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PDB 
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Phospho-sites

Showing 7 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
15 PhosphoT PRIDE yes
23 PhosphoS PRIDE yes
35 PhosphoY PRIDE yes
96 PhosphoY PRIDE yes
153 PhosphoS UP, PRIDE Combined yes
163 PhosphoS UP, PRIDE Combined yes
165 PhosphoY 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 11 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
15 12 17 4 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
23 23 30 1 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
35 31 38 5 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
96 92 101 5 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD001565 1 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain
96 94 101 3 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD003198 1 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line
153 140 155 14 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
153 151 162 3 4
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD002436 1 Monitoring cellular phosphorylation signaling pathways into chromatin and down to the gene level Homo sapiens (Human) COMPLETE 2015-11-09 HeLa cell -
PXD001546 8 Reproducibility of label-free single-shot phosphoproteomics applied to CRC cell lines Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
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
163 156 172 8 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD001333 1 Anion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC Homo sapiens (Human) PARTIAL 2015-04-23 HeLa cell -
PXD004452 3 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
163 163 172 1 2
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
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 -
165 156 172 10 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD001333 1 Anion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC Homo sapiens (Human) PARTIAL 2015-04-23 HeLa cell
165 163 172 3 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD001333 1 Anion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC Homo sapiens (Human) PARTIAL 2015-04-23 HeLa cell

Structures

Showing 6 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
6G5I J EM 3.5 Monomer 2 0.0 15, 23, 35, 96, 153, 163, 165
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
15 15 THR C 1 88.10769653320312 53.67539596557617
23 23 SER C 1 97.81075286865234 0.0
35 35 TYR C 1 18.52888298034668 0.0
96 96 TYR H 1 96.74765014648438 0.0
153 153 SER H 1 8.55388069152832 8.55388069152832
163 163 SER C 1 5.585761547088623 0.0
165 165 TYR C 1 135.44851684570312 38.54792785644531
6G5H J EM 3.5999999046325684 Monomer 2 0.0 15, 23, 35, 96, 153, 163, 165
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
15 15 THR C 1 83.23479461669922 47.605167388916016
23 23 SER H 1 86.38471984863281 0.0
35 35 TYR C 1 17.092517852783203 0.0
96 96 TYR H 1 108.67745208740234 0.0
153 153 SER H 1 14.496384620666504 13.489239692687988
163 163 SER C 1 8.156527519226074 0.0
165 165 TYR C 1 127.95574951171875 24.085542678833008
6G18 J EM 3.5999999046325684 Monomer 2 0.0 15, 23, 35, 96, 153, 163, 165
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
15 15 THR C 1 84.11263275146484 48.242515563964844
23 23 SER H 1 92.86630249023438 0.0
35 35 TYR H 1 22.064327239990234 0.0
96 96 TYR H 1 102.27631378173828 0.0
153 153 SER C 1 11.305821418762207 11.137896537780762
163 163 SER C 1 3.749356269836426 0.0
165 165 TYR C 1 130.12432861328125 31.654809951782227
5A2Q J EM 3.9000000953674316 Monomer 2 0.0 15, 23, 35, 96, 153, 163, 165
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
15 15 THR C 1 79.19110107421875 39.66692352294922
23 23 SER H 1 84.2925033569336 0.0
35 35 TYR H 1 25.274789810180664 0.0
96 96 TYR H 1 103.76851654052734 0.0
153 153 SER C 1 15.968218803405762 14.046147346496582
163 163 SER C 1 7.861488342285156 0.0
165 165 TYR H 1 128.7719268798828 26.860870361328125
5FLX J EM 3.9000000953674316 Monomer 1 0.0 15, 23, 35, 96, 153, 163, 165
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
15 15 THR C 1 102.55162048339844 52.87035369873047
23 23 SER H 1 88.83450317382812 0.0
35 35 TYR H 1 24.63347625732422 0.0
96 96 TYR H 1 76.30973052978516 0.0
153 153 SER C 1 28.472366333007812 1.4747174978256226
163 163 SER C 1 62.415367126464844 23.575122833251953
165 165 TYR C 1 154.81796264648438 0.0
5OA3 J EM 4.300000190734863 Monomer 2 0.0 15, 23, 35, 96, 153, 163, 165
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
15 15 THR C 1 78.92570495605469 42.08046340942383
23 23 SER H 1 84.67481231689453 0.0
35 35 TYR H 1 23.757205963134766 0.0
96 96 TYR H 1 103.76634216308594 0.0
153 153 SER H 1 18.034297943115234 16.524747848510742
163 163 SER C 1 7.841275691986084 0.0
165 165 TYR H 1 135.83116149902344 29.983551025390625

Mutations

Showing 1 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
137 V F Unclassified A breast cancer sample