UniProtKB - P06858 (LIPL_HUMAN)
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- BLAST>sp|P06858|LIPL_HUMAN Lipoprotein lipase OS=Homo sapiens OX=9606 GN=LPL PE=1 SV=1 MESKALLVLTLAVWLQSLTASRGGVAAADQRRDFIDIESKFALRTPEDTAEDTCHLIPGV AESVATCHFNHSSKTFMVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQEH YPVSAGYTKLVGQDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRIT GLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQ PGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCSSKEAFEKG LCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTESETHTNQ AFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMLKLKWKSDSYFSWSDW WSSPGFAIQKIRVKAGETQKKVIFCSREKVSHLQKGKAPAVFVKCHDKSLNKKSG
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Lipoprotein lipase
LPL
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome.<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
<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"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. - Ref.74"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 LPL DEFICIENCY ARG-404, CHARACTERIZATION OF VARIANT LPL DEFICIENCY ARG-404, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
<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"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. - Ref.74"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 LPL DEFICIENCY ARG-404, CHARACTERIZATION OF VARIANT LPL DEFICIENCY ARG-404, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the ‘Function’ 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 | Nucleophile | 1 | |
<p>This subsection of the ‘Function’ 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 | 183 | Charge relay system | 1 | |
<p>This subsection of the ‘Function’ 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 | 268 | Charge relay system | 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
- 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
- heparin 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
- lipoprotein lipase activity 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
- 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
- receptor 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
- triglyceride binding Source: Ensembl
- triglyceride lipase activity Source: BHF-UCL <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
<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 - Biological processi
- cholesterol homeostasis Source: BHF-UCL <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
- chylomicron remodeling Source: Reactome
- fatty acid biosynthetic process Source: BHF-UCL <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
- low-density lipoprotein particle mediated signaling Source: BHF-UCL <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
- phospholipid metabolic process 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
- positive regulation of chemokine secretion Source: BHF-UCL <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
- positive regulation of cholesterol storage Source: BHF-UCL <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
- positive regulation of inflammatory response 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
- 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
- positive regulation of sequestering of triglyceride Source: BHF-UCL <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
- regulation of lipoprotein lipase activity Source: Reactome
- response to cold Source: Ensembl
- response to drug Source: Ensembl
- response to glucose Source: AgBase
- retinoid metabolic process Source: Reactome
- triglyceride biosynthetic process 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
- triglyceride catabolic process 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
- 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
- triglyceride metabolic process 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
- very-low-density lipoprotein particle remodeling Source: BHF-UCL <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
<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 |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.1.1.34. 2681. |
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. |
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_and_taxonomy_section">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:3.1.1.342 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
Short name: LPL |
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the <span class="caps">NCBI</span> 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_and_taxonomy_section">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_and_taxonomy_section">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
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000175445.14. |
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. |
<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
Extracellular region or secreted
- Secreted 2 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.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. - Ref.74"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 LPL DEFICIENCY ARG-404, CHARACTERIZATION OF VARIANT LPL DEFICIENCY ARG-404, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
- Secreted 2 Publications
Plasma membrane
- Cell membrane By similarity; GPI-anchor By similarity
Note: Locates to the plasma membrane of microvilli of hepatocytes with triacyl-glycerol-rich lipoproteins (TRL). Some of the bound LPL is then internalized and located inside non-coated endocytic vesicles (By similarity).By similarity
Extracellular region or secreted
- chylomicron Source: UniProtKB-KW
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
- extracellular matrix Source: Ensembl
- extracellular region Source: Reactome
- extracellular space 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
- very-low-density lipoprotein particle Source: UniProtKB-KW
Plasma Membrane
- plasma membrane Source: UniProtKB-SubCell
Other locations
- anchored component of membrane Source: UniProtKB-KW
- cell surface Source: Ensembl
<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>Keywords - Cellular componenti
Cell membrane, Chylomicron, 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"><span class="caps">OMIM</span></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
