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PDB 
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Phospho-sites

Showing 9 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
8 PhosphoS UP Combined
181 PhosphoT PRIDE yes
249 PhosphoS PRIDE yes
399 PhosphoS UP, PRIDE Combined yes
403 PhosphoS PRIDE yes
484 PhosphoS PRIDE yes
554 PhosphoS PRIDE yes
555 PhosphoS UP, PRIDE Combined yes
667 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 9 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
181 173 194 9 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD001060 2 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell
249 247 254 3 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD002286 5 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 -
399 396 404 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
399 397 404 3 3
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD000612 6 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD003531 1 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
403 397 404 7 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
484 477 486 8 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD000612 1 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
554 551 564 4 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
555 551 564 5 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD000612 18 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
PXD000680 5 Stable isotope labeling of phosphoproteins for large-scale phosphorylation rate determination Homo sapiens (Human) COMPLETE 2014-04-15 HeLa cell,HEK-293 cell -
667 665 677 3 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD000612 3 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture

Structures

Showing 4 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
5KNN A X-ray 2.680000066757202 Monomer [A5A]A:500 0.1 8, 181, 249, 399, 403
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 8 SER H 0.77 50.418373107910156 0.0
181 181 THR C 1.0 61.76682662963867 0.0
249 249 SER H 1.0 0.0 0.0
399 399 SER H 0.95 80.1466293334961 0.0
403 403 SER C 0.34 57.14730453491211 0.0
4XEM A X-ray 1.2799999713897705 Monomer A 0.0 8, 181, 249
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 8 SER H 0.77 65.82284545898438 0.0
181 181 THR C 1.0 55.5531120300293 0.0
249 249 SER H 1.0 0.0 0.0
4XEO A X-ray 1.3799999952316284 Monomer [SO4]A:504 0.036228154 8, 181, 249
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 8 SER H 0.77 67.48607635498047 0.0
181 181 THR C 1.0 54.6794319152832 0.0
249 249 SER H 1.0 0.0 0.0
5V59 A X-ray 2.0299999713897705 Monomer [8X1]A:501 0.1 8, 181, 249
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 8 SER H 0.77 68.76622009277344 0.0
181 181 THR C 1.0 55.52680206298828 0.0
249 249 SER H 1.0 0.0 0.0

Mutations

Showing 7 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
71 N Y Disease Charcot-Marie-Tooth disease 2N (CMT2N) [MIM:613287]
81 K T Disease Epileptic encephalopathy, early infantile, 29 (EIEE29) [MIM:616339]
275 G D Polymorphism
329 R H Disease Charcot-Marie-Tooth disease 2N (CMT2N) [MIM:613287]
608 T M Unclassified
751 R G Disease Epileptic encephalopathy, early infantile, 29 (EIEE29) [MIM:616339]
913 G D Disease Epileptic encephalopathy, early infantile, 29 (EIEE29) [MIM:616339]