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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
426 SER PRIDE
429 THR PRIDE
878 THR PRIDE yes
1433 SER 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 4 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
426 413 436 14 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000218 1 System-level analysis of cancer and stomal cell specific proteomes reveals extensive reprogramming of phosphorylation networks by tumor microenvironment Homo sapiens (Human),Mus musculus (Mouse) COMPLETE 2014-04-01 Epithelial cell, colon
429 413 436 17 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000218 1 System-level analysis of cancer and stomal cell specific proteomes reveals extensive reprogramming of phosphorylation networks by tumor microenvironment Homo sapiens (Human),Mus musculus (Mouse) COMPLETE 2014-04-01 Epithelial cell, colon
878 850 879 29 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
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
1433 1413 1440 21 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 -

Structures

Showing 11 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
4A5W A X-ray 3.5 4 B 1.0 426, 429, 878, 1433
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
162 162 THR E 0.92 3.9998908042907715 0.0
184 184 SER E 0.83 61.797542572021484 0.0
426 426 SER C 0.67 79.03307342529297 0.0
429 429 THR E 0.53 57.641136169433594 24.285396575927734
878 878 THR C 0.3 58.316688537597656 0.0
1433 1433 SER E 0.14 67.3382568359375 0.0
5I5K A X-ray 4.199999809265137 2 B 0.0 426, 429, 878, 1433
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
162 162 THR E 0.92 20.439926147460938 0.0
184 184 SER E 0.83 72.2460708618164 0.0
426 426 SER C 0.67 93.75779724121094 0.0
429 429 THR C 0.53 30.45505142211914 0.0
878 878 THR C 0.3 123.90629577636719 0.0
1433 1433 SER E 0.14 53.54304504394531 0.0
3PVM A X-ray 4.300000190734863 2 B 1.0 426, 429, 878, 1433
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
162 162 THR E 0.92 4.094663619995117 0.0
184 184 SER E 0.83 56.283634185791016 0.0
426 426 SER C 0.67 83.50358581542969 16.883014678955078
429 429 THR E 0.53 40.00328063964844 0.0
878 878 THR E 0.3 94.40365600585938 28.20680809020996
1433 1433 SER E 0.14 42.250518798828125 0.0
3PRX A X-ray 4.300000190734863 4 B 1.0 426, 429, 878, 1433
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
162 162 THR E 0.92 2.9439477920532227 0.0
184 184 SER E 0.83 53.95954132080078 0.0
426 426 SER C 0.67 85.07140350341797 22.627397537231445
429 429 THR E 0.53 39.65498352050781 0.0
878 878 THR C 0.3 74.60176086425781 26.04656410217285
1433 1433 SER E 0.14 32.18600845336914 0.0
5HCC B X-ray 2.5899999141693115 4 A 1.0 426, 429, 1433
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
162 162 THR E 0.92 16.92160415649414 0.0
184 184 SER E 0.83 77.24488067626953 11.688301086425781
426 426 SER C 0.67 82.32218170166016 0.0
429 429 THR E 0.53 45.015106201171875 0.0
1433 1433 SER E 0.14 26.803781509399414 0.0
5HCD B X-ray 2.9800000190734863 4 A 1.0 426, 429, 1433
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
162 162 THR E 0.92 16.207033157348633 0.0
184 184 SER E 0.83 73.53266143798828 12.25012493133545
426 426 SER C 0.67 82.58262634277344 0.0
429 429 THR E 0.53 45.49030685424805 0.0
1433 1433 SER E 0.14 26.6820125579834 0.0
3CU7 A X-ray 3.0999999046325684 2 [CD]A:2006 0.24311356 426, 429, 1433
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
162 162 THR E 0.92 5.139621734619141 0.0
184 184 SER E 0.83 63.09297180175781 0.0
426 426 SER C 0.67 73.01165771484375 0.0
429 429 THR E 0.53 34.43650436401367 0.0
1433 1433 SER E 0.14 30.223188400268555 0.0
5HCE B X-ray 3.119999885559082 4 A 1.0 426, 429, 1433
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
162 162 THR E 0.92 16.912227630615234 0.0
184 184 SER E 0.83 76.21054077148438 13.246825218200684
426 426 SER C 0.67 83.73915100097656 0.0
429 429 THR E 0.53 46.804203033447266 0.0
1433 1433 SER E 0.14 28.939712524414062 0.0
3KLS A X-ray 3.5999999046325684 2 [CD]A:1678 0.26382104 426, 429, 1433
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
162 162 THR E 0.92 6.833795547485352 0.0
184 184 SER E 0.83 64.0455322265625 0.0
426 426 SER C 0.67 79.40756225585938 0.0
429 429 THR E 0.53 25.438539505004883 0.0
1433 1433 SER E 0.14 36.520042419433594 0.0
3KM9 A X-ray 4.199999809265137 Monomer [CD]A:1678 0.089452215 426, 429, 1433
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
162 162 THR C 0.92 8.360465049743652 0.0
184 184 SER C 0.83 73.7640151977539 0.0
426 426 SER C 0.67 67.42837524414062 0.0
429 429 THR C 0.53 18.86094856262207 0.0
1433 1433 SER C 0.14 45.454689025878906 0.0
4E0S A X-ray 4.210000038146973 4 B 1.0 426, 429, 1433
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
162 162 THR E 0.92 7.195971965789795 0.0
184 184 SER E 0.83 64.73674774169922 0.0
426 426 SER C 0.67 63.262454986572266 0.0
429 429 THR E 0.53 38.637577056884766 15.808012962341309
1433 1433 SER C 0.14 36.688045501708984 0.0

Mutations

Showing 17 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
145 V I Polymorphism
354 L M Polymorphism
389 T I Polymorphism
449 R G Polymorphism
518 F S Polymorphism
802 V I Polymorphism
885 R H Polymorphism
928 R Q Polymorphism
933 G V Polymorphism
966 D Y Polymorphism
1033 I T Polymorphism
1037 D N Polymorphism
1043 Q K Polymorphism
1053 M L Polymorphism
1310 S N Polymorphism
1365 V A Polymorphism
1437 E D Polymorphism