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Ex.: O00571, ddx3x (keyword), ATP-dependent RNA helicase DDX3X, PXD000680 or 3JRV

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PDB 
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Phospho-sites

Showing 3 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
47 PhosphoS UP, PRIDE Experimental yes
246 PhosphoS PRIDE yes
688 PhosphoS 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 4 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
47 47 66 1 2
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 -
PXD000836 1 HOPE-fixation of lung tissue allows retrospective proteome and phosphoproteome studies Homo sapiens (Human) PARTIAL 2014-05-22 lung
246 238 248 9 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD006482 1 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney
688 681 692 8 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
688 683 692 6 3
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 -
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 -
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 28 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
4NMX B X-ray 1.850000023841858 3 A 1.0 246
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
246 246 SER E 0.57 42.074913024902344 0.0
249 249 SER E 0.89 5.556371688842773 0.0
2QTW B X-ray 1.899999976158142 2 A 0.75261647 246
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
246 246 SER E 0.57 42.03335189819336 0.0
249 249 SER E 0.89 5.005101680755615 0.0
2P4E A X-ray 1.9800000190734863 2 P 0.33228403 246
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
246 246 SER E 0.57 45.647708892822266 0.0
249 249 SER E 0.89 5.693268775939941 0.0
5VLK A X-ray 2.200000047683716 3 [CA]A:501 0.56252146 246
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
246 246 SER E 0.57 42.16658401489258 0.0
249 249 SER E 0.89 6.567890167236328 0.0
2PMW B X-ray 2.299999952316284 2 A 0.48733145 246
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
246 246 SER E 0.57 49.3991584777832 0.0
249 249 SER E 0.89 6.133778095245361 0.0
2W2N A X-ray 2.299999952316284 2 P 0.6709556 246
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
246 246 SER E 0.57 29.81295394897461 0.0
249 249 SER E 0.89 6.706233024597168 0.0
5OCA B X-ray 2.299999952316284 4 A 0.39965874 246
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
246 246 SER C 0.57 31.970834732055664 0.0
249 249 SER E 0.89 4.866611480712891 0.0
3H42 B X-ray 2.299999952316284 4 A 0.6812808 246
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
246 246 SER E 0.57 29.269668579101562 0.0
249 249 SER E 0.89 7.695741653442383 0.0
2W2Q A X-ray 2.3299999237060547 3 P 0.6618686 246
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
246 246 SER C 0.57 27.722579956054688 0.0
249 249 SER E 0.89 5.818288803100586 0.0
5VLL A X-ray 2.369999885559082 3 [CA]A:501 0.57167727 246
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
246 246 SER E 0.57 46.64857482910156 0.0
249 249 SER E 0.89 6.353958606719971 0.0
2W2M A X-ray 2.4000000953674316 2 P 0.6863744 246
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
246 246 SER E 0.57 21.693220138549805 0.0
249 249 SER E 0.89 6.283455848693848 0.0
5VLA A X-ray 2.4000000953674316 2 Z 0.5076171 246
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
246 246 SER E 0.57 41.56758499145508 0.0
249 249 SER E 0.89 5.595810890197754 0.0
3BPS A X-ray 2.4100000858306885 2 P 1.0 246
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
246 246 SER E 0.57 24.88140106201172 0.0
249 249 SER E 0.89 2.2649013996124268 0.0
4NE9 A X-ray 2.5999999046325684 3 P 1.0 246
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
246 246 SER E 0.57 28.259700775146484 0.0
249 249 SER E 0.89 6.2315144538879395 0.0
2W2O A X-ray 2.619999885559082 2 P 1.0 246
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
246 246 SER E 0.57 38.725677490234375 0.0
249 249 SER E 0.89 4.907903671264648 0.0
2W2P A X-ray 2.619999885559082 3 P 1.0 246
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
246 246 SER E 0.57 30.187299728393555 0.0
249 249 SER E 0.89 6.977651119232178 0.0
4OV6 B X-ray 2.690000057220459 3 A 1.0 246
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
246 246 SER E 0.57 40.054840087890625 0.0
249 249 SER E 0.89 6.456851482391357 0.0
3SQO A X-ray 2.700000047683716 2 P 1.0 246
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
246 246 SER E 0.57 36.10083770751953 0.0
249 249 SER E 0.89 4.620554447174072 0.0
3GCX A X-ray 2.700000047683716 2 P 1.0 246
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
246 246 SER E 0.57 23.224790573120117 0.0
249 249 SER E 0.89 2.0638887882232666 0.0
3GCW A X-ray 2.700000047683716 2 P 1.0 246
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
246 246 SER E 0.57 24.460086822509766 0.0
249 249 SER E 0.89 2.6195240020751953 0.0
2XTJ A X-ray 2.700000047683716 4 P 0.67633104 246
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
246 246 SER C 0.57 24.591384887695312 0.0
249 249 SER E 0.89 5.250452041625977 0.0
5VLH A X-ray 2.859999895095825 3 [CA]A:501 0.5507263 246
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
246 246 SER E 0.57 41.7872428894043 0.0
249 249 SER E 0.89 5.616788387298584 0.0
5VLP A X-ray 2.9000000953674316 4 Z 0.37507385 246
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
246 246 SER E 0.57 21.58709716796875 0.0
249 249 SER E 0.89 5.543183326721191 0.0
4K8R B X-ray 3.2200000286102295 6 A 1.0 246
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
246 246 SER E 0.57 30.635427474975586 0.0
249 249 SER E 0.89 7.228617191314697 0.0
3P5B A X-ray 3.299999952316284 2 P 0.668046 246
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
246 246 SER E 0.57 12.126529693603516 0.0
249 249 SER E 0.89 4.927953243255615 0.0
5VL7 B X-ray 3.5 4 A 1.0 246
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
246 246 SER E 0.57 30.946168899536133 0.0
249 249 SER E 0.89 4.340176105499268 0.0
3P5C A X-ray 4.199999809265137 2 P 0.6683522 246
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
246 246 SER E 0.57 12.193822860717773 0.0
249 249 SER E 0.89 4.970694065093994 0.0
3M0C B X-ray 7.010000228881836 2 A 1.0 246
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
246 246 SER E 0.57 42.456871032714844 0.0
249 249 SER E 0.89 4.937664031982422 0.0

