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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 13 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
36 SER PRIDE yes
62 TYR UP, PRIDE Combined yes
63 TYR PRIDE yes
66 TYR UP, PRIDE Similarity yes
142 SER PRIDE yes
234 SER PRIDE yes
279 TYR PRIDE yes
304 TYR PRIDE yes
546 TYR UP, PRIDE Similarity yes
562 SER PRIDE
568 THR PRIDE
570 THR PRIDE
584 TYR 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 17 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
36 36 46 1 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 12 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
62 56 70 7 6
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 32 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD001565 24 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain -
PXD003531 3 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD006482 1 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney -
PXD004452 3 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
PXD003198 143 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line -
63 56 70 8 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
PXD003198 12 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line -
66 56 70 11 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001565 1 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain -
PXD003198 8 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line
142 139 152 4 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
234 232 242 3 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
279 279 289 1 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001060 13 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell
304 290 317 15 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
546 541 550 6 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
546 542 550 5 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001060 5 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell
546 543 550 4 4
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 -
PXD000612 20 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 6 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line
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 -
562 551 582 12 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 20 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
562 551 577 12 4
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
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 37 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 2 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 -
PXD004452 2 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
568 551 577 18 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 28 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 2 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 - -
570 551 577 20 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 25 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
584 578 594 7 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 3 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 1 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line -
584 583 594 2 8
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001060 99 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell
PXD000612 68 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD001546 2 Reproducibility of label-free single-shot phosphoproteomics applied to CRC cell lines Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
