Sequence information
Variant position: 464 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 729 The length of the canonical sequence.
Location on the sequence:
RWLIELIKDDYNETVHKKTE
V VITLDFCIRNIEKTVKVYEK
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 RWLIELIKDDYNETVHKKTEV VITLDFCIRNIEKTVKVYEK
Mouse RWLVELVKDDYNETVHKKTEV VITLDFCIRNIEKTVKVYEK
Xenopus laevis RWLSELMKEEYNENVHRNTEV SLKLNFCNRTTEKDLKIYEQ
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 – 729
Serine/threonine-protein kinase TBK1
Coiled coil
407 – 657
Mutagenesis
448 – 448
E -> R. Decreases phosphorylation and kinase activity. Abolishes dimerization; when associated with R-355.
Mutagenesis
459 – 459
H -> E. Abolishes dimerization and decreases kinase activity but no effect on phosphorylation; when associated with E-466 and E-470.
Mutagenesis
466 – 466
I -> E. Abolishes dimerization and decreases kinase activity but no effect on phosphorylation; when associated with E-459 and E-470.
Mutagenesis
470 – 470
F -> E. Abolishes dimerization and decreases kinase activity but no effect on phosphorylation; when associated with E-459 and E-466.
Helix
408 – 480
Literature citations
Copy number variations on chromosome 12q14 in patients with normal tension glaucoma.
Fingert J.H.; Robin A.L.; Stone J.L.; Roos B.R.; Davis L.K.; Scheetz T.E.; Bennett S.R.; Wassink T.H.; Kwon Y.H.; Alward W.L.; Mullins R.F.; Sheffield V.C.; Stone E.M.;
Hum. Mol. Genet. 20:2482-2494(2011)
Cited for: INVOLVEMENT IN GLC1P; TISSUE SPECIFICITY; VARIANTS PHE-151; ILE-306 AND ALA-464;
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] GLN-271; GLU-291; HIS-296; ARG-410 AND ALA-464;
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.