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PDB 
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Phospho-sites

Showing 5 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
367 SER PRIDE
371 SER PRIDE
559 THR UP Experimental
643 SER PRIDE yes
694 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 4 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
367 367 385 1 1
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
371 367 385 5 1
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
643 636 650 8 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
694 692 701 3 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
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

Structures

Showing 4 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
4IDT A X-ray 2.4000000953674316 2 [T28]A:701 0.1 367, 371, 559, 643
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
367 367 SER C 0.35 90.07090759277344 0.0
371 371 SER E 0.68 97.7474594116211 0.0
559 559 THR E 1.0 47.99559783935547 0.0
643 643 SER C 0.96 37.189308166503906 0.0
4DN5 A X-ray 2.5 2 [AGS]A:1008 0.40231246 367, 371, 559, 643
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
367 367 SER C 0.35 105.0412826538086 0.0
371 371 SER E 0.68 103.95652770996094 0.0
559 559 THR E 1.0 26.278076171875 0.0
643 643 SER C 0.96 34.3688850402832 0.0
4IDV A X-ray 2.9000000953674316 Monomer C 0.0 559, 643
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
559 559 THR C 1.0 30.901241302490234 0.0
643 643 SER C 0.96 29.420150756835938 0.0
4G3D A X-ray 2.9000000953674316 4 B 0.62113655 559, 643
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
559 559 THR C 1.0 24.25902557373047 0.0
643 643 SER C 0.96 42.07993698120117 0.0

Mutations

Showing 7 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
140 S N Polymorphism
255 T M Polymorphism
514 G K Unclassified A lung neuroendocrine carcinoma sample
674 H Y Polymorphism
764 T A Polymorphism
852 T I Unclassified An ovarian mucinous carcinoma sample
928 P H Polymorphism