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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 14 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
179 SER PRIDE yes
269 SER PRIDE
275 SER PRIDE
399 TYR PRIDE yes
458 THR UP, PRIDE Combined yes
730 THR PRIDE yes
821 SER PRIDE yes
923 THR PRIDE yes
925 THR UP, PRIDE Combined yes
926 THR UP, PRIDE Combined yes
932 TYR PRIDE yes
934 TYR PRIDE yes
1029 THR PRIDE yes
1033 SER 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 22 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
179 158 189 22 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
269 261 280 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
275 261 280 15 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
399 394 406 6 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001565 2 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain
399 396 406 4 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 8 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
458 452 466 7 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001333 1 Anion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC Homo sapiens (Human) PARTIAL 2015-04-23 HeLa cell
730 725 739 6 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
821 811 825 11 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001550 1 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 cell culture
923 919 930 5 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD003531 1 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
925 919 929 7 3
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 9 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 - -
PXD005366 3 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
925 919 930 7 5
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 -
PXD003531 2 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD001333 1 Anion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC Homo sapiens (Human) PARTIAL 2015-04-23 HeLa cell
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 3 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
926 909 930 18 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004415 11 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte
926 909 929 18 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004415 1 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte
926 919 930 8 8
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001060 8 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell -
PXD000612 43 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 7 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
PXD004940 3 Performance of the Orbitrap Fusion Lumos Tribrid in single-shot analyses of human samples Homo sapiens (Human) PARTIAL 2017-03-09 HeLa cell -
PXD001333 6 Anion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC Homo sapiens (Human) PARTIAL 2015-04-23 HeLa cell -
PXD005366 86 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 8 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
PXD001550 1 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
926 919 929 8 5
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 -
PXD000474 3 Simulated phosphopeptide spectral library for confident site localization Homo sapiens (Human) PARTIAL 2015-03-17 HeLa cell -
PXD002286 4 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 - -
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 -
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
932 931 940 2 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 -
PXD003531 2 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
934 931 940 4 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
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
PXD001565 3 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain -
1029 1026 1034 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
1029 1026 1032 4 3
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001060 2 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell -
PXD003531 1 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
