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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 6 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
54 SER UP Similarity
62 SER UP Similarity
118 SER UP Similarity
163 SER UP Experimental
191 SER PRIDE yes
194 SER UP Experimental

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 1 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
191 171 192 21 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

Structures

Showing 11 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
3NCE A X-ray 2.0 2 B 0.20557354 191
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
54 26 SER H 0.69 1.4137967824935913 0.0
62 34 SER H 0.92 31.79822540283203 7.366629600524902
118 90 SER H 0.68 2.365313768386841 0.0
163 135 SER H 0.63 60.164791107177734 0.0
191 163 SER H 0.61 44.06236267089844 0.0
194 166 SER H 0.79 19.82491111755371 0.0
3N06 A X-ray 2.0 2 B 0.26788038 191
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
54 26 SER H 0.69 1.7826697826385498 0.0
62 34 SER H 0.92 33.90912628173828 0.0
118 90 SER H 0.68 1.8392572402954102 0.0
163 135 SER H 0.63 65.91979217529297 0.0
191 163 SER H 0.61 40.75690460205078 0.0
194 166 SER H 0.79 9.100092887878418 0.0
3NCB A X-ray 2.0999999046325684 2 B 0.29202878 191
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
54 26 SER H 0.69 1.493938684463501 0.0
62 34 SER H 0.92 19.884519577026367 0.12163496762514114
118 90 SER H 0.68 2.0858395099639893 0.0
163 135 SER H 0.63 68.32427215576172 0.0
191 163 SER H 0.61 41.00055694580078 0.0
194 166 SER H 0.79 25.120664596557617 0.0
3N0P A X-ray 2.0999999046325684 2 B 0.28286976 191
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
54 26 SER H 0.69 1.4198073148727417 0.0
62 34 SER H 0.92 38.28911209106445 1.0055692195892334
118 90 SER H 0.68 2.0046586990356445 0.0
163 135 SER H 0.63 70.80493927001953 0.0
191 163 SER H 0.61 41.78452682495117 0.0
194 166 SER H 0.79 12.106563568115234 0.0
3MZG A X-ray 2.0999999046325684 2 B 0.2732597 191
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
54 26 SER H 0.69 1.2538636922836304 0.0
62 34 SER H 0.92 32.08237075805664 0.0
118 90 SER H 0.68 2.0064704418182373 0.0
163 135 SER H 0.63 72.25811767578125 0.0
191 163 SER H 0.61 36.353660583496094 0.0
194 166 SER H 0.79 13.442350387573242 0.0
3D48 P X-ray 2.5 2 R 1.0 191
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
54 26 SER H 0.69 2.4167983531951904 0.0
62 34 SER H 0.92 30.152101516723633 0.0
118 90 SER H 0.68 1.776759386062622 0.0
163 135 SER H 0.63 91.32547760009766 0.0
191 163 SER H 0.61 50.083656311035156 0.0
194 166 SER H 0.79 14.950654029846191 0.0
3NCC A X-ray 2.5 2 B 0.28364733 191
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
54 26 SER H 0.69 1.7859923839569092 0.0
62 34 SER H 0.92 26.86789321899414 0.7370001077651978
118 90 SER H 0.68 1.8744550943374634 0.0
163 135 SER H 0.63 67.09342193603516 0.0
191 163 SER H 0.61 43.542232513427734 0.0
194 166 SER H 0.79 12.758243560791016 0.0
2Q98 A X-ray 2.700000047683716 4 A 0.1 191
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
54 26 SER H 0.69 2.037604808807373 0.0
62 34 SER H 0.92 35.646141052246094 0.0
118 90 SER H 0.68 2.9268248081207275 0.0
163 135 SER H 0.63 65.7731704711914 0.0
191 163 SER H 0.61 51.1042366027832 0.0
194 166 SER H 0.79 40.655174255371094 0.0
3NCF A X-ray 2.799999952316284 2 B 0.28545156 191
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
54 26 SER H 0.69 1.252516746520996 0.0
62 34 SER H 0.92 43.332489013671875 7.7228875160217285
118 90 SER H 0.68 2.453343629837036 0.0
163 135 SER H 0.63 58.90568923950195 0.0
191 163 SER H 0.61 33.599361419677734 0.0
194 166 SER H 0.79 14.783430099487305 0.0
3NPZ A X-ray 3.3499999046325684 3 B 1.0 191
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
54 26 SER H 0.69 1.6642305850982666 0.0
62 34 SER H 0.92 26.93140983581543 0.0
118 90 SER H 0.68 5.779906272888184 0.0
163 135 SER H 0.63 64.47954559326172 0.0
191 163 SER C 0.61 82.13318634033203 0.0
194 166 SER H 0.79 17.459814071655273 0.0
3EW3 A X-ray 3.799999952316284 3 C 0.42017245 191
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
54 26 SER H 0.69 2.470458745956421 0.0
62 34 SER H 0.92 25.571399688720703 0.0
118 90 SER H 0.68 3.8813822269439697 0.0
163 135 SER H 0.63 81.8841781616211 0.0
191 163 SER H 0.61 73.4852294921875 0.0
194 166 SER H 0.79 50.97056198120117 0.0

Mutations

Showing 0 results

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