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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q8IV16: Variant p.Cys89Phe

Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1
Gene: GPIHBP1
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Variant information Variant position: help 89 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 Phenylalanine (F) at position 89 (C89F, p.Cys89Phe). 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 large size and aromatic (F) 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 HLPP1D; drastically affects interaction with LPL; promotes formation of dimers and oligomers 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 89 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 KSLPRDERCNLTQNCSHGQT C TTLIAHGNTESGLLTTHSTW 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                         KSLPRDERCNLTQNCSHGQT-CTTLIAHGNTESGLLTTHSTW

Mouse                         QVLHSGESCNQTQSCSSSKPFCITLVSHSGTDKGYLTTYSM
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
Disulfide bond 83 – 110
Mutagenesis 71 – 71 L -> A. Promotes formation of dimers and oligomers reducing number of monomers.
Mutagenesis 91 – 91 T -> A. Promotes formation of dimers and oligomers reducing number of monomers.
Mutagenesis 92 – 92 L -> A. Only slightly increased formation of dimers and oligomers. No effect on number of monomers. Loss of LPL interaction.
Mutagenesis 93 – 93 I -> A. Promotes formation of dimers and oligomers reducing number of monomers.
Mutagenesis 101 – 101 G -> S. Promotes formation of dimers and oligomers reducing number of monomers. Retained some interaction with LPL.
Mutagenesis 104 – 104 T -> A. Promotes formation of dimers and oligomers reducing number of monomers. Retained some interaction with LPL.
Mutagenesis 105 – 105 T -> A. Promotes formation of dimers and oligomers reducing number of monomers.
Mutagenesis 106 – 106 H -> L. Promotes formation of dimers and oligomers severely reducing number of monomers.
Mutagenesis 107 – 107 S -> A. Promotes formation of dimers and oligomers reducing number of monomers.
Mutagenesis 108 – 108 T -> A. Retained some interaction with LPL. No effect on number of monomers.
Mutagenesis 109 – 109 W -> CPT. Promotes formation of dimers and oligomers reducing number of monomers. Loss of LPL interaction.
Mutagenesis 109 – 109 W -> SYHAF. Loss of interaction with LPL. Only slightly increased formation of dimers and oligomers. No effect on number of monomers.
Beta strand 88 – 98



Literature citations
GPIHBP1 C89F neomutation and hydrophobic C-terminal domain G175R mutation in two pedigrees with severe hyperchylomicronemia.
Charriere S.; Peretti N.; Bernard S.; Di Filippo M.; Sassolas A.; Merlin M.; Delay M.; Debard C.; Lefai E.; Lachaux A.; Moulin P.; Marcais C.;
J. Clin. Endocrinol. Metab. 96:E1675-E1679(2011)
Cited for: VARIANTS HLPP1D PHE-89 AND ARG-175; VARIANT CYS-14; CHARACTERIZATION OF VARIANTS HLPP1D PHE-89 AND ARG-175; CHARACTERIZATION OF VARIANT CYS-14; 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.