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UniProtKB - P06858 (LIPL_HUMAN)
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>sp|P06858|LIPL_HUMAN Lipoprotein lipase OS=Homo sapiens OX=9606 GN=LPL PE=1 SV=1 MESKALLVLTLAVWLQSLTASRGGVAAADQRRDFIDIESKFALRTPEDTAEDTCHLIPGV AESVATCHFNHSSKTFMVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQEH YPVSAGYTKLVGQDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRIT GLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQ PGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCSSKEAFEKG LCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTESETHTNQ AFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMLKLKWKSDSYFSWSDW WSSPGFAIQKIRVKAGETQKKVIFCSREKVSHLQKGKAPAVFVKCHDKSLNKKSGCommunity curation ()Add a publicationFeedback
Protein
Lipoprotein lipase
Gene
LPL
Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage (PubMed:8675619, PubMed:11342582, PubMed:27578112).
Although it has both phospholipase and triglyceride lipase activities it is primarily a triglyceride lipase with low but detectable phospholipase activity (PubMed:7592706, PubMed:12032167).
Mediates margination of triglyceride-rich lipoprotein particles in capillaries (PubMed:24726386).
Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans (PubMed:11342582, PubMed:27811232).
7 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.11"Human hepatic and lipoprotein lipase: the loop covering the catalytic site mediates lipase substrate specificity."
Dugi K.A., Dichek H.L., Santamarina-Fojo S.
J. Biol. Chem. 270:25396-25401(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, REGION, MUTAGENESIS OF 244-ASN--VAL-264; 245-ILE--LEU-263; 245-ILE--ALA-248 AND 262-GLN--LEU-263. - Ref.12"Severe hypertriglyceridemia, reduced high density lipoprotein, and neonatal death in lipoprotein lipase knockout mice. Mild hypertriglyceridemia with impaired very low density lipoprotein clearance in heterozygotes."
Weinstock P.H., Bisgaier C.L., Aalto-Setaelae K., Radner H., Ramakrishnan R., Levak-Frank S., Essenburg A.D., Zechner R., Breslow J.L.
J. Clin. Invest. 96:2555-2568(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.13"Heparin-binding defective lipoprotein lipase is unstable and causes abnormalities in lipid delivery to tissues."
Lutz E.P., Merkel M., Kako Y., Melford K., Radner H., Breslow J.L., Bensadoun A., Goldberg I.J.
J. Clin. Invest. 107:1183-1192(2001) [PubMed] [Europe PMC] [Abstract]Cited for: HEPARIN-BINDING, CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-430; ARG-432 AND LYS-434. - Ref.14"Characterization of the lipolytic activity of endothelial lipase."
McCoy M.G., Sun G.-S., Marchadier D., Maugeais C., Glick J.M., Rader D.J.
J. Lipid Res. 43:921-929(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.20"The GPIHBP1-LPL complex is responsible for the margination of triglyceride-rich lipoproteins in capillaries."
Goulbourne C.N., Gin P., Tatar A., Nobumori C., Hoenger A., Jiang H., Grovenor C.R., Adeyo O., Esko J.D., Goldberg I.J., Reue K., Tontonoz P., Bensadoun A., Beigneux A.P., Young S.G., Fong L.G.
Cell Metab. 19:849-860(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, MUTAGENESIS OF TRP-417 AND 420-TRP-TRP-421. - Ref.23"Mobility of 'HSPG-bound' LPL explains how LPL is able to reach GPIHBP1 on capillaries."
Allan C.M., Larsson M., Jung R.S., Ploug M., Bensadoun A., Beigneux A.P., Fong L.G., Young S.G.
J. Lipid Res. 58:216-225(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH GPIHBP1, SUBCELLULAR LOCATION. - Ref.87"Identification and characterization of two novel mutations in the LPL gene causing type I hyperlipoproteinemia."
Pingitore P., Lepore S.M., Pirazzi C., Mancina R.M., Motta B.M., Valenti L., Berge K.E., Retterstoel K., Leren T.P., Wiklund O., Romeo S.
J. Clin. Lipidol. 10:816-823(2016) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 ARG-404, CHARACTERIZATION OF VARIANT HLPP1 ARG-404, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
- a triacylglycerolEC:3.1.1.34
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Manual assertion based on experiment ini
- Ref.10"Rapid and simple isolation procedure for lipoprotein lipase from human milk."
Zechner R.
Biochim. Biophys. Acta 1044:20-25(1990) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 28-44, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY. - Ref.11"Human hepatic and lipoprotein lipase: the loop covering the catalytic site mediates lipase substrate specificity."
Dugi K.A., Dichek H.L., Santamarina-Fojo S.
J. Biol. Chem. 270:25396-25401(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, REGION, MUTAGENESIS OF 244-ASN--VAL-264; 245-ILE--LEU-263; 245-ILE--ALA-248 AND 262-GLN--LEU-263. - Ref.13"Heparin-binding defective lipoprotein lipase is unstable and causes abnormalities in lipid delivery to tissues."
Lutz E.P., Merkel M., Kako Y., Melford K., Radner H., Breslow J.L., Bensadoun A., Goldberg I.J.
J. Clin. Invest. 107:1183-1192(2001) [PubMed] [Europe PMC] [Abstract]Cited for: HEPARIN-BINDING, CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-430; ARG-432 AND LYS-434. - Ref.14"Characterization of the lipolytic activity of endothelial lipase."
McCoy M.G., Sun G.-S., Marchadier D., Maugeais C., Glick J.M., Rader D.J.
J. Lipid Res. 43:921-929(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.15"Calcium triggers folding of lipoprotein lipase into active dimers."
Zhang L., Lookene A., Wu G., Olivecrona G.
J. Biol. Chem. 280:42580-42591(2005) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, SUBUNIT, CALCIUM BINDING. - Ref.22"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) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, INTERACTION WITH GPIHBP1, SUBUNIT, CHARACTERIZATION OF VARIANT HLPP1 TYR-445. - Ref.24"A disordered acidic domain in GPIHBP1 harboring a sulfated tyrosine regulates lipoprotein lipase."
Kristensen K.K., Midtgaard S.R., Mysling S., Kovrov O., Hansen L.B., Skar-Gislinge N., Beigneux A.P., Kragelund B.B., Olivecrona G., Young S.G., Joergensen T.J.D., Fong L.G., Ploug M.
Proc. Natl. Acad. Sci. U.S.A. 115:E6020-E6029(2018) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH GPIHBP1, ACTIVITY REGULATION, CATALYTIC ACTIVITY. - Ref.26"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) [PubMed] [Europe PMC] [Abstract]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. - Ref.42"Human lipoprotein lipase. Analysis of the catalytic triad by site-directed mutagenesis of Ser-132, Asp-156, and His-241."
Emmerich J., Beg O.U., Peterson J., Previato L., Brunzell J.D., Brewer H.B. Jr., Santamarina-Fojo S.
J. Biol. Chem. 267:4161-4165(1992) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANTS HLPP1 ASN-183 AND GLY-183, MUTAGENESIS OF SER-159 AND HIS-268, CATALYTIC ACTIVITY, ACTIVE SITE, SUBCELLULAR LOCATION, HEPARIN-BINDING. - Ref.80"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) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANTS HLPP1 THR-203; GLU-215; THR-221; SER-232 AND LEU-234, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.87"Identification and characterization of two novel mutations in the LPL gene causing type I hyperlipoproteinemia."
Pingitore P., Lepore S.M., Pirazzi C., Mancina R.M., Motta B.M., Valenti L., Berge K.E., Retterstoel K., Leren T.P., Wiklund O., Romeo S.
J. Clin. Lipidol. 10:816-823(2016) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 ARG-404, CHARACTERIZATION OF VARIANT HLPP1 ARG-404, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
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Manual assertion based on experiment ini
- Ref.10"Rapid and simple isolation procedure for lipoprotein lipase from human milk."
Zechner R.
Biochim. Biophys. Acta 1044:20-25(1990) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 28-44, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY. - Ref.11"Human hepatic and lipoprotein lipase: the loop covering the catalytic site mediates lipase substrate specificity."
Dugi K.A., Dichek H.L., Santamarina-Fojo S.
J. Biol. Chem. 270:25396-25401(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, REGION, MUTAGENESIS OF 244-ASN--VAL-264; 245-ILE--LEU-263; 245-ILE--ALA-248 AND 262-GLN--LEU-263. - Ref.13"Heparin-binding defective lipoprotein lipase is unstable and causes abnormalities in lipid delivery to tissues."
Lutz E.P., Merkel M., Kako Y., Melford K., Radner H., Breslow J.L., Bensadoun A., Goldberg I.J.
J. Clin. Invest. 107:1183-1192(2001) [PubMed] [Europe PMC] [Abstract]Cited for: HEPARIN-BINDING, CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-430; ARG-432 AND LYS-434. - Ref.14"Characterization of the lipolytic activity of endothelial lipase."
McCoy M.G., Sun G.-S., Marchadier D., Maugeais C., Glick J.M., Rader D.J.
J. Lipid Res. 43:921-929(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.15"Calcium triggers folding of lipoprotein lipase into active dimers."
Zhang L., Lookene A., Wu G., Olivecrona G.
J. Biol. Chem. 280:42580-42591(2005) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, SUBUNIT, CALCIUM BINDING. - Ref.22"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) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, INTERACTION WITH GPIHBP1, SUBUNIT, CHARACTERIZATION OF VARIANT HLPP1 TYR-445. - Ref.24"A disordered acidic domain in GPIHBP1 harboring a sulfated tyrosine regulates lipoprotein lipase."
Kristensen K.K., Midtgaard S.R., Mysling S., Kovrov O., Hansen L.B., Skar-Gislinge N., Beigneux A.P., Kragelund B.B., Olivecrona G., Young S.G., Joergensen T.J.D., Fong L.G., Ploug M.
Proc. Natl. Acad. Sci. U.S.A. 115:E6020-E6029(2018) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH GPIHBP1, ACTIVITY REGULATION, CATALYTIC ACTIVITY. - Ref.26"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) [PubMed] [Europe PMC] [Abstract]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. - Ref.42"Human lipoprotein lipase. Analysis of the catalytic triad by site-directed mutagenesis of Ser-132, Asp-156, and His-241."
Emmerich J., Beg O.U., Peterson J., Previato L., Brunzell J.D., Brewer H.B. Jr., Santamarina-Fojo S.
J. Biol. Chem. 267:4161-4165(1992) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANTS HLPP1 ASN-183 AND GLY-183, MUTAGENESIS OF SER-159 AND HIS-268, CATALYTIC ACTIVITY, ACTIVE SITE, SUBCELLULAR LOCATION, HEPARIN-BINDING. - Ref.80"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) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANTS HLPP1 THR-203; GLU-215; THR-221; SER-232 AND LEU-234, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.87"Identification and characterization of two novel mutations in the LPL gene causing type I hyperlipoproteinemia."
Pingitore P., Lepore S.M., Pirazzi C., Mancina R.M., Motta B.M., Valenti L., Berge K.E., Retterstoel K., Leren T.P., Wiklund O., Romeo S.
J. Clin. Lipidol. 10:816-823(2016) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 ARG-404, CHARACTERIZATION OF VARIANT HLPP1 ARG-404, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
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a triacylglycerol- Search proteins in UniProtKB for this molecule.
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Manual assertion based on experiment ini
- Ref.11"Human hepatic and lipoprotein lipase: the loop covering the catalytic site mediates lipase substrate specificity."
Dugi K.A., Dichek H.L., Santamarina-Fojo S.
J. Biol. Chem. 270:25396-25401(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, REGION, MUTAGENESIS OF 244-ASN--VAL-264; 245-ILE--LEU-263; 245-ILE--ALA-248 AND 262-GLN--LEU-263. - Ref.14"Characterization of the lipolytic activity of endothelial lipase."
McCoy M.G., Sun G.-S., Marchadier D., Maugeais C., Glick J.M., Rader D.J.
J. Lipid Res. 43:921-929(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION.
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Manual assertion based on experiment ini
- Ref.11"Human hepatic and lipoprotein lipase: the loop covering the catalytic site mediates lipase substrate specificity."
Dugi K.A., Dichek H.L., Santamarina-Fojo S.
J. Biol. Chem. 270:25396-25401(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, REGION, MUTAGENESIS OF 244-ASN--VAL-264; 245-ILE--LEU-263; 245-ILE--ALA-248 AND 262-GLN--LEU-263. - Ref.14"Characterization of the lipolytic activity of endothelial lipase."
McCoy M.G., Sun G.-S., Marchadier D., Maugeais C., Glick J.M., Rader D.J.
J. Lipid Res. 43:921-929(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION.
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- 1,2,3-tri-(9Z-octadecenoyl)-glycerol
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Manual assertion based on experiment ini
- Ref.14"Characterization of the lipolytic activity of endothelial lipase."
McCoy M.G., Sun G.-S., Marchadier D., Maugeais C., Glick J.M., Rader D.J.
J. Lipid Res. 43:921-929(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
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<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.14"Characterization of the lipolytic activity of endothelial lipase."
McCoy M.G., Sun G.-S., Marchadier D., Maugeais C., Glick J.M., Rader D.J.
J. Lipid Res. 43:921-929(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION.
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Manual assertion based on experiment ini
- Ref.11"Human hepatic and lipoprotein lipase: the loop covering the catalytic site mediates lipase substrate specificity."
Dugi K.A., Dichek H.L., Santamarina-Fojo S.
J. Biol. Chem. 270:25396-25401(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, REGION, MUTAGENESIS OF 244-ASN--VAL-264; 245-ILE--LEU-263; 245-ILE--ALA-248 AND 262-GLN--LEU-263.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.11"Human hepatic and lipoprotein lipase: the loop covering the catalytic site mediates lipase substrate specificity."
Dugi K.A., Dichek H.L., Santamarina-Fojo S.
J. Biol. Chem. 270:25396-25401(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, REGION, MUTAGENESIS OF 244-ASN--VAL-264; 245-ILE--LEU-263; 245-ILE--ALA-248 AND 262-GLN--LEU-263.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine- Search proteins in UniProtKB for this molecule.
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+H2O- Search proteins in UniProtKB for this molecule.
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=(9Z)-octadecenoate- Search proteins in UniProtKB for this molecule.
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+(9Z-octadecenoyl)-sn-glycero-3-phosphocholine- Search proteins in UniProtKB for this molecule.
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+H+- Search proteins in UniProtKB for this molecule.
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- 1,2,3-tributanoylglycerol
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Manual assertion based on experiment ini
- Ref.11"Human hepatic and lipoprotein lipase: the loop covering the catalytic site mediates lipase substrate specificity."
Dugi K.A., Dichek H.L., Santamarina-Fojo S.
J. Biol. Chem. 270:25396-25401(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, REGION, MUTAGENESIS OF 244-ASN--VAL-264; 245-ILE--LEU-263; 245-ILE--ALA-248 AND 262-GLN--LEU-263.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.11"Human hepatic and lipoprotein lipase: the loop covering the catalytic site mediates lipase substrate specificity."
Dugi K.A., Dichek H.L., Santamarina-Fojo S.
J. Biol. Chem. 270:25396-25401(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, REGION, MUTAGENESIS OF 244-ASN--VAL-264; 245-ILE--LEU-263; 245-ILE--ALA-248 AND 262-GLN--LEU-263.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
1,2,3-tributanoylglycerol- Search proteins in UniProtKB for this molecule.
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+H2O- Search proteins in UniProtKB for this molecule.
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=butanoate- Search proteins in UniProtKB for this molecule.
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+dibutanoylglycerol- Search proteins in UniProtKB for this molecule.
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- 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine
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Manual assertion based on experiment ini
- Ref.14"Characterization of the lipolytic activity of endothelial lipase."
