UniProtKB/Swiss-Prot P35968: Variant p.Val848Glu

• Variant information
• Sequence information
• Literature citations
• All

Variant information

Variant position: 848 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: LB/B 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: From Valine (V) to Glutamate (E) at position 848 (V848E, p.Val848Glu). 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: Change from medium size and hydrophobic (V) to medium size and acidic (E) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: -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: Strongly reduced autophosphorylation and kinase activity. Any additional useful information about the variant.
Other resources: Links to websites of interest for the variant.

• Variant rs1139776 [ dbSNP | Ensembl ]

Sequence information

Variant position: 848 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 1356 The length of the canonical sequence.
Location on the sequence: EFPRDRLKLGKPLGRGAFGQ V IEADAFGIDKTATCRTVAVK 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.
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
Chain	20 – 1356	Vascular endothelial growth factor receptor 2
Topological domain	786 – 1356	Cytoplasmic
Domain	834 – 1162	Protein kinase
Binding site	840 – 848
Binding site	868 – 868
Alternative sequence	679 – 1356	Missing. In isoform 2.
Alternative sequence	713 – 1356	Missing. In isoform 3.
Mutagenesis	868 – 868	K -> M. Loss of enzyme activity.
Beta strand	844 – 858

Literature citations

Identification of a new endothelial cell growth factor receptor tyrosine kinase.
Terman B.I.; Carrion M.E.; Kovacs E.; Rasmussen B.A.; Eddy R.L.; Shows T.B.;
Oncogene 6:1677-1683(1991)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-1356 (ISOFORM 1); VARIANT GLU-848; Vascular endothelial growth factor receptor KDR tyrosine kinase activity is increased by autophosphorylation of two activation loop tyrosine residues.
Kendall R.L.; Rutledge R.Z.; Mao X.; Tebben A.J.; Hungate R.W.; Thomas K.A.;
J. Biol. Chem. 274:6453-6460(1999)
Cited for: CATALYTIC ACTIVITY; CHARACTERIZATION OF VARIANT GLU-848; PHOSPHORYLATION AT TYR-1054 AND TYR-1059; ACTIVITY REGULATION;