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PDB 
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Phospho-sites

Showing 18 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
43 PhosphoY PRIDE yes
825 PhosphoT PRIDE
839 PhosphoT PRIDE
980 PhosphoY UP Experimental
1009 PhosphoS PRIDE yes
1014 PhosphoY PRIDE yes
1040 PhosphoS PRIDE yes
1052 PhosphoS PRIDE yes
1161 PhosphoY UP, PRIDE Experimental
1165 PhosphoY UP, PRIDE Experimental yes
1166 PhosphoY UP, PRIDE Experimental yes
1278 PhosphoS UP Similarity
1282 PhosphoS UP Similarity
1313 PhosphoS PRIDE yes
1339 PhosphoS PRIDE yes
1346 PhosphoY PRIDE yes
1365 PhosphoS PRIDE yes
1366 PhosphoT 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 20 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
43 41 47 3 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 -
825 825 843 1 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 -
839 825 843 15 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 -
1009 1004 1019 6 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD000612 2 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
1014 1004 1019 11 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD000612 2 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
1040 1034 1055 7 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
1052 1034 1055 19 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
1161 1159 1168 3 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD000612 6 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 -
1161 1159 1167 3 1
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
1165 1159 1168 7 3
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
PXD001565 2 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain -
PXD003198 9 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line -
1166 1151 1168 16 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD000612 2 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
1166 1159 1168 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 13 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line -
1313 1287 1319 27 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
1339 1325 1343 15 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 -
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 -
PXD004452 7 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
1339 1338 1343 2 5
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD004252 1 Modulating the selectivity of affinity absorbents to multi-phosphopeptides by a novel competitive substitution strategy Homo sapiens (Human) PARTIAL 2016-08-03 cell culture -
PXD003531 4 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
PXD002286 3 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 -
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 -
1339 1338 1353 2 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
1339 1338 1354 2 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
1346 1338 1353 9 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
1365 1358 1367 8 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
1366 1358 1367 9 4
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD000612 42 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 4 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 - -