PXD001565 13 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain -
PXD002286 16 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 - -
PXD004452 2 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
PXD001550 2 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
PXD003198 4 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line -

Structures

Showing 43 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
5EHP A X-ray 1.850000023841858 Monomer [PO4]A:605 0.02795989 36, 62, 63, 66, 142, 234, 279, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
36 36 SER C 1.0 114.48564910888672 20.532066345214844
62 62 TYR C 1.0 23.91357421875 0.0
63 63 TYR E 1.0 3.847632646560669 0.0
66 66 TYR C 1.0 114.82814025878906 0.0
142 142 SER C 1.0 124.59574127197266 0.0
234 234 SER H 0.92 47.07889175415039 0.0
279 279 TYR C 0.87 28.84457015991211 0.0
304 304 TYR C 1.0 1.5976927280426025 0.0
2SHP A X-ray 2.0 Monomer B 0.0 36, 62, 63, 66, 142, 234, 279, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
36 36 SER C 1.0 89.69082641601562 0.0
62 62 TYR C 1.0 28.285215377807617 0.0
63 63 TYR E 1.0 16.8708553314209 0.0
66 66 TYR C 1.0 165.75833129882812 0.0
142 142 SER C 1.0 78.3212661743164 0.0
234 234 SER H 0.92 70.52359008789062 0.0
279 279 TYR C 0.87 12.897171020507812 0.0
304 304 TYR E 1.0 2.9251482486724854 0.0
4OHI A X-ray 2.200000047683716 Monomer A 0.0 36, 62, 63, 66, 142, 234, 279, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
36 36 SER C 1.0 92.42782592773438 0.0
62 62 TYR C 1.0 18.403390884399414 0.0
63 63 TYR E 1.0 4.7243170738220215 0.0
66 66 TYR C 1.0 142.00721740722656 0.0
142 142 SER C 1.0 92.32679748535156 0.0
234 234 SER H 0.92 60.16166687011719 0.0
279 279 TYR C 0.87 28.23554039001465 0.0
304 304 TYR E 1.0 2.1132938861846924 0.0
4H1O A X-ray 2.200000047683716 Monomer A 0.0 36, 62, 63, 66, 142, 234, 279, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
36 36 SER C 1.0 87.42813873291016 0.0
62 62 TYR C 1.0 11.138160705566406 0.0
63 63 TYR E 1.0 5.040760517120361 0.0
66 66 TYR C 1.0 97.66957092285156 0.0
142 142 SER C 1.0 92.80399322509766 0.0
234 234 SER H 0.92 41.819480895996094 0.0
279 279 TYR C 0.87 28.516130447387695 0.0
304 304 TYR C 1.0 2.6478803157806396 0.0
4DGP A X-ray 2.299999952316284 Monomer A 0.0 36, 62, 63, 66, 142, 234, 279, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
36 36 SER C 1.0 82.44409942626953 67.8109359741211
62 62 TYR C 1.0 11.10738468170166 0.0
63 63 TYR E 1.0 4.869704246520996 0.0
66 66 TYR C 1.0 110.6034927368164 85.49683380126953
142 142 SER C 1.0 103.79914855957031 0.0
234 234 SER H 0.92 68.72100830078125 0.0
279 279 TYR C 0.87 27.634578704833984 0.0
304 304 TYR E 1.0 1.8443195819854736 0.0
4OHL A X-ray 2.4000000953674316 Monomer B 0.0 36, 62, 63, 66, 142, 234, 279, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
36 36 SER C 1.0 85.4941177368164 0.0
62 62 TYR C 1.0 14.871649742126465 0.0
63 63 TYR E 1.0 3.8905749320983887 0.0
66 66 TYR C 1.0 155.5463104248047 0.0
142 142 SER C 1.0 90.71827697753906 0.0
234 234 SER C 0.92 64.61639404296875 0.0
279 279 TYR C 0.87 31.54264259338379 0.0
304 304 TYR E 1.0 2.749314069747925 0.0
4OHE A X-ray 2.509999990463257 Monomer A 0.0 36, 62, 63, 66, 142, 234, 279, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
36 36 SER C 1.0 106.33023834228516 0.0
62 62 TYR C 1.0 23.430444717407227 0.0
63 63 TYR E 1.0 5.497074127197266 0.0
66 66 TYR C 1.0 117.41385650634766 0.0
