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PDB 
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Phospho-sites

Showing 2 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
365 PhosphoS PRIDE yes
413 PhosphoY 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 2 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
365 361 369 5 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD002436 1 Monitoring cellular phosphorylation signaling pathways into chromatin and down to the gene level Homo sapiens (Human) COMPLETE 2015-11-09 HeLa cell
413 405 418 9 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 2 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
5XF7 A X-ray 2.380000114440918 Monomer A 0.0 365, 413
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
347 347 TYR E 1.0 30.81572914123535 0.0
365 365 SER H 0.76 28.75238609313965 0.0
413 413 TYR E 0.93 16.798362731933594 0.0
4NWY A X-ray 2.0 2 C 0.92526716 365
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
347 347 TYR E 1.0 55.173805236816406 0.0
365 365 SER H 0.76 52.826332092285156 0.0

Mutations

Showing 7 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
26 A T Polymorphism
106 E Q Unclassified A colorectal cancer sample
446 D N Polymorphism
447 V I Polymorphism
475 L R Polymorphism
527 R K Polymorphism
529 G E Polymorphism