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
40 TYR PRIDE yes
414 SER PRIDE yes
512 TYR UP Combined
559 TYR PRIDE yes
565 SER 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 4 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
40 36 47 5 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
414 395 417 20 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD002436 1 Monitoring cellular phosphorylation signaling pathways into chromatin and down to the gene level Homo sapiens (Human) COMPLETE 2015-11-09 HeLa cell
559 557 576 3 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004415 1 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte
565 563 576 3 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004415 9 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte

Structures

Showing 33 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
4HCU A X-ray 1.4299999475479126 Monomer [13L]A:701 0.0 414, 512, 559, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
414 414 SER C 1.0 71.59712982177734 0.0
512 512 TYR H 1.0 38.07006072998047 0.0
559 559 TYR C 0.87 14.638628005981445 0.0
565 565 SER H 0.57 75.60675048828125 0.0
4HCT A X-ray 1.4800000190734863 Monomer [18R]A:701 0.1 414, 512, 559, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
414 414 SER C 1.0 73.6352310180664 0.0
512 512 TYR H 1.0 54.53826141357422 0.0
559 559 TYR C 0.87 14.981284141540527 0.0
565 565 SER H 0.57 73.5763168334961 0.0
4HCV A X-ray 1.4800000190734863 Monomer A 0.0 414, 512, 559, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
414 414 SER C 1.0 73.54132080078125 0.0
512 512 TYR H 1.0 40.74354934692383 0.0
559 559 TYR C 0.87 13.766352653503418 0.0
565 565 SER H 0.57 75.14879608154297 0.0
4M15 A X-ray 1.5199999809265137 Monomer [ADP]A:702 0.050597493 414, 512, 559, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
414 414 SER C 1.0 76.37960052490234 0.0
512 512 TYR H 1.0 28.633272171020508 0.0
559 559 TYR C 0.87 23.683971405029297 0.0
565 565 SER H 0.57 72.97813415527344 0.0
4M14 A X-ray 1.5499999523162842 Monomer [QWS]A:702 0.06896292 414, 512, 559, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
414 414 SER C 1.0 72.38946533203125 0.0
512 512 TYR H 1.0 39.449440002441406 0.0
559 559 TYR C 0.87 23.056781768798828 0.0
565 565 SER H 0.57 71.70875549316406 0.0
3T9T A X-ray 1.649999976158142 Monomer A 0.0 414, 512, 559, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
414 414 SER C 1.0 66.73716735839844 0.0
512 512 TYR H 1.0 50.97756576538086 0.0
559 559 TYR C 0.87 14.205300331115723 0.0
565 565 SER H 0.57 67.8363037109375 0.0
4M0Y A X-ray 1.7000000476837158 Monomer A 0.0 414, 512, 559, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
414 414 SER C 1.0 68.14788055419922 0.0
512 512 TYR H 1.0 39.684505462646484 0.0
559 559 TYR C 0.87 25.919471740722656 0.0
565 565 SER H 0.57 74.3725814819336 0.0
4M13 A X-ray 1.850000023841858 Monomer [1E0]A:701 0.1 414, 512, 559, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
414 414 SER C 1.0 62.94858932495117 0.0
512 512 TYR H 1.0 32.671966552734375 0.0
559 559 TYR C 0.87 6.021281719207764 0.0
565 565 SER H 0.57 71.8919448852539 0.0
3MJ2 A X-ray 1.899999976158142 Monomer [MJG]A:1 0.1 414, 512, 559, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
414 414 SER C 1.0 69.34650421142578 0.0
512 512 TYR H 1.0 73.81888580322266 0.0
559 559 TYR H 0.87 4.599777698516846 0.0
565 565 SER H 0.57 80.57402801513672 0.0
4M0Z A X-ray 2.0 Monomer A 0.0 414, 512, 559, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
414 414 SER C 1.0 65.32806396484375 0.0
512 512 TYR H 1.0 35.345481872558594 0.0
559 559 TYR C 0.87 10.601164817810059 0.0
565 565 SER H 0.57 72.41744995117188 0.0
4M12 A X-ray 2.1500000953674316 Monomer A 0.0 414, 512, 559, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
414 414 SER C 1.0 64.37061309814453 0.0
512 512 TYR H 1.0 35.775569915771484 0.0
559 559 TYR C 0.87 20.195247650146484 0.0
565 565 SER H 0.57 73.11959075927734 0.0
3MIY A X-ray 1.6699999570846558 2 B 0.99736834 414, 559, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
414 414 SER C 1.0 86.26449584960938 85.04478454589844
559 559 TYR C 0.87 6.388416767120361 0.0
565 565 SER H 0.57 75.1388168334961 0.0
4PQN A X-ray 1.7100000381469727 Monomer A 0.0 414, 559, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
414 414 SER C 1.0 75.29146575927734 38.793392181396484
559 559 TYR H 0.87 5.8306097984313965 0.0
565 565 SER H 0.57 86.44574737548828 0.0
3MJ1 A X-ray 1.7200000286102295 Monomer [614]A:1 0.1 414, 559, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
414 414 SER C 1.0 72.91816711425781 0.0
559 559 TYR C 0.87 16.252119064331055 0.0
565 565 SER H 0.57 79.2168960571289 0.0
3V5L A X-ray 1.8600000143051147 2 [0G1]A:701 0.57621884 414, 559, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
