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Protein Page:
LPL (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
LPL 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. Defects in LPL are the cause of lipoprotein lipase deficiency (LPL deficiency); also known as familial chylomicronemia or hyperlipoproteinemia type I. LPL deficiency chylomicronemia is a 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. Belongs to the AB hydrolase superfamily. Lipase family. Note: This description may include information from UniProtKB.
Protein type: Lipid Metabolism - glycerolipid; Membrane protein, GPI anchor; Phospholipase; EC 3.1.1.34
Cellular Component: extracellular matrix; extracellular space; chylomicron; cell surface; plasma membrane; extracellular region
Molecular Function: heparin binding; triacylglycerol lipase activity; lipoprotein lipase activity; protein binding; apolipoprotein binding; phospholipase activity; triglyceride binding; receptor binding
Biological Process: response to drug; phototransduction, visible light; triacylglycerol metabolic process; phospholipid metabolic process; triacylglycerol catabolic process; lipoprotein metabolic process; triacylglycerol biosynthetic process; response to cold; retinoid metabolic process; fatty acid biosynthetic process
Reference #:  P06858 (UniProtKB)
Alt. Names/Synonyms: HDLCQ11; LIPD; LIPL; Lipoprotein lipase; LPL
Gene Symbols: LPL
Molecular weight: 53,162 Da
Basal Isoelectric point: 8.37  Predict pI for various phosphorylation states
Select Structure to View Below

LPL

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 S17-p TLAVWLQsLtAsRGG
0 1 T19-p AVWLQsLtAsRGGVA
0 1 S21-p WLQsLtAsRGGVAAA
0 1 K40 DFIDIESKFALRTPE
0 1 T75-p HFNHSSKtFMVIHGW
0 1 K129 PVSAGYTKLVGQDVA
0 1 K265 GDVDQLVKCSHERSI
0 1 S304-p FEKGLCLsCRKNRCN
0 1 K327 VRAKRSSKMyLKTRS
0 1 Y329-p AKRSSKMyLKTRSQM
0 1 Y343-p MPYKVFHyQVKIHFS
0 1 K408-ac ELLMLKLkWKSDSYF
0 1 T438-p IRVKAGEtQKKVIFC
  mouse

 
S17 VLGVWLQSLTAFRGG
T19 GVWLQSLTAFRGGVA
F21 WLQSLTAFRGGVAAA
K40-ub DFSDIESkFALRTPE
T75 HFNHSSKTFVVIHGW
K129-ub PVSAGYTkLVGNDVA
K265-ub GDVDQLVkCSHERSI
S304 FEKGLCLSCRKNRCN
K327-ac VRAKRSSkMYLKTRS
Y329 AKRSSkMYLKTRSQM
Y343 MPYKVFHYQVKIHFS
K408 ELLMMKLKWISDSYF
T438 IRVKAGETQKKVIFC
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