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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P06858: Variant p.Cys445Tyr

Lipoprotein lipase
Gene: LPL
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Variant information Variant position: help 445 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 Tyrosine (Y) at position 445 (C445Y, p.Cys445Tyr). 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 (Y) 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 HLPP1; has 48% of normal activity in vitro; decreased levels of activity account for by the lower protein mass levels of the mutants rather than by decreased enzymatic activities; loss of interaction with GPIHBP1. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 445 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 475 The length of the canonical sequence.
Location on the sequence: help GFAIQKIRVKAGETQKKVIF C SREKVSHLQKGKAPAVFVKC 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.
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 28 – 475 Lipoprotein lipase
Domain 341 – 464 PLAT
Region 443 – 467 Interaction with GPIHBP1
Disulfide bond 445 – 465
Mutagenesis 430 – 430 K -> N. Impaired heparin-binding; when associated with N-432 and N-437.
Mutagenesis 432 – 432 R -> N. Impaired heparin-binding; when associated with N-430 and N-437.
Mutagenesis 434 – 434 K -> N. Impaired heparin-binding; when associated with N-430 and N-432.
Beta strand 440 – 454



Literature citations
The acidic domain of the endothelial membrane protein GPIHBP1 stabilizes lipoprotein lipase activity by preventing unfolding of its catalytic domain.
Mysling S.; Kristensen K.K.; Larsson M.; Beigneux A.P.; Gaardsvoll H.; Fong L.G.; Bensadouen A.; Joergensen T.J.; Young S.G.; Ploug M.;
Elife 5:E12095-E12095(2016)
Cited for: CATALYTIC ACTIVITY; INTERACTION WITH GPIHBP1; SUBUNIT; CHARACTERIZATION OF VARIANT HLPP1 TYR-445; Structure of the lipoprotein lipase-GPIHBP1 complex that mediates plasma triglyceride hydrolysis.
Birrane G.; Beigneux A.P.; Dwyer B.; Strack-Logue B.; Kristensen K.K.; Francone O.L.; Fong L.G.; Mertens H.D.T.; Pan C.Q.; Ploug M.; Young S.G.; Meiyappan M.;
Proc. Natl. Acad. Sci. U.S.A. 116:1723-1732(2019)
Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 28-475 IN COMPLEX WITH GPIHBP1 AND CALCIUM ION; CATALYTIC ACTIVITY; ACTIVE SITE; SUBCELLULAR LOCATION; SUBUNIT; DISULFIDE BOND; GLYCOSYLATION AT ASN-70 AND ASN-386; MUTAGENESIS OF SER-159 AND ASP-202; CHARACTERIZATION OF VARIANTS HLPP1 VAL-201; ARG-404 AND TYR-445; A new mutation destroying disulphide bridging in the C-terminal domain of lipoprotein lipase.
Henderson H.E.; Hassan F.; Marais D.; Hayden M.R.;
Biochem. Biophys. Res. Commun. 227:189-194(1996)
Cited for: VARIANT HLPP1 TYR-445; CHARACTERIZATION OF VARIANT HLPP1 TYR-445;
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.