142 142 SER C 1.0 83.64144897460938 0.0
234 234 SER H 0.92 69.83265686035156 0.0
279 279 TYR C 0.87 41.296913146972656 0.0
304 304 TYR C 1.0 2.378877878189087 0.0
4H34 A X-ray 2.700000047683716 Monomer A 0.0 36, 62, 63, 66, 142, 234, 279, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
36 36 SER C 1.0 96.18827056884766 0.0
62 62 TYR C 1.0 22.270055770874023 0.0
63 63 TYR E 1.0 2.8822414875030518 0.0
66 66 TYR C 1.0 150.46710205078125 0.0
142 142 SER C 1.0 90.1569595336914 0.0
234 234 SER H 0.92 59.77573013305664 5.620026111602783
279 279 TYR C 0.87 25.884944915771484 0.0
304 304 TYR C 1.0 0.9913637638092041 0.0
4OHH A X-ray 2.700000047683716 Monomer A 0.0 36, 62, 63, 66, 142, 234, 279, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
36 36 SER C 1.0 99.61695861816406 80.33503723144531
62 62 TYR C 1.0 13.724201202392578 0.0
63 63 TYR E 1.0 3.5280096530914307 0.0
66 66 TYR C 1.0 120.73428344726562 86.86573028564453
142 142 SER C 1.0 71.44607543945312 0.237061008810997
234 234 SER C 0.92 98.5738754272461 0.0
279 279 TYR C 0.87 26.855772018432617 0.0
304 304 TYR E 1.0 3.4294776916503906 0.0
4OHD A X-ray 2.700000047683716 Monomer A 0.0 36, 62, 63, 66, 142, 234, 279, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
36 36 SER C 1.0 111.30923461914062 0.0
62 62 TYR C 1.0 43.03504180908203 0.0
63 63 TYR E 1.0 2.76483154296875 0.0
66 66 TYR C 1.0 108.4584732055664 0.0
142 142 SER C 1.0 93.39744567871094 0.0
234 234 SER H 0.92 53.479087829589844 0.0
279 279 TYR C 0.87 30.779399871826172 0.0
304 304 TYR E 1.0 1.349122166633606 0.0
5XZR A X-ray 2.799999952316284 Monomer A 0.0 36, 62, 63, 66, 142, 234, 279, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
36 36 SER C 1.0 102.25582122802734 0.0
62 62 TYR C 1.0 30.20897674560547 0.0
63 63 TYR E 1.0 7.112785816192627 0.0
66 66 TYR C 1.0 98.12069702148438 0.0
142 142 SER C 1.0 88.86981201171875 0.0
234 234 SER C 0.92 51.226627349853516 0.0
279 279 TYR C 0.87 25.417306900024414 0.0
304 304 TYR C 1.0 2.372929096221924 0.0
5EHR A X-ray 1.7000000476837158 Monomer [PO4]A:603 0.032779 36, 62, 63, 66, 234, 279, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
36 36 SER C 1.0 116.51252746582031 20.43227195739746
62 62 TYR C 1.0 28.968555450439453 0.0
63 63 TYR E 1.0 3.6861348152160645 0.0
66 66 TYR C 1.0 166.8818817138672 0.0
234 234 SER H 0.92 45.4785041809082 0.0
279 279 TYR C 0.87 27.933246612548828 0.0
304 304 TYR C 1.0 1.7238833904266357 0.0
5I6V A X-ray 1.8700000047683716 Monomer B 0.0 62, 63, 66, 142, 234, 279, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
62 62 TYR C 1.0 31.271469116210938 0.0
63 63 TYR E 1.0 4.020841598510742 0.0
66 66 TYR C 1.0 53.810604095458984 0.0
142 142 SER C 1.0 83.75789642333984 0.0
234 234 SER H 0.92 59.48858642578125 0.0
279 279 TYR C 0.87 31.4266300201416 0.0
304 304 TYR E 1.0 1.1115942001342773 0.0
6BMV A X-ray 2.049999952316284 Monomer [PO4]A:602 0.05744462 36, 62, 63, 66, 234, 279, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
36 36 SER C 1.0 113.46700286865234 17.572647094726562
62 62 TYR C 1.0 40.05179214477539 0.0
63 63 TYR E 1.0 4.103938102722168 0.0
66 66 TYR C 1.0 166.5302276611328 0.0
234 234 SER H 0.92 45.41001892089844 0.0
279 279 TYR C 0.87 47.68401336669922 0.0
304 304 TYR C 1.0 1.869747519493103 0.0
4NWF A X-ray 2.0999999046325684 Monomer B 0.0 62, 63, 66, 142, 234, 279, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
62 62 TYR C 1.0 24.363800048828125 0.0
63 63 TYR E 1.0 4.458512306213379 0.0
66 66 TYR C 1.0 181.58294677734375 0.0
