UniProtKB/SwissProt variant VAR

Variant information

Variant position:

155

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

Type of variant:

Unclassified

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 Serine (S) to Arginine (R) at position 155 (S155R, p.Ser155Arg).

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 small size and polar (S) to large size and basic (R)

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

BLOSUM score:

-1

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:

In a colorectal adenocarcinoma sample; somatic mutation; reduces interaction with TPX2.

Any additional useful information about the variant.

Sequence information

Variant position:

155

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

Protein sequence length:

403

The length of the canonical sequence.

Location on the sequence:

IGRPLGKGKFGNVYLAREKQ S KFILALKVLFKAQLEKAGVE

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                         IGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVE

Mouse                         IGRPLGKGKFGNVYLARERQSKFILALKVLFKTQLEKANVE

Rat                           IGRPLGKGKFGNVYLAREKQSKFILALKVLFKVQLEKAGVE

Pig                           IGRPLGKGKFGNVYLAREKQSKFILALKVLFKTQLEKAGVE

Bovine                        IGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVE

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	1 – 403	Aurora kinase A
Domain	133 – 383	Protein kinase
Binding site	143 – 143	ATP; via amide nitrogen
Binding site	162 – 162	ATP
Mutagenesis	162 – 162	K -> R. Loss of kinase activity.
Mutagenesis	165 – 165	F -> A. Decreases the interaction with phosphatase type 1 isoforms.
Turn	153 – 155

Literature citations

A cancer-associated aurora A mutant is mislocalized and misregulated due to loss of interaction with TPX2.
Bibby R.A.; Tang C.; Faisal A.; Drosopoulos K.; Lubbe S.; Houlston R.; Bayliss R.; Linardopoulos S.;
J. Biol. Chem. 284:33177-33184(2009)
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 127-388 IN COMPLEX WITH ADP; CHARACTERIZATION OF VARIANTS ARG-155 AND MET-174; INTERACTION WITH TPX2;

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] ILE-31; LEU-50; ILE-57; ARG-155; MET-174 AND VAL-373;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O14965: Variant p.Ser155Arg