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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 11 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
10 SER UP, PRIDE Combined yes
97 SER PRIDE yes
111 SER PRIDE
112 SER UP, PRIDE Combined
125 TYR PRIDE yes
241 TYR PRIDE yes
298 SER PRIDE yes
320 SER PRIDE yes
394 SER PRIDE yes
506 SER UP Experimental
723 TYR 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 16 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
10 2 17 9 3
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 18 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
PXD000680 5 Stable isotope labeling of phosphoproteins for large-scale phosphorylation rate determination Homo sapiens (Human) COMPLETE 2014-04-15 HeLa cell,HEK-293 cell -
97 94 101 4 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
111 105 117 7 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 14 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
111 105 130 7 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 17 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
111 107 130 5 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 54 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
111 107 117 5 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 31 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 2 Anion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC Homo sapiens (Human) PARTIAL 2015-04-23 HeLa cell
112 105 130 8 4
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 69 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 5 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD005366 2 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
PXD004452 6 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
112 105 117 8 4
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 135 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 5 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD001333 27 Anion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC Homo sapiens (Human) PARTIAL 2015-04-23 HeLa cell -
PXD004452 11 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
112 107 130 6 5
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 217 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 53 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD001333 11 Anion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC Homo sapiens (Human) PARTIAL 2015-04-23 HeLa cell -
PXD005366 10 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
PXD004452 24 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
112 107 117 6 4
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 369 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 92 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD001333 9 Anion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC Homo sapiens (Human) PARTIAL 2015-04-23 HeLa cell -
PXD004452 28 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
125 118 130 8 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
241 240 245 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
298 292 299 7 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
320 317 324 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
394 392 400 3 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 121 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
723 721 727 3 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 45 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD003198 5 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line

