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Protein

Lipoprotein lipase

Gene

LPL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

The primary function of this lipase is the hydrolysis of triglycerides of circulating chylomicrons and very low density lipoproteins (VLDL) (PubMed:27578112). Binding to heparin sulfate proteogylcans at the cell surface is vital to the function. The apolipoprotein, APOC2, acts as a coactivator of LPL activity in the presence of lipids on the luminal surface of vascular endothelium (By similarity).By similarity2 Publications

<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. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei159Nucleophile1
Active sitei183Charge relay system1
Active sitei268Charge relay system1

<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
  • heparin binding Source: UniProtKB
  • lipoprotein lipase activity Source: UniProtKB
  • phospholipase activity Source: BHF-UCL
  • signaling receptor binding Source: BHF-UCL
  • triglyceride binding Source: Ensembl
  • triglyceride lipase activity Source: BHF-UCL

GO - Biological processi

<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 functionHeparin-binding, Hydrolase
Biological processLipid degradation, Lipid metabolism

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
3.1.1.34 2681

Reactome - a knowledgebase of biological pathways and processes

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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

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SIGNORi
P06858

Protein family/group databases

ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins

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ESTHERi
human-LPL Lipoprotein_Lipase

Chemistry databases

SwissLipids knowledge resource for lipid biology

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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)
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>OrganismiHomo 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 NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 8

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000175445.14

Human Gene Nomenclature Database

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HGNCi
HGNC:6677 LPL

Online Mendelian Inheritance in Man (OMIM)

