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 5 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
13 PhosphoS UP, PRIDE Combined yes
14 PhosphoY PRIDE yes
18 PhosphoS UP Combined
130 PhosphoS PRIDE yes
138 PhosphoY 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 5 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
13 11 21 3 5
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 -
PXD006482 3 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney -
PXD002286 54 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 - -
PXD005366 1 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 1 Stable isotope labeling of phosphoproteins for large-scale phosphorylation rate determination Homo sapiens (Human) COMPLETE 2014-04-15 HeLa cell,HEK-293 cell -
14 11 21 4 3
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD001060 4 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell -
PXD001565 1 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain -
PXD002286 4 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 -
130 128 139 3 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD000612 8 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD001333 8 Anion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC Homo sapiens (Human) PARTIAL 2015-04-23 HeLa cell
130 130 139 1 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
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
138 130 146 9 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

Structures

Showing 8 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
1N52 B X-ray 2.109999895095825 2 A 0.28860447 13, 14, 18, 130, 138
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
13 13 SER H 1.0 69.75486755371094 11.84106731414795
14 14 TYR H 1.0 132.06350708007812 86.63208770751953
18 18 SER C 1.0 36.969303131103516 0.0
130 130 SER C 1.0 47.675655364990234 0.0
138 138 TYR H 1.0 126.81885528564453 0.0
1H2T Z X-ray 2.1500000953674316 2 C 0.44402376 13, 14, 18, 130, 138
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
13 13 SER H 1.0 68.13314819335938 12.022578239440918
14 14 TYR H 1.0 128.59999084472656 84.9371566772461
18 18 SER C 1.0 35.202667236328125 0.0
130 130 SER C 1.0 80.85369110107422 0.0
138 138 TYR C 1.0 160.70065307617188 0.0
1H2U X X-ray 2.4000000953674316 2 A 0.510721 13, 14, 18, 130, 138
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
13 13 SER H 1.0 69.28146362304688 13.319475173950195
14 14 TYR H 1.0 132.43707275390625 85.84676361083984
18 18 SER C 1.0 35.06173324584961 0.0
130 130 SER C 1.0 41.66644287109375 0.0
138 138 TYR C 1.0 147.39511108398438 0.0
6D0Y A X-ray 2.680000066757202 2 [GTA]A:201 0.1 13, 14, 18, 130, 138
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
13 13 SER C 1.0 69.06695556640625 0.0
14 14 TYR C 1.0 128.444580078125 0.0
18 18 SER C 1.0 35.46992874145508 0.0
130 130 SER C 1.0 40.84268569946289 0.0
138 138 TYR C 1.0 153.53233337402344 54.323699951171875
5OOB B X-ray 2.7899999618530273 3 A 0.6411071 13, 14, 18, 130, 138
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
13 13 SER H 1.0 69.45519256591797 14.210354804992676
14 14 TYR H 1.0 132.38011169433594 87.4603271484375
18 18 SER C 1.0 35.888179779052734 0.0
130 130 SER C 1.0 44.29160690307617 0.0
138 138 TYR H 1.0 177.39649963378906 0.0
5OO6 B X-ray 2.799999952316284 3 A 0.67078364 13, 14, 18, 130, 138
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
13 13 SER C 1.0 72.5197525024414 14.602027893066406
14 14 TYR C 1.0 132.080810546875 83.04474639892578
18 18 SER C 1.0 37.60344696044922 0.0
130 130 SER C 1.0 35.34769821166992 0.0
138 138 TYR H 1.0 190.63087463378906 0.0
1N54 B X-ray 2.7200000286102295 2 A 0.69058037 13, 14, 18
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
13 13 SER C 1.0 90.87342834472656 16.01417350769043
14 14 TYR C 1.0 139.02047729492188 85.20928192138672
18 18 SER C 1.0 74.95378875732422 0.0
3FEY B X-ray 2.200000047683716 2 A 0.1 13, 14
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
13 13 SER C 1.0 106.59874725341797 23.42974281311035
14 14 TYR C 1.0 133.3702392578125 84.55120086669922

Mutations

Showing 0 results

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