142 142 SER C 1.0 91.26202392578125 0.0
234 234 SER C 0.92 104.89946746826172 0.0
279 279 TYR C 0.87 30.854143142700195 0.0
304 304 TYR C 1.0 1.5658955574035645 0.0
6BMR A X-ray 2.2100000381469727 Monomer [PO4]A:602 0.023466246 36, 62, 63, 66, 234, 279, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
36 36 SER C 1.0 113.60325622558594 16.458662033081055
62 62 TYR C 1.0 34.618980407714844 0.0
63 63 TYR E 1.0 4.82705020904541 0.0
66 66 TYR C 1.0 144.9517059326172 0.0
234 234 SER C 0.92 38.386146545410156 0.0
279 279 TYR C 0.87 26.74224090576172 0.0
304 304 TYR C 1.0 1.2546931505203247 0.0
4DGX A X-ray 2.299999952316284 Monomer A 0.0 36, 62, 63, 66, 142, 234, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
36 36 SER C 1.0 98.60021209716797 0.0
62 62 TYR C 1.0 27.996116638183594 0.0
63 63 TYR E 1.0 5.230280876159668 0.0
66 66 TYR C 1.0 127.84738159179688 0.0
142 142 SER C 1.0 82.19647216796875 0.0
234 234 SER C 0.92 64.3885498046875 0.0
304 304 TYR E 1.0 1.040484070777893 0.0
5IBS A X-ray 2.319999933242798 Monomer B 0.0 62, 63, 66, 142, 234, 279, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
62 62 TYR C 1.0 22.569766998291016 0.0
63 63 TYR E 1.0 4.262855529785156 0.0
66 66 TYR C 1.0 100.39791870117188 0.0
142 142 SER C 1.0 93.79964447021484 0.0
234 234 SER C 0.92 62.84318161010742 0.0
279 279 TYR C 0.87 28.426143646240234 0.0
304 304 TYR E 1.0 0.9851807951927185 0.0
6BMX A X-ray 2.4200000762939453 Monomer [DYV]A:601 0.044879954 36, 62, 63, 66, 234, 279, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
36 36 SER C 1.0 114.20904541015625 0.0
62 62 TYR C 1.0 33.089988708496094 0.0
63 63 TYR E 1.0 4.242525577545166 0.0
66 66 TYR C 1.0 150.00953674316406 0.0
234 234 SER C 0.92 45.32628631591797 0.0
279 279 TYR C 0.87 26.466548919677734 0.0
304 304 TYR C 1.0 2.0773332118988037 0.0
4NWG A X-ray 2.450000047683716 Monomer B 0.0 62, 63, 66, 142, 234, 279, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
62 62 TYR C 1.0 29.72650146484375 0.0
63 63 TYR E 1.0 3.206381320953369 0.0
66 66 TYR C 1.0 153.60464477539062 0.0
142 142 SER C 1.0 77.45140838623047 0.0
234 234 SER C 0.92 110.11915588378906 0.0
279 279 TYR C 0.87 32.47315979003906 0.0
304 304 TYR C 1.0 2.3604626655578613 0.0
6BMY A X-ray 2.0899999141693115 Monomer [5OD]A:601 0.041388333 62, 63, 66, 234, 279, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
62 62 TYR C 1.0 27.679601669311523 0.0
63 63 TYR E 1.0 3.979827642440796 0.0
66 66 TYR C 1.0 164.82989501953125 0.0
234 234 SER H 0.92 44.6093635559082 0.0
279 279 TYR C 0.87 27.50262451171875 0.0
304 304 TYR E 1.0 1.477365493774414 0.0
4GWF A X-ray 2.0999999046325684 Monomer B 0.0 62, 63, 66, 142, 234, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
62 62 TYR C 1.0 35.59061813354492 0.0
63 63 TYR E 1.0 5.223153114318848 0.0
66 66 TYR C 1.0 161.3507537841797 0.0
142 142 SER C 1.0 93.83812713623047 0.0
234 234 SER H 0.92 48.385189056396484 0.0
304 304 TYR C 1.0 1.6433789730072021 0.0
6BMW A X-ray 2.0999999046325684 Monomer [5OD]A:601 0.032921627 62, 63, 66, 234, 279, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
62 62 TYR C 1.0 27.30376625061035 0.0
63 63 TYR E 1.0 3.7413389682769775 0.0
66 66 TYR C 1.0 165.9387664794922 0.0
234 234 SER H 0.92 43.340179443359375 0.0
279 279 TYR C 0.87 26.625295639038086 0.0
304 304 TYR C 1.0 0.7388824820518494 0.0
6BMU A X-ray 2.119999885559082 Monomer [5OD]A:601 0.046897795 62, 63, 66, 234, 279, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
