Welcome to Scop3P

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

  • 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 6 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
80 TYR PRIDE yes
128 SER PRIDE yes
428 THR PRIDE yes
429 TYR UP, PRIDE Similarity yes
496 TYR UP, PRIDE Combined yes
498 SER 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 7 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
80 77 98 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
128 127 135 2 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD005366 4 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
428 410 436 19 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000680 2 Stable isotope labeling of phosphoproteins for large-scale phosphorylation rate determination Homo sapiens (Human) COMPLETE 2014-04-15 HeLa cell,HEK-293 cell
429 419 436 11 3
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001565 15 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain -
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
PXD003198 6 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line -
496 484 504 13 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD003198 1 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line
496 484 503 13 3
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001060 1 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell -
PXD001565 10 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain
PXD003198 7 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line -
498 484 503 15 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001565 1 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain

Structures

Showing 6 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
2UV3 A X-ray 1.7999999523162842 4 B 0.19602267
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
80 50 TYR E 1.0 34.82289123535156 0.0
92 62 THR E 0.65 24.707162857055664 2.7325546741485596
128 98 SER C 0.62 122.9109878540039 0.0
2JJS A X-ray 1.850000023841858 2 C 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
80 50 TYR E 1.0 22.231271743774414 4.416412830352783
92 62 THR E 0.65 20.697484970092773 0.8624609708786011
128 98 SER C 0.62 123.48050689697266 44.332305908203125
4CMM A X-ray 1.9199999570846558 2 B 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
80 50 TYR E 1.0 28.08507537841797 3.7970664501190186
92 62 THR E 0.65 38.15287399291992 0.0
128 98 SER C 0.62 111.3362045288086 56.17457580566406
6BIT G X-ray 2.190000057220459 4 J 0.012545362
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
80 50 TYR E 1.0 28.639371871948242 3.265331983566284
92 62 THR E 0.65 38.31723403930664 0.0
128 98 SER C 0.62 99.42416381835938 1.102529525756836
2JJT A X-ray 2.299999952316284 4 C 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
80 50 TYR E 1.0 35.67215347290039 4.513315677642822
92 62 THR E 0.65 45.20669937133789 2.6762378215789795
128 98 SER C 0.62 124.75870513916016 44.93632507324219
2WNG A X-ray 2.490000009536743 Monomer A 0.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
80 50 TYR E 1.0 48.29948425292969 0.0
92 62 THR E 0.65 81.74308013916016 0.0
128 98 SER C 0.62 114.68186950683594 0.0

Mutations

Showing 43 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
20 A P Polymorphism
40 D E Polymorphism
44 L S Polymorphism
50 T S Polymorphism
52 T I Polymorphism
54 R H Polymorphism
57 A V Polymorphism
61 I N Polymorphism
68 W R Polymorphism
75 G A Polymorphism
77 E K Polymorphism
81 N H Polymorphism
95 D E Polymorphism
96 L S Polymorphism
100 N E Polymorphism
107 R S Polymorphism
109 G S Polymorphism
125 R Q Polymorphism
132 V T Polymorphism
134 F L Polymorphism
163 Q D Unclassified
181 T S Polymorphism
190 E Q Polymorphism
214 K N Polymorphism
220 E G Polymorphism
222 V I Polymorphism
236 Q R Polymorphism
251 R Q Polymorphism
261 Q L Polymorphism
263 V M Polymorphism
271 V I Polymorphism
276 R T Polymorphism
302 V L Polymorphism
339 P S Polymorphism
353 P L Polymorphism
357 G S Polymorphism
367 S P Polymorphism
370 R Q Polymorphism
389 A E Polymorphism
443 Q R Polymorphism
460 P L Polymorphism
486 A L Unclassified
491 P L Polymorphism