UniProtKB/Swiss-Prot P06858: Variant p.Gly215Glu

• Variant information
• Sequence information
• Literature citations
• All

Variant information

Variant position: 215 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: LP/P [Disclaimer: Variants classification is intended for research purposes only, not for clinical and diagnostic use. The label disease variant is assigned according to literature reports on probable disease-association that can be based on theoretical reasons. This label must not be considered as a definitive proof for the pathogenic role of a variant.] 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 Glutamate (E) at position 215 (G215E, p.Gly215Glu). 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 medium size and acidic (E) 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: In HLPP1; loss of activity. Any additional useful information about the variant.
Other resources: Links to websites of interest for the variant.

• Variant rs118204057 [ dbSNP | Ensembl ]

Sequence information

Variant position: 215 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 475 The length of the canonical sequence.
Location on the sequence: PSRLSPDDADFVDVLHTFTR G SPGRSIGIQKPVGHVDIYPN 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: 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	28 – 475	Lipoprotein lipase
Binding site	197 – 197
Binding site	199 – 199
Binding site	202 – 202
Mutagenesis	199 – 199	S -> G. Loss of enzyme activity.
Mutagenesis	201 – 201	D -> E. No effect on enzyme activity.
Mutagenesis	202 – 202	D -> E. Loss of enzyme activity.

