Variant position: 67 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 GKYLMGDLLGEGSYGKVKEV LDSETLCRRAVKILKKKKLRR
Mouse GKYLMGDLLGEGSYGKVKEV LDSETLCRRAVKILKKKKLRR
Rat GKYLMGDLLGEGSYGKVKEV LDSETLCRRAVKILKKKKLRR
Chicken GKYLMGDLLGEGSYGKVKEM LDSETLCRRAVKILKKKKLRR
Xenopus laevis GKYLMGDLLGEGSYGKVKEM LDSDTLCRRAVKILKKKKLRR
Slime mold KHYILGEVLGEGAYGKVKDG MDSFTQKRVAVKILKRARLKK
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
48 – 48 N6-acetyllysine
48 – 48 K -> Q. No effect on basal nucleocytoplasmic localization, but fails to translocate to the cytoplasm when coexpressed with SIRT1.
48 – 48 K -> R. Enhanced phosphorylation at Thr-336 and Ser-428, enhanced cytoplasmic localization and increased kinase activity.
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.
62 – 68
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.;
Cited for: VARIANTS PJS PRO-67 AND 303-ILE--GLN-306 DELINS ASN;
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