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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 15 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
3 PhosphoT UP, PRIDE Experimental yes
14 PhosphoS UP Experimental
75 PhosphoT UP Experimental
97 PhosphoS UP Experimental
173 PhosphoS PRIDE yes
175 PhosphoS PRIDE yes
237 PhosphoT UP Experimental
244 PhosphoT UP Experimental
253 PhosphoT UP Experimental
386 PhosphoS UP Experimental
390 PhosphoT PRIDE yes
396 PhosphoS UP Experimental
398 PhosphoS UP Experimental
404 PhosphoT UP Experimental
427 PhosphoS UP Experimental

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
3 1 7 3 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD005366 1 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
173 173 193 1 3
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD001060 4 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell
PXD000612 4 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 - -
173 173 194 1 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD001060 19 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial 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
175 173 194 3 5
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD001060 49 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 -
PXD002436 1 Monitoring cellular phosphorylation signaling pathways into chromatin and down to the gene level Homo sapiens (Human) COMPLETE 2015-11-09 HeLa cell -
PXD006482 1 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney -
PXD000680 9 Stable isotope labeling of phosphoproteins for large-scale phosphorylation rate determination Homo sapiens (Human) COMPLETE 2014-04-15 HeLa cell,HEK-293 cell
175 173 193 3 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
PXD003531 1 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD002286 40 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 - -
390 381 409 10 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD001060 1 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell

