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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 8 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
26 SER PRIDE
28 SER PRIDE
320 THR PRIDE yes
801 TYR UP Experimental
996 TYR UP Experimental
1054 TYR UP Experimental
1059 TYR UP Experimental
1281 SER PRIDE 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
26 19 33 8 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD002436 1 Monitoring cellular phosphorylation signaling pathways into chromatin and down to the gene level Homo sapiens (Human) COMPLETE 2015-11-09 HeLa cell
28 19 33 10 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD002436 1 Monitoring cellular phosphorylation signaling pathways into chromatin and down to the gene level Homo sapiens (Human) COMPLETE 2015-11-09 HeLa cell
320 317 327 4 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
1281 1278 1289 4 2
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
PXD002286 1 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 - -

Structures

Showing 36 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
4AGC A X-ray 2.0 Monomer [AXI]A:2000 0.1 801, 996, 1054, 1059
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
801 801 TYR C 1.0 85.9080581665039 0.0
996 996 TYR C 0.65 191.41529846191406 0.0
1054 1054 TYR C 1.0 136.53318786621094 0.0
1059 1059 TYR C 1.0 8.3777494430542 0.0
2XIR A X-ray 1.5 Monomer A 0.0 996, 1054, 1059
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
996 996 TYR C 0.65 198.54342651367188 0.0
1054 1054 TYR C 1.0 98.93601989746094 0.0
1059 1059 TYR C 1.0 21.805679321289062 0.0
3VO3 A X-ray 1.52 Monomer [0KF]A:2001 0.1419568 996, 1054, 1059
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
996 996 TYR C 0.65 94.16363525390625 0.0
1054 1054 TYR C 1.0 130.79296875 0.0
1059 1059 TYR C 1.0 9.05850887298584 0.0
3VHE A X-ray 1.55 Monomer A 0.0 996, 1054, 1059
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
996 996 TYR C 0.65 104.21794891357422 0.0
1054 1054 TYR C 1.0 136.22373962402344 0.0
1059 1059 TYR C 1.0 8.65542984008789 0.0
3VNT A X-ray 1.64 Monomer [0JA]A:2001 0.15952522 996, 1054, 1059
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
996 996 TYR C 0.65 167.4865264892578 0.0
1054 1054 TYR C 1.0 160.65830993652344 0.0
1059 1059 TYR C 1.0 17.680971145629883 0.0
4ASE A X-ray 1.83 Monomer [AV9]A:3169 0.1 996, 1054, 1059
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
996 996 TYR C 0.65 197.23619079589844 0.0
1054 1054 TYR C 1.0 129.26673889160156 0.0
1059 1059 TYR C 1.0 15.351308822631836 0.0
3WZE A X-ray 1.9 Monomer [BAX]A:1201 0.065451644 996, 1054, 1059
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
996 996 TYR C 0.65 106.50768280029297 0.0
1054 1054 TYR C 1.0 162.3685302734375 0.0
1059 1059 TYR C 1.0 19.87030601501465 0.0
4AG8 A X-ray 1.95 Monomer [AXI]A:2000 0.1 996, 1054, 1059
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
996 996 TYR C 0.65 193.4281463623047 0.0
1054 1054 TYR C 1.0 157.1929931640625 0.0
1059 1059 TYR C 1.0 19.64693260192871 0.0
4ASD A X-ray 2.03 Monomer [BAX]A:1500 0.1 996, 1054, 1059
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
996 996 TYR C 0.65 192.80496215820312 0.0
1054 1054 TYR C 1.0 147.2598114013672 0.0
1059 1059 TYR C 1.0 18.680761337280273 0.0
3U6J A X-ray 2.15 Monomer [03X]A:1 0.1 996, 1054, 1059
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
996 996 TYR H 0.65 50.62815475463867 0.0
1054 1054 TYR C 1.0 123.11153411865234 0.0
1059 1059 TYR C 1.0 16.939348220825195 0.0
3VID A X-ray 2.3 Monomer [4TT]A:2001 0.1 996, 1054, 1059
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
996 996 TYR C 0.65 58.23638916015625 0.0
1054 1054 TYR C 1.0 244.55332946777344 0.0
1059 1059 TYR H 1.0 166.7617645263672 0.0
3VHK A X-ray 2.49 Monomer A 0.0 996, 1054, 1059
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
996 996 TYR C 0.65 162.23406982421875 0.0
1054 1054 TYR C 1.0 117.89376068115234 0.0
1059 1059 TYR C 1.0 15.786994934082031 0.0
4AGD A X-ray 2.81 Monomer A 0.0 996, 1054, 1059
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
996 996 TYR C 0.65 209.98751831054688 0.0
