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Phospho-sites

Showing 4 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
426 PhosphoS PRIDE
429 PhosphoT PRIDE
878 PhosphoT PRIDE yes
1433 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 4 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
426 413 436 14 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues
PXD000218 1 System-level analysis of cancer and stomal cell specific proteomes reveals extensive reprogramming of phosphorylation networks by tumor microenvironment Homo sapiens (Human),Mus musculus (Mouse) COMPLETE 2014-04-01 Epithelial cell, colon
429 413 436 17 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues
PXD000218 1 System-level analysis of cancer and stomal cell specific proteomes reveals extensive reprogramming of phosphorylation networks by tumor microenvironment Homo sapiens (Human),Mus musculus (Mouse) COMPLETE 2014-04-01 Epithelial cell, colon
878 850 879 29 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues
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
1433 1413 1440 21 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues
PXD002286 1 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 -

Structures

Showing 11 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
4A5W A X-ray 3.50 A 4 B 1.0 426, 429, 878, 1433
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
426 426 SER C 0.67 79.033074562 0.0
429 429 THR E 0.53 57.641137531 24.285397285
878 878 THR C 0.3 58.316686764 0.0
1433 1433 SER E 0.14 67.338257392 0.0
5I5K A X-ray 4.20 A 2 B 0.0 426, 429, 878, 1433
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
426 426 SER C 0.67 93.757799103 0.0
429 429 THR C 0.53 30.455051864 0.0
878 878 THR C 0.3 123.90629756 0.0
1433 1433 SER E 0.14 53.543044201 0.0
3PRX A X-ray 4.30 A 4 B 1.0 426, 429, 878, 1433
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
426 426 SER C 0.67 85.071406992 22.627397524
429 429 THR E 0.53 39.654983956 0.0
878 878 THR C 0.3 74.60175796 26.046563727
1433 1433 SER E 0.14 32.186009304 0.0
3PVM A X-ray 4.30 A 2 B 1.0 426, 429, 878, 1433
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
426 426 SER C 0.67 83.503585448 16.883014099
429 429 THR E 0.53 40.003279728 0.0
878 878 THR E 0.3 94.403653284 28.206808074
1433 1433 SER E 0.14 42.250518526 0.0
5HCC A X-ray 2.59 A 4 B 1.0 426, 429, 1433
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
426 426 SER C 0.67 82.32218426 0.0
429 429 THR E 0.53 45.01510721 0.0
1433 1433 SER E 0.14 26.803782198 0.0
5HCD B X-ray 2.98 A 4 A 1.0 426, 429, 1433
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
426 426 SER C 0.67 82.582624812 0.0
429 429 THR E 0.53 45.490306285 0.0
1433 1433 SER E 0.14 26.682012191 0.0
3CU7 A X-ray 3.10 A 2 [CD]A:2006 0.243114 426, 429, 1433
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
426 426 SER C 0.67 73.011656712 0.0
429 429 THR E 0.53 34.436505921 0.0
1433 1433 SER E 0.14 30.223188921 0.0
5HCE B X-ray 3.12 A 4 A 1.0 426, 429, 1433
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
426 426 SER C 0.67 83.739154013 0.0
429 429 THR E 0.53 46.804203349 0.0
1433 1433 SER E 0.14 28.939712971 0.0
3KLS A X-ray 3.60 A 2 [CD]A:1678 0.263821 426, 429, 1433
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
426 426 SER C 0.67 79.407559306 0.0
429 429 THR E 0.53 25.438538555 0.0
1433 1433 SER E 0.14 36.520040809 0.0
3KM9 A X-ray 4.20 A Monomer [CD]A:1678 0.0894522 426, 429, 1433
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
426 426 SER C 0.67 67.428378147 0.0
429 429 THR C 0.53 18.860949287 0.0
1433 1433 SER C 0.14 45.4546905 0.0
4E0S A X-ray 4.21 A 4 B 1.0 426, 429, 1433
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
426 426 SER C 0.67 63.26245419 0.0
429 429 THR E 0.53 38.637576973 15.80801255
1433 1433 SER C 0.14 36.688047236 0.0

Mutations

Showing 17 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
145 V I Polymorphism -
354 L M Polymorphism -
389 T I Polymorphism -
449 R G Polymorphism -
518 F S Polymorphism -
802 V I Polymorphism -
885 R C Polymorphism -
928 R Q Polymorphism -
933 G V Polymorphism -
966 D Y Polymorphism -
1033 I T Polymorphism -
1037 D N Polymorphism -
1043 Q K Polymorphism -
1053 M L Polymorphism -
1310 S N Polymorphism -
1365 V A Polymorphism -
1437 E D Polymorphism -