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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
56 PhosphoS UP, PRIDE Similarity yes
103 PhosphoT PRIDE yes
139 PhosphoT PRIDE yes
220 PhosphoT PRIDE yes
484 PhosphoS PRIDE
485 PhosphoS PRIDE
520 PhosphoS PRIDE yes
566 PhosphoS UP, PRIDE Combined yes
588 PhosphoS 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 14 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
56 34 60 23 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD004452 4 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
56 34 62 23 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
103 97 114 7 6
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 -
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 -
PXD001333 2 Anion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC Homo sapiens (Human) PARTIAL 2015-04-23 HeLa cell -
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 -
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 -
103 97 115 7 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD001550 6 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 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 -
103 99 115 5 3
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 -
PXD001546 2 Reproducibility of label-free single-shot phosphoproteomics applied to CRC cell lines Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
PXD001550 4 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 cell culture
103 99 114 5 5
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD000612 23 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
PXD004940 1 Performance of the Orbitrap Fusion Lumos Tribrid in single-shot analyses of human samples Homo sapiens (Human) PARTIAL 2017-03-09 HeLa cell -
PXD001333 4 Anion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC Homo sapiens (Human) PARTIAL 2015-04-23 HeLa cell -
PXD005366 6 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 5 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
139 131 150 9 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD003531 3 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
220 218 224 3 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
484 475 493 10 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 -
485 475 493 11 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 -
520 514 529 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
566 542 569 25 2
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 -
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
566 560 569 7 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD003531 11 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
588 570 596 19 11
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 -
PXD001060 2 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell -
PXD000612 15 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 5 Reproducibility of label-free single-shot phosphoproteomics applied to CRC cell lines Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
PXD004415 11 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte -
PXD000474 2 Simulated phosphopeptide spectral library for confident site localization Homo sapiens (Human) PARTIAL 2015-03-17 HeLa cell -
PXD003531 5 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD004940 1 Performance of the Orbitrap Fusion Lumos Tribrid in single-shot analyses of human samples Homo sapiens (Human) PARTIAL 2017-03-09 HeLa cell -
PXD004452 10 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
PXD001550 9 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 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 -

