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UniProtKB/Swiss-Prot P36871: Variant p.Gly121Arg

Phosphoglucomutase-1
Gene: PGM1
Variant information

Variant position:  121
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  LP/P [Disclaimer]
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 Glycine (G) to Arginine (R) at position 121 (G121R, p.Gly121Arg).
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 glycine (G) to large size and basic (R)
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 CDG1T; there is 7% enzyme residual phosphoglucomutase activity.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  121
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:   CIIRKIKAIGGIILTASHNP  G GPNGDFGIKFNISNGGPAPE
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                         CIIR---KIKAIGGIILTASHNPGGPNGDFGIKFNISNGGPAPE

Mouse                         CIIR---KIKAIGGIILTASHNPGGPNGDFGIKFNISNGGP

Rat                           CIIR---KIKAIGGIILTASHNPGGPNGDFGIKFNISNGGP

Bovine                        CIIR---KIKAIGGIILTASHNPGGPNGDFGIKFNISNGGP

Rabbit                        CIIR---KIKAIGGIILTASHNPGGPNGDFGIKFNISNGGP

Slime mold                    AIVR---ARSALGAIILTASHNPGGPNGDFGIKYNMSNGGP

Baker's yeast                 HIIRTYEEKCTGGGIILTASHNPGGPENDLGIKYNLPNGGP

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.

TypePositionsDescription
Chain 1 – 562 Phosphoglucomutase-1
Active site 117 – 117 Phosphoserine intermediate
Metal binding 117 – 117 Magnesium; via phosphate group
Binding site 130 – 130 Substrate
Modified residue 115 – 115 Phosphothreonine
Modified residue 117 – 117 Phosphoserine
Modified residue 134 – 134 Phosphoserine
Alternative sequence 1 – 197 Missing. In isoform 3.


Literature citations

Induced structural disorder as a molecular mechanism for enzyme dysfunction in phosphoglucomutase 1 deficiency.
Stiers K.M.; Kain B.N.; Graham A.C.; Beamer L.J.;
J. Mol. Biol. 428:1493-1505(2016)
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF WILD-TYPE; VARIANT CDG1T ARG-121 AND VARIANT ARG-291 IN COMPLEX WITH MAGNESIUM; COFACTOR;

Gene identification in the congenital disorders of glycosylation type I by whole-exome sequencing.
Timal S.; Hoischen A.; Lehle L.; Adamowicz M.; Huijben K.; Sykut-Cegielska J.; Paprocka J.; Jamroz E.; van Spronsen F.J.; Korner C.; Gilissen C.; Rodenburg R.J.; Eidhof I.; Van den Heuvel L.; Thiel C.; Wevers R.A.; Morava E.; Veltman J.; Lefeber D.J.;
Hum. Mol. Genet. 21:4151-4161(2012)
Cited for: VARIANT CDG1T ARG-121;

Multiple phenotypes in phosphoglucomutase 1 deficiency.
Tegtmeyer L.C.; Rust S.; van Scherpenzeel M.; Ng B.G.; Losfeld M.E.; Timal S.; Raymond K.; He P.; Ichikawa M.; Veltman J.; Huijben K.; Shin Y.S.; Sharma V.; Adamowicz M.; Lammens M.; Reunert J.; Witten A.; Schrapers E.; Matthijs G.; Jaeken J.; Rymen D.; Stojkovic T.; Laforet P.; Petit F.; Aumaitre O.; Czarnowska E.; Piraud M.; Podskarbi T.; Stanley C.A.; Matalon R.; Burda P.; Seyyedi S.; Debus V.; Socha P.; Sykut-Cegielska J.; van Spronsen F.; de Meirleir L.; Vajro P.; DeClue T.; Ficicioglu C.; Wada Y.; Wevers R.A.; Vanderschaeghe D.; Callewaert N.; Fingerhut R.; van Schaftingen E.; Freeze H.H.; Morava E.; Lefeber D.J.; Marquardt T.;
N. Engl. J. Med. 370:533-542(2014)
Cited for: VARIANTS CDG1T ALA-19; TYR-38; ARG-41; HIS-62; ALA-115; ARG-121; TYR-263; GLY-263; ARG-291; ARG-330; LYS-377; LYS-388 AND PRO-516;

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; 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.