Variant position: 561 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 1089 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 SLIVLVVIWKQKPRYEIRWR VIESISPDGHEYIYVDPMQLP
Mouse SLIVLVVIWKQKPRYEIRWR VIESISPDGHEYIYVDPMQLP
Rat SLIVLVVIWKQKPRYEIRWR VIESISPDGHEYIYVDPMQLP
Chicken SLIVLVIIWKQKPRYEIRWR VIESISPDGHEYIYVDPMQLP
Xenopus laevis SLIVLVIIWKQKPRYEIRWR VIESISPDGHEYIYVDPMQLP
Zebrafish SLIVLVIIWKQKPRYEIRWR VIESVSPDGHEYIYVDPMQLP
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
24 – 1089 Platelet-derived growth factor receptor alpha
550 – 1089 Cytoplasmic
572 – 572 Phosphotyrosine; by autocatalysis
574 – 574 Phosphotyrosine; by autocatalysis
219 – 1089 Missing. In isoform 2.
572 – 572 Y -> F. Abolishes interaction with SRC-family members and impairs internalization of the activated receptor; when associated with F-574.
574 – 574 Y -> F. Abolishes interaction with SRC-family members and impairs internalization of the activated receptor; when associated with F-572.
560 – 565
PDGFRA activating mutations in gastrointestinal stromal tumors.
Heinrich M.C.; Corless C.L.; Duensing A.; McGreevey L.; Chen C.J.; Joseph N.; Singer S.; Griffith D.J.; Haley A.; Town A.; Demetri G.D.; Fletcher C.D.; Fletcher J.A.;
Cited for: FUNCTION IN PHOSPHORYLATION OF AKT1; MAP KINASES; STAT1 AND STAT3; INVOLVEMENT IN GIST; VARIANTS ASP-561; VAL-842; 842-ASP--HIS-845 DEL AND 845-HIS--PRO-448 DEL; CHARACTERIZATION OF VARIANTS ASP-561; VAL-842; 842-ASP--HIS-845 DEL AND 845-HIS--PRO-448 DEL;
PDGFRA mutations in gastrointestinal stromal tumors: frequency, spectrum and in vitro sensitivity to imatinib.
Corless C.L.; Schroeder A.; Griffith D.; Town A.; McGreevey L.; Harrell P.; Shiraga S.; Bainbridge T.; Morich J.; Heinrich M.C.;
J. Clin. Oncol. 23:5357-5364(2005)
Cited for: INVOLVEMENT IN GIST; VARIANTS ASP-561; LYS-659; TYR-842; VAL-842; 842-ASP--HIS-845 DEL 845-HIS--PRO-448 DEL AND CYS-849; CHARACTERIZATION OF VARIANTS ASP-561; LYS-659; TYR-842; VAL-842; 842-ASP--HIS-845 DEL 845-HIS--PRO-448 DEL AND CYS-849; ACTIVITY REGULATION;
Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.