Variant position: 86 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 433 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 VLDSETLCRRAVKILKKKKL RRIPNGEANVKKEIQLLRRLR
Mouse VLDSETLCRRAVKILKKKKL RRIPNGEANVKKEIQLLRRLR
Rat VLDSETLCRRAVKILKKKKL RRIPNGEANVKKEIQLLRRLR
Chicken MLDSETLCRRAVKILKKKKL RRIPNGEANVKKEIQLLRRLR
Xenopus laevis MLDSDTLCRRAVKILKKKKL RRIPNGEANVKKEIQLLRRLR
Slime mold GMDSFTQKRVAVKILKRARL KKIPGGEASVLKEINITKKLH
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 – 430 Serine/threonine-protein kinase STK11
49 – 309 Protein kinase
45 – 90 Sufficient for interaction with SIRT1
78 – 78 ATP
96 – 96 N6-acetyllysine
97 – 97 N6-acetyllysine
74 – 74 R -> A. Impaired formation of a heterotrimeric complex with STRADA and CAB39; when associated with A-204.
78 – 78 K -> I. Loss of kinase activity, leading to greatly reduced autophosphorylation.
78 – 78 K -> M. Loss of kinase activity, leading to reduced autophosphorylation and acting as a dominant-negative mutant.
96 – 96 K -> R. No effect on kinase activity.
97 – 97 K -> R. No effect on kinase activity.
82 – 87
Structure of the LKB1-STRAD-MO25 complex reveals an allosteric mechanism of kinase activation.
Zeqiraj E.; Filippi B.M.; Deak M.; Alessi D.R.; van Aalten D.M.;
Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 43-347 IN COMPLEX WITH STRADA AND CAB39; ENZYME REGULATION; CHARACTERIZATION OF VARIANTS SPORADIC CANCER MET-66; GLY-86; ARG-123; SER-157; ASP-163; PRO-170; SER-171; ARG-174; TYR-176; ASN-177; GLU-181; GLN-199; THR-205; PHE-216; VAL-223; PRO-230; PRO-232; ARG-245; PRO-250; HIS-272; TYR-277; GLN-285 AND SER-315; MUTAGENESIS OF ARG-74; ASP-194 AND PHE-204;
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.