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PDB 
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Phospho-sites

Showing 19 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
24 THR PRIDE yes
40 SER UP, PRIDE Combined yes
48 SER PRIDE
50 SER PRIDE
71 THR PRIDE yes
94 SER UP Combined
114 SER PRIDE yes
120 SER UP, PRIDE Combined yes
121 TYR PRIDE yes
141 SER PRIDE
143 SER UP, PRIDE Combined
160 SER UP, PRIDE Combined yes
260 THR PRIDE yes
455 THR PRIDE yes
469 SER UP, PRIDE Combined yes
473 SER UP, PRIDE Combined yes
479 SER PRIDE yes
490 SER PRIDE
495 THR UP, PRIDE Combined

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 23 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
24 1 33 24 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 3 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
40 34 42 7 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 9 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
48 46 58 3 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
50 46 58 5 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
50 50 58 1 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 14 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD002286 10 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 -
71 71 80 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
114 86 115 29 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
120 116 126 5 3
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 9 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
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 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
121 116 126 6 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
141 140 149 2 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 9 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
141 141 149 1 2
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
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 -
143 140 149 4 3
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 17 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD003531 13 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
PXD004452 10 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
143 141 149 3 4
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004252 2 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 19 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD003531 4 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD005366 37 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 -
143 141 146 3 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD002286 16 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 - -
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
160 155 163 6 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 12 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
260 247 272 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
455 449 457 7 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD003531 5 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
455 449 463 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
469 464 477 6 3
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 4 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD001333 5 Anion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC Homo sapiens (Human) PARTIAL 2015-04-23 HeLa cell -
PXD002286 9 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 -
473 464 486 10 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
479 464 486 16 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004452 3 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
490 487 499 4 2
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 - -
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
495 487 499 9 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD002286 10 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 -
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 -

