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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O76090: Variant p.Ile73Asn

Bestrophin-1
Gene: BEST1
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Variant information Variant position: help 73 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 Isoleucine (I) to Asparagine (N) at position 73 (I73N, p.Ile73Asn). 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 hydrophobic (I) to medium size and polar (N) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -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

Variant description: help In VMD2; abolishes membrane insertion.. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 73 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 585 The length of the canonical sequence.
Location on the sequence: help ALTEEQQLMFEKLTLYCDSY I QLIPISFVLGFYVTLVVTRW 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: 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 1 – 585 Bestrophin-1
Transmembrane 61 – 82 Helical
Mutagenesis 69 – 69 C -> A. Impairs inactivation of ligand-gated anion channel activity by sulfhydryl-reactive agents; when associated with A-23; A-42; A-221 and A-251.
Turn 72 – 75



Literature citations
Insertion and topology of normal and mutant bestrophin-1 in the endoplasmic reticulum membrane.
Milenkovic V.M.; Rivera A.; Horling F.; Weber B.H.;
J. Biol. Chem. 282:1313-1321(2007)
Cited for: TOPOLOGY; VARIANTS VMD2 ASN-73; HIS-85; ARG-140 AND PHE-281 DEL; CHARACTERIZATION OF VARIANTS VMD2 ASN-73; HIS-85; ARG-140 AND PHE-281 DEL; Identification of novel VMD2 gene mutations in patients with Best vitelliform macular dystrophy.
Marchant D.; Gogat K.; Boutboul S.; Pequignot M.; Sternberg C.; Dureau P.; Roche O.; Uteza Y.; Hache J.C.; Puech B.; Puech V.; Dumur V.; Mouillon M.; Munier F.L.; Schorderet D.F.; Marsac C.; Dufier J.-L.; Abitbol M.;
Hum. Mutat. 17:235-235(2001)
Cited for: VARIANTS VMD2 PHE-16; CYS-17; ASN-73; HIS-92; CYS-218; HIS-218; LEU-235 AND SER-296;
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.