PXD001374 2 Label-free quantitative phosphoproteomics with novel pairwise abundance normalization reveals synergistic RAS and CIP2A signaling Homo sapiens (Human) PARTIAL 2015-08-24 HeLa cell -
1033 1026 1045 8 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004452 2 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
1033 1026 1034 8 1
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
1033 1033 1045 1 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001333 1 Anion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC Homo sapiens (Human) PARTIAL 2015-04-23 HeLa cell

Structures

Showing 42 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
3HQD A X-ray 2.190000057220459 Monomer [ANP]A:601 0.03972541 179, 269, 275
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER E 0.81 44.261962890625 0.0
164 164 TYR E 1.0 41.35121154785156 0.0
179 179 SER C 0.75 52.10562515258789 0.0
269 269 SER C 0.96 53.578548431396484 0.0
275 275 SER H 1.0 1.2272629737854004 0.0
4AS7 A X-ray 2.4000000953674316 1 [6LX]A:1375 0.15774399 179, 269, 275
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER E 0.81 78.64524841308594 0.0
164 164 TYR E 1.0 12.724157333374023 0.0
179 179 SER C 0.75 45.5108642578125 0.0
269 269 SER C 0.96 6.0478363037109375 0.0
275 275 SER C 1.0 81.05751037597656 0.0
4BXN A X-ray 2.7899999618530273 Monomer [CL]A:1376 0.019178668 179, 269, 275
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER C 0.81 50.50492477416992 0.0
164 164 TYR E 1.0 27.29144287109375 0.0
179 179 SER C 0.75 65.15528106689453 0.0
269 269 SER H 0.96 0.0 0.0
275 275 SER C 1.0 82.3897933959961 0.0
1X88 A X-ray 1.7999999523162842 2 [ADP]A:601 0.040526114 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER C 0.81 47.290740966796875 0.0
164 164 TYR E 1.0 16.00331687927246 0.0
179 179 SER C 0.75 45.76378631591797 0.0
269 269 SER C 0.96 15.661829948425293 0.0
2PG2 A X-ray 1.850000023841858 2 [ADP]A:601 0.04798196 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER C 0.81 39.78422164916992 0.0
164 164 TYR E 1.0 19.9072265625 0.0
179 179 SER C 0.75 59.46080017089844 0.0
269 269 SER C 0.96 21.029600143432617 0.0
2X7C A X-ray 1.899999976158142 2 [ADP]A:601 0.23607509 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER C 0.81 47.9836311340332 0.0
164 164 TYR E 1.0 21.265460968017578 0.0
179 179 SER C 0.75 37.27157211303711 0.0
269 269 SER C 0.96 20.18643569946289 0.0
1Q0B A X-ray 1.899999976158142 2 [ADP]A:601 0.3087385 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER E 0.81 41.1498908996582 0.0
164 164 TYR E 1.0 26.88191032409668 0.0
179 179 SER C 0.75 77.8543930053711 0.0
269 269 SER C 0.96 21.365949630737305 0.0
3K5E A X-ray 1.9700000286102295 Monomer [ADP]A:603 0.046509974 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER C 0.81 32.31977844238281 0.0
164 164 TYR E 1.0 22.565824508666992 0.0
179 179 SER C 0.75 62.36119842529297 0.0
269 269 SER C 0.96 21.471935272216797 0.0
2WOG A X-ray 2.0 3 C 0.35831967 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER E 0.81 45.44194793701172 0.0
164 164 TYR E 1.0 21.31487464904785 0.0
179 179 SER C 0.75 27.643218994140625 26.933937072753906
269 269 SER C 0.96 19.9157772064209 0.0
3L9H A X-ray 2.0 2 [ADP]A:501 0.08743173 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER E 0.81 53.97236251831055 0.0
164 164 TYR E 1.0 29.816247940063477 0.0
179 179 SER C 0.75 67.05988311767578 0.0
269 269 SER C 0.96 20.90294647216797 0.0
2UYI A X-ray 2.0999999046325684 2 [ADP]A:601 0.38002574 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER C 0.81 40.02188491821289 0.0
164 164 TYR E 1.0 20.81570816040039 0.0
179 179 SER C 0.75 56.03558349609375 0.0
269 269 SER C 0.96 22.260290145874023 0.0
1II6 A X-ray 2.0999999046325684 2 [ADP]A:2601 0.043867126 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER E 0.81 62.55460739135742 0.0
164 164 TYR E 1.0 15.077446937561035 0.0
179 179 SER C 0.75 53.39577102661133 0.0
269 269 SER C 0.96 24.687273025512695 0.0
2FME A X-ray 2.0999999046325684 Monomer [ADP]A:371 0.039641194 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER E 0.81 45.520748138427734 0.0
