UniProtKB/SwissProt variant VAR

Variant information

Variant position:

764

The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:

Polymorphism

The variants are classified into three categories: Disease, Polymorphism and Unclassified.

Disease: Variants implicated in disease according to literature reports.
Polymorphism: Variants not reported to be implicated in disease.
Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:

From Arginine (R) to Cysteine (C) at position 764 (R764C, p.Arg764Cys).

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 large size and basic (R) to medium size and polar (C)

The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:

-3

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

Other resources:

Links to websites of interest for the variant.

Variant rs34392012 [ dbSNP | Ensembl ]

Sequence information

Variant position:

764

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:

PMLERKEVSKYSDIQRSLYD R PASYKKKSMLDSEVKNLLSD

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                         PMLERKEVSKYSDIQRSLYDRPASYKKKSMLDSEVKNLLSD

Mouse                         PMLERKEVSKYSDIQRSLYDRPASYKKKSMLDSEVKNLLSD

Rat                           PMLERKEVSKYSDIQRSLYDRPASYKKKSMLDSEAKNLLSD

Chicken                       PMLERKEGSKYSDIQRSVYDRPASYKKKSLSESEVKNLLSD

Xenopus laevis                PMLEMKEPSKYSDIQRSLYDRPASYKKKPL--SEVKNILSD

Zebrafish                     PMLEMNEASKYSPIQRSDYDHPPSHRQ---FNDEAESLLSD

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	24 – 1089	Platelet-derived growth factor receptor alpha
Topological domain	550 – 1089	Cytoplasmic
Domain	593 – 954	Protein kinase
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	762 – 762	Y -> F. Abolishes interaction with CRK.

Literature citations

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.;
Nature 446:153-158(2007)
Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASP-79; ASP-426; PRO-478; CYS-764; ARG-829; LYS-996 AND ASN-1071;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P16234: Variant p.Arg764Cys