414 414 SER C 1.0 86.91128540039062 0.0
559 559 TYR C 0.87 16.875751495361328 0.0
565 565 SER H 0.57 82.42032623291016 0.0
4L7S A X-ray 2.0299999713897705 2 B 0.3120548 414, 559, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
414 414 SER C 1.0 84.41725158691406 83.02127838134766
559 559 TYR C 0.87 8.151666641235352 0.0
565 565 SER H 0.57 82.95027923583984 0.0
3QGW A X-ray 2.0999999046325684 Monomer [PQC]A:1 0.1 414, 559, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
414 414 SER C 1.0 85.82906341552734 0.0
559 559 TYR C 0.87 12.640352249145508 0.0
565 565 SER H 0.57 82.81757354736328 0.0
3QGY A X-ray 2.0999999046325684 2 [PQC]A:1 0.1 414, 559, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
414 414 SER C 1.0 74.92070007324219 0.0
559 559 TYR C 0.87 11.340505599975586 0.0
565 565 SER H 0.57 83.38717651367188 0.0
4RFM A X-ray 2.0999999046325684 Monomer [3P6]A:701 0.1 414, 559, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
414 414 SER C 1.0 68.85798645019531 0.0
559 559 TYR C 0.87 13.775164604187012 0.0
565 565 SER H 0.57 80.23514556884766 0.0
4MF1 A X-ray 2.109999895095825 2 B 0.69498354 414, 559, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
414 414 SER C 1.0 87.31952667236328 85.6834716796875
559 559 TYR C 0.87 5.344930648803711 0.0
565 565 SER H 0.57 74.77346801757812 0.0
4KIO A X-ray 2.180000066757202 4 C 0.35483348 414, 559, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
414 414 SER C 1.0 83.29698181152344 82.31634521484375
559 559 TYR C 0.87 15.000823020935059 0.0
565 565 SER H 0.57 85.36599731445312 0.0
3V8W A X-ray 2.2699999809265137 2 [0G2]A:701 0.3982969 414, 559, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
414 414 SER C 1.0 88.92040252685547 0.0
559 559 TYR C 0.87 57.350189208984375 0.0
565 565 SER H 0.57 81.60163879394531 0.0
1SM2 A X-ray 2.299999952316284 Monomer [STU]A:301 0.1 414, 559, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
414 414 SER C 1.0 79.809814453125 0.0
559 559 TYR C 0.87 10.265864372253418 0.0
565 565 SER H 0.57 103.02254486083984 0.0
4QD6 A X-ray 2.450000047683716 2 B 0.8172719 414, 559, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
414 414 SER C 1.0 67.71810913085938 0.0
559 559 TYR C 0.87 13.557580947875977 0.0
565 565 SER H 0.57 83.11162567138672 0.0
1SNU A X-ray 2.5 2 B 0.7716271 414, 559, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
414 414 SER C 1.0 81.84233093261719 56.52401351928711
559 559 TYR C 0.87 10.871918678283691 0.0
565 565 SER H 0.57 101.26734161376953 0.0
4PP9 A X-ray 2.5799999237060547 2 [SO4]A:701 0.35738456 414, 559, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
414 414 SER C 1.0 89.66254425048828 0.0
559 559 TYR C 0.87 29.373804092407227 0.0
565 565 SER H 0.57 86.63964080810547 0.0
3V5J A X-ray 2.5899999141693115 4 [0F2]A:701 0.35570505 414, 559, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
414 414 SER C 1.0 86.1629638671875 0.0
559 559 TYR C 0.87 16.95958709716797 0.0
565 565 SER H 0.57 85.28907775878906 0.0
4MF0 A X-ray 2.6700000762939453 2 B 1.0 414, 559, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
414 414 SER C 1.0 60.062618255615234 0.0
559 559 TYR C 0.87 14.524120330810547 0.0
565 565 SER H 0.57 87.38897705078125 0.0
4PPA A X-ray 2.6700000762939453 2 B 0.8870148 414, 559, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
414 414 SER C 1.0 66.07367706298828 0.0
559 559 TYR C 0.87 30.761871337890625 0.0
565 565 SER H 0.57 82.8243179321289 0.0
4PPB A X-ray 2.819999933242798 2 B 0.8220793 414, 559, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
414 414 SER C 1.0 69.06098175048828 0.0
559 559 TYR C 0.87 15.358593940734863 0.0
565 565 SER H 0.57 69.24341583251953 0.0
4PPC A X-ray 2.950000047683716 2 B 0.81742877 414, 559, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
414 414 SER C 1.0 65.44805908203125 17.048227310180664
559 559 TYR C 0.87 11.587247848510742 0.0
565 565 SER H 0.57 75.2967300415039 0.0
1SNX A X-ray 3.200000047683716 2 B 0.1 414, 559, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
414 414 SER C 1.0 78.97743225097656 59.547386169433594
559 559 TYR C 0.87 5.193731307983398 0.0
565 565 SER H 0.57 107.90185546875 0.0
3V8T A X-ray 2.0 2 B 0.36802 414, 559
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
414 414 SER C 1.0 87.43110656738281 86.4813232421875
559 559 TYR C 0.87 117.84215545654297 0.0

Mutations

Showing 7 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
19 R K Unclassified A metastatic melanoma sample
23 P L Unclassified A metastatic melanoma sample
193 R Q Polymorphism
335 R W Disease Lymphoproliferative syndrome 1 (LPFS1) [MIM:613011]
451 R Q Unclassified A gastric adenocarcinoma sample
581 R W Polymorphism
587 V I Polymorphism