Mutations

Showing 38 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
46 R L Polymorphism
53 A V Polymorphism
57 E K Polymorphism
77 T I Polymorphism
93 R C Polymorphism
106 G R Polymorphism
114 V A Polymorphism
127 S R Disease Hypercholesterolemia, autosomal dominant, 3 (HCHOLA3) [MIM:603776]
129 D G Disease Hypercholesterolemia, autosomal dominant, 3 (HCHOLA3) [MIM:603776]
157 N K Polymorphism
174 P S Polymorphism
215 R H Disease Hypercholesterolemia, autosomal dominant, 3 (HCHOLA3) [MIM:603776]
216 F L Disease Hypercholesterolemia, autosomal dominant, 3 (HCHOLA3) [MIM:603776]
218 R S Disease Hypercholesterolemia, autosomal dominant, 3 (HCHOLA3) [MIM:603776]
219 Q E Polymorphism
237 R W Polymorphism
239 A D Polymorphism
253 L F Polymorphism
357 R H Disease Hypercholesterolemia, autosomal dominant, 3 (HCHOLA3) [MIM:603776]
374 D Y Disease Hypercholesterolemia, autosomal dominant, 3 (HCHOLA3) [MIM:603776]
391 H N Polymorphism
394 G S Unclassified
417 H Q Polymorphism
425 N S Polymorphism
443 A T Polymorphism
452 G D Polymorphism
469 R W Polymorphism
474 V I Polymorphism
482 E G Polymorphism
496 R W Disease Hypercholesterolemia, autosomal dominant, 3 (HCHOLA3) [MIM:603776]
515 F L Polymorphism
522 A T Polymorphism
553 H R Polymorphism
554 Q E Polymorphism
616 P L Polymorphism
619 Q P Polymorphism
668 S R Polymorphism
670 G E Polymorphism