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Search for the desired protein with Uniprot accession, protein name/keyword, ProteomeXchange ID or PDB id

Ex.: O00571, ddx3x (keyword), ATP-dependent RNA helicase DDX3X, PXD000680 or 3JRV

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PDB 
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Phospho-sites

Showing 11 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
80 SER PRIDE
81 THR PRIDE
83 SER PRIDE
93 THR PRIDE yes
105 THR PRIDE
111 THR PRIDE
119 SER PRIDE
123 THR PRIDE
128 SER PRIDE yes
202 THR PRIDE yes
223 SER UP, PRIDE Combined yes

3D structure is not available

Display Settings

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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
80 79 88 2 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
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
81 79 88 3 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
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
81 80 88 2 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
83 80 88 4 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
93 89 124 5 1
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
105 89 124 17 2
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 -
PXD004415 1 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte
111 89 124 23 3
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004252 13 Modulating the selectivity of affinity absorbents to multi-phosphopeptides by a novel competitive substitution strategy Homo sapiens (Human) PARTIAL 2016-08-03 cell culture -
PXD004415 1 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte
PXD001546 1 Reproducibility of label-free single-shot phosphoproteomics applied to CRC cell lines Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
119 89 124 31 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004252 4 Modulating the selectivity of affinity absorbents to multi-phosphopeptides by a novel competitive substitution strategy Homo sapiens (Human) PARTIAL 2016-08-03 cell culture
119 119 130 1 4
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 4 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 3 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary 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 -
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 -
123 89 124 35 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004252 10 Modulating the selectivity of affinity absorbents to multi-phosphopeptides by a novel competitive substitution strategy Homo sapiens (Human) PARTIAL 2016-08-03 cell culture
128 125 154 4 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001546 1 Reproducibility of label-free single-shot phosphoproteomics applied to CRC cell lines Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
PXD001550 2 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 cell culture
202 199 220 4 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
223 221 231 3 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 11 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
223 222 231 2 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

Structures

Showing 25 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
5AQM B X-ray 1.6299999952316284 Monomer A 0.09415717
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
223 152 SER C 0.84 30.178932189941406 0.0
5AQL B X-ray 1.690000057220459 Monomer A 0.10926489
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
223 152 SER C 0.84 31.004749298095703 0.0
5AQV B X-ray 1.75 2 A 0.69909704
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
223 152 SER C 0.84 30.079822540283203 0.0
5AQF B X-ray 1.8799999952316284 2 A 0.43034223
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
223 152 SER C 0.84 31.88783073425293 0.0
5AQT B X-ray 1.899999976158142 2 A 0.6117492
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
223 152 SER C 0.84 32.65693664550781 0.0
1HX1 B X-ray 1.899999976158142 2 A 0.12973933
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
223 152 SER C 0.84 29.36944007873535 0.0
3LDQ B X-ray 1.899999976158142 2 A 0.07744897
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
223 152 SER C 0.84 36.023284912109375 0.0
5AQR B X-ray 1.909999966621399 2 A 0.23585351
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
223 152 SER C 0.84 32.105777740478516 0.0
5AQU B X-ray 1.9199999570846558 2 A 0.34225255
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
223 152 SER C 0.84 29.638704299926758 0.0
5AQJ B X-ray 1.9600000381469727 2 [GOL]B:1261 0.1
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
223 152 SER C 0.84 26.86125946044922 0.2899036407470703
5AQI B X-ray 1.9800000190734863 Monomer A 0.59044224
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
223 152 SER C 0.84 36.919864654541016 0.0
5AQH B X-ray 2.0 2 A 0.62122446
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
223 152 SER C 0.84 29.885934829711914 0.0
3FZH B X-ray 2.0 Monomer A 0.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
223 152 SER C 0.84 23.29688835144043 0.0
5AQS B X-ray 2.0 2 A 0.7932364
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
223 152 SER C 0.84 35.39970016479492 0.0
5AQP B X-ray 2.0799999237060547 2 A 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
223 152 SER C 0.84 30.449718475341797 0.0
5AQK B X-ray 2.0899999141693115 2 A 0.3834224
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
223 152 SER C 0.84 29.112010955810547 0.0
3FZK B X-ray 2.0999999046325684 2 A 0.03928104
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
223 152 SER C 0.84 28.2617130279541 0.0
3M3Z B X-ray 2.0999999046325684 2 A 0.08216104
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
223 152 SER C 0.84 31.482192993164062 0.0
5AQO B X-ray 2.119999885559082 2 A 0.50188047
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
223 152 SER C 0.84 27.2252254486084 0.0
3FZL B X-ray 2.200000047683716 Monomer A 0.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
223 152 SER C 0.84 26.128225326538086 0.0
3FZF B X-ray 2.200000047683716 Monomer A 0.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
223 152 SER C 0.84 29.990591049194336 0.0
5AQG B X-ray 2.240000009536743 2 A 0.51846826
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
223 152 SER C 0.84 27.474485397338867 0.0
3FZM B X-ray 2.299999952316284 2 A 0.06756386
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
223 152 SER C 0.84 25.21673583984375 0.0
5AQN B X-ray 2.450000047683716 2 A 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
223 152 SER C 0.84 30.5678653717041 0.0
5AQQ B X-ray 2.7200000286102295 2 A 0.28422195
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
223 152 SER C 0.84 28.113609313964844 0.0

Mutations

Showing 0 results

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