Lipoprotein lipase deficiency (LPL deficiency)55 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.17"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 LPL DEFICIENCY THR-271, INVOLVEMENT IN LPL. - Ref.18"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 LPL DEFICIENCY GLU-215. - Ref.19"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 LPL DEFICIENCY GLU-215. - Ref.20"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 LPL DEFICIENCY THR-203. - Ref.21"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 LPL DEFICIENCY THR-221 AND HIS-270. - Ref.22"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 LPL DEFICIENCY GLY-183. - Ref.23"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 LPL DEFICIENCY GLU-169. - Ref.24"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 LPL DEFICIENCY THR-221. - Ref.25"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 LPL DEFICIENCY GLU-231 AND HIS-270, CHARACTERIZATION OF VARIANTS LPL DEFICIENCY GLU-231 AND HIS-270. - Ref.26"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 LPL DEFICIENCY LEU-234. - Ref.27"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 LPL DEFICIENCY ARG-113. - Ref.28"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 LPL DEFICIENCY ARG-184. - Ref.29"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 LPL DEFICIENCY ASN-277. - Ref.30"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 LPL DEFICIENCY ASN-183; GLY-183 AND SER-243. - Ref.32"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 LPL DEFICIENCY GLU-222. - Ref.33"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 LPL DEFICIENCY GLU-215; HIS-270 AND ASN-277. - Ref.34"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 LPL DEFICIENCY ARG-113; ARG-163; GLU-215; THR-221 AND SER-232. - Ref.35"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 LPL DEFICIENCY THR-361. - Ref.36"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 LPL DEFICIENCY GLU-207. - Ref.37"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 LPL DEFICIENCY CYS-199. - Ref.38"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 LPL DEFICIENCY SER-102. - Ref.39"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 LPL DEFICIENCY SER-181. - Ref.40"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 LPL DEFICIENCY VAL-392. - Ref.41"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 LPL DEFICIENCY SER-70, CHARACTERIZATION OF VARIANT LPL DEFICIENCY SER-70. - Ref.42"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 LPL DEFICIENCY HIS-270 AND CYS-270. - Ref.43"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 LPL DEFICIENCY LEU-96 AND GLU-215, CHARACTERIZATION OF VARIANT LPL DEFICIENCY LEU-96. - Ref.44"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 LPL DEFICIENCY CYS-199; ARG-279; THR-288 AND SER-318, CHARACTERIZATION OF VARIANTS LPL DEFICIENCY ARG-279 AND THR-288. - Ref.45"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 LPL DEFICIENCY VAL-437. - Ref.46"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 LPL DEFICIENCY SER-318. - Ref.47"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 LPL DEFICIENCY TYR-445, CHARACTERIZATION OF VARIANT LPL DEFICIENCY TYR-445. - Ref.48"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: VARIANT LPL DEFICIENCY SER-318, VARIANT ASN-36. - Ref.49"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 LPL DEFICIENCY ASN-277 AND LYS-437. - Ref.50"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 LPL DEFICIENCY GLY-190 AND GLU-215. - Ref.51"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 LPL DEFICIENCY HIS-289, VARIANT ASN-36, CHARACTERIZATION OF VARIANT LPL DEFICIENCY HIS-289, CHARACTERIZATION OF VARIANT ASN-36. - Ref.52"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 LPL DEFICIENCY ALA-128; GLU-215; ARG-215; CYS-270; ASN-277 AND PRO-313. - Ref.53"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 LPL DEFICIENCY ARG-286. - Ref.55"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 LPL DEFICIENCY ALA-128; HIS-183; GLU-215; ARG-215; LEU-234; CYS-270 AND ASN-277. - Ref.56"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 LPL DEFICIENCY THR-252 AND HIS-270. - Ref.57"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 LPL DEFICIENCY LYS-448, CHARACTERIZATION OF VARIANT LPL DEFICIENCY LYS-448. - Ref.58"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 LPL DEFICIENCY GLU-215 AND GLY-286. - Ref.59"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: VARIANTS LPL DEFICIENCY THR-288 AND SER-318, VARIANT ASN-36. - Ref.60"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 LPL DEFICIENCY SER-318, VARIANTS MET-370 AND ALA-379. - Ref.62"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 LPL DEFICIENCY LEU-297, CHARACTERIZATION OF VARIANT LPL DEFICIENCY LEU-297. - Ref.63"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 LPL DEFICIENCY ARG-132 AND GLU-231, CHARACTERIZATION OF VARIANTS LPL DEFICIENCY ARG-132 AND GLU-231. - Ref.64"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 LPL DEFICIENCY TRP-266. - Ref.65"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 LPL DEFICIENCY ASP-210, CHARACTERIZATION OF VARIANT LPL DEFICIENCY ASP-210. - Ref.66"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 LPL DEFICIENCY VAL-181, CHARACTERIZATION OF VARIANT LPL DEFICIENCY VAL-181. - Ref.67"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 LPL DEFICIENCY THR-98; ILE-208; VAL-279; ARG-279; TYR-310; ARG-325 AND PHE-365, CHARACTERIZATION OF VARIANTS LPL DEFICIENCY THR-98; ILE-208; VAL-279; ARG-279; TYR-310; ARG-325 AND PHE-365. - Ref.68"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 LPL DEFICIENCY PHE-303, CHARACTERIZATION OF VARIANT LPL DEFICIENCY PHE-303. - Ref.69"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: VARIANT LPL DEFICIENCY SER-318, VARIANT ASN-36. - Ref.70"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 LPL DEFICIENCY VAL-201. - Ref.71"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 LPL DEFICIENCY GLU-215 AND ARG-328. - Ref.72"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 LPL DEFICIENCY 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.73"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 LPL DEFICIENCY GLU-186; GLU-215 AND THR-221. - Ref.74"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 LPL DEFICIENCY ARG-404, CHARACTERIZATION OF VARIANT LPL DEFICIENCY ARG-404, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
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]
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]
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]
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]
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]
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]
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]
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]
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]
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]
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]
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]
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.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]
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]
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]
Reina M., Brunzell J.D., Deeb S.S.
J. Lipid Res. 33:1823-1832(1992) [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]
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]
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]
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]
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]
