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

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PDB 
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Phospho-sites

Showing 15 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
31 SER PRIDE
35 SER PRIDE
86 TYR UP Experimental
361 THR PRIDE
363 SER PRIDE yes
367 THR PRIDE
386 THR PRIDE yes
409 TYR UP Experimental
465 TYR UP Experimental
562 SER PRIDE yes
598 THR PRIDE yes
603 TYR UP Experimental
636 SER PRIDE yes
651 TYR UP Experimental
742 THR UP, PRIDE Combined yes

3D structure is not available

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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
31 27 43 5 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
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
35 27 43 9 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
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
361 356 368 6 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
363 361 368 3 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD002286 1 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 -
367 356 368 12 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
386 374 390 13 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD002286 1 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 -
PXD004452 2 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
562 554 564 9 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD002286 3 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 -
598 598 615 1 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD002286 1 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 -
636 627 648 10 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD002286 2 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 -
742 742 748 1 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD002286 1 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 -

Structures

Showing 44 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
4PKG G X-ray 1.7999999523162842 2 A 0.44287494 86
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
86 86 TYR C 1.0 60.57491683959961 0.0
4PKH B X-ray 2.1500000953674316 2 A 0.3834467 86
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
86 86 TYR C 1.0 63.290897369384766 0.0
4PKI G X-ray 2.299999952316284 2 A 0.41546866 86
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
86 86 TYR C 1.0 55.623844146728516 0.0
5FAF A X-ray 1.0499999523162842 2 [CA]A:301 0.32297242
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
265 238 THR C 0.51 81.50566864013672 0.0
287 260 THR C 0.9 139.89108276367188 0.0
2FH1 A X-ray 1.5499999523162842 Monomer [CA]A:2002 0.034528065
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
465 438 TYR C 0.94 49.26275634765625 0.0
562 535 SER C 0.79 81.28681182861328 0.0
598 571 THR C 0.94 9.647587776184082 0.0
603 576 TYR E 0.97 19.72159194946289 0.0
636 609 SER C 0.78 80.99322509765625 0.0
651 624 TYR C 1.0 39.48899841308594 0.0
742 715 THR C 1.0 91.62538146972656 0.0
3CIP G X-ray 1.600000023841858 4 A 0.14015865
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
86 35 TYR C 1.0 61.76893997192383 0.0
1KCQ A X-ray 1.649999976158142 2 [CD]A:262 0.35800922
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
265 238 THR C 0.51 81.73179626464844 0.0
287 260 THR C 0.9 113.18804931640625 0.0
5O2Z A X-ray 1.7000000476837158 4 B 0.39349076
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
265 238 THR C 0.51 85.2421646118164 0.0
5FAE A X-ray 1.7000000476837158 2 [SO4]A:302 0.18462925
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
265 238 THR C 0.51 83.49040222167969 0.0
3CI5 G X-ray 1.7000000476837158 4 A 0.12675796
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
86 35 TYR C 1.0 64.33523559570312 0.0
1D4X G X-ray 1.75 4 A 0.2496101
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
86 35 TYR C 1.0 61.178001403808594 0.0
1NM1 G X-ray 1.7999999523162842 4 A 0.22663137
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
86 35 TYR C 1.0 63.5818977355957 0.0
1NLV G X-ray 1.7999999523162842 4 A 0.18646352
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
86 35 TYR C 1.0 64.01103973388672 0.0
1NMD G X-ray 1.899999976158142 4 A 0.2990235
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
86 35 TYR C 1.0 62.88408279418945 0.0
1YAG G X-ray 1.899999976158142 4 A 0.3558122
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
86 35 TYR C 1.0 61.171226501464844 0.0
1T44 G X-ray 2.0 2 A 0.35687873
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
86 59 TYR C 1.0 64.50969696044922 0.0
1P8X A X-ray 2.0 Monomer [CA]A:1002 0.035485495
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
465 438 TYR C 0.94 50.032386779785156 0.0
562 535 SER C 0.79 82.81610870361328 0.0
598 571 THR C 0.94 11.457763671875 0.0
603 576 TYR E 0.97 19.701459884643555 0.0
636 609 SER C 0.78 83.2628402709961 0.0
651 624 TYR C 1.0 38.6772575378418 0.0
742 715 THR C 1.0 15.79394817352295 0.0
2FF3 A X-ray 2.0 2 B 0.2572267
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
86 59 TYR C 1.0 60.163448333740234 0.0
1ESV S X-ray 2.0 2 A 0.24659538
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
86 35 TYR C 1.0 61.912864685058594 0.0
1C0G S X-ray 2.0 2 A 0.28475496
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
86 37 TYR C 1.0 64.44125366210938 0.0
2FF6 G X-ray 2.049999952316284 2 A 0.24897124
