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 3 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
168 PhosphoY UP Combined
221 PhosphoY PRIDE yes
351 PhosphoS UP, PRIDE Combined 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 3 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
221 211 227 11 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
351 348 365 4 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD003531 1 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
351 348 366 4 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

Structures

Showing 5 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
6ALJ A X-ray 1.8899999856948853 4 [CW2]A:602 0.6003359 168, 221, 351
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
92 92 SER C 1.0 21.84599494934082 0.0
168 168 TYR E 0.91 86.02506256103516 0.0
218 218 SER H 0.8 1.324059009552002 0.0
221 221 TYR H 0.86 34.62028503417969 0.0
351 351 SER C 0.88 60.25569534301758 0.0
6B5G A X-ray 2.200000047683716 4 C 0.43747917 168, 221, 351
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
92 92 SER C 1.0 23.000768661499023 0.0
168 168 TYR E 0.91 89.92655181884766 32.26365661621094
218 218 SER H 0.8 1.2542206048965454 0.0
221 221 TYR H 0.86 35.98286056518555 0.0
351 351 SER C 0.88 60.23785400390625 0.0
6B5H A X-ray 2.299999952316284 4 B 0.53735936 168, 221, 351
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
92 92 SER C 1.0 23.203773498535156 0.0
168 168 TYR E 0.91 92.03743743896484 40.411842346191406
218 218 SER H 0.8 0.7373219132423401 0.0
221 221 TYR H 0.86 33.80481719970703 0.0
351 351 SER C 0.88 61.4164924621582 0.0
6B5I A X-ray 2.5999999046325684 4 C 0.75181013 168, 221, 351
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
92 92 SER C 1.0 21.240541458129883 0.0
168 168 TYR E 0.91 88.50487518310547 39.44121170043945
218 218 SER H 0.8 1.2610657215118408 0.0
221 221 TYR H 0.86 31.10103988647461 0.0
351 351 SER C 0.88 62.107398986816406 0.0
4X2Q A X-ray 2.940000057220459 4 B 0.7384571
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
92 74 SER C 1.0 16.916818618774414 0.0
168 150 TYR E 0.91 98.17657470703125 25.689496994018555
218 200 SER H 0.8 0.9927439093589783 0.0
221 203 TYR H 0.86 28.618410110473633 0.0
351 333 SER C 0.88 53.912906646728516 0.0

Mutations

Showing 4 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
50 E G Polymorphism
110 A V Polymorphism
348 V I Polymorphism
436 E K Polymorphism