UniProtKB/Swiss-Prot Q8IV16: Variant p.Phe14Cys

Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1
Gene: GPIHBP1
Feedback?

Variant information Variant position:

14 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 Phenylalanine (F) to Cysteine (C) at position 14 (F14C, p.Phe14Cys). 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 large size and aromatic (F) to medium size and polar (C) 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:

It may act as a disease modifier preserving from severe HLPP1D; when associated in cis with R-68; does not affect interaction with LPL when associated in cis with R-68. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs11538389 [ dbSNP | Ensembl ]

Sequence information Variant position:

14 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:

MKALGAVLLALLL F GRPGRGQTQQEEEEEDEDHG 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                         MKALGAVLLALLLFGRPGRGQTQQEEEEEDEDHG

Mouse                         MKALRAVLLILLLSGQPGSGWAQ---EDGDADPE

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
Signal peptide	1 – 20

Literature citations
Isolation and characterization of human HBP1 gene.
Shan Y.X.; Yu L.;
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; VARIANT CYS-14; Submission
Mural R.J.; Istrail S.; Sutton G.G.; Florea L.; Halpern A.L.; Mobarry C.M.; Lippert R.; Walenz B.; Shatkay H.; Dew I.; Miller J.R.; Flanigan M.J.; Edwards N.J.; Bolanos R.; Fasulo D.; Halldorsson B.V.; Hannenhalli S.; Turner R.; Yooseph S.; Lu F.; Nusskern D.R.; Shue B.C.; Zheng X.H.; Zhong F.; Delcher A.L.; Huson D.H.; Kravitz S.A.; Mouchard L.; Reinert K.; Remington K.A.; Clark A.G.; Waterman M.S.; Eichler E.E.; Adams M.D.; Hunkapiller M.W.; Myers E.W.; Venter J.C.;
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]; VARIANT CYS-14; The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
The MGC Project Team;
Genome Res. 14:2121-2127(2004)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]; VARIANT CYS-14; 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; Novel combined GPIHBP1 mutations in a patient with hypertriglyceridemia associated with CAD.
Yamamoto H.; Onishi M.; Miyamoto N.; Oki R.; Ueda H.; Ishigami M.; Hiraoka H.; Matsuzawa Y.; Kihara S.;
J. Atheroscler. Thromb. 20:777-784(2013)
Cited for: VARIANT CYS-14; VARIANT HLPP1D ARG-68; CHARACTERIZATION OF VARIANT CYS-14; CHARACTERIZATION OF VARIANT HLPP1D ARG-68;

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.