62 62 TYR C 1.0 26.048725128173828 0.0
63 63 TYR E 1.0 3.787463903427124 0.0
66 66 TYR C 1.0 160.54714965820312 0.0
234 234 SER H 0.92 42.469024658203125 0.0
279 279 TYR C 0.87 27.31941032409668 0.0
304 304 TYR C 1.0 1.6033135652542114 0.0
5IBM A X-ray 2.180000066757202 Monomer B 0.0 62, 63, 66, 234, 279, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
62 62 TYR C 1.0 21.81542205810547 0.0
63 63 TYR E 1.0 4.986799240112305 0.0
66 66 TYR C 1.0 97.8132095336914 0.0
234 234 SER C 0.92 61.8527717590332 0.0
279 279 TYR C 0.87 32.44293975830078 0.0
304 304 TYR E 1.0 1.8587905168533325 0.0
6BN5 A X-ray 2.2200000286102295 Monomer [DZJ]A:601 0.1 62, 63, 66, 234, 279, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
62 62 TYR C 1.0 30.780012130737305 0.0
63 63 TYR E 1.0 4.917276859283447 0.0
66 66 TYR C 1.0 173.7697296142578 0.0
234 234 SER C 0.92 79.0410385131836 0.0
279 279 TYR C 0.87 32.05016326904297 0.0
304 304 TYR E 1.0 1.810514211654663 0.0
5DF6 A X-ray 1.7799999713897705 3 C 0.35245043 36, 62, 63, 66, 142
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
36 36 SER C 1.0 100.86538696289062 0.0
62 62 TYR C 1.0 62.890377044677734 0.0
63 63 TYR E 1.0 39.98308563232422 0.0
66 66 TYR C 1.0 101.42338562011719 0.0
142 142 SER C 1.0 95.21510314941406 21.929805755615234
5X7B A X-ray 2.450000047683716 3 N 1.0 36, 62, 63, 66, 142
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
36 36 SER C 1.0 112.36795806884766 0.0
62 62 TYR C 1.0 84.91183471679688 0.0
63 63 TYR E 1.0 39.19837951660156 0.0
66 66 TYR C 1.0 117.07856750488281 0.0
142 142 SER C 1.0 81.2366943359375 20.077653884887695
5X94 A X-ray 2.5999999046325684 3 N 1.0 36, 62, 63, 66, 142
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
36 36 SER C 1.0 104.9588394165039 0.0
62 62 TYR C 1.0 54.46965789794922 0.0
63 63 TYR E 1.0 36.38191223144531 0.0
66 66 TYR C 1.0 111.3180923461914 0.0
142 142 SER C 1.0 84.87251281738281 17.7117919921875
3TKZ A X-ray 1.7999999523162842 3 P 1.0 36, 62, 63, 66
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
36 36 SER C 1.0 84.19889068603516 13.366583824157715
62 62 TYR C 1.0 56.51992416381836 0.0
63 63 TYR E 1.0 39.907020568847656 0.0
66 66 TYR C 1.0 115.95197296142578 23.963401794433594
3TL0 A X-ray 2.049999952316284 2 B 0.54182506 36, 62, 63, 66
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
36 36 SER C 1.0 83.39112854003906 13.488520622253418
62 62 TYR C 1.0 55.83723068237305 0.0
63 63 TYR E 1.0 43.640846252441406 0.0
66 66 TYR C 1.0 115.75733947753906 0.0
4QSY A X-ray 2.0999999046325684 2 B 1.0 36, 62, 63, 66
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
36 36 SER C 1.0 91.08677673339844 14.82922077178955
62 62 TYR C 1.0 58.02404022216797 0.0
63 63 TYR E 1.0 40.67493438720703 0.0
66 66 TYR C 1.0 118.37178802490234 1.2299187183380127
4JE4 A X-ray 2.309999942779541 2 B 1.0 36, 62, 63, 66
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
36 36 SER C 1.0 99.66295623779297 76.05626678466797
62 62 TYR C 1.0 60.28692626953125 0.0
63 63 TYR E 1.0 42.197383880615234 0.0
66 66 TYR C 1.0 119.77645874023438 25.647550582885742
3ZM1 A X-ray 1.399999976158142 Monomer A 0.0 279, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
279 279 TYR C 0.87 79.8901596069336 0.0
304 304 TYR E 1.0 2.638113260269165 0.0
3ZM2 A X-ray 1.5 Monomer A 0.0 279, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
279 279 TYR C 0.87 78.99003601074219 0.0
304 304 TYR E 1.0 2.4884531497955322 0.0