McCoy M.G., Sun G.-S., Marchadier D., Maugeais C., Glick J.M., Rader D.J.
J. Lipid Res. 43:921-929(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.14"Characterization of the lipolytic activity of endothelial lipase."
McCoy M.G., Sun G.-S., Marchadier D., Maugeais C., Glick J.M., Rader D.J.
J. Lipid Res. 43:921-929(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION.
Source: Rhea- Search for this reaction in UniProtKB.
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1,2-dihexadecanoyl-sn-glycero-3-phosphocholine- Search proteins in UniProtKB for this molecule.
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+hexadecanoyl-sn-glycero-3-phosphocholine- Search proteins in UniProtKB for this molecule.
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<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi
The apolipoprotein APOC2 acts as a coactivator of LPL activity (PubMed:12032167). Ca2+ binding promotes protein stability and formation of the active homodimer (PubMed:16179346). Interaction with GPIHBP1 protects LPL against inactivation by ANGPTL4 (PubMed:27929370, PubMed:29899144). Inhibited by NaCl (PubMed:12032167).4 Publications
Manual assertion based on experiment ini
- Ref.14"Characterization of the lipolytic activity of endothelial lipase."
McCoy M.G., Sun G.-S., Marchadier D., Maugeais C., Glick J.M., Rader D.J.
J. Lipid Res. 43:921-929(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.15"Calcium triggers folding of lipoprotein lipase into active dimers."
Zhang L., Lookene A., Wu G., Olivecrona G.
J. Biol. Chem. 280:42580-42591(2005) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, SUBUNIT, CALCIUM BINDING. - Ref.21"The angiopoietin-like protein ANGPTL4 catalyzes unfolding of the hydrolase domain in lipoprotein lipase and the endothelial membrane protein GPIHBP1 counteracts this unfolding."
Mysling S., Kristensen K.K., Larsson M., Kovrov O., Bensadouen A., Joergensen T.J., Olivecrona G., Young S.G., Ploug M.
Elife 5:0-0(2016) [PubMed] [Europe PMC] [Abstract]Cited for: ACTIVITY REGULATION, INTERACTION WITH GPIHBP1. - Ref.24"A disordered acidic domain in GPIHBP1 harboring a sulfated tyrosine regulates lipoprotein lipase."
Kristensen K.K., Midtgaard S.R., Mysling S., Kovrov O., Hansen L.B., Skar-Gislinge N., Beigneux A.P., Kragelund B.B., Olivecrona G., Young S.G., Joergensen T.J.D., Fong L.G., Ploug M.
Proc. Natl. Acad. Sci. U.S.A. 115:E6020-E6029(2018) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH GPIHBP1, ACTIVITY REGULATION, CATALYTIC ACTIVITY.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 159 | Nucleophile2 Publications Manual assertion based on experiment ini
| 1 | |
| Active sitei | 183 | Charge relay system1 Publication Manual assertion inferred by curator fromi
Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 194 | Calcium; via carbonyl oxygen1 Publication Manual assertion inferred by curator fromi
| 1 | |
| Metal bindingi | 197 | Calcium; via carbonyl oxygen1 Publication Manual assertion inferred by curator fromi
| 1 | |
| Metal bindingi | 199 | Calcium; via carbonyl oxygen1 Publication Manual assertion inferred by curator fromi
| 1 | |
| Metal bindingi | 202 | Calcium1 Publication Manual assertion inferred by curator fromi
| 1 | |
| Active sitei | 268 | Charge relay system1 Publication Manual assertion inferred by curator fromi
Manual assertion based on experiment ini
| 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- 1-acyl-2-lysophosphatidylserine acylhydrolase activity Source: UniProtKB-EC
- apolipoprotein binding Source: BHF-UCL
<p>Inferred from Physical Interaction</p>
<p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p>
Inferred from physical interactioni
- "Mechanism of triglyceride lowering in mice expressing human apolipoprotein A5."
Fruchart-Najib J., Bauge E., Niculescu L.S., Pham T., Thomas B., Rommens C., Majd Z., Brewer B., Pennacchio L.A., Fruchart J.C.
Biochem Biophys Res Commun 319:397-404(2004) [PubMed] [Europe PMC] [Abstract]
- calcium ion binding Source: UniProtKB
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- Ref.15"Calcium triggers folding of lipoprotein lipase into active dimers."
Zhang L., Lookene A., Wu G., Olivecrona G.
J. Biol. Chem. 280:42580-42591(2005) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, SUBUNIT, CALCIUM BINDING. - Ref.26"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) [PubMed] [Europe PMC] [Abstract]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.
- heparan sulfate proteoglycan binding Source: UniProtKB
<p>Inferred from Mutant Phenotype</p>
<p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p>
Inferred from mutant phenotypei
- Ref.13"Heparin-binding defective lipoprotein lipase is unstable and causes abnormalities in lipid delivery to tissues."
Lutz E.P., Merkel M., Kako Y., Melford K., Radner H., Breslow J.L., Bensadoun A., Goldberg I.J.
J. Clin. Invest. 107:1183-1192(2001) [PubMed] [Europe PMC] [Abstract]Cited for: HEPARIN-BINDING, CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-430; ARG-432 AND LYS-434.
- heparin binding Source: UniProtKBInferred from direct assayi
- Ref.13"Heparin-binding defective lipoprotein lipase is unstable and causes abnormalities in lipid delivery to tissues."
Lutz E.P., Merkel M., Kako Y., Melford K., Radner H., Breslow J.L., Bensadoun A., Goldberg I.J.
J. Clin. Invest. 107:1183-1192(2001) [PubMed] [Europe PMC] [Abstract]Cited for: HEPARIN-BINDING, CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-430; ARG-432 AND LYS-434. - Ref.31"Lipoprotein lipase Bethesda: a single amino acid substitution (Ala-176-->Thr) leads to abnormal heparin binding and loss of enzymic activity."
Beg O.U., Meng M.S., Skarlatos S.I., Previato L., Brunzell J.D., Brewer H.B. Jr., Fojo S.S.
Proc. Natl. Acad. Sci. U.S.A. 87:3474-3478(1990) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 THR-203.
- lipase activity Source: GO_Central
<p>Inferred from Biological aspect of Ancestor</p>
<p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iba">GO evidence code guide</a></p>
Inferred from biological aspect of ancestori
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
- lipoprotein lipase activity Source: UniProtKBInferred from direct assayi
- Ref.13"Heparin-binding defective lipoprotein lipase is unstable and causes abnormalities in lipid delivery to tissues."
Lutz E.P., Merkel M., Kako Y., Melford K., Radner H., Breslow J.L., Bensadoun A., Goldberg I.J.
J. Clin. Invest. 107:1183-1192(2001) [PubMed] [Europe PMC] [Abstract]Cited for: HEPARIN-BINDING, CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-430; ARG-432 AND LYS-434. - Ref.31"Lipoprotein lipase Bethesda: a single amino acid substitution (Ala-176-->Thr) leads to abnormal heparin binding and loss of enzymic activity."
Beg O.U., Meng M.S., Skarlatos S.I., Previato L., Brunzell J.D., Brewer H.B. Jr., Fojo S.S.
Proc. Natl. Acad. Sci. U.S.A. 87:3474-3478(1990) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 THR-203. - Ref.10"Rapid and simple isolation procedure for lipoprotein lipase from human milk."
Zechner R.
Biochim. Biophys. Acta 1044:20-25(1990) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 28-44, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY. - Ref.87"Identification and characterization of two novel mutations in the LPL gene causing type I hyperlipoproteinemia."
Pingitore P., Lepore S.M., Pirazzi C., Mancina R.M., Motta B.M., Valenti L., Berge K.E., Retterstoel K., Leren T.P., Wiklund O., Romeo S.
J. Clin. Lipidol. 10:816-823(2016) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 ARG-404, CHARACTERIZATION OF VARIANT HLPP1 ARG-404, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION. - Ref.26"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) [PubMed] [Europe PMC] [Abstract]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.
- lipoprotein particle binding Source: UniProtKBInferred from direct assayi
- Ref.13"Heparin-binding defective lipoprotein lipase is unstable and causes abnormalities in lipid delivery to tissues."
Lutz E.P., Merkel M., Kako Y., Melford K., Radner H., Breslow J.L., Bensadoun A., Goldberg I.J.
J. Clin. Invest. 107:1183-1192(2001) [PubMed] [Europe PMC] [Abstract]Cited for: HEPARIN-BINDING, CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-430; ARG-432 AND LYS-434.
- phosphatidylserine 1-acylhydrolase activity Source: UniProtKB-EC
- phospholipase A1 activity Source: UniProtKBInferred from direct assayi
- Ref.14"Characterization of the lipolytic activity of endothelial lipase."
McCoy M.G., Sun G.-S., Marchadier D., Maugeais C., Glick J.M., Rader D.J.
J. Lipid Res. 43:921-929(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.11"Human hepatic and lipoprotein lipase: the loop covering the catalytic site mediates lipase substrate specificity."
Dugi K.A., Dichek H.L., Santamarina-Fojo S.
J. Biol. Chem. 270:25396-25401(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, REGION, MUTAGENESIS OF 244-ASN--VAL-264; 245-ILE--LEU-263; 245-ILE--ALA-248 AND 262-GLN--LEU-263.
- phospholipase activity Source: BHF-UCL
<p>Inferred from Sequence or Structural Similarity<br />Used for any analysis based on sequence alignment, structure comparison, or evaluation of sequence features such as composition.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iss">GO evidence code guide</a></p>
Inferred from sequence or structural similarityi
- "Apolipoprotein C-II39-62 activates lipoprotein lipase by direct lipid-independent binding."
MacPhee C.E., Hatters D.M., Sawyer W.H., Howlett G.J.
Biochemistry 39:3433-3440(2000) [PubMed] [Europe PMC] [Abstract]
- protein homodimerization activity Source: UniProtKBInferred from direct assayi
- Ref.15"Calcium triggers folding of lipoprotein lipase into active dimers."
Zhang L., Lookene A., Wu G., Olivecrona G.
J. Biol. Chem. 280:42580-42591(2005) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, SUBUNIT, CALCIUM BINDING.
- protein-membrane adaptor activity Source: ARUK-UCL
<p>Traceable Author Statement</p>
<p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p>
Traceable author statementi
- "MicroRNA-27a/b regulates cellular cholesterol efflux, influx and esterification/hydrolysis in THP-1 macrophages."
Zhang M., Wu J.F., Chen W.J., Tang S.L., Mo Z.C., Tang Y.Y., Li Y., Wang J.L., Liu X.Y., Peng J., Chen K., He P.P., Lv Y.C., Ouyang X.P., Yao F., Tang D.P., Cayabyab F.S., Zhang D.W. , Zheng X.L., Tian G.P., Tang C.K.
Atherosclerosis 234:54-64(2014) [PubMed] [Europe PMC] [Abstract]
- signaling receptor binding Source: BHF-UCLInferred from physical interactioni
- "Sortilin/neurotensin receptor-3 binds and mediates degradation of lipoprotein lipase."
Nielsen M.S., Jacobsen C., Olivecrona G., Gliemann J., Petersen C.M.
J. Biol. Chem. 274:8832-8836(1999) [PubMed] [Europe PMC] [Abstract]
- triglyceride binding Source: Ensembl
- triglyceride lipase activity Source: UniProtKBInferred from direct assayi
- Ref.14"Characterization of the lipolytic activity of endothelial lipase."
McCoy M.G., Sun G.-S., Marchadier D., Maugeais C., Glick J.M., Rader D.J.
J. Lipid Res. 43:921-929(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION. - Ref.11"Human hepatic and lipoprotein lipase: the loop covering the catalytic site mediates lipase substrate specificity."
Dugi K.A., Dichek H.L., Santamarina-Fojo S.
J. Biol. Chem. 270:25396-25401(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, REGION, MUTAGENESIS OF 244-ASN--VAL-264; 245-ILE--LEU-263; 245-ILE--ALA-248 AND 262-GLN--LEU-263.
GO - Biological processi
- cellular response to fatty acid Source: ARUK-UCL
- cellular response to nutrient Source: ARUK-UCL
- cholesterol homeostasis Source: BHF-UCLInferred from mutant phenotypei
- "MicroRNA-590 attenuates lipid accumulation and pro-inflammatory cytokine secretion by targeting lipoprotein lipase gene in human THP-1 macrophages."
He P.P., Ouyang X.P., Tang Y.Y., Liao L., Wang Z.B., Lv Y.C., Tian G.P., Zhao G.J., Huang L., Yao F., Xie W., Tang Y.L., Chen W.J., Zhang M., Li Y., Wu J.F., Peng J., Liu X.Y. , Zheng X.L., Yin W.D., Tang C.K.
Biochimie 106:81-90(2014) [PubMed] [Europe PMC] [Abstract]
- chylomicron remodeling Source: UniProtKBInferred from mutant phenotypei
- Ref.13"Heparin-binding defective lipoprotein lipase is unstable and causes abnormalities in lipid delivery to tissues."
Lutz E.P., Merkel M., Kako Y., Melford K., Radner H., Breslow J.L., Bensadoun A., Goldberg I.J.
J. Clin. Invest. 107:1183-1192(2001) [PubMed] [Europe PMC] [Abstract]Cited for: HEPARIN-BINDING, CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-430; ARG-432 AND LYS-434.
- fatty acid biosynthetic process Source: BHF-UCLInferred from direct assayi
- "Effect of serum and C-apoproteins from very low density lipoproteins on human postheparin plasma hepatic lipase."
Kinnunen P.K., Ehnolm C.
FEBS Lett 65:354-357(1976) [PubMed] [Europe PMC] [Abstract]
- fatty acid metabolic process Source: UniProtKBInferred from direct assayi
- Ref.13"Heparin-binding defective lipoprotein lipase is unstable and causes abnormalities in lipid delivery to tissues."
Lutz E.P., Merkel M., Kako Y., Melford K., Radner H., Breslow J.L., Bensadoun A., Goldberg I.J.
J. Clin. Invest. 107:1183-1192(2001) [PubMed] [Europe PMC] [Abstract]Cited for: HEPARIN-BINDING, CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-430; ARG-432 AND LYS-434. - Ref.87"Identification and characterization of two novel mutations in the LPL gene causing type I hyperlipoproteinemia."
Pingitore P., Lepore S.M., Pirazzi C., Mancina R.M., Motta B.M., Valenti L., Berge K.E., Retterstoel K., Leren T.P., Wiklund O., Romeo S.
J. Clin. Lipidol. 10:816-823(2016) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 ARG-404, CHARACTERIZATION OF VARIANT HLPP1 ARG-404, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
- lipid catabolic process Source: GO_CentralInferred from biological aspect of ancestori
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
- low-density lipoprotein particle mediated signaling Source: BHF-UCLInferred from mutant phenotypei
- "MicroRNA-590 attenuates lipid accumulation and pro-inflammatory cytokine secretion by targeting lipoprotein lipase gene in human THP-1 macrophages."
He P.P., Ouyang X.P., Tang Y.Y., Liao L., Wang Z.B., Lv Y.C., Tian G.P., Zhao G.J., Huang L., Yao F., Xie W., Tang Y.L., Chen W.J., Zhang M., Li Y., Wu J.F., Peng J., Liu X.Y. , Zheng X.L., Yin W.D., Tang C.K.
Biochimie 106:81-90(2014) [PubMed] [Europe PMC] [Abstract]
- negative regulation of cellular response to insulin stimulus Source: Ensembl
- phospholipid metabolic process Source: BHF-UCLInferred from sequence or structural similarityi
- "Apolipoprotein C-II39-62 activates lipoprotein lipase by direct lipid-independent binding."
MacPhee C.E., Hatters D.M., Sawyer W.H., Howlett G.J.
