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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P06858: Variant p.Ile221Thr

Lipoprotein lipase
Gene: LPL
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Variant information Variant position: help 221 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 Isoleucine (I) to Threonine (T) at position 221 (I221T, p.Ile221Thr). 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 hydrophobic (I) to medium size and polar (T) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -1 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; loss of activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 221 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 DDADFVDVLHTFTRGSPGRS I GIQKPVGHVDIYPNGGTFQP 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
Binding site 202 – 202
Mutagenesis 201 – 201 D -> E. No effect on enzyme activity.
Mutagenesis 202 – 202 D -> E. Loss of enzyme activity.
Beta strand 219 – 222



Literature citations
Identification of two separate allelic mutations in the lipoprotein lipase gene of a patient with the familial hyperchylomicronemia syndrome.
Dichek H.L.; Fojo S.S.; Beg O.U.; Skarlatos S.I.; Brunzell J.D.; Cutler G.B. Jr.; Brewer H.B. Jr.;
J. Biol. Chem. 266:473-477(1991)
Cited for: VARIANTS HLPP1 THR-221 AND HIS-270; Amino acid substitution (Ile194-->Thr) in exon 5 of the lipoprotein lipase gene causes lipoprotein lipase deficiency in three unrelated probands. Support for a multicentric origin.
Henderson H.E.; Ma Y.; Hassan F.; Monsalve M.V.; Marais A.D.; Winkler F.; Gubernator K.; Peterson J.; Brunzell J.D.; Hayden M.R.;
J. Clin. Invest. 87:2005-2011(1991)
Cited for: VARIANT HLPP1 THR-221; 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; 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; 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;
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.