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MIMi
609708 gene

neXtProt; the human protein knowledge platform

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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 Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Lipoprotein lipase deficiency (LPL deficiency)55 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionRecessive disorder usually manifesting in childhood. On a normal diet, patients often present with abdominal pain, hepatosplenomegaly, lipemia retinalis, eruptive xanthomata, and massive hypertriglyceridemia, sometimes complicated with acute pancreatitis.
See also OMIM:238600
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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_01194836D → N in LPL deficiency; has approximately 80% of the specific activity of wild-type enzyme. 4 PublicationsCorresponds to variant dbSNP:rs1801177EnsemblClinVar.1
Natural variantiVAR_05791470N → S in LPL deficiency; produces an inactive protein which is not secreted into the media. 2 Publications1
Natural variantiVAR_05791596V → L in LPL deficiency; gives rise to a 80% decrease in specific catalytic activity. 1 PublicationCorresponds to variant dbSNP:rs373088068Ensembl.1
Natural variantiVAR_05791698A → 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 PublicationCorresponds to variant dbSNP:rs145657341Ensembl.1
Natural variantiVAR_004211102R → S in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs118204073EnsemblClinVar.1
Natural variantiVAR_004212113W → G in LPL deficiency. 1
Natural variantiVAR_004213113W → R in LPL deficiency. 2 PublicationsCorresponds to variant dbSNP:rs118204069EnsemblClinVar.1
Natural variantiVAR_057917128T → A in LPL deficiency. 2 Publications1
Natural variantiVAR_057918132G → R in LPL deficiency; synthesized as a catalytically inactive form. 2 Publications1
Natural variantiVAR_004214163H → R in LPL deficiency. 1 Publication1
Natural variantiVAR_004215169G → E in LPL deficiency; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs118204063EnsemblClinVar.1
Natural variantiVAR_004216181G → S in LPL deficiency. 1 Publication1
Natural variantiVAR_057919181G → V in LPL deficiency; synthesized as a catalytically inactive form. 2 Publications1
Natural variantiVAR_004217183D → G in LPL deficiency; lacks both triolein and tributyrin esterase activities. 3 PublicationsCorresponds to variant dbSNP:rs118204064EnsemblClinVar.1
Natural variantiVAR_057920183D → H in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs781614031Ensembl.1
Natural variantiVAR_004218183D → N in LPL deficiency; lacks both triolein and tributyrin esterase activities. 2 PublicationsCorresponds to variant dbSNP:rs781614031Ensembl.1
Natural variantiVAR_004219184P → R in LPL deficiency; Nijmegen; loss of activity. 1 Publication1
Natural variantiVAR_004220185A → T in LPL deficiency; 3.2% of activity. Corresponds to variant dbSNP:rs748349562Ensembl.1
Natural variantiVAR_057921186G → E in LPL deficiency. 1 Publication1
Natural variantiVAR_057922190E → G in LPL deficiency. 1 Publication1
Natural variantiVAR_004221199S → C in LPL deficiency; mild hypertriglyceridemia; partial activity. 2 PublicationsCorresponds to variant dbSNP:rs118204072EnsemblClinVar.1
Natural variantiVAR_057923201D → V in LPL deficiency. 1 Publication1
Natural variantiVAR_004222203A → T in LPL deficiency; Bethesda; loss of activity and abnormal heparin binding. 1 PublicationCorresponds to variant dbSNP:rs118204056EnsemblClinVar.1
Natural variantiVAR_004223207D → E in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs118204076EnsemblClinVar.1
Natural variantiVAR_057924208V → 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 PublicationCorresponds to variant dbSNP:rs568397156Ensembl.1
Natural variantiVAR_057925210H → D in LPL deficiency; complete loss of enzyme activity. 1 Publication1
Natural variantiVAR_004224210H → Q in LPL deficiency; loss of activity. 1
Natural variantiVAR_004225215G → E in LPL deficiency; loss of activity. 12 PublicationsCorresponds to variant dbSNP:rs118204057EnsemblClinVar.1
Natural variantiVAR_057926215G → R in LPL deficiency. 2 Publications1
Natural variantiVAR_004226220S → R in LPL deficiency; 2.0% of activity. Corresponds to variant dbSNP:rs757546424Ensembl.1
Natural variantiVAR_004227221I → T in LPL deficiency; loss of activity. 5 PublicationsCorresponds to variant dbSNP:rs118204061EnsemblClinVar.1
Natural variantiVAR_004228222G → E in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs118204075EnsemblClinVar.1
Natural variantiVAR_057927225K → R in LPL deficiency. 1 Publication1
Natural variantiVAR_057928227V → A in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs528243561Ensembl.1
Natural variantiVAR_004229231D → E in LPL deficiency; loss of activity. 3 PublicationsCorresponds to variant dbSNP:rs118204067EnsemblClinVar.1
Natural variantiVAR_004230232I → S in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs770601263Ensembl.1
Natural variantiVAR_004231234P → L in LPL deficiency; loss of activity. 2 PublicationsCorresponds to variant dbSNP:rs118204060EnsemblClinVar.1
Natural variantiVAR_004232243C → S in LPL deficiency; loss of activity. 1 Publication1
Natural variantiVAR_057929252I → T in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs118204080EnsemblClinVar.1
Natural variantiVAR_057930266C → W in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs118204082EnsemblClinVar.1
Natural variantiVAR_057931270R → C in LPL deficiency. 4 PublicationsCorresponds to variant dbSNP:rs118204077EnsemblClinVar.1
Natural variantiVAR_004233270R → H in LPL deficiency; loss of activity. 6 PublicationsCorresponds to variant dbSNP:rs118204062EnsemblClinVar.1
Natural variantiVAR_004234271S → T in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs118204059EnsemblClinVar.1
Natural variantiVAR_004235277D → N in LPL deficiency; 5% of full activity. 5 PublicationsCorresponds to variant dbSNP:rs118204068EnsemblClinVar.1
Natural variantiVAR_004236278S → C in LPL deficiency. 1
Natural variantiVAR_057932279L → 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 PublicationsCorresponds to variant dbSNP:rs35414700Ensembl.1
Natural variantiVAR_057933279L → 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 PublicationCorresponds to variant dbSNP:rs371282890Ensembl.1
Natural variantiVAR_004237286S → G in LPL deficiency. 1 Publication1
Natural variantiVAR_004238286S → R in LPL deficiency. 1 Publication1
Natural variantiVAR_011949288A → T in LPL deficiency; the LPL mass level is approximately 67% of the normal; the activity is 32% of the nornal. 3 PublicationsCorresponds to variant dbSNP:rs1800011Ensembl.1
Natural variantiVAR_057934289Y → H in LPL deficiency; no enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs1161884343Ensembl.1
Natural variantiVAR_057935297F → 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 Publications1
Natural variantiVAR_057936303L → 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 Publication1
Natural variantiVAR_057937305C → R in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs773235712Ensembl.1
Natural variantiVAR_057938310C → 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 PublicationCorresponds to variant dbSNP:rs1409123950Ensembl.1
Natural variantiVAR_057939313L → P in LPL deficiency. 1 Publication1
Natural variantiVAR_004239318N → S in LPL deficiency; loss of activity; frequent mutation. 8 PublicationsCorresponds to variant dbSNP:rs268EnsemblClinVar.1
Natural variantiVAR_057940325S → 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 PublicationCorresponds to variant dbSNP:rs761265900Ensembl.1
Natural variantiVAR_057941328M → R in LPL deficiency. 1 Publication1
Natural variantiVAR_004240328M → T in LPL deficiency. Corresponds to variant dbSNP:rs1181582051Ensembl.1
Natural variantiVAR_057942330L → F in LPL deficiency. 1 Publication1
Natural variantiVAR_004241330L → P in LPL deficiency. 1
Natural variantiVAR_004242361A → T in LPL deficiency. 2 PublicationsCorresponds to variant dbSNP:rs118204071EnsemblClinVar.1
Natural variantiVAR_057943365S → 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 PublicationCorresponds to variant dbSNP:rs546542623Ensembl.1
Natural variantiVAR_004243392L → V in LPL deficiency; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs118204078EnsemblClinVar.1
Natural variantiVAR_077541404M → R in LPL deficiency; decreased protein secretion; loss of lipoprotein lipase activity. 1 Publication1
Natural variantiVAR_004244423 – 424Missing in LPL deficiency; affects the protein folding. 2
Natural variantiVAR_004245437E → K in LPL deficiency. 1 Publication1
Natural variantiVAR_004246437E → V in LPL deficiency. 1 Publication1
Natural variantiVAR_057944445C → 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 PublicationCorresponds to variant dbSNP:rs118204079EnsemblClinVar.1
Natural variantiVAR_057945448E → K in LPL deficiency; results in a moderate reduction in catalytic activity. 1 PublicationCorresponds to variant dbSNP:rs149089920Ensembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Mutagenesisi159S → G: Lacks both triolein and tributyrin esterase activities. 1 Publication1
Mutagenesisi159S → T: Lacks both triolein and tributyrin esterase activities. 1 Publication1
Mutagenesisi268H → G: Lacks both triolein and tributyrin esterase activities. 1 Publication1
Mutagenesisi268H → Q: Lacks both triolein and tributyrin esterase activities. 1 Publication1

