Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P06858 (LIPL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 179. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lipoprotein lipase

Short name=LPL
EC=3.1.1.34
Gene names
Name:LPL
Synonyms:LIPD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length475 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The primary function of this lipase is the hydrolysis of triglycerides of circulating chylomicrons and very low density lipoproteins (VLDL). 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.

Catalytic activity

Triacylglycerol + H2O = diacylglycerol + a carboxylate. Ref.11

Subunit structure

Homodimer By similarity. Interacts with APOC2; the interaction activates LPL activity in the presence of lipids. Interacts with GPIHBP1. Ref.12

Subcellular location

Cell membrane By similarity; Lipid-anchorGPI-anchor By similarity. Secreted 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.

Post-translational modification

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

Involvement in disease

Lipoprotein lipase deficiency (LPL deficiency) [MIM:238600]: Recessive 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Contains 1 PLAT domain.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentCell membrane
Chylomicron
Membrane
Secreted
VLDL
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Hyperlipidemia
   DomainSignal
   LigandHeparin-binding
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
GPI-anchor
Lipoprotein
Nitration
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processchylomicron remodeling

Inferred by curator PubMed 3973011. Source: BHF-UCL

fatty acid biosynthetic process

Inferred from direct assay PubMed 182536. Source: BHF-UCL

lipoprotein metabolic process

Traceable author statement. Source: Reactome

phospholipid metabolic process

Inferred from sequence or structural similarity PubMed 10727238. Source: BHF-UCL

phototransduction, visible light

Traceable author statement. Source: Reactome

positive regulation of cholesterol storage

Inferred from mutant phenotype PubMed 12573449. Source: BHF-UCL

positive regulation of macrophage derived foam cell differentiation

Inferred by curator PubMed 12573449. Source: BHF-UCL

positive regulation of sequestering of triglyceride

Inferred from mutant phenotype PubMed 12573449. Source: BHF-UCL

response to cold

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

retinoid metabolic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

triglyceride biosynthetic process

Inferred from electronic annotation. Source: Ensembl

triglyceride catabolic process

Inferred from direct assay PubMed 182536PubMed 3973011. Source: BHF-UCL

triglyceride homeostasis

Inferred from genetic interaction PubMed 17018885. Source: BHF-UCL

triglyceride metabolic process

Inferred from sequence or structural similarity PubMed 10727238. Source: BHF-UCL

very-low-density lipoprotein particle remodeling

Inferred from direct assay PubMed 3973011. Source: BHF-UCL

   Cellular_componentanchored component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

cell surface

Inferred from electronic annotation. Source: Ensembl

chylomicron

Inferred from electronic annotation. Source: UniProtKB-KW

extracellular matrix

Inferred from electronic annotation. Source: Ensembl

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 12573449. Source: BHF-UCL

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

very-low-density lipoprotein particle

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionapolipoprotein binding

Inferred from physical interaction PubMed 15178420. Source: BHF-UCL

heparin binding

Inferred from direct assay PubMed 12573449. Source: BHF-UCL

lipoprotein lipase activity

Inferred from direct assay PubMed 3973011. Source: BHF-UCL

phospholipase activity

Inferred from sequence or structural similarity PubMed 10727238. Source: BHF-UCL

receptor binding

Inferred from physical interaction PubMed 10085125. Source: BHF-UCL

triglyceride binding

Inferred from electronic annotation. Source: Ensembl

triglyceride lipase activity

Inferred from direct assay PubMed 12573449PubMed 182536. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Ref.10
Chain28 – 475448Lipoprotein lipase
PRO_0000017775

Regions

Domain341 – 464124PLAT
Region346 – 44196Heparin-binding By similarity

Sites

Active site1591Nucleophile
Active site1831Charge relay system
Active site2681Charge relay system

Amino acid modifications

Modified residue1211Nitrated tyrosine By similarity
Modified residue1911Nitrated tyrosine By similarity
Modified residue3431Nitrated tyrosine By similarity
Glycosylation701N-linked (GlcNAc...) Ref.13
Glycosylation3861N-linked (GlcNAc...) Potential
Disulfide bond54 ↔ 67 By similarity
Disulfide bond243 ↔ 266 By similarity
Disulfide bond291 ↔ 310 By similarity
Disulfide bond302 ↔ 305 By similarity
Disulfide bond445 ↔ 465 By similarity