Biochemistry 39:3433-3440(2000) [PubMed] [Europe PMC] [Abstract]
- positive regulation of chemokine (C-X-C motif) ligand 2 production Source: ARUK-UCL
- positive regulation of chemokine production Source: BHF-UCLInferred from mutant phenotypei
- "MicroRNA-590 attenuates lipid accumulation and pro-inflammatory cytokine secretion by targeting lipoprotein lipase gene in human THP-1 macrophages."
He P.P., Ouyang X.P., Tang Y.Y., Liao L., Wang Z.B., Lv Y.C., Tian G.P., Zhao G.J., Huang L., Yao F., Xie W., Tang Y.L., Chen W.J., Zhang M., Li Y., Wu J.F., Peng J., Liu X.Y. , Zheng X.L., Yin W.D., Tang C.K.
Biochimie 106:81-90(2014) [PubMed] [Europe PMC] [Abstract]
- positive regulation of cholesterol storage Source: BHF-UCLInferred from mutant phenotypei
- "VLDL-induced triglyceride accumulation in human macrophages is mediated by modulation of LPL lipolytic activity in the absence of change in LPL mass."
Milosavljevic D., Kontush A., Griglio S., Le Naour G., Thillet J., Chapman M.J.
Biochim Biophys Acta 1631:51-60(2003) [PubMed] [Europe PMC] [Abstract]
- positive regulation of fat cell differentiation Source: ARUK-UCLInferred from mutant phenotypei
- positive regulation of inflammatory response Source: ARUK-UCL
- positive regulation of interleukin-1 beta production Source: ARUK-UCL
- positive regulation of interleukin-6 production Source: ARUK-UCL
- positive regulation of lipid storage Source: ARUK-UCLTraceable author statementi
- "MicroRNA-27a/b regulates cellular cholesterol efflux, influx and esterification/hydrolysis in THP-1 macrophages."
Zhang M., Wu J.F., Chen W.J., Tang S.L., Mo Z.C., Tang Y.Y., Li Y., Wang J.L., Liu X.Y., Peng J., Chen K., He P.P., Lv Y.C., Ouyang X.P., Yao F., Tang D.P., Cayabyab F.S., Zhang D.W. , Zheng X.L., Tian G.P., Tang C.K.
Atherosclerosis 234:54-64(2014) [PubMed] [Europe PMC] [Abstract]
- positive regulation of macrophage derived foam cell differentiation Source: BHF-UCL
<p>Inferred by Curator</p>
<p>Used for cases where an annotation is not supported by any evidence but can be reasonably inferred by a curator from other GO annotations for which evidence<br />is available.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ic">GO evidence code guide</a></p>
Inferred by curatori
- "VLDL-induced triglyceride accumulation in human macrophages is mediated by modulation of LPL lipolytic activity in the absence of change in LPL mass."
Milosavljevic D., Kontush A., Griglio S., Le Naour G., Thillet J., Chapman M.J.
Biochim Biophys Acta 1631:51-60(2003) [PubMed] [Europe PMC] [Abstract]
- positive regulation of sequestering of triglyceride Source: BHF-UCLInferred from mutant phenotypei
- "VLDL-induced triglyceride accumulation in human macrophages is mediated by modulation of LPL lipolytic activity in the absence of change in LPL mass."
Milosavljevic D., Kontush A., Griglio S., Le Naour G., Thillet J., Chapman M.J.
Biochim Biophys Acta 1631:51-60(2003) [PubMed] [Europe PMC] [Abstract]
- positive regulation of tumor necrosis factor production Source: ARUK-UCL
- response to bacterium Source: Ensembl
- response to cold Source: Ensembl
- response to glucose Source: AgBase
- response to xenobiotic stimulus Source: Ensembl
- triglyceride biosynthetic process Source: Ensembl
- triglyceride catabolic process Source: UniProtKBInferred from direct assayi
- Ref.13"Heparin-binding defective lipoprotein lipase is unstable and causes abnormalities in lipid delivery to tissues."
Lutz E.P., Merkel M., Kako Y., Melford K., Radner H., Breslow J.L., Bensadoun A., Goldberg I.J.
J. Clin. Invest. 107:1183-1192(2001) [PubMed] [Europe PMC] [Abstract]Cited for: HEPARIN-BINDING, CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-430; ARG-432 AND LYS-434. - Ref.31"Lipoprotein lipase Bethesda: a single amino acid substitution (Ala-176-->Thr) leads to abnormal heparin binding and loss of enzymic activity."
Beg O.U., Meng M.S., Skarlatos S.I., Previato L., Brunzell J.D., Brewer H.B. Jr., Fojo S.S.
Proc. Natl. Acad. Sci. U.S.A. 87:3474-3478(1990) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 THR-203. - Ref.10"Rapid and simple isolation procedure for lipoprotein lipase from human milk."
Zechner R.
Biochim. Biophys. Acta 1044:20-25(1990) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 28-44, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY. - Ref.87"Identification and characterization of two novel mutations in the LPL gene causing type I hyperlipoproteinemia."
Pingitore P., Lepore S.M., Pirazzi C., Mancina R.M., Motta B.M., Valenti L., Berge K.E., Retterstoel K., Leren T.P., Wiklund O., Romeo S.
J. Clin. Lipidol. 10:816-823(2016) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 ARG-404, CHARACTERIZATION OF VARIANT HLPP1 ARG-404, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION. - Ref.26"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) [PubMed] [Europe PMC] [Abstract]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.
- triglyceride homeostasis Source: BHF-UCL
<p>Inferred from Genetic Interaction</p>
<p>Used to describe "traditional" genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p>
Inferred from genetic interactioni
- "Reduction of plasma triglycerides in apolipoprotein C-II transgenic mice overexpressing lipoprotein lipase in muscle."
Pulawa L.K., Jensen D.R., Coates A., Eckel R.H.
J Lipid Res 48:145-151(2007) [PubMed] [Europe PMC] [Abstract]
- triglyceride metabolic process Source: BHF-UCLInferred from sequence or structural similarityi
- "Apolipoprotein C-II39-62 activates lipoprotein lipase by direct lipid-independent binding."
MacPhee C.E., Hatters D.M., Sawyer W.H., Howlett G.J.
Biochemistry 39:3433-3440(2000) [PubMed] [Europe PMC] [Abstract]
- very-low-density lipoprotein particle remodeling Source: BHF-UCLInferred from direct assayi
- "Modulation of lipoprotein lipase activity by apolipoproteins. Effect of apolipoprotein C-III."
Wang C.S., McConathy W.J., Kloer H.U., Alaupovic P.
J Clin Invest 75:384-390(1985) [PubMed] [Europe PMC] [Abstract]
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Heparin-binding, Hydrolase |
| Biological process | Lipid degradation, Lipid metabolism |
| Ligand | Calcium, Metal-binding |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.1.1.34, 2681 |
Pathway Commons web resource for biological pathway data More...PathwayCommonsi | P06858 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-381340, Transcriptional regulation of white adipocyte differentiation R-HSA-8963889, Assembly of active LPL and LIPC lipase complexes R-HSA-8963901, Chylomicron remodeling R-HSA-975634, Retinoid metabolism and transport |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | P06858 |
SIGNOR Signaling Network Open Resource More...SIGNORi | P06858 |
Protein family/group databases
ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins More...ESTHERi | human-LPL, Lipoprotein_Lipase |
Chemistry databases
SwissLipids knowledge resource for lipid biology More...SwissLipidsi | SLP:000000568 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Lipoprotein lipase (EC:3.1.1.34
Manual assertion based on experiment ini
Short name: LPL Alternative name(s): Phospholipase A1 (EC:3.1.1.32
Manual assertion based on experiment ini
|
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:LPL Synonyms:LIPD |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Human Gene Nomenclature Database More...HGNCi | HGNC:6677, LPL |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 609708, gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P06858 |
Eukaryotic Pathogen, Vector and Host Database Resources More...VEuPathDBi | HostDB:ENSG00000175445 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Plasma membrane
- Cell membrane By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
; Peripheral membrane protein By similarityManual assertion inferred from sequence similarity toi
; Extracellular side By similarityManual assertion inferred from sequence similarity toi
- Cell membrane By similarity
Extracellular region or secreted
- Secreted 7 Publications
Manual assertion based on experiment ini
- Ref.10"Rapid and simple isolation procedure for lipoprotein lipase from human milk."
Zechner R.
Biochim. Biophys. Acta 1044:20-25(1990) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 28-44, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY. - Ref.13"Heparin-binding defective lipoprotein lipase is unstable and causes abnormalities in lipid delivery to tissues."
Lutz E.P., Merkel M., Kako Y., Melford K., Radner H., Breslow J.L., Bensadoun A., Goldberg I.J.
J. Clin. Invest. 107:1183-1192(2001) [PubMed] [Europe PMC] [Abstract]Cited for: HEPARIN-BINDING, CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-430; ARG-432 AND LYS-434. - Ref.26"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) [PubMed] [Europe PMC] [Abstract]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. - Ref.42"Human lipoprotein lipase. Analysis of the catalytic triad by site-directed mutagenesis of Ser-132, Asp-156, and His-241."
Emmerich J., Beg O.U., Peterson J., Previato L., Brunzell J.D., Brewer H.B. Jr., Santamarina-Fojo S.
J. Biol. Chem. 267:4161-4165(1992) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANTS HLPP1 ASN-183 AND GLY-183, MUTAGENESIS OF SER-159 AND HIS-268, CATALYTIC ACTIVITY, ACTIVE SITE, SUBCELLULAR LOCATION, HEPARIN-BINDING. - Ref.80"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) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANTS HLPP1 THR-203; GLU-215; THR-221; SER-232 AND LEU-234, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.81"Novel LPL mutation (L303F) found in a patient associated with coronary artery disease and severe systemic atherosclerosis."
Saika Y., Sakai N., Takahashi M., Maruyama T., Kihara S., Ouchi N., Ishigami M., Hiraoka H., Nakamura T., Yamashita S., Matsuzawa Y.
Eur. J. Clin. Invest. 33:216-222(2003) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 PHE-303, CHARACTERIZATION OF VARIANT HLPP1 PHE-303, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.87"Identification and characterization of two novel mutations in the LPL gene causing type I hyperlipoproteinemia."
Pingitore P., Lepore S.M., Pirazzi C., Mancina R.M., Motta B.M., Valenti L., Berge K.E., Retterstoel K., Leren T.P., Wiklund O., Romeo S.
J. Clin. Lipidol. 10:816-823(2016) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 ARG-404, CHARACTERIZATION OF VARIANT HLPP1 ARG-404, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
- extracellular matrix 1 Publication
Manual assertion based on experiment ini
- Ref.23"Mobility of 'HSPG-bound' LPL explains how LPL is able to reach GPIHBP1 on capillaries."
Allan C.M., Larsson M., Jung R.S., Ploug M., Bensadoun A., Beigneux A.P., Fong L.G., Young S.G.
J. Lipid Res. 58:216-225(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH GPIHBP1, SUBCELLULAR LOCATION.
Note: Newly synthesized LPL binds to cell surface heparan proteoglycans and is then released by heparanase. Subsequently, it becomes attached to heparan proteoglycan on endothelial cells (PubMed:27811232). Locates to the plasma membrane of microvilli of hepatocytes with triglyceride-rich lipoproteins (TRL). Some of the bound LPL is then internalized and located inside non-coated endocytic vesicles (By similarity).By similarity- Secreted 7 Publications
- Ref.23"Mobility of 'HSPG-bound' LPL explains how LPL is able to reach GPIHBP1 on capillaries."
Allan C.M., Larsson M., Jung R.S., Ploug M., Bensadoun A., Beigneux A.P., Fong L.G., Young S.G.
J. Lipid Res. 58:216-225(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH GPIHBP1, SUBCELLULAR LOCATION.
Manual assertion inferred from sequence similarity toi
1 PublicationManual assertion based on experiment ini
Extracellular region or secreted
- chylomicron Source: UniProtKB-KW
- extracellular region Source: Reactome
- extracellular space Source: UniProtKBInferred from direct assayi
- Ref.13"Heparin-binding defective lipoprotein lipase is unstable and causes abnormalities in lipid delivery to tissues."
Lutz E.P., Merkel M., Kako Y., Melford K., Radner H., Breslow J.L., Bensadoun A., Goldberg I.J.
J. Clin. Invest. 107:1183-1192(2001) [PubMed] [Europe PMC] [Abstract]Cited for: HEPARIN-BINDING, CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-430; ARG-432 AND LYS-434. - Ref.10"Rapid and simple isolation procedure for lipoprotein lipase from human milk."
Zechner R.
Biochim. Biophys. Acta 1044:20-25(1990) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 28-44, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY. - Ref.87"Identification and characterization of two novel mutations in the LPL gene causing type I hyperlipoproteinemia."
Pingitore P., Lepore S.M., Pirazzi C., Mancina R.M., Motta B.M., Valenti L., Berge K.E., Retterstoel K., Leren T.P., Wiklund O., Romeo S.
J. Clin. Lipidol. 10:816-823(2016) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 ARG-404, CHARACTERIZATION OF VARIANT HLPP1 ARG-404, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION. - Ref.26"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) [PubMed] [Europe PMC] [Abstract]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.
- very-low-density lipoprotein particle Source: UniProtKB-KW
Plasma Membrane
- plasma membrane Source: UniProtKB-SubCell
Other locations
- catalytic complex Source: ComplexPortalInferred from physical interactioni
- Ref.26"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) [PubMed] [Europe PMC] [Abstract]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.
- cell surface Source: Ensembl
- catalytic complex Source: ComplexPortalInferred from physical interactioni
Keywords - Cellular componenti
Cell membrane, Chylomicron, Extracellular matrix, Membrane, Secreted, VLDL<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Hyperlipoproteinemia 1 (HLPP1)55 PublicationsManual assertion based on experiment ini
- Ref.22"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) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, INTERACTION WITH GPIHBP1, SUBUNIT, CHARACTERIZATION OF VARIANT HLPP1 TYR-445. - Ref.26"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) [PubMed] [Europe PMC] [Abstract]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. - Ref.28"Compound heterozygote for lipoprotein lipase deficiency: Ser-->Thr244 and transition in 3' splice site of intron 2 (AG-->AA) in the lipoprotein lipase gene."
Hata A., Emi M., Luc G., Basdevant A., Gambert P., Iverius P.-H., Lalouel J.-M.
Am. J. Hum. Genet. 47:721-726(1990) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 THR-271, INVOLVEMENT IN HLPP1. - Ref.29"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) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 GLU-215. - Ref.30"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) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 GLU-215. - Ref.31"Lipoprotein lipase Bethesda: a single amino acid substitution (Ala-176-->Thr) leads to abnormal heparin binding and loss of enzymic activity."
Beg O.U., Meng M.S., Skarlatos S.I., Previato L., Brunzell J.D., Brewer H.B. Jr., Fojo S.S.
Proc. Natl. Acad. Sci. U.S.A. 87:3474-3478(1990) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 THR-203. - Ref.32"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) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HLPP1 THR-221 AND HIS-270. - Ref.33"Catalytic triad residue mutation (Asp156-->Gly) causing familial lipoprotein lipase deficiency. Co-inheritance with a nonsense mutation (Ser447-->Ter) in a Turkish family."
Faustinella F., Chang A., van Biervliet J.P., Rosseneu M., Vinaimont N., Smith L.C., Chen S.-H., Chan L.
J. Biol. Chem. 266:14418-14424(1991) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 GLY-183. - Ref.34"Familial chylomicronemia (type I hyperlipoproteinemia) due to a single missense mutation in the lipoprotein lipase gene."
Ameis D., Kobayashi J., Davis R.C., Ben-Zeev O., Malloy M.J., Kane J.P., Lee G., Wong H., Havel R.J., Schotz M.C.
