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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
40 PhosphoS UP, PRIDE Combined yes
96 PhosphoS UP, PRIDE Combined yes
101 PhosphoS UP Similarity
106 PhosphoT PRIDE yes
108 PhosphoS UP, PRIDE Combined yes
148 PhosphoT UP Combined
177 PhosphoS PRIDE yes
182 PhosphoS UP, PRIDE Similarity yes
192 PhosphoY PRIDE yes

3D structure is not available

Display Settings

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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 8 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
40 36 53 5 3
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
PXD003531 34 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD004452 10 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
96 84 102 13 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD004415 1 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte
96 90 102 7 3
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD004415 2 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte
PXD002286 8 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 - -
PXD006482 2 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney -
106 103 126 4 3
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 -
PXD004415 1 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte
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 -
108 103 126 6 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD004415 1 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte
177 173 199 5 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD001060 1 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell
182 173 199 10 3
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD001060 2 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell -
PXD006482 5 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney -
PXD000680 2 Stable isotope labeling of phosphoproteins for large-scale phosphorylation rate determination Homo sapiens (Human) COMPLETE 2014-04-15 HeLa cell,HEK-293 cell
192 173 199 20 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

Structures

Showing 6 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
5ISO B X-ray 2.630000114440918 3 A 0.9233108 96, 101, 106, 148, 177, 192
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
94 94 SER E 1.0 0.0 0.0
96 96 SER H 1.0 56.32470703125 0.0
101 101 SER C 0.79 59.63007736206055 0.0
106 106 THR E 1.0 100.48678588867188 41.612056732177734
148 148 THR C 1.0 75.45684814453125 0.0
177 177 SER C 1.0 75.66983032226562 5.648133277893066
180 180 SER C 1.0 128.5679473876953 0.0
187 187 TYR C 1.0 225.32089233398438 186.4886016845703
192 192 TYR C 1.0 205.9529571533203 86.35685729980469
6B1U B X-ray 2.7699999809265137 3 A 0.8340816 96, 101, 106, 148, 192
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
94 94 SER E 1.0 1.1835896968841553 0.0
96 96 SER H 1.0 59.99147415161133 0.0
101 101 SER C 0.79 57.460227966308594 0.0
106 106 THR E 1.0 113.17059326171875 50.17727279663086
148 148 THR C 1.0 57.96923828125 0.0
187 187 TYR C 1.0 231.2964630126953 194.0894012451172
192 192 TYR C 1.0 182.96803283691406 90.74285125732422
5EZV B X-ray 2.990000009536743 3 A 0.8573636 96, 101, 106, 148, 192
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
94 94 SER E 1.0 1.516422986984253 0.0
96 96 SER H 1.0 55.00345993041992 0.0
101 101 SER C 0.79 55.786617279052734 0.0
106 106 THR E 1.0 108.97758483886719 43.976234436035156
148 148 THR C 1.0 74.32543182373047 0.0
187 187 TYR C 1.0 227.92013549804688 178.8623046875
192 192 TYR C 1.0 177.14369201660156 92.60468292236328
4ZHX B X-ray 2.990000009536743 3 A 0.86132973 96, 101, 106, 148
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
94 94 SER E 1.0 0.0 0.0
96 96 SER C 1.0 54.9986686706543 0.0
101 101 SER C 0.79 61.999351501464844 0.0
106 106 THR E 1.0 107.65245819091797 49.37344741821289
148 148 THR C 1.0 66.33513641357422 0.0
192 191 TYR C 1.0 120.98563385009766 60.55097198486328
4CFE B X-ray 3.0199999809265137 3 A 0.91211236 96, 101, 106, 148
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
94 94 SER E 1.0 0.0 0.0
96 96 SER C 1.0 65.50518798828125 0.0
101 101 SER C 0.79 56.94609069824219 0.0
106 106 THR E 1.0 103.41970825195312 44.99130630493164
148 148 THR C 1.0 63.50698471069336 0.0
4CFF B X-ray 3.9200000762939453 3 A 0.8444922 96, 101, 106, 148
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
94 94 SER E 1.0 0.0 0.0
96 96 SER C 1.0 67.56375885009766 0.0
101 101 SER C 0.79 54.96355056762695 0.0
106 106 THR E 1.0 108.93199157714844 43.04736328125
148 148 THR C 1.0 61.808387756347656 0.0

Mutations

Showing 0 results

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