PXD005366 4 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 -
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -

Structures

Showing 24 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
5FXS A X-ray 1.899999976158142 Monomer [OZN]A:2290 0.0717976 980, 1009, 1014, 1040, 1052, 1161, 1165, 1166, 1278, 1282
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
980 980 TYR C 0.89 180.92897033691406 0.0
987 987 TYR C 1.0 31.595458984375 0.0
1009 1009 SER C 1.0 107.76323699951172 0.0
1014 1014 TYR E 1.0 47.12120819091797 0.0
1040 1040 SER C 1.0 45.848182678222656 0.0
1052 1052 SER H 1.0 24.75829315185547 0.0
1161 1161 TYR C 1.0 36.07958221435547 0.0
1165 1165 TYR C 1.0 12.589402198791504 0.0
1166 1166 TYR E 1.0 45.28529357910156 0.0
1278 1278 SER C 1.0 3.766190767288208 0.0
1282 1282 SER C 1.0 40.031898498535156 0.0
5FXQ A X-ray 2.299999952316284 Monomer [GD5]A:2287 0.1 980, 1009, 1014, 1040, 1052, 1161, 1165, 1166, 1278, 1282
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
980 980 TYR C 0.89 177.2405242919922 0.0
987 987 TYR C 1.0 32.210044860839844 0.0
1009 1009 SER C 1.0 91.20952606201172 0.0
1014 1014 TYR E 1.0 46.83562469482422 0.0
1040 1040 SER C 1.0 43.82392883300781 0.0
1052 1052 SER H 1.0 18.539522171020508 0.0
1161 1161 TYR C 1.0 36.58470153808594 0.0
1165 1165 TYR C 1.0 15.766621589660645 0.0
1166 1166 TYR E 1.0 37.47306823730469 0.0
1278 1278 SER C 1.0 3.5017802715301514 0.0
1282 1282 SER C 1.0 39.627777099609375 0.0
5FXR A X-ray 2.4000000953674316 Monomer [8LN]A:2284 0.1 980, 1009, 1014, 1040, 1052, 1161, 1165, 1166, 1278, 1282
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
980 980 TYR C 0.89 188.66017150878906 0.0
987 987 TYR C 1.0 33.1619873046875 0.0
1009 1009 SER C 1.0 86.99566650390625 0.0
1014 1014 TYR E 1.0 47.24977493286133 0.0
1040 1040 SER C 1.0 46.4893798828125 0.0
1052 1052 SER H 1.0 18.728694915771484 0.0
1161 1161 TYR C 1.0 27.807519912719727 0.0
1165 1165 TYR C 1.0 20.77744483947754 0.0
1166 1166 TYR E 1.0 48.75206756591797 0.0
1278 1278 SER C 1.0 2.7463109493255615 0.0
1282 1282 SER C 1.0 65.63432312011719 0.0
3LW0 A X-ray 1.7899999618530273 Monomer [CCX]A:1 0.054564875 1009, 1014, 1040, 1052, 1161, 1165, 1166, 1278, 1282
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
987 987 TYR C 1.0 24.55077362060547 0.0
1009 1009 SER C 1.0 28.67719078063965 0.0
1014 1014 TYR E 1.0 56.20929718017578 0.0
1040 1040 SER C 1.0 53.67401885986328 0.0
1052 1052 SER H 1.0 39.306915283203125 0.0
1161 1161 TYR C 1.0 12.177504539489746 0.0
1165 1165 TYR C 1.0 19.46330451965332 0.0
1166 1166 TYR E 1.0 38.216365814208984 0.0
1278 1278 SER C 1.0 4.0790324211120605 0.0
1282 1282 SER C 1.0 41.15512466430664 0.0
4D2R A X-ray 2.0999999046325684 Monomer [CL]A:2287 0.08732639 1009, 1014, 1040, 1052, 1161, 1165, 1166, 1278, 1282
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
987 987 TYR C 1.0 24.3143367767334 0.0
1009 1009 SER C 1.0 57.000518798828125 0.0
1014 1014 TYR E 1.0 51.65499496459961 0.0
1040 1040 SER C 1.0 53.29228973388672 0.0
1052 1052 SER H 1.0 24.153823852539062 0.0
1161 1161 TYR H 1.0 9.720422744750977 0.0
1165 1165 TYR C 1.0 52.81535720825195 0.0
1166 1166 TYR E 1.0 52.297607421875 0.0
1278 1278 SER C 1.0 4.000838279724121 0.0
