UniProtKB/Swiss-Prot Q15831: Variant p.Arg87Lys

Serine/threonine-protein kinase STK11
Gene: STK11
Feedback?

Variant information Variant position:

87 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

US 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:

From Arginine (R) to Lysine (K) at position 87 (R87K, p.Arg87Lys). 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:

Similar physico-chemical property. Both residues are large size and basic. 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 a metastatic melanoma sample; somatic mutation. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs1568690463 [ dbSNP | Ensembl ]

Sequence information Variant position:

87 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:

LDSETLCRRAVKILKKKKLR R IPNGEANVKKEIQLLRRLRH 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                         LDSETLCRRAVKILKKKKLRRIPNGEANVKKEIQLLRRLRH

Mouse                         LDSETLCRRAVKILKKKKLRRIPNGEANVKKEIQLLRRLRH

Rat                           LDSETLCRRAVKILKKKKLRRIPNGEANVKKEIQLLRRLRH

Chicken                       LDSETLCRRAVKILKKKKLRRIPNGEANVKKEIQLLRRLRH

Xenopus laevis                LDSDTLCRRAVKILKKKKLRRIPNGEANVKKEIQLLRRLRH

Slime mold                    MDSFTQKRVAVKILKRARLKKIPGGEASVLKEINITKKLHN

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
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	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
Patterns of somatic mutation in human cancer genomes.
Greenman C.; Stephens P.; Smith R.; Dalgliesh G.L.; Hunter C.; Bignell G.; Davies H.; Teague J.; Butler A.; Stevens C.; Edkins S.; O'Meara S.; Vastrik I.; Schmidt E.E.; Avis T.; Barthorpe S.; Bhamra G.; Buck G.; Choudhury B.; Clements J.; Cole J.; Dicks E.; Forbes S.; Gray K.; Halliday K.; Harrison R.; Hills K.; Hinton J.; Jenkinson A.; Jones D.; Menzies A.; Mironenko T.; Perry J.; Raine K.; Richardson D.; Shepherd R.; Small A.; Tofts C.; Varian J.; Webb T.; West S.; Widaa S.; Yates A.; Cahill D.P.; Louis D.N.; Goldstraw P.; Nicholson A.G.; Brasseur F.; Looijenga L.; Weber B.L.; Chiew Y.-E.; DeFazio A.; Greaves M.F.; Green A.R.; Campbell P.; Birney E.; Easton D.F.; Chenevix-Trench G.; Tan M.-H.; Khoo S.K.; Teh B.T.; Yuen S.T.; Leung S.Y.; Wooster R.; Futreal P.A.; Stratton M.R.;
Nature 446:153-158(2007)
Cited for: VARIANT [LARGE SCALE ANALYSIS] LYS-87;

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.