Keywords - Diseasei

Disease mutation, Hyperlipidemia

Organism-specific databases

DisGeNET

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DisGeNETi
4023

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
LPL

MalaCards human disease database

More...
MalaCardsi
LPL
MIMi238600 phenotype

Open Targets

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OpenTargetsi
ENSG00000175445

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
309015 Familial lipoprotein lipase deficiency
70470 Hyperlipoproteinemia type 5

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA232

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2060

Drug and drug target database

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DrugBanki
DB09278 Activated charcoal
DB06439 Tyloxapol

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
LPL

Domain mapping of disease mutations (DMDM)

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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 keyPosition(s)DescriptionActionsGraphical viewLength
<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 peptidei1 – 271 PublicationAdd BLAST27
<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_000001777528 – 475Lipoprotein lipaseAdd BLAST448

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi54 ↔ 67PROSITE-ProRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi70N-linked (GlcNAc...) asparagine1 Publication1
<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 residuei121Nitrated tyrosineBy similarity1
Modified residuei191Nitrated tyrosineBy similarity1
Disulfide bondi243 ↔ 266PROSITE-ProRule annotation
Disulfide bondi291 ↔ 310PROSITE-ProRule annotation
Disulfide bondi302 ↔ 305PROSITE-ProRule annotation
Modified residuei343Nitrated tyrosineBy similarity1
Glycosylationi386N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi445 ↔ 465PROSITE-ProRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein, Nitration

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P06858

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P06858

MaxQB - The MaxQuant DataBase

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MaxQBi
P06858

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P06858

PeptideAtlas

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PeptideAtlasi
P06858

PRoteomics IDEntifications database

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PRIDEi
P06858

ProteomicsDB human proteome resource

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ProteomicsDBi
51936

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P06858

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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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

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Bgeei
ENSG00000175445 Expressed in 223 organ(s), highest expression level in adipose tissue

