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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
117 PhosphoS UP Combined
340 PhosphoS UP, PRIDE Combined yes
351 PhosphoT PRIDE yes
495 PhosphoS UP, PRIDE Combined yes
499 PhosphoS UP, PRIDE Combined yes
564 PhosphoS UP, PRIDE Combined yes
577 PhosphoS 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 7 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
340 334 350 7 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD006482 1 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney
351 351 376 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
495 493 502 3 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD000612 6 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 2 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
499 493 502 7 3
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD000612 5 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 3 Anion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC Homo sapiens (Human) PARTIAL 2015-04-23 HeLa cell
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 -
564 558 572 7 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD000612 3 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
564 558 573 7 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD000612 3 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
577 574 590 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

Structures

Showing 22 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
3MI9 B X-ray 2.0999999046325684 3 A 0.8824995 117
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
117 117 SER C 0.79 86.2006607055664 0.0
3BLH B X-ray 2.4800000190734863 2 A 1.0 117
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
117 117 SER C 0.79 95.06855773925781 0.0
2PK2 A X-ray 2.6700000762939453 Monomer B 0.0 117
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
117 117 SER C 0.79 104.3399658203125 0.0
3BLR B X-ray 2.799999952316284 2 A 0.38377398 117
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
117 117 SER C 0.79 93.00847625732422 0.0
3MY1 B X-ray 2.799999952316284 2 A 0.3443814 117
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
117 117 SER C 0.79 95.02152252197266 0.0
3BLQ B X-ray 2.9000000953674316 2 A 0.6194015 117
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
117 117 SER C 0.79 97.21858215332031 0.0
4OR5 B X-ray 2.9000000953674316 16 E 0.53751355 117
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
117 117 SER C 0.79 85.44432830810547 0.0
4IMY B X-ray 2.940000057220459 3 G 1.0 117
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
117 117 SER C 0.79 99.69664764404297 0.0
3TN8 B X-ray 2.950000047683716 2 A 0.4425811 117
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
117 117 SER C 0.79 94.6428451538086 0.0
4BCH B X-ray 2.9600000381469727 2 A 0.46220705 117
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
117 117 SER C 0.79 95.96121215820312 0.0
4OGR B X-ray 3.0 4 C 1.0 117
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
117 117 SER C 0.79 98.05264282226562 0.0
3MIA B X-ray 3.0 3 A 0.5417807 117
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
117 117 SER C 0.79 88.01565551757812 0.0
3LQ5 B X-ray 3.0 2 A 1.0 117
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
117 117 SER C 0.79 99.51414489746094 0.0
4BCF B X-ray 3.009999990463257 2 A 0.579091 117
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
117 117 SER C 0.79 94.1916732788086 0.0
4BCG B X-ray 3.0799999237060547 2 A 0.65419066 117
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
117 117 SER C 0.79 96.2520523071289 0.0
4BCI B X-ray 3.0999999046325684 2 A 0.955918 117
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
117 117 SER C 0.79 99.18821716308594 0.0
4BCJ B X-ray 3.1600000858306885 2 A 0.57391685 117
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
117 117 SER C 0.79 98.1202621459961 0.0
3TNH B X-ray 3.200000047683716 2 A 1.0 117
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
117 117 SER C 0.79 95.5954818725586 0.0
4EC9 B X-ray 3.2100000381469727 2 A 1.0 117
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
117 117 SER C 0.79 93.83010864257812 0.0
3TNI B X-ray 3.2300000190734863 2 A 1.0 117
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
117 117 SER C 0.79 97.03816223144531 0.0
4EC8 B X-ray 3.5999999046325684 2 A 1.0 117
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
117 117 SER C 0.79 94.40605926513672 0.0
5L1Z B X-ray 5.900000095367432 4 C 0.9984581 117
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
117 117 SER C 0.79 92.78097534179688 0.0

Mutations

Showing 2 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
362 H R Polymorphism
541 R C Polymorphism