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PDB 
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Phospho-sites

Showing 3 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
14 PhosphoY PRIDE
16 PhosphoS PRIDE
130 PhosphoS UP Similarity

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 2 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
14 8 19 7 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
16 8 19 9 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 8 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
6BSX A X-ray 1.649999976158142 Monomer [GDP]A:203 0.0546544 14, 16, 130
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 14 TYR C 0.6 61.34470748901367 0.0
16 16 SER C 0.35 92.67243194580078 33.06968307495117
130 130 SER C 1.0 50.39936828613281 0.0
3T5G A X-ray 1.7000000476837158 Monomer [GDP]A:201 0.057339948 14, 16, 130
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 14 TYR C 0.6 58.193519592285156 0.0
16 16 SER C 0.35 80.05282592773438 31.172517776489258
130 130 SER C 1.0 51.62961196899414 0.0
1XTQ A X-ray 2.0 Monomer [GDP]A:201 0.051826872 14, 16, 130
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 14 TYR C 0.6 26.938758850097656 0.0
16 16 SER C 0.35 88.16837310791016 33.20782470703125
130 130 SER C 1.0 36.88199996948242 0.0
3SEA A X-ray 2.0 4 [GDP]A:201 0.195527 14, 16, 130
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 14 TYR C 0.6 38.23189163208008 0.0
16 16 SER C 0.35 94.555908203125 33.846500396728516
130 130 SER C 1.0 46.58714294433594 0.0
5YXH A X-ray 2.0399999618530273 Monomer [GDP]A:201 0.056779098 14, 16, 130
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 14 TYR C 0.6 33.7612190246582 0.0
16 16 SER C 0.35 82.30072784423828 30.193212509155273
130 130 SER C 1.0 43.885169982910156 0.0
6BT0 A X-ray 2.5999999046325684 Monomer [GDP]A:202 0.055925947 14, 16, 130
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 14 TYR C 0.6 25.928102493286133 0.0
16 16 SER C 0.35 91.38943481445312 33.43488693237305
130 130 SER C 1.0 49.75788497924805 0.0
1XTR A X-ray 2.6500000953674316 Monomer [GNP]A:179 0.04603444 14, 16, 130
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 14 TYR C 0.6 41.640708923339844 0.0
16 16 SER C 0.35 66.98426055908203 20.48430824279785
130 130 SER C 1.0 46.533809661865234 0.0
1XTS A X-ray 2.799999952316284 Monomer [GTP]A:179 0.04970446 14, 16, 130
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 14 TYR E 0.6 38.98570251464844 0.0
16 16 SER C 0.35 58.730411529541016 21.895395278930664
130 130 SER C 1.0 50.295291900634766 0.0

Mutations

Showing 1 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
139 E K Unclassified A colorectal cancer sample