CleanEx database of gene expression profiles

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CleanExi
HS_LPL

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P06858 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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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

Homodimer (By similarity). Interacts with APOC2; the interaction activates LPL activity in the presence of lipids (By similarity). Interacts with GPIHBP1 (PubMed:17997385). Interacts with SEL1L and LMF1 (PubMed:25066055).By similarity2 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
110205, 19 interactors

Protein interaction database and analysis system

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IntActi
P06858, 15 interactors

Molecular INTeraction database

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MINTi
P06858

STRING: functional protein association networks

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STRINGi
9606.ENSP00000309757

Chemistry databases

BindingDB database of measured binding affinities

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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

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ProteinModelPortali
P06858

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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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 keyPosition(s)DescriptionActionsGraphical viewLength
<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>Domaini341 – 464PLATPROSITE-ProRule annotationAdd BLAST124

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Regioni346 – 441Heparin-bindingBy similarityAdd BLAST96

<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

Belongs to the AB hydrolase superfamily. Lipase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410IJUA Eukaryota
ENOG4111GMM LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000157178

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000038553

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG002259

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P06858

KEGG Orthology (KO)

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KOi
K01059

Identification of Orthologs from Complete Genome Data

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OMAi
FAIEKIR

Database of Orthologous Groups

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OrthoDBi
534956at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P06858

TreeFam database of animal gene trees

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TreeFami
TF324997

Family and domain databases

Conserved Domains Database

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CDDi
cd00707 Pancreat_lipase_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.40.50.1820, 1 hit

Integrated resource of protein families, domains and functional sites

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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

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PANTHERi
PTHR11610 PTHR11610, 1 hit
PTHR11610:SF3 PTHR11610:SF3, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00151 Lipase, 1 hit
PF01477 PLAT, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF000865 Lipoprotein_lipase_LIPH, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00822 LIPOLIPASE
PR00821 TAGLIPASE

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00308 LH2, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF49723 SSF49723, 1 hit
SSF53474 SSF53474, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR03230 lipo_lipase, 1 hit

PROSITE; a protein domain and family database

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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>Sequence (1+)i

<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.

This entry has 1 described isoform and 5 potential isoforms that are computationally mapped.Show allAlign All