Natural variations

Natural variant361D → N in LPL deficiency; has approximately 80% of the specific activity of wild-type enzyme. Ref.47 Ref.50 Ref.58 Ref.69
Corresponds to variant rs1801177 [ dbSNP | Ensembl ].
VAR_011948
Natural variant701N → S in LPL deficiency; produces an inactive protein which is not secreted into the media. Ref.40 Ref.72
VAR_057914
Natural variant711H → Q.
Corresponds to variant rs11542065 [ dbSNP | Ensembl ].
VAR_049819
Natural variant961V → L in LPL deficiency; gives rise to a 80% decrease in specific catalytic activity. Ref.42
VAR_057915
Natural variant981A → 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. Ref.67
VAR_057916
Natural variant1021R → S in LPL deficiency. Ref.37
VAR_004211
Natural variant1131W → G in LPL deficiency.
VAR_004212
Natural variant1131W → R in LPL deficiency. Ref.26 Ref.33
VAR_004213
Natural variant1281T → A in LPL deficiency. Ref.51 Ref.54
VAR_057917
Natural variant1321G → R in LPL deficiency; synthesized as a catalytically inactive form. Ref.63 Ref.72
VAR_057918
Natural variant1631H → R in LPL deficiency. Ref.33
VAR_004214
Natural variant1691G → E in LPL deficiency; loss of activity. Ref.22
VAR_004215
Natural variant1811G → S in LPL deficiency. Ref.38
VAR_004216
Natural variant1811G → V in LPL deficiency; synthesized as a catalytically inactive form. Ref.66 Ref.72
VAR_057919
Natural variant1831D → G in LPL deficiency; lacks both triolein and tributyrin esterase activities. Ref.21 Ref.29 Ref.30
VAR_004217
Natural variant1831D → H in LPL deficiency. Ref.54
VAR_057920
Natural variant1831D → N in LPL deficiency; lacks both triolein and tributyrin esterase activities. Ref.29 Ref.30
VAR_004218
Natural variant1841P → R in LPL deficiency; Nijmegen; loss of activity. Ref.27
VAR_004219
Natural variant1851A → T in LPL deficiency; 3.2% of activity.
VAR_004220
Natural variant1861G → E in LPL deficiency. Ref.73
VAR_057921
Natural variant1901E → G in LPL deficiency. Ref.49
VAR_057922
Natural variant1991S → C in LPL deficiency; mild hypertriglyceridemia; partial activity. Ref.36 Ref.43
VAR_004221
Natural variant2011D → V in LPL deficiency. Ref.70
VAR_057923
Natural variant2031A → T in LPL deficiency; Bethesda; loss of activity and abnormal heparin binding. Ref.19
VAR_004222
Natural variant2071D → E in LPL deficiency. Ref.35
VAR_004223
Natural variant2081V → 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. Ref.67
VAR_057924
Natural variant2101H → D in LPL deficiency; complete loss of enzyme activity. Ref.65
VAR_057925
Natural variant2101H → Q in LPL deficiency; loss of activity.
VAR_004224
Natural variant2151G → E in LPL deficiency; loss of activity. Ref.17 Ref.18 Ref.32 Ref.33 Ref.42 Ref.49 Ref.51 Ref.54 Ref.57 Ref.71 Ref.72 Ref.73
VAR_004225
Natural variant2151G → R in LPL deficiency. Ref.51 Ref.54
VAR_057926
Natural variant2201S → R in LPL deficiency; 2.0% of activity.
VAR_004226
Natural variant2211I → T in LPL deficiency; loss of activity. Ref.20 Ref.23 Ref.33 Ref.72 Ref.73
VAR_004227
Natural variant2221G → E in LPL deficiency. Ref.31
VAR_004228
Natural variant2251K → R in LPL deficiency. Ref.72
VAR_057927
Natural variant2271V → A in LPL deficiency. Ref.72
VAR_057928
Natural variant2311D → E in LPL deficiency; loss of activity. Ref.24 Ref.63 Ref.72
VAR_004229
Natural variant2321I → S in LPL deficiency. Ref.33
VAR_004230
