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Phospho-sites

Showing 6 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
2 PhosphoS PRIDE
3 PhosphoT PRIDE
19 PhosphoS UP, PRIDE Combined yes
28 PhosphoS UP Similarity
128 PhosphoY UP, PRIDE Combined yes
133 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 6 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
2 1 16 2 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD001333 1 Anion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC Homo sapiens (Human) PARTIAL 2015-04-23 HeLa cell
3 1 16 3 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD001333 1 Anion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC Homo sapiens (Human) PARTIAL 2015-04-23 HeLa cell
19 17 25 3 10
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD004252 3 Modulating the selectivity of affinity absorbents to multi-phosphopeptides by a novel competitive substitution strategy Homo sapiens (Human) PARTIAL 2016-08-03 cell culture -
PXD001060 10 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell -
PXD000612 2 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
PXD001546 1 Reproducibility of label-free single-shot phosphoproteomics applied to CRC cell lines Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
PXD003531 12 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD006482 9 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney -
PXD005366 39 Robust, sensitive and automated phosphopeptide enrichment optimized for low sample amounts applied to primary hippocampal neurons Homo sapiens (Human),Rattus norvegicus (Rat) PARTIAL 2016-12-14 cell culture -
PXD004452 2 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
PXD001550 10 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
PXD000680 14 Stable isotope labeling of phosphoproteins for large-scale phosphorylation rate determination Homo sapiens (Human) COMPLETE 2014-04-15 HeLa cell,HEK-293 cell -
19 18 25 2 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
128 121 129 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
133 132 143 2 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 1 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
3I2B A X-ray 2.299999952316284 6 [NI]A:146 0.63772446 19, 28, 128, 133
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
19 19 SER E 0.7 59.639827728271484 0.0
21 21 SER E 0.88 34.80974578857422 0.0
28 28 SER C 0.83 21.669870376586914 0.0
128 128 TYR E 0.79 55.437679290771484 0.0
133 133 TYR E 0.76 51.38883972167969 0.0

Mutations

Showing 21 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
16 R C Disease Hyperphenylalaninemia, BH4-deficient, A (HPABH4A) [MIM:261640]
25 R G Disease Hyperphenylalaninemia, BH4-deficient, A (HPABH4A) [MIM:261640]
26 L F Disease Hyperphenylalaninemia, BH4-deficient, A (HPABH4A) [MIM:261640]
35 E G Disease Hyperphenylalaninemia, BH4-deficient, A (HPABH4A) [MIM:261640]
36 N K Disease Hyperphenylalaninemia, BH4-deficient, A (HPABH4A) [MIM:261640]
47 N D Disease Hyperphenylalaninemia, BH4-deficient, A (HPABH4A) [MIM:261640]
52 N S Disease Hyperphenylalaninemia, BH4-deficient, A (HPABH4A) [MIM:261640]
56 V M Disease Hyperphenylalaninemia, BH4-deficient, A (HPABH4A) [MIM:261640]
67 T M Disease Hyperphenylalaninemia, BH4-deficient, A (HPABH4A) [MIM:261640]
70 V D Disease Hyperphenylalaninemia, BH4-deficient, A (HPABH4A) [MIM:261640]
87 P S Disease Hyperphenylalaninemia, BH4-deficient, A (HPABH4A) [MIM:261640]
96 D N Disease Hyperphenylalaninemia, BH4-deficient, A (HPABH4A) [MIM:261640]
97 V M Disease Hyperphenylalaninemia, BH4-deficient, A (HPABH4A) [MIM:261640]
99 Y C Disease Hyperphenylalaninemia, BH4-deficient, A (HPABH4A) [MIM:261640]
100 F V Disease Hyperphenylalaninemia, BH4-deficient, A (HPABH4A) [MIM:261640]
106 T M Disease Hyperphenylalaninemia, BH4-deficient, A (HPABH4A) [MIM:261640]
114 I V Disease Hyperphenylalaninemia, BH4-deficient, A (HPABH4A) [MIM:261640]
116 D G Disease Hyperphenylalaninemia, BH4-deficient, A (HPABH4A) [MIM:261640]
124 V L Disease Hyperphenylalaninemia, BH4-deficient, A (HPABH4A) [MIM:261640]
129 K E Disease Hyperphenylalaninemia, BH4-deficient, A (HPABH4A) [MIM:261640]
136 D V Disease Hyperphenylalaninemia, BH4-deficient, A (HPABH4A) [MIM:261640]