Sequence information
Variant position: 155 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 403 The length of the canonical sequence.
Location on the sequence:
IGRPLGKGKFGNVYLAREKQ
S KFILALKVLFKAQLEKAGVE
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 IGRPLGKGKFGNVYLAREKQS KFILALKVLFKAQLEKAGVE
Mouse IGRPLGKGKFGNVYLARERQS KFILALKVLFKTQLEKANVE
Rat IGRPLGKGKFGNVYLAREKQS KFILALKVLFKVQLEKAGVE
Pig IGRPLGKGKFGNVYLAREKQS KFILALKVLFKTQLEKAGVE
Bovine IGRPLGKGKFGNVYLAREKQS KFILALKVLFKAQLEKAGVE
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 – 403
Aurora kinase A
Domain
133 – 383
Protein kinase
Binding site
143 – 143
ATP; via amide nitrogen
Binding site
162 – 162
ATP
Mutagenesis
162 – 162
K -> R. Loss of kinase activity.
Mutagenesis
165 – 165
F -> A. Decreases the interaction with phosphatase type 1 isoforms.
Turn
153 – 155
Literature citations
A cancer-associated aurora A mutant is mislocalized and misregulated due to loss of interaction with TPX2.
Bibby R.A.; Tang C.; Faisal A.; Drosopoulos K.; Lubbe S.; Houlston R.; Bayliss R.; Linardopoulos S.;
J. Biol. Chem. 284:33177-33184(2009)
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 127-388 IN COMPLEX WITH ADP; CHARACTERIZATION OF VARIANTS ARG-155 AND MET-174; INTERACTION WITH TPX2;
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] ILE-31; LEU-50; ILE-57; ARG-155; MET-174 AND VAL-373;
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.