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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 4 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
8 TYR PRIDE yes
199 TYR PRIDE yes
243 SER UP Combined
250 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 5 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
8 2 20 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
199 197 206 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
250 239 255 12 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD003531 2 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
250 242 255 9 17
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004252 25 Modulating the selectivity of affinity absorbents to multi-phosphopeptides by a novel competitive substitution strategy Homo sapiens (Human) PARTIAL 2016-08-03 cell culture -
PXD000474 9 Simulated phosphopeptide spectral library for confident site localization Homo sapiens (Human) PARTIAL 2015-03-17 HeLa cell -
PXD004447 1 Mirroring the charged termini; ETD/HCD fragmentation characteristics of LysargiNase and tryptic peptides and their benefits for peptide sequencing in proteomics Homo sapiens (Human) PARTIAL 2016-12-02 cell culture -
PXD003531 142 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD004940 66 Performance of the Orbitrap Fusion Lumos Tribrid in single-shot analyses of human samples Homo sapiens (Human) PARTIAL 2017-03-09 HeLa cell -
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 -
PXD006482 53 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney -
PXD002286 17 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 - -
PXD005366 421 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 -
PXD001374 28 Label-free quantitative phosphoproteomics with novel pairwise abundance normalization reveals synergistic RAS and CIP2A signaling Homo sapiens (Human) PARTIAL 2015-08-24 HeLa cell
PXD004452 30 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
PXD002394 4 Proteomic and phosphoproteomic analysis of cisplatin resistance in patient derived serous ovarian cancer Homo sapiens (Human) PARTIAL 2017-05-02 cell suspension culture -
PXD001550 106 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
PXD000680 86 Stable isotope labeling of phosphoproteins for large-scale phosphorylation rate determination Homo sapiens (Human) COMPLETE 2014-04-15 HeLa cell,HEK-293 cell -
PXD000836 8 HOPE-fixation of lung tissue allows retrospective proteome and phosphoproteome studies Homo sapiens (Human) PARTIAL 2014-05-22 lung -
PXD000612 569 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 35 Reproducibility of label-free single-shot phosphoproteomics applied to CRC cell lines Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
250 246 255 5 4
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 -
PXD003531 7 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 -
PXD004452 4 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -

