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PDB 
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Phospho-sites

Showing 13 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
4 PhosphoT UP Experimental
7 PhosphoT UP Experimental
11 PhosphoS UP Experimental
12 PhosphoT UP Experimental
29 PhosphoS UP, PRIDE Experimental yes
42 PhosphoY UP Experimental
46 PhosphoT PRIDE yes
58 PhosphoS UP, PRIDE Experimental yes
59 PhosphoT PRIDE yes
81 PhosphoT UP, PRIDE Experimental yes
87 PhosphoS UP Similarity
100 PhosphoY PRIDE yes
108 PhosphoT UP, PRIDE Combined 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 14 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
29 25 37 5 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
29 28 37 2 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD004252 3 Modulating the selectivity of affinity absorbents to multi-phosphopeptides by a novel competitive substitution strategy Homo sapiens (Human) PARTIAL 2016-08-03 cell culture
PXD002436 1 Monitoring cellular phosphorylation signaling pathways into chromatin and down to the gene level Homo sapiens (Human) COMPLETE 2015-11-09 HeLa cell -
29 29 37 1 6
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD004252 3 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 72 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD002436 1 Monitoring cellular phosphorylation signaling pathways into chromatin and down to the gene level Homo sapiens (Human) COMPLETE 2015-11-09 HeLa cell -
PXD003531 6 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD002286 5 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 - -
PXD004452 5 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
29 29 41 1 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD001374 1 Label-free quantitative phosphoproteomics with novel pairwise abundance normalization reveals synergistic RAS and CIP2A signaling Homo sapiens (Human) PARTIAL 2015-08-24 HeLa cell
46 42 50 5 3
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD003531 11 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD006482 1 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney
PXD005366 7 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 -
58 54 64 5 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD004415 1 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte
58 55 64 4 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD004415 2 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte
58 58 64 1 6
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD003531 33 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
PXD002286 77 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 - -
PXD005366 12 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 -
PXD001550 3 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
PXD004452 11 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 -
58 58 65 1 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 -
PXD003531 2 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
PXD004452 4 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
59 58 64 2 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD002286 32 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 - -
PXD004452 2 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
59 58 65 2 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
81 74 84 8 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD006482 2 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney
100 85 116 16 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD004415 1 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte -
PXD004452 11 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
108 85 116 24 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