Structures

Showing 15 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
1A31 A X-ray 2.0999999046325684 Monomer [5IU]C:10 0.052131608 241, 298, 320, 394, 506
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
241 241 TYR E 0.82 46.66011047363281 0.0
298 298 SER H 0.76 89.86868286132812 0.0
320 320 SER C 0.79 50.7126579284668 0.0
394 394 SER C 0.71 98.15677642822266 0.0
506 506 SER H 1.0 20.528663635253906 0.0
1K4T A X-ray 2.0999999046325684 4 [HG]A:900 0.56634206 241, 298, 320, 394, 506
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
241 241 TYR E 0.82 51.454898834228516 0.0
298 298 SER C 0.76 86.71690368652344 0.0
320 320 SER C 0.79 50.41926574707031 0.0
394 394 SER C 0.71 92.63896942138672 0.0
506 506 SER H 1.0 17.469648361206055 0.0
1RRJ A X-ray 2.299999952316284 3 C 0.8798226 241, 298, 320, 394, 506
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
241 241 TYR E 0.82 56.68383026123047 0.0
298 298 SER C 0.76 87.92672729492188 0.0
320 320 SER C 0.79 50.88212585449219 0.0
394 394 SER C 0.71 95.34647369384766 0.0
506 506 SER C 1.0 18.614091873168945 0.0
1A35 A X-ray 2.5 3 C 1.0 241, 298, 320, 394, 506
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
241 241 TYR E 0.82 63.045772552490234 0.0
298 298 SER H 0.76 87.77342224121094 0.0
320 320 SER C 0.79 70.07963562011719 0.0
394 394 SER C 0.71 97.2496109008789 0.0
506 506 SER C 1.0 8.4443941116333 0.0
1RR8 C X-ray 2.5999999046325684 3 A 0.6696959 241, 298, 320, 394, 506
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
241 241 TYR E 0.82 51.46702575683594 0.0
298 298 SER C 0.76 85.91242980957031 0.0
320 320 SER C 0.79 55.350704193115234 0.0
394 394 SER C 0.71 86.66935729980469 0.0
506 506 SER C 1.0 20.508562088012695 0.0
1EJ9 A X-ray 2.5999999046325684 3 C 1.0 241, 298, 320, 394, 506
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
241 241 TYR E 0.82 55.54125213623047 0.0
298 298 SER C 0.76 87.19060516357422 0.0
320 320 SER C 0.79 61.39223861694336 0.0
394 394 SER C 0.71 91.2033462524414 0.0
506 506 SER C 1.0 20.670547485351562 0.0
1A36 A X-ray 2.799999952316284 3 C 1.0 241, 298, 320, 394, 506
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
241 241 TYR E 0.82 46.126251220703125 0.0
298 298 SER H 0.76 90.42603302001953 0.0
320 320 SER C 0.79 65.27747344970703 0.0
394 394 SER C 0.71 97.63484191894531 0.0
506 506 SER H 1.0 18.865177154541016 0.0
1SC7 A X-ray 3.0 4 D 1.0 241, 298, 320, 394, 506
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
241 241 TYR E 0.82 56.98725128173828 0.0
298 298 SER H 0.76 89.51058959960938 0.0
320 320 SER C 0.79 62.43342590332031 0.0
394 394 SER C 0.71 102.02476501464844 0.0
506 506 SER C 1.0 19.265750885009766 0.0
1SEU A X-ray 3.0 4 D 1.0 241, 298, 320, 394, 506
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
241 241 TYR E 0.82 63.10797882080078 0.0
298 298 SER C 0.76 87.7952651977539 0.0
320 320 SER C 0.79 54.310062408447266 0.0
394 394 SER C 0.71 94.87702941894531 0.0
506 506 SER H 1.0 17.133893966674805 0.0
1T8I A X-ray 3.0 4 D 1.0 241, 298, 320, 394, 506
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
241 241 TYR E 0.82 53.631832122802734 0.0
298 298 SER H 0.76 90.69985961914062 0.0
320 320 SER C 0.79 48.09613800048828 0.0
394 394 SER C 0.71 105.04652404785156 0.0
506 506 SER H 1.0 19.1330623626709 0.0
1TL8 A X-ray 3.0999999046325684 4 D 0.9618189 241, 298, 320, 394, 506
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
241 241 TYR E 0.82 62.24699783325195 0.0
298 298 SER C 0.76 88.43550109863281 0.0
320 320 SER C 0.79 73.07598876953125 0.0
394 394 SER C 0.71 98.79845428466797 0.0
506 506 SER C 1.0 17.106006622314453 0.0
1NH3 A X-ray 3.0999999046325684 4 D 1.0 241, 298, 320, 394, 506
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
241 241 TYR E 0.82 109.57058715820312 0.0
298 298 SER H 0.76 93.67034912109375 0.0
320 320 SER C 0.79 66.6221923828125 0.0
394 394 SER C 0.71 101.45337677001953 0.0
506 506 SER C 1.0 24.497947692871094 0.0
1R49 A X-ray 3.130000114440918 3 C 1.0 241, 298, 320, 394, 506
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
241 241 TYR E 0.82 53.317108154296875 0.0
298 298 SER C 0.76 88.98533630371094 0.0
320 320 SER C 0.79 71.36479949951172 0.0
394 394 SER C 0.71 99.93883514404297 0.0
506 506 SER C 1.0 20.8006649017334 0.0
1LPQ A X-ray 3.140000104904175 3 C 1.0 241, 298, 320, 394, 506
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
241 241 TYR E 0.82 66.46345520019531 0.0
298 298 SER C 0.76 88.56221008300781 0.0
320 320 SER C 0.79 65.99596405029297 0.0
394 394 SER C 0.71 95.24307250976562 0.0
506 506 SER C 1.0 21.302623748779297 0.0
1K4S A X-ray 3.200000047683716 2 [5IU]B:10 0.1 241, 298, 320, 394, 506
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
241 241 TYR C 0.82 80.47554016113281 0.0
298 298 SER C 0.76 83.14955139160156 0.0
320 320 SER C 0.79 60.31008529663086 0.0
394 394 SER C 0.71 86.33403015136719 0.0
506 506 SER C 1.0 17.403335571289062 0.0

Mutations

Showing 6 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
214 G S Polymorphism
326 K R Unclassified Breast cancer
370 M T Unclassified CPT-resistant leukemia
533 D G Unclassified CPT-resistant leukemia
722 N S Unclassified CPT-resistant leukemia
729 T A Unclassified CPT-resistant lung cancer