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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 PhosphoS PRIDE
28 PhosphoS PRIDE
320 PhosphoT PRIDE yes
801 PhosphoY UP Experimental
996 PhosphoY UP Experimental
1054 PhosphoY UP Experimental
1059 PhosphoY UP Experimental
1281 PhosphoS 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 1.5199999809265137 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 1.5499999523162842 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 1.6399999856948853 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 1.8300000429153442 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 1.899999976158142 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 1.9500000476837158 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 2.0299999713897705 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 2.1500000953674316 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 2.299999952316284 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 2.490000009536743 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 2.809999942779541 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 1.600000023841858 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 1.5700000524520874 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 1.9500000476837158 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 2.0999999046325684 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 2.200000047683716 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 2.200000047683716 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 2.4000000953674316 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 2.4000000953674316 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 2.6500000953674316 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 2.700000047683716 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
3S37 X X-ray 2.700000047683716 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 2.700000047683716 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
3CPB A X-ray 2.700000047683716 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
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 2.9000000953674316 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 2.950000047683716 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 3.0999999046325684 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 3.200000047683716 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 2.049999952316284 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 2.1500000953674316 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]