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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 4 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
193 SER PRIDE yes
251 TYR PRIDE
252 SER PRIDE
261 SER 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 4 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
193 191 200 3 3
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004252 1 Modulating the selectivity of affinity absorbents to multi-phosphopeptides by a novel competitive substitution strategy Homo sapiens (Human) PARTIAL 2016-08-03 cell culture
PXD001060 1 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell -
PXD005366 5 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 -
251 247 258 5 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
252 247 258 6 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
261 247 261 15 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

Structures

Showing 10 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
2GHT A X-ray 1.7999999523162842 2 C 0.5692843 193, 251, 252
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
193 193 SER H 1.0 56.93803024291992 0.0
251 251 TYR H 0.93 37.04698181152344 0.0
252 252 SER H 1.0 84.58358001708984 0.0
2GHQ A X-ray 2.049999952316284 2 C 0.575168 193, 251, 252
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
193 193 SER H 1.0 57.39364242553711 0.0
251 251 TYR H 0.93 39.812374114990234 0.0
252 252 SER H 1.0 82.66764831542969 0.0
1TA0 A X-ray 2.0999999046325684 Monomer [MG]A:273 0.09650439 193, 251, 252
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
193 193 SER H 1.0 62.08363342285156 0.0
251 251 TYR H 0.93 27.939950942993164 0.0
252 252 SER H 1.0 88.64618682861328 0.0
4YH1 A X-ray 2.200000047683716 2 [MG]A:301 0.41815367 193, 251, 252
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
193 193 SER H 1.0 61.096534729003906 0.0
251 251 TYR H 0.93 59.6783332824707 0.0
252 252 SER H 1.0 79.03128051757812 0.0
3L0Y A X-ray 2.299999952316284 Monomer [MG]A:257 0.1 193, 251, 252
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
193 193 SER H 1.0 62.80451583862305 0.0
251 251 TYR H 0.93 65.18689727783203 0.0
252 252 SER H 1.0 89.3890151977539 0.0
1T9Z A X-ray 2.299999952316284 Monomer [MG]A:273 0.09246948 193, 251, 252
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
193 193 SER H 1.0 60.93403625488281 0.0
251 251 TYR H 0.93 25.70732307434082 0.0
252 252 SER H 1.0 86.56092071533203 0.0
3PGL A X-ray 2.3499999046325684 Monomer [MG]A:1 0.1 193, 251, 252
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
193 193 SER H 1.0 58.367225646972656 0.0
251 251 TYR H 0.93 18.650394439697266 0.0
252 252 SER H 1.0 80.55635070800781 0.0
3L0B A X-ray 2.3499999046325684 Monomer [MG]A:257 0.1 193, 251, 252
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
193 193 SER H 1.0 61.377586364746094 0.0
251 251 TYR H 0.93 21.123228073120117 0.0
252 252 SER H 1.0 83.6888656616211 0.0
4YGY A X-ray 2.359999895095825 2 [MG]A:301 0.41088235 193, 251, 252
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
193 193 SER H 1.0 62.180362701416016 0.0
251 251 TYR H 0.93 62.11650848388672 0.0
252 252 SER H 1.0 84.62799835205078 0.0
3L0C A X-ray 2.450000047683716 Monomer [PO4]A:596 0.04755219 193, 251, 252
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
193 193 SER H 1.0 60.525001525878906 0.0
251 251 TYR H 0.93 67.90797424316406 0.0
252 252 SER H 1.0 72.9659423828125 0.0

Mutations

Showing 1 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
56 A T Polymorphism