P06858-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MESKALLVLT LAVWLQSLTA SRGGVAAADQ RRDFIDIESK FALRTPEDTA
60 70 80 90 100
EDTCHLIPGV AESVATCHFN HSSKTFMVIH GWTVTGMYES WVPKLVAALY
110 120 130 140 150
KREPDSNVIV VDWLSRAQEH YPVSAGYTKL VGQDVARFIN WMEEEFNYPL
160 170 180 190 200
DNVHLLGYSL GAHAAGIAGS LTNKKVNRIT GLDPAGPNFE YAEAPSRLSP
210 220 230 240 250
DDADFVDVLH TFTRGSPGRS IGIQKPVGHV DIYPNGGTFQ PGCNIGEAIR
260 270 280 290 300
VIAERGLGDV DQLVKCSHER SIHLFIDSLL NEENPSKAYR CSSKEAFEKG
310 320 330 340 350
LCLSCRKNRC NNLGYEINKV RAKRSSKMYL KTRSQMPYKV FHYQVKIHFS
360 370 380 390 400
GTESETHTNQ AFEISLYGTV AESENIPFTL PEVSTNKTYS FLIYTEVDIG
410 420 430 440 450
ELLMLKLKWK SDSYFSWSDW WSSPGFAIQK IRVKAGETQK KVIFCSREKV
460 470
SHLQKGKAPA VFVKCHDKSL NKKSG
Length:475
Mass (Da):53,162
Last modified:January 1, 1988 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iFBD00FCD334FB8AA
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E5RHN7E5RHN7_HUMAN
Lipoprotein lipase
LPL
105Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E5RJI0E5RJI0_HUMAN
Lipoprotein lipase
LPL
129Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E7EW14E7EW14_HUMAN
Lipoprotein lipase
LPL
115Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E5RJZ4E5RJZ4_HUMAN
Lipoprotein lipase
LPL
39Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A3B3IT60A0A3B3IT60_HUMAN
Lipoprotein lipase
LPL
38Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01194836D → N in LPL deficiency; has approximately 80% of the specific activity of wild-type enzyme. 4 PublicationsCorresponds to variant dbSNP:rs1801177EnsemblClinVar.1
Natural variantiVAR_05791470N → S in LPL deficiency; produces an inactive protein which is not secreted into the media. 2 Publications1
Natural variantiVAR_04981971H → Q. Corresponds to variant dbSNP:rs11542065EnsemblClinVar.1
Natural variantiVAR_05791596V → L in LPL deficiency; gives rise to a 80% decrease in specific catalytic activity. 1 PublicationCorresponds to variant dbSNP:rs373088068Ensembl.1
Natural variantiVAR_05791698A → 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 PublicationCorresponds to variant dbSNP:rs145657341Ensembl.1
Natural variantiVAR_004211102R → S in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs118204073EnsemblClinVar.1
Natural variantiVAR_004212113W → G in LPL deficiency. 1
Natural variantiVAR_004213113W → R in LPL deficiency. 2 PublicationsCorresponds to variant dbSNP:rs118204069EnsemblClinVar.1
Natural variantiVAR_057917128T → A in LPL deficiency. 2 Publications1
Natural variantiVAR_057918132G → R in LPL deficiency; synthesized as a catalytically inactive form. 2 Publications1
Natural variantiVAR_004214163H → R in LPL deficiency. 1 Publication1
Natural variantiVAR_004215169G → E in LPL deficiency; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs118204063EnsemblClinVar.1
Natural variantiVAR_004216181G → S in LPL deficiency. 1 Publication1
Natural variantiVAR_057919181G → V in LPL deficiency; synthesized as a catalytically inactive form. 2 Publications1
Natural variantiVAR_004217183D → G in LPL deficiency; lacks both triolein and tributyrin esterase activities. 3 PublicationsCorresponds to variant dbSNP:rs118204064EnsemblClinVar.1
Natural variantiVAR_057920183D → H in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs781614031Ensembl.1
Natural variantiVAR_004218183D → N in LPL deficiency; lacks both triolein and tributyrin esterase activities. 2 PublicationsCorresponds to variant dbSNP:rs781614031Ensembl.1
Natural variantiVAR_004219184P → R in LPL deficiency; Nijmegen; loss of activity. 1 Publication1
Natural variantiVAR_004220185A → T in LPL deficiency; 3.2% of activity. Corresponds to variant dbSNP:rs748349562Ensembl.1
Natural variantiVAR_057921186G → E in LPL deficiency. 1 Publication1
Natural variantiVAR_057922190E → G in LPL deficiency. 1 Publication1
Natural variantiVAR_004221199S → C in LPL deficiency; mild hypertriglyceridemia; partial activity. 2 PublicationsCorresponds to variant dbSNP:rs118204072EnsemblClinVar.1
Natural variantiVAR_057923201D → V in LPL deficiency. 1 Publication1
Natural variantiVAR_004222203A → T in LPL deficiency; Bethesda; loss of activity and abnormal heparin binding. 1 PublicationCorresponds to variant dbSNP:rs118204056EnsemblClinVar.1
Natural variantiVAR_004223207D → E in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs118204076EnsemblClinVar.1
Natural variantiVAR_057924208V → 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 PublicationCorresponds to variant dbSNP:rs568397156Ensembl.1
Natural variantiVAR_057925210H → D in LPL deficiency; complete loss of enzyme activity. 1 Publication1
Natural variantiVAR_004224210H → Q in LPL deficiency; loss of activity. 1
Natural variantiVAR_004225215G → E in LPL deficiency; loss of activity. 12 PublicationsCorresponds to variant dbSNP:rs118204057EnsemblClinVar.1
Natural variantiVAR_057926215G → R in LPL deficiency. 2 Publications1
Natural variantiVAR_004226220S → R in LPL deficiency; 2.0% of activity. Corresponds to variant dbSNP:rs757546424Ensembl.1
Natural variantiVAR_004227221I → T in LPL deficiency; loss of activity. 5 PublicationsCorresponds to variant dbSNP:rs118204061EnsemblClinVar.1
