Variant position: 50 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:
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 KTGDLFAIKVFNNISFLRPV DVQMREFEVLKKLNHKNIVKL
Mouse KTGDLYAVKVFNNISFLRPV DVQMREFEVLKKLNHKNIVKL
Xenopus laevis KTGDLYAVKVFNSLSFQRPA DVQMREFEVLKKLNHKNIVKL
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
1 – 729 Serine/threonine-protein kinase TBK1
9 – 310 Protein kinase
38 – 38 ATP
30 – 30 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
30 – 30 K -> R. Decreases ubiquitination. Abolishes ubiquitination, phosphorylation and kinase activity; when associated with R-401.
33 – 33 D -> A. Decreases phosphorylation and kinase activity.
38 – 38 K -> A. Loss of kinase activity.
49 – 61
Heterozygous TBK1 mutations impair TLR3 immunity and underlie herpes simplex encephalitis of childhood.
Herman M.; Ciancanelli M.; Ou Y.H.; Lorenzo L.; Klaudel-Dreszler M.; Pauwels E.; Sancho-Shimizu V.; Perez de Diego R.; Abhyankar A.; Israelsson E.; Guo Y.; Cardon A.; Rozenberg F.; Lebon P.; Tardieu M.; Heropolitanska-Pliszka E.; Chaussabel D.; White M.A.; Abel L.; Zhang S.Y.; Casanova J.L.;
J. Exp. Med. 209:1567-1582(2012)
Cited for: INVOLVEMENT IN IIAE8; VARIANTS IIAE8 ALA-50 AND ALA-159; CHARACTERIZATION OF VARIANTS IIAE8 ALA-50 AND ALA-159; MUTAGENESIS OF LYS-38; PHOSPHORYLATION AT SER-172; FUNCTION;
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.