Variant position: 589 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 1106 The length of the canonical sequence.
Location on the sequence:
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human IESVSSDGHEYIYVDPMQLP YDSTWELPRDQLVLGRTLGSG
Mouse IESVSSDGHEYIYVDPVQLP YDSTWELPRDQLVLGRTLGSG
Rat IESVSSDGHEYIYVDPVQLP YDSTWELPRDQLVLGRTLGSG
Dog IESVSSDGHEYIYVDPMQLP YDSTWELPRDQLVLGRTLGSG
Sequence annotation in neighborhood: The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Type Positions Description
33 – 1106 Platelet-derived growth factor receptor beta
554 – 1106 Cytoplasmic
579 – 579 Phosphotyrosine; by autocatalysis
581 – 581 Phosphotyrosine; by autocatalysis
589 – 589 Phosphotyrosine; by autocatalysis
337 – 1106 Missing. In isoform 2.
579 – 579 Y -> F. Loss of kinase activity; when associated with F-581. Strongly reduces interaction with SRC family kinases. No effect on interaction with GRB10.
581 – 581 Y -> F. Loss of kinase activity; when associated with F-579. No effect on interaction with GRB10.
Patterns of somatic mutation in human cancer genomes.
Greenman C.; Stephens P.; Smith R.; Dalgliesh G.L.; Hunter C.; Bignell G.; Davies H.; Teague J.; Butler A.; Stevens C.; Edkins S.; O'Meara S.; Vastrik I.; Schmidt E.E.; Avis T.; Barthorpe S.; Bhamra G.; Buck G.; Choudhury B.; Clements J.; Cole J.; Dicks E.; Forbes S.; Gray K.; Halliday K.; Harrison R.; Hills K.; Hinton J.; Jenkinson A.; Jones D.; Menzies A.; Mironenko T.; Perry J.; Raine K.; Richardson D.; Shepherd R.; Small A.; Tofts C.; Varian J.; Webb T.; West S.; Widaa S.; Yates A.; Cahill D.P.; Louis D.N.; Goldstraw P.; Nicholson A.G.; Brasseur F.; Looijenga L.; Weber B.L.; Chiew Y.-E.; DeFazio A.; Greaves M.F.; Green A.R.; Campbell P.; Birney E.; Easton D.F.; Chenevix-Trench G.; Tan M.-H.; Khoo S.K.; Teh B.T.; Yuen S.T.; Leung S.Y.; Wooster R.; Futreal P.A.; Stratton M.R.;
Cited for: VARIANTS [LARGE SCALE ANALYSIS] PHE-29; LYS-282; LYS-485; HIS-589; TYR-718 AND ILE-882;
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