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]
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]
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]
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]
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]
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]
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]
Henderson H.E., Hassan F., Marais D., Hayden M.R.
Biochem. Biophys. Res. Commun. 227:189-194(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]
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., Santer R., Richter W., Assmann G.
Hum. Mutat. 8:392-392(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]
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]
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., 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]
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., Leisegang F., Hassan F., Hayden M., Marais D.
Clin. Chim. Acta 269:1-12(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]
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]
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]
Takagi A., Ikeda Y., Takeda E., Yamamoto A.
Biochim. Biophys. Acta 1502:433-446(2000) [PubMed] [Europe PMC] [Abstract]
Ikeda Y., Goji K., Takagi A.
Clin. Sci. 99:569-578(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]
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]
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]
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]
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]
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]
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]
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]
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]
Santer R., Gokcay G., Demirkol M., Gal A., Lukacs Z.
J. Inherit. Metab. Dis. 28:137-140(2005) [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]
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_011948 | 36 | D → N in LPL deficiency; has approximately 80% of the specific activity of wild-type enzyme. 4 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
| 1 | |
<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 LPL deficiency; produces an inactive protein which is not secreted into the media. 2 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
| 1 | |
<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_057915 | 96 | V → L in LPL deficiency; gives rise to a 80% decrease in specific catalytic activity. 1 Publication <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
| 1 | |
<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_057916 | 98 | A → T in LPL deficiency; 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 <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
| 1 | |
<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_004211 | 102 | R → S in LPL deficiency. 1 Publication <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
| 1 | |
<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_004212 | 113 | W → G in LPL deficiency. | 1 | |
<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_004213 | 113 | W → R in LPL deficiency. 2 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
| 1 | |
<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_057917 | 128 | T → A in LPL deficiency. 2 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
| 1 | |
<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_057918 | 132 | G → R in LPL deficiency; synthesized as a catalytically inactive form. 2 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
| 1 | |
<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_004214 | 163 | H → R in LPL deficiency. 1 Publication <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
| 1 | |
<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_004215 | 169 | G → E in LPL deficiency; loss of activity. 1 Publication <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
| 1 | |
<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_004216 | 181 | G → S in LPL deficiency. 1 Publication <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
| 1 | |
<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_057919 | 181 | G → V in LPL deficiency; synthesized as a catalytically inactive form. 2 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
| 1 | |
<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_004217 | 183 | D → G in LPL deficiency; lacks both triolein and tributyrin esterase activities. 3 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
| 1 | |
<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_057920 | 183 | D → H in LPL deficiency. 1 Publication <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
| 1 | |
<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_004218 | 183 | D → N in LPL deficiency; lacks both triolein and tributyrin esterase activities. 2 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
| 1 | |
<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_004219 | 184 | P → R in LPL deficiency; Nijmegen; loss of activity. 1 Publication <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
| 1 | |
<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_004220 | 185 | A → T in LPL deficiency; 3.2% of activity. Corresponds to variant dbSNP:rs748349562Ensembl. | 1 | |
<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_057921 | 186 | G → E in LPL deficiency. 1 Publication <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
| 1 | |
<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_057922 | 190 | E → G in LPL deficiency. 1 Publication <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
| 1 | |
<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_004221 | 199 | S → C in LPL deficiency; mild hypertriglyceridemia; partial activity. 2 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
| 1 | |
<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_057923 | 201 | D → V in LPL deficiency. 1 Publication <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
| 1 | |
<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_004222 | 203 | A → T in LPL deficiency; Bethesda; loss of activity and abnormal heparin binding. 1 Publication <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
| 1 | |
<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_004223 | 207 | D → E in LPL deficiency. 1 Publication <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
| 1 | |
<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_057924 | 208 | V → I in LPL deficiency; 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 <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
| 1 | |
<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_057925 | 210 | H → D in LPL deficiency; complete loss of enzyme activity. 1 Publication <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
| 1 | |
<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_004224 | 210 | H → Q in LPL deficiency; loss of activity. | 1 | |
