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Protein Page:
LIPC (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
LIPC Hepatic lipase has the capacity to catalyze hydrolysis of phospholipids, mono-, di-, and triglycerides, and acyl-CoA thioesters. It is an important enzyme in HDL metabolism. Hepatic lipase binds heparin. Defects in LIPC are the cause of hepatic lipase deficiency (HL deficiency). A disorder characterized