UniProtKB/Swiss-Prot Q8IV16: Variant p.Gly56Arg

Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1
Gene: GPIHBP1
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Variant information Variant position:

56 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

LB/B 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:

From Glycine (G) to Arginine (R) at position 56 (G56R, p.Gly56Arg). 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 glycine (G) to large size and basic (R) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

-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:

No discernible effect on interaction with LPL, chylomicrons or APOA5. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs587777636 [ dbSNP | Ensembl ]

Sequence information Variant position:

56 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:

DDYDEEDEDEVEEEETNRLP G GRSRVLLRCYTCKSLPRDER 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                         DDYD-EEDEDEVEEEETNRLPGGRSRVLLRCYTCKSLPRDER

Mouse                         ENYNYDDDDDEEEEEETNMIPGSRDRAPLQCYFCQVLHSGE

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
Chain	21 – 151	Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1
Modified residue	38 – 38	Sulfotyrosine
Mutagenesis	38 – 38	Y -> F. Loss of sulfotyrosine formation.
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.

Literature citations
Normal binding of lipoprotein lipase, chylomicrons, and apo-AV to GPIHBP1 containing a G56R amino acid substitution.
Gin P.; Beigneux A.P.; Davies B.; Young M.F.; Ryan R.O.; Bensadoun A.; Fong L.G.; Young S.G.;
Biochim. Biophys. Acta 1771:1464-1468(2007)
Cited for: INTERACTION WITH APOA5 AND LPL; CHARACTERIZATION OF VARIANT ARG-56; Homozygous missense mutation (G56R) in glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 (GPI-HBP1) in two siblings with fasting chylomicronemia (MIM 144650).
Wang J.; Hegele R.A.;
Lipids Health Dis. 6:23-23(2007)
Cited for: VARIANT ARG-56;

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.