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PDB 
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Phospho-sites

Showing 10 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
406 SER PRIDE yes
578 SER PRIDE yes
674 SER PRIDE yes
756 SER UP, PRIDE Similarity yes
765 SER PRIDE yes
766 SER UP, PRIDE Combined yes
1042 THR PRIDE yes
1051 THR PRIDE
1059 THR PRIDE
1113 THR 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 12 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
406 400 420 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
578 552 579 27 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004452 2 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
674 672 678 3 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD002286 1 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 -
756 725 759 32 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004452 12 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
756 725 763 32 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000680 12 Stable isotope labeling of phosphoproteins for large-scale phosphorylation rate determination Homo sapiens (Human) COMPLETE 2014-04-15 HeLa cell,HEK-293 cell
765 764 778 2 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001060 5 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell -
PXD003531 4 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
766 764 778 3 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
766 765 778 2 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001060 2 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell
1042 1033 1046 10 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 2 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
1051 1050 1065 2 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
1059 1050 1065 10 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
1113 1105 1118 9 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

Structures

Showing 5 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
6F9N A X-ray 2.5 2 B 1.0 578, 674, 1042, 1051, 1059, 1113
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
578 578 SER E 1.0 0.0 0.0
674 674 SER C 0.9 120.33826446533203 0.0
1038 1038 THR E 0.95 0.7353252172470093 0.0
1039 1039 SER E 1.0 7.124538421630859 0.0
1042 1042 THR E 0.79 61.66707992553711 0.0
1051 1051 THR C 1.0 89.18164825439453 19.634044647216797
1059 1059 THR E 0.76 86.64288330078125 0.0
1110 1110 SER C 1.0 15.653966903686523 0.0
1113 1113 THR C 1.0 45.699588775634766 0.0
6BLY A EM 3.359999895095825 Monomer B 0.0 578, 1042, 1051, 1059, 1113
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
578 578 SER E 1.0 0.0 0.0
1038 1038 THR E 0.95 2.5916712284088135 0.0
1039 1039 SER E 1.0 10.200692176818848 0.0
1042 1042 THR E 0.79 53.715904235839844 0.0
1051 1051 THR C 1.0 64.47022247314453 0.0
1059 1059 THR E 0.76 99.86216735839844 0.0
1110 1110 SER C 1.0 24.728063583374023 0.0
1113 1113 THR C 1.0 61.75459671020508 0.0
6BM0 A EM 3.799999952316284 Monomer B 0.0 578, 1042, 1051, 1059, 1113
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
578 578 SER E 1.0 1.1036617755889893 0.0
1038 1038 THR E 0.95 1.720069408416748 0.0
1039 1039 SER C 1.0 11.38563346862793 0.0
1042 1042 THR E 0.79 50.128997802734375 0.0
1051 1051 THR C 1.0 66.40328979492188 0.0
1059 1059 THR E 0.76 110.5949935913086 0.0
1110 1110 SER C 1.0 23.868745803833008 0.0
1113 1113 THR C 1.0 47.203216552734375 0.0
6FBS A EM 3.069999933242798 Monomer B 0.0 578, 1042, 1059, 1113
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
578 578 SER E 1.0 0.0 0.0
1038 1038 THR E 0.95 1.2285844087600708 0.0
1039 1039 SER E 1.0 6.419914722442627 0.0
1042 1042 THR E 0.79 62.78413391113281 0.0
1059 1059 THR C 0.76 74.41311645507812 0.0
1110 1110 SER C 1.0 21.056808471679688 0.0
1113 1113 THR C 1.0 61.54884338378906 0.0
6FUW A EM 3.069999933242798 Monomer B 0.0 578, 1042, 1059, 1113
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
578 578 SER E 1.0 0.0 0.0
1038 1038 THR E 0.95 1.2285844087600708 0.0
1039 1039 SER E 1.0 6.419914722442627 0.0
1042 1042 THR E 0.79 62.78413391113281 0.0
1059 1059 THR C 0.76 74.41311645507812 0.0
1110 1110 SER C 1.0 21.056808471679688 0.0
1113 1113 THR C 1.0 61.54884338378906 0.0

Mutations

Showing 0 results

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