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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 9 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
6 SER PRIDE yes
181 SER PRIDE yes
202 THR UP Combined
209 TYR UP, PRIDE Similarity yes
340 SER PRIDE yes
411 TYR UP, PRIDE Experimental yes
442 SER PRIDE yes
462 SER UP, PRIDE Combined yes
522 TYR UP, PRIDE Experimental 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 9 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
6 1 18 6 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
181 178 185 4 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD003531 4 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
209 202 213 8 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD003531 2 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
340 339 346 2 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD002286 7 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 -
411 405 414 7 8
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001060 11 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell -
PXD004252 2 Modulating the selectivity of affinity absorbents to multi-phosphopeptides by a novel competitive substitution strategy Homo sapiens (Human) PARTIAL 2016-08-03 cell culture -
PXD000612 82 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 9 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
PXD001565 9 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain -
PXD005366 13 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 -
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 -
PXD003198 36 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line -
411 405 418 7 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 143 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
PXD003198 7 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line -
442 423 455 20 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD002286 1 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 -
462 456 468 7 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
522 496 526 27 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD003198 1 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line

Structures

Showing 27 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
2C0I A X-ray 2.299999952316284 2 [CA]A:1507 0.32684845 202
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
181 160 SER E 0.98 0.0 0.0
202 181 THR C 1.0 47.451560974121094 0.0
209 188 TYR E 1.0 77.05582427978516 0.0
340 319 SER E 1.0 19.286062240600586 0.0
435 414 THR C 1.0 56.26482391357422 0.0
442 421 SER H 1.0 6.744794845581055 0.0
462 441 SER C 0.92 49.183067321777344 0.0
506 485 TYR H 0.96 86.74480438232422 0.0
2C0O A X-ray 2.8499999046325684 2 [CA]A:1507 0.32074767 202
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
181 160 SER E 0.98 0.0 0.0
202 181 THR C 1.0 42.29662322998047 0.0
209 188 TYR E 1.0 72.16262817382812 0.0
340 319 SER E 1.0 19.73623275756836 0.0
435 414 THR C 1.0 61.5736083984375 0.0
442 421 SER H 1.0 9.034021377563477 0.0
462 441 SER C 0.92 46.101402282714844 0.0
506 485 TYR H 0.96 94.71651458740234 0.0
5H0B A X-ray 1.649999976158142 Monomer [OOQ]A:601 0.1
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
181 186 SER E 0.98 0.5939850807189941 0.0
202 207 THR E 1.0 62.486907958984375 0.0
209 214 TYR E 1.0 43.40842819213867 0.0