164 164 TYR E 1.0 25.248456954956055 0.0
179 179 SER C 0.75 37.607234954833984 0.0
269 269 SER H 0.96 5.115640640258789 0.0
2UYM A X-ray 2.109999895095825 2 [ADP]A:601 0.33968014 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER C 0.81 45.25602340698242 0.0
164 164 TYR E 1.0 19.444786071777344 0.0
179 179 SER C 0.75 61.39845275878906 0.0
269 269 SER C 0.96 22.66752815246582 0.0
2X2R A X-ray 2.200000047683716 3 B 0.354084 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER E 0.81 46.865142822265625 0.0
164 164 TYR E 1.0 22.530780792236328 0.0
179 179 SER C 0.75 28.33757972717285 0.0
269 269 SER C 0.96 22.405834197998047 0.0
3CJO A X-ray 2.2799999713897705 2 [ADP]A:601 0.042294636 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER C 0.81 38.422977447509766 0.0
164 164 TYR E 1.0 25.913349151611328 0.0
179 179 SER C 0.75 61.525455474853516 0.0
269 269 SER C 0.96 18.600353240966797 0.0
2FKY A X-ray 2.299999952316284 2 [ADP]A:601 0.04984438 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER E 0.81 38.722877502441406 0.0
164 164 TYR E 1.0 26.637773513793945 0.0
179 179 SER C 0.75 74.56861114501953 0.0
269 269 SER C 0.96 20.843305587768555 0.0
2GM1 A X-ray 2.299999952316284 Monomer [ADP]A:372 0.027902318 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER E 0.81 52.798622131347656 0.0
164 164 TYR E 1.0 27.11623191833496 0.0
179 179 SER C 0.75 50.597434997558594 0.0
269 269 SER H 0.96 3.207409381866455 0.0
2X7D A X-ray 2.299999952316284 2 [ADP]A:601 0.026050529 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER C 0.81 47.3239631652832 0.0
164 164 TYR E 1.0 21.604148864746094 0.0
179 179 SER C 0.75 42.176578521728516 0.0
269 269 SER C 0.96 22.662220001220703 0.0
4ZCA A X-ray 2.299999952316284 2 [ADP]A:601 0.3724003 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER E 0.81 59.17268371582031 0.0
164 164 TYR E 1.0 16.675764083862305 0.0
179 179 SER C 0.75 59.706382751464844 0.0
269 269 SER C 0.96 23.914337158203125 0.0
4ZHI A X-ray 2.299999952316284 Monomer [ADP]A:601 0.1 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER E 0.81 65.88095092773438 0.0
164 164 TYR E 1.0 21.68222999572754 0.0
179 179 SER C 0.75 46.707000732421875 0.0
269 269 SER C 0.96 58.7893180847168 0.0
2X7E A X-ray 2.4000000953674316 2 [ADP]A:600 0.034628183 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER C 0.81 47.837833404541016 0.0
164 164 TYR E 1.0 19.59196662902832 0.0
179 179 SER C 0.75 55.65437698364258 0.0
269 269 SER C 0.96 14.924416542053223 0.0
3K3B A X-ray 2.4000000953674316 2 [ADP]A:370 0.3169032 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER E 0.81 59.9493522644043 0.0
164 164 TYR E 1.0 38.10725402832031 0.0
179 179 SER C 0.75 63.586341857910156 0.0
269 269 SER C 0.96 23.305908203125 0.0
4A5Y A X-ray 2.450000047683716 2 [G7X]A:1365 0.32334796 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER E 0.81 72.12283325195312 0.0
164 164 TYR E 1.0 17.844823837280273 0.0
179 179 SER C 0.75 35.36101150512695 0.0
269 269 SER C 0.96 17.45602035522461 0.0
2Q2Y A X-ray 2.5 2 [ADP]A:601 0.046902776 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER E 0.81 42.580421447753906 0.0
164 164 TYR E 1.0 25.35881233215332 0.0
179 179 SER C 0.75 67.15518188476562 0.0
269 269 SER C 0.96 20.618301391601562 0.0
1YRS A X-ray 2.5 2 [ADP]A:601 0.0409479 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER C 0.81 42.89872741699219 0.0
164 164 TYR E 1.0 25.92914390563965 0.0
179 179 SER C 0.75 74.86392211914062 0.0
269 269 SER C 0.96 21.007511138916016 0.0
4B7B A X-ray 2.5 Monomer [CO]A:1387 0.005525843 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER E 0.81 75.04669952392578 0.0
164 164 TYR E 1.0 46.52783203125 0.0
179 179 SER C 0.75 68.7000732421875 0.0
269 269 SER C 0.96 4.979777812957764 0.0
2FL2 A X-ray 2.5 2 [ADP]A:601 0.05466186 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER E 0.81 38.83542251586914 0.0
164 164 TYR E 1.0 26.010791778564453 0.0
179 179 SER C 0.75 77.59036254882812 0.0
269 269 SER C 0.96 19.891300201416016 0.0