J. Clin. Invest. 87:1165-1170(1991) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 GLU-169. - Ref.35"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) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 THR-221. - Ref.36"Heterogeneous mutations in the human lipoprotein lipase gene in patients with familial lipoprotein lipase deficiency."
Gotoda T., Yamada N., Kawamura M., Kozaki K., Mori N., Ishibashi S., Shimano H., Takaku F., Yazaki Y., Furuichi Y., Murase T.
J. Clin. Invest. 88:1856-1864(1991) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HLPP1 GLU-231 AND HIS-270, CHARACTERIZATION OF VARIANTS HLPP1 GLU-231 AND HIS-270. - Ref.37"A mutation in the human lipoprotein lipase gene as the most common cause of familial chylomicronemia in French Canadians."
Ma Y., Henderson H.E., Ven Murthy M.R., Roederer G., Monsalve M.V., Clarke L.A., Normand T., Julien P., Gagne C., Lambert M., Davignon J., Lupien P.J., Brunzell J., Hayden M.R.
N. Engl. J. Med. 324:1761-1766(1991) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 LEU-234. - Ref.38"A missense mutation (Trp86-->Arg) in exon 3 of the lipoprotein lipase gene: a cause of familial chylomicronemia."
Ishimura-Oka K., Faustinella F., Kihara S., Smith L.C., Oka K., Chan L.
Am. J. Hum. Genet. 50:1275-1280(1992) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 ARG-113. - Ref.39"A missense mutation Pro157Arg in lipoprotein lipase (LPLNijmegen) resulting in loss of catalytic activity."
Bruin T., Kastelein J.J., van Diermen D.E., Ma Y., Henderson H.E., Stuyt P.M., Stalenhoef A.F.H., Sturk A., Brunzell J.D., Hayden M.R.
Eur. J. Biochem. 208:267-272(1992) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 ARG-184. - Ref.40"A missense mutation (Asp250-->Asn) in exon 6 of the human lipoprotein lipase gene causes chylomicronemia in patients of different ancestries."
Ma Y., Wilson B.I., Bijvoet S., Henderson H.E., Cramb E., Roederer G., Ven Murthy M.R., Julien P., Bakker H.D., Kastelein J.J., Brunzell J.D., Hayden M.R.
Genomics 13:649-653(1992) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 ASN-277. - Ref.41"Two naturally occurring mutations at the first and second bases of codon aspartic acid 156 in the proposed catalytic triad of human lipoprotein lipase. In vivo evidence that aspartic acid 156 is essential for catalysis."
Ma Y.H., Bruin T., Tuzgol S., Wilson B.I., Roederer G., Liu M.S., Davignon J., Kastelein J.J., Brunzell J.D., Hayden M.R.
J. Biol. Chem. 267:1918-1923(1992) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HLPP1 ASN-183; GLY-183 AND SER-243. - Ref.42"Human lipoprotein lipase. Analysis of the catalytic triad by site-directed mutagenesis of Ser-132, Asp-156, and His-241."
Emmerich J., Beg O.U., Peterson J., Previato L., Brunzell J.D., Brewer H.B. Jr., Santamarina-Fojo S.
J. Biol. Chem. 267:4161-4165(1992) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANTS HLPP1 ASN-183 AND GLY-183, MUTAGENESIS OF SER-159 AND HIS-268, CATALYTIC ACTIVITY, ACTIVE SITE, SUBCELLULAR LOCATION, HEPARIN-BINDING. - Ref.43"Missense mutations in exon 5 of the human lipoprotein lipase gene. Inactivation correlates with loss of dimerization."
Hata A., Ridinger D.N., Sutherland S.D., Emi M., Kwong L.K., Shuhua J., Lubbers A., Guy-Grand B., Basdevant A., Iverius P.H., Wilson D.E., Lalouel J.-M.
J. Biol. Chem. 267:20132-20139(1992) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 GLU-222. - Ref.44"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) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HLPP1 GLU-215; HIS-270 AND ASN-277. - Ref.45"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) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HLPP1 ARG-113; ARG-163; GLU-215; THR-221 AND SER-232. - Ref.46"A missense mutation (Ala334-->Thr) in exon 7 of the lipoprotein lipase gene in a case with type I hyperlipidemia."
Kobayashi J., Sasaki N., Tashiro J., Inadera H., Saito Y., Yoshida S.
Biochem. Biophys. Res. Commun. 191:1046-1054(1993) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 THR-361. - Ref.47"A novel missense mutation in the gene for lipoprotein lipase resulting in a highly conservative amino acid substitution (Asp180-->Glu) causes familial chylomicronemia (type I hyperlipoproteinemia)."
Haubenwallner S., Horl G., Shachter N.S., Presta E., Fried S.K., Hofler G., Kostner G.M., Breslow J.L., Zechner R.
Genomics 18:392-396(1993) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 GLU-207. - Ref.48"Gene-environment interaction in the conversion of a mild-to-severe phenotype in a patient homozygous for a Ser172-->Cys mutation in the lipoprotein lipase gene."
Ma Y., Liu M.-S., Ginzinger D., Frohlich J., Brunzell J.D., Hayden M.R.
J. Clin. Invest. 91:1953-1958(1993) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 CYS-199. - Ref.49"Mutations in exon 3 of the lipoprotein lipase gene segregating in a family with hypertriglyceridemia, pancreatitis, and non-insulin-dependent diabetes."
Wilson D.E., Hata A., Kwong L.K., Lingam A., Shuhua J., Ridinger D.N., Yeager C., Kaltenborn K.C., Iverius P.-H., Lalouel J.-M.
J. Clin. Invest. 92:203-211(1993) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 SER-102. - Ref.50"Recurrent pancreatitis and chylomicronemia in an extended Dutch kindred is caused by a Gly154-->Ser substitution in lipoprotein lipase."
Bruin T., Tuzgol S., van Diermen D.E., Hoogerbrugge-Van der Linden N., Brunzell J.D., Hayden M.R., Kastelein J.J.
J. Lipid Res. 34:2109-2119(1993) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 SER-181. - Ref.51"A new Italian case of lipoprotein lipase deficiency: a Leu365-> Val change resulting in loss of enzyme activity."
Chimienti G.P.G., Resta F., di Perma V., Tarricone C., Lovecchio M., Collacicco A.M., Capurso A.
Biochem. Biophys. Res. Commun. 199:570-576(1994) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 VAL-392. - Ref.52"A naturally occurring mutation at the second base of codon asparagine 43 in the proposed N-linked glycosylation site of human lipoprotein lipase: in vivo evidence that asparagine 43 is essential for catalysis and secretion."
Kobayashi J., Inadera H., Fujita Y., Talley G., Morisaki N., Yoshida S., Saito Y., Fojo S.S., Brewer H.B. Jr.
Biochem. Biophys. Res. Commun. 205:506-515(1994) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 SER-70, CHARACTERIZATION OF VARIANT HLPP1 SER-70. - Ref.53"Recurrent missense mutations at the first and second base of codon Arg243 in human lipoprotein lipase in patients of different ancestries."
Ma Y., Liu M.-S., Chitayat D., Bruin T., Beisiegel U., Benlian P., Foubert L., De Gennes J.L., Funke H., Forsythe I., Blaichman S., Papanikolaou M., Erkelens D.W., Kastelein J., Brunzell J.D., Hayden M.R.
Hum. Mutat. 3:52-58(1994) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HLPP1 HIS-270 AND CYS-270. - Ref.54"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) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HLPP1 LEU-96 AND GLU-215, CHARACTERIZATION OF VARIANT HLPP1 LEU-96. - Ref.55"High frequency of mutations in the human lipoprotein lipase gene in pregnancy-induced chylomicronemia: possible association with apolipoprotein E2 isoform."
Ma Y., Ooi T.C., Liu M.-S., Zhang H., McPherson R., Edwards A.L., Forsythe I.J., Frohlich J., Brunzell J.D., Hayden M.R.
J. Lipid Res. 35:1066-1075(1994) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HLPP1 CYS-199; ARG-279 AND THR-288, CHARACTERIZATION OF VARIANTS HLPP1 ARG-279 AND THR-288. - Ref.56"A novel missense mutation in the C-terminal domain of lipoprotein lipase (Glu410-->Val) leads to enzyme inactivation and familial chylomicronemia."
Previato L., Guardamagna O., Dugi K.A., Ronan R., Talley G.D., Santamarina-Fojo S., Brewer H.B. Jr.
J. Lipid Res. 35:1552-1560(1994) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 VAL-437. - Ref.58"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) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 TYR-445, CHARACTERIZATION OF VARIANT HLPP1 TYR-445. - Ref.60"Compound heterozygosity for a known (D250N) and a novel (E410K) missense mutation in the C-terminal domain of lipoprotein lipase causes familial chylomicronemia."
Wiebusch H., Funke H., Bruin T., Bucher H., von Eckardstein A., Kastelein J.J.P., Assmann G.
Hum. Mutat. 8:381-383(1996) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HLPP1 ASN-277 AND LYS-437. - Ref.61"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) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HLPP1 GLY-190 AND GLU-215. - Ref.62"Homozygosity for two point mutations in the lipoprotein lipase (LPL) gene in a patient with familial LPL deficiency: LPL(Asp9-->Asn, Tyr262-->His)."
Rouis M., Lohse P., Dugi K.A., Lohse P., Beg O.U., Ronan R., Talley G.D., Brunzell J.D., Santamarina-Fojo S.
J. Lipid Res. 37:651-661(1996) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 HIS-289, VARIANT FCHL3 ASN-36, CHARACTERIZATION OF VARIANT HLPP1 HIS-289, CHARACTERIZATION OF VARIANT FCHL3 ASN-36. - Ref.63"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) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HLPP1 ALA-128; GLU-215; ARG-215; CYS-270; ASN-277 AND PRO-313. - Ref.64"A single Ser259Arg mutation in the gene for lipoprotein lipase causes chylomicronemia in Moroccans of Berber ancestry."
Foubert L., Bruin T., de Gennes J.-L., Ehrenborg E., Furioli J., Kastelein J.J., Benlian P., Hayden M.R.
Hum. Mutat. 10:179-185(1997) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 ARG-286. - Ref.66"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) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HLPP1 ALA-128; HIS-183; GLU-215; ARG-215; LEU-234; CYS-270 AND ASN-277. - Ref.67"Ile225Thr loop mutation in the lipoprotein lipase (LPL) gene is a de novo event."
Henderson H.E., Bijvoet S.M., Mannens M.A.M.M., Bruin T., Erkelens D.W., Hayden M.R., Kastelein J.J.P.
Am. J. Med. Genet. 78:313-316(1998) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HLPP1 THR-252 AND HIS-270. - Ref.68"A novel Glu421Lys substitution in the lipoprotein lipase gene in pregnancy-induced hypertriglyceridemic pancreatitis."
Henderson H., Leisegang F., Hassan F., Hayden M., Marais D.
Clin. Chim. Acta 269:1-12(1998) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 LYS-448, CHARACTERIZATION OF VARIANT HLPP1 LYS-448. - Ref.69"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) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HLPP1 GLU-215 AND GLY-286. - Ref.70"Common genetic variants of lipoprotein lipase and apolipoproteins AI-CIII that relate to coronary artery disease: a study in Chinese and European subjects."
Zhang Q., Liu Y., Liu B.W., Fan P., Cavanna J., Galton D.J.
Mol. Genet. Metab. 64:177-183(1998) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 THR-288, VARIANTS FCHL3 ASN-36 AND SER-318. - Ref.74"A newly identified lipoprotein lipase (LPL) gene mutation (F270L) in a Japanese patient with familial LPL deficiency."
Takagi A., Ikeda Y., Takeda E., Yamamoto A.
Biochim. Biophys. Acta 1502:433-446(2000) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 LEU-297, CHARACTERIZATION OF VARIANT HLPP1 LEU-297. - Ref.75"A compound heterozygote for a novel missense mutation (G105R) in exon 3 and a missense mutation (D204E) in exon 5 of the lipoprotein lipase gene in a Japanese infant with hyperchylomicronaemia."
Ikeda Y., Goji K., Takagi A.
Clin. Sci. 99:569-578(2000) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HLPP1 ARG-132 AND GLU-231, CHARACTERIZATION OF VARIANTS HLPP1 ARG-132 AND GLU-231. - Ref.76"Type I hyperlipoproteinemia due to a novel loss of function mutation of lipoprotein lipase, Cys(239)-->Trp, associated with recurrent severe pancreatitis."
Hoffmann M.M., Jacob S., Luft D., Schmuelling R.-M., Rett K., Maerz W., Haering H.-U., Matthaei S.
J. Clin. Endocrinol. Metab. 85:4795-4798(2000) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 TRP-266. - Ref.77"Two novel mutations in the lipoprotein lipase gene in a family with marked hypertriglyceridemia in heterozygous carriers. Potential interaction with the polymorphic marker D1S104 on chromosome 1q21-q23."
Hoelzl B., Kraft H.G., Wiebusch H., Sandhofer A., Patsch J., Sandhofer F., Paulweber B.
J. Lipid Res. 41:734-741(2000) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 ASP-210, CHARACTERIZATION OF VARIANT HLPP1 ASP-210. - Ref.78"Novel compound heterozygous mutations for lipoprotein lipase deficiency. A G-to-T transversion at the first position of exon 5 causing G154V missense mutation and a 5' splice site mutation of intron 8."
Ikeda Y., Takagi A., Nakata Y., Sera Y., Hyoudou S., Hamamoto K., Nishi Y., Yamamoto A.
J. Lipid Res. 42:1072-1081(2001) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 VAL-181, CHARACTERIZATION OF VARIANT HLPP1 VAL-181. - Ref.79"Genotype-phenotype studies of six novel LPL mutations in Chinese patients with hypertriglyceridemia."
Chan L.Y.S., Lam C.-W., Mak Y.-T., Tomlinson B., Tsang M.-W., Baum L., Masarei J.R.L., Pang C.-P.
Hum. Mutat. 20:232-233(2002) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HLPP1 THR-98; ILE-208; VAL-279; ARG-279; TYR-310; ARG-325 AND PHE-365, CHARACTERIZATION OF VARIANTS HLPP1 THR-98; ILE-208; VAL-279; ARG-279; TYR-310; ARG-325 AND PHE-365. - Ref.80"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) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANTS HLPP1 THR-203; GLU-215; THR-221; SER-232 AND LEU-234, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.81"Novel LPL mutation (L303F) found in a patient associated with coronary artery disease and severe systemic atherosclerosis."
Saika Y., Sakai N., Takahashi M., Maruyama T., Kihara S., Ouchi N., Ishigami M., Hiraoka H., Nakamura T., Yamashita S., Matsuzawa Y.
Eur. J. Clin. Invest. 33:216-222(2003) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 PHE-303, CHARACTERIZATION OF VARIANT HLPP1 PHE-303, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.83"Identification of the first Lebanese mutation in the LPL gene and description of a rapid detection method."
Abifadel M., Jambart S., Allard D., Rabes J.-P., Varret M., Derre A., Chouery E., Salem N., Junien C., Aydenian H., Boileau C.
Clin. Genet. 65:158-161(2004) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 VAL-201. - Ref.84"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) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HLPP1 GLU-215 AND ARG-328. - Ref.85"Mutations in Japanese subjects with primary hyperlipidemia -- results from the Research Committee of the Ministry of Health and Welfare of Japan since 1996."
The research committee on primary hyperlipidemia of the ministry of health and welfare of Japan
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) [PubMed] [Europe PMC] [Abstract]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. - Ref.86"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) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HLPP1 GLU-186; GLU-215 AND THR-221. - Ref.87"Identification and characterization of two novel mutations in the LPL gene causing type I hyperlipoproteinemia."