<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_004225 | 215 | G → E in LPL deficiency; loss of activity. 12 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
| 1 | |
<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_057926 | 215 | G → R in LPL deficiency. 2 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
| 1 | |
<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_004226 | 220 | S → R in LPL deficiency; 2.0% of activity. Corresponds to variant dbSNP:rs757546424Ensembl. | 1 | |
<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_004227 | 221 | I → T in LPL deficiency; loss of activity. 5 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
| 1 | |
<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_004228 | 222 | G → E in LPL deficiency. 1 Publication <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
| 1 | |
<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_057927 | 225 | K → R in LPL deficiency. 1 Publication <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
| 1 | |
<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_057928 | 227 | V → A in LPL deficiency. 1 Publication <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
| 1 | |
<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_004229 | 231 | D → E in LPL deficiency; loss of activity. 3 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
| 1 | |
<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_004230 | 232 | I → S in LPL deficiency. 1 Publication <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
| 1 | |
<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_004231 | 234 | P → L in LPL deficiency; loss of activity. 2 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
| 1 | |
<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_004232 | 243 | C → S in LPL deficiency; loss of activity. 1 Publication <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
| 1 | |
<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_057929 | 252 | I → T in LPL deficiency. 1 Publication <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
| 1 | |
<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_057930 | 266 | C → W in LPL deficiency. 1 Publication <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
| 1 | |
<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_057931 | 270 | R → C in LPL deficiency. 4 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
| 1 | |
<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_004233 | 270 | R → H in LPL deficiency; loss of activity. 6 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
| 1 | |
<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_004234 | 271 | S → T in LPL deficiency. 1 Publication <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
| 1 | |
<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_004235 | 277 | D → N in LPL deficiency; 5% of full activity. 5 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
| 1 | |
<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_004236 | 278 | S → C in LPL deficiency. | 1 | |
<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_057932 | 279 | L → R in LPL deficiency; decreases the specific activity of the enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 2 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
| 1 | |
<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_057933 | 279 | L → V in LPL deficiency; decreases the specific activity of the enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 1 Publication <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
| 1 | |
<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_004237 | 286 | S → G in LPL deficiency. 1 Publication <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
| 1 | |
<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_004238 | 286 | S → R in LPL deficiency. 1 Publication <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
| 1 | |
<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_011949 | 288 | A → T in LPL deficiency; the LPL mass level is approximately 67% of the normal; the activity is 32% of the nornal. 3 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
| 1 | |
<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_057934 | 289 | Y → H in LPL deficiency; no enzyme activity. 1 Publication <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
| 1 | |
<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_057936 | 303 | L → F in LPL deficiency; 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 <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
| 1 | |
<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_057937 | 305 | C → R in LPL deficiency. 1 Publication <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
| 1 | |
<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_057938 | 310 | C → Y in LPL deficiency; 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 <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
| 1 | |
<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_057939 | 313 | L → P in LPL deficiency. 1 Publication <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
| 1 | |
<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_004239 | 318 | N → S in LPL deficiency; loss of activity; frequent mutation. 8 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
| 1 | |
<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_057940 | 325 | S → R in LPL deficiency; 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 <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
| 1 | |
<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_057941 | 328 | M → R in LPL deficiency. 1 Publication <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
| 1 | |
<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_004240 | 328 | M → T in LPL deficiency. | 1 | |
<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_057942 | 330 | L → F in LPL deficiency. 1 Publication <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
| 1 | |
<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_004241 | 330 | L → P in LPL deficiency. | 1 | |
<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_004242 | 361 | A → T in LPL deficiency. 2 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
| 1 | |
<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_057943 | 365 | S → F in LPL deficiency; 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 <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
| 1 | |
<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_004243 | 392 | L → V in LPL deficiency; loss of activity. 1 Publication <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
| 1 | |
<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_077541 | 404 | M → R in LPL deficiency; decreased protein secretion; loss of lipoprotein lipase activity. 1 Publication <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
| 1 | |
<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_004244 | 423 – 424 | Missing in LPL deficiency; affects the protein folding. | 2 | |