Structures

Showing 15 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
1QWT A X-ray 2.0999999046325684 8 A 0.16044004 237, 244, 253, 386, 390, 396, 398, 404, 427
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
237 237 THR C 0.39 109.31147003173828 0.0
244 244 THR E 0.6 33.74533462524414 0.0
253 253 THR C 0.61 123.93473815917969 0.0
386 386 SER C 0.59 125.12532806396484 0.0
390 390 THR E 0.52 75.12104034423828 0.0
396 396 SER C 0.71 33.46675491333008 0.0
398 398 SER C 0.84 52.399192810058594 0.0
404 404 THR C 0.27 54.20956039428711 0.0
427 427 SER C NaN 163.5680389404297 51.8549919128418
5JEL A X-ray 1.600000023841858 4 A 1.0 237, 244, 253, 386, 390, 396, 398, 404
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
237 237 THR C 0.39 123.62981414794922 0.0
244 244 THR E 0.6 57.6594352722168 0.0
253 253 THR C 0.61 107.54438781738281 99.96561431884766
386 386 SER C 0.59 78.74359893798828 0.0
390 390 THR E 0.52 88.81488037109375 0.0
396 396 SER C 0.71 36.46735763549805 0.0
398 398 SER C 0.84 32.03927993774414 0.0
404 404 THR E 0.27 32.980674743652344 0.0
5JEO A X-ray 1.7200000286102295 4 B 0.43268895 237, 244, 253, 386, 390, 396, 398, 404
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
237 237 THR C 0.39 123.48229217529297 0.0
244 244 THR E 0.6 57.6016731262207 0.0
253 253 THR C 0.61 106.14036560058594 0.0
386 386 SER C 0.59 78.27460479736328 0.0
390 390 THR E 0.52 92.20986938476562 0.0
396 396 SER C 0.71 30.920364379882812 0.0
398 398 SER C 0.84 35.92087936401367 0.0
404 404 THR E 0.27 29.894163131713867 0.0
3A77 A X-ray 1.7999999523162842 Monomer [MPD]A:3002 0.1 237, 244, 253, 390, 396, 398, 404, 427
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
237 237 THR C 0.39 173.86871337890625 0.0
244 244 THR C 0.6 88.80056762695312 0.0
253 253 THR C 0.61 115.3777847290039 0.0
390 390 THR E 0.52 83.96611785888672 0.0
396 396 SER C 0.71 30.07213592529297 0.0
398 398 SER C 0.84 37.37129211425781 0.0
404 404 THR C 0.27 45.5045166015625 0.0
427 427 SER C NaN 157.3260040283203 0.0
5JEJ A X-ray 2.0 5 B 1.0 237, 244, 253, 386, 390, 396, 398, 404
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
237 237 THR C 0.39 117.8369369506836 0.0
244 244 THR E 0.6 63.83920669555664 0.0
253 253 THR C 0.61 117.40066528320312 112.01265716552734
386 386 SER C 0.59 99.8901596069336 0.0
390 390 THR E 0.52 92.05036926269531 0.0
396 396 SER C 0.71 32.591346740722656 0.0
398 398 SER C 0.84 36.450904846191406 0.0
404 404 THR C 0.27 27.866661071777344 0.0
5JEK A X-ray 2.4000000953674316 2 C 1.0 237, 244, 253, 386, 390, 396, 398, 404
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
237 237 THR C 0.39 120.19949340820312 0.0
244 244 THR E 0.6 31.31837272644043 0.0
253 253 THR C 0.61 129.8023223876953 0.0
386 386 SER C 0.59 56.16588592529297 0.0
390 390 THR E 0.52 94.87109375 0.0
396 396 SER C 0.71 35.51920700073242 0.0
398 398 SER C 0.84 33.45265197753906 0.0
404 404 THR E 0.27 33.576904296875 0.0
5JER A X-ray 2.9100000858306885 2 E 1.0 237, 244, 253, 386, 390, 396, 398, 404
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
237 237 THR C 0.39 116.376953125 0.0
244 244 THR E 0.6 60.70707702636719 0.0
253 253 THR C 0.61 102.68429565429688 102.05781555175781
386 386 SER C 0.59 72.64750671386719 0.0
390 390 THR E 0.52 95.4875259399414 0.0
396 396 SER C 0.71 29.01495933532715 0.0
398 398 SER C 0.84 30.731321334838867 0.0
404 404 THR E 0.27 25.375396728515625 0.0
1J2F A X-ray 2.299999952316284 Monomer B 0.0 244, 253, 386, 390, 396, 398, 404
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
244 244 THR E 0.6 75.78480529785156 0.0
253 253 THR C 0.61 127.11735534667969 0.0
386 386 SER C 0.59 99.67725372314453 0.0
390 390 THR E 0.52 89.8392105102539 0.0
396 396 SER C 0.71 28.464906692504883 0.0
398 398 SER C 0.84 41.09059524536133 0.0
404 404 THR E 0.27 25.886205673217773 0.0
5JEM A X-ray 2.5 4 B 1.0 237, 244, 253, 390, 398
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
237 237 THR C 0.39 128.32525634765625 0.0
244 244 THR E 0.6 58.69493865966797 0.0
253 253 THR C 0.61 128.91685485839844 90.03491973876953
390 390 THR C 0.52 109.95032501220703 0.0
398 398 SER C 0.84 160.61351013183594 13.420194625854492
1ZOQ A X-ray 2.369999885559082 2 C 1.0 237, 244, 253, 386
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
237 237 THR C 0.39 125.91642761230469 0.0
244 244 THR E 0.6 50.363243103027344 0.0
253 253 THR C 0.61 123.12711334228516 0.0
386 386 SER C 0.59 115.6114501953125 0.0
1T2K A X-ray 3.0 6 F 1.0 3, 14, 75, 97
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
3 3 THR C 0.76 182.79583740234375 0.0
14 14 SER H 0.61 44.6392707824707 0.0
75 75 THR H 0.76 43.42747497558594 5.189037799835205
97 97 SER C 0.89 25.245559692382812 0.0
2O6G E X-ray 3.0999999046325684 6 C 1.0 3, 14, 75, 97
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
3 3 THR C 0.76 181.8397216796875 0.0
14 14 SER H 0.61 47.50922393798828 0.0
75 75 THR H 0.76 67.88019561767578 6.160531997680664
97 97 SER C 0.89 26.38482666015625 0.0
3QU6 A X-ray 2.299999952316284 6 [ZN]A:116 0.26311255 14, 75, 97
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 14 SER H 0.61 46.99496078491211 0.0
75 75 THR H 0.76 37.1030158996582 0.0
97 97 SER C 0.89 4.23597526550293 0.0
2PI0 A X-ray 2.309999942779541 6 F 0.1 14, 75, 97
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 14 SER H 0.61 51.342533111572266 0.0
75 75 THR H 0.76 48.00057601928711 4.501306533813477
97 97 SER C 0.89 30.559825897216797 0.0
2O61 A X-ray 2.799999952316284 4 E 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 2014 SER H 0.61 47.993099212646484 0.0
75 2075 THR H 0.76 48.24468231201172 0.0
97 2097 SER C 0.89 24.469812393188477 2.6159961223602295

Mutations

Showing 5 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
96 R Q Polymorphism
107 Y F Polymorphism
285 R Q Disease Encephalopathy, acute, infection-induced, Herpes-specific, 7 (IIAE7) [MIM:616532]
377 E K Polymorphism
427 S T Polymorphism