Pingitore P., Lepore S.M., Pirazzi C., Mancina R.M., Motta B.M., Valenti L., Berge K.E., Retterstoel K., Leren T.P., Wiklund O., Romeo S.
J. Clin. Lipidol. 10:816-823(2016) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 ARG-404, CHARACTERIZATION OF VARIANT HLPP1 ARG-404, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
Ref.22
"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) [PubMed] [Europe PMC] [Abstract]
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) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, INTERACTION WITH GPIHBP1, SUBUNIT, CHARACTERIZATION OF VARIANT HLPP1 TYR-445.
Ref.26
"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) [PubMed] [Europe PMC] [Abstract]
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) [PubMed] [Europe PMC] [Abstract]
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.
Ref.28
"Compound heterozygote for lipoprotein lipase deficiency: Ser-->Thr244 and transition in 3' splice site of intron 2 (AG-->AA) in the lipoprotein lipase gene."
Hata A., Emi M., Luc G., Basdevant A., Gambert P., Iverius P.-H., Lalouel J.-M.
Am. J. Hum. Genet. 47:721-726(1990) [PubMed] [Europe PMC] [Abstract]
Hata A., Emi M., Luc G., Basdevant A., Gambert P., Iverius P.-H., Lalouel J.-M.
Am. J. Hum. Genet. 47:721-726(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1 THR-271, INVOLVEMENT IN HLPP1.
Ref.29
"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) [PubMed] [Europe PMC] [Abstract]
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) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1 GLU-215.
Ref.30
"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) [PubMed] [Europe PMC] [Abstract]
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) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1 GLU-215.
Ref.31
"Lipoprotein lipase Bethesda: a single amino acid substitution (Ala-176-->Thr) leads to abnormal heparin binding and loss of enzymic activity."
Beg O.U., Meng M.S., Skarlatos S.I., Previato L., Brunzell J.D., Brewer H.B. Jr., Fojo S.S.
Proc. Natl. Acad. Sci. U.S.A. 87:3474-3478(1990) [PubMed] [Europe PMC] [Abstract]
Beg O.U., Meng M.S., Skarlatos S.I., Previato L., Brunzell J.D., Brewer H.B. Jr., Fojo S.S.
Proc. Natl. Acad. Sci. U.S.A. 87:3474-3478(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1 THR-203.
Ref.32
"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) [PubMed] [Europe PMC] [Abstract]
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) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLPP1 THR-221 AND HIS-270.
Ref.33
"Catalytic triad residue mutation (Asp156-->Gly) causing familial lipoprotein lipase deficiency. Co-inheritance with a nonsense mutation (Ser447-->Ter) in a Turkish family."
Faustinella F., Chang A., van Biervliet J.P., Rosseneu M., Vinaimont N., Smith L.C., Chen S.-H., Chan L.
J. Biol. Chem. 266:14418-14424(1991) [PubMed] [Europe PMC] [Abstract]
Faustinella F., Chang A., van Biervliet J.P., Rosseneu M., Vinaimont N., Smith L.C., Chen S.-H., Chan L.
J. Biol. Chem. 266:14418-14424(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1 GLY-183.
Ref.34
"Familial chylomicronemia (type I hyperlipoproteinemia) due to a single missense mutation in the lipoprotein lipase gene."
Ameis D., Kobayashi J., Davis R.C., Ben-Zeev O., Malloy M.J., Kane J.P., Lee G., Wong H., Havel R.J., Schotz M.C.
J. Clin. Invest. 87:1165-1170(1991) [PubMed] [Europe PMC] [Abstract]
Ameis D., Kobayashi J., Davis R.C., Ben-Zeev O., Malloy M.J., Kane J.P., Lee G., Wong H., Havel R.J., Schotz M.C.
J. Clin. Invest. 87:1165-1170(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1 GLU-169.
Ref.35
"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) [PubMed] [Europe PMC] [Abstract]
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) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1 THR-221.
Ref.36
"Heterogeneous mutations in the human lipoprotein lipase gene in patients with familial lipoprotein lipase deficiency."
Gotoda T., Yamada N., Kawamura M., Kozaki K., Mori N., Ishibashi S., Shimano H., Takaku F., Yazaki Y., Furuichi Y., Murase T.
J. Clin. Invest. 88:1856-1864(1991) [PubMed] [Europe PMC] [Abstract]
Gotoda T., Yamada N., Kawamura M., Kozaki K., Mori N., Ishibashi S., Shimano H., Takaku F., Yazaki Y., Furuichi Y., Murase T.
J. Clin. Invest. 88:1856-1864(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLPP1 GLU-231 AND HIS-270, CHARACTERIZATION OF VARIANTS HLPP1 GLU-231 AND HIS-270.
Ref.37
"A mutation in the human lipoprotein lipase gene as the most common cause of familial chylomicronemia in French Canadians."
Ma Y., Henderson H.E., Ven Murthy M.R., Roederer G., Monsalve M.V., Clarke L.A., Normand T., Julien P., Gagne C., Lambert M., Davignon J., Lupien P.J., Brunzell J., Hayden M.R.
N. Engl. J. Med. 324:1761-1766(1991) [PubMed] [Europe PMC] [Abstract]
Ma Y., Henderson H.E., Ven Murthy M.R., Roederer G., Monsalve M.V., Clarke L.A., Normand T., Julien P., Gagne C., Lambert M., Davignon J., Lupien P.J., Brunzell J., Hayden M.R.
N. Engl. J. Med. 324:1761-1766(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1 LEU-234.
Ref.38
"A missense mutation (Trp86-->Arg) in exon 3 of the lipoprotein lipase gene: a cause of familial chylomicronemia."
Ishimura-Oka K., Faustinella F., Kihara S., Smith L.C., Oka K., Chan L.
Am. J. Hum. Genet. 50:1275-1280(1992) [PubMed] [Europe PMC] [Abstract]
Ishimura-Oka K., Faustinella F., Kihara S., Smith L.C., Oka K., Chan L.
Am. J. Hum. Genet. 50:1275-1280(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1 ARG-113.
Ref.39
"A missense mutation Pro157Arg in lipoprotein lipase (LPLNijmegen) resulting in loss of catalytic activity."
Bruin T., Kastelein J.J., van Diermen D.E., Ma Y., Henderson H.E., Stuyt P.M., Stalenhoef A.F.H., Sturk A., Brunzell J.D., Hayden M.R.
Eur. J. Biochem. 208:267-272(1992) [PubMed] [Europe PMC] [Abstract]
Bruin T., Kastelein J.J., van Diermen D.E., Ma Y., Henderson H.E., Stuyt P.M., Stalenhoef A.F.H., Sturk A., Brunzell J.D., Hayden M.R.
Eur. J. Biochem. 208:267-272(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1 ARG-184.
Ref.40
"A missense mutation (Asp250-->Asn) in exon 6 of the human lipoprotein lipase gene causes chylomicronemia in patients of different ancestries."
Ma Y., Wilson B.I., Bijvoet S., Henderson H.E., Cramb E., Roederer G., Ven Murthy M.R., Julien P., Bakker H.D., Kastelein J.J., Brunzell J.D., Hayden M.R.
Genomics 13:649-653(1992) [PubMed] [Europe PMC] [Abstract]
Ma Y., Wilson B.I., Bijvoet S., Henderson H.E., Cramb E., Roederer G., Ven Murthy M.R., Julien P., Bakker H.D., Kastelein J.J., Brunzell J.D., Hayden M.R.
Genomics 13:649-653(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1 ASN-277.
Ref.41
"Two naturally occurring mutations at the first and second bases of codon aspartic acid 156 in the proposed catalytic triad of human lipoprotein lipase. In vivo evidence that aspartic acid 156 is essential for catalysis."
Ma Y.H., Bruin T., Tuzgol S., Wilson B.I., Roederer G., Liu M.S., Davignon J., Kastelein J.J., Brunzell J.D., Hayden M.R.
J. Biol. Chem. 267:1918-1923(1992) [PubMed] [Europe PMC] [Abstract]
Ma Y.H., Bruin T., Tuzgol S., Wilson B.I., Roederer G., Liu M.S., Davignon J., Kastelein J.J., Brunzell J.D., Hayden M.R.
J. Biol. Chem. 267:1918-1923(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLPP1 ASN-183; GLY-183 AND SER-243.
Ref.42
"Human lipoprotein lipase. Analysis of the catalytic triad by site-directed mutagenesis of Ser-132, Asp-156, and His-241."
Emmerich J., Beg O.U., Peterson J., Previato L., Brunzell J.D., Brewer H.B. Jr., Santamarina-Fojo S.
J. Biol. Chem. 267:4161-4165(1992) [PubMed] [Europe PMC] [Abstract]
Emmerich J., Beg O.U., Peterson J., Previato L., Brunzell J.D., Brewer H.B. Jr., Santamarina-Fojo S.
J. Biol. Chem. 267:4161-4165(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS HLPP1 ASN-183 AND GLY-183, MUTAGENESIS OF SER-159 AND HIS-268, CATALYTIC ACTIVITY, ACTIVE SITE, SUBCELLULAR LOCATION, HEPARIN-BINDING.
Ref.43
"Missense mutations in exon 5 of the human lipoprotein lipase gene. Inactivation correlates with loss of dimerization."
Hata A., Ridinger D.N., Sutherland S.D., Emi M., Kwong L.K., Shuhua J., Lubbers A., Guy-Grand B., Basdevant A., Iverius P.H., Wilson D.E., Lalouel J.-M.
J. Biol. Chem. 267:20132-20139(1992) [PubMed] [Europe PMC] [Abstract]
Hata A., Ridinger D.N., Sutherland S.D., Emi M., Kwong L.K., Shuhua J., Lubbers A., Guy-Grand B., Basdevant A., Iverius P.H., Wilson D.E., Lalouel J.-M.
J. Biol. Chem. 267:20132-20139(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1 GLU-222.
Ref.44
"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) [PubMed] [Europe PMC] [Abstract]
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) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLPP1 GLU-215; HIS-270 AND ASN-277.
Ref.45
"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) [PubMed] [Europe PMC] [Abstract]
Reina M., Brunzell J.D., Deeb S.S.
J. Lipid Res. 33:1823-1832(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLPP1 ARG-113; ARG-163; GLU-215; THR-221 AND SER-232.
Ref.46
"A missense mutation (Ala334-->Thr) in exon 7 of the lipoprotein lipase gene in a case with type I hyperlipidemia."
Kobayashi J., Sasaki N., Tashiro J., Inadera H., Saito Y., Yoshida S.
Biochem. Biophys. Res. Commun. 191:1046-1054(1993) [PubMed] [Europe PMC] [Abstract]
Kobayashi J., Sasaki N., Tashiro J., Inadera H., Saito Y., Yoshida S.
Biochem. Biophys. Res. Commun. 191:1046-1054(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1 THR-361.
Ref.47
"A novel missense mutation in the gene for lipoprotein lipase resulting in a highly conservative amino acid substitution (Asp180-->Glu) causes familial chylomicronemia (type I hyperlipoproteinemia)."
Haubenwallner S., Horl G., Shachter N.S., Presta E., Fried S.K., Hofler G., Kostner G.M., Breslow J.L., Zechner R.
Genomics 18:392-396(1993) [PubMed] [Europe PMC] [Abstract]
Haubenwallner S., Horl G., Shachter N.S., Presta E., Fried S.K., Hofler G., Kostner G.M., Breslow J.L., Zechner R.
Genomics 18:392-396(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1 GLU-207.
Ref.48
"Gene-environment interaction in the conversion of a mild-to-severe phenotype in a patient homozygous for a Ser172-->Cys mutation in the lipoprotein lipase gene."
Ma Y., Liu M.-S., Ginzinger D., Frohlich J., Brunzell J.D., Hayden M.R.
J. Clin. Invest. 91:1953-1958(1993) [PubMed] [Europe PMC] [Abstract]
Ma Y., Liu M.-S., Ginzinger D., Frohlich J., Brunzell J.D., Hayden M.R.
J. Clin. Invest. 91:1953-1958(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1 CYS-199.
Ref.49
"Mutations in exon 3 of the lipoprotein lipase gene segregating in a family with hypertriglyceridemia, pancreatitis, and non-insulin-dependent diabetes."
Wilson D.E., Hata A., Kwong L.K., Lingam A., Shuhua J., Ridinger D.N., Yeager C., Kaltenborn K.C., Iverius P.-H., Lalouel J.-M.
J. Clin. Invest. 92:203-211(1993) [PubMed] [Europe PMC] [Abstract]
Wilson D.E., Hata A., Kwong L.K., Lingam A., Shuhua J., Ridinger D.N., Yeager C., Kaltenborn K.C., Iverius P.-H., Lalouel J.-M.
J. Clin. Invest. 92:203-211(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1 SER-102.
Ref.50
"Recurrent pancreatitis and chylomicronemia in an extended Dutch kindred is caused by a Gly154-->Ser substitution in lipoprotein lipase."
Bruin T., Tuzgol S., van Diermen D.E., Hoogerbrugge-Van der Linden N., Brunzell J.D., Hayden M.R., Kastelein J.J.
J. Lipid Res. 34:2109-2119(1993) [PubMed] [Europe PMC] [Abstract]
Bruin T., Tuzgol S., van Diermen D.E., Hoogerbrugge-Van der Linden N., Brunzell J.D., Hayden M.R., Kastelein J.J.
J. Lipid Res. 34:2109-2119(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1 SER-181.
Ref.51
"A new Italian case of lipoprotein lipase deficiency: a Leu365-> Val change resulting in loss of enzyme activity."
Chimienti G.P.G., Resta F., di Perma V., Tarricone C., Lovecchio M., Collacicco A.M., Capurso A.
Biochem. Biophys. Res. Commun. 199:570-576(1994) [PubMed] [Europe PMC] [Abstract]
Chimienti G.P.G., Resta F., di Perma V., Tarricone C., Lovecchio M., Collacicco A.M., Capurso A.
Biochem. Biophys. Res. Commun. 199:570-576(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1 VAL-392.
Ref.52
"A naturally occurring mutation at the second base of codon asparagine 43 in the proposed N-linked glycosylation site of human lipoprotein lipase: in vivo evidence that asparagine 43 is essential for catalysis and secretion."
Kobayashi J., Inadera H., Fujita Y., Talley G., Morisaki N., Yoshida S., Saito Y., Fojo S.S., Brewer H.B. Jr.
Biochem. Biophys. Res. Commun. 205:506-515(1994) [PubMed] [Europe PMC] [Abstract]
Kobayashi J., Inadera H., Fujita Y., Talley G., Morisaki N., Yoshida S., Saito Y., Fojo S.S., Brewer H.B. Jr.
Biochem. Biophys. Res. Commun. 205:506-515(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1 SER-70, CHARACTERIZATION OF VARIANT HLPP1 SER-70.
Ref.53
"Recurrent missense mutations at the first and second base of codon Arg243 in human lipoprotein lipase in patients of different ancestries."
Ma Y., Liu M.-S., Chitayat D., Bruin T., Beisiegel U., Benlian P., Foubert L., De Gennes J.L., Funke H., Forsythe I., Blaichman S., Papanikolaou M., Erkelens D.W., Kastelein J., Brunzell J.D., Hayden M.R.
Hum. Mutat. 3:52-58(1994) [PubMed] [Europe PMC] [Abstract]
Ma Y., Liu M.-S., Chitayat D., Bruin T., Beisiegel U., Benlian P., Foubert L., De Gennes J.L., Funke H., Forsythe I., Blaichman S., Papanikolaou M., Erkelens D.W., Kastelein J., Brunzell J.D., Hayden M.R.
Hum. Mutat. 3:52-58(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLPP1 HIS-270 AND CYS-270.
Ref.54
"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) [PubMed] [Europe PMC] [Abstract]
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) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLPP1 LEU-96 AND GLU-215, CHARACTERIZATION OF VARIANT HLPP1 LEU-96.