<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_004245 | 437 | E → K in LPL deficiency. 1 Publication <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
| 1 | |
<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_004246 | 437 | E → V in LPL deficiency. 1 Publication <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
| 1 | |
<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_057944 | 445 | C → Y in LPL deficiency; 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. 1 Publication <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
| 1 | |
<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_057945 | 448 | E → K in LPL deficiency; results in a moderate reduction in catalytic activity. 1 Publication <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
| 1 |
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘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: Lacks both triolein and tributyrin esterase activities. 1 Publication <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
| 1 | |
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘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 → T: Lacks both triolein and tributyrin esterase activities. 1 Publication <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
| 1 | |
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘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 | 268 | H → G: Lacks both triolein and tributyrin esterase activities. 1 Publication <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
| 1 | |
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘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 | 268 | H → Q: Lacks both triolein and tributyrin esterase activities. 1 Publication <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
| 1 |
<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>Keywords - Diseasei
Disease mutation, 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. |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 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. 70470. Hyperlipoproteinemia type 5. |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA232. |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL2060. |
Drug and drug target database More...DrugBanki | DB09278. Activated charcoal. DB06439. Tyloxapol. |
Polymorphism and mutation 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 <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
| 27 | |
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<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 <span class="caps">PTM</span> / 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 | ||
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / 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...) asparagine1 Publication <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
| 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 | Nitrated tyrosineBy 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 | 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 | 191 | Nitrated tyrosineBy 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 | 1 | |
<p>This subsection of the <span class="caps">PTM</span> / 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 | 243 ↔ 266 | 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 | ||
<p>This subsection of the <span class="caps">PTM</span> / 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 | 291 ↔ 310 | 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 | ||
<p>This subsection of the <span class="caps">PTM</span> / 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 | 302 ↔ 305 | 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 | ||
<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 | 343 | Nitrated tyrosineBy 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 | 1 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / 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 | 386 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
<p>This subsection of the <span class="caps">PTM</span> / 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 | 445 ↔ 465 | 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 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span>/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
<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
<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>Keywords - PTMi
Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein, NitrationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | 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. |
PTM databases
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
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000175445. |
CleanEx database of gene expression profiles More...CleanExi | HS_LPL. |
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 | HPA048749. |
<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_section">‘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_section">‘Function’</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<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
2 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.12"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.15"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.
<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
- 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
- receptor 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
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 110205. 19 interactors. |
Protein interaction database and analysis system More...IntActi | P06858. 15 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. |
<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
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P06858. |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P06858. |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | 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_and_domains_section">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 <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 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 | 346 – 441 | Heparin-bindingBy similarityAdd BLAST | 96 |
<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
<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>Keywords - Domaini
SignalPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG410IJUA. Eukaryota. ENOG4111GMM. LUCA. |
Ensembl GeneTree More...GeneTreei | ENSGT00760000119069. |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000038553. |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG002259. |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P06858. |
KEGG Orthology (KO) More...KOi | K01059. |
Identification of Orthologs from Complete Genome Data More...OMAi | HYQVKIH. |
Database of Orthologous Groups More...OrthoDBi | EOG091G052B. |
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/vitellogenin. 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.
