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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P25189: Variant p.Arg98Cys

Myelin protein P0
Gene: MPZ
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Variant information Variant position: help 98 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 Arginine (R) to Cysteine (C) at position 98 (R98C, p.Arg98Cys). 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 basic (R) 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 CMT1B and DSS; severe. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 98 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 SIFHYAKGQPYIDEVGTFKE R IQWVGDPRWKDGSIVIHNLD 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                         SIFHYAKGQPYIDEVGTFKERIQWVGDPRWKDGSIVIHNLD

Mouse                         SIFHYAKGQPYIDEVGAFKERIQWVGDPRWKDGSIVIHNLD

Rat                           SIFHYAKGQPYIDEVGTFKERIQWVGDPSWKDGSIVIHNLD

Bovine                        SIFHYAKGQPYIDEVGTFKERIQWVGDPHRKDGSIVIHNLD

Horse                         SIFHYAKGQPYIDEVGTFKERIQWVGDPQWKDGSIVIHNLD

Chicken                       SIFHYGKGQPYIDDVGSFKERMEWVGNPRRKDGSIVIHNLD

Xenopus laevis                SIVHFAKGLSSID-AGIFKDRIEWVGSPKWKDASIVVHNLE

Xenopus tropicalis            SIFHYAKGQPSID-AGVFKDRIEWVGSPKWKDASIVLHNLE
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
Disulfide bond 50 – 127



Literature citations
Two divergent types of nerve pathology in patients with different P0 mutations in Charcot-Marie-Tooth disease.
Gabreeels-Festen A.A.W.M.; Hoogendijk J.E.; Meijerink P.H.; Gabreeels F.J.M.; Bolhuis P.A.; van Beersum S.; Kulkens T.; Nelis E.; Jennekens F.G.; de Visser M.; van Engelen B.G.; van Broeckhoven C.; Mariman E.C.;
Neurology 47:761-765(1996)
Cited for: VARIANTS CMT1B/DSS ILE-34; CYS-98; HIS-98; ARG-130 AND LEU-135; Clinical phenotypes of different MPZ (P0) mutations may include Charcot-Marie-Tooth type 1B, Dejerine-Sottas, and congenital hypomyelination.
Warner L.E.; Hilz M.J.; Appel S.H.; Killian J.M.; Kolodry E.H.; Karpati G.; Carpenter S.; Watters G.V.; Wheeler C.; Witt D.; Bodell A.; Nelis E.; van Broeckhoven C.; Lupski J.R.;
Neuron 17:451-460(1996)
Cited for: VARIANTS CMT1B CYS-98 AND SER-98; VARIANT DSS CYS-98; VARIANT CHN2 215-GLN--LYS-248 DEL; Mutational analysis of the MPZ, PMP22 and Cx32 genes in patients of Spanish ancestry with Charcot-Marie-Tooth disease and hereditary neuropathy with liability to pressure palsies.
Bort S.; Nelis E.; Timmerman V.; Sevilla T.; Cruz-Martinez A.; Martinez F.; Millan J.M.; Arpa J.; Vilchez J.J.; Prieto F.; van Broeckhoven C.; Palau F.;
Hum. Genet. 99:746-754(1997)
Cited for: VARIANT CMT1B LEU-78; VARIANT DSS CYS-98; Charcot-Marie-Tooth disease type I and related demyelinating neuropathies: mutation analysis in a large cohort of Italian families.
Mostacciuolo M.L.; Righetti E.; Zortea M.; Bosello V.; Schiavon F.; Vallo L.; Merlini L.; Siciliano G.; Fabrizi G.M.; Rizzuto N.; Milani M.; Baratta S.; Taroni F.;
Hum. Mutat. 18:32-41(2001)
Cited for: VARIANTS CMT1B PHE-63 AND MET-124; VARIANTS DSS CYS-98 AND 124-THR-PHE-125 DEL; Demyelinating and axonal features of Charcot-Marie-Tooth disease with mutations of myelin-related proteins (PMP22, MPZ and Cx32): a clinicopathological study of 205 Japanese patients.
Hattori N.; Yamamoto M.; Yoshihara T.; Koike H.; Nakagawa M.; Yoshikawa H.; Ohnishi A.; Hayasaka K.; Onodera O.; Baba M.; Yasuda H.; Saito T.; Nakashima K.; Kira J.; Kaji R.; Oka N.; Sobue G.;
Brain 126:134-151(2003)
Cited for: VARIANTS CMT1B TYR-35; PHE-62; SER-63 DEL; CYS-68; GLU-93; CYS-98 AND PHE-146; VARIANTS CMT2I VAL-75; ARG-81; MET-124; ARG-130 AND ARG-167;
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.