Ref.55
"High frequency of mutations in the human lipoprotein lipase gene in pregnancy-induced chylomicronemia: possible association with apolipoprotein E2 isoform."
Ma Y., Ooi T.C., Liu M.-S., Zhang H., McPherson R., Edwards A.L., Forsythe I.J., Frohlich J., Brunzell J.D., Hayden M.R.
J. Lipid Res. 35:1066-1075(1994) [PubMed] [Europe PMC] [Abstract]
Ma Y., Ooi T.C., Liu M.-S., Zhang H., McPherson R., Edwards A.L., Forsythe I.J., Frohlich J., Brunzell J.D., Hayden M.R.
J. Lipid Res. 35:1066-1075(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLPP1 CYS-199; ARG-279 AND THR-288, CHARACTERIZATION OF VARIANTS HLPP1 ARG-279 AND THR-288.
Ref.56
"A novel missense mutation in the C-terminal domain of lipoprotein lipase (Glu410-->Val) leads to enzyme inactivation and familial chylomicronemia."
Previato L., Guardamagna O., Dugi K.A., Ronan R., Talley G.D., Santamarina-Fojo S., Brewer H.B. Jr.
J. Lipid Res. 35:1552-1560(1994) [PubMed] [Europe PMC] [Abstract]
Previato L., Guardamagna O., Dugi K.A., Ronan R., Talley G.D., Santamarina-Fojo S., Brewer H.B. Jr.
J. Lipid Res. 35:1552-1560(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1 VAL-437.
Ref.58
"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) [PubMed] [Europe PMC] [Abstract]
Henderson H.E., Hassan F., Marais D., Hayden M.R.
Biochem. Biophys. Res. Commun. 227:189-194(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1 TYR-445, CHARACTERIZATION OF VARIANT HLPP1 TYR-445.
Ref.60
"Compound heterozygosity for a known (D250N) and a novel (E410K) missense mutation in the C-terminal domain of lipoprotein lipase causes familial chylomicronemia."
Wiebusch H., Funke H., Bruin T., Bucher H., von Eckardstein A., Kastelein J.J.P., Assmann G.
Hum. Mutat. 8:381-383(1996) [PubMed] [Europe PMC] [Abstract]
Wiebusch H., Funke H., Bruin T., Bucher H., von Eckardstein A., Kastelein J.J.P., Assmann G.
Hum. Mutat. 8:381-383(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLPP1 ASN-277 AND LYS-437.
Ref.61
"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) [PubMed] [Europe PMC] [Abstract]
Wiebusch H., Funke H., Santer R., Richter W., Assmann G.
Hum. Mutat. 8:392-392(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLPP1 GLY-190 AND GLU-215.
Ref.62
"Homozygosity for two point mutations in the lipoprotein lipase (LPL) gene in a patient with familial LPL deficiency: LPL(Asp9-->Asn, Tyr262-->His)."
Rouis M., Lohse P., Dugi K.A., Lohse P., Beg O.U., Ronan R., Talley G.D., Brunzell J.D., Santamarina-Fojo S.
J. Lipid Res. 37:651-661(1996) [PubMed] [Europe PMC] [Abstract]
Rouis M., Lohse P., Dugi K.A., Lohse P., Beg O.U., Ronan R., Talley G.D., Brunzell J.D., Santamarina-Fojo S.
J. Lipid Res. 37:651-661(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1 HIS-289, VARIANT FCHL3 ASN-36, CHARACTERIZATION OF VARIANT HLPP1 HIS-289, CHARACTERIZATION OF VARIANT FCHL3 ASN-36.
Ref.63
"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) [PubMed] [Europe PMC] [Abstract]
Benlian P., De Gennes J.L., Foubert L., Zhang H., Gagne S.E., Hayden M.
N. Engl. J. Med. 335:848-854(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLPP1 ALA-128; GLU-215; ARG-215; CYS-270; ASN-277 AND PRO-313.
Ref.64
"A single Ser259Arg mutation in the gene for lipoprotein lipase causes chylomicronemia in Moroccans of Berber ancestry."
Foubert L., Bruin T., de Gennes J.-L., Ehrenborg E., Furioli J., Kastelein J.J., Benlian P., Hayden M.R.
Hum. Mutat. 10:179-185(1997) [PubMed] [Europe PMC] [Abstract]
Foubert L., Bruin T., de Gennes J.-L., Ehrenborg E., Furioli J., Kastelein J.J., Benlian P., Hayden M.R.
Hum. Mutat. 10:179-185(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1 ARG-286.
Ref.66
"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) [PubMed] [Europe PMC] [Abstract]
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) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLPP1 ALA-128; HIS-183; GLU-215; ARG-215; LEU-234; CYS-270 AND ASN-277.
Ref.67
"Ile225Thr loop mutation in the lipoprotein lipase (LPL) gene is a de novo event."
Henderson H.E., Bijvoet S.M., Mannens M.A.M.M., Bruin T., Erkelens D.W., Hayden M.R., Kastelein J.J.P.
Am. J. Med. Genet. 78:313-316(1998) [PubMed] [Europe PMC] [Abstract]
Henderson H.E., Bijvoet S.M., Mannens M.A.M.M., Bruin T., Erkelens D.W., Hayden M.R., Kastelein J.J.P.
Am. J. Med. Genet. 78:313-316(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLPP1 THR-252 AND HIS-270.
Ref.68
"A novel Glu421Lys substitution in the lipoprotein lipase gene in pregnancy-induced hypertriglyceridemic pancreatitis."
Henderson H., Leisegang F., Hassan F., Hayden M., Marais D.
Clin. Chim. Acta 269:1-12(1998) [PubMed] [Europe PMC] [Abstract]
Henderson H., Leisegang F., Hassan F., Hayden M., Marais D.
Clin. Chim. Acta 269:1-12(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1 LYS-448, CHARACTERIZATION OF VARIANT HLPP1 LYS-448.
Ref.69
"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) [PubMed] [Europe PMC] [Abstract]
Evans D., Wendt D., Ahle S., Guerra A., Beisiegel U.
Hum. Mutat. 12:217-217(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLPP1 GLU-215 AND GLY-286.
Ref.70
"Common genetic variants of lipoprotein lipase and apolipoproteins AI-CIII that relate to coronary artery disease: a study in Chinese and European subjects."
Zhang Q., Liu Y., Liu B.W., Fan P., Cavanna J., Galton D.J.
Mol. Genet. Metab. 64:177-183(1998) [PubMed] [Europe PMC] [Abstract]
Zhang Q., Liu Y., Liu B.W., Fan P., Cavanna J., Galton D.J.
Mol. Genet. Metab. 64:177-183(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1 THR-288, VARIANTS FCHL3 ASN-36 AND SER-318.
Ref.74
"A newly identified lipoprotein lipase (LPL) gene mutation (F270L) in a Japanese patient with familial LPL deficiency."
Takagi A., Ikeda Y., Takeda E., Yamamoto A.
Biochim. Biophys. Acta 1502:433-446(2000) [PubMed] [Europe PMC] [Abstract]
Takagi A., Ikeda Y., Takeda E., Yamamoto A.
Biochim. Biophys. Acta 1502:433-446(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1 LEU-297, CHARACTERIZATION OF VARIANT HLPP1 LEU-297.
Ref.75
"A compound heterozygote for a novel missense mutation (G105R) in exon 3 and a missense mutation (D204E) in exon 5 of the lipoprotein lipase gene in a Japanese infant with hyperchylomicronaemia."
Ikeda Y., Goji K., Takagi A.
Clin. Sci. 99:569-578(2000) [PubMed] [Europe PMC] [Abstract]
Ikeda Y., Goji K., Takagi A.
Clin. Sci. 99:569-578(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLPP1 ARG-132 AND GLU-231, CHARACTERIZATION OF VARIANTS HLPP1 ARG-132 AND GLU-231.
Ref.76
"Type I hyperlipoproteinemia due to a novel loss of function mutation of lipoprotein lipase, Cys(239)-->Trp, associated with recurrent severe pancreatitis."
Hoffmann M.M., Jacob S., Luft D., Schmuelling R.-M., Rett K., Maerz W., Haering H.-U., Matthaei S.
J. Clin. Endocrinol. Metab. 85:4795-4798(2000) [PubMed] [Europe PMC] [Abstract]
Hoffmann M.M., Jacob S., Luft D., Schmuelling R.-M., Rett K., Maerz W., Haering H.-U., Matthaei S.
J. Clin. Endocrinol. Metab. 85:4795-4798(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1 TRP-266.
Ref.77
"Two novel mutations in the lipoprotein lipase gene in a family with marked hypertriglyceridemia in heterozygous carriers. Potential interaction with the polymorphic marker D1S104 on chromosome 1q21-q23."
Hoelzl B., Kraft H.G., Wiebusch H., Sandhofer A., Patsch J., Sandhofer F., Paulweber B.
J. Lipid Res. 41:734-741(2000) [PubMed] [Europe PMC] [Abstract]
Hoelzl B., Kraft H.G., Wiebusch H., Sandhofer A., Patsch J., Sandhofer F., Paulweber B.
J. Lipid Res. 41:734-741(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1 ASP-210, CHARACTERIZATION OF VARIANT HLPP1 ASP-210.
Ref.78
"Novel compound heterozygous mutations for lipoprotein lipase deficiency. A G-to-T transversion at the first position of exon 5 causing G154V missense mutation and a 5' splice site mutation of intron 8."
Ikeda Y., Takagi A., Nakata Y., Sera Y., Hyoudou S., Hamamoto K., Nishi Y., Yamamoto A.
J. Lipid Res. 42:1072-1081(2001) [PubMed] [Europe PMC] [Abstract]
Ikeda Y., Takagi A., Nakata Y., Sera Y., Hyoudou S., Hamamoto K., Nishi Y., Yamamoto A.
J. Lipid Res. 42:1072-1081(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1 VAL-181, CHARACTERIZATION OF VARIANT HLPP1 VAL-181.
Ref.79
"Genotype-phenotype studies of six novel LPL mutations in Chinese patients with hypertriglyceridemia."
Chan L.Y.S., Lam C.-W., Mak Y.-T., Tomlinson B., Tsang M.-W., Baum L., Masarei J.R.L., Pang C.-P.
Hum. Mutat. 20:232-233(2002) [PubMed] [Europe PMC] [Abstract]
Chan L.Y.S., Lam C.-W., Mak Y.-T., Tomlinson B., Tsang M.-W., Baum L., Masarei J.R.L., Pang C.-P.
Hum. Mutat. 20:232-233(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLPP1 THR-98; ILE-208; VAL-279; ARG-279; TYR-310; ARG-325 AND PHE-365, CHARACTERIZATION OF VARIANTS HLPP1 THR-98; ILE-208; VAL-279; ARG-279; TYR-310; ARG-325 AND PHE-365.
Ref.80
"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) [PubMed] [Europe PMC] [Abstract]
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) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS HLPP1 THR-203; GLU-215; THR-221; SER-232 AND LEU-234, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Ref.81
"Novel LPL mutation (L303F) found in a patient associated with coronary artery disease and severe systemic atherosclerosis."
Saika Y., Sakai N., Takahashi M., Maruyama T., Kihara S., Ouchi N., Ishigami M., Hiraoka H., Nakamura T., Yamashita S., Matsuzawa Y.
Eur. J. Clin. Invest. 33:216-222(2003) [PubMed] [Europe PMC] [Abstract]
Saika Y., Sakai N., Takahashi M., Maruyama T., Kihara S., Ouchi N., Ishigami M., Hiraoka H., Nakamura T., Yamashita S., Matsuzawa Y.
Eur. J. Clin. Invest. 33:216-222(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1 PHE-303, CHARACTERIZATION OF VARIANT HLPP1 PHE-303, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Ref.83
"Identification of the first Lebanese mutation in the LPL gene and description of a rapid detection method."
Abifadel M., Jambart S., Allard D., Rabes J.-P., Varret M., Derre A., Chouery E., Salem N., Junien C., Aydenian H., Boileau C.
Clin. Genet. 65:158-161(2004) [PubMed] [Europe PMC] [Abstract]
Abifadel M., Jambart S., Allard D., Rabes J.-P., Varret M., Derre A., Chouery E., Salem N., Junien C., Aydenian H., Boileau C.
Clin. Genet. 65:158-161(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1 VAL-201.
Ref.84
"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) [PubMed] [Europe PMC] [Abstract]
Kavazarakis E., Stabouli S., Gourgiotis D., Roumeliotou K., Traeger-Synodinos J., Bossios A., Fretzayas A., Kanavakis E.
Eur. J. Pediatr. 163:462-466(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLPP1 GLU-215 AND ARG-328.
Ref.85
"Mutations in Japanese subjects with primary hyperlipidemia -- results from the Research Committee of the Ministry of Health and Welfare of Japan since 1996."
The research committee on primary hyperlipidemia of the ministry of health and welfare of Japan
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) [PubMed] [Europe PMC] [Abstract]
The research committee on primary hyperlipidemia of the ministry of health and welfare of Japan
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) [PubMed] [Europe PMC] [Abstract]
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.
Ref.86
"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) [PubMed] [Europe PMC] [Abstract]
Santer R., Gokcay G., Demirkol M., Gal A., Lukacs Z.
J. Inherit. Metab. Dis. 28:137-140(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLPP1 GLU-186; GLU-215 AND THR-221.
Ref.87
"Identification and characterization of two novel mutations in the LPL gene causing type I hyperlipoproteinemia."
Pingitore P., Lepore S.M., Pirazzi C., Mancina R.M., Motta B.M., Valenti L., Berge K.E., Retterstoel K., Leren T.P., Wiklund O., Romeo S.
J. Clin. Lipidol. 10:816-823(2016) [PubMed] [Europe PMC] [Abstract]
Pingitore P., Lepore S.M., Pirazzi C., Mancina R.M., Motta B.M., Valenti L., Berge K.E., Retterstoel K., Leren T.P., Wiklund O., Romeo S.
J. Clin. Lipidol. 10:816-823(2016) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1 ARG-404, CHARACTERIZATION OF VARIANT HLPP1 ARG-404, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive metabolic disorder characterized by defective breakdown of dietary fats, impaired clearance of chylomicrons from plasma causing the plasma to have a milky appearance, and severe hypertriglyceridemia. On a normal diet, patients often present with abdominal pain, hepatosplenomegaly, lipemia retinalis, eruptive xanthomata, and massive hypertriglyceridemia, sometimes complicated with acute pancreatitis.
