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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q8IV16: Variant p.Cys65Ser

Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1
Gene: GPIHBP1
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Variant information Variant position: help 65 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 Cysteine (C) to Serine (S) at position 65 (C65S, p.Cys65Ser). 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 (C) to small size and polar (S) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -1 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 HLPP1D; does not affect protein expression at the cell surface; does not interact with LPL; promotes formation of dimers and oligomers severely reducing number of monomers. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 65 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 184 The length of the canonical sequence.
Location on the sequence: help EVEEEETNRLPGGRSRVLLR C YTCKSLPRDERCNLTQNCSH 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                         EVEEEETNRLPGGRSRVLLRCYTCKSLPRDERCNLTQNCSH

Mouse                         EEEEEETNMIPGSRDRAPLQCYFCQVLHSGESCNQTQSCSS
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 21 – 151 Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1
Domain 63 – 148 UPAR/Ly6
Glycosylation 78 – 78 N-linked (GlcNAc...) asparagine
Disulfide bond 65 – 89
Mutagenesis 66 – 66 Y -> A. Promotes formation of dimers and oligomers reducing number of monomers.
Mutagenesis 71 – 71 L -> A. Promotes formation of dimers and oligomers reducing number of monomers.
Beta strand 64 – 66



Literature citations
Mutation of conserved cysteines in the Ly6 domain of GPIHBP1 in familial chylomicronemia.
Olivecrona G.; Ehrenborg E.; Semb H.; Makoveichuk E.; Lindberg A.; Hayden M.R.; Gin P.; Davies B.S.; Weinstein M.M.; Fong L.G.; Beigneux A.P.; Young S.G.; Olivecrona T.; Hernell O.;
J. Lipid Res. 51:1535-1545(2010)
Cited for: VARIANTS HLPP1D SER-65 AND GLY-68; CHARACTERIZATION OF VARIANTS HLPP1D SER-65 AND GLY-68; GPIHBP1 missense mutations often cause multimerization of GPIHBP1 and thereby prevent lipoprotein lipase binding.
Beigneux A.P.; Fong L.G.; Bensadoun A.; Davies B.S.; Oberer M.; Gaardsvoll H.; Ploug M.; Young S.G.;
Circ. Res. 116:624-632(2015)
Cited for: CHARACTERIZATION OF VARIANTS HLPP1D SER-65; TYR-65; ARG-68; GLY-68; TYR-68; PHE-89; ARG-108 AND PRO-115; SUBUNIT; INTERACTION WITH LPL; MUTAGENESIS OF TYR-66; LEU-71; THR-91; LEU-92; ILE-93; GLY-101; THR-104; THR-105; HIS-106; SER-107; THR-108; TRP-109; GLN-115 AND VAL-126;
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.