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UniProtKB/Swiss-Prot P25189: Variant p.Lys130Arg

Myelin protein P0
Gene: MPZ
Variant information

Variant position:  130
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  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:  From Lysine (K) to Arginine (R) at position 130 (K130R, p.Lys130Arg).
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:  Similar physico-chemical property. Both residues are large size and basic.
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  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:  In CMT1B, CMT2I and DSS.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  130
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  248
The length of the canonical sequence.

Location on the sequence:   GSIVIHNLDYSDNGTFTCDV  K NPPDIVGKTSQVTLYVFEKV
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: 
The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         GSIVIHNLDYSDNGTFTCDVKNPPDIVGKTSQVTLYVFEKV

Mouse                         GSIVIHNLDYSDNGTFTCDVKNPPDIVGKTSQVTLYVFEKV

Rat                           GSIVIHNLDYSDNGTFTCDVKNPPDIVGKTSQVTLYVFEKV

Bovine                        GSIVIHNLDYGDNGTFTCDVKNPPDIVGKTSQVTLYVFEKV

Horse                         GSIVIHNLDYSDNGTFTCDVKNPPDIVGKTSQVTLYVFEKV

Chicken                       GSIVIHNLDYTDNGTFTCDVKNPPDIVGKSSQVTLYVLEKV

Xenopus laevis                ASIVVHNLELTDNGTFTCDVKNPPDVVGKSSYVHLQVQEKG

Xenopus tropicalis            ASIVLHNLELIDNGTFTCDVKNPPDVVGKSSYVHLQVQEKG

Sequence annotation in neighborhood:  
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
Beta strand 123 – 131


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;

Mutations in the peripheral myelin protein zero and connexin32 genes detected by non-isotopic RNase cleavage assay and their phenotypes in Japanese patients with Charcot-Marie-Tooth disease.
Yoshihara T.; Yamamoto M.; Doyu M.; Misu K.; Hattori N.; Hasegawa Y.; Mokuno K.; Mitsuma T.; Sobue G.;
Hum. Mutat. 16:177-178(2000)
Cited for: VARIANTS CMT PHE-32; CYS-68; MET-124 AND ARG-130;

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;

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.