2FL6 A X-ray 2.5 2 [ADP]A:601 0.37934676 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER E 0.81 40.023033142089844 0.0
164 164 TYR E 1.0 25.736968994140625 0.0
179 179 SER C 0.75 76.08610534667969 0.0
269 269 SER C 0.96 21.66400718688965 0.0
3KEN A X-ray 2.5 3 A 0.316402 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER E 0.81 47.9547004699707 0.0
164 164 TYR E 1.0 16.977619171142578 0.0
179 179 SER C 0.75 28.690649032592773 28.19991683959961
269 269 SER C 0.96 21.810749053955078 0.0
2G1Q A X-ray 2.509999990463257 2 [ADP]A:601 0.43121436 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER C 0.81 41.35768127441406 0.0
164 164 TYR E 1.0 27.409727096557617 0.0
179 179 SER C 0.75 61.33370590209961 0.0
269 269 SER C 0.96 13.360833168029785 0.0
4A28 A X-ray 2.549999952316284 2 [ADP]A:1365 0.050451845 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER E 0.81 61.331058502197266 0.0
164 164 TYR C 1.0 21.193492889404297 0.0
179 179 SER C 0.75 42.82889938354492 0.0
269 269 SER C 0.96 21.394968032836914 0.0
4AP0 A X-ray 2.5899999141693115 2 [G7X]A:2001 0.26259124 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER E 0.81 54.38719177246094 0.0
164 164 TYR E 1.0 24.753986358642578 0.0
179 179 SER C 0.75 48.78234100341797 0.0
269 269 SER H 0.96 0.16770832240581512 0.0
2XAE A X-ray 2.5999999046325684 3 B 0.22471057 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER E 0.81 46.07555389404297 0.0
164 164 TYR E 1.0 18.76227569580078 0.0
179 179 SER C 0.75 27.960098266601562 0.0
269 269 SER C 0.96 21.763572692871094 0.0
2IEH A X-ray 2.700000047683716 2 [K]A:607 0.05543427 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER C 0.81 36.8748779296875 0.0
164 164 TYR E 1.0 25.666748046875 0.0
179 179 SER C 0.75 76.85641479492188 0.0
269 269 SER C 0.96 17.003915786743164 0.0
4A51 A X-ray 2.75 7 [ADP]A:601 0.20316343 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER E 0.81 50.205204010009766 0.0
164 164 TYR E 1.0 18.820697784423828 0.0
179 179 SER C 0.75 32.41798782348633 0.0
269 269 SER C 0.96 21.666954040527344 0.0
4A50 A X-ray 2.75 3 A 0.3528251 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER E 0.81 44.87520980834961 0.0
164 164 TYR E 1.0 16.133365631103516 0.0
179 179 SER C 0.75 34.5511589050293 0.0
269 269 SER C 0.96 12.338133811950684 0.0
4BBG A X-ray 2.75 3 A 0.14023134 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER E 0.81 47.62686538696289 0.0
164 164 TYR E 1.0 15.880719184875488 0.0
179 179 SER C 0.75 30.618654251098633 0.0
269 269 SER C 0.96 13.213342666625977 0.0
4A1Z A X-ray 2.799999952316284 2 [ADP]A:2601 0.39598992 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER E 0.81 56.19013977050781 0.0
164 164 TYR E 1.0 35.952022552490234 0.0
179 179 SER C 0.75 52.646751403808594 0.0
269 269 SER C 0.96 21.721454620361328 0.0
3WPN A X-ray 2.799999952316284 Monomer A 0.0 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER E 0.81 64.24061584472656 0.0
164 164 TYR E 1.0 73.5280532836914 0.0
179 179 SER C 0.75 74.46806335449219 0.0
269 269 SER C 0.96 104.40647888183594 0.0
2Q2Z A X-ray 3.0 Monomer [ADP]A:601 0.045464497 179, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER C 0.81 34.23938751220703 0.0
164 164 TYR C 1.0 25.152952194213867 0.0
179 179 SER C 0.75 69.72673034667969 0.0
269 269 SER C 0.96 18.617849349975586 0.0
3ZCW A X-ray 1.690000057220459 Monomer [ADP]A:1364 0.03903597 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
39 39 SER E 0.81 60.001495361328125 0.0
164 164 TYR E 1.0 38.32257080078125 0.0
269 269 SER C 0.96 14.73295783996582 0.0

Mutations

Showing 5 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
144 F L Disease Microcephaly with or without chorioretinopathy, lymphedema, or mental retardation (MCLMR) [MIM:152950]
234 R C Disease Microcephaly with or without chorioretinopathy, lymphedema, or mental retardation (MCLMR) [MIM:152950]
235 S C Disease Microcephaly with or without chorioretinopathy, lymphedema, or mental retardation (MCLMR) [MIM:152950]
944 R C Disease Microcephaly with or without chorioretinopathy, lymphedema, or mental retardation (MCLMR) [MIM:152950]
1042 L F Polymorphism