P06858 (LIPL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lipoprotein lipase
Short name=LPL
EC=3.1.1.34

Gene names

Name:	LPL
Synonyms:	LIPD

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	475 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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-anchor › GPI-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 process	Lipid degradation Lipid metabolism
Cellular component	Cell membrane Chylomicron Membrane Secreted VLDL
Coding sequence diversity	Polymorphism
Disease	Disease mutation Hyperlipidemia
Domain	Signal
Ligand	Heparin-binding
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein GPI-anchor Lipoprotein Nitration
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	chylomicron 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_component	anchored 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_function	apolipoprotein 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 27	27	Ref.10
	Chain	28 – 475	448	Lipoprotein lipase		PRO_0000017775
Regions
	Domain	341 – 464	124	PLAT
	Region	346 – 441	96	Heparin-binding By similarity
Sites
	Active site	159	1	Nucleophile
	Active site	183	1	Charge relay system
	Active site	268	1	Charge relay system
Amino acid modifications
	Modified residue	121	1	Nitrated tyrosine By similarity
	Modified residue	191	1	Nitrated tyrosine By similarity
	Modified residue	343	1	Nitrated tyrosine By similarity
	Glycosylation	70	1	N-linked (GlcNAc...) Ref.13
	Glycosylation	386	1	N-linked (GlcNAc...) Potential
	Disulfide bond	54 ↔ 67		By similarity
	Disulfide bond	243 ↔ 266		By similarity
	Disulfide bond	291 ↔ 310		By similarity
	Disulfide bond	302 ↔ 305		By similarity
	Disulfide bond	445 ↔ 465		By similarity
Natural variations
	Natural variant	36	1	D → 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 variant	70	1	N → S in LPL deficiency; produces an inactive protein which is not secreted into the media. Ref.40 Ref.72		VAR_057914
	Natural variant	71	1	H → Q. Corresponds to variant rs11542065 [ dbSNP | Ensembl ].		VAR_049819
	Natural variant	96	1	V → L in LPL deficiency; gives rise to a 80% decrease in specific catalytic activity. Ref.42		VAR_057915
	Natural variant	98	1	A → T in LPL deficiency; decreases the specific activity of the enzyme; reduces the secretion of the mutant protein significantly; the total LPL mass is reduced compared to that of the wild-type construct. Ref.67		VAR_057916
	Natural variant	102	1	R → S in LPL deficiency. Ref.37		VAR_004211
	Natural variant	113	1	W → G in LPL deficiency.		VAR_004212
	Natural variant	113	1	W → R in LPL deficiency. Ref.26 Ref.33		VAR_004213
	Natural variant	128	1	T → A in LPL deficiency. Ref.51 Ref.54		VAR_057917
	Natural variant	132	1	G → R in LPL deficiency; synthesized as a catalytically inactive form. Ref.63 Ref.72		VAR_057918
	Natural variant	163	1	H → R in LPL deficiency. Ref.33		VAR_004214
	Natural variant	169	1	G → E in LPL deficiency; loss of activity. Ref.22		VAR_004215
	Natural variant	181	1	G → S in LPL deficiency. Ref.38		VAR_004216
	Natural variant	181	1	G → V in LPL deficiency; synthesized as a catalytically inactive form. Ref.66 Ref.72		VAR_057919
	Natural variant	183	1	D → G in LPL deficiency; lacks both triolein and tributyrin esterase activities. Ref.21 Ref.29 Ref.30		VAR_004217
	Natural variant	183	1	D → H in LPL deficiency. Ref.54		VAR_057920
	Natural variant	183	1	D → N in LPL deficiency; lacks both triolein and tributyrin esterase activities. Ref.29 Ref.30		VAR_004218
	Natural variant	184	1	P → R in LPL deficiency; Nijmegen; loss of activity. Ref.27		VAR_004219
	Natural variant	185	1	A → T in LPL deficiency; 3.2% of activity.		VAR_004220
	Natural variant	186	1	G → E in LPL deficiency. Ref.73		VAR_057921
	Natural variant	190	1	E → G in LPL deficiency. Ref.49		VAR_057922
	Natural variant	199	1	S → C in LPL deficiency; mild hypertriglyceridemia; partial activity. Ref.36 Ref.43		VAR_004221
	Natural variant	201	1	D → V in LPL deficiency. Ref.70		VAR_057923
	Natural variant	203	1	A → T in LPL deficiency; Bethesda; loss of activity and abnormal heparin binding. Ref.19		VAR_004222
	Natural variant	207	1	D → E in LPL deficiency. Ref.35		VAR_004223
	Natural variant	208	1	V → I in LPL deficiency; decreases the specific activity of the enzyme; has a mild effect on the secretion of the mutant enzyme; the total LPL mass is reduced compared to that of the wild-type construct. Ref.67		VAR_057924
	Natural variant	210	1	H → D in LPL deficiency; complete loss of enzyme activity. Ref.65		VAR_057925
	Natural variant	210	1	H → Q in LPL deficiency; loss of activity.		VAR_004224
	Natural variant	215	1	G → 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 variant	215	1	G → R in LPL deficiency. Ref.51 Ref.54		VAR_057926
	Natural variant	220	1	S → R in LPL deficiency; 2.0% of activity.		VAR_004226
	Natural variant	221	1	I → T in LPL deficiency; loss of activity. Ref.20 Ref.23 Ref.33 Ref.72 Ref.73		VAR_004227
	Natural variant	222	1	G → E in LPL deficiency. Ref.31		VAR_004228