Literature citations

Missense mutation (Gly-->Glu188) of human lipoprotein lipase imparting functional deficiency.
Emi M.; Wilson D.E.; Iverius P.H.; Wiu L.; Hata A.; Hegele R.; Williams R.R.; Lalouel J.-M.;
J. Biol. Chem. 265:5910-5916(1990)
Cited for: VARIANT HLPP1 GLU-215; A missense mutation at codon 188 of the human lipoprotein lipase gene is a frequent cause of lipoprotein lipase deficiency in persons of different ancestries.
Monsalve M.V.; Henderson H.; Roederer G.; Julien P.; Deeb S.; Kastelein J.J.P.; Peritz L.; Devlin R.; Bruin T.; Murthy M.R.V.; Gagne C.; Davignon J.; Lupien P.J.; Brunzell J.D.; Hayden M.R.;
J. Clin. Invest. 86:728-734(1990)
Cited for: VARIANT HLPP1 GLU-215; A missense (Asp250-->Asn) mutation in the lipoprotein lipase gene in two unrelated families with familial lipoprotein lipase deficiency.
Ishimura-Oka K.; Semenkovich C.F.; Faustinella F.; Goldberg I.J.; Shachter N.; Smith L.C.; Coleman T.; Hide W.A.; Brown W.V.; Oka K.;
J. Lipid Res. 33:745-754(1992)
Cited for: VARIANTS HLPP1 GLU-215; HIS-270 AND ASN-277; Molecular basis of familial chylomicronemia: mutations in the lipoprotein lipase and apolipoprotein C-II genes.
Reina M.; Brunzell J.D.; Deeb S.S.;
J. Lipid Res. 33:1823-1832(1992)
Cited for: VARIANTS HLPP1 ARG-113; ARG-163; GLU-215; THR-221 AND SER-232; A compound heterozygote for lipoprotein lipase deficiency, Val69-->Leu and Gly188-->Glu: correlation between in vitro LPL activity and clinical expression.
Bruin T.; Tuzgoel S.; Mulder W.J.; van den Ende A.E.; Jansen H.; Hayden M.R.; Kastelein J.J.P.;
J. Lipid Res. 35:438-445(1994)
Cited for: VARIANTS HLPP1 LEU-96 AND GLU-215; CHARACTERIZATION OF VARIANT HLPP1 LEU-96; A novel missense (E163G) mutation in the catalytic subunit of lipoprotein lipase causes familial chylomicronemia.
Wiebusch H.; Funke H.; Santer R.; Richter W.; Assmann G.;
Hum. Mutat. 8:392-392(1996)
Cited for: VARIANTS HLPP1 GLY-190 AND GLU-215; Premature atherosclerosis in patients with familial chylomicronemia caused by mutations in the lipoprotein lipase gene.
Benlian P.; De Gennes J.L.; Foubert L.; Zhang H.; Gagne S.E.; Hayden M.;
N. Engl. J. Med. 335:848-854(1996)
Cited for: VARIANTS HLPP1 ALA-128; GLU-215; ARG-215; CYS-270; ASN-277 AND PRO-313; Familial lipoprotein lipase (LPL) deficiency: a catalogue of LPL gene mutations identified in 20 patients from the UK, Sweden, and Italy.
Mailly F.; Palmen J.; Muller D.P.R.; Gibbs T.; Lloyd J.; Brunzell J.; Durrington P.; Mitropoulos K.; Betteridge J.; Watts G.; Lithell H.; Angelico F.; Humphries S.E.; Talmud P.J.;
Hum. Mutat. 10:465-473(1997)
Cited for: VARIANTS HLPP1 GLY-113; THR-185; GLN-210; GLU-215; ARG-220; LEU-234; SER-318; THR-328 AND PRO-330; Assessment of French patients with LPL deficiency for French Canadian mutations.
Foubert L.; De Gennes J.L.; Lagarde J.P.; Ehrenborg E.; Raisonnier A.; Girardet J.P.; Hayden M.R.; Benlian P.;
J. Med. Genet. 34:672-675(1997)
Cited for: VARIANTS HLPP1 ALA-128; HIS-183; GLU-215; ARG-215; LEU-234; CYS-270 AND ASN-277; Compound heterozygosity for a new (S259G) and a previously described (G188E) mutation in lipoprotein lipase (LPL) as a cause of chylomicronemia.
Evans D.; Wendt D.; Ahle S.; Guerra A.; Beisiegel U.;
Hum. Mutat. 12:217-217(1998)
Cited for: VARIANTS HLPP1 GLU-215 AND GLY-286; Structural and functional consequences of missense mutations in exon 5 of the lipoprotein lipase gene.
Peterson J.; Ayyobi A.F.; Ma Y.; Henderson H.; Reina M.; Deeb S.S.; Santamarina-Fojo S.; Hayden M.R.; Brunzell J.D.;
J. Lipid Res. 43:398-406(2002)
Cited for: CHARACTERIZATION OF VARIANTS HLPP1 THR-203; GLU-215; THR-221; SER-232 AND LEU-234; CATALYTIC ACTIVITY; SUBUNIT; SUBCELLULAR LOCATION; TISSUE SPECIFICITY; Severe hypertriglyceridaemia in a Greek infant: a clinical, biochemical and genetic study.
Kavazarakis E.; Stabouli S.; Gourgiotis D.; Roumeliotou K.; Traeger-Synodinos J.; Bossios A.; Fretzayas A.; Kanavakis E.;
Eur. J. Pediatr. 163:462-466(2004)
Cited for: VARIANTS HLPP1 GLU-215 AND ARG-328; Mutations in Japanese subjects with primary hyperlipidemia -- results from the Research Committee of the Ministry of Health and Welfare of Japan since 1996.
Maruyama T.; Yamashita S.; Matsuzawa Y.; Bujo H.; Takahashi K.; Saito Y.; Ishibashi S.; Ohashi K.; Shionoiri F.; Gotoda T.; Yamada N.; Kita T.;
J. Atheroscler. Thromb. 11:131-145(2004)
Cited for: VARIANTS HLPP1 SER-70; ARG-132; VAL-181; GLU-215; THR-221; ARG-225; ALA-227; GLU-231; CYS-270; HIS-270; THR-288; LEU-297; ARG-305; PHE-330 AND THR-361; Hyperchylomicronaemia due to lipoprotein lipase deficiency as a cause of false-positive newborn screening for biotinidase deficiency.
Santer R.; Gokcay G.; Demirkol M.; Gal A.; Lukacs Z.;
J. Inherit. Metab. Dis. 28:137-140(2005)
Cited for: VARIANTS HLPP1 GLU-186; GLU-215 AND THR-221;