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
Natural variant
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_011948 | 36 | D → N in LPL deficiency; has approximately 80% of the specific activity of wild-type enzyme. 4 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
| 1 | |
<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 LPL deficiency; produces an inactive protein which is not secreted into the media. 2 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
| 1 | |
<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_049819 | 71 | H → Q. Corresponds to variant dbSNP:rs11542065Ensembl. | 1 | |
<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_057915 | 96 | V → L in LPL deficiency; gives rise to a 80% decrease in specific catalytic activity. 1 Publication <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
| 1 | |
<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_057916 | 98 | A → T in LPL deficiency; 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 <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
| 1 | |
<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_004211 | 102 | R → S in LPL deficiency. 1 Publication <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
| 1 | |
<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_004212 | 113 | W → G in LPL deficiency. | 1 | |
<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_004213 | 113 | W → R in LPL deficiency. 2 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
| 1 | |
<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_057917 | 128 | T → A in LPL deficiency. 2 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
| 1 | |
<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_057918 | 132 | G → R in LPL deficiency; synthesized as a catalytically inactive form. 2 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
| 1 | |
<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_004214 | 163 | H → R in LPL deficiency. 1 Publication <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
| 1 | |
<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_004215 | 169 | G → E in LPL deficiency; loss of activity. 1 Publication <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
| 1 | |
<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_004216 | 181 | G → S in LPL deficiency. 1 Publication <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
| 1 | |
<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_057919 | 181 | G → V in LPL deficiency; synthesized as a catalytically inactive form. 2 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
| 1 | |
<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_004217 | 183 | D → G in LPL deficiency; lacks both triolein and tributyrin esterase activities. 3 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
| 1 | |
<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_057920 | 183 | D → H in LPL deficiency. 1 Publication <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
| 1 | |
<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_004218 | 183 | D → N in LPL deficiency; lacks both triolein and tributyrin esterase activities. 2 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
| 1 | |
<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_004219 | 184 | P → R in LPL deficiency; Nijmegen; loss of activity. 1 Publication <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
| 1 | |
<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_004220 | 185 | A → T in LPL deficiency; 3.2% of activity. Corresponds to variant dbSNP:rs748349562Ensembl. | 1 | |
<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_057921 | 186 | G → E in LPL deficiency. 1 Publication <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
| 1 | |
<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_057922 | 190 | E → G in LPL deficiency. 1 Publication <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
| 1 | |
<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_004221 | 199 | S → C in LPL deficiency; mild hypertriglyceridemia; partial activity. 2 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
| 1 | |
<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_057923 | 201 | D → V in LPL deficiency. 1 Publication <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
| 1 | |
<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_004222 | 203 | A → T in LPL deficiency; Bethesda; loss of activity and abnormal heparin binding. 1 Publication <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
| 1 | |
<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_004223 | 207 | D → E in LPL deficiency. 1 Publication <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
| 1 | |
<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_057924 | 208 | V → I in LPL deficiency; 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 <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
| 1 | |
<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_057925 | 210 | H → D in LPL deficiency; complete loss of enzyme activity. 1 Publication <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
| 1 | |
<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_004224 | 210 | H → Q in LPL deficiency; loss of activity. | 1 | |
<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_004225 | 215 | G → E in LPL deficiency; loss of activity. 12 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
| 1 | |
<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_057926 | 215 | G → R in LPL deficiency. 2 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
| 1 | |
<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_004226 | 220 | S → R in LPL deficiency; 2.0% of activity. Corresponds to variant dbSNP:rs757546424Ensembl. | 1 | |
<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_004227 | 221 | I → T in LPL deficiency; loss of activity. 5 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
| 1 | |
<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_004228 | 222 | G → E in LPL deficiency. 1 Publication <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
| 1 | |
<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_057927 | 225 | K → R in LPL deficiency. 1 Publication <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
| 1 | |
<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_057928 | 227 | V → A in LPL deficiency. 1 Publication <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
| 1 | |
<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_004229 | 231 | D → E in LPL deficiency; loss of activity. 3 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
| 1 | |
<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_004230 | 232 | I → S in LPL deficiency. 1 Publication <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
| 1 | |
