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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 4 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
122 PhosphoS PRIDE yes
124 PhosphoS UP, PRIDE Combined yes
132 PhosphoS PRIDE yes
257 PhosphoS UP 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 3 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
122 119 126 4 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
124 119 126 6 6
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD000612 22 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 3 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
PXD002286 9 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 - -
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
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 -
132 127 133 6 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD005366 3 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

Structures

Showing 8 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
5IYC C EM 3.9000000953674316 Monomer K 0.0 122, 124, 132, 257
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
122 122 SER E 1.0 19.807567596435547 0.0
124 124 SER C 0.37 21.605310440063477 0.0
132 132 SER C 1.0 18.813989639282227 0.0
257 257 SER H 1.0 59.61933898925781 12.697434425354004
5IYD C EM 3.9000000953674316 Monomer K 0.0 122, 124, 132, 257
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
122 122 SER E 1.0 31.562820434570312 0.0
124 124 SER C 0.37 23.99593734741211 0.0
132 132 SER C 1.0 7.669917583465576 0.0
257 257 SER H 1.0 66.3626708984375 19.41942596435547
5IYB C EM 3.9000000953674316 Monomer K 0.0 122, 124, 132, 257
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
122 122 SER E 1.0 25.794240951538086 0.0
124 124 SER C 0.37 27.882844924926758 0.0
132 132 SER C 1.0 10.543556213378906 0.0
257 257 SER H 1.0 55.871490478515625 15.67216968536377
5IYA C EM 5.400000095367432 Monomer K 0.0 122, 124, 132, 257
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
122 122 SER E 1.0 19.612960815429688 0.0
124 124 SER C 0.37 12.889853477478027 0.0
132 132 SER C 1.0 9.816073417663574 0.0
257 257 SER H 1.0 66.590087890625 16.611122131347656
5IY9 C EM 6.300000190734863 Monomer K 0.0 122, 124, 132, 257
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
122 122 SER E 1.0 31.36092185974121 0.0
124 124 SER C 0.37 24.372783660888672 0.0
132 132 SER C 1.0 7.569331645965576 0.0
257 257 SER H 1.0 66.344970703125 19.74307632446289
5IY6 C EM 7.199999809265137 Monomer K 0.0 122, 124, 132, 257
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
122 122 SER E 1.0 19.681045532226562 0.0
124 124 SER C 0.37 12.766213417053223 0.0
132 132 SER C 1.0 10.062915802001953 0.0
257 257 SER H 1.0 66.250244140625 16.153797149658203
5IY8 C EM 7.900000095367432 Monomer K 0.0 122, 124, 132, 257
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
122 122 SER E 1.0 19.122129440307617 0.0
124 124 SER C 0.37 21.852516174316406 0.0
132 132 SER C 1.0 19.085756301879883 0.0
257 257 SER H 1.0 59.5915641784668 12.999863624572754
5IY7 C EM 8.600000381469727 Monomer K 0.0 122, 124, 132, 257
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
122 122 SER E 1.0 26.452585220336914 0.0
124 124 SER C 0.37 26.768978118896484 0.0
132 132 SER C 1.0 10.159965515136719 0.0
257 257 SER H 1.0 56.7692756652832 16.165401458740234

Mutations

Showing 0 results

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