphism
197 R H Polymorphism
362 V F Polymorphism
363 G S Polymorphism
386 V M Polymorphism
442 R Q Polymorphism
684 I S Polymorphism
703 R W Polymorphism
732 H R Unclassified A colorectal adenocarcinoma sample
820 P H Polymorphism
928 A V Polymorphism
1104 P A Polymorphism
1163 E G Polymorphism