<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_004231 | 234 | P → L in LPL deficiency; loss of activity. 2 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
| 1 | |
<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_004232 | 243 | C → S in LPL deficiency; loss of activity. 1 Publication <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
| 1 | |
<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_057929 | 252 | I → T in LPL deficiency. 1 Publication <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
| 1 | |
<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_057930 | 266 | C → W in LPL deficiency. 1 Publication <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
| 1 | |
<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_057931 | 270 | R → C in LPL deficiency. 4 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
| 1 | |
<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_004233 | 270 | R → H in LPL deficiency; loss of activity. 6 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
| 1 | |
<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_004234 | 271 | S → T in LPL deficiency. 1 Publication <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
| 1 | |
<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_004235 | 277 | D → N in LPL deficiency; 5% of full activity. 5 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
| 1 | |
<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_004236 | 278 | S → C in LPL deficiency. | 1 | |
<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_057932 | 279 | L → R in LPL deficiency; decreases the specific activity of the enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 2 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
| 1 | |
<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_057933 | 279 | L → V in LPL deficiency; decreases the specific activity of the enzyme; the total LPL mass is reduced compared to that of the wild-type construct. 1 Publication <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
| 1 | |
<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_004237 | 286 | S → G in LPL deficiency. 1 Publication <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
| 1 | |
<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_004238 | 286 | S → R in LPL deficiency. 1 Publication <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
| 1 | |
<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_011949 | 288 | A → T in LPL deficiency; the LPL mass level is approximately 67% of the normal; the activity is 32% of the nornal. 3 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
| 1 | |
<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_057934 | 289 | Y → H in LPL deficiency; no enzyme activity. 1 Publication <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
| 1 | |
<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_057935 | 297 | F → L in LPL deficiency 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 <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
| 1 | |
<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_057936 | 303 | L → F in LPL deficiency; 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 <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
| 1 | |
<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_057937 | 305 | C → R in LPL deficiency. 1 Publication <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
| 1 | |
<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_057938 | 310 | C → Y in LPL deficiency; 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 <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
| 1 | |
<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_057939 | 313 | L → P in LPL deficiency. 1 Publication <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
| 1 | |
<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_004239 | 318 | N → S in LPL deficiency; loss of activity; frequent mutation. 8 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
| 1 | |
<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_057940 | 325 | S → R in LPL deficiency; 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 <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
| 1 | |
<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_057941 | 328 | M → R in LPL deficiency. 1 Publication <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
| 1 | |
<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_004240 | 328 | M → T in LPL deficiency. | 1 | |
<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_057942 | 330 | L → F in LPL deficiency. 1 Publication <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
| 1 | |
<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_004241 | 330 | L → P in LPL deficiency. | 1 | |
<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_004242 | 361 | A → T in LPL deficiency. 2 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
| 1 | |
<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_057943 | 365 | S → F in LPL deficiency; 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 <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
| 1 | |
<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_011950 | 370 | V → M1 Publication <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
| 1 | |
<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_011951 | 379 | T → A1 Publication <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
| 1 | |
<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_004243 | 392 | L → V in LPL deficiency; loss of activity. 1 Publication <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
| 1 | |
<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_077541 | 404 | M → R in LPL deficiency; decreased protein secretion; loss of lipoprotein lipase activity. 1 Publication <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
| 1 | |
<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_004244 | 423 – 424 | Missing in LPL deficiency; affects the protein folding. | 2 | |
<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_011952 | 427 | A → T1 Publication <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
| 1 | |
<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_004245 | 437 | E → K in LPL deficiency. 1 Publication <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
| 1 | |
<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_004246 | 437 | E → V in LPL deficiency. 1 Publication <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
| 1 | |
<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_057944 | 445 | C → Y in LPL deficiency; 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. 1 Publication <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
| 1 | |
<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_057945 | 448 | E → K in LPL deficiency; results in a moderate reduction in catalytic activity. 1 Publication <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
