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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P36871: Variant p.Glu377Lys

Phosphoglucomutase-1
Gene: PGM1
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Variant information Variant position: help 377 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help 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: help From Glutamate (E) to Lysine (K) at position 377 (E377K, p.Glu377Lys). 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: help Change from medium size and acidic (E) to large size and basic (K) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 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
Variant description: help In CDG1T; decreases strongly solubility. Any additional useful information about the variant.


Sequence information Variant position: help 377 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 562 The length of the canonical sequence.
Location on the sequence: help TGWKFFGNLMDASKLSLCGE E SFGTGSDHIREKDGLWAVLA 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         TGWKFFGNLMDASKLSLCGEESFGTGSDHIREKDGLWAVLA

Mouse                         TGWKFFGNLMDASKLSLCGEESFGTGSDHIREKDGLWAVLA

Rat                           TGWKFFGNLMDASKLSLCGEESFGTGSDHIREKDGLWAVLA

Bovine                        TGWKFFGNLMDASKLSLCGEESFGTGSDHIREKDGLWAVLA

Rabbit                        TGWKFFGNLMDASKLSLCGEESFGTGSDHIREKDGLWAVLA

Slime mold                    TGWKFFGNLMDAGTLSICGEESFGTGSDHIREKDGIWAIIC

Baker's yeast                 TGWKFFCALFDAKKLSICGEESFGTGSNHIREKDGLWAIIA
Sequence annotation in neighborhood: help 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
Binding site 357 – 357
Binding site 376 – 376
Binding site 378 – 378
Binding site 389 – 389
Modified residue 369 – 369 Phosphoserine
Modified residue 378 – 378 Phosphoserine
Turn 377 – 379



Literature citations
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; 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.