Structures

Showing 22 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
5LN3 G EM 6.800000190734863 Monomer F 0.0 8, 199, 243
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 8 TYR C 1.0 60.7630500793457 0.0
199 199 TYR H 1.0 36.77065658569336 0.0
243 243 SER H 1.0 62.135536193847656 0.0
5LE5 F X-ray 1.7999999523162842 3 G 0.1500294
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 7 TYR C 1.0 120.49017333984375 61.248348236083984
199 198 TYR H 1.0 25.889904022216797 0.0
243 242 SER H 1.0 40.01272964477539 0.0
5LEY F X-ray 1.899999976158142 2 G 0.15092877
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 7 TYR C 1.0 122.6427993774414 61.80089569091797
199 198 TYR H 1.0 23.954944610595703 0.0
243 242 SER H 1.0 38.34393310546875 0.0
5LF4 F X-ray 1.9900000095367432 2 G 0.14990106
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 7 TYR C 1.0 123.49654388427734 62.594573974609375
199 198 TYR H 1.0 23.99042510986328 0.0
243 242 SER H 1.0 38.17291259765625 0.0
5LF7 F X-ray 2.0 4 G 0.15694144
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 7 TYR C 1.0 123.39689636230469 62.16160202026367
199 198 TYR H 1.0 27.517213821411133 0.0
243 242 SER H 1.0 38.36269760131836 0.0
5LF1 F X-ray 2.0 4 G 0.15765227
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 7 TYR C 1.0 123.49319458007812 64.4405517578125
199 198 TYR H 1.0 25.038923263549805 0.0
243 242 SER H 1.0 39.454498291015625 0.0
5LF6 F X-ray 2.069999933242798 3 G 0.1569598
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 7 TYR C 1.0 126.78948211669922 64.34502410888672
199 198 TYR H 1.0 24.037172317504883 0.0
243 242 SER H 1.0 38.61812973022461 0.0
5LF3 F X-ray 2.0999999046325684 4 G 0.15710993
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 7 TYR C 1.0 123.0212631225586 60.99027633666992
199 198 TYR H 1.0 26.46786880493164 0.0
243 242 SER H 1.0 36.33438491821289 0.0
5LEZ F X-ray 2.190000057220459 22 E 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 7 TYR C 1.0 122.33521270751953 0.0
199 198 TYR H 1.0 27.44106674194336 0.0
243 242 SER H 1.0 38.95928955078125 0.0
5LEX F X-ray 2.200000047683716 28 E 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 7 TYR C 1.0 124.79547882080078 0.0
199 198 TYR H 1.0 27.078136444091797 0.0
243 242 SER H 1.0 38.49877166748047 0.0
5LF0 F X-ray 2.4100000858306885 4 G 0.15843356
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 7 TYR C 1.0 124.13166046142578 61.64921569824219
199 198 TYR H 1.0 24.858991622924805 0.0
243 242 SER H 1.0 40.794189453125 0.0
4R3O G X-ray 2.5999999046325684 28 F 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 7 TYR C 1.0 86.4308090209961 0.0
199 198 TYR H 1.0 32.087955474853516 0.0
243 242 SER H 1.0 44.02053451538086 0.0
4R67 G X-ray 2.890000104904175 28 A 0.33184355
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 7 TYR C 1.0 86.6644058227539 59.62923049926758
199 198 TYR H 1.0 27.41315269470215 0.0
243 242 SER H 1.0 41.18548583984375 0.0
5A0Q G EM 3.5 Monomer F 0.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
199 198 TYR H 1.0 130.4452667236328 0.0
5DSV A X-ray 3.75 14 B 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 7 TYR C 1.0 82.73747253417969 49.890960693359375
199 198 TYR H 1.0 23.2523250579834 0.0
243 242 SER H 1.0 28.800472259521484 0.0
6AVO J EM 3.799999952316284 Monomer K 0.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 7 TYR C 1.0 131.9983367919922 75.54135131835938
199 198 TYR H 1.0 34.72663497924805 0.0
243 242 SER H 1.0 36.14164733886719 0.0
5M32 F EM 3.799999952316284 Monomer E 0.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 7 TYR C 1.0 131.08599853515625 0.0
199 198 TYR H 1.0 39.8218994140625 0.0
5T0G M EM 4.400000095367432 Monomer G 0.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 7 TYR C 1.0 107.0414047241211 67.28424072265625
199 198 TYR H 1.0 85.6659164428711 0.0
243 242 SER C 1.0 19.3565673828125 0.0
5GJQ X EM 4.5 7 B 0.47161484
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 7 TYR C 1.0 88.71818542480469 65.3950424194336
199 198 TYR H 1.0 33.744449615478516 0.0
243 242 SER H 1.0 46.512413024902344 0.0
5T0H M EM 6.800000190734863 Monomer G 0.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 7 TYR C 1.0 130.13059997558594 68.77034759521484
199 198 TYR H 1.0 65.31051635742188 0.0
243 242 SER C 1.0 30.83257293701172 0.0
5T0J M EM 8.0 Monomer G 0.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 7 TYR C 1.0 114.13436889648438 58.8617057800293
199 198 TYR H 1.0 99.78187561035156 0.0
243 242 SER C 1.0 4.903552532196045 0.0
5T0I M EM 8.0 Monomer G 0.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 7 TYR C 1.0 110.7437973022461 75.32270050048828
199 198 TYR H 1.0 123.23128509521484 0.0
243 242 SER C 1.0 16.309146881103516 0.0

Mutations

Showing 0 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease