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PDB 
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Phospho-sites

Showing 8 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
10 SER UP, PRIDE Combined yes
19 SER UP, PRIDE Similarity yes
20 TYR UP, PRIDE Combined yes
34 SER PRIDE yes
52 THR PRIDE yes
106 SER PRIDE yes
123 TYR PRIDE yes
132 SER 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 8 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
10 7 22 4 2
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
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 -
19 7 22 13 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004415 3 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte
20 7 22 14 4
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 -
PXD001565 3 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain -
PXD003198 8 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line
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 -
34 28 39 7 5
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004252 1 Modulating the selectivity of affinity absorbents to multi-phosphopeptides by a novel competitive substitution strategy Homo sapiens (Human) PARTIAL 2016-08-03 cell culture
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 -
PXD001333 6 Anion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC Homo sapiens (Human) PARTIAL 2015-04-23 HeLa cell -
PXD005366 2 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 -
PXD000680 11 Stable isotope labeling of phosphoproteins for large-scale phosphorylation rate determination Homo sapiens (Human) COMPLETE 2014-04-15 HeLa cell,HEK-293 cell -
52 40 53 13 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 4 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
106 101 120 6 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 1 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
123 122 128 2 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 1 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
132 130 145 3 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000680 2 Stable isotope labeling of phosphoproteins for large-scale phosphorylation rate determination Homo sapiens (Human) COMPLETE 2014-04-15 HeLa cell,HEK-293 cell

Structures

Showing 8 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
3KAS A X-ray 2.4000000953674316 2 [K]A:1 0.70242876 123, 132
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
123 123 TYR C 0.72 171.2797393798828 0.0
132 132 SER H 0.83 30.296348571777344 0.0
1DE4 C X-ray 2.799999952316284 6 F 0.6934935 123, 132
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
123 123 TYR C 0.72 170.83409118652344 0.0
132 132 SER H 0.83 31.953943252563477 0.0
1CX8 A X-ray 3.200000047683716 2 B 0.5567299 123, 132
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
123 123 TYR C 0.72 162.4397735595703 0.0
132 132 SER H 0.83 28.301008224487305 0.0
3S9L A X-ray 3.2200000286102295 2 A 0.67429316 123, 132
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
123 123 TYR C 0.72 153.45767211914062 0.0
132 132 SER H 0.83 35.03409194946289 0.0
3S9N A X-ray 3.25 2 A 1.0 123, 132
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
123 123 TYR C 0.72 154.618408203125 0.0
132 132 SER H 0.83 37.67414855957031 0.0
3S9M A X-ray 3.319999933242798 2 A 1.0 123, 132
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
123 123 TYR C 0.72 147.7183074951172 0.0
132 132 SER H 0.83 33.25446319580078 0.0
1SUV A EM 7.5 Monomer B 0.0 123, 132
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
123 123 TYR C 0.72 163.734130859375 0.0
132 132 SER H 0.83 28.939502716064453 0.0
2NSU A EM 27.0 Monomer B 0.0 123, 132
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
123 123 TYR C 0.72 165.84927368164062 0.0
132 132 SER H 0.83 28.575462341308594 0.0

Mutations

Showing 5 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
20 Y H Disease Immunodeficiency 46 (IMD46) [MIM:616740]
142 G S Polymorphism
212 L V Polymorphism
420 G S Polymorphism
677 R H Polymorphism