Natural variant2341P → L in LPL deficiency; loss of activity. Ref.25 Ref.54
VAR_004231
Natural variant2431C → S in LPL deficiency; loss of activity. Ref.29
VAR_004232
Natural variant2521I → T in LPL deficiency. Ref.55
VAR_057929
Natural variant2661C → W in LPL deficiency. Ref.64
VAR_057930
Natural variant2701R → C in LPL deficiency. Ref.41 Ref.51 Ref.54 Ref.72
VAR_057931
Natural variant2701R → H in LPL deficiency; loss of activity. Ref.20 Ref.24 Ref.32 Ref.41 Ref.55 Ref.72
VAR_004233
Natural variant2711S → T in LPL deficiency. Ref.16
Corresponds to variant rs28934893 [ dbSNP | Ensembl ].
VAR_004234
Natural variant2771D → N in LPL deficiency; 5% of full activity. Ref.28 Ref.32 Ref.48 Ref.51 Ref.54
VAR_004235
Natural variant2781S → C in LPL deficiency.
VAR_004236
Natural variant2791L → 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. Ref.43 Ref.67
Corresponds to variant rs35414700 [ dbSNP | Ensembl ].
VAR_057932
Natural variant2791L → 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. Ref.67
VAR_057933
Natural variant2861S → G in LPL deficiency. Ref.57
VAR_004237
Natural variant2861S → R in LPL deficiency. Ref.52
VAR_004238
Natural variant2881A → T Associated with LPL deficiency; the LPL mass level is approximately 67% of the normal; the activity is 32% of the nornal. Ref.43 Ref.58 Ref.72
Corresponds to variant rs1800011 [ dbSNP | Ensembl ].
VAR_011949
Natural variant2891Y → H in LPL deficiency; no enzyme activity. Ref.50
VAR_057934
Natural variant2971F → 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. Ref.62 Ref.72
VAR_057935
Natural variant3031L → 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. Ref.68
VAR_057936
Natural variant3051C → R in LPL deficiency. Ref.72
VAR_057937
Natural variant3101C → 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. Ref.67
VAR_057938
Natural variant3131L → P in LPL deficiency. Ref.51
VAR_057939
Natural variant3181N → S in LPL deficiency; loss of activity; frequent mutation. Ref.5 Ref.8 Ref.43 Ref.45 Ref.47 Ref.58 Ref.59 Ref.69
Corresponds to variant rs268 [ dbSNP | Ensembl ].
VAR_004239
Natural variant3251S → 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. Ref.67
VAR_057940
Natural variant3281M → R in LPL deficiency. Ref.71
VAR_057941
Natural variant3281M → T in LPL deficiency.
VAR_004240
Natural variant3301L → F in LPL deficiency. Ref.72
VAR_057942
Natural variant3301L → P in LPL deficiency.
VAR_004241
Natural variant3611A → T in LPL deficiency. Ref.34 Ref.72
VAR_004242
Natural variant3651S → 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. Ref.67
VAR_057943
Natural variant3701V → M. Ref.59
Corresponds to variant rs298 [ dbSNP | Ensembl ].
VAR_011950
Natural variant3791T → A. Ref.59
Corresponds to variant rs300 [ dbSNP | Ensembl ].
VAR_011951
Natural variant3921L → V in LPL deficiency; loss of activity. Ref.39
VAR_004243
Natural variant423 – 4242Missing in LPL deficiency; affects the protein folding.
VAR_004244
Natural variant4271A → T. Ref.60
Corresponds to variant rs5934 [ dbSNP | Ensembl ].
VAR_011952
Natural variant4371E → K in LPL deficiency. Ref.48
VAR_004245
Natural variant4371E → V in LPL deficiency. Ref.44
VAR_004246
Natural variant4451C → 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. Ref.46
VAR_057944
Natural variant4481E → K in LPL deficiency; results in a moderate reduction in catalytic activity. Ref.56
VAR_057945

