UniProtKB/Swiss-Prot P36871: Variant p.Lys68Met

Phosphoglucomutase-1
Gene: PGM1
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Variant information Variant position:

68 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 Lysine (K) to Methionine (M) at position 68 (K68M, p.Lys68Met). 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:

Change from large size and basic (K) to medium size and hydrophobic (M) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

-1 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
Polymorphism:

Many polymorphic variants of PGM1 exist. 8 different alleles are known: PGM1*1+, PGM1*1-, PGM1*2+, PGM1*2-, PGM1*3+, PGM1*3-, PGM1*7+ and PGM1*7-. The sequence of PGM1*1+ is shown here. Additional information on the polymorphism described.
Variant description:

In allele PGM1*7+, allele PGM1*7-, allele PGM1*3+ and allele PGM1*3-; phosphoglucomutase activity is similar to wild-type. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs200390982 [ dbSNP | Ensembl ]

Sequence information Variant position:

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

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

EPAQRQEATLVVGGDGRFYM K EAIQLIARIAAANGIGRLVI 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                         EPAQRQEATLVVGGDGRFYMKEAIQLIARIAAANGIGRLVI

Mouse                         EPALRQEATLVVGGDGRFYMTEAIQLIVRIAAANGIGRLVI

Rat                           EPALRQEATLVVGGDGRFYMTEAIQLIVRIAAANGIGRLVI

Bovine                        EPAQRQEATLVVGGDGRFYMKEAIQLIVRIAAANGIGRLVI

Rabbit                        EPAQRQEATLVVGGDGRFYMKEAIQLIVRIAAANGIGRLVI

Slime mold                    PEDKLKGSTIVVGGDGRYYNNDAIQLIFQIAAANGVGKILV

Baker's yeast                 -PNGSEGTTLVVGGDGRFYNDVIMNKIAAVGAANGVRKLVI

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 – 562	Phosphoglucomutase-1
Alternative sequence	1 – 197	Missing. In isoform 3.
Alternative sequence	1 – 77	MVKIVTVKTQAYQDQKPGTSGLRKRVKVFQSSANYAENFIQSIISTVEPAQRQEATLVVGGDGRFYMKEAIQLIARI -> MSDFEEWISGTYRKMEEGPLPLLTFATAPYHDQKPGTSGLRKKTYYFEEKPCYLENFIQSIFFSIDLKDRQGSSLVVGGDGRYFNKSAIETIVQM. In isoform 2.
Helix	67 – 80

Literature citations
Intragenic recombination at the human phosphoglucomutase 1 locus: predictions fulfilled.
Takahashi N.; Neels J.V.;
Proc. Natl. Acad. Sci. U.S.A. 90:10725-10729(1993)
Cited for: VARIANTS MET-68; CYS-221 AND HIS-420; Compromised catalysis and potential folding defects in in vitro studies of missense mutants associated with hereditary phosphoglucomutase 1 deficiency.
Lee Y.; Stiers K.M.; Kain B.N.; Beamer L.J.;
J. Biol. Chem. 289:32010-32019(2014)
Cited for: CHARACTERIZATION OF VARIANTS CDG1T ALA-19; TYR-38; ARG-41; HIS-62; ALA-115; ARG-121; GLY-263; TYR-263; ARG-291; ARG-330; LYS-377; LYS-388 AND PRO-516; VARIANTS MET-68; CYS-221 AND HIS-420; FUNCTION; CATALYTIC ACTIVITY; BIOPHYSICOCHEMICAL PROPERTIES; ACTIVE SITE; PHOSPHORYLATION AT SER-117; ACTIVITY REGULATION;

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.