1282 1282 SER C 1.0 43.48524475097656 0.0
3O23 A X-ray 2.0999999046325684 Monomer [MQY]A:1 0.1 1009, 1014, 1040, 1052, 1161, 1165, 1166, 1278, 1282
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1009 1009 SER C 1.0 106.23806762695312 0.0
1014 1014 TYR E 1.0 54.35017395019531 0.0
1040 1040 SER C 1.0 67.10269927978516 0.0
1052 1052 SER H 1.0 46.875511169433594 0.0
1161 1161 TYR C 1.0 15.353830337524414 0.0
1165 1165 TYR C 1.0 56.371700286865234 0.0
1166 1166 TYR E 1.0 55.67512130737305 0.0
1278 1278 SER C 1.0 3.443713665008545 0.0
1282 1282 SER C 1.0 64.99246978759766 0.0
1JQH A X-ray 2.0999999046325684 3 B 0.40448976 1009, 1014, 1040, 1052, 1165, 1166, 1278, 1282
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
987 987 TYR E 1.0 30.118968963623047 24.55707359313965
1009 1009 SER C 1.0 100.22822570800781 0.0
1014 1014 TYR E 1.0 48.37030792236328 0.0
1040 1040 SER C 1.0 60.92625045776367 0.0
1052 1052 SER H 1.0 25.592485427856445 0.0
1165 1165 TYR C 1.0 233.51712036132812 0.0
1166 1166 TYR C 1.0 81.68296813964844 0.0
1278 1278 SER C 1.0 3.9360907077789307 0.0
1282 1282 SER C 1.0 39.8218994140625 0.0
3LVP A X-ray 3.0 Monomer [PDR]A:1 0.1 1009, 1014, 1040, 1052, 1161, 1278, 1282
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1009 1009 SER C 1.0 106.0158920288086 0.0
1014 1014 TYR E 1.0 50.63644027709961 0.0
1040 1040 SER C 1.0 73.69982147216797 0.0
1052 1052 SER H 1.0 38.7286262512207 0.0
1161 1161 TYR C 1.0 228.93035888671875 0.0
1278 1278 SER C 1.0 0.612247109413147 0.0
1282 1282 SER C 1.0 26.884695053100586 0.0
2ZM3 A X-ray 2.5 8 A 1.0 1009, 1014, 1040, 1052, 1278, 1282
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
987 987 TYR C 1.0 88.72418212890625 0.0
1009 1009 SER C 1.0 94.16837310791016 31.896329879760742
1014 1014 TYR E 1.0 46.16443634033203 0.0
1040 1040 SER C 1.0 66.47566986083984 0.0
1052 1052 SER H 1.0 36.18280792236328 0.0
1278 1278 SER C 1.0 7.147312641143799 0.0
1282 1282 SER C 1.0 33.76251983642578 0.0
3F5P A X-ray 2.9000000953674316 8 F 0.594276 1009, 1014, 1040, 1052, 1278, 1282
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
987 987 TYR H 1.0 81.71659088134766 77.2845230102539
1009 1009 SER C 1.0 93.85710144042969 0.0
1014 1014 TYR E 1.0 45.157344818115234 0.0
1040 1040 SER C 1.0 65.95842742919922 0.33458107709884644
1052 1052 SER H 1.0 47.84391403198242 0.0
1278 1278 SER C 1.0 3.322542905807495 0.0
1282 1282 SER C 1.0 40.497615814208984 0.0
1P4O A X-ray 1.5 2 B 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
980 950 TYR C 0.89 194.4298553466797 158.04876708984375
987 957 TYR C 1.0 36.25339889526367 0.0
1009 979 SER C 1.0 87.63361358642578 0.0
1014 984 TYR E 1.0 53.6312255859375 0.0
1040 1010 SER C 1.0 54.38360595703125 14.778472900390625
1052 1022 SER H 1.0 32.63648986816406 0.0
1161 1131 TYR H 1.0 7.3923659324646 0.0
1165 1135 TYR C 1.0 40.38742446899414 0.0
1166 1136 TYR E 1.0 52.9754638671875 0.0
1278 1248 SER C 1.0 5.725467681884766 0.0
1282 1252 SER C 1.0 39.49201202392578 0.0
2OJ9 A X-ray 2.0 Monomer [BMI]A:301 0.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
987 957 TYR C 1.0 28.01114845275879 0.0
1009 979 SER C 1.0 45.369197845458984 1.7572461366653442
1014 984 TYR E 1.0 61.824256896972656 0.0