Structures

Showing 18 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
5B0Z A X-ray 1.9900000095367432 10 B 0.8359074 59
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
42 41 TYR C NaN 114.08785247802734 0.0
46 45 THR H NaN 57.50202560424805 0.0
58 57 SER C NaN 43.99418258666992 8.74749755859375
59 58 THR C NaN 129.77635192871094 8.992476463317871
81 80 THR C NaN 94.1046371459961 0.0
87 86 SER H NaN 89.71401977539062 0.0
97 96 SER H NaN 35.58592224121094 35.084327697753906
100 99 TYR H NaN 91.98905944824219 75.41106414794922
108 107 THR H NaN 0.0 0.0
3R93 E X-ray 2.059999942779541 2 A 1.0 12
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
7 6 THR E NaN 125.91814422607422 83.8342056274414
11 10 SER C NaN 106.39244842529297 62.658451080322266
12 11 THR C NaN 128.64418029785156 0.0
3AV1 A X-ray 2.5 10 B 1.0 59
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
42 41 TYR C NaN 117.69635009765625 0.0
46 45 THR H NaN 56.98793029785156 0.0
58 57 SER C NaN 42.22064971923828 7.621340751647949
59 58 THR C NaN 136.8612823486328 10.528558731079102
81 80 THR C NaN 96.40544128417969 2.3276515007019043
87 86 SER H NaN 84.68939208984375 0.0
97 96 SER H NaN 34.65664291381836 34.65664291381836
100 99 TYR H NaN 89.53661346435547 80.33402252197266
108 107 THR H NaN 0.12316373735666275 0.0
5B0Y A X-ray 2.559999942779541 10 B 0.9556356 59
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
42 41 TYR C NaN 114.44904327392578 0.0
46 45 THR H NaN 58.491790771484375 0.0
58 57 SER C NaN 48.0672607421875 8.564379692077637
59 58 THR C NaN 133.853515625 7.047605991363525
81 80 THR C NaN 90.70796203613281 3.130854606628418
87 86 SER H NaN 89.55924987792969 0.0
97 96 SER H NaN 35.431278228759766 35.431278228759766
100 99 TYR H NaN 91.41392517089844 82.30168151855469
108 107 THR H NaN 0.0 0.0
5B40 A X-ray 3.3299999237060547 10 B 1.0 59
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
42 41 TYR C NaN 236.7241973876953 0.0
46 45 THR H NaN 49.919246673583984 0.0
58 57 SER C NaN 33.86982345581055 10.892996788024902
59 58 THR C NaN 133.28504943847656 5.51611328125
81 80 THR C NaN 71.48661804199219 0.0
87 86 SER H NaN 93.14704895019531 0.0
97 96 SER H NaN 45.84308624267578 45.00932693481445
100 99 TYR H NaN 97.34331512451172 86.24533081054688
108 107 THR H NaN 0.3359238803386688 0.3359238803386688
6FML M EM 4.340000152587891 Monomer N 0.0 59
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
42 41 TYR C NaN 149.08810424804688 0.0
46 45 THR H NaN 54.476314544677734 0.0
58 57 SER C NaN 37.79532241821289 7.131393909454346
59 58 THR C NaN 127.6499252319336 11.069056510925293
81 80 THR C NaN 106.9157485961914 0.0
87 86 SER H NaN 90.10826110839844 0.0
97 96 SER H NaN 33.067527770996094 32.94440460205078
100 99 TYR H NaN 90.79939270019531 73.3204116821289
108 107 THR H NaN 0.0 0.0
2X4W B X-ray 1.5 8 A 0.95072776
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
29 28 SER C NaN 167.15219116210938 35.035179138183594
33 32 THR C NaN 127.27986145019531 86.08187866210938
3MO8 B X-ray 1.690000057220459 2 A 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
33 3 THR C NaN 125.33486938476562 92.44140625
42 12 TYR C NaN 182.91358947753906 85.28993225097656
2X4Y B X-ray 1.7000000476837158 4 A 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
29 28 SER H NaN 93.44473266601562 28.90772819519043
33 32 THR C NaN 127.90654754638672 86.00782012939453
42 41 TYR C NaN 267.3390197753906 0.0
4MZG A X-ray 1.7000000476837158 4 B 0.10949725
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
4 3 THR E NaN 120.83177947998047 34.774051666259766
7 6 THR C NaN 123.40404510498047 0.0
2X4X B X-ray 1.850000023841858 4 A 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
29 28 SER C NaN 165.2826690673828 27.311264038085938
33 32 THR C NaN 133.9820098876953 89.81767272949219
42 41 TYR C NaN 257.4656982421875 5.542591094970703
4OUC B X-ray 1.899999976158142 2 A 0.12874977
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
4 3 THR C NaN 137.91026306152344 104.53034210205078
7 6 THR C NaN 95.42778778076172 15.95195484161377
5VAC C X-ray 1.9500000476837158 2 A 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
29 28 SER E NaN 108.73782348632812 107.61074829101562
33 32 THR C NaN 115.88697814941406 37.17217254638672
4MZF A X-ray 2.0999999046325684 2 B 0.024427354
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
4 3 THR E NaN 125.41170501708984 46.37419891357422
7 6 THR C NaN 136.7035369873047 1.1068308353424072
4MZH B X-ray 2.200000047683716 2 A 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
4 3 THR E NaN 128.51841735839844 44.17836380004883
7 6 THR C NaN 128.7757110595703 5.397639274597168
5CIU C X-ray 2.240000009536743 2 B 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
33 32 THR C NaN 196.22544860839844 52.20101547241211
3DB3 B X-ray 2.4000000953674316 2 A 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
11 10 SER C NaN 156.73678588867188 56.84894943237305
5BO0 A X-ray 2.9100000858306885 8 C 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
59 58 THR C NaN 172.15184020996094 50.29775619506836
81 80 THR C NaN 103.58102416992188 0.0
87 86 SER H NaN 99.70802307128906 44.04189682006836
97 96 SER H NaN 33.926109313964844 0.0
100 99 TYR H NaN 86.29944610595703 0.0
108 107 THR H NaN 0.5045952200889587 0.0

Mutations

Showing 2 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
91 M T Polymorphism
128 A V Polymorphism