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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P16234: Variant p.Arg748Gly

Platelet-derived growth factor receptor alpha
Gene: PDGFRA
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Variant information Variant position: help 748 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help US The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance

Residue change: help From Arginine (R) to Glycine (G) at position 748 (R748G, p.Arg748Gly). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Change from large size and basic (R) to glycine (G) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -2 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page

Variant description: help In a hypereosinophilic syndrome sample; constitutively activated kinase. Any additional useful information about the variant.


Sequence information Variant position: help 748 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 1089 The length of the canonical sequence.
Location on the sequence: help NGDYMDMKQADTTQYVPMLE R KEVSKYSDIQRSLYDRPASY 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human                         NGDYMDMKQADTTQYVPMLERKEVSKYSDIQRSLYDRPASY

Mouse                         NGDYMDMKQADTTQYVPMLERKEVSKYSDIQRSLYDRPASY

Rat                           NGDYVDMKQADTTQYVPMLERKEVSKYSDIQRSLYDRPASY

Chicken                       TGEYMDMKQADTTQYVPMLERKEGSKYSDIQRSVYDRPASY

Xenopus laevis                NGDYMDMKQADTMQYVPMLEMKEPSKYSDIQRSLYDRPASY

Zebrafish                     KGDYMDMKQADTMQYVPMLEMNEASKYSPIQRSDYDHPPSH

Sequence annotation in neighborhood: help 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.
TypePositionsDescription
Chain 24 – 1089 Platelet-derived growth factor receptor alpha
Topological domain 550 – 1089 Cytoplasmic
Domain 593 – 954 Protein kinase
Modified residue 731 – 731 Phosphotyrosine; by autocatalysis
Modified residue 742 – 742 Phosphotyrosine; by autocatalysis
Modified residue 754 – 754 Phosphotyrosine; by autocatalysis
Modified residue 762 – 762 Phosphotyrosine; by autocatalysis
Modified residue 768 – 768 Phosphotyrosine; by autocatalysis
Alternative sequence 219 – 1089 Missing. In isoform 2.
Alternative sequence 744 – 1089 Missing. In isoform 3.
Mutagenesis 731 – 731 Y -> F. No effect on autophosphorylation and phosphorylation of PLCG1. Abolishes activation of phosphatidylinositol 3-kinase.
Mutagenesis 742 – 742 Y -> F. No effect on autophosphorylation and phosphorylation of PLCG1. Abolishes activation of phosphatidylinositol 3-kinase.
Mutagenesis 762 – 762 Y -> F. Abolishes interaction with CRK.



Literature citations
Novel imatinib-sensitive PDGFRA-activating point mutations in hypereosinophilic syndrome induce growth factor independence and leukemia-like disease.
Elling C.; Erben P.; Walz C.; Frickenhaus M.; Schemionek M.; Stehling M.; Serve H.; Cross N.C.; Hochhaus A.; Hofmann W.K.; Berdel W.E.; Muller-Tidow C.; Reiter A.; Koschmieder S.;
Blood 117:2935-2943(2011)
Cited for: FUNCTION IN PHOSPHORYLATION OF STAT 5A AND/OR STAT5B; ROLE IN HYPEREOSINOPHILIC SYNDROME; VARIANTS GLY-481; PRO-507; MET-562; ARG-570; GLN-650; SER-659; PRO-705; GLY-748 AND SER-849; CHARACTERIZATION OF VARIANTS GLY-481; PRO-507; MET-562; ARG-570; GLN-650; SER-659; PRO-705; GLY-748 AND SER-849; ACTIVITY REGULATION;
Disclaimer: 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.