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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P25189: Variant p.His39Pro

Myelin protein P0
Gene: MPZ
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Variant information Variant position: help 39 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 Histidine (H) to Proline (P) at position 39 (H39P, p.His39Pro). 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 polar (H) to medium size and hydrophobic (P) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -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: help In CMT1B; slightly reduces intercellular adhesion; does not affect targeting to the cell membrane. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 39 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 FSSLVLSPAQAIVVYTDREV H GAVGSRVTLHCSFWSSEWVS 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                         FSSLVLSPAQAIVVYTDREVHGAVGSRVTLHCSFWSSEWVS

Mouse                         FSSLVLSPALAIVVYTDREIYGAVGSQVTLHCSFWSSEWVS

Rat                           FSSLVLSPTLAIVVYTDREVYGAVGSQVTLHCSFWSSEWVS

Bovine                        FSSLVLSPVQAIVVYTDKEVHGAVGSQVTLYCSFWSSEWVS

Horse                         FSSLVLSPAQAIVVYTDKEVYGAVGSRVTLHCSFWSSEWVS

Chicken                       LSASGPSPTLAIHVYTPREVYGTVGSHVTLSCSFWSSEWIS

Xenopus laevis                LSALVLTPTLAIEVYTDREVYGTAGSRVTLSCSFWSSEWIS

Xenopus tropicalis            LSALVLPPTLAIEVYTDREVYGTVGSRVTLSCSFWSSEWIS

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
Beta strand 36 – 41



Literature citations
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; 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.