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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q15831: Variant p.Leu67Pro

Serine/threonine-protein kinase STK11
Gene: STK11
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Variant information Variant position: help 67 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance
Residue change: help From Leucine (L) to Proline (P) at position 67 (L67P, p.Leu67Pro). 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: help Similar physico-chemical property. Both residues are medium size and hydrophobic. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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: help In PJS; abolishes kinase activity, leading to loss of autophosphorylation. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 67 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 433 The length of the canonical sequence.
Location on the sequence: help GKYLMGDLLGEGSYGKVKEV L DSETLCRRAVKILKKKKLRR 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         GKYLMGDLLGEGSYGKVKEVLDSETLCRRAVKILKKKKLRR

Mouse                         GKYLMGDLLGEGSYGKVKEVLDSETLCRRAVKILKKKKLRR

Rat                           GKYLMGDLLGEGSYGKVKEVLDSETLCRRAVKILKKKKLRR

Chicken                       GKYLMGDLLGEGSYGKVKEMLDSETLCRRAVKILKKKKLRR

Xenopus laevis                GKYLMGDLLGEGSYGKVKEMLDSDTLCRRAVKILKKKKLRR

Slime mold                    KHYILGEVLGEGAYGKVKDGMDSFTQKRVAVKILKRARLKK
Sequence annotation in neighborhood: help 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
Modified residue 48 – 48 N6-acetyllysine
Mutagenesis 48 – 48 K -> Q. No effect on basal nucleocytoplasmic localization, but fails to translocate to the cytoplasm when coexpressed with SIRT1.
Mutagenesis 48 – 48 K -> R. Enhanced phosphorylation at Thr-336 and Ser-428, enhanced cytoplasmic localization and increased kinase activity.
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.
Beta strand 62 – 68



Literature citations
Loss of LKB1 kinase activity in Peutz-Jeghers syndrome, and evidence for allelic and locus heterogeneity.
Mehenni H.; Gehrig C.; Nezu J.; Oku A.; Shimane M.; Rossier C.; Guex N.; Blouin J.L.; Scott H.S.; Antonarakis S.E.;
Am. J. Hum. Genet. 63:1641-1650(1998)
Cited for: VARIANTS PJS 50-LEU--ASP-53 DEL; ASN-176 AND CYS-308; CHARACTERIZATION OF VARIANTS PJS PRO-67; ASN-176 AND CYS-308; MUTAGENESIS OF LYS-78; A serine/threonine kinase gene defective in Peutz-Jeghers syndrome.
Hemminki A.; Markie D.; Tomlinson I.; Avizienyte E.; Roth S.; Loukola A.; Bignell G.; Warren W.; Aminoff M.; Hoeglund P.; Jaervinen H.; Kristo P.; Pelin K.; Ridanpaeae M.; Salovaara R.; Toro T.; Bodmer W.; Olschwang S.; Olsen A.S.; Stratton M.R.; de la Chapelle A.; Aaltonen L.A.;
Nature 391:184-187(1998)
Cited for: VARIANTS PJS PRO-67 AND 303-ILE--GLN-306 DELINS ASN;
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.