340 345 SER E 1.0 12.62536334991455 11.523194313049316
411 416 TYR H 1.0 108.98556518554688 0.0
435 440 THR C 1.0 58.505096435546875 0.0
442 447 SER H 1.0 10.538389205932617 0.0
462 467 SER C 0.92 52.56719970703125 0.0
506 511 TYR H 0.96 88.92511749267578 0.0
5ZJ6 A X-ray 1.7000000476837158 Monomer [VSE]A:601 0.1
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
340 345 SER E 1.0 19.722755432128906 18.485445022583008
411 416 TYR H 1.0 107.2060317993164 0.0
435 440 THR C 1.0 58.95562744140625 0.0
442 447 SER H 1.0 11.089010238647461 0.0
462 467 SER C 0.92 52.42317581176758 0.0
506 511 TYR H 0.96 90.05921936035156 0.0
5H0H A X-ray 1.7200000286102295 Monomer [OOV]A:601 0.1
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
181 186 SER E 0.98 0.72552490234375 0.0
202 207 THR E 1.0 58.79705810546875 0.0
209 214 TYR E 1.0 42.050025939941406 0.0
340 345 SER E 1.0 11.109427452087402 10.62048625946045
411 416 TYR H 1.0 112.74000549316406 0.0
435 440 THR C 1.0 56.74404525756836 0.0
442 447 SER H 1.0 10.661511421203613 0.0
462 467 SER C 0.92 52.4088134765625 0.0
506 511 TYR H 0.96 87.95186614990234 0.0
5H0G A X-ray 1.7999999523162842 Monomer [OOU]A:601 0.1
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
181 186 SER E 0.98 0.35465192794799805 0.0
202 207 THR E 1.0 62.818023681640625 0.0
209 214 TYR E 1.0 43.58915710449219 0.0
340 345 SER E 1.0 18.2937068939209 17.870201110839844
411 416 TYR H 1.0 104.80138397216797 0.0
435 440 THR C 1.0 59.125858306884766 0.0
442 447 SER H 1.0 10.089593887329102 0.0
462 467 SER C 0.92 53.68771743774414 0.0
506 511 TYR H 0.96 85.23086547851562 0.0
4U5W B X-ray 1.8600000143051147 4 A 0.17892434
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
181 185 SER E 0.98 24.806245803833008 0.0
202 206 THR E 1.0 69.54167938232422 0.0
209 213 TYR E 1.0 46.720829010009766 0.0
5H09 A X-ray 1.9500000476837158 Monomer [OOO]A:601 0.1
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
181 186 SER E 0.98 0.11759091168642044 0.0
202 207 THR E 1.0 62.8953971862793 0.0
209 214 TYR E 1.0 39.14099884033203 0.0
340 345 SER E 1.0 14.204061508178711 12.319684028625488
411 416 TYR H 1.0 110.91663360595703 0.0
435 440 THR C 1.0 60.05918884277344 0.0
442 447 SER H 1.0 10.747105598449707 0.0
462 467 SER C 0.92 53.55364990234375 0.0
506 511 TYR H 0.96 89.54717254638672 0.0
1QCF A X-ray 2.0 Monomer [PP1]A:532 0.1
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
181 185 SER E 0.98 0.0 0.0
202 206 THR E 1.0 69.46050262451172 0.0
209 213 TYR E 1.0 20.578153610229492 0.0
340 345 SER E 1.0 16.036909103393555 10.926284790039062
411 416 TYR H 1.0 18.2344913482666 0.0
435 440 THR C 1.0 59.88225173950195 0.0
442 447 SER H 1.0 8.32470703125 0.0
462 467 SER C 0.92 49.64473342895508 0.0
506 511 TYR H 0.96 106.76021575927734 0.0
2HK5 A X-ray 2.0 Monomer [1BM]A:499 0.1
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
340 323 SER E 1.0 20.32988739013672 5.556641101837158
411 394 TYR E 1.0 64.33140563964844 0.0
435 418 THR C 1.0 21.47279167175293 0.0
442 425 SER H 1.0 9.152957916259766 0.0
462 445 SER C 0.92 55.65277099609375 0.0
506 489 TYR H 0.96 92.32355499267578 0.0
5H0E A X-ray 2.0999999046325684 Monomer [OOS]A:601 0.1
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
181 186 SER E 0.98 0.237061008810997 0.0
202 207 THR E 1.0 61.60437774658203 0.0
