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PDB 
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Phospho-sites

Showing 6 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
8 SER UP Combined
11 SER PRIDE yes
37 THR UP Combined
69 SER UP Combined
205 SER PRIDE yes
209 SER 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 5 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
11 1 33 11 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
205 192 212 14 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000680 3 Stable isotope labeling of phosphoproteins for large-scale phosphorylation rate determination Homo sapiens (Human) COMPLETE 2014-04-15 HeLa cell,HEK-293 cell
205 192 215 14 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004415 23 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte
209 192 212 18 13
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001060 11 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell -
PXD003531 106 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD001333 2 Anion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC Homo sapiens (Human) PARTIAL 2015-04-23 HeLa cell -
PXD005366 117 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 -
PXD004452 134 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
PXD001374 3 Label-free quantitative phosphoproteomics with novel pairwise abundance normalization reveals synergistic RAS and CIP2A signaling Homo sapiens (Human) PARTIAL 2015-08-24 HeLa cell -
PXD002394 11 Proteomic and phosphoproteomic analysis of cisplatin resistance in patient derived serous ovarian cancer Homo sapiens (Human) PARTIAL 2017-05-02 cell suspension culture -
PXD001550 64 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
PXD000680 111 Stable isotope labeling of phosphoproteins for large-scale phosphorylation rate determination Homo sapiens (Human) COMPLETE 2014-04-15 HeLa cell,HEK-293 cell -
PXD000612 61 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD002436 5 Monitoring cellular phosphorylation signaling pathways into chromatin and down to the gene level Homo sapiens (Human) COMPLETE 2015-11-09 HeLa cell
PXD004415 124 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte -
PXD001546 24 Reproducibility of label-free single-shot phosphoproteomics applied to CRC cell lines Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
209 192 215 18 3
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004415 22 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte -
PXD004452 6 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
PXD001374 8 Label-free quantitative phosphoproteomics with novel pairwise abundance normalization reveals synergistic RAS and CIP2A signaling Homo sapiens (Human) PARTIAL 2015-08-24 HeLa cell -

Structures

Showing 9 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
4DGL A X-ray 3.0 4 B 1.0 8, 11, 37, 69, 205, 209
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 8 SER C 1.0 102.60459899902344 0.0
11 11 SER H 0.93 54.678016662597656 0.0
37 37 THR C 0.92 97.84305572509766 0.0
69 69 SER H 0.94 57.58987045288086 0.0
197 197 TYR H 0.62 95.04043579101562 68.1462173461914
205 205 SER H 0.72 63.27836227416992 14.766161918640137
209 209 SER C 0.46 55.98643493652344 0.0
4MD7 A X-ray 3.0999999046325684 4 B 1.0 8, 11, 37, 69, 205
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 8 SER C 1.0 48.367366790771484 0.0
11 11 SER H 0.93 33.79703140258789 0.0
37 37 THR C 0.92 87.7430648803711 0.0
69 69 SER H 0.94 43.058929443359375 0.0
197 197 TYR H 0.62 95.0540771484375 57.70541000366211
205 205 SER H 0.72 94.64321899414062 11.88942813873291
1JWH C X-ray 3.0999999046325684 4 D 0.5972848 8, 11, 37, 69, 205
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 8 SER C 1.0 50.748844146728516 0.0
11 11 SER H 0.93 59.805938720703125 0.0
37 37 THR C 0.92 85.47563171386719 0.0
69 69 SER H 0.94 87.47388458251953 0.0
197 197 TYR H 0.62 160.37872314453125 0.0
205 205 SER C 0.72 128.75326538085938 29.488895416259766
4MD8 A X-ray 3.299999952316284 4 B 1.0 8, 11, 37, 69, 205
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 8 SER C 1.0 47.54342269897461 0.0
11 11 SER H 0.93 33.17111587524414 0.0
37 37 THR C 0.92 89.40412139892578 0.0
69 69 SER H 0.94 41.34729766845703 0.0
197 197 TYR H 0.62 92.61500549316406 57.766658782958984
205 205 SER H 0.72 97.59359741210938 13.222826957702637
4NH1 C X-ray 3.299999952316284 4 D 1.0 8, 11, 37, 69, 205
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 8 SER C 1.0 43.36662673950195 0.0
11 11 SER H 0.93 52.66762161254883 0.0
37 37 THR C 0.92 90.1490478515625 0.0
69 69 SER H 0.94 13.996485710144043 0.0
197 197 TYR H 0.62 98.43962860107422 64.98966979980469
205 205 SER C 0.72 92.92738342285156 21.381135940551758
4MD9 A X-ray 3.5 4 B 1.0 8, 11, 37, 69, 205
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 8 SER C 1.0 42.788753509521484 0.0
11 11 SER H 0.93 37.29996109008789 0.0
37 37 THR C 0.92 96.0779037475586 0.0
69 69 SER H 0.94 32.87076950073242 0.0
197 197 TYR H 0.62 94.76007080078125 69.11653137207031
205 205 SER H 0.72 85.83281707763672 15.34250545501709
1QF8 A X-ray 1.7400000095367432 2 [MG]A:217 0.1 8, 11, 37, 69
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 8 SER C 1.0 47.12985610961914 0.0
11 11 SER H 0.93 42.98993682861328 0.0
37 37 THR C 0.92 83.51412963867188 0.0
69 69 SER H 0.94 34.90510177612305 0.0
3EED A X-ray 2.799999952316284 4 [SO4]A:195 0.4240199 8, 11, 37, 69
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 8 SER C 1.0 43.28019714355469 0.0
11 11 SER H 0.93 41.83977127075195 0.0
37 37 THR C 0.92 96.4226303100586 0.0
69 69 SER H 0.94 60.24381637573242 0.0
1DS5 E X-ray 3.1600000858306885 2 B 0.36028564
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
197 197 TYR E 0.62 91.41292572021484 17.808094024658203

Mutations

Showing 0 results

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