Variant position: 115 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 184 The length of the canonical sequence.
Location on the 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.
Human HGNTESGLLTTHSTWCTDSC QPITKTVEGTQVTMTCCQSSL
Mouse HSGTDKGYLTTYSMWCTDTC QPIIKTVGGTQMTQTCCQSTL
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.
Type Positions Description
21 – 151 Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1
63 – 148 UPAR/Ly6
114 – 130
101 – 101 G -> S. Promotes formation of dimers and oligomers reducing number of monomers. Retained some interaction with LPL.
104 – 104 T -> A. Promotes formation of dimers and oligomers reducing number of monomers. Retained some interaction with LPL.
105 – 105 T -> A. Promotes formation of dimers and oligomers reducing number of monomers.
106 – 106 H -> L. Promotes formation of dimers and oligomers severely reducing number of monomers.
107 – 107 S -> A. Promotes formation of dimers and oligomers reducing number of monomers.
108 – 108 T -> A. Retained some interaction with LPL. No effect on number of monomers.
109 – 109 W -> CPT. Promotes formation of dimers and oligomers reducing number of monomers. Loss of LPL interaction.
109 – 109 W -> SYHAF. Loss of interaction with LPL. Only slightly increased formation of dimers and oligomers. No effect on number of monomers.
115 – 115 Q -> K. No effect on number of monomers.
126 – 126 V -> A. Promotes formation of dimers and oligomers reducing number of monomers.
Chylomicronemia with a mutant GPIHBP1 (Q115P) that cannot bind lipoprotein lipase.
Beigneux A.P.; Franssen R.; Bensadoun A.; Gin P.; Melford K.; Peter J.; Walzem R.L.; Weinstein M.M.; Davies B.S.J.; Kuivenhoven J.A.; Kastelein J.J.P.; Fong L.G.; Dallinga-Thie G.M.; Young S.G.;
Arterioscler. Thromb. Vasc. Biol. 29:956-962(2009)
Cited for: VARIANT HLPP1D PRO-115; CHARACTERIZATION OF VARIANT HLPP1D PRO-115; INTERACTION WITH LPL; SUBCELLULAR LOCATION; FUNCTION;
Mutations in LPL, APOC2, APOA5, GPIHBP1 and LMF1 in patients with severe hypertriglyceridaemia.
Surendran R.P.; Visser M.E.; Heemelaar S.; Wang J.; Peter J.; Defesche J.C.; Kuivenhoven J.A.; Hosseini M.; Peterfy M.; Kastelein J.J.; Johansen C.T.; Hegele R.A.; Stroes E.S.; Dallinga-Thie G.M.;
J. Intern. Med. 272:185-196(2012)
Cited for: VARIANTS HLPP1D TYR-65; ARG-108; PRO-115 AND PHE-144;
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;
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.