1054 1054 TYR C 1.0 130.7654266357422 0.0
1059 1059 TYR C 1.0 11.739362716674805 0.0
3EWH A X-ray 1.6 Monomer [K11]A:1 0.13092645 996, 1059
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
996 996 TYR H 0.65 49.15550994873047 0.0
1059 1059 TYR C 1.0 28.356386184692383 0.0
3WZD A X-ray 1.57 Monomer [SO4]A:1211 0.035172865 996
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
996 996 TYR H 0.65 49.982391357421875 0.0
3BE2 A X-ray 1.75 Monomer A 0.0 996
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
996 996 TYR H 0.65 54.49136734008789 39.50505065917969
2P2H A X-ray 1.95 2 [994]A:501 0.1 996
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
996 996 TYR H 0.65 49.81829071044922 0.0
2QU6 A X-ray 2.1 Monomer [857]A:501 0.1 996
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
996 996 TYR H 0.65 30.406408309936523 0.0
3S35 X X-ray 2.2 3 [CA]X:1 0.109456696 320
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
291 291 THR E 0.8 18.68616485595703 0.0
320 320 THR E 0.79 6.059531211853027 0.0
3EFL A X-ray 2.2 Monomer A 0.0 996
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
996 996 TYR H 0.65 30.78363800048828 0.0
2P2I A X-ray 2.4 Monomer A 0.0 996
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
996 996 TYR H 0.65 38.876224517822266 0.0
3CPC A X-ray 2.4 Monomer A 0.0 996
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
996 996 TYR H 0.65 29.084739685058594 21.601802825927734
3CP9 A X-ray 2.5 Monomer [C19]A:501 0.1 996
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
996 996 TYR H 0.65 34.42256546020508 0.0
2RL5 A X-ray 2.65 Monomer [2RL]A:501 0.1 996
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
996 996 TYR H 0.65 52.5991096496582 0.0
2X1W L X-ray 2.7 8 C 0.2165697 320
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
291 291 THR E 0.8 22.238536834716797 0.0
320 320 THR E 0.79 8.758522033691406 0.0
3CPB A X-ray 2.7 Monomer [C92]A:1 0.1 996
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
996 996 TYR H 0.65 32.27475357055664 0.0
3S37 X X-ray 2.7 3 H 0.26573008 320
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
291 291 THR E 0.8 18.33450698852539 0.0
320 320 THR E 0.79 6.927603721618652 0.0
3B8R A X-ray 2.7 Monomer [887]A:201 0.18246251 996
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
996 996 TYR H 0.65 37.572776794433594 0.0
3B8Q A X-ray 2.75 Monomer [900]A:501 0.1 996
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
996 996 TYR H 0.65 29.012767791748047 0.0
3DTW A X-ray 2.9 Monomer [A96]A:501 0.1 996
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
996 996 TYR C 0.65 43.4158821105957 0.0
2QU5 A X-ray 2.95 Monomer [276]A:501 0.1 996
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
996 996 TYR C 0.65 35.52878952026367 0.0
2X1X R X-ray 3.1 4 E 1.0 320
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
291 291 THR E 0.8 28.266178131103516 0.0
320 320 THR E 0.79 9.132425308227539 0.0
3S36 X X-ray 3.2 3 H 1.0 320
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
291 291 THR E 0.8 20.061832427978516 0.0
320 320 THR E 0.79 14.576103210449219 0.0
2OH4 A X-ray 2.05 Monomer [SO4]A:301 0.051153976
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
996 994 TYR C 0.65 182.4619140625 0.0
3CJF A X-ray 2.15 Monomer [SO4]A:1 0.040565725
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1054 1052 TYR E 1.0 12.36684799194336 0.0
3CJG A X-ray 2.25 Monomer [SO4]A:1 0.05759912
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
996 994 TYR C 0.65 131.46505737304688 0.0

Mutations

Showing 16 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
2 Q R Unclassified A lung adenocarcinoma sample
136 V M Polymorphism
248 A G Unclassified A renal clear cell carcinoma sample
275 R L Unclassified A colorectal cancer sample
297 V I Polymorphism
462 L V Polymorphism
472 Q H Polymorphism
482 C R Disease Hemangioma, capillary infantile (HCI) [MIM:602089]
539 G R Polymorphism
689 T M Polymorphism
814 D N Polymorphism
848 V E Polymorphism
873 G R Unclassified A colorectal cancer sample
952 V I Polymorphism
1065 A T Polymorphism
1147 P S Disease Hemangioma, capillary infantile (HCI) [MIM:602089]