Related information in OMIM| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_057914 | 70 | N → S in HLPP1; produces an inactive protein which is not secreted into the media. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_057915 | 96 | V → L in HLPP1; gives rise to a 80% decrease in specific catalytic activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_057916 | 98 | A → T in HLPP1; decreases the specific activity of the enzyme; reduces the secretion of the mutant protein significantly; the total LPL mass is reduced compared to that of the wild-type construct. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_004211 | 102 | R → S in HLPP1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_004212 | 113 | W → G in HLPP1. | 1 | |
| Natural variantiVAR_004213 | 113 | W → R in HLPP1. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_057917 | 128 | T → A in HLPP1. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_057918 | 132 | G → R in HLPP1; synthesized as a catalytically inactive form. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_004214 | 163 | H → R in HLPP1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_004215 | 169 | G → E in HLPP1; loss of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_004216 | 181 | G → S in HLPP1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_057919 | 181 | G → V in HLPP1; synthesized as a catalytically inactive form. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_004217 | 183 | D → G in HLPP1; lacks both triolein and tributyrin esterase activities. 3 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_057920 | 183 | D → H in HLPP1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_004218 | 183 | D → N in HLPP1; lacks both triolein and tributyrin esterase activities. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_004219 | 184 | P → R in HLPP1; Nijmegen; loss of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_004220 | 185 | A → T in HLPP1; 3.2% of activity. Corresponds to variant dbSNP:rs748349562Ensembl. | 1 | |
| Natural variantiVAR_057921 | 186 | G → E in HLPP1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_057922 | 190 | E → G in HLPP1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_004221 | 199 | S → C in HLPP1; mild hypertriglyceridemia; partial activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_057923 | 201 | D → V in HLPP1; almost complete loss of enzyme activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_004222 | 203 | A → T in HLPP1; Bethesda; loss of activity and abnormal heparin binding. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_004223 | 207 | D → E in HLPP1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_057924 | 208 | V → I in HLPP1; decreases the specific activity of the enzyme; has a mild effect on the secretion of the mutant enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_057925 | 210 | H → D in HLPP1; complete loss of enzyme activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_004224 | 210 | H → Q in HLPP1; loss of activity. | 1 | |
| Natural variantiVAR_004225 | 215 | G → E in HLPP1; loss of activity. 13 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_057926 | 215 | G → R in HLPP1. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_004226 | 220 | S → R in HLPP1; 2.0% of activity. Corresponds to variant dbSNP:rs757546424Ensembl. | 1 | |
| Natural variantiVAR_004227 | 221 | I → T in HLPP1; loss of activity. 6 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_004228 | 222 | G → E in HLPP1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_057927 | 225 | K → R in HLPP1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_057928 | 227 | V → A in HLPP1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_004229 | 231 | D → E in HLPP1; loss of activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_004230 | 232 | I → S in HLPP1; loss of activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_004231 | 234 | P → L in HLPP1; loss of activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_004232 | 243 | C → S in HLPP1; loss of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_057929 | 252 | I → T in HLPP1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_057930 | 266 | C → W in HLPP1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_057931 | 270 | R → C in HLPP1. 4 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_004233 | 270 | R → H in HLPP1; loss of activity. 6 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_004234 | 271 | S → T in HLPP1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_004235 | 277 | D → N in HLPP1; 5% of full activity. 5 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_004236 | 278 | S → C in HLPP1. | 1 | |
| Natural variantiVAR_057932 | 279 | L → R in HLPP1; decreases the specific activity of the enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_057933 | 279 | L → V in HLPP1; decreases the specific activity of the enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_004237 | 286 | S → G in HLPP1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_004238 | 286 | S → R in HLPP1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_011949 | 288 | A → T in HLPP1; the LPL mass level is approximately 67% of the normal; the activity is 32% of the nornal. 3 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_057934 | 289 | Y → H in HLPP1; no enzyme activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_057935 | 297 | F → L in HLPP1 and hyperlipidemia; synthesized as a catalytically inactive form; total amount is almost equal to that of the normal enzyme; non-releasable by heparin due to the abnormal structure of the mutant protein. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_057936 | 303 | L → F in HLPP1; approximately 6% of normal LPL activity and 40% of LPL mass are detected in the patient's postheparin plasma; results in the production of a functionally inactive enzyme. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_057937 | 305 | C → R in HLPP1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_057938 | 310 | C → Y in HLPP1; decreases the specific activity of the enzyme; reduces the secretion of the mutant protein significantly; the total LPL mass is reduced compared to that of the wild-type construct. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_057939 | 313 | L → P in HLPP1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_057940 | 325 | S → R in HLPP1; has no effect on the specific activity of the enzyme; has a mild effect on the secretion of the mutant enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_057941 | 328 | M → R in HLPP1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_004240 | 328 | M → T in HLPP1. Corresponds to variant dbSNP:rs1181582051Ensembl. | 1 | |
| Natural variantiVAR_057942 | 330 | L → F in HLPP1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_004241 | 330 | L → P in HLPP1. | 1 | |
| Natural variantiVAR_004242 | 361 | A → T in HLPP1. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_057943 | 365 | S → F in HLPP1; increases the specific activity of the enzyme; has a mild effect on the secretion of the mutant enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_004243 | 392 | L → V in HLPP1; loss of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_077541 | 404 | M → R in HLPP1; decreased protein secretion; loss of interaction with GPIHBP1; decreased lipoprotein lipase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_004244 | 423 – 424 | Missing in HLPP1; affects the protein folding. | 2 | |
| Natural variantiVAR_004245 | 437 | E → K in HLPP1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_004246 | 437 | E → V in HLPP1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_057944 | 445 | C → Y 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. 3 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_057945 | 448 | E → K in HLPP1; results in a moderate reduction in catalytic activity. 1 Publication Manual assertion based on experiment ini
| 1 |
Hyperlipidemia, familial combined, 3 (FCHL3)6 PublicationsManual assertion based on experiment ini
- Ref.57"A lipoprotein lipase mutation (Asn291Ser) is associated with reduced HDL cholesterol levels in premature atherosclerosis."
Reymer P.W.A., Gagne E., Groenemeyer B.E., Zhang H., Forsyth I., Jansen H., Seidell J.C., Kromhout D., Lie K.E., Kastelein J.J., Hayden M.R.
Nat. Genet. 10:28-34(1995) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT FCHL3 SER-318. - Ref.59"Lipoprotein lipase gene mutations D9N and N291S in four pedigrees with familial combined hyperlipidaemia."
de Bruin T.W.A., Mailly F., van Barlingen H.H.J.J., Fisher R., Castro Cabezas M., Talmud P., Dallinga-Thie G.M., Humphries S.E.
Eur. J. Clin. Invest. 26:631-639(1996) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS FCHL3 ASN-36 AND SER-318. - Ref.62"Homozygosity for two point mutations in the lipoprotein lipase (LPL) gene in a patient with familial LPL deficiency: LPL(Asp9-->Asn, Tyr262-->His)."
Rouis M., Lohse P., Dugi K.A., Lohse P., Beg O.U., Ronan R., Talley G.D., Brunzell J.D., Santamarina-Fojo S.
J. Lipid Res. 37:651-661(1996) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 HIS-289, VARIANT FCHL3 ASN-36, CHARACTERIZATION OF VARIANT HLPP1 HIS-289, CHARACTERIZATION OF VARIANT FCHL3 ASN-36. - Ref.70"Common genetic variants of lipoprotein lipase and apolipoproteins AI-CIII that relate to coronary artery disease: a study in Chinese and European subjects."
Zhang Q., Liu Y., Liu B.W., Fan P., Cavanna J., Galton D.J.
Mol. Genet. Metab. 64:177-183(1998) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 THR-288, VARIANTS FCHL3 ASN-36 AND SER-318. - Ref.71"DNA sequence diversity in a 9.7-kb region of the human lipoprotein lipase gene."
Nickerson D.A., Taylor S.L., Weiss K.M., Clark A.G., Hutchinson R.G., Stengaerd J., Salomaa V., Vartiainen E., Boerwinkle E., Sing C.F.
Nat. Genet. 19:233-240(1998) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT FCHL3 SER-318, VARIANTS MET-370 AND ALA-379. - Ref.82"Association of extreme blood lipid profile phenotypic variation with 11 reverse cholesterol transport genes and 10 non-genetic cardiovascular disease risk factors."
Morabia A., Cayanis E., Costanza M.C., Ross B.M., Flaherty M.S., Alvin G.B., Das K., Gilliam T.C.
Hum. Mol. Genet. 12:2733-2743(2003) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS FCHL3 ASN-36 AND SER-318.
Ref.57
"A lipoprotein lipase mutation (Asn291Ser) is associated with reduced HDL cholesterol levels in premature atherosclerosis."
Reymer P.W.A., Gagne E., Groenemeyer B.E., Zhang H., Forsyth I., Jansen H., Seidell J.C., Kromhout D., Lie K.E., Kastelein J.J., Hayden M.R.
Nat. Genet. 10:28-34(1995) [PubMed] [Europe PMC] [Abstract]
Reymer P.W.A., Gagne E., Groenemeyer B.E., Zhang H., Forsyth I., Jansen H., Seidell J.C., Kromhout D., Lie K.E., Kastelein J.J., Hayden M.R.
Nat. Genet. 10:28-34(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FCHL3 SER-318.
Ref.59
"Lipoprotein lipase gene mutations D9N and N291S in four pedigrees with familial combined hyperlipidaemia."
de Bruin T.W.A., Mailly F., van Barlingen H.H.J.J., Fisher R., Castro Cabezas M., Talmud P., Dallinga-Thie G.M., Humphries S.E.
Eur. J. Clin. Invest. 26:631-639(1996) [PubMed] [Europe PMC] [Abstract]
de Bruin T.W.A., Mailly F., van Barlingen H.H.J.J., Fisher R., Castro Cabezas M., Talmud P., Dallinga-Thie G.M., Humphries S.E.
Eur. J. Clin. Invest. 26:631-639(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FCHL3 ASN-36 AND SER-318.
Ref.62
"Homozygosity for two point mutations in the lipoprotein lipase (LPL) gene in a patient with familial LPL deficiency: LPL(Asp9-->Asn, Tyr262-->His)."
Rouis M., Lohse P., Dugi K.A., Lohse P., Beg O.U., Ronan R., Talley G.D., Brunzell J.D., Santamarina-Fojo S.
J. Lipid Res. 37:651-661(1996) [PubMed] [Europe PMC] [Abstract]
Rouis M., Lohse P., Dugi K.A., Lohse P., Beg O.U., Ronan R., Talley G.D., Brunzell J.D., Santamarina-Fojo S.
J. Lipid Res. 37:651-661(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1 HIS-289, VARIANT FCHL3 ASN-36, CHARACTERIZATION OF VARIANT HLPP1 HIS-289, CHARACTERIZATION OF VARIANT FCHL3 ASN-36.
Ref.70
"Common genetic variants of lipoprotein lipase and apolipoproteins AI-CIII that relate to coronary artery disease: a study in Chinese and European subjects."
Zhang Q., Liu Y., Liu B.W., Fan P., Cavanna J., Galton D.J.
Mol. Genet. Metab. 64:177-183(1998) [PubMed] [Europe PMC] [Abstract]
Zhang Q., Liu Y., Liu B.W., Fan P., Cavanna J., Galton D.J.
Mol. Genet. Metab. 64:177-183(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLPP1 THR-288, VARIANTS FCHL3 ASN-36 AND SER-318.
Ref.71
"DNA sequence diversity in a 9.7-kb region of the human lipoprotein lipase gene."
Nickerson D.A., Taylor S.L., Weiss K.M., Clark A.G., Hutchinson R.G., Stengaerd J., Salomaa V., Vartiainen E., Boerwinkle E., Sing C.F.
Nat. Genet. 19:233-240(1998) [PubMed] [Europe PMC] [Abstract]
Nickerson D.A., Taylor S.L., Weiss K.M., Clark A.G., Hutchinson R.G., Stengaerd J., Salomaa V., Vartiainen E., Boerwinkle E., Sing C.F.
Nat. Genet. 19:233-240(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FCHL3 SER-318, VARIANTS MET-370 AND ALA-379.
Ref.82
"Association of extreme blood lipid profile phenotypic variation with 11 reverse cholesterol transport genes and 10 non-genetic cardiovascular disease risk factors."
Morabia A., Cayanis E., Costanza M.C., Ross B.M., Flaherty M.S., Alvin G.B., Das K., Gilliam T.C.
Hum. Mol. Genet. 12:2733-2743(2003) [PubMed] [Europe PMC] [Abstract]
Morabia A., Cayanis E., Costanza M.C., Ross B.M., Flaherty M.S., Alvin G.B., Das K., Gilliam T.C.
Hum. Mol. Genet. 12:2733-2743(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FCHL3 ASN-36 AND SER-318.
Disease susceptibility is associated with variants affecting the gene represented in this entry.
Disease descriptionA disorder characterized by a variable pattern of elevated levels of serum total cholesterol, triglycerides or both. It is observed in a percentage of individuals with premature coronary heart disease. FCHL3 inheritance is autosomal dominant.
Related information in OMIM| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Natural variantiVAR_011948 | 36 | D → N in FCHL3; associated with disease susceptibility; has approximately 80% of the specific activity of wild-type enzyme. 4 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_004239 | 318 | N → S in FCHL3; associated with disease susceptibility; loss of activity; frequent mutation. 7 Publications Manual assertion based on experiment ini
| 1 |
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 159 | S → G: Loss of enzyme activity with triolein and tributyrin. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 159 | S → T: Loss of enzyme activity with triolein and tributyrin. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 183 | D → G or N: Loss of enzyme activity with triolein and tributyrin. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 199 | S → G: Loss of enzyme activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 201 | D → E: No effect on enzyme activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 202 | D → E: Loss of enzyme activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 244 – 264 | NIGEA…VDQLV → HFLELYRHIAQHGFNAITQT I: Reduced triglyceride hydrolase activity and increased phospholipase activity. 1 Publication Manual assertion based on experiment ini
| 21 | |
| Mutagenesisi | 245 – 263 | IGEAI…DVDQL → GIAEIRVIEARGGLDVDLQ: Loss of both triglyceride hydrolase and phospholipase activity. 1 Publication Manual assertion based on experiment ini
| 19 | |
| Mutagenesisi | 245 – 248 | IGEA → GIAE: Loss of triglyceride hydrolase activity while phospholipase activity remains intact. 1 Publication Manual assertion based on experiment ini
| 4 | |
| Mutagenesisi | 262 – 263 | QL → LQ: Loss of triglyceride hydrolase activity while phospholipase activity remains intact. 1 Publication Manual assertion based on experiment ini
| 2 | |
| Mutagenesisi | 268 | H → G: Loss of enzyme activity with triolein and tributyrin. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 268 | H → Q: Loss of enzyme activity with triolein and tributyrin. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 417 | W → A: Loss of interaction with lipoprotein particles, but no effect on interaction with GPIHBP1; when associated with 420-A-A-421. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 420 – 421 | WW → AA: Loss of interaction with lipoprotein particles, but no effect on interaction with GPIHBP1; when associated with A-417. 1 Publication Manual assertion based on experiment ini
| 2 | |
| Mutagenesisi | 430 | K → N: Impaired heparin-binding; when associated with N-432 and N-437. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 432 | R → N: Impaired heparin-binding; when associated with N-430 and N-437. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 434 | K → N: Impaired heparin-binding; when associated with N-430 and N-432. 1 Publication Manual assertion based on experiment ini
| 1 |
Keywords - Diseasei
Disease variant, HyperlipidemiaOrganism-specific databases
DisGeNET More...DisGeNETi | 4023 |
GeneReviews a resource of expert-authored, peer-reviewed disease descriptions. More...GeneReviewsi | LPL |
MalaCards human disease database More...MalaCardsi | LPL |
| MIMi | 144250, phenotype 238600, phenotype |
Open Targets More...OpenTargetsi | ENSG00000175445 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 309015, Familial lipoprotein lipase deficiency |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA232 |
Miscellaneous databases
Pharos NIH Druggable Genome Knowledgebase More...Pharosi | P06858, Tchem |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL2060 |
Drug and drug target database More...DrugBanki | DB13751, Glycyrrhizic acid DB09568, Omega-3-carboxylic acids DB13928, Semaglutide DB06439, Tyloxapol |
DrugCentral More...DrugCentrali | P06858 |
Genetic variation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | LPL |
Domain mapping of disease mutations (DMDM) More...DMDMi | 126314 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei | 1 – 27 | 1 Publication Manual assertion based on experiment ini
| 27 | |
| <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000017775 | 28 – 475 | Lipoprotein lipaseAdd BLAST | 448 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 54 ↔ 67 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Combined sources<p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0007744">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 70 | N-linked (GlcNAc...) asparagineCombined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 1 | |
| <p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 121 | 3'-nitrotyrosineBy similarity Manual assertion inferred from sequence similarity toi | 1 | |
| Modified residuei | 191 | 3'-nitrotyrosineBy similarity Manual assertion inferred from sequence similarity toi | 1 | |
| Disulfide bondi | 243 ↔ 266 | PROSITE-ProRule annotation Manual assertion according to rulesi Combined sourcesManual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| ||
| Disulfide bondi | 291 ↔ 310 | PROSITE-ProRule annotation Manual assertion according to rulesi Combined sourcesManual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| ||
| Disulfide bondi | 302 ↔ 305 | PROSITE-ProRule annotation Manual assertion according to rulesi Combined sourcesManual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| ||
| Modified residuei | 343 | 3'-nitrotyrosineBy similarity Manual assertion inferred from sequence similarity toi | 1 | |
| Glycosylationi | 386 | N-linked (GlcNAc...) asparagineCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Disulfide bondi | 445 ↔ 465 | PROSITE-ProRule annotation Manual assertion according to rulesi Combined sourcesManual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
|
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity.By similarity
Manual assertion inferred from sequence similarity toi
Keywords - PTMi
Disulfide bond, Glycoprotein, NitrationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P06858 |
jPOST - Japan Proteome Standard Repository/Database More...jPOSTi | P06858 |
MassIVE - Mass Spectrometry Interactive Virtual Environment More...MassIVEi | P06858 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P06858 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P06858 |
PeptideAtlas More...PeptideAtlasi | P06858 |
PRoteomics IDEntifications database More...PRIDEi | P06858 |
ProteomicsDB: a multi-organism proteome resource More...ProteomicsDBi | 51936 |
PTM databases
GlyConnect protein glycosylation platform More...GlyConnecti | 2940, 18 N-Linked glycans (1 site) |
GlyGen: Computational and Informatics Resources for Glycoscience More...GlyGeni | P06858, 2 sites, 21 N-linked glycans (1 site) |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P06858 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P06858 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
Detected in blood plasma (PubMed:2340307, PubMed:11893776, PubMed:12641539). Detected in milk (at protein level) (PubMed:2340307).3 Publications
Manual assertion based on experiment ini
- Ref.10"Rapid and simple isolation procedure for lipoprotein lipase from human milk."