Experimental info

Mutagenesis1591S → G: Lacks both triolein and tributyrin esterase activities. Ref.30
Mutagenesis1591S → T: Lacks both triolein and tributyrin esterase activities. Ref.30
Mutagenesis2681H → G: Lacks both triolein and tributyrin esterase activities. Ref.30
Mutagenesis2681H → Q: Lacks both triolein and tributyrin esterase activities. Ref.30

Sequences

Sequence LengthMass (Da)Tools
P06858 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: FBD00FCD334FB8AA

FASTA47553,162
        10         20         30         40         50         60 
MESKALLVLT LAVWLQSLTA SRGGVAAADQ RRDFIDIESK FALRTPEDTA EDTCHLIPGV 

        70         80         90        100        110        120 
AESVATCHFN HSSKTFMVIH GWTVTGMYES WVPKLVAALY KREPDSNVIV VDWLSRAQEH 

       130        140        150        160        170        180 
YPVSAGYTKL VGQDVARFIN WMEEEFNYPL DNVHLLGYSL GAHAAGIAGS LTNKKVNRIT 

       190        200        210        220        230        240 
GLDPAGPNFE YAEAPSRLSP DDADFVDVLH TFTRGSPGRS IGIQKPVGHV DIYPNGGTFQ 

       250        260        270        280        290        300 
PGCNIGEAIR VIAERGLGDV DQLVKCSHER SIHLFIDSLL NEENPSKAYR CSSKEAFEKG 

       310        320        330        340        350        360 
LCLSCRKNRC NNLGYEINKV RAKRSSKMYL KTRSQMPYKV FHYQVKIHFS GTESETHTNQ 

       370        380        390        400        410        420 
AFEISLYGTV AESENIPFTL PEVSTNKTYS FLIYTEVDIG ELLMLKLKWK SDSYFSWSDW 

       430        440        450        460        470 
WSSPGFAIQK IRVKAGETQK KVIFCSREKV SHLQKGKAPA VFVKCHDKSL NKKSG 

« Hide

References

« Hide 'large scale' references
[1]"Human lipoprotein lipase complementary DNA sequence."
Wion K.L., Kirchgessner T.G., Lusis A.J., Schotz M.C., Lawn R.M.
Science 235:1638-1641(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Nucleotide sequence of human cDNA coding for a lipoprotein lipase (LPL) cloned from placental cDNA library."
Gotoda T., Senda M., Gamou T., Furuichi Y., Oka K.
Nucleic Acids Res. 17:2351-2352(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[3]"DNA sequence of lipoprotein lipase cDNA cloned from human monocytic leukemia THP-1 cells."
Takagi A., Ikeda Y., Yamamoto A.
Nucleic Acids Res. 18:6436-6436(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"The lipoprotein lipase-encoding human gene: sequence from intron-6 to intron-9 and presence in intron-7 of a 40-million-year-old Alu sequence."
Chuat J.-C., Raisonnier A., Etienne J., Galibert F.
Gene 110:257-261(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-318.
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Cerebellum.
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-318.
Tissue: Brain.
[9]"Characterization of the human lipoprotein lipase (LPL) promoter: evidence of two cis-regulatory regions, LP-alpha and LP-beta, of importance for the differentiation-linked induction of the LPL gene during adipogenesis."
Enerbaeck S., Ohlsson B.G., Samuelsson L., Bjursell G.
Mol. Cell. Biol. 12:4622-4633(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5.
[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.
Tissue: Milk.
[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.
[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.
[13]"Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry."
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.
Proteomics 8:3833-3847(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70.
Tissue: Milk.
[14]"Lipoprotein lipase. Molecular model based on the pancreatic lipase X-ray structure: consequences for heparin binding and catalysis."
van Tilbeurgh H., Roussel A., Lalouel J.-M., Cambillau C.
J. Biol. Chem. 269:4626-4633(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
[15]"Genetic variants affecting human lipoprotein and hepatic lipases."
Hayden M.R., Ma Y., Brunzell J., Henderson H.E.
Curr. Opin. Lipidol. 2:104-109(1991)
Cited for: REVIEW ON VARIANTS.
[16]"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.
[17]"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.
[18]"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.
[19]"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.
[20]"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.
[21]"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.
[22]"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.
[23]"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.
[24]"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.
[25]"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.
[26]"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.
[27]"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.
[28]"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.
[29]"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.
[30]"Human lipoprotein lipase. Analysis of the catalytic triad by site-directed mutagenesis of Ser-132, Asp-156, and His-241."
Emmerich J., Beg O.U., Peterson J., Previato L., Brunzell J.D., Brewer H.B. Jr., Santamarina-Fojo S.
J. Biol. Chem. 267:4161-4165(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS LPL DEFICIENCY ASN-183 AND GLY-183, MUTAGENESIS OF SER-159 AND HIS-268.
[31]"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.
[32]"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.
[33]"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.
[34]"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.
[35]"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.
[36]"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.
[37]"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.
[38]"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.
[39]"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.
[40]"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.
[41]"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.
[42]"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.
[43]"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.
[44]"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.
[45]"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.
[46]"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.
[47]"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.
[48]"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.
[49]"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.
[50]"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.
[51]"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.
[52]"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.
[53]"Familial lipoprotein lipase (LPL) deficiency: a catalogue of LPL gene mutations identified in 20 patients from the UK, Sweden, and Italy."
Mailly F., Palmen J., Muller D.P.R., Gibbs T., Lloyd J., Brunzell J., Durrington P., Mitropoulos K., Betteridge J., Watts G., Lithell H., Angelico F., Humphries S.E., Talmud P.J.
Hum. Mutat. 10:465-473(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS.
[54]"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.
[55]"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.
[56]"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.
[57]"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.
[58]"Common genetic variants of lipoprotein lipase and apolipoproteins AI-CIII that relate to coronary artery disease: a study in Chinese and European subjects."
Zhang Q., Liu Y., Liu B.W., Fan P., Cavanna J., Galton D.J.
Mol. Genet. Metab. 64:177-183(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LPL DEFICIENCY SER-318, VARIANTS ASN-36 AND THR-288.
[59]"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.
[60]"Characterization of single-nucleotide polymorphisms in coding regions of human genes."
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT THR-427.
[61]Erratum
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 23:373-373(1999)
[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.
[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.
[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.
[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.
[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.
[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.
[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.
[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.
[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.
[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.
[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.
[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.
+Additional computationally mapped references.

