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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 3 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
320 TYR PRIDE
322 THR UP, PRIDE Similarity
326 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 3 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
320 302 335 19 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001550 1 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 cell culture
322 302 335 21 4
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD002286 5 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 - -
PXD001550 20 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 cell culture
PXD004452 4 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
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 -
326 302 335 25 4
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
PXD002286 14 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 - -
PXD001550 87 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
PXD000680 14 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 14 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
3X01 A X-ray 2.1500000953674316 2 B 0.64847887
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
44 44 SER H 1.0 1.9623976945877075 0.0
404 404 SER H 1.0 1.1122231483459473 0.0
3X02 A X-ray 2.450000047683716 4 B 0.51958656
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
44 44 SER H 1.0 0.9817078709602356 0.0
404 404 SER H 1.0 10.524450302124023 0.0
3X05 A X-ray 2.5 2 B 0.6717609
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
44 44 SER H 1.0 1.3516449928283691 0.0
404 404 SER H 1.0 1.8675791025161743 0.0
3X0C A X-ray 2.549999952316284 4 B 0.7173956
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
44 44 SER H 1.0 1.7160935401916504 0.0
404 404 SER H 1.0 8.814216613769531 0.0
3WZZ A X-ray 2.5999999046325684 2 B 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
44 44 SER H 1.0 1.473779559135437 0.0
404 404 SER H 1.0 0.0 0.0
3X0B A X-ray 2.5999999046325684 2 B 0.7289829
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
44 44 SER H 1.0 0.12166932225227356 0.0
404 404 SER H 1.0 3.955845594406128 0.0
3X07 A X-ray 2.5999999046325684 2 B 0.8350107
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
44 44 SER H 1.0 1.3484822511672974 0.0
404 404 SER H 1.0 4.170758247375488 0.0
3X0A A X-ray 2.5999999046325684 2 B 0.65617514
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
44 44 SER H 1.0 1.349469780921936 0.0
404 404 SER H 1.0 9.765579223632812 0.0
3X04 A X-ray 2.5999999046325684 2 B 0.5821165
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
44 44 SER H 1.0 1.4713091850280762 0.0
404 404 SER H 1.0 9.159406661987305 0.0
3X06 A X-ray 2.6500000953674316 2 B 0.6565149
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
44 44 SER H 1.0 1.105347990989685 0.0
404 404 SER H 1.0 9.553510665893555 0.0
3X09 A X-ray 2.700000047683716 2 B 0.7037483
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
44 44 SER H 1.0 1.7193996906280518 0.0
404 404 SER H 1.0 3.1006178855895996 0.0
3X03 A X-ray 2.700000047683716 2 B 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
44 44 SER H 1.0 1.228004813194275 0.0
404 404 SER H 1.0 5.3620734214782715 0.0
3X08 A X-ray 2.75 2 B 0.7708333
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
44 44 SER H 1.0 1.4726030826568604 0.0
404 404 SER H 1.0 7.3936004638671875 0.0
1BO1 A X-ray 3.0 2 B 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
44 44 SER H 1.0 0.2447987049818039 0.0
404 404 SER H 1.0 12.625908851623535 0.0

Mutations

Showing 0 results

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