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UniProtKB/Swiss-Prot P14136: Variant p.Arg239His

Glial fibrillary acidic protein
Gene: GFAP
Variant information

Variant position:  239
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 Arginine (R) to Histidine (H) at position 239 (R239H, p.Arg239His).
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 basic (R) to medium size and polar (H)
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 ALXDRD.
Any additional useful information about the variant.

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

Sequence information

Variant position:  239
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  432
The length of the canonical sequence.

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.






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.

Chain 1 – 432 Glial fibrillary acidic protein
Domain 69 – 377 IF rod
Region 231 – 252 Coil 2A

Literature citations

Mutations in GFAP, encoding glial fibrillary acidic protein, are associated with Alexander disease.
Brenner M.; Johnson A.B.; Boespflug-Tanguy O.; Rodriguez D.; Goldman J.E.; Messing A.;
Nat. Genet. 27:117-120(2001)

Infantile Alexander disease: spectrum of GFAP mutations and genotype-phenotype correlation.
Rodriguez D.; Gauthier F.; Bertini E.; Bugiani M.; Brenner M.; N'guyen S.; Goizet C.; Gelot A.; Surtees R.; Pedespan J.M.; Hernandorena X.; Troncoso M.; Uziel G.; Messing A.; Ponsot G.; Pham-Dinh D.; Dautigny A.; Boespflug-Tanguy O.;
Am. J. Hum. Genet. 69:1134-1140(2001)
Cited for: VARIANTS ALXDRD PHE-76; TYR-77; HIS-79; CYS-88; SER-88; CYS-239 AND HIS-239;

Glial fibrillary acidic protein mutations in infantile, juvenile, and adult forms of Alexander disease.
Li R.; Johnson A.B.; Salomons G.; Goldman J.E.; Naidu S.; Quinlan R.; Cree B.; Ruyle S.Z.; Banwell B.; D'Hooghe M.; Siebert J.R.; Rolf C.M.; Cox H.; Reddy A.; Gutierrez-Solana L.G.; Collins A.; Weller R.O.; Messing A.; van der Knaap M.S.; Brenner M.;
Ann. Neurol. 57:310-326(2005)
Cited for: VARIANTS LEU-47; ILE-115; ASN-157 AND GLN-223; VARIANTS ALXDRD GLN-63; THR-73; PHE-76; VAL-76; SER-77; CYS-79; CYS-88; PRO-97; LYS-207; GLN-207; LYS-210; PRO-235; CYS-239; HIS-239; PRO-239; VAL-244; GLY-253; GLU-279; PRO-352; VAL-359; PRO-364; HIS-366; LYS-373; GLN-373; GLY-374 AND TRP-416; CHARACTERIZATION OF VARIANTS ALXDRD GLN-63; LYS-210; VAL-244 AND GLY-253; CHARACTERIZATION OF VARIANT ILE-115;

GFAP mutations and polymorphisms in 13 unrelated Italian patients affected by Alexander disease.
Caroli F.; Biancheri R.; Seri M.; Rossi A.; Pessagno A.; Bugiani M.; Corsolini F.; Savasta S.; Romano S.; Antonelli C.; Romano A.; Pareyson D.; Gambero P.; Uziel G.; Ravazzolo R.; Ceccherini I.; Filocamo M.;
Clin. Genet. 72:427-433(2007)
Cited for: VARIANTS ALXDRD TRP-70; GLN-70; LYS-73; SER-77; CYS-79; PRO-79; CYS-88; HIS-239; PRO-239; PRO-359 AND TRP-416;

Follow-up study of 22 Chinese children with Alexander disease and analysis of parental origin of de novo GFAP mutations.
Zang L.; Wang J.; Jiang Y.; Gu Q.; Gao Z.; Yang Y.; Xiao J.; Wu Y.;
J. Hum. Genet. 58:183-188(2013)
Cited for: VARIANTS ALXDRD PHE-76; LYS-77; LEU-79; HIS-79; CYS-79; CYS-88; SER-88; CYS-239; HIS-239; ASP-373; GLN-374 AND PHE-385;

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.