UniProtKB/SwissProt variant VAR

Variant information

Variant position:

343

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 Aspartate (D) to Glycine (G) at position 343 (D343G, p.Asp343Gly).

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 acidic (D) to glycine (G)

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 rs45496794 [ dbSNP | Ensembl ]

Sequence information

Variant position:

343

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

Protein sequence length:

360

The length of the canonical sequence.

Location on the sequence:

YDQSFESRDLLIDEWKSLTY D EVISFVPPPLDQEEMES

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                         YDQSFESRDLLIDEWKSLTYDEVISFVPPPLDQEEMES

                              YDQSFESRDLLIDEWKSLTYDEVVSFVPPPLDQEEMES

Chimpanzee                    YDQSFESRDLLIDEWKSLTYDEVISFVPPPLDQEEMES

Mouse                         YDQSFESRDLLIDEWKSLTYDEVISFVPPPLDQEEMES

Rat                           YDQSFESRDFLIDEWKSLTYDEVISFVPPPLDQEEMES

Xenopus laevis                YDQSFESRELDIEEWKRLTYEEVTCFVPPPLDSEEMES

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	2 – 360	Mitogen-activated protein kinase 14
Modified residue	323 – 323	Phosphotyrosine; by ZAP70
Alternative sequence	255 – 360	ARNYIQSLTQMPKMNFANVFIGANPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHDPDDEPVADPYDQSFESRDLLIDEWKSLTYDEVISFVPPPLDQEEMES -> VS. In isoform 5.
Alternative sequence	281 – 360	AVDLLEKMLVLDSDKRITAAQALAHAYFAQYHDPDDEPVADPYDQSFESRDLLIDEWKSLTYDEVISFVPPPLDQEEMES -> GKLTIYPHLMDIELVMI. In isoform Mxi2.
Alternative sequence	308 – 360	Missing. In isoform Exip.
Mutagenesis	327 – 327	F -> L. Emulation of the active state. Increase in activity; when associated with A-176.
Mutagenesis	327 – 327	F -> S. Emulation of the active state. Increase in activity; when associated with A-176.
Mutagenesis	337 – 337	W -> R. Loss of kinase activity.
Helix	334 – 347

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] VAL-51; ARG-322 AND GLY-343;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q16539: Variant p.Asp343Gly