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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O15305: Variant p.Phe119Leu

Phosphomannomutase 2
Gene: PMM2
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Variant information Variant position: help 119 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 Phenylalanine (F) to Leucine (L) at position 119 (F119L, p.Phe119Leu). 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 large size and aromatic (F) to medium size and hydrophobic (L) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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; partial loss of activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 119 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 LINYCLSYIAKIKLPKKRGT F IEFRNGMLNVSPIGRSCSQE 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                         LINYCLSYIAKIKLPKKRGTFIEFRNGMLNVSPIGRSCSQE

Mouse                         LINYCLSYIANIKLPKKRGTFIEFRNGMLNVSPIGRSCSQE

Bovine                        LINYCLSYIAKIKLPKKRGTFIEFRNGMLNVSPIGRSCSQE

Slime mold                    FINFVLHYVADLDIPIKRGTFVEFRNGMLNISPIGRNCSQQ
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 123 – 123
Binding site 134 – 134
Alternative sequence 117 – 119 GTF -> KKI. In isoform 2.
Beta strand 119 – 122



Literature citations
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; Genotypes and phenotypes of patients in the UK with carbohydrate-deficient glycoprotein syndrome type 1.
Imtiaz F.; Worthington V.; Champion M.; Beesley C.; Charlwood J.; Clayton P.; Keir G.; Mian N.; Winchester B.;
J. Inherit. Metab. Dis. 23:162-174(2000)
Cited for: VARIANTS CDG1A LEU-119; ASN-132; HIS-141; ASN-148; SER-183; ALA-208; MET-231 AND MET-237; A new insight into PMM2 mutations in the French population.
Le Bizec C.; Vuillaumier-Barrot S.; Barnier A.; Dupre T.; Durand G.; Seta N.;
Hum. Mutat. 25:504-505(2005)
Cited for: VARIANTS CDG1A TYR-9; SER-20; ARG-32; HIS-37; LEU-44; TYR-65; SER-69; PHE-103; VAL-108; LEU-113; LEU-119; GLN-123; MET-129; ALA-131; THR-132; PHE-132; LYS-139; CYS-141; HIS-141; THR-153; SER-157; TRP-162; VAL-176; HIS-177; SER-214; SER-226; MET-231; ARG-237; MET-237 AND SER-241; VARIANTS ARG-42 AND ALA-197; CHARACTERIZATION OF VARIANTS CDG1A SER-20; HIS-37; PHE-132; LYS-139; CYS-141; HIS-141; VAL-176 AND HIS-177;
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.