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
86 59 TYR C 1.0 61.65168762207031 0.0
1YVN G X-ray 2.0999999046325684 4 A 0.27349237
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
86 35 TYR C 1.0 61.32902908325195 0.0
1MDU A X-ray 2.200000047683716 2 B 0.26462212
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
86 35 TYR C 1.0 60.00617218017578 0.0
1EQY S X-ray 2.299999952316284 2 A 0.2730857
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
86 35 TYR C 1.0 63.166412353515625 0.0
3A5N S X-ray 2.359999895095825 2 C 0.24574773
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
86 37 TYR C 1.0 60.20778274536133 0.0
5UBO S X-ray 2.390000104904175 2 A 0.20017472
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
86 35 TYR C 1.0 60.58367919921875 0.0
4Z94 G X-ray 2.4000000953674316 2 A 0.37353638
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
86 35 TYR C 1.0 61.74803924560547 0.0
3A5L S X-ray 2.4000000953674316 2 C 0.25636515
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
86 37 TYR C 1.0 61.05384063720703 0.0
1C0F S X-ray 2.4000000953674316 2 A 0.28081208
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
86 37 TYR C 1.0 62.42273712158203 0.0
1DEJ S X-ray 2.4000000953674316 2 A 0.2766129
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
86 37 TYR C 1.0 63.955318450927734 0.0
3A5M S X-ray 2.4000000953674316 2 C 0.2705956
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
86 37 TYR C 1.0 61.82936477661133 0.0
3A5O S X-ray 2.4000000953674316 2 C 0.23688021
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
86 37 TYR C 1.0 60.46267318725586 0.0
2FH2 A X-ray 2.5 Monomer [CA]A:1002 0.050125875
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
465 438 TYR C 0.94 48.64914321899414 0.0
562 535 SER C 0.79 80.71222686767578 0.0
598 571 THR C 0.94 9.088103294372559 0.0
603 576 TYR E 0.97 20.88939094543457 0.0
636 609 SER C 0.78 81.6276626586914 0.0
651 624 TYR C 1.0 41.076725006103516 0.0
742 715 THR C 1.0 92.51903533935547 0.0
5DD2 A X-ray 2.5999999046325684 Monomer [CA]A:202 0.059034847
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
86 59 TYR C 1.0 62.280826568603516 0.0
1P8Z G X-ray 2.5999999046325684 4 A 0.2938502
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
86 59 TYR C 1.0 65.2469253540039 0.0
4S10 C X-ray 2.609999895095825 2 [CA]C:301 0.1
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
265 238 THR C 0.51 94.45050811767578 0.0
2FH3 A X-ray 2.869999885559082 Monomer [CA]A:1002 0.034592323
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
465 438 TYR C 0.94 49.07538604736328 0.0
562 535 SER C 0.79 79.18987274169922 0.0
598 571 THR C 0.94 10.820773124694824 0.0
603 576 TYR E 0.97 21.893062591552734 0.0
636 609 SER C 0.78 83.79560089111328 0.0
651 624 TYR C 1.0 35.975563049316406 0.0
742 715 THR C 1.0 93.4030532836914 0.0
1H1V G X-ray 3.0 2 A 0.17606962
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
465 438 TYR C 0.94 27.962430953979492 0.0
562 535 SER C 0.79 89.42847442626953 0.0
598 571 THR E 0.94 12.263997077941895 0.0
603 576 TYR E 0.97 20.385944366455078 0.0
636 609 SER C 0.78 81.42512512207031 0.0
651 624 TYR C 1.0 37.90537643432617 0.0
742 715 THR C 1.0 10.743402481079102 0.0
3FFN A X-ray 3.0 8 A 0.50306964
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
86 59 TYR C 1.0 51.5287971496582 0.0
265 238 THR C 0.51 87.46473693847656 0.0
361 334 THR H 0.96 4.8126325607299805 0.0
363 336 SER H 0.84 49.56355667114258 0.0
367 340 THR H 0.69 106.93497467041016 0.0
386 359 THR C 0.95 7.816911697387695 0.0
409 382 TYR C 0.95 12.846521377563477 0.0
465 438 TYR C 0.94 61.07842254638672 0.0
562 535 SER C 0.79 89.17990112304688 0.0
598 571 THR C 0.94 14.047745704650879 0.0
603 576 TYR E 0.97 25.503232955932617 0.0
636 609 SER C 0.78 87.3936538696289 0.0
651 624 TYR C 1.0 53.24997329711914 0.0
742 715 THR C 1.0 3.3625786304473877 0.0
3FFK A X-ray 3.0 2 B 0.28067747
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
86 59 TYR C 1.0 64.42909240722656 0.0
265 238 THR C 0.51 85.49754333496094 0.0
287 260 THR C 0.9 65.13937377929688 0.0
361 334 THR H 0.96 22.121463775634766 0.0
363 336 SER H 0.84 49.930580139160156 0.0
367 340 THR H 0.69 115.96989440917969 0.0
386 359 THR C 0.95 32.65099334716797 16.720352172851562
2FH4 A X-ray 3.0 Monomer B 0.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
465 438 TYR C 0.94 49.03118133544922 0.0
562 535 SER C 0.79 42.727691650390625 0.0
598 571 THR C 0.94 19.733732223510742 0.0
603 576 TYR C 0.97 14.853095054626465 0.0
636 609 SER C 0.78 75.84645080566406 0.0
651 624 TYR C 1.0 20.415372848510742 0.0
742 715 THR C 1.0 96.73258972167969 0.0
3TU5 B X-ray 3.0 4 A 0.20454438
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
86 35 TYR C 1.0 61.393592834472656 0.0
3CJB G X-ray 3.2100000381469727 2 A 0.33753878
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
86 35 TYR C 1.0 63.883697509765625 0.0
3CJC G X-ray 3.9000000953674316 3 A 0.19351763
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
86 35 TYR C 1.0 51.83812713623047 0.0

Mutations

Showing 7 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
22 S L Unclassified A breast cancer sample
129 A T Polymorphism
201 T I Unclassified A breast cancer sample
214 D N Disease Amyloidosis 5 (AMYL5) [MIM:105120]
231 N D Polymorphism
611 S N Unclassified A breast cancer sample
668 R L Polymorphism