3ZM3 A X-ray 1.5 Monomer A 0.0 279, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
279 279 TYR C 0.87 84.79098510742188 0.0
304 304 TYR C 1.0 2.506573438644409 0.0
3ZM0 A X-ray 1.5 Monomer A 0.0 279, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
279 279 TYR C 0.87 88.93977355957031 0.0
304 304 TYR E 1.0 2.9755172729492188 0.0
4RDD A X-ray 1.600000023841858 Monomer [3LU]A:600 0.1 279, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
279 279 TYR C 0.87 89.7843246459961 0.0
304 304 TYR E 1.0 1.3403109312057495 0.0
3B7O A X-ray 1.600000023841858 2 A 0.7720096 279, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
279 279 TYR C 0.87 71.69305419921875 0.0
304 304 TYR E 1.0 1.7176086902618408 0.0
3O5X A X-ray 2.0 Monomer [JZG]A:1 0.1 279, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
279 279 TYR C 0.87 81.24351501464844 0.0
304 304 TYR C 1.0 1.6302556991577148 0.0
3MOW A X-ray 2.299999952316284 Monomer [B2B]A:1 0.1 279, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
279 279 TYR C 0.87 78.35245513916016 62.30708312988281
304 304 TYR C 1.0 1.785710334777832 0.0
4PVG A X-ray 2.4000000953674316 Monomer A 0.0 279, 304
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
279 279 TYR C 0.87 80.91313934326172 0.0
304 304 TYR E 1.0 0.7348968386650085 0.0
4JEG A X-ray 2.299999952316284 2 B 1.0 142
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
142 142 SER C 1.0 85.34249114990234 44.479366302490234

Mutations

Showing 38 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
2 T I Disease Noonan syndrome 1 (NS1) [MIM:163950]
42 T A Disease Noonan syndrome 1 (NS1) [MIM:163950]
58 N K Disease Noonan syndrome 1 (NS1) [MIM:163950]
59 T A Disease Noonan syndrome 1 (NS1) [MIM:163950]
60 G V Polymorphism
61 D G Disease Noonan syndrome 1 (NS1) [MIM:163950]
62 Y D Disease Noonan syndrome 1 (NS1) [MIM:163950]
63 Y C Disease Noonan syndrome 1 (NS1) [MIM:163950]
69 E Q Disease Noonan syndrome 1 (NS1) [MIM:163950]
71 F L Polymorphism
72 A T Disease Leukemia, juvenile myelomonocytic (JMML) [MIM:607785]
73 T I Disease Noonan syndrome 1 (NS1) [MIM:163950]
76 E V Disease Leukemia, juvenile myelomonocytic (JMML) [MIM:607785]
79 Q P Disease Noonan syndrome 1 (NS1) [MIM:163950]
106 D A Disease Noonan syndrome 1 (NS1) [MIM:163950]
139 E D Disease Noonan syndrome 1 (NS1) [MIM:163950]
256 Q R Disease Noonan syndrome 1 (NS1) [MIM:163950]
261 L F Disease Noonan syndrome 1 (NS1) [MIM:163950]
262 L R Disease Noonan syndrome 1 (NS1) [MIM:163950]
265 R Q Disease Noonan syndrome 1 (NS1) [MIM:163950]
279 Y C Disease LEOPARD syndrome 1 (LPRD1) [MIM:151100]
282 I V Disease Noonan syndrome 1 (NS1) [MIM:163950]
285 F S Disease Noonan syndrome 1 (NS1) [MIM:163950]
308 N D Disease Noonan syndrome 1 (NS1) [MIM:163950]
309 I V Unclassified Noonan syndrome 1 (NS1) [MIM:163950]
415 T M Disease Noonan syndrome 1 (NS1) [MIM:163950]
465 A T Disease LEOPARD syndrome 1 (LPRD1) [MIM:151100]
468 G A Disease LEOPARD syndrome 1 (LPRD1) [MIM:151100]
472 T M Disease LEOPARD syndrome 1 (LPRD1) [MIM:151100]
495 P S Disease Noonan syndrome 1 (NS1) [MIM:163950]
502 R W Disease LEOPARD syndrome 1 (LPRD1) [MIM:151100]
505 R K Disease Noonan syndrome 1 (NS1) [MIM:163950]
506 S T Disease Noonan syndrome 1 (NS1) [MIM:163950]
507 G R Disease Noonan syndrome 1 (NS1) [MIM:163950]
508 M V Disease Noonan syndrome 1 (NS1) [MIM:163950]
510 Q R Disease Noonan syndrome 1 (NS1) [MIM:163950]
514 Q E Disease LEOPARD syndrome 1 (LPRD1) [MIM:151100]
564 L F Unclassified Noonan syndrome 1 (NS1) [MIM:163950]