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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P25189: Variant p.Asp75Val

Myelin protein P0
Gene: MPZ
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Variant information Variant position: help 75 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 Valine (V) at position 75 (D75V, p.Asp75Val). 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 (D) to medium size and hydrophobic (V) 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 CMT2J and CMT2I. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 75 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 SEWVSDDISFTWRYQPEGGR D AISIFHYAKGQPYIDEVGTF 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                         SEWVSDDISFTWRYQPEGGRDAISIFHYAKGQPYIDEVGTF

Mouse                         SEWVSDDISFTWRYQPEGGRDAISIFHYAKGQPYIDEVGAF

Rat                           SEWVSDDISFTWRYQPEGGRDAISIFHYAKGQPYIDEVGTF

Bovine                        SEWVSDDLSFTWRYQPEGGRDAISIFHYAKGQPYIDEVGTF

Horse                         SEWVSDDISFTWRYQPEGGRDAISIFHYAKGQPYIDEVGTF

Chicken                       SEWISEDISYTWHFQAEGSRDSISIFHYGKGQPYIDDVGSF

Xenopus laevis                SEWISDDISVTWHYQPDHSREMYSIVHFAKGLSSID-AGIF

Xenopus tropicalis            SEWISDDVSVTWHYQPDHSREMYSIFHYAKGQPSID-AGVF
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
An axonal form of Charcot-Marie-Tooth disease showing distinctive features in association with mutations in the peripheral myelin protein zero gene (Thr124Met or Asp75Val).
Misu K.; Yoshihara T.; Shikama Y.; Awaki E.; Yamamoto M.; Hattori N.; Hirayama M.; Takegami T.; Nakashima K.; Sobue G.;
J. Neurol. Neurosurg. Psych. 69:806-811(2000)
Cited for: VARIANTS CMT2J VAL-75 AND MET-124; Molecular analysis in Japanese patients with Charcot-Marie-Tooth disease: DGGE analysis for PMP22, MPZ, and Cx32/GJB1 mutations.
Numakura C.; Lin C.; Ikegami T.; Guldberg P.; Hayasaka K.;
Hum. Mutat. 20:392-398(2002)
Cited for: VARIANTS CMT1B SER-63 DEL; ILE-65; CYS-68; CYS-82; MET-124; ARG-163 AND ARG-170; VARIANTS CMT2 VAL-75 AND ILE-113; 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.