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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 9 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
202 PhosphoS PRIDE yes
208 PhosphoY PRIDE yes
220 PhosphoY PRIDE yes
264 PhosphoS PRIDE yes
290 PhosphoY PRIDE yes
295 PhosphoT PRIDE yes
314 PhosphoS PRIDE yes
432 PhosphoS PRIDE yes
565 PhosphoS PRIDE 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 9 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
202 200 225 3 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
208 208 225 1 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD001565 2 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain -
PXD006482 2 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney
220 196 225 25 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
264 255 266 10 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD002286 2 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 -
290 286 294 5 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD001565 1 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain
295 295 305 1 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
314 312 331 3 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD002286 2 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 -
432 427 437 6 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
565 553 569 13 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 5 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
5UZ0 A X-ray 1.7899999618530273 2 B 0.7094466 202, 208, 220, 264, 290, 295, 314, 432, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
112 112 SER C 0.74 53.106380462646484 0.0
202 202 SER C 1.0 6.574075698852539 5.414546012878418
208 208 TYR C 1.0 70.66834259033203 16.570653915405273
220 220 TYR E 0.97 96.393310546875 78.21711730957031
264 264 SER E 0.95 0.0 0.0
290 290 TYR H 0.51 95.74138641357422 0.0
295 295 THR H 0.82 77.81314849853516 0.0
314 314 SER C 1.0 0.0 0.0
432 432 SER C 1.0 0.0 0.0
565 565 SER C 1.0 18.63020133972168 0.0
1PKX A X-ray 1.899999976158142 2 B 0.9085814 202, 208, 220, 264, 290, 295, 314, 432, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
112 112 SER C 0.74 52.79521942138672 0.0
202 202 SER C 1.0 5.244266033172607 3.078259229660034
208 208 TYR C 1.0 79.76040649414062 13.912674903869629
220 220 TYR E 0.97 96.70635223388672 76.86869812011719
264 264 SER E 0.95 0.0 0.0
290 290 TYR H 0.51 85.59703063964844 0.0
295 295 THR H 0.82 80.45645904541016 0.0
314 314 SER C 1.0 0.0 0.0
432 432 SER C 1.0 0.0 0.0
565 565 SER C 1.0 21.173057556152344 0.0
5UY8 A X-ray 2.390000104904175 2 B 0.7159884 202, 208, 220, 264, 290, 295, 314, 432, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
112 112 SER C 0.74 50.52082443237305 0.0
202 202 SER C 1.0 6.107992172241211 4.57618522644043
208 208 TYR C 1.0 67.22330474853516 17.44317054748535
220 220 TYR E 0.97 98.70999145507812 79.06420135498047
264 264 SER E 0.95 0.0 0.0
290 290 TYR H 0.51 92.70784759521484 0.0
295 295 THR H 0.82 72.28126525878906 0.0
314 314 SER C 1.0 0.0 0.0
432 432 SER C 1.0 0.0 0.0
565 565 SER C 1.0 14.7860689163208 0.0
1P4R A X-ray 2.549999952316284 2 B 0.78093946 202, 208, 220, 264, 290, 295, 314, 432, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
112 112 SER C 0.74 46.51174545288086 0.0
202 202 SER C 1.0 5.9942426681518555 4.494541645050049
208 208 TYR C 1.0 70.8812484741211 14.153717041015625
220 220 TYR E 0.97 95.33861541748047 76.57624053955078
264 264 SER E 0.95 0.0 0.0
290 290 TYR H 0.51 96.36638641357422 0.0
295 295 THR H 0.82 81.23319244384766 0.0
314 314 SER C 1.0 0.0 0.0
432 432 SER C 1.0 0.0 0.0
565 565 SER C 1.0 18.47101402282715 0.0
1PL0 A X-ray 2.5999999046325684 2 B 0.83041793 202, 208, 220, 264, 290, 295, 314, 432, 565
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
112 112 SER C 0.74 52.05244064331055 0.0
202 202 SER C 1.0 6.133419990539551 3.1808254718780518
208 208 TYR C 1.0 70.72863006591797 16.359987258911133
220 220 TYR E 0.97 104.74246215820312 74.07795715332031
264 264 SER E 0.95 0.0 0.0
290 290 TYR H 0.51 105.0682373046875 0.0
295 295 THR H 0.82 78.41072082519531 0.0
314 314 SER C 1.0 0.12265688180923462 0.0
432 432 SER C 1.0 0.0 0.0
565 565 SER C 1.0 26.3273868560791 0.0

Mutations

Showing 2 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
116 T S Polymorphism
426 K R Disease AICAR transformylase/IMP cyclohydrolase deficiency (AICAR) [MIM:608688]