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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 3 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
168 TYR UP Combined
221 TYR PRIDE yes
351 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 3 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
221 211 227 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
351 348 365 4 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD003531 1 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
351 348 366 4 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 5 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
6ALJ A X-ray 1.8899999856948853 4 [CW2]A:602 0.6003359 168, 221, 351
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
92 92 SER C 1.0 21.84599494934082 0.0
168 168 TYR E 0.91 86.02506256103516 0.0
218 218 SER H 0.8 1.324059009552002 0.0
221 221 TYR H 0.86 34.62028503417969 0.0
351 351 SER C 0.88 60.25569534301758 0.0
6B5G A X-ray 2.200000047683716 4 C 0.43747917 168, 221, 351
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
92 92 SER C 1.0 23.000768661499023 0.0
168 168 TYR E 0.91 89.92655181884766 32.26365661621094
218 218 SER H 0.8 1.2542206048965454 0.0
221 221 TYR H 0.86 35.98286056518555 0.0
351 351 SER C 0.88 60.23785400390625 0.0
6B5H A X-ray 2.299999952316284 4 B 0.53735936 168, 221, 351
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
92 92 SER C 1.0 23.203773498535156 0.0
168 168 TYR E 0.91 92.03743743896484 40.411842346191406
218 218 SER H 0.8 0.7373219132423401 0.0
221 221 TYR H 0.86 33.80481719970703 0.0
351 351 SER C 0.88 61.4164924621582 0.0
6B5I A X-ray 2.5999999046325684 4 C 0.75181013 168, 221, 351
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
92 92 SER C 1.0 21.240541458129883 0.0
168 168 TYR E 0.91 88.50487518310547 39.44121170043945
218 218 SER H 0.8 1.2610657215118408 0.0
221 221 TYR H 0.86 31.10103988647461 0.0
351 351 SER C 0.88 62.107398986816406 0.0
4X2Q A X-ray 2.940000057220459 4 B 0.7384571
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
92 74 SER C 1.0 16.916818618774414 0.0
168 150 TYR E 0.91 98.17657470703125 25.689496994018555
218 200 SER H 0.8 0.9927439093589783 0.0
221 203 TYR H 0.86 28.618410110473633 0.0
351 333 SER C 0.88 53.912906646728516 0.0

Mutations

Showing 4 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
50 E G Polymorphism
110 A V Polymorphism
348 V I Polymorphism
436 E K Polymorphism