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UniProtKB/Swiss-Prot P25189: Variant p.His81Arg

Myelin protein P0
Gene: MPZ
Variant information

Variant position:  81
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 Histidine (H) to Arginine (R) at position 81 (H81R, p.His81Arg).
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:  Change from medium size and polar (H) to large size and basic (R)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  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:  In CMT1B and CMT2I; severe; reduces intercellular adhesion; does not affect targeting to the cell membrane.
Any additional useful information about the variant.

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



Sequence information

Variant position:  81
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:   DISFTWRYQPEGGRDAISIF  H YAKGQPYIDEVGTFKERIQW
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                         DISFTWRYQPEGGRDAISIFHYAKGQPYIDEVGTFKERIQW

Mouse                         DISFTWRYQPEGGRDAISIFHYAKGQPYIDEVGAFKERIQW

Rat                           DISFTWRYQPEGGRDAISIFHYAKGQPYIDEVGTFKERIQW

Bovine                        DLSFTWRYQPEGGRDAISIFHYAKGQPYIDEVGTFKERIQW

Horse                         DISFTWRYQPEGGRDAISIFHYAKGQPYIDEVGTFKERIQW

Chicken                       DISYTWHFQAEGSRDSISIFHYGKGQPYIDDVGSFKERMEW

Xenopus laevis                DISVTWHYQPDHSREMYSIVHFAKGLSSID-AGIFKDRIEW

Xenopus tropicalis            DVSVTWHYQPDHSREMYSIFHYAKGQPSID-AGVFKDRIEW

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
Disulfide bond 50 – 127
Beta strand 77 – 83


Literature citations

Novel mutation of the myelin P0 gene in a CMT1B family.
Sorour E.; Macmillan J.; Upadhyaya M.;
Hum. Mutat. 9:74-77(1997)
Cited for: VARIANT CMT1B ARG-81;

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;

Different cellular and molecular mechanisms for early and late-onset myelin protein zero mutations.
Grandis M.; Vigo T.; Passalacqua M.; Jain M.; Scazzola S.; La Padula V.; Brucal M.; Benvenuto F.; Nobbio L.; Cadoni A.; Mancardi G.L.; Kamholz J.; Shy M.E.; Schenone A.;
Hum. Mol. Genet. 17:1877-1889(2008)
Cited for: CHARACTERIZATION OF VARIANTS CMT1B 51-SER--TRP-57 DEL; PRO-39; ARG-81 AND MET-124; FUNCTION; SUBCELLULAR LOCATION;

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.