1040 1010 SER C 1.0 66.37113189697266 0.0
1052 1022 SER H 1.0 26.31713104248047 0.0
1161 1131 TYR C 1.0 32.2476692199707 0.0
1165 1135 TYR C 1.0 12.924490928649902 0.0
1166 1136 TYR E 1.0 62.032630920410156 0.0
1278 1248 SER C 1.0 3.784485101699829 0.0
1282 1252 SER C 1.0 36.2740592956543 0.0
3I81 A X-ray 2.0799999237060547 Monomer [EBI]A:201 0.1
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
987 957 TYR C 1.0 39.24732208251953 0.0
1009 979 SER C 1.0 69.71300506591797 0.0
1014 984 TYR E 1.0 58.7142448425293 0.0
1040 1010 SER C 1.0 55.94289779663086 0.0
1052 1022 SER H 1.0 28.568265914916992 0.0
1161 1131 TYR C 1.0 21.413070678710938 0.0
1165 1135 TYR C 1.0 53.73993682861328 0.0
1166 1136 TYR E 1.0 65.44678497314453 0.0
1278 1248 SER C 1.0 4.618980884552002 0.0
1282 1252 SER C 1.0 46.23724365234375 0.0
1K3A A X-ray 2.0999999046325684 2 B 0.9569788
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1009 979 SER C 1.0 100.02146911621094 0.0
1014 984 TYR E 1.0 51.760318756103516 0.0
1040 1010 SER C 1.0 53.22007369995117 0.0
1052 1022 SER H 1.0 51.77349853515625 0.0
1278 1248 SER C 1.0 5.049986362457275 0.0
1282 1252 SER C 1.0 33.615264892578125 0.0
3NW7 A X-ray 2.109999895095825 Monomer A 0.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
987 957 TYR C 1.0 63.21358871459961 0.0
1009 979 SER C 1.0 55.9703369140625 0.0
1014 984 TYR E 1.0 58.7782096862793 0.0
1040 1010 SER C 1.0 54.789485931396484 0.0
1052 1022 SER H 1.0 32.196781158447266 0.0
1161 1131 TYR C 1.0 33.16702651977539 0.0
1165 1135 TYR C 1.0 18.099369049072266 0.0
1166 1136 TYR E 1.0 31.491355895996094 0.0
1278 1248 SER C 1.0 4.617961883544922 0.0
1282 1252 SER C 1.0 44.13029861450195 7.48222017288208
3NW5 A X-ray 2.140000104904175 Monomer [LGX]A:1 0.1
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
987 957 TYR C 1.0 32.20095443725586 0.0
1009 979 SER C 1.0 13.838229179382324 0.0
1014 984 TYR E 1.0 54.901031494140625 0.0
1040 1010 SER C 1.0 48.44986343383789 0.0
1052 1022 SER H 1.0 26.394392013549805 0.0
1161 1131 TYR C 1.0 40.233009338378906 7.490145206451416
1165 1135 TYR C 1.0 56.58551025390625 0.0
1166 1136 TYR E 1.0 45.507442474365234 0.0
1278 1248 SER C 1.0 4.704381465911865 0.0
1282 1252 SER C 1.0 43.24711227416992 0.0
3NW6 A X-ray 2.200000047683716 Monomer [LGW]A:1 0.1
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
987 957 TYR C 1.0 36.12460708618164 0.0
1009 979 SER C 1.0 58.0356330871582 0.0
1014 984 TYR E 1.0 51.14891815185547 0.0
1040 1010 SER C 1.0 44.006961822509766 0.0
1052 1022 SER H 1.0 30.065113067626953 0.0
1161 1131 TYR C 1.0 20.809289932250977 0.0
1165 1135 TYR C 1.0 55.22202682495117 0.0
1166 1136 TYR E 1.0 51.30145263671875 0.0
1278 1248 SER C 1.0 5.478364944458008 0.0
1282 1252 SER C 1.0 39.29290008544922 0.0
5HZN A X-ray 2.200000047683716 8 B 0.53804964
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
987 984 TYR C 1.0 42.87841033935547 0.0
1009 1006 SER C 1.0 4.887092113494873 0.0
1014 1011 TYR E 1.0 55.17290115356445 0.0
1040 1037 SER C 1.0 34.00412368774414 1.168968677520752
1052 1049 SER H 1.0 32.0120964050293 0.0
1161 1158 TYR C 1.0 65.62467956542969 32.87735366821289
1165 1162 TYR C 1.0 146.071533203125 135.93797302246094
1166 1163 TYR E 1.0 175.34092712402344 142.1457061767578