Natural variantiVAR_004228222G → E in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs118204075EnsemblClinVar.1
Natural variantiVAR_057927225K → R in LPL deficiency. 1 Publication1
Natural variantiVAR_057928227V → A in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs528243561Ensembl.1
Natural variantiVAR_004229231D → E in LPL deficiency; loss of activity. 3 PublicationsCorresponds to variant dbSNP:rs118204067EnsemblClinVar.1
Natural variantiVAR_004230232I → S in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs770601263Ensembl.1
Natural variantiVAR_004231234P → L in LPL deficiency; loss of activity. 2 PublicationsCorresponds to variant dbSNP:rs118204060EnsemblClinVar.1
Natural variantiVAR_004232243C → S in LPL deficiency; loss of activity. 1 Publication1
Natural variantiVAR_057929252I → T in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs118204080EnsemblClinVar.1
Natural variantiVAR_057930266C → W in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs118204082EnsemblClinVar.1
Natural variantiVAR_057931270R → C in LPL deficiency. 4 PublicationsCorresponds to variant dbSNP:rs118204077EnsemblClinVar.1
Natural variantiVAR_004233270R → H in LPL deficiency; loss of activity. 6 PublicationsCorresponds to variant dbSNP:rs118204062EnsemblClinVar.1
Natural variantiVAR_004234271S → T in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs118204059EnsemblClinVar.1
Natural variantiVAR_004235277D → N in LPL deficiency; 5% of full activity. 5 PublicationsCorresponds to variant dbSNP:rs118204068EnsemblClinVar.1
Natural variantiVAR_004236278S → C in LPL deficiency. 1
Natural variantiVAR_057932279L → 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 PublicationsCorresponds to variant dbSNP:rs35414700Ensembl.1
Natural variantiVAR_057933279L → 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 PublicationCorresponds to variant dbSNP:rs371282890Ensembl.1
Natural variantiVAR_004237286S → G in LPL deficiency. 1 Publication1
Natural variantiVAR_004238286S → R in LPL deficiency. 1 Publication1
Natural variantiVAR_011949288A → T in LPL deficiency; the LPL mass level is approximately 67% of the normal; the activity is 32% of the nornal. 3 PublicationsCorresponds to variant dbSNP:rs1800011Ensembl.1
Natural variantiVAR_057934289Y → H in LPL deficiency; no enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs1161884343Ensembl.1
Natural variantiVAR_057935297F → 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 Publications1
Natural variantiVAR_057936303L → 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 Publication1
Natural variantiVAR_057937305C → R in LPL deficiency. 1 PublicationCorresponds to variant dbSNP:rs773235712Ensembl.1
Natural variantiVAR_057938310C → 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 PublicationCorresponds to variant dbSNP:rs1409123950Ensembl.1
Natural variantiVAR_057939313L → P in LPL deficiency. 1 Publication1
Natural variantiVAR_004239318N → S in LPL deficiency; loss of activity; frequent mutation. 8 PublicationsCorresponds to variant dbSNP:rs268EnsemblClinVar.1
Natural variantiVAR_057940325S → 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 PublicationCorresponds to variant dbSNP:rs761265900Ensembl.1
Natural variantiVAR_057941328M → R in LPL deficiency. 1 Publication1
Natural variantiVAR_004240328M → T in LPL deficiency. Corresponds to variant dbSNP:rs1181582051Ensembl.1
Natural variantiVAR_057942330L → F in LPL deficiency. 1 Publication1
Natural variantiVAR_004241330L → P in LPL deficiency. 1
Natural variantiVAR_004242361A → T in LPL deficiency. 2 PublicationsCorresponds to variant dbSNP:rs118204071EnsemblClinVar.1
Natural variantiVAR_057943365S → 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 PublicationCorresponds to variant dbSNP:rs546542623Ensembl.1
Natural variantiVAR_011950370V → M1 PublicationCorresponds to variant dbSNP:rs298Ensembl.1
Natural variantiVAR_011951379T → A1 PublicationCorresponds to variant dbSNP:rs300EnsemblClinVar.1
Natural variantiVAR_004243392L → V in LPL deficiency; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs118204078EnsemblClinVar.1
Natural variantiVAR_077541404M → R in LPL deficiency; decreased protein secretion; loss of lipoprotein lipase activity. 1 Publication1
Natural variantiVAR_004244423 – 424Missing in LPL deficiency; affects the protein folding. 2
Natural variantiVAR_011952427A → T1 PublicationCorresponds to variant dbSNP:rs5934EnsemblClinVar.1
Natural variantiVAR_004245437E → K in LPL deficiency. 1 Publication1
Natural variantiVAR_004246437E → V in LPL deficiency. 1 Publication1
Natural variantiVAR_057944445C → 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 PublicationCorresponds to variant dbSNP:rs118204079EnsemblClinVar.1
Natural variantiVAR_057945448E → K in LPL deficiency; results in a moderate reduction in catalytic activity. 1 PublicationCorresponds to variant dbSNP:rs149089920Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links 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
ENST00000650287; ENSP00000497642; 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

