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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 3 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
173 PhosphoT PRIDE yes
177 PhosphoS PRIDE yes
450 PhosphoS PRIDE 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 3 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
173 147 181 27 3
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD001060 3 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell -
PXD000612 7 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
177 147 181 31 4
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD000612 54 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD003531 15 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD004452 4 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
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
450 447 452 4 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD004452 4 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon

Structures

Showing 55 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
2BCQ A X-ray 1.649999976158142 4 T 0.29484177 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 40.75673294067383 0.0
5IIJ A X-ray 1.7200000286102295 4 D 0.31242937 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 39.2585334777832 0.0
2BCR A X-ray 1.75 4 T 0.29244134 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 40.78788757324219 0.0
5III A X-ray 1.7999999523162842 4 D 0.32946926 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 42.13046646118164 0.0
4XA5 A X-ray 1.899999976158142 4 D 0.33917978 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 29.10720443725586 0.0
2PFN A X-ray 1.899999976158142 4 D 0.2058666 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 39.428123474121094 0.0
5IIM A X-ray 1.940000057220459 4 T 0.3470663 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 40.64561080932617 0.0
3UPQ A X-ray 1.9500000476837158 4 [SO4]A:5 0.17717353 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 26.469886779785156 0.0
1XSN A X-ray 1.9500000476837158 4 T 0.3035882 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 34.966827392578125 0.0
3HWT A X-ray 1.9500000476837158 4 T 0.37017146 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 41.0770378112793 0.0
3HW8 A X-ray 1.9500000476837158 4 D 0.20380968 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 40.786685943603516 0.0
5IIL A X-ray 1.9600000381469727 4 T 0.39824674 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 36.983116149902344 0.0
5IIK A X-ray 1.9800000190734863 4 T 0.3662896 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 36.98476791381836 0.0
2BCV A X-ray 2.0 4 T 0.27079567 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 40.91685485839844 0.0
3PNC A X-ray 2.0 4 C 0.23222902 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 31.38820457458496 0.0
2PFO A X-ray 2.0 4 D 0.20581481 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 40.354671478271484 0.0
3MDC A X-ray 2.0 4 D 0.17102903 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 32.5919189453125 0.0
4FO6 A X-ray 2.009999990463257 4 P 0.23321553 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 36.57789993286133 0.0
3MDA A X-ray 2.0299999713897705 4 D 0.29463115 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 35.18627166748047 0.0
5IIO A X-ray 2.0799999237060547 3 D 0.5713156 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 25.847293853759766 0.0
2PFQ A X-ray 2.0999999046325684 4 T 0.3086704 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 33.293880462646484 0.0
1RZT A X-ray 2.0999999046325684 4 [NA]A:2001 0.43788713 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 30.609304428100586 0.0
4K4H A X-ray 2.0999999046325684 4 B 0.21024542 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 29.175125122070312 0.0
2PFP A X-ray 2.0999999046325684 4 T 0.22705115 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 37.808773040771484 0.0
3UQ0 A X-ray 2.140000104904175 4 [SO4]A:2 0.21374628 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 40.29404067993164 0.0
4K4G A X-ray 2.1500000953674316 4 D 0.20401911 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 24.869903564453125 0.0
4X5V A X-ray 2.1500000953674316 4 T 0.4467201 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 42.61502456665039 0.0
5IIN A X-ray 2.1500000953674316 4 T 0.3764249 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 36.87800598144531 0.0
1XSP A X-ray 2.200000047683716 4 T 0.30383816 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 26.29387092590332 0.0
3PMN A X-ray 2.200000047683716 4 C 0.12878132 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 31.057571411132812 0.0
2BCU A X-ray 2.200000047683716 4 T 0.30967692 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 26.64829444885254 0.0
3C5G A X-ray 2.200000047683716 4 D 0.24581727 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 27.403682708740234 0.0
2BCS A X-ray 2.200000047683716 4 T 0.2815819 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 38.49538803100586 0.0
4K4I A X-ray 2.25 4 D 0.21661372 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 29.129886627197266 0.0
3C5F A X-ray 2.25 16 T 0.3070221 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 30.045888900756836 0.0
3UQ2 A X-ray 2.25 4 D 0.38277176 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 33.62834167480469 0.0
1XSL A X-ray 2.299999952316284 3 D 0.5933169 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 28.498144149780273 0.0
5CP2 A X-ray 2.359999895095825 4 [SO4]A:601 0.39566073 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 31.450828552246094 0.0
4XUS A X-ray 2.4000000953674316 4 T 0.3728221 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 36.61017990112305 0.0
2GWS A X-ray 2.4000000953674316 4 [NA]A:940 0.45571682 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 29.077083587646484 0.0
3MGH A X-ray 2.4000000953674316 4 D 0.5591562 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 27.572975158691406 0.0
5CWR A X-ray 2.5 4 P 0.3143771 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 28.95867919921875 0.0
5CA7 A X-ray 2.5199999809265137 4 B 0.16222978 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 26.903854370117188 0.0
3PML A X-ray 2.5999999046325684 16 D 0.29054025 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 30.32752227783203 0.0
3MGI A X-ray 2.5999999046325684 4 D 0.3703988 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 34.6335334777832 0.0
5DKW A X-ray 2.690000057220459 4 P 0.38810164 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 25.430063247680664 0.0
5CR0 A X-ray 2.75 8 P 1.0 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 23.873249053955078 0.0
4XQ8 A X-ray 2.799999952316284 8 B 0.20517442 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 33.41376876831055 0.0
5DDM A X-ray 2.799999952316284 4 [SO4]A:601 0.21977831 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 26.079572677612305 0.0
5CJ7 A X-ray 2.9000000953674316 4 P 1.0 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 27.00689125061035 0.0
5CHG A X-ray 2.9000000953674316 4 P 0.5164728 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 28.016769409179688 0.0
4XRH A X-ray 3.0 4 B 0.21717197 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 31.67524528503418 0.0
3HX0 A X-ray 3.0 4 D 0.44132593 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 41.978580474853516 0.0
5CB1 A X-ray 3.299999952316284 8 A 1.0 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 45.0692253112793 0.0
5DDY A X-ray 3.359999895095825 8 A 0.29723746 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
450 450 SER H 0.47 39.38615036010742 0.0

Mutations

Showing 2 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
221 T P Polymorphism
438 R W Polymorphism