Home  |  Contact

UniProtKB/Swiss-Prot Q16539: Variant p.Ala51Val

Mitogen-activated protein kinase 14
Gene: MAPK14
Variant information

Variant position:  51
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  US
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 Alanine (A) to Valine (V) at position 51 (A51V, p.Ala51Val).
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 hydrophobic (A) to medium size and hydrophobic (V)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  0
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 gastric adenocarcinoma sample; somatic mutation.
Any additional useful information about the variant.



Sequence information

Variant position:  51
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:   GSGAYGSVCAAFDTKTGLRV  A VKKLSRPFQSIIHAKRTYRE
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                         GSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRE

                              GSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRE

Chimpanzee                    GSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRE

Mouse                         GSGAYGSVCAAFDTKTGHRVAVKKLSRPFQSIIHAKRTYRE

Rat                           GSGAYGSVCAAFDTKTGHRVAVKKLSRPFQSIIHAKRTYRE

Xenopus laevis                GSGAYGSVCSSFDTRTALRIAVKKLSRPFQSIIHAKRTYRE

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.

TypePositionsDescription
Chain 2 – 360 Mitogen-activated protein kinase 14
Domain 24 – 308 Protein kinase
Binding site 35 – 35 Inhibitor
Binding site 53 – 53 ATP
Binding site 53 – 53 Inhibitor
Binding site 71 – 71 Inhibitor
Modified residue 53 – 53 N6-acetyllysine
Mutagenesis 34 – 34 A -> V. Lowered kinase activity.
Mutagenesis 53 – 53 K -> R. Loss of kinase activity.
Mutagenesis 54 – 54 K -> R. Impairs MAP2K6/MKK6-dependent autophosphorylation.
Mutagenesis 69 – 69 Y -> H. Lowered kinase activity.
Beta strand 48 – 54


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;

Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.