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PDB 
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Phospho-sites

Showing 7 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
50 SER PRIDE yes
107 THR PRIDE yes
153 TYR UP Experimental
301 THR PRIDE yes
302 SER UP, PRIDE Combined yes
307 SER UP, PRIDE Combined yes
310 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 6 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
50 46 56 5 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD003531 1 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
107 101 116 7 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
301 293 324 9 2
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 -
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
302 293 324 10 2
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
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
307 293 324 15 2
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 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 -
310 293 324 18 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 6 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture

Structures

Showing 10 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
4RHW E X-ray 2.0999999046325684 6 C 0.0829317 50
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
50 50 SER C 0.64 49.85384750366211 0.0
1NW9 B X-ray 2.4000000953674316 2 A 1.0 153
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
153 153 TYR C 0.92 11.498761177062988 0.0
317 317 THR E 0.44 63.55348587036133 39.6086540222168
1JXQ A X-ray 2.799999952316284 3 B 1.0 153
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
153 153 TYR E 0.92 17.809911727905273 0.0
2AR9 A X-ray 2.799999952316284 2 B 1.0 153
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
153 153 TYR E 0.92 15.535761833190918 0.0
3V3K A X-ray 3.490000009536743 2 C 1.0 153
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
153 153 TYR C 0.92 17.058364868164062 0.0
5JUY O EM 4.099999904632568 Monomer E 0.0 50
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
50 50 SER C 0.64 49.55718994140625 0.0
5WVE S EM 4.400000095367432 Monomer O 0.0 50
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
50 50 SER C 0.64 46.102821350097656 0.0
3D9T C X-ray 1.5 2 A 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
317 2 THR E 0.44 121.12167358398438 46.3913688659668
3YGS P X-ray 2.5 Monomer C 0.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
50 51 SER C 0.64 46.558433532714844 0.0
5WVC B X-ray 2.990000009536743 Monomer [IOD]B:402 0.1
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
50 250 SER C 0.64 50.11977767944336 0.0

Mutations

Showing 11 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
28 A V Polymorphism
99 S L Polymorphism
102 T I Polymorphism
106 L V Polymorphism
114 E D Polymorphism
136 F L Polymorphism
173 R H Polymorphism
176 G R Polymorphism
185 I M Polymorphism
192 R C Polymorphism
221 Q R Polymorphism