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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 5 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
72 THR PRIDE yes
264 THR PRIDE yes
272 THR PRIDE
274 THR PRIDE
399 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 6 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
72 66 76 7 4
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 -
PXD003531 12 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 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
72 66 81 7 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
264 264 271 1 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
272 272 278 1 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
274 272 278 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
399 395 403 5 8
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001060 20 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell -
PXD004252 12 Modulating the selectivity of affinity absorbents to multi-phosphopeptides by a novel competitive substitution strategy Homo sapiens (Human) PARTIAL 2016-08-03 cell culture -
PXD003531 50 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
PXD004940 6 Performance of the Orbitrap Fusion Lumos Tribrid in single-shot analyses of human samples Homo sapiens (Human) PARTIAL 2017-03-09 HeLa cell -
PXD006482 2 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney -
PXD005366 7 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 -
PXD000680 3 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 9 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
5K7M B X-ray 1.649999976158142 2 A 1.0 264, 272, 274, 399
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
264 264 THR E 1.0 6.1672682762146 0.0
272 272 THR C 1.0 68.57270812988281 0.0
274 274 THR C 1.0 19.018964767456055 0.0
399 399 SER C 0.88 140.87718200683594 29.561534881591797
5K7W B X-ray 1.649999976158142 2 A 1.0 264, 272, 274, 399
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
264 264 THR E 1.0 2.098762273788452 0.0
272 272 THR C 1.0 75.92576599121094 0.0
274 274 THR C 1.0 15.9554443359375 0.0
399 399 SER C 0.88 144.91380310058594 30.231264114379883
5K7U B X-ray 1.7000000476837158 2 A 1.0 264, 272, 274, 399
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
264 264 THR E 1.0 2.0990066528320312 0.0
272 272 THR C 1.0 64.85404205322266 0.0
274 274 THR C 1.0 29.73371696472168 0.0
399 399 SER C 0.88 154.25120544433594 30.15894889831543
5IL2 B X-ray 1.6100000143051147 2 A 1.0 264, 272, 274
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
264 264 THR E 1.0 5.8310651779174805 0.0
272 272 THR C 1.0 76.2702407836914 0.0
274 274 THR C 1.0 83.05854797363281 22.227102279663086
5IL1 B X-ray 1.7100000381469727 2 A 1.0 264, 272, 274
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
264 264 THR E 1.0 5.786099433898926 0.0
272 272 THR C 1.0 67.57711791992188 0.0
274 274 THR C 1.0 75.32847595214844 10.71795654296875
5IL0 B X-ray 1.8799999952316284 4 A 0.87965465 264, 272, 274
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
264 264 THR E 1.0 5.874245643615723 0.0
272 272 THR C 1.0 90.75579833984375 0.0
274 274 THR C 1.0 91.64360809326172 0.0
5TEY B X-ray 1.7999999523162842 2 A 0.40646207 264, 272
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
264 264 THR E 1.0 4.624479293823242 0.0
272 272 THR C 1.0 85.12245178222656 0.0
5L6D B X-ray 1.850000023841858 2 A 0.83050203 264
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
264 264 THR E 1.0 5.631591320037842 0.0
5L6E B X-ray 1.899999976158142 2 A 0.8294995 264
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
264 264 THR E 1.0 5.9201788902282715 0.0

Mutations

Showing 0 results

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