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

<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:
EMBLi
GenBanki
DDBJi
Links 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
CCDSiCCDS6012.1
PIRiA26082 LIHUL
RefSeqiNP_000228.1, NM_000237.2
UniGeneiHs.180878

3D structure databases

ProteinModelPortaliP06858
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110205, 19 interactors
IntActiP06858, 15 interactors
MINTiP06858
STRINGi9606.ENSP00000309757

Chemistry databases

BindingDBiP06858
ChEMBLiCHEMBL2060
DrugBankiDB09278 Activated charcoal
DB06439 Tyloxapol
SwissLipidsiSLP:000000568

Protein family/group databases

ESTHERihuman-LPL Lipoprotein_Lipase

PTM databases

iPTMnetiP06858
PhosphoSitePlusiP06858

Polymorphism and mutation databases

BioMutaiLPL
DMDMi126314

Proteomic databases

EPDiP06858
jPOSTiP06858
MaxQBiP06858
PaxDbiP06858
PeptideAtlasiP06858
PRIDEiP06858
ProteomicsDBi51936

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
4023
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000311322; ENSP00000309757; ENSG00000175445
ENST00000650287; ENSP00000497642; ENSG00000175445
GeneIDi4023
KEGGihsa:4023
UCSCiuc003wzk.5 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4023
DisGeNETi4023
EuPathDBiHostDB:ENSG00000175445.14

GeneCards: human genes, protein and diseases

More...
GeneCardsi
LPL
GeneReviewsiLPL
HGNCiHGNC:6677 LPL
HPAiHPA048749
MalaCardsiLPL
MIMi238600 phenotype
609708 gene
neXtProtiNX_P06858
OpenTargetsiENSG00000175445
Orphaneti309015 Familial lipoprotein lipase deficiency
70470 Hyperlipoproteinemia type 5
PharmGKBiPA232

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IJUA Eukaryota
ENOG4111GMM LUCA
GeneTreeiENSGT00940000157178
HOGENOMiHOG000038553
HOVERGENiHBG002259
InParanoidiP06858
KOiK01059
OMAiFAIEKIR
OrthoDBi534956at2759
PhylomeDBiP06858
TreeFamiTF324997

Enzyme and pathway databases

BRENDAi3.1.1.34 2681
ReactomeiR-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
SIGNORiP06858

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

BgeeiENSG00000175445 Expressed in 223 organ(s), highest expression level in adipose tissue
CleanExiHS_LPL
ExpressionAtlasiP06858 baseline and differential
GenevisibleiP06858 HS

Family and domain databases

CDDicd00707 Pancreat_lipase_like, 1 hit
Gene3Di3.40.50.1820, 1 hit
InterProiView 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
PANTHERiPTHR11610 PTHR11610, 1 hit
PTHR11610:SF3 PTHR11610:SF3, 1 hit
PfamiView protein in Pfam
PF00151 Lipase, 1 hit
PF01477 PLAT, 1 hit
PIRSFiPIRSF000865 Lipoprotein_lipase_LIPH, 1 hit
PRINTSiPR00822 LIPOLIPASE
PR00821 TAGLIPASE
SMARTiView protein in SMART
SM00308 LH2, 1 hit
SUPFAMiSSF49723 SSF49723, 1 hit
SSF53474 SSF53474, 1 hit
TIGRFAMsiTIGR03230 lipo_lipase, 1 hit
PROSITEiView protein in PROSITE
PS00120 LIPASE_SER, 1 hit
PS50095 PLAT, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<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 nameiLIPL_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>AccessioniPrimary (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 historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: January 16, 2019
This is version 227 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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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