UniProtKB/Swiss-Prot P09467: Variant p.Arg218Lys

Fructose-1,6-bisphosphatase 1
Gene: FBP1
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Variant information Variant position:

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

LB/B 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 218 (R218K, p.Arg218Lys). 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
Other resources:

Links to websites of interest for the variant.

Variant rs1769259 [ dbSNP | Ensembl ]

Sequence information Variant position:

218 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

338 The length of the canonical sequence.
Location on the sequence:

DKDVKIKKKGKIYSLNEGYA R DFDPAVTEYIQRKKFPPDNS 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                         DKDVKIKKKGKIYSLNEGYARDFDPAVTEYIQRKKFPPDNS

Mouse                         DRDVKMKKKGNIYSLNEGYAKDFDPAINEYLQRKKFPPDGS

Rat                           DRDVKIKKKGNIYSINEGYAKDFDPAINEYIQRKKFPPDNS

Pig                           DRDVKIKKKGSIYSINEGYAKEFDPAITEYIQRKKFPPDNS

Bovine                        DRDVKIKKKGSIYSLNEGYAKDFDPALTEYVQRKKFPPDNS

Rabbit                        DKNVKIKKKGNIYSLNEGYAKDFDPAVTEYIQKKKFPPDNS

Sheep                         DRDVKIKKKGSIYSLNEGYAKDFDPALTEYVQRKKFPPDNS

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	2 – 338	Fructose-1,6-bisphosphatase 1
Modified residue	216 – 216	Phosphotyrosine
Helix	214 – 219

Literature citations
Activation of the fructose 1,6-bisphosphatase gene by 1,25-dihydroxyvitamin D3 during monocytic differentiation.
Solomon D.H.; Raynal M.-C.; Tejwani G.A.; Cayre Y.E.;
Proc. Natl. Acad. Sci. U.S.A. 85:6904-6908(1988)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; VARIANT LYS-218; Isolation of a human liver fructose-1,6-bisphosphatase cDNA and expression of the protein in Escherichia coli. Role of Asp-118 and Asp-121 in catalysis.
El-Maghrabi M.R.; Gidh-Jain M.; Austin L.R.; Pilkis S.J.;
J. Biol. Chem. 268:9466-9472(1993)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; PROTEIN SEQUENCE OF 2-11; CATALYTIC ACTIVITY; MUTAGENESIS OF ASP-119 AND ASP-122; VARIANT LYS-218; cDNA sequences encoding human fructose 1,6-bisphosphatase from monocytes, liver and kidney: application of monocytes to molecular analysis of human fructose 1,6-bisphosphatase deficiency.
Kikawa Y.; Inuzuka M.; Takano T.; Shigematsu Y.; Nakai A.; Yamamoto Y.; Jin B.Y.; Koga J.; Taketo A.; Sudo M.;
Biochem. Biophys. Res. Commun. 199:687-693(1994)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; VARIANT LYS-218; Human fructose-1,6-bisphosphatase gene (FBP1): exon-intron organization, localization to chromosome bands 9q22.2-q22.3, and mutation screening in subjects with fructose-1,6-bisphosphatase deficiency.
El-Maghrabi M.R.; Lang A.J.; Jiang W.; Yamagata K.; Stoffel M.; Takeda J.; Fernald A.A.; le Beau M.M.; Bell G.I.; Baker L.; Pilkis S.J.;
Genomics 27:520-525(1995)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANT LYS-218; cDNA sequence and kinetic properties of human lung fructose(1, 6)bisphosphatase.
Skalecki K.; Rakus D.; Wisniewski J.R.; Kolodziej J.; Dzugaj A.;
Arch. Biochem. Biophys. 365:1-9(1999)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; CHARACTERIZATION; VARIANT LYS-218; Submission
Totoki Y.; Toyoda A.; Takeda T.; Sakaki Y.; Tanaka A.; Yokoyama S.;
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]; VARIANT LYS-218; Submission
NIEHS SNPs program;
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANTS LYS-218; ILE-233 AND LEU-255;

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.