Structures

Showing 9 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
5VCZ A X-ray 1.5 Monomer [XZN]A:401 0.1566004 94, 114, 120, 121, 141, 143, 160, 260
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
94 94 SER C 0.92 16.38259506225586 0.0
97 97 TYR C 1.0 29.709754943847656 0.0
114 114 SER E 0.79 52.372154235839844 0.0
120 120 SER C 1.0 110.60428619384766 0.0
121 121 TYR C 0.94 101.6285629272461 0.0
141 141 SER E 0.89 10.816899299621582 0.0
143 143 SER C 0.71 56.387794494628906 0.0
160 160 SER H 0.84 5.034548282623291 0.0
260 260 THR C 0.49 60.71490478515625 0.0
319 319 TYR C 0.71 95.8849868774414 0.0
5VCY A X-ray 1.559999942779541 Monomer [DB8]A:401 0.11571936 94, 114, 120, 121, 141, 143, 160, 260
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
94 94 SER C 0.92 17.259586334228516 0.0
97 97 TYR C 1.0 29.674541473388672 0.0
114 114 SER E 0.79 51.252479553222656 0.0
120 120 SER C 1.0 112.54241180419922 0.0
121 121 TYR C 0.94 95.04055786132812 0.0
141 141 SER E 0.89 12.838374137878418 0.0
143 143 SER C 0.71 54.854923248291016 0.0
160 160 SER H 0.84 10.889931678771973 0.0
260 260 THR C 0.49 66.65907287597656 0.0
319 319 TYR C 0.71 95.1500015258789 0.0
5VD1 A X-ray 1.7000000476837158 Monomer [P48]A:401 0.15186411 94, 114, 120, 121, 141, 143, 160, 260
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
94 94 SER C 0.92 17.00118064880371 0.0
97 97 TYR C 1.0 29.059154510498047 0.0
114 114 SER E 0.79 51.913047790527344 0.0
120 120 SER C 1.0 111.31375885009766 0.0
121 121 TYR C 0.94 102.10062408447266 24.63100814819336
141 141 SER E 0.89 11.916471481323242 0.0
143 143 SER C 0.71 55.2451286315918 0.0
160 160 SER H 0.84 4.794704914093018 0.0
260 260 THR C 0.49 66.20443725585938 0.0
319 319 TYR C 0.71 92.66961669921875 0.0
5VD3 A X-ray 1.7999999523162842 Monomer [H8H]A:401 0.16243628 94, 114, 120, 121, 141, 143, 160, 260
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
94 94 SER C 0.92 19.01448631286621 0.0
97 97 TYR C 1.0 28.9373836517334 0.0
114 114 SER E 0.79 51.705223083496094 1.4444105625152588
120 120 SER C 1.0 111.76539611816406 0.0
121 121 TYR C 0.94 96.59918975830078 7.494133472442627
141 141 SER E 0.89 11.290958404541016 0.0
143 143 SER C 0.71 59.66878128051758 0.0
160 160 SER H 0.84 6.964008808135986 0.0
260 260 THR C 0.49 94.01400756835938 0.0
319 319 TYR C 0.71 94.02677917480469 0.0
5VD0 A X-ray 2.130000114440918 Monomer [8X7]A:401 0.117905624 94, 114, 120, 121, 141, 143, 160, 260
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
94 94 SER C 0.92 19.167707443237305 0.0
97 97 TYR C 1.0 29.2811336517334 0.0
114 114 SER E 0.79 53.21950149536133 0.0
120 120 SER C 1.0 112.52812194824219 0.0
121 121 TYR C 0.94 96.69210815429688 22.13588523864746
141 141 SER E 0.89 13.04185676574707 0.0
143 143 SER C 0.71 56.6024169921875 0.0
160 160 SER H 0.84 8.012728691101074 0.0
260 260 THR C 0.49 74.9955062866211 0.0
319 319 TYR C 0.71 92.91686248779297 0.0
5VCW A X-ray 2.25 2 [93J]A:401 0.052368436 94, 114, 120, 121, 141, 143, 160, 260
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
94 94 SER C 0.92 9.15758228302002 0.0
97 97 TYR C 1.0 26.36264419555664 0.0
114 114 SER E 0.79 53.07913589477539 0.0
120 120 SER C 1.0 103.8321533203125 0.0
121 121 TYR C 0.94 101.08987426757812 0.0
141 141 SER E 0.89 14.27883243560791 0.0
143 143 SER C 0.71 51.948143005371094 0.0
160 160 SER H 0.84 10.144888877868652 0.0
260 260 THR C 0.49 85.15361785888672 0.0
319 319 TYR C 0.71 107.71985626220703 0.0
5VCX A X-ray 2.700000047683716 Monomer [H8H]A:401 0.09518678 94, 114, 120, 121, 141, 143, 160, 260
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
94 94 SER C 0.92 18.19365882873535 0.0
97 97 TYR C 1.0 25.178613662719727 0.0
114 114 SER E 0.79 52.504356384277344 3.119163990020752
120 120 SER C 1.0 106.99223327636719 0.0
121 121 TYR C 0.94 98.49862670898438 12.39630126953125
141 141 SER E 0.89 9.374227523803711 0.0
143 143 SER C 0.71 61.69856643676758 0.0
160 160 SER H 0.84 10.485095977783203 0.0
260 260 THR C 0.49 90.52778625488281 0.0
319 319 TYR C 0.71 78.40260314941406 0.0
3P1A A X-ray 1.7000000476837158 Monomer A 0.0 94, 114, 120, 121, 141, 143, 160
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
94 94 SER C 0.92 17.987407684326172 0.0
97 97 TYR C 1.0 31.87835693359375 0.0
114 114 SER E 0.79 53.36142349243164 32.50303268432617
120 120 SER C 1.0 112.3736801147461 0.0
121 121 TYR C 0.94 100.14404296875 0.0
141 141 SER E 0.89 13.650740623474121 0.0
143 143 SER C 0.71 56.48516082763672 0.0
160 160 SER H 0.84 10.272723197937012 0.0
319 319 TYR C 0.71 97.4767837524414 0.0
5VCV A X-ray 1.9199999570846558 Monomer [CL]A:402 0.05001072 94, 114, 120, 121, 141, 143, 160
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
94 94 SER C 0.92 15.764394760131836 0.0
97 97 TYR C 1.0 27.412199020385742 0.0
114 114 SER E 0.79 50.31962966918945 0.0
120 120 SER C 1.0 109.39429473876953 0.0
121 121 TYR C 0.94 98.15266418457031 0.0
141 141 SER E 0.89 14.398344993591309 0.0
143 143 SER C 0.71 42.63390350341797 0.0
160 160 SER H 0.84 15.153799057006836 0.0
319 319 TYR C 0.71 96.81512451171875 0.0

Mutations

Showing 6 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
103 E Q Polymorphism
140 R C Polymorphism
246 R H Polymorphism
351 E K Polymorphism
417 P R Polymorphism
445 V A Polymorphism