UniProtKB/Swiss-Prot Q15831: Variant p.Arg86Gly

Serine/threonine-protein kinase STK11
Gene: STK11
Chromosomal location: 19p13.3
Variant information

Variant position:  86
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Unclassified
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants have been found in patients and disease-association is reported in literature. However, this classification is not a definitive assessment of variant pathogenicity.
  • Polymorphism: No disease-association has been reported.
  • Unclassified: Variants have been found in patients but disease-association remains unclear.

Residue change:  From Arginine (R) to Glycine (G) at position 86 (R86G, p.Arg86Gly).
Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.

Physico-chemical properties:  Change from large size and basic (R) to glycine (G)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -2
The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page

Variant description:  In sporadic cancer; somatic mutation; no effect on kinase activity nor in heterotrimeric complex assembly with STRADA and CAB39.
Any additional useful information about the variant.



Sequence information

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:   VLDSETLCRRAVKILKKKKL  R RIPNGEANVKKEIQLLRRLR
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                         VLDSETLCRRAVKILKKKKLRRIPNGEANVKKEIQLLRRLR

Mouse                         VLDSETLCRRAVKILKKKKLRRIPNGEANVKKEIQLLRRLR

Rat                           VLDSETLCRRAVKILKKKKLRRIPNGEANVKKEIQLLRRLR

Chicken                       MLDSETLCRRAVKILKKKKLRRIPNGEANVKKEIQLLRRLR

Xenopus laevis                MLDSDTLCRRAVKILKKKKLRRIPNGEANVKKEIQLLRRLR

Slime mold                    GMDSFTQKRVAVKILKRARLKKIPGGEASVLKEINITKKLH

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.

TypePositionsDescription
Chain 1 – 430 Serine/threonine-protein kinase STK11
Domain 49 – 309 Protein kinase
Region 45 – 90 Sufficient for interaction with SIRT1
Binding site 78 – 78 ATP
Modified residue 96 – 96 N6-acetyllysine
Modified residue 97 – 97 N6-acetyllysine
Mutagenesis 74 – 74 R -> A. Impaired formation of a heterotrimeric complex with STRADA and CAB39; when associated with A-204.
Mutagenesis 78 – 78 K -> I. Loss of kinase activity, leading to greatly reduced autophosphorylation.
Mutagenesis 78 – 78 K -> M. Loss of kinase activity, leading to reduced autophosphorylation and acting as a dominant-negative mutant.
Mutagenesis 96 – 96 K -> R. No effect on kinase activity.
Mutagenesis 97 – 97 K -> R. No effect on kinase activity.
Helix 82 – 87


Literature citations

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.;
Science 326:1707-1711(2009)
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;

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.