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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
82 PhosphoS UP, PRIDE Combined yes
255 PhosphoS PRIDE yes
266 PhosphoT 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 3 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
82 78 90 5 3
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD000612 34 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD005366 17 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 10 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
255 252 262 4 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
266 263 271 4 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

Structures

Showing 16 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
5FUQ A X-ray 2.0399999618530273 2 B 0.5643124 82, 255, 266
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
20 20 TYR H 0.49 30.98600959777832 0.0
72 72 SER H 0.61 3.066887378692627 0.0
82 82 SER C 0.89 17.443754196166992 0.0
255 255 SER C 0.87 0.0 0.0
266 266 THR C 0.69 115.96115112304688 0.0
5A4K A X-ray 2.0899999141693115 2 D 0.6643179 82, 255, 266
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
20 20 TYR H 0.49 56.63865280151367 0.0
72 72 SER H 0.61 2.3816981315612793 0.0
82 82 SER C 0.89 16.832138061523438 0.0
255 255 SER C 0.87 0.0 0.0
266 266 THR C 0.69 120.48558044433594 0.0
4CF6 A X-ray 2.690000057220459 2 B 0.60394645 82, 255, 266
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
20 20 TYR H 0.49 43.42994689941406 0.0
72 72 SER H 0.61 3.3988442420959473 0.0
82 82 SER C 0.89 9.257213592529297 0.0
255 255 SER C 0.87 0.0 0.0
266 266 THR C 0.69 117.12834167480469 0.24581113457679749
4CET A X-ray 2.200000047683716 2 A 0.41693312 82
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
20 20 TYR H 0.49 46.533538818359375 0.0
72 72 SER H 0.61 3.314268112182617 0.0
82 82 SER C 0.89 10.529576301574707 0.0
1D4A A X-ray 1.7000000476837158 2 C 0.64036316
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
20 19 TYR H 0.49 64.46686553955078 0.0
72 71 SER H 0.61 2.3335487842559814 0.0
82 81 SER C 0.89 18.86988067626953 0.0
255 254 SER C 0.87 0.0 0.0
266 265 THR C 0.69 104.04143524169922 0.0
1KBQ A X-ray 1.7999999523162842 2 C 0.53141415
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
20 19 TYR H 0.49 60.558433532714844 0.0
72 71 SER H 0.61 2.452474594116211 0.0
82 81 SER C 0.89 19.506610870361328 0.0
255 254 SER C 0.87 0.0 0.0
266 265 THR C 0.69 99.06745147705078 0.0
1H69 A X-ray 1.8600000143051147 2 C 0.510531
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
20 19 TYR H 0.49 51.69453811645508 0.0
72 71 SER H 0.61 2.3248531818389893 0.0
82 81 SER C 0.89 16.42841339111328 0.0
255 254 SER C 0.87 0.0 0.0
266 265 THR C 0.69 108.87140655517578 0.0
1H66 A X-ray 2.0 2 C 0.71443933
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
20 19 TYR H 0.49 61.386844635009766 0.0
72 71 SER H 0.61 2.449521064758301 0.0
82 81 SER C 0.89 18.397689819335938 0.0
255 254 SER C 0.87 0.0 0.0
266 265 THR C 0.69 116.637939453125 0.0
5EA2 A X-ray 2.009999990463257 2 C 0.66354036
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
20 19 TYR H 0.49 49.3774299621582 0.0
72 71 SER H 0.61 2.519754409790039 0.0
82 81 SER C 0.89 18.362348556518555 0.0
255 254 SER C 0.87 0.0 0.0
266 265 THR C 0.69 122.5561752319336 0.0
1QBG A X-ray 2.299999952316284 2 B 0.6245283
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
20 19 TYR H 0.49 49.213348388671875 0.0
72 71 SER H 0.61 3.068735361099243 0.0
82 81 SER C 0.89 18.248613357543945 0.0
255 254 SER C 0.87 0.0 0.0
266 265 THR C 0.69 108.23365783691406 2.8458609580993652
1KBO A X-ray 2.299999952316284 2 C 0.58027554
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
20 19 TYR H 0.49 57.74977493286133 0.0
72 71 SER H 0.61 1.845064640045166 0.0
82 81 SER C 0.89 20.62755012512207 0.0
255 254 SER C 0.87 0.12287786602973938 0.0
266 265 THR C 0.69 95.81416320800781 0.0
3JSX A X-ray 2.450000047683716 2 B 0.66020846
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
20 19 TYR H 0.49 46.67253112792969 0.0
72 71 SER H 0.61 1.8436142206192017 0.0
82 81 SER C 0.89 22.11056137084961 0.0
255 254 SER C 0.87 0.0 0.0
266 265 THR C 0.69 118.71733093261719 0.0
1GG5 A X-ray 2.5 2 C 0.55773383
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
20 19 TYR H 0.49 49.64934539794922 0.0
72 71 SER H 0.61 2.2116987705230713 0.0
82 81 SER C 0.89 16.255359649658203 0.0
255 254 SER C 0.87 0.12287786602973938 0.0
266 265 THR C 0.69 109.59327697753906 0.0
1DXO A X-ray 2.5 2 C 0.55781436
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
20 19 TYR H 0.49 38.265960693359375 0.0
72 71 SER H 0.61 2.329777240753174 0.0
82 81 SER C 0.89 15.721501350402832 0.0
255 254 SER C 0.87 0.0 0.0
266 265 THR C 0.69 113.115478515625 0.0
2F1O A X-ray 2.75 2 C 0.6613957
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
20 19 TYR H 0.49 45.73555374145508 0.0
72 71 SER H 0.61 2.457529067993164 0.0
82 81 SER C 0.89 14.889328002929688 0.0
255 254 SER C 0.87 0.0 0.0
266 265 THR C 0.69 124.05667877197266 0.0
5EAI A X-ray 2.9000000953674316 2 B 0.6110384
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
20 19 TYR H 0.49 49.29922103881836 0.0
72 71 SER H 0.61 2.0884647369384766 0.0
82 81 SER C 0.89 16.888839721679688 0.0
255 254 SER C 0.87 0.0 0.0
266 265 THR C 0.69 116.1386489868164 0.0

Mutations

Showing 3 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
139 R W Polymorphism
187 P S Polymorphism
269 Q H Polymorphism