1278 1275 SER C 1.0 4.588665962219238 0.0
1282 1279 SER C 1.0 43.05990982055664 0.0
3D94 A X-ray 2.299999952316284 Monomer [CA]A:2 0.099998735
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
987 957 TYR C 1.0 35.09261703491211 0.0
1009 979 SER C 1.0 3.1126351356506348 0.0
1014 984 TYR E 1.0 51.05025100708008 0.0
1040 1010 SER C 1.0 52.20682144165039 0.0
1052 1022 SER H 1.0 22.844165802001953 0.0
1161 1131 TYR C 1.0 47.30291748046875 3.3121583461761475
1165 1135 TYR C 1.0 171.8229217529297 0.0
1166 1136 TYR C 1.0 181.11325073242188 0.0
1278 1248 SER C 1.0 4.2740797996521 0.0
1282 1252 SER C 1.0 39.98003005981445 0.0
1IGR A X-ray 2.5999999046325684 Monomer [SO4]A:495 0.027654557
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
43 13 TYR H 0.8 18.08807373046875 0.0
168 138 TYR E 1.0 97.94174194335938 0.0
1M7N A X-ray 2.700000047683716 2 B 0.1
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
987 984 TYR C 1.0 35.56278991699219 0.0
1009 1006 SER C 1.0 85.17935943603516 0.0
1014 1011 TYR E 1.0 48.59865188598633 0.0
1040 1037 SER C 1.0 55.28782653808594 17.459842681884766
1052 1049 SER H 1.0 28.00673484802246 0.0
1161 1158 TYR H 1.0 11.298519134521484 0.0
1165 1162 TYR C 1.0 43.6578483581543 0.0
1166 1163 TYR E 1.0 57.42434310913086 0.0
1278 1275 SER C 1.0 2.731872320175171 0.0
1282 1279 SER C 1.0 30.7203311920166 0.0
3QQU A X-ray 2.9000000953674316 Monomer D 0.13209932
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1009 1006 SER C 1.0 71.42321014404297 0.0
1014 1011 TYR E 1.0 45.97709655761719 0.0
1040 1037 SER C 1.0 52.833045959472656 43.57051086425781
1052 1049 SER C 1.0 46.41423034667969 33.954383850097656
1161 1158 TYR C 1.0 13.481999397277832 0.0
1165 1162 TYR C 1.0 47.4739875793457 0.0
1166 1163 TYR E 1.0 57.31168746948242 0.0
1278 1275 SER C 1.0 5.986740589141846 0.0
1282 1279 SER C 1.0 33.26155090332031 0.0
5U8R A X-ray 3.0 2 A 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
43 13 TYR H 0.8 97.86155700683594 0.0
168 138 TYR E 1.0 75.64044952392578 19.734407424926758
825 795 THR C 1.0 0.6223835945129395 0.0
839 809 THR E 0.73 65.21430969238281 0.0
5U8Q A X-ray 3.2699999809265137 8 B 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
43 13 TYR C 0.8 42.27124786376953 0.0
168 138 TYR E 1.0 58.35029220581055 0.0
825 795 THR C 1.0 0.0 0.0
839 809 THR E 0.73 71.04133605957031 0.0

Mutations

Showing 18 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
105 V L Unclassified
138 R Q Disease Insulin-like growth factor 1 resistance (IGF1RES) [MIM:270450]
145 K N Disease Insulin-like growth factor 1 resistance (IGF1RES) [MIM:270450]
359 N Y Disease Insulin-like growth factor 1 resistance (IGF1RES) [MIM:270450]
388 V M Polymorphism
437 R H Polymorphism
511 R Q Polymorphism
595 R H Polymorphism
605 R H Polymorphism
739 R Q Disease Insulin-like growth factor 1 resistance (IGF1RES) [MIM:270450]
808 H R Polymorphism
828 A T Polymorphism
857 N S Polymorphism
865 Y C Disease Insulin-like growth factor 1 resistance (IGF1RES) [MIM:270450]
1256 R S Disease Insulin-like growth factor 1 resistance (IGF1RES) [MIM:270450]
1337 R C Disease Insulin-like growth factor 1 resistance (IGF1RES) [MIM:270450]
1338 A T Polymorphism
1347 A V Unclassified A lung squamous cell carcinoma sample