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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q16539: Variant p.Pro322Arg

Mitogen-activated protein kinase 14
Gene: MAPK14
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Variant information Variant position: help 322 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help 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: help From Proline (P) to Arginine (R) at position 322 (P322R, p.Pro322Arg). 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: help Change from medium size and hydrophobic (P) to large size and basic (R) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -2 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: help In a lung adenocarcinoma sample; somatic mutation. Any additional useful information about the variant.


Sequence information Variant position: help 322 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 360 The length of the canonical sequence.
Location on the sequence: help ALAHAYFAQYHDPDDEPVAD P YDQSFESRDLLIDEWKSLTY 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human                         ALAHAYFAQYHDPDDEPVADPYDQSFESRDLLIDEWKSLTY

                              ALAHAYFAQYHDPDDEPVADPYDQSFESRDLLIDEWKSLTY

Chimpanzee                    ALAHAYFAQYHDPDDEPVADPYDQSFESRDLLIDEWKSLTY

Mouse                         ALAHAYFAQYHDPDDEPVADPYDQSFESRDLLIDEWKSLTY

Rat                           ALAHAYFAQYHDPDDEPVAEPYDQSFESRDFLIDEWKSLTY

Xenopus laevis                ALAHSYFAQYHDPDDEPIAEPYDQSFESRELDIEEWKRLTY

Sequence annotation in neighborhood: help 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
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 320 – 320 A -> T. Lowered kinase activity.
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.



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.