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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 6 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
8 SER PRIDE yes
67 SER PRIDE yes
299 SER UP, PRIDE Combined yes
318 SER UP Experimental
349 SER UP, PRIDE Combined yes
351 THR 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 6 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
8 8 15 1 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
67 65 73 3 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
299 297 308 3 4
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001060 4 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell
PXD000836 1 HOPE-fixation of lung tissue allows retrospective proteome and phosphoproteome studies Homo sapiens (Human) PARTIAL 2014-05-22 lung -
PXD003531 3 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD006482 2 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney -
349 336 357 14 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 24 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
349 346 357 4 8
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004252 2 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 1 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell -
PXD000612 24 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 -
PXD002286 37 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 - -
PXD005366 5 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 2 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
PXD000680 4 Stable isotope labeling of phosphoproteins for large-scale phosphorylation rate determination Homo sapiens (Human) COMPLETE 2014-04-15 HeLa cell,HEK-293 cell -
351 346 357 6 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD002286 3 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 -

Structures

Showing 7 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
2A2A A X-ray 1.4700000286102295 2 [NA]A:3178 0.33007535
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
67 57 SER C 0.2 10.695772171020508 0.0
299 289 SER C 0.45 14.010531425476074 0.0
1WRZ B X-ray 2.0 2 A 0.38856247
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
318 308 SER H 0.47 54.880577087402344 54.22863006591797
2CKE A X-ray 2.799999952316284 Monomer B 0.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
67 57 SER C 0.2 15.082134246826172 7.843157768249512
299 289 SER C 0.45 16.787715911865234 0.0
1ZWS A X-ray 2.9000000953674316 Monomer B 0.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
67 57 SER C 0.2 15.987996101379395 8.174270629882812
2A27 A X-ray 3.0 Monomer [DTT]A:1001 0.1
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
67 57 SER C 0.2 10.032661437988281 0.0
299 289 SER C 0.45 13.243245124816895 0.0
1WMK A X-ray 3.5999999046325684 Monomer E 0.1
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
67 57 SER C 0.2 28.388010025024414 22.65802574157715
299 289 SER C 0.45 10.846330642700195 0.0
1Z9X A X-ray 3.930000066757202 Monomer B 0.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
67 57 SER C 0.2 19.038015365600586 12.57166862487793
299 289 SER C 0.45 15.231247901916504 0.0

Mutations

Showing 2 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
60 R W Polymorphism
271 R W Polymorphism