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UniProtKB/Swiss-Prot P60201: Variant p.Trp212Arg

Myelin proteolipid protein
Gene: PLP1
Variant information

Variant position:  212
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Disease [Disclaimer]
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Tryptophan (W) to Arginine (R) at position 212 (W212R, p.Trp212Arg).
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 large size and aromatic (W) to large size and basic (R)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -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

Involvement in disease:  Leukodystrophy, hypomyelinating, 1 (HLD1) [MIM:312080]: A X-linked recessive disorder of the central nervous system in which myelin is not formed properly. Clinically characterized by nystagmus, spastic quadriplegia, ataxia, and developmental delay. {ECO:0000269|PubMed:10417279, ECO:0000269|PubMed:10425042, ECO:0000269|PubMed:11093273, ECO:0000269|PubMed:11786921, ECO:0000269|PubMed:1376966, ECO:0000269|PubMed:1384324, ECO:0000269|PubMed:15712223, ECO:0000269|PubMed:1707231, ECO:0000269|PubMed:1708672, ECO:0000269|PubMed:1715570, ECO:0000269|PubMed:2479017, ECO:0000269|PubMed:2480601, ECO:0000269|PubMed:2773936, ECO:0000269|PubMed:7531827, ECO:0000269|PubMed:7539213, ECO:0000269|PubMed:7541731, ECO:0000269|PubMed:7573159, ECO:0000269|PubMed:7679906, ECO:0000269|PubMed:7683951, ECO:0000269|PubMed:7684886, ECO:0000269|PubMed:8037216, ECO:0000269|PubMed:8909455, ECO:0000269|PubMed:9008538, ECO:0000269|PubMed:9143933, ECO:0000269|PubMed:9482656, ECO:0000269|PubMed:9633722, ECO:0000269|PubMed:9747038, ECO:0000269|PubMed:9788732, ECO:0000269|PubMed:9894878, ECO:0000269|PubMed:9934976}. Note=The disease is caused by mutations affecting the gene represented in this entry.
The name and a short description of the disease associated with the variant. For more information about the disease, the user can refer to OMIM, following the link provided after the disease acronym.

Variant description:  In HLD1.
Any additional useful information about the variant.



Sequence information

Variant position:  212
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  277
The length of the canonical sequence.

Location on the sequence:   KTSASIGSLCADARMYGVLP  W NAFPGKVCGSNLLSICKTAE
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.

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 2 – 277 Myelin proteolipid protein
Topological domain 178 – 233 Extracellular
Lipidation 199 – 199 O-palmitoyl serine
Disulfide bond 184 – 228
Disulfide bond 201 – 220


Literature citations

Proteolipoprotein gene analysis in 82 patients with sporadic Pelizaeus-Merzbacher Disease: duplications, the major cause of the disease, originate more frequently in male germ cells, but point mutations do not.
Mimault C.; Giraud G.; Courtois V.; Cailloux F.; Boire J.Y.; Dastugue B.; Boespflug-Tanguy O.; Baethmann M.; Bertini E.; Cuisset J.M.; Gaertner J.; Hanefeld F.; Kohlschutter A.; Landrieu P.; Mayer M.; Peudenier S.; Rodriguez D.; Rating D.; Surtees R.; Uziel G.; Vallee L.; Voit T.;
Am. J. Hum. Genet. 65:360-369(1999)
Cited for: VARIANTS HLD1 TYR-35; THR-39; CYS-60; ARG-74; ARG-169; CYS-175; CYS-181; ASN-183; ASN-203; GLU-203; GLY-203; HIS-210; ARG-212; SER-216; TYR-228; PRO-234; GLU-246 AND GLU-248;

Genotype-phenotype correlation in inherited brain myelination defects due to proteolipid protein gene mutations.
Cailloux F.; Gauthier-Barichard F.; Mimault C.; Isabelle V.; Courtois V.; Giraud G.; Dastugue B.; Boespflug-Tanguy O.; Baethmann M.; Bertini E.; Cuisset J.M.; Gaertner J.; Hanefeld F.; Kohlschutter A.; Landrieu P.; Mayer M.; Peudenier S.; Rodriguez D.; Rating D.; Surtees R.; Uziel G.; Vallee L.; Voit T.;
Eur. J. Hum. Genet. 8:837-845(2000)
Cited for: VARIANTS HLD1 PRO-31; LEU-32; SER-51; ARG-74; CYS-181; GLU-203; ARG-212 AND ALA-216; VARIANT SPG2 TYR-130;

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.