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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 7 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
7 PhosphoS PRIDE yes
175 PhosphoS UP Experimental
185 PhosphoY PRIDE yes
186 PhosphoT UP, PRIDE Combined yes
347 PhosphoS UP, PRIDE Combined yes
362 PhosphoT UP, PRIDE Experimental yes
363 PhosphoT UP, PRIDE Experimental 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 8 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
7 4 18 4 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD005366 1 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
185 179 188 7 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD003531 9 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
186 179 188 8 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD003531 1 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
347 344 358 4 8
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD001060 7 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell -
PXD001546 8 Reproducibility of label-free single-shot phosphoproteomics applied to CRC cell lines Homo sapiens (Human) PARTIAL 2015-04-15 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 -
PXD005366 4 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 -
PXD002394 1 Proteomic and phosphoproteomic analysis of cisplatin resistance in patient derived serous ovarian cancer Homo sapiens (Human) PARTIAL 2017-05-02 cell suspension culture -
PXD004452 3 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
PXD000680 7 Stable isotope labeling of phosphoproteins for large-scale phosphorylation rate determination Homo sapiens (Human) COMPLETE 2014-04-15 HeLa cell,HEK-293 cell -
347 345 358 3 6
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD001060 22 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell
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 -
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 -
PXD005366 17 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 -
PXD001550 4 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
PXD000680 17 Stable isotope labeling of phosphoproteins for large-scale phosphorylation rate determination Homo sapiens (Human) COMPLETE 2014-04-15 HeLa cell,HEK-293 cell -
347 346 358 2 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD000612 9 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 1 Anion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC Homo sapiens (Human) PARTIAL 2015-04-23 HeLa cell
362 359 370 4 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
363 359 370 5 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

Structures

Showing 21 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
3MY1 A X-ray 2.799999952316284 2 B 0.3443814 7, 175, 185
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
7 7 SER C 0.77 106.45809173583984 6.662539482116699
175 175 SER C 1.0 64.35103607177734 0.0
185 185 TYR C 1.0 13.176512718200684 0.0
3BLR A X-ray 2.799999952316284 2 B 0.38377398 7, 175, 185
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
7 7 SER C 0.77 171.8199462890625 30.666339874267578
175 175 SER C 1.0 65.83990478515625 0.0
185 185 TYR C 1.0 12.68930721282959 0.0
3BLQ A X-ray 2.9000000953674316 2 B 0.6194015 7, 175, 185
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
7 7 SER C 0.77 174.175048828125 27.78719711303711
175 175 SER C 1.0 118.20606994628906 0.0
185 185 TYR C 1.0 16.781023025512695 0.0
4BCH A X-ray 2.9600000381469727 2 B 0.46220705 7, 175, 185
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
7 7 SER C 0.77 151.5660400390625 27.560083389282227
175 175 SER C 1.0 55.28863525390625 0.0
185 185 TYR C 1.0 10.401883125305176 0.0
3LQ5 A X-ray 3.0 2 B 1.0 7, 175, 185
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
7 7 SER C 0.77 110.88184356689453 9.273591995239258
175 175 SER C 1.0 57.11975860595703 0.0
185 185 TYR C 1.0 15.20363998413086 0.0
4BCF A X-ray 3.009999990463257 2 B 0.579091 7, 175, 185
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
7 7 SER C 0.77 113.2487564086914 2.699401617050171
175 175 SER C 1.0 60.09761428833008 0.0
185 185 TYR C 1.0 10.638753890991211 0.0
4BCG A X-ray 3.0799999237060547 2 B 0.65419066 7, 175, 185
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
7 7 SER C 0.77 151.30262756347656 25.91080665588379
175 175 SER C 1.0 65.62841033935547 0.0
185 185 TYR C 1.0 11.93514633178711 0.0
4BCI A X-ray 3.0999999046325684 2 B 0.955918 7, 175, 185
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
7 7 SER C 0.77 117.9443359375 2.72725248336792
175 175 SER C 1.0 62.30040740966797 0.0
185 185 TYR C 1.0 14.028154373168945 0.0
4BCJ A X-ray 3.1600000858306885 2 B 0.57391685 7, 175, 185
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
7 7 SER C 0.77 111.68643188476562 4.660714149475098
175 175 SER C 1.0 60.336708068847656 0.0
185 185 TYR C 1.0 12.29325008392334 0.0
4EC9 A X-ray 3.2100000381469727 2 B 1.0 7, 175, 185
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
7 7 SER C 0.77 166.38201904296875 14.751070976257324
175 175 SER C 1.0 60.71758270263672 0.0
185 185 TYR C 1.0 11.477869987487793 0.0
3TNI A X-ray 3.2300000190734863 2 B 1.0 7, 175, 185
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
7 7 SER C 0.77 176.6660919189453 14.018708229064941
175 175 SER C 1.0 116.2719497680664 0.0
185 185 TYR C 1.0 20.072229385375977 0.0
4EC8 A X-ray 3.5999999046325684 2 B 1.0 7, 175, 185
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
7 7 SER C 0.77 105.67616271972656 4.938658714294434
175 175 SER C 1.0 70.16648864746094 0.0
185 185 TYR C 1.0 13.510327339172363 0.0
3MI9 A X-ray 2.0999999046325684 3 B 0.8824995 175, 185
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
175 175 SER C 1.0 55.73612594604492 0.0
185 185 TYR C 1.0 11.451619148254395 0.0
3BLH A X-ray 2.4800000190734863 2 B 1.0 175, 185
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
175 175 SER C 1.0 62.28628158569336 0.0
185 185 TYR C 1.0 11.468744277954102 0.0
4OR5 A X-ray 2.9000000953674316 16 [SO4]A:404 0.29068416 175, 185
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
175 175 SER C 1.0 60.579837799072266 0.0
185 185 TYR C 1.0 15.450339317321777 0.0
4IMY A X-ray 2.940000057220459 3 B 0.79989326 175, 185
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
175 175 SER C 1.0 45.482486724853516 0.0
185 185 TYR C 1.0 13.034912109375 0.0
3TN8 A X-ray 2.950000047683716 2 B 0.4425811 175, 185
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
175 175 SER C 1.0 69.65309143066406 0.0
185 185 TYR C 1.0 12.752616882324219 0.0
3MIA A X-ray 3.0 3 B 0.5417807 175, 185
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
175 175 SER C 1.0 57.699745178222656 0.0
185 185 TYR C 1.0 9.181069374084473 0.0
4OGR A X-ray 3.0 4 B 1.0 175, 185
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
175 175 SER C 1.0 49.18510818481445 0.0
185 185 TYR C 1.0 8.51563835144043 0.0
3TNH A X-ray 3.200000047683716 2 B 1.0 175, 185
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
175 175 SER C 1.0 118.85344696044922 0.0
185 185 TYR C 1.0 21.777782440185547 0.0
5L1Z A X-ray 5.900000095367432 4 B 0.99660367 175, 185
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
175 175 SER C 1.0 58.381195068359375 0.0
185 185 TYR C 1.0 11.365005493164062 0.0

Mutations

Showing 2 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
59 F L Polymorphism
231 G A Polymorphism