Sequence information
Variant position: 696 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:
IYPSSNTLVEMTLGMKKLKE
E MEGVVKELAENNHILERFGS
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 IYPSSNTLVEMTLGMKKLKEE MEGVVKELAENNHILERFGS
Mouse IYPSSNTLVEMTLGMKKLKEE MEGVVKELAENNHILERFGS
Xenopus laevis IYSSPNTLVEMTLGMRKLKED MEGVVKELEENNHILERFGA
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
Region
621 – 729
Interaction with AZI2, TANK and TBKBP1
Coiled coil
658 – 713
Modified residue
716 – 716
Phosphoserine
Mutagenesis
690 – 690
M -> A. Decreases interaction with TANK.
Mutagenesis
693 – 693
L -> A. Almost abolishes interaction with TANK.
Mutagenesis
694 – 694
K -> E. Strongly decreases interaction with TANK and TBKBP1. No effect on phosphorylation.
Mutagenesis
704 – 704
L -> A. Strongly decreases interaction with AZI2, TANK and TBKBP1. No effect on phosphorylation.
Mutagenesis
708 – 708
N -> A. Decreases interaction with TANK.
Mutagenesis
711 – 711
L -> A. Almost abolishes interaction with TANK.
Helix
680 – 714
Literature citations
Whole-genome sequencing reveals important role for TBK1 and OPTN mutations in frontotemporal lobar degeneration without motor neuron disease.
Pottier C.; Bieniek K.F.; Finch N.; van de Vorst M.; Baker M.; Perkersen R.; Brown P.; Ravenscroft T.; van Blitterswijk M.; Nicholson A.M.; DeTure M.; Knopman D.S.; Josephs K.A.; Parisi J.E.; Petersen R.C.; Boylan K.B.; Boeve B.F.; Graff-Radford N.R.; Veltman J.A.; Gilissen C.; Murray M.E.; Dickson D.W.; Rademakers R.;
Acta Neuropathol. 130:77-92(2015)
Cited for: INVOLVEMENT IN FTDALS4; VARIANTS FTDALS4 ILE-306; GLU-401 AND LYS-696;
Haploinsufficiency of TBK1 causes familial ALS and fronto-temporal dementia.
Freischmidt A.; Wieland T.; Richter B.; Ruf W.; Schaeffer V.; Mueller K.; Marroquin N.; Nordin F.; Huebers A.; Weydt P.; Pinto S.; Press R.; Millecamps S.; Molko N.; Bernard E.; Desnuelle C.; Soriani M.H.; Dorst J.; Graf E.; Nordstroem U.; Feiler M.S.; Putz S.; Boeckers T.M.; Meyer T.; Winkler A.S.; Winkelman J.; de Carvalho M.; Thal D.R.; Otto M.; Braennstroem T.; Volk A.E.; Kursula P.; Danzer K.M.; Lichtner P.; Dikic I.; Meitinger T.; Ludolph A.C.; Strom T.M.; Andersen P.M.; Weishaupt J.H.;
Nat. Neurosci. 18:631-636(2015)
Cited for: INVOLVEMENT IN FTDALS4; VARIANTS FTDALS4 HIS-47; CYS-105; THR-305; GLN-308; GLN-357; ARG-559; VAL-571; VAL-598; GLU-643 DEL AND LYS-696; CHARACTERIZATION OF VARIANTS FTDALS4 HIS-47; GLN-308; GLN-357; ARG-559 AND LYS-696;
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.