Web resources

GeneReviews
SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Lipoprotein lipase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRLIHUL. A26082.
RefSeqNP_000228.1. NM_000237.2.
UniGeneHs.180878.

3D structure databases

ProteinModelPortalP06858.
SMRP06858. Positions 4-466.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110205. 19 interactions.
IntActP06858. 11 interactions.
MINTMINT-1369348.
STRING9606.ENSP00000309757.

Chemistry

BindingDBP06858.
ChEMBLCHEMBL2060.
DrugBankDB00636. Clofibrate.
DB01241. Gemfibrozil.
DB01083. Orlistat.

PTM databases

PhosphoSiteP06858.

Polymorphism databases

DMDM126314.

Proteomic databases

PaxDbP06858.
PRIDEP06858.

Protocols and materials databases

DNASU4023.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000311322; ENSP00000309757; ENSG00000175445.
GeneID4023.
KEGGhsa:4023.
UCSCuc003wzk.4. human.

Organism-specific databases

CTD4023.
GeneCardsGC08P019759.
HGNCHGNC:6677. LPL.
HPAHPA048749.
MIM238600. phenotype.
609708. gene.
neXtProtNX_P06858.
Orphanet309015. Familial lipoprotein lipase deficiency.
70470. Hyperlipoproteinemia type 5.
PharmGKBPA232.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG40923.
HOGENOMHOG000038553.
HOVERGENHBG002259.
InParanoidP06858.
KOK01059.
OMAESVANCH.
PhylomeDBP06858.
TreeFamTF324997.

Enzyme and pathway databases

BRENDA3.1.1.34. 2681.
ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

ArrayExpressP06858.
BgeeP06858.
CleanExHS_LPL.
GenevestigatorP06858.

Family and domain databases

Gene3D2.60.60.20. 1 hit.
InterProIPR000734. Lipase.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002330. Lipo_Lipase.
IPR016272. Lipoprotein_lipase_LIPH.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERPTHR11610. PTHR11610. 1 hit.
PTHR11610:SF3. PTHR11610:SF3. 1 hit.
PfamPF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PIRSFPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSPR00822. LIPOLIPASE.
PR00821. TAGLIPASE.
SMARTSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMSSF49723. SSF49723. 1 hit.
TIGRFAMsTIGR03230. lipo_lipase. 1 hit.
PROSITEPS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiLipoprotein_lipase.
GenomeRNAi4023.
NextBio15776.
PROP06858.
SOURCESearch...

Entry information

Entry nameLIPL_HUMAN
AccessionPrimary (citable) accession number: P06858
Secondary accession number(s): B2R5T9 expand/collapse secondary AC list , Q16282, Q16283, Q96FC4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: April 16, 2014
This is version 179 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM