Variant position: 194 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 HKDIKPGNLLLTTGGTLKIS DLGVAEALHPFAADDTCRTSQ
Mouse HKDIKPGNLLLTTNGTLKIS DLGVAEALHPFAVDDTCRTSQ
Rat HKDIKPGNLLLTTNGTLKIS DLGVAEALHPFAVDDTCRTSQ
Chicken HKDIKPGNLLLTTNGTLKIS DLGVAEALHPFAEDDTCRTSQ
Xenopus laevis HKDIKPGNLLLTTDGTLKIS DLGVAEALHPFAEGDTCRTSQ
Slime mold HRDIKPDNILFTHANVLKLS DFGVAEDSSQLEDFECLSRSY
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
176 – 176 Proton acceptor
189 – 189 Phosphothreonine; by autocatalysis
189 – 189 T -> A. Reduced phosphorylation.
194 – 194 D -> A. Loss of kinase activity.
204 – 204 F -> A. No effect. Impaired formation of a heterotrimeric complex with STRADA and CAB39; when associated with A-74.
LKB1 somatic mutations in sporadic cancers.
Avizienyte E.; Loukola A.; Roth S.; Hemminki A.; Tarkkanen M.; Salovaara R.; Arola J.; Butzow R.; Husgafvel-Pursiainen K.; Kokkola A.; Jarvinen H.; Aaltonen L.A.;
Am. J. Pathol. 154:677-681(1999)
Cited for: VARIANT LUNG CANCER VAL-194;
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