UniProtKB/Swiss-Prot Q15831: Variant p.Phe157Ser

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

Variant position:  157
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 Phenylalanine (F) to Serine (S) at position 157 (F157S, p.Phe157Ser).
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 aromatic (F) to small size and polar (S)
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; impairs heterotrimeric complex assembly with STRADA and CAB39.
Any additional useful information about the variant.



Sequence information

Variant position:  157
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:   QEMLDSVPEKRFPVCQAHGY  F CQLIDGLEYLHSQGIVHKDI
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                         QEMLDSVPEKRFPVCQAHGYFCQLIDGLEYLHSQGIVHKDI

Mouse                         QEMLDSVPEKRFPVCQAHGYFRQLIDGLEYLHSQGIVHKDI

Rat                           QEMLDSVPEKRFPVCQAHGYFRQLIDGLEYLHSQGIVHKDI

Chicken                       QEMLDSVPEKRFPVFQAHGYFCQLIDGLEYLHSQGIVHKDI

Xenopus laevis                QEMLDSVQDKHFPVFQAHGYFCQLIDGLEYLHSQGIVHKDI

Slime mold                    QNILENAPNGRLPPHQSQFIFRQLIEACEYIHSQKILHRDI

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
Active site 176 – 176 Proton acceptor
Helix 150 – 169


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.