209 214 TYR E 1.0 38.08830261230469 0.0
340 345 SER E 1.0 15.44067668914795 12.402108192443848
411 416 TYR H 1.0 115.10909271240234 0.0
435 440 THR C 1.0 59.567298889160156 0.0
442 447 SER H 1.0 9.924273490905762 0.0
462 467 SER C 0.92 52.13633728027344 0.0
506 511 TYR H 0.96 87.48873901367188 0.0
2C0T A X-ray 2.1500000953674316 2 [CA]A:1507 0.26658952
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
181 160 SER E 0.98 0.0 0.0
209 188 TYR C 1.0 76.06439971923828 0.0
340 319 SER E 1.0 18.87049102783203 0.0
435 414 THR C 1.0 59.8039436340332 0.0
442 421 SER H 1.0 9.118515968322754 0.0
462 441 SER C 0.92 52.38829803466797 0.0
506 485 TYR H 0.96 95.6434555053711 0.0
3VS3 A X-ray 2.1700000762939453 2 [CL]A:603 0.28251263
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
181 186 SER E 0.98 0.0 0.0
202 207 THR E 1.0 47.786376953125 0.0
209 214 TYR E 1.0 42.591861724853516 0.0
340 345 SER E 1.0 18.298173904418945 0.0
435 440 THR C 1.0 56.390201568603516 0.0
442 447 SER H 1.0 9.054266929626465 0.0
462 467 SER C 0.92 50.03953170776367 0.0
506 511 TYR H 0.96 102.5705337524414 0.0
3VRZ A X-ray 2.2200000286102295 2 [CL]A:602 0.29211414
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
181 186 SER E 0.98 0.0 0.0
202 207 THR C 1.0 96.348876953125 0.0
209 214 TYR E 1.0 70.43609619140625 0.0
340 345 SER E 1.0 17.534635543823242 0.0
435 440 THR C 1.0 65.9053955078125 0.0
442 447 SER H 1.0 7.028440952301025 0.0
462 467 SER C 0.92 39.02677917480469 0.0
506 511 TYR H 0.96 95.35140228271484 0.0
3VS6 A X-ray 2.369999885559082 2 [CL]A:602 0.25007713
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
181 186 SER E 0.98 0.0 0.0
202 207 THR E 1.0 59.51398468017578 0.0
209 214 TYR E 1.0 49.336917877197266 0.0
340 345 SER E 1.0 19.759180068969727 0.0
435 440 THR C 1.0 62.04307556152344 0.0
442 447 SER H 1.0 10.976701736450195 0.0
462 467 SER C 0.92 47.30438232421875 0.0
506 511 TYR H 0.96 102.84990692138672 0.0
3VS1 A X-ray 2.4600000381469727 2 [CL]A:603 0.2855376
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
181 186 SER E 0.98 0.0 0.0
340 345 SER E 1.0 18.213481903076172 0.0
435 440 THR C 1.0 58.49001693725586 0.0
442 447 SER H 1.0 7.82053279876709 0.0
462 467 SER C 0.92 53.37751007080078 0.0
506 511 TYR H 0.96 102.87641906738281 0.0
3VRY A X-ray 2.4800000190734863 2 [CL]A:602 0.37231275
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
181 186 SER E 0.98 0.0 0.0
209 214 TYR E 1.0 86.50528717041016 0.0
340 345 SER E 1.0 17.63654327392578 0.0
435 440 THR C 1.0 57.06332778930664 0.0
442 447 SER H 1.0 8.139681816101074 0.0
462 467 SER C 0.92 46.15565490722656 0.0
506 511 TYR H 0.96 99.15161895751953 0.0
1AD5 A X-ray 2.5999999046325684 2 [CA]B:1 0.031754192
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
181 185 SER E 0.98 0.0 0.0
202 206 THR E 1.0 57.534305572509766 0.0
209 213 TYR E 1.0 61.84366226196289 0.0
340 345 SER E 1.0 13.984455108642578 0.0
435 440 THR C 1.0 58.866817474365234 0.0
442 447 SER H 1.0 7.112670421600342 0.0
462 467 SER C 0.92 75.10362243652344 0.0
506 511 TYR H 0.96 90.77760314941406 0.0
3VS2 A X-ray 2.609999895095825 2 [CL]A:603 0.2797171
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
181 186 SER E 0.98 0.0 0.0
202 207 THR C 1.0 75.97738647460938 0.0
209 214 TYR E 1.0 59.24367141723633 0.0
340 345 SER E 1.0 18.458023071289062 0.0
435 440 THR C 1.0 57.742919921875 0.0