Zechner R.
Biochim. Biophys. Acta 1044:20-25(1990) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 28-44, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY. - Ref.80"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) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANTS HLPP1 THR-203; GLU-215; THR-221; SER-232 AND LEU-234, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.81"Novel LPL mutation (L303F) found in a patient associated with coronary artery disease and severe systemic atherosclerosis."
Saika Y., Sakai N., Takahashi M., Maruyama T., Kihara S., Ouchi N., Ishigami M., Hiraoka H., Nakamura T., Yamashita S., Matsuzawa Y.
Eur. J. Clin. Invest. 33:216-222(2003) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HLPP1 PHE-303, CHARACTERIZATION OF VARIANT HLPP1 PHE-303, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000175445, Expressed in adipose tissue and 237 other tissues |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P06858, baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P06858, HS |
Organism-specific databases
Human Protein Atlas More...HPAi | ENSG00000175445, Tissue enhanced (adipose tissue, heart muscle) |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Homodimer (PubMed:16179346, PubMed:26725083, PubMed:11893776) (Probable).
Interacts with GPIHBP1 with 1:1 stoichiometry (PubMed:17997385, PubMed:27929370, PubMed:26725083, PubMed:27811232, PubMed:29899144, PubMed:30559189).
Interacts with APOC2; the interaction activates LPL activity in the presence of lipids (By similarity). Interaction with heparan sulfate proteoglycans is required to protect LPL against loss of activity (PubMed:11342582). Associates with lipoprotein particles in blood plasma (PubMed:11342582, PubMed:11893776).
Interacts with LMF1 and SEL1L; interaction with SEL1L is required to prevent aggregation of newly synthesized LPL in the endoplasmic reticulum (ER), and for normal export of LPL from the ER to the extracellular space (PubMed:25066055).
Interacts with SORL1; SORL1 acts as a sorting receptor, promoting LPL localization to endosomes and later to lysosomes, leading to degradation of newly synthesized LPL (PubMed:21385844).
By similarityManual assertion inferred from sequence similarity toi
1 PublicationManual assertion inferred by curator fromi
- Ref.26"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) [PubMed] [Europe PMC] [Abstract]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.
Manual assertion based on experiment ini
- Ref.13"Heparin-binding defective lipoprotein lipase is unstable and causes abnormalities in lipid delivery to tissues."
Lutz E.P., Merkel M., Kako Y., Melford K., Radner H., Breslow J.L., Bensadoun A., Goldberg I.J.
J. Clin. Invest. 107:1183-1192(2001) [PubMed] [Europe PMC] [Abstract]Cited for: HEPARIN-BINDING, CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-430; ARG-432 AND LYS-434. - Ref.15"Calcium triggers folding of lipoprotein lipase into active dimers."
Zhang L., Lookene A., Wu G., Olivecrona G.
J. Biol. Chem. 280:42580-42591(2005) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, SUBUNIT, CALCIUM BINDING. - Ref.16"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) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH GPIHBP1. - Ref.18"SorLA regulates the activity of lipoprotein lipase by intracellular trafficking."
Klinger S.C., Glerup S., Raarup M.K., Mari M.C., Nyegaard M., Koster G., Prabakaran T., Nilsson S.K., Kjaergaard M.M., Bakke O., Nykjaer A., Olivecrona G., Petersen C.M., Nielsen M.S.
J. Cell Sci. 124:1095-1105(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SORL1. - Ref.19"The ER-associated degradation adaptor protein Sel1L regulates LPL secretion and lipid metabolism."
Sha H., Sun S., Francisco A.B., Ehrhardt N., Xue Z., Liu L., Lawrence P., Mattijssen F., Guber R.D., Panhwar M.S., Brenna J.T., Shi H., Xue B., Kersten S., Bensadoun A., Peterfy M., Long Q., Qi L.
Cell Metab. 20:458-470(2014) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SEL1L AND LMF1. - Ref.21"The angiopoietin-like protein ANGPTL4 catalyzes unfolding of the hydrolase domain in lipoprotein lipase and the endothelial membrane protein GPIHBP1 counteracts this unfolding."
Mysling S., Kristensen K.K., Larsson M., Kovrov O., Bensadouen A., Joergensen T.J., Olivecrona G., Young S.G., Ploug M.
Elife 5:0-0(2016) [PubMed] [Europe PMC] [Abstract]Cited for: ACTIVITY REGULATION, INTERACTION WITH GPIHBP1. - Ref.22"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) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, INTERACTION WITH GPIHBP1, SUBUNIT, CHARACTERIZATION OF VARIANT HLPP1 TYR-445. - Ref.23"Mobility of 'HSPG-bound' LPL explains how LPL is able to reach GPIHBP1 on capillaries."
Allan C.M., Larsson M., Jung R.S., Ploug M., Bensadoun A., Beigneux A.P., Fong L.G., Young S.G.
J. Lipid Res. 58:216-225(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH GPIHBP1, SUBCELLULAR LOCATION. - Ref.24"A disordered acidic domain in GPIHBP1 harboring a sulfated tyrosine regulates lipoprotein lipase."
Kristensen K.K., Midtgaard S.R., Mysling S., Kovrov O., Hansen L.B., Skar-Gislinge N., Beigneux A.P., Kragelund B.B., Olivecrona G., Young S.G., Joergensen T.J.D., Fong L.G., Ploug M.
Proc. Natl. Acad. Sci. U.S.A. 115:E6020-E6029(2018) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH GPIHBP1, ACTIVITY REGULATION, CATALYTIC ACTIVITY. - Ref.26"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) [PubMed] [Europe PMC] [Abstract]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. - Ref.80"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) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANTS HLPP1 THR-203; GLU-215; THR-221; SER-232 AND LEU-234, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
P06858
GO - Molecular functioni
- apolipoprotein binding Source: BHF-UCLInferred from physical interactioni
- "Mechanism of triglyceride lowering in mice expressing human apolipoprotein A5."
Fruchart-Najib J., Bauge E., Niculescu L.S., Pham T., Thomas B., Rommens C., Majd Z., Brewer B., Pennacchio L.A., Fruchart J.C.
Biochem Biophys Res Commun 319:397-404(2004) [PubMed] [Europe PMC] [Abstract]
- heparan sulfate proteoglycan binding Source: UniProtKBInferred from mutant phenotypei
- Ref.13"Heparin-binding defective lipoprotein lipase is unstable and causes abnormalities in lipid delivery to tissues."
Lutz E.P., Merkel M., Kako Y., Melford K., Radner H., Breslow J.L., Bensadoun A., Goldberg I.J.
J. Clin. Invest. 107:1183-1192(2001) [PubMed] [Europe PMC] [Abstract]Cited for: HEPARIN-BINDING, CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-430; ARG-432 AND LYS-434.
- protein homodimerization activity Source: UniProtKBInferred from direct assayi
- Ref.15"Calcium triggers folding of lipoprotein lipase into active dimers."
Zhang L., Lookene A., Wu G., Olivecrona G.
J. Biol. Chem. 280:42580-42591(2005) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, SUBUNIT, CALCIUM BINDING.
- signaling receptor binding Source: BHF-UCLInferred from physical interactioni
- "Sortilin/neurotensin receptor-3 binds and mediates degradation of lipoprotein lipase."
Nielsen M.S., Jacobsen C., Olivecrona G., Gliemann J., Petersen C.M.
J. Biol. Chem. 274:8832-8836(1999) [PubMed] [Europe PMC] [Abstract]
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGRID) More...BioGRIDi | 110205, 23 interactors |
ComplexPortal: manually curated resource of macromolecular complexes More...ComplexPortali | CPX-6091, LPL-GPIHBP1 triglyceride-rich lipoprotein processing complex |
Protein interaction database and analysis system More...IntActi | P06858, 30 interactors |
Molecular INTeraction database More...MINTi | P06858 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000309757 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P06858 |
Miscellaneous databases
RNAct, Protein-RNA interaction predictions for model organisms. More...RNActi | P06858, protein |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 31 – 34 | Combined sources <p>Information inferred from a combination of experimental and computational evidence, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000213">More...</a></p> Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 40 – 44 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 54 – 56 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 61 – 66 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 71 – 73 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 75 – 79 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 84 – 87 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 91 – 102 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 12 | |
| Beta strandi | 106 – 112 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 114 – 117 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 121 – 124 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 125 – 127 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 128 – 146 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 19 | |
| Helixi | 150 – 152 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 153 – 158 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 160 – 169 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
| Beta strandi | 172 – 174 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 176 – 183 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
| Turni | 187 – 189 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 194 – 196 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 200 – 202 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 203 – 209 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| Beta strandi | 219 – 222 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 228 – 234 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| Turni | 235 – 238 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Turni | 241 – 243 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 247 – 253 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 262 – 280 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 19 | |
| Beta strandi | 282 – 284 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 287 – 290 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 294 – 298 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 308 – 314 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| Beta strandi | 326 – 330 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 334 – 337 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 341 – 350 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
| Beta strandi | 356 – 370 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 15 | |
| Beta strandi | 372 – 384 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 13 | |
| Beta strandi | 387 – 397 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 11 | |
| Beta strandi | 401 – 409 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 9 | |
| Turni | 414 – 417 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 425 – 428 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 430 – 435 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Turni | 436 – 439 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 440 – 454 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 15 | |
| Beta strandi | 460 – 469 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 |
3D structure databases
Small Angle Scattering Biological Data Bank More...SASBDBi | P06858 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P06858 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 341 – 464 | PLATPROSITE-ProRule annotation Manual assertion according to rulesi Add BLAST | 124 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 32 – 53 | Interaction with GPIHBP11 Publication Manual assertion based on experiment ini
| 22 | |
| Regioni | 243 – 266 | Essential for determining substrate specificity1 Publication Manual assertion based on experiment ini
| 24 | |
| Regioni | 417 – 421 | Important for interaction with lipoprotein particles1 Publication Manual assertion based on experiment ini
| 5 | |
| Regioni | 430 – 434 | Important for heparin binding1 Publication Manual assertion based on experiment ini
| 5 | |
| Regioni | 443 – 467 | Interaction with GPIHBP12 Publications Manual assertion based on experiment ini
| 25 |
<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Keywords - Domaini
SignalPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG502QQ7P, Eukaryota |
Ensembl GeneTree More...GeneTreei | ENSGT00940000157178 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | CLU_027171_1_0_1 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P06858 |
Identification of Orthologs from Complete Genome Data More...OMAi | TRDMMPY |
Database of Orthologous Groups More...OrthoDBi | 534956at2759 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P06858 |
TreeFam database of animal gene trees More...TreeFami | TF324997 |
Family and domain databases
Conserved Domains Database More...CDDi | cd00707, Pancreat_lipase_like, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.40.50.1820, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR029058, AB_hydrolase IPR013818, Lipase IPR016272, Lipase_LIPH IPR033906, Lipase_N IPR002330, Lipo_Lipase IPR001024, PLAT/LH2_dom IPR036392, PLAT/LH2_dom_sf IPR000734, TAG_lipase |
The PANTHER Classification System More...PANTHERi | PTHR11610, PTHR11610, 1 hit PTHR11610:SF3, PTHR11610:SF3, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00151, Lipase, 1 hit PF01477, PLAT, 1 hit |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF000865, Lipoprotein_lipase_LIPH, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00822, LIPOLIPASE PR00821, TAGLIPASE |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00308, LH2, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF49723, SSF49723, 1 hit SSF53474, SSF53474, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR03230, lipo_lipase, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00120, LIPASE_SER, 1 hit PS50095, PLAT, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
This entry has 1 described isoform and 5 potential isoforms that are computationally mapped.Show allAlign All
P06858-1 [UniParc]FASTAAdd to basketAdded to basket
« Hide
Show »10 20 30 40 50
MESKALLVLT LAVWLQSLTA SRGGVAAADQ RRDFIDIESK FALRTPEDTA
60 70 80 90 100
EDTCHLIPGV AESVATCHFN HSSKTFMVIH GWTVTGMYES WVPKLVAALY
110 120 130 140 150
KREPDSNVIV VDWLSRAQEH YPVSAGYTKL VGQDVARFIN WMEEEFNYPL
160 170 180 190 200
DNVHLLGYSL GAHAAGIAGS LTNKKVNRIT GLDPAGPNFE YAEAPSRLSP
210 220 230 240 250
DDADFVDVLH TFTRGSPGRS IGIQKPVGHV DIYPNGGTFQ PGCNIGEAIR
260 270 280 290 300
VIAERGLGDV DQLVKCSHER SIHLFIDSLL NEENPSKAYR CSSKEAFEKG
310 320 330 340 350
LCLSCRKNRC NNLGYEINKV RAKRSSKMYL KTRSQMPYKV FHYQVKIHFS
360 370 380 390 400
GTESETHTNQ AFEISLYGTV AESENIPFTL PEVSTNKTYS FLIYTEVDIG
410 420 430 440 450
ELLMLKLKWK SDSYFSWSDW WSSPGFAIQK IRVKAGETQK KVIFCSREKV
460 470
SHLQKGKAPA VFVKCHDKSL NKKSG
Length:475
Mass (Da):53,162
Last modified:January 1, 1988 - v1
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:iFBD00FCD334FB8AA
<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi
There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket| Entry | Entry name | Protein names | Gene names | Length | Annotation | ||
|---|---|---|---|---|---|---|---|
| E5RJI0 | E5RJI0_HUMAN | Phospholipase A1 Phospholipase A1 | LPL | 129 | Annotation score: Annotation score:2 out of 5 <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p> | ||
| E5RHN7 | E5RHN7_HUMAN | Phospholipase A1 Phospholipase A1 | LPL | 105 | Annotation score: Annotation score:2 out of 5 <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'c | ||