UniProtKB/SwissProt variant VAR

Variant information

Variant position:

162

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 Histidine (H) to Asparagine (N) at position 162 (H162N, p.His162Asn).

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:

Similar physico-chemical property. Both residues are medium size and polar.

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

Other resources:

Links to websites of interest for the variant.

Variant rs55850759 [ dbSNP | Ensembl ]

Sequence information

Variant position:

162

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

Protein sequence length:

487

The length of the canonical sequence.

Location on the sequence:

FMRKIHRDIKAGNILLNTEG H AKLADFGVAGQLTDTMAKRN

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                         FMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRN

Rhesus macaque                FMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRN

Mouse                         FMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRN

Bovine                        FMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRN

Chicken                       FMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRN

Xenopus laevis                FMRKIHRDIKAGNILLSCEGTAKLADFGVAGQLTDTMAKRN

Xenopus tropicalis            FMRKIHRDIKAGNILLNSEGTAKLADFGVAGQLTDTMAKRN

Slime mold                    SVRKIHRDIKAGNILMNHKGESKLADFGVSGQLSDTMAKRQ

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 – 487	Serine/threonine-protein kinase 4
Chain	1 – 326	Serine/threonine-protein kinase 4 37kDa subunit
Domain	30 – 281	Protein kinase
Active site	149 – 149	Proton acceptor
Mutagenesis	175 – 175	T -> A. No effect on activity.
Mutagenesis	177 – 177	T -> A. No effect on activity.

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] ASN-162; GLN-310; MET-312; THR-355 AND LEU-416;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q13043: Variant p.His162Asn