	Natural variant	225	1	K → R in LPL deficiency. Ref.72		VAR_057927
	Natural variant	227	1	V → A in LPL deficiency. Ref.72		VAR_057928
	Natural variant	231	1	D → E in LPL deficiency; loss of activity. Ref.24 Ref.63 Ref.72		VAR_004229
	Natural variant	232	1	I → S in LPL deficiency. Ref.33		VAR_004230
	Natural variant	234	1	P → L in LPL deficiency; loss of activity. Ref.25 Ref.54		VAR_004231
	Natural variant	243	1	C → S in LPL deficiency; loss of activity. Ref.29		VAR_004232
	Natural variant	252	1	I → T in LPL deficiency. Ref.55		VAR_057929
	Natural variant	266	1	C → W in LPL deficiency. Ref.64		VAR_057930
	Natural variant	270	1	R → C in LPL deficiency. Ref.41 Ref.51 Ref.54 Ref.72		VAR_057931
	Natural variant	270	1	R → H in LPL deficiency; loss of activity. Ref.20 Ref.24 Ref.32 Ref.41 Ref.55 Ref.72		VAR_004233
	Natural variant	271	1	S → T in LPL deficiency. Ref.16 Corresponds to variant rs28934893 [ dbSNP | Ensembl ].		VAR_004234
	Natural variant	277	1	D → N in LPL deficiency; 5% of full activity. Ref.28 Ref.32 Ref.48 Ref.51 Ref.54		VAR_004235
	Natural variant	278	1	S → C in LPL deficiency.		VAR_004236
	Natural variant	279	1	L → R in LPL deficiency; decreases the specific activity of the enzyme; the total LPL mass is reduced compared to that of the wild-type construct. Ref.43 Ref.67 Corresponds to variant rs35414700 [ dbSNP | Ensembl ].		VAR_057932
	Natural variant	279	1	L → V in LPL deficiency; decreases the specific activity of the enzyme; the total LPL mass is reduced compared to that of the wild-type construct. Ref.67		VAR_057933
	Natural variant	286	1	S → G in LPL deficiency. Ref.57		VAR_004237
	Natural variant	286	1	S → R in LPL deficiency. Ref.52		VAR_004238
	Natural variant	288	1	A → 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 variant	289	1	Y → H in LPL deficiency; no enzyme activity. Ref.50		VAR_057934
	Natural variant	297	1	F → L in LPL deficiency and hyperlipidemia; synthesized as a catalytically inactive form; total amount is almost equal to that of the normal enzyme; non-releasable by heparin due to the abnormal structure of the mutant protein. Ref.62 Ref.72		VAR_057935
	Natural variant	303	1	L → F in LPL deficiency; approximately 6% of normal LPL activity and 40% of LPL mass are detected in the patient's postheparin plasma; results in the production of a functionally inactive enzyme. Ref.68		VAR_057936
	Natural variant	305	1	C → R in LPL deficiency. Ref.72		VAR_057937
	Natural variant	310	1	C → Y in LPL deficiency; decreases the specific activity of the enzyme; reduces the secretion of the mutant protein significantly; the total LPL mass is reduced compared to that of the wild-type construct. Ref.67		VAR_057938
	Natural variant	313	1	L → P in LPL deficiency. Ref.51		VAR_057939
	Natural variant	318	1	N → 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 variant	325	1	S → R in LPL deficiency; has no effect on the specific activity of the enzyme; has a mild effect on the secretion of the mutant enzyme; the total LPL mass is reduced compared to that of the wild-type construct. Ref.67		VAR_057940
	Natural variant	328	1	M → R in LPL deficiency. Ref.71		VAR_057941
	Natural variant	328	1	M → T in LPL deficiency.		VAR_004240
	Natural variant	330	1	L → F in LPL deficiency. Ref.72		VAR_057942
	Natural variant	330	1	L → P in LPL deficiency.		VAR_004241
	Natural variant	361	1	A → T in LPL deficiency. Ref.34 Ref.72		VAR_004242
	Natural variant	365	1	S → F in LPL deficiency; increases the specific activity of the enzyme; has a mild effect on the secretion of the mutant enzyme; the total LPL mass is reduced compared to that of the wild-type construct. Ref.67		VAR_057943
	Natural variant	370	1	V → M. Ref.59 Corresponds to variant rs298 [ dbSNP | Ensembl ].		VAR_011950
	Natural variant	379	1	T → A. Ref.59 Corresponds to variant rs300 [ dbSNP | Ensembl ].		VAR_011951
	Natural variant	392	1	L → V in LPL deficiency; loss of activity. Ref.39		VAR_004243
	Natural variant	423 – 424	2	Missing in LPL deficiency; affects the protein folding.		VAR_004244
	Natural variant	427	1	A → T. Ref.60 Corresponds to variant rs5934 [ dbSNP | Ensembl ].		VAR_011952
	Natural variant	437	1	E → K in LPL deficiency. Ref.48		VAR_004245
	Natural variant	437	1	E → V in LPL deficiency. Ref.44		VAR_004246
	Natural variant	445	1	C → Y in LPL deficiency; has 48% of normal activity in vitro; decreased levels of activity account for by the lower protein mass levels of the mutants rather than by decreased enzymatic activities. Ref.46		VAR_057944
	Natural variant	448	1	E → K in LPL deficiency; results in a moderate reduction in catalytic activity. Ref.56		VAR_057945
Experimental info
	Mutagenesis	159	1	S → G: Lacks both triolein and tributyrin esterase activities. Ref.30
	Mutagenesis	159	1	S → T: Lacks both triolein and tributyrin esterase activities. Ref.30
	Mutagenesis	268	1	H → G: Lacks both triolein and tributyrin esterase activities. Ref.30
	Mutagenesis	268	1	H → Q: Lacks both triolein and tributyrin esterase activities. Ref.30

