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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 5 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
389 PhosphoS UP Combined
398 PhosphoT PRIDE
399 PhosphoT PRIDE
536 PhosphoY PRIDE yes
545 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 6 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
398 395 401 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
399 395 401 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
536 531 549 6 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
536 535 549 2 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
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
545 535 554 11 4
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD000612 11 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
PXD006482 2 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney -
PXD004452 5 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
545 535 549 11 9
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 -
PXD000612 5 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD000474 1 Simulated phosphopeptide spectral library for confident site localization Homo sapiens (Human) PARTIAL 2015-03-17 HeLa cell
PXD003531 32 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD006482 5 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney -
PXD005366 54 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 -
PXD004452 8 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
PXD001550 3 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
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 -

Structures

Showing 7 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
4MFU A X-ray 2.740000009536743 Monomer A 0.0 389, 398, 399, 536, 545
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
389 389 SER C 1.0 27.599712371826172 0.0
398 398 THR C 0.9 8.755311012268066 0.0
399 399 THR C 0.9 31.796186447143555 0.0
536 536 TYR H 1.0 38.08466720581055 0.0
545 545 SER C 0.94 28.9635066986084 0.0
4HNM A X-ray 2.9000000953674316 Monomer A 0.0 389, 398, 399, 536, 545
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
389 389 SER C 1.0 24.71591567993164 5.2826619148254395
398 398 THR C 0.9 40.13818359375 0.0
399 399 THR C 0.9 55.821048736572266 0.0
536 536 TYR H 1.0 31.034055709838867 0.0
545 545 SER C 0.94 55.279075622558594 0.0
4CB8 A X-ray 2.9000000953674316 Monomer [SO4]A:1565 0.05167622 389, 398, 399, 536, 545
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
389 389 SER C 1.0 21.75531578063965 0.0
398 398 THR C 0.9 20.846097946166992 0.0
399 399 THR C 0.9 49.861637115478516 0.0
536 536 TYR H 1.0 36.4679069519043 0.0
545 545 SER - 0.94 43.79966354370117 0.0
4MFV A X-ray 2.9200000762939453 Monomer B 0.0 389, 398, 399, 536, 545
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
389 389 SER C 1.0 28.14179229736328 0.0
398 398 THR C 0.9 19.4907169342041 0.0
399 399 THR C 0.9 19.853452682495117 0.0
536 536 TYR H 1.0 39.544044494628906 0.0
545 545 SER C 0.94 47.76872634887695 0.0
4CB9 A X-ray 3.0 Monomer A 0.0 389, 398, 399, 536, 545
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
389 389 SER C 1.0 12.80654239654541 0.0
398 398 THR C 0.9 39.51215362548828 0.0
399 399 THR C 0.9 62.0643310546875 0.0
536 536 TYR H 1.0 34.903907775878906 0.0
545 545 SER - 0.94 35.64385986328125 0.0
4CBA A X-ray 3.0999999046325684 4 [SO4]A:1564 0.290273 389, 398, 399, 536, 545
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
389 389 SER C 1.0 21.3242244720459 0.0
398 398 THR C 0.9 103.92908477783203 0.0
399 399 THR C 0.9 76.56370544433594 0.0
536 536 TYR H 1.0 37.10079574584961 0.0
545 545 SER C 0.94 49.24078369140625 0.0
4HM9 A X-ray 3.0999999046325684 Monomer A 0.0 389, 398, 399, 536, 545
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
389 389 SER C 1.0 14.740560531616211 0.0
398 398 THR C 0.9 39.9895133972168 0.0
399 399 THR C 0.9 62.56887435913086 0.0
536 536 TYR H 1.0 41.20869064331055 0.0
545 545 SER C 0.94 45.21088409423828 0.0

Mutations

Showing 1 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
507 N D Polymorphism