| 1 |
Sequence databases
Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | M15856 mRNA. Translation: AAB59536.1. X14390 mRNA. Translation: CAA32564.1. X54516 mRNA. Translation: CAA38372.1. M76722 Genomic DNA. Translation: AAA59528.1. S76076 Genomic DNA. Translation: AAB21000.1. S76077 Genomic DNA. Translation: AAB20999.1. BT006726 mRNA. Translation: AAP35372.1. AK312311 mRNA. Translation: BAG35236.1. CH471080 Genomic DNA. Translation: EAW63764.1. BC011353 mRNA. Translation: AAH11353.1. X68111 Genomic DNA. Translation: CAA48230.1. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS6012.1. |
Protein sequence database of the Protein Information Resource More...PIRi | A26082. LIHUL. |
NCBI Reference Sequences More...RefSeqi | NP_000228.1. NM_000237.2. |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.180878. |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000311322; ENSP00000309757; ENSG00000175445. |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 4023. |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:4023. |
UCSC genome browser More...UCSCi | uc003wzk.5. human. |
<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>Keywords - Coding sequence diversityi
Polymorphism<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
Protein | Similar proteins | Organisms | Length | Cluster ID | Cluster name | Size | |
---|---|---|---|---|---|---|---|
P06858 | A0A1B1RVA9 E5RHN7 Q4JIZ7 E5RJI0 Q71UV2 O77644 E7EW14 | Homo sapiens (Human) Pan troglodytes (Chimpanzee) | 475 | UniRef100_P06858 | Cluster: Lipoprotein lipase | 8 |
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
SHMPD The Singapore human mutation and polymorphism database |
Wikipedia Lipoprotein lipase entry |
Sequence databases
Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | M15856 mRNA. Translation: AAB59536.1. X14390 mRNA. Translation: CAA32564.1. X54516 mRNA. Translation: CAA38372.1. M76722 Genomic DNA. Translation: AAA59528.1. S76076 Genomic DNA. Translation: AAB21000.1. S76077 Genomic DNA. Translation: AAB20999.1. BT006726 mRNA. Translation: AAP35372.1. AK312311 mRNA. Translation: BAG35236.1. CH471080 Genomic DNA. Translation: EAW63764.1. BC011353 mRNA. Translation: AAH11353.1. X68111 Genomic DNA. Translation: CAA48230.1. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS6012.1. |
Protein sequence database of the Protein Information Resource More...PIRi | A26082. LIHUL. |
NCBI Reference Sequences More...RefSeqi | NP_000228.1. NM_000237.2. |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.180878. |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P06858. |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P06858. |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 110205. 19 interactors. |
Protein interaction database and analysis system More...IntActi | P06858. 15 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. |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL2060. |
Drug and drug target database More...DrugBanki | DB09278. Activated charcoal. DB06439. Tyloxapol. |
SwissLipids knowledge resource for lipid biology More...SwissLipidsi | SLP:000000568. |
Protein family/group databases
ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins More...ESTHERi | human-LPL. Lipoprotein_Lipase. |
PTM databases
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. |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | LPL. |
Domain mapping of disease mutations (DMDM) More...DMDMi | 126314. |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | 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. |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 4023. |
Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000311322; ENSP00000309757; ENSG00000175445. |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 4023. |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:4023. |
UCSC genome browser More...UCSCi | uc003wzk.5. human. |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 4023. |
DisGeNET More...DisGeNETi | 4023. |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000175445.14. |
GeneCards: human genes, protein and diseases More...GeneCardsi | LPL. |
GeneReviews a resource of expert-authored, peer-reviewed disease descriptions. More...GeneReviewsi | LPL. |
Human Gene Nomenclature Database More...HGNCi | HGNC:6677. LPL. |
Human Protein Atlas More...HPAi | HPA048749. |
MalaCards human disease database More...MalaCardsi | LPL. |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 238600. phenotype. 609708. gene. |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P06858. |
Open Targets More...OpenTargetsi | ENSG00000175445. |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 309015. Familial lipoprotein lipase deficiency. 70470. Hyperlipoproteinemia type 5. |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA232. |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG410IJUA. Eukaryota. ENOG4111GMM. LUCA. |
Ensembl GeneTree More...GeneTreei | ENSGT00760000119069. |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000038553. |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG002259. |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P06858. |
KEGG Orthology (KO) More...KOi | K01059. |
Identification of Orthologs from Complete Genome Data More...OMAi | HYQVKIH. |
Database of Orthologous Groups More...OrthoDBi | EOG091G052B. |
Database for complete collections of gene phylogenies More...PhylomeDBi | P06858. |
TreeFam database of animal gene trees More...TreeFami | TF324997. |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.1.1.34. 2681. |
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. |
SIGNOR Signaling Network Open Resource More...SIGNORi | P06858. |
Miscellaneous databases
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | Lipoprotein_lipase. |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 4023. |
Protein Ontology More...PROi | PR:P06858. |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000175445. |
CleanEx database of gene expression profiles More...CleanExi | HS_LPL. |
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. |
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/vitellogenin. 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. |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | LIPL_HUMAN | |
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P06858Primary (citable) accession number: P06858 Secondary accession number(s): B2R5T9 , Q16282, Q16283, Q96FC4 | |
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 1, 1988 |
Last sequence update: | January 1, 1988 | |
Last modified: | March 28, 2018 | |
This is version 218 of the entry and version 1 of the sequence. See complete history. | ||
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. |