Sequences

	Sequence		Length	Mass (Da)
	P06858 [UniParc]. Last modified January 1, 1988. Version 1. Checksum: FBD00FCD334FB8AA	FASTA	475	53,162
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
PIR	LIHUL. A26082.
RefSeq	NP_000228.1. NM_000237.2.
UniGene	Hs.180878.
3D structure databases
ProteinModelPortal	P06858.
SMR	P06858. Positions 4-466.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	110205. 19 interactions.
IntAct	P06858. 11 interactions.
MINT	MINT-1369348.
STRING	9606.ENSP00000309757.
Chemistry
BindingDB	P06858.
ChEMBL	CHEMBL2060.
DrugBank	DB00636. Clofibrate. DB01241. Gemfibrozil. DB01083. Orlistat.
PTM databases
PhosphoSite	P06858.
Polymorphism databases
DMDM	126314.
Proteomic databases
PaxDb	P06858.
PRIDE	P06858.
Protocols and materials databases
DNASU	4023.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000311322; ENSP00000309757; ENSG00000175445.
GeneID	4023.
KEGG	hsa:4023.
UCSC	uc003wzk.4. human.
Organism-specific databases
CTD	4023.
GeneCards	GC08P019759.
HGNC	HGNC:6677. LPL.
HPA	HPA048749.
MIM	238600. phenotype. 609708. gene.
neXtProt	NX_P06858.
Orphanet	309015. Familial lipoprotein lipase deficiency. 70470. Hyperlipoproteinemia type 5.
PharmGKB	PA232.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG40923.
HOGENOM	HOG000038553.
HOVERGEN	HBG002259.
InParanoid	P06858.
KO	K01059.
OMA	ESVANCH.
PhylomeDB	P06858.
TreeFam	TF324997.
Enzyme and pathway databases
BRENDA	3.1.1.34. 2681.
Reactome	REACT_111045. Developmental Biology. REACT_111102. Signal Transduction. REACT_111217. Metabolism. REACT_116125. Disease.
Gene expression databases
ArrayExpress	P06858.
Bgee	P06858.
CleanEx	HS_LPL.
Genevestigator	P06858.
Family and domain databases
Gene3D	2.60.60.20. 1 hit.
InterPro	IPR000734. Lipase. IPR008976. Lipase_LipOase. IPR013818. Lipase_N. IPR002330. Lipo_Lipase. IPR016272. Lipoprotein_lipase_LIPH. IPR001024. PLAT/LH2_dom. [Graphical view]
PANTHER	PTHR11610. PTHR11610. 1 hit. PTHR11610:SF3. PTHR11610:SF3. 1 hit.
Pfam	PF00151. Lipase. 1 hit. PF01477. PLAT. 1 hit. [Graphical view]
PIRSF	PIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTS	PR00822. LIPOLIPASE. PR00821. TAGLIPASE.
SMART	SM00308. LH2. 1 hit. [Graphical view]
SUPFAM	SSF49723. SSF49723. 1 hit.
TIGRFAMs	TIGR03230. lipo_lipase. 1 hit.
PROSITE	PS00120. LIPASE_SER. 1 hit. PS50095. PLAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GeneWiki	Lipoprotein_lipase.
GenomeRNAi	4023.
NextBio	15776.
PRO	P06858.
SOURCE	Search...

Entry information

Entry name

LIPL_HUMAN

Accession

Primary (citable) accession number: P06858
Secondary accession number(s): B2R5T9 , 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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.