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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O15305: Variant p.Asp223Glu

Phosphomannomutase 2
Gene: PMM2
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Variant information Variant position: help 223 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 Aspartate (D) to Glutamate (E) at position 223 (D223E, p.Asp223Glu). 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 Similar physico-chemical property. Both residues are medium size and acidic. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 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: help In CDG1A; normal activity but lower affinity for alpha-D-mannose 1-phosphate. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 223 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 246 The length of the canonical sequence.
Location on the sequence: help TIYFFGDKTMPGGNDHEIFT D PRTMGYSVTAPEDTRRICEL 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                         TIYFFGDKTMPGGNDHEIFTDPR-TMGYSVTAPEDTRRICEL

Mouse                         TIYFFGDKTMPGGNDHEIFTDPR-TVGYTVTAPEDTRRICE

Bovine                        TIYFFGDKTMPGGNDHEIFTDPR-TVGYTVAAPEDTRRICE

Slime mold                    TLYFFGDKTFLGGNDYEIANHPRITQSFTVKSPANTLAILN
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 2 – 246 Phosphomannomutase 2
Binding site 209 – 209
Binding site 221 – 221
Binding site 223 – 223
Binding site 226 – 226
Alternative sequence 120 – 246 Missing. In isoform 2.



Literature citations
Absence of homozygosity for predominant mutations in PMM2 in Danish patients with carbohydrate-deficient glycoprotein syndrome type 1.
Kjaergaard S.; Skovby F.; Schwartz M.;
Eur. J. Hum. Genet. 6:331-336(1998)
Cited for: VARIANTS CDG1A ARG-117 AND GLU-223; Carbohydrate-deficient glycoprotein syndrome type 1A: expression and characterisation of wild type and mutant PMM2 in E. coli.
Kjaergaard S.; Skovby F.; Schwartz M.;
Eur. J. Hum. Genet. 7:884-888(1999)
Cited for: VARIANT CDG1A GLY-192; CHARACTERIZATION OF VARIANTS CDG1A ARG-117; LEU-119; HIS-141; GLY-192; GLU-223 AND ARG-237; Mutations in PMM2 that cause congenital disorders of glycosylation, type Ia (CDG-Ia).
Matthijs G.; Schollen E.; Bjursell C.; Erlandson A.; Freeze H.; Imtiaz F.; Kjaergaard S.; Martinsson T.; Schwartz M.; Seta N.; Vuillaumier-Barrot S.; Westphal V.; Winchester B.;
Hum. Mutat. 16:386-394(2000)
Cited for: VARIANTS CDG1A TYR-9; CYS-11; ARG-32; ALA-44; TYR-65; MET-67; SER-69; CYS-76; LYS-101; PHE-103; CYS-106; VAL-108; LEU-113; ARG-117; LEU-119; THR-120; GLN-123; MET-129; ALA-131; ASN-132; THR-132; LYS-139; HIS-141; ASN-148; GLY-151; THR-153; SER-157; TRP-162; VAL-172; ARG-175; SER-183; GLY-185; GLY-188; GLY-192; ARG-195; SER-206; ALA-208; ILE-216; SER-216; GLU-217; LEU-218; GLU-223; SER-226; ARG-228; CYS-228; SER-229; MET-231; THR-233; ARG-237; MET-237; GLY-238 AND SER-241; VARIANT ALA-197; PMM2 mutation spectrum, including 10 novel mutations, in a large CDG type 1A family material with a focus on Scandinavian families.
Bjursell C.; Erlandson A.; Nordling M.; Nilsson S.; Wahlstroem J.; Stibler H.; Kristiansson B.; Martinsson T.;
Hum. Mutat. 16:395-400(2000)
Cited for: VARIANTS CDG1A TYR-9; CYS-11; MET-67; LEU-113; ARG-117; LEU-119; GLN-123; MET-129; HIS-141; VAL-172; ARG-175; SER-183; GLY-185; GLY-192; SER-216; GLU-217; GLU-223; ARG-228; MET-231 AND ARG-237;
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.