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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P25189: Variant p.Gly123Cys

Myelin protein P0
Gene: MPZ
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Variant information Variant position: help 123 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 Glycine (G) to Cysteine (C) at position 123 (G123C, p.Gly123Cys). 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 glycine (G) to medium size and polar (C) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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 DSS and CMT1B. Any additional useful information about the variant.


Sequence information Variant position: help 123 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 248 The length of the canonical sequence.
Location on the sequence: help GDPRWKDGSIVIHNLDYSDN G TFTCDVKNPPDIVGKTSQVT 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                         GDPRWKDGSIVIHNLDYSDNGTFTCDVKNPPDIVGKTSQVT

Mouse                         GDPRWKDGSIVIHNLDYSDNGTFTCDVKNPPDIVGKTSQVT

Rat                           GDPSWKDGSIVIHNLDYSDNGTFTCDVKNPPDIVGKTSQVT

Bovine                        GDPHRKDGSIVIHNLDYGDNGTFTCDVKNPPDIVGKTSQVT

Horse                         GDPQWKDGSIVIHNLDYSDNGTFTCDVKNPPDIVGKTSQVT

Chicken                       GNPRRKDGSIVIHNLDYTDNGTFTCDVKNPPDIVGKSSQVT

Xenopus laevis                GSPKWKDASIVVHNLELTDNGTFTCDVKNPPDVVGKSSYVH

Xenopus tropicalis            GSPKWKDASIVLHNLELIDNGTFTCDVKNPPDVVGKSSYVH
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 30 – 248 Myelin protein P0
Topological domain 30 – 153 Extracellular
Domain 30 – 143 Ig-like V-type
Glycosylation 122 – 122 N-linked (GlcNAc...) (complex) asparagine
Disulfide bond 50 – 127
Beta strand 123 – 130



Literature citations
Charcot-Marie-Tooth disease and related neuropathies: mutation distribution and genotype-phenotype correlation.
Boerkoel C.F.; Takashima H.; Garcia C.A.; Olney R.K.; Johnson J.; Berry K.; Russo P.; Kennedy S.; Teebi A.S.; Scavina M.; Williams L.L.; Mancias P.; Butler I.J.; Krajewski K.; Shy M.; Lupski J.R.;
Ann. Neurol. 51:190-201(2002)
Cited for: VARIANTS CMT1B LEU-78 AND CYS-82; VARIANTS CMT2I ASN-89; MET-92 AND MET-162; VARIANTS DSS CYS-123 AND GLU-136; Phenotypic clustering in MPZ mutations.
Shy M.E.; Jani A.; Krajewski K.; Grandis M.; Lewis R.A.; Li J.; Shy R.R.; Balsamo J.; Lilien J.; Garbern J.Y.; Kamholz J.;
Brain 127:371-384(2004)
Cited for: VARIANTS CMT1B PRO-39; PHE-44; CYS-50 DEL; HIS-98; CYS-123; ARG-130; THR-140 AND SER-227;
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.