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 YDQSFESRDLLIDEWKSLTYD EVISFVPPPLDQEEMES
YDQSFESRDLLIDEWKSLTYD EVVSFVPPPLDQEEMES
Chimpanzee YDQSFESRDLLIDEWKSLTYD EVISFVPPPLDQEEMES
Mouse YDQSFESRDLLIDEWKSLTYD EVISFVPPPLDQEEMES
Rat YDQSFESRDFLIDEWKSLTYD EVISFVPPPLDQEEMES
Xenopus laevis YDQSFESRELDIEEWKRLTYE EVTCFVPPPLDSEEMES
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;
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.