442 447 SER H 1.0 7.851083755493164 0.0
462 467 SER C 0.92 53.202003479003906 0.0
506 511 TYR H 0.96 112.94638061523438 0.0
3NHN A X-ray 2.609999895095825 Monomer A 0.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
181 185 SER E 0.98 15.447672843933105 0.0
202 206 THR E 1.0 72.3629379272461 0.0
209 213 TYR E 1.0 34.801658630371094 0.0
3VS4 A X-ray 2.75 2 [CL]A:602 0.2804466
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
181 186 SER E 0.98 0.0 0.0
209 214 TYR E 1.0 72.90111541748047 0.0
340 345 SER E 1.0 19.068140029907227 0.0
435 440 THR C 1.0 58.47999954223633 0.0
442 447 SER H 1.0 7.975344657897949 0.0
462 467 SER C 0.92 46.7916374206543 0.0
506 511 TYR H 0.96 109.40556335449219 0.0
3VS5 A X-ray 2.8499999046325684 2 [CA]A:602 0.36001182
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
181 186 SER E 0.98 0.0 0.0
202 207 THR C 1.0 118.443603515625 0.0
209 214 TYR E 1.0 64.29297637939453 0.0
340 345 SER E 1.0 19.284133911132812 0.0
435 440 THR C 1.0 61.43170928955078 0.0
442 447 SER H 1.0 7.975346088409424 0.0
462 467 SER C 0.92 44.996368408203125 0.0
506 511 TYR H 0.96 92.34266662597656 0.0
4LUD A X-ray 2.8499999046325684 2 [CL]A:605 0.27232653
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
181 186 SER E 0.98 0.0 0.0
202 207 THR E 1.0 52.60921096801758 0.0
209 214 TYR E 1.0 37.765316009521484 0.0
340 345 SER E 1.0 17.54903793334961 0.0
435 440 THR C 1.0 66.23178100585938 0.0
442 447 SER H 1.0 7.72489595413208 0.0
462 467 SER C 0.92 70.07048797607422 0.0
506 511 TYR H 0.96 104.82254791259766 0.0
3VS0 A X-ray 2.930000066757202 2 [CL]A:603 0.4279896
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
181 186 SER E 0.98 0.0 0.0
209 214 TYR E 1.0 72.17652130126953 0.0
340 345 SER E 1.0 16.32961082458496 0.0
435 440 THR C 1.0 63.86335754394531 0.0
442 447 SER H 1.0 7.723243713378906 0.0
462 467 SER C 0.92 48.804264068603516 0.0
506 511 TYR H 0.96 100.24144744873047 0.0
3VS7 A X-ray 3.0 2 [CL]A:603 0.2923916
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
181 186 SER E 0.98 0.0 0.0
202 207 THR E 1.0 48.81705093383789 0.0
209 214 TYR E 1.0 64.86585998535156 0.0
340 345 SER E 1.0 18.263410568237305 0.0
435 440 THR C 1.0 58.037784576416016 0.0
442 447 SER H 1.0 1.4742568731307983 0.0
462 467 SER C 0.92 50.90135955810547 0.0
506 511 TYR H 0.96 113.33495330810547 0.0
2HCK A X-ray 3.0 Monomer [CA]B:1 0.053375363
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
181 185 SER E 0.98 0.0 0.0
202 206 THR E 1.0 72.14237976074219 0.0
209 213 TYR E 1.0 59.68123245239258 0.0
340 345 SER E 1.0 22.65789222717285 0.0
435 440 THR C 1.0 57.8784294128418 0.0
442 447 SER H 1.0 8.709395408630371 0.0
462 467 SER C 0.92 52.34794235229492 0.0
506 511 TYR H 0.96 97.17315673828125 0.0
4LUE A X-ray 3.0399999618530273 2 [CL]A:603 0.29247823
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
181 186 SER E 0.98 0.0 0.0
202 207 THR C 1.0 106.44405364990234 0.0
209 214 TYR E 1.0 60.84235382080078 0.0
340 345 SER E 1.0 24.229324340820312 0.0
435 440 THR C 1.0 56.022342681884766 0.0
442 447 SER H 1.0 8.576476097106934 0.0
462 467 SER C 0.92 59.65218734741211 0.0
506 511 TYR H 0.96 104.35785675048828 0.0

Mutations

Showing 4 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
44 A T Polymorphism
105 M L Polymorphism
399 D G Unclassified An ovarian mucinous carcinoma sample
502 P Q Polymorphism