Welcome to Scop3P

Search for the desired protein with Uniprot accession, protein name/keyword, ProteomeXchange ID or PDB id

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

  • Zoom in and zoom out (both with mouse and buttons on the right top corner) to see modificationson the protein
  • Slide the chart to see other modifications (both with mouse and buttons on the right topcorner)
  • Hover on the modification to see more information and position on the structure.
PDB 
 AlphaFold
Phospho-sites

Showing 8 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
25 PhosphoS PRIDE yes
27 PhosphoY UP, PRIDE Combined yes
37 PhosphoT PRIDE yes
45 PhosphoT PRIDE yes
68 PhosphoS PRIDE yes
83 PhosphoY PRIDE
84 PhosphoS PRIDE
122 PhosphoT PRIDE yes

3D structure is not available

Display Settings

Hover over to see the values, zoom (in/out) or drag by using the mouse pointer.

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 10 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
25 22 31 4 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
27 20 31 8 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
27 22 31 6 3
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD000612 22 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 3 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain -
PXD003198 4 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line -
27 22 32 6 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD001565 4 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain
37 33 38 5 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
45 43 55 3 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD000612 2 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
68 66 74 3 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
83 75 95 9 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
84 75 95 10 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
122 108 136 15 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD004452 4 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon

Structures

Showing 5 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
5AOX B X-ray 2.0399999618530273 3 A 0.9658566 25, 27, 37, 68, 83, 84
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
22 22 THR C 0.26 134.41571044921875 12.24182415008545
25 25 SER C 1.0 61.655303955078125 37.382755279541016
27 27 TYR E 0.39 132.55145263671875 38.79461669921875
29 29 THR E 1.0 57.24081039428711 30.53995132446289
37 37 THR C 1.0 123.39433288574219 0.0
68 68 SER E 1.0 30.513748168945312 0.0
83 83 TYR H 1.0 42.0371208190918 41.567386627197266
84 84 SER H 1.0 40.88285827636719 21.439739227294922
4UYK B X-ray 3.2200000286102295 3 A 1.0 25, 27, 37, 68, 83, 84
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
22 22 THR C 0.26 145.74371337890625 14.52541732788086
25 25 SER C 1.0 70.2585220336914 39.178646087646484
27 27 TYR E 0.39 142.76841735839844 54.88313674926758
29 29 THR E 1.0 63.89505386352539 37.091007232666016
37 37 THR C 1.0 124.30498504638672 0.0
68 68 SER E 1.0 4.097668647766113 0.0
83 83 TYR H 1.0 37.05160140991211 36.58319091796875
84 84 SER H 1.0 66.01288604736328 45.703208923339844
4UYJ B X-ray 3.3499999046325684 3 A 1.0 25, 27, 37, 68, 83, 84
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
22 22 THR C 0.26 143.5175018310547 16.950580596923828
25 25 SER C 1.0 69.51756286621094 37.21518325805664
27 27 TYR E 0.39 146.5874786376953 58.15636444091797
29 29 THR E 1.0 61.715911865234375 38.25346755981445
37 37 THR C 1.0 133.4825439453125 0.0
68 68 SER E 1.0 5.835856914520264 0.0
83 83 TYR H 1.0 43.94544219970703 43.94544219970703
84 84 SER H 1.0 61.6186408996582 38.78335189819336
1E8O B X-ray 3.200000047683716 10 A 1.0 25, 27, 68, 83, 84
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
22 22 THR C 0.26 127.47579956054688 8.842691421508789
25 25 SER C 1.0 56.02424621582031 45.888816833496094
27 27 TYR E 0.39 127.086669921875 54.44683837890625
29 29 THR E 1.0 76.90147399902344 47.74983596801758
68 68 SER E 1.0 13.311820983886719 0.0
83 83 TYR H 1.0 43.962501525878906 43.04131317138672
84 84 SER H 1.0 38.55021286010742 25.032625198364258
1RY1 D EM 12.0 Monomer C 0.0 25, 27, 68, 83, 84
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
22 22 THR C 0.26 139.7171173095703 11.44991683959961
25 25 SER C 1.0 67.85450744628906 46.093265533447266
27 27 TYR E 0.39 144.57736206054688 49.68720245361328
29 29 THR E 1.0 67.25053405761719 40.46669387817383
68 68 SER E 1.0 15.31045150756836 0.0
83 83 TYR H 1.0 30.273061752319336 29.1888427734375
84 84 SER H 1.0 39.52044677734375 21.652233123779297

Mutations

Showing 6 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
51 P S Polymorphism
68 S I Polymorphism
124 P A Polymorphism
125 T A Polymorphism
127 A T Polymorphism
130 T A Polymorphism