Structures

Showing 31 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
5JI8 A X-ray 1.4199999570846558 Monomer A 0.0 139, 220
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
139 139 THR C 0.92 85.74383544921875 0.0
220 220 THR C 1.0 38.46015548706055 0.0
5IGM A X-ray 1.600000023841858 2 B 0.4692754 139, 220
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
139 139 THR C 0.92 47.43905258178711 2.19191837310791
220 220 THR C 1.0 43.4987678527832 0.0
5E9V A X-ray 1.7999999523162842 2 B 0.5409832 139, 220
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
139 139 THR C 0.92 50.71784973144531 2.189161777496338
220 220 THR C 1.0 39.06135559082031 0.0
5TWX A X-ray 2.549999952316284 8 B 0.71386206 139, 220
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
139 139 THR C 0.92 36.476009368896484 0.0
220 220 THR C 1.0 35.41261291503906 0.0
5I40 A X-ray 1.0399999618530273 Monomer A 0.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
139 23 THR C 0.92 52.116127014160156 0.0
220 104 THR C 1.0 39.92900466918945 0.0
5I7X A X-ray 1.1799999475479126 Monomer [67B]A:201 0.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
139 23 THR C 0.92 52.22156524658203 0.0
220 104 THR C 1.0 40.61027526855469 0.0
4UIT A X-ray 1.2999999523162842 1 [N1D]A:1123 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
139 23 THR C 0.92 52.3869514465332 0.0
220 104 THR C 1.0 42.234378814697266 14.657838821411133
5I7Y A X-ray 1.4500000476837158 Monomer [69G]A:201 0.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
139 23 THR C 0.92 44.525482177734375 0.0
220 104 THR C 1.0 39.12337875366211 0.0
4YY6 A X-ray 1.4500000476837158 2 Z 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
139 23 THR C 0.92 54.63253402709961 0.0
220 104 THR C 1.0 39.15827178955078 2.1528472900390625
4YY4 A X-ray 1.4700000286102295 Monomer [DMS]A:201 0.1
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
139 23 THR C 0.92 129.57823181152344 0.0
220 104 THR C 1.0 40.92400360107422 0.0
4YYI A X-ray 1.5 2 C 0.1
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
139 23 THR C 0.92 89.77444458007812 0.0
220 104 THR C 1.0 37.955448150634766 0.0
4YYD A X-ray 1.5199999809265137 2 Z 0.42984176
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
139 23 THR C 0.92 133.21585083007812 0.0
220 104 THR C 1.0 40.25299835205078 0.0
5EU1 A X-ray 1.600000023841858 2 B 0.94469494
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
139 23 THR C 0.92 52.66425323486328 1.8762025833129883
220 104 THR C 1.0 44.63794708251953 0.0
4UIU A X-ray 1.6399999856948853 Monomer [TVU]A:1123 0.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
139 23 THR C 0.92 53.2188606262207 0.0
220 104 THR C 1.0 40.573062896728516 16.844125747680664
5MKY A X-ray 1.6699999570846558 1 [I0D]A:201 0.65831065
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
139 23 THR C 0.92 54.38948440551758 0.0
220 104 THR C 1.0 46.48126983642578 0.0
5F25 A X-ray 1.6799999475479126 2 B 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
139 23 THR C 0.92 54.85215759277344 1.7222768068313599
220 104 THR C 1.0 43.812644958496094 0.0
4XY8 A X-ray 1.7000000476837158 2 [BR]A:202 0.5351617
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
139 23 THR C 0.92 59.68849563598633 0.0
220 104 THR C 1.0 37.16370391845703 14.398327827453613
5IGN A X-ray 1.7000000476837158 2 [6B2]A:201 0.62827927
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
139 23 THR C 0.92 58.25712966918945 0.0
220 104 THR C 1.0 24.442846298217773 0.0
4UIV A X-ray 1.7200000286102295 Monomer [XZB]A:1124 0.1
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
139 23 THR C 0.92 49.206947326660156 0.0
220 104 THR C 1.0 36.59488296508789 19.05047607421875
4NQN A X-ray 1.7300000190734863 Monomer [Y1Z]A:201 0.1
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
139 23 THR C 0.92 60.504180908203125 0.0
220 104 THR C 1.0 42.08539581298828 0.0
4UIW A X-ray 1.7300000190734863 Monomer [H1B]A:1124 0.1
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
139 23 THR C 0.92 50.87958526611328 0.0
220 104 THR C 1.0 36.94724655151367 19.892593383789062
4YYH A X-ray 1.7400000095367432 Monomer [KCR]Z:8 0.1
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
139 23 THR C 0.92 56.38180923461914 0.0
220 104 THR C 1.0 37.62078857421875 0.0
4YYK A X-ray 1.7899999618530273 Monomer [KCR]C:8 0.1
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
139 23 THR C 0.92 55.70934295654297 0.0
220 104 THR C 1.0 38.71343994140625 0.0
4Z6H A X-ray 1.7999999523162842 2 B 0.50728804
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
139 23 THR C 0.92 56.242984771728516 0.8259549140930176
220 104 THR C 1.0 40.963741302490234 0.0
5F2P A X-ray 1.7999999523162842 2 B 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
139 23 THR C 0.92 55.012142181396484 1.718088984489441
220 104 THR C 1.0 42.824947357177734 0.0
5F1H A X-ray 1.8200000524520874 2 B 0.94862014
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
139 23 THR C 0.92 55.37758255004883 1.2494637966156006
220 104 THR C 1.0 43.821102142333984 0.0
4YYJ A X-ray 1.850000023841858 2 C 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
139 23 THR C 0.92 59.15996170043945 0.0
220 104 THR C 1.0 39.30817413330078 0.16792519390583038
4Z6I A X-ray 1.9500000476837158 4 B 0.49405095
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
139 23 THR C 0.92 52.22126770019531 2.5304861068725586
220 104 THR C 1.0 40.01523971557617 0.0
4YYG A X-ray 2.0999999046325684 2 B 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
139 23 THR C 0.92 108.2193832397461 0.0
220 104 THR C 1.0 41.74695587158203 0.0
3HME A X-ray 2.2300000190734863 2 B 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
139 23 THR C 0.92 53.62905502319336 3.507596015930176
220 104 THR C 1.0 40.162261962890625 0.0
5F1L A X-ray 2.299999952316284 2 B 0.964435
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
139 23 THR C 0.92 57.88070297241211 1.572604775428772
220 104 THR C 1.0 46.515621185302734 0.0

Mutations

Showing 3 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
170 A T Polymorphism
266 A T Polymorphism
389 A T Polymorphism