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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
55 SER UP Experimental
56 SER UP Experimental
61 SER UP Experimental
103 TYR PRIDE yes
115 SER PRIDE
122 THR UP, PRIDE Combined
124 SER PRIDE yes
128 SER PRIDE yes
160 SER UP Experimental
193 SER UP, PRIDE Combined yes
195 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 10 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
103 97 111 7 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
115 112 131 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
122 112 131 11 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
122 119 131 4 5
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 24 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD002436 4 Monitoring cellular phosphorylation signaling pathways into chromatin and down to the gene level Homo sapiens (Human) COMPLETE 2015-11-09 HeLa cell -
PXD003531 1 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
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 -
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
124 117 131 8 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD002436 4 Monitoring cellular phosphorylation signaling pathways into chromatin and down to the gene level Homo sapiens (Human) COMPLETE 2015-11-09 HeLa cell
124 119 131 6 4
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 53 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 15 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD002286 3 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 - -
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
128 119 131 10 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD003531 8 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
193 191 205 3 3
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD006482 2 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney
PXD001550 2 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
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 -
195 191 205 5 5
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000836 4 HOPE-fixation of lung tissue allows retrospective proteome and phosphoproteome studies Homo sapiens (Human) PARTIAL 2014-05-22 lung -
PXD004415 2 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte
PXD006482 3 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney -
PXD001550 4 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
PXD000680 12 Stable isotope labeling of phosphoproteins for large-scale phosphorylation rate determination Homo sapiens (Human) COMPLETE 2014-04-15 HeLa cell,HEK-293 cell -
195 191 210 5 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

Structures

Showing 7 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
3TQ6 A X-ray 2.450000047683716 6 C 1.0 55, 56, 61, 103, 115, 122, 124, 128, 160, 193, 195
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
55 55 SER C 0.6 60.25761032104492 13.94550609588623
56 56 SER H 0.76 16.479248046875 0.0
61 61 SER H 0.59 11.886754989624023 6.457544803619385
103 103 TYR H 0.66 63.418094635009766 0.0
115 115 SER H 0.57 61.6134033203125 0.0
122 122 THR C 0.8 71.2989501953125 0.0
124 124 SER H 0.81 78.47062683105469 0.0
128 128 SER H 0.75 36.62074661254883 0.0
160 160 SER C 0.83 53.693511962890625 25.896291732788086
193 193 SER C 0.58 64.62516784667969 0.0
195 195 SER H 0.76 93.25283813476562 0.0
200 200 TYR H 1.0 17.31415557861328 0.0
4NNU A X-ray 2.809999942779541 6 C 1.0 55, 56, 61, 103, 115, 122, 124, 128, 160, 193, 195
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
55 55 SER C 0.6 56.497108459472656 10.895658493041992
56 56 SER H 0.76 24.029687881469727 0.0
61 61 SER H 0.59 12.23385238647461 10.294763565063477
103 103 TYR H 0.66 70.60445404052734 0.0
115 115 SER H 0.57 43.61494064331055 0.0
122 122 THR C 0.8 71.24246978759766 0.0
124 124 SER H 0.81 69.13516998291016 0.0
128 128 SER H 0.75 56.55118942260742 0.0
160 160 SER C 0.83 53.326026916503906 47.75816345214844
193 193 SER C 0.58 52.93658447265625 0.0
195 195 SER C 0.76 85.12822723388672 0.0
200 200 TYR H 1.0 19.196895599365234 0.0
4NOD A X-ray 2.9000000953674316 6 G 1.0 55, 56, 61, 103, 115, 122, 124, 128, 160, 193, 195
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
55 55 SER C 0.6 53.98989486694336 0.0
56 56 SER H 0.76 17.651155471801758 0.0
61 61 SER H 0.59 13.511407852172852 0.0
103 103 TYR H 0.66 61.517127990722656 0.0
115 115 SER H 0.57 59.228271484375 0.0
122 122 THR C 0.8 73.75227355957031 0.0
124 124 SER H 0.81 82.20075988769531 0.0
128 128 SER H 0.75 52.99864959716797 0.0
160 160 SER C 0.83 49.5761604309082 0.0
193 193 SER C 0.58 63.503387451171875 0.0
195 195 SER H 0.76 102.11357879638672 0.0
200 200 TYR H 1.0 35.07725524902344 0.0
6ERQ C X-ray 4.5 8 D 1.0 55, 56, 61, 103, 115, 122, 124, 128, 160, 193, 195
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
55 55 SER C 0.6 45.473243713378906 29.747909545898438
56 56 SER H 0.76 23.552566528320312 19.82280158996582
61 61 SER H 0.59 13.2449312210083 0.0
103 103 TYR H 0.66 64.87657928466797 52.48186111450195
115 115 SER H 0.57 50.26795959472656 0.0
122 122 THR C 0.8 97.12545013427734 0.0
124 124 SER C 0.81 58.62229537963867 0.0
128 128 SER H 0.75 37.3484992980957 0.0
160 160 SER C 0.83 53.557315826416016 0.0
193 193 SER C 0.58 51.676116943359375 0.0
195 195 SER C 0.76 75.57197570800781 0.0
200 200 TYR H 1.0 25.24063491821289 0.0
6ERP C X-ray 4.5 5 E 1.0 55, 56, 61, 103, 115, 122, 124, 128, 160, 193, 195
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
55 55 SER C 0.6 44.968414306640625 10.822165489196777
56 56 SER H 0.76 24.302186965942383 0.0
61 61 SER H 0.59 13.228646278381348 6.256738662719727
103 103 TYR H 0.66 69.06474304199219 0.0
115 115 SER H 0.57 52.40181350708008 0.0
122 122 THR C 0.8 64.3368911743164 0.0
124 124 SER H 0.81 79.40789794921875 0.0
128 128 SER H 0.75 43.30474853515625 0.0
160 160 SER C 0.83 52.359989166259766 43.19633865356445
193 193 SER C 0.58 52.54319381713867 0.0
195 195 SER C 0.76 75.44564056396484 0.0
200 200 TYR H 1.0 23.470924377441406 0.0
3TMM A X-ray 2.5 3 C 1.0 103
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
55 13 SER C 0.6 58.15133285522461 13.220991134643555
56 14 SER H 0.76 25.962099075317383 0.0
61 19 SER H 0.59 11.887290954589844 6.5236077308654785
103 61 TYR H 0.66 60.373680114746094 0.0
115 73 SER H 0.57 50.171878814697266 0.0
122 80 THR C 0.8 68.42548370361328 0.0
124 82 SER H 0.81 80.93628692626953 0.0
128 86 SER H 0.75 46.57604217529297 0.0
160 118 SER C 0.83 52.35082244873047 43.47623062133789
193 151 SER C 0.58 49.4089469909668 0.0
195 153 SER C 0.76 75.76335906982422 0.0
200 158 TYR H 1.0 20.564674377441406 0.0
3FGH A X-ray 1.350000023841858 2 [NA]A:181 0.22169301
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
160 118 SER C 0.83 49.525203704833984 0.0
193 151 SER C 0.58 64.21327209472656 10.84099006652832
195 153 SER H 0.76 84.91665649414062 15.688080787658691
200 158 TYR H 1.0 21.91652488708496 0.0

Mutations

Showing 2 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
12 S T Polymorphism
178 P L Disease Mitochondrial DNA depletion syndrome 15, hepatocerebral type (MTDPS15) [MIM:617156]