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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 5 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
14 TYR PRIDE
16 SER PRIDE
316 SER UP, PRIDE Combined
321 SER UP, PRIDE Combined
331 THR PRIDE

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 5 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
14 13 26 2 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD003198 1 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line
16 13 26 4 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD003198 1 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line
316 302 341 15 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000680 13 Stable isotope labeling of phosphoproteins for large-scale phosphorylation rate determination Homo sapiens (Human) COMPLETE 2014-04-15 HeLa cell,HEK-293 cell
321 302 341 20 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000680 15 Stable isotope labeling of phosphoproteins for large-scale phosphorylation rate determination Homo sapiens (Human) COMPLETE 2014-04-15 HeLa cell,HEK-293 cell
331 302 341 30 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
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

Structures

Showing 11 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
5IYC N EM 3.9000000953674316 Monomer O 0.0 14, 16, 316, 321, 331
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 14 TYR H 0.93 61.57052993774414 27.508039474487305
16 16 SER H 0.83 52.943382263183594 33.45764923095703
316 316 SER H 1.0 95.71904754638672 0.0
321 321 SER C 1.0 92.14030456542969 0.0
331 331 THR C 1.0 119.29620361328125 6.383736610412598
5IYB N EM 3.9000000953674316 Monomer O 0.0 14, 16, 316, 321, 331
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 14 TYR H 0.93 55.145782470703125 29.14731788635254
16 16 SER H 0.83 54.09209060668945 28.665828704833984
316 316 SER H 1.0 84.28132629394531 0.0
321 321 SER C 1.0 92.41837310791016 0.0
331 331 THR C 1.0 117.9957275390625 0.0
5IYD N EM 3.9000000953674316 Monomer O 0.0 14, 16, 316, 321, 331
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 14 TYR H 0.93 54.41038131713867 28.012248992919922
16 16 SER H 0.83 54.71715545654297 36.29551315307617
316 316 SER H 1.0 94.055419921875 0.0
321 321 SER C 1.0 81.87200164794922 0.0
331 331 THR C 1.0 106.05047607421875 31.82216453552246
5IYA N EM 5.400000095367432 Monomer O 0.0 14, 16, 316, 321, 331
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 14 TYR H 0.93 55.65378952026367 3.6020214557647705
16 16 SER H 0.83 57.19138717651367 34.34282684326172
316 316 SER H 1.0 57.953548431396484 0.0
321 321 SER C 1.0 87.93508911132812 0.0
331 331 THR C 1.0 99.10259246826172 26.631126403808594
5IY9 N EM 6.300000190734863 Monomer O 0.0 14, 16, 316, 321, 331
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 14 TYR H 0.93 54.622711181640625 28.463037490844727
16 16 SER H 0.83 53.615047454833984 36.31258773803711
316 316 SER H 1.0 95.67428588867188 0.0
321 321 SER C 1.0 78.2774887084961 0.0
331 331 THR C 1.0 106.34387969970703 32.14458465576172
5IY6 N EM 7.199999809265137 Monomer O 0.0 14, 16, 316, 321, 331
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 14 TYR H 0.93 55.658878326416016 3.6020214557647705
16 16 SER H 0.83 56.56348419189453 33.72795104980469
316 316 SER H 1.0 57.13138961791992 0.0
321 321 SER C 1.0 88.1902084350586 0.0
331 331 THR C 1.0 98.40856170654297 26.84375
5IY8 N EM 7.900000095367432 Monomer O 0.0 14, 16, 316, 321, 331
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 14 TYR H 0.93 63.631710052490234 27.675992965698242
16 16 SER H 0.83 52.55695724487305 33.02123260498047
316 316 SER H 1.0 95.72701263427734 0.0
321 321 SER C 1.0 91.97523498535156 0.0
331 331 THR C 1.0 119.7761001586914 6.502649307250977
5IY7 N EM 8.600000381469727 Monomer O 0.0 14, 16, 316, 321, 331
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 14 TYR H 0.93 54.20799255371094 28.9516544342041
16 16 SER H 0.83 54.299156188964844 28.680662155151367
316 316 SER H 1.0 84.26593017578125 0.0
321 321 SER C 1.0 90.88340759277344 0.0
331 331 THR C 1.0 118.6339340209961 0.0
1NVP C X-ray 2.0999999046325684 3 D 1.0 14, 16, 331
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 14 TYR H 0.93 92.98326110839844 39.55253219604492
16 16 SER H 0.83 56.7378044128418 3.336331367492676
331 331 THR C 1.0 38.734474182128906 0.0
5FUR B EM 8.5 Monomer D 0.0 14, 16, 331
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 14 TYR H 0.93 93.06848907470703 36.86983108520508
16 16 SER H 0.83 56.956111907958984 26.348711013793945
331 331 THR C 1.0 37.65525817871094 0.0
5M4S A X-ray 2.380000114440918 Monomer A 0.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 116 TYR H 0.93 38.51972579956055 0.0
16 118 SER H 0.83 15.505805969238281 0.0

Mutations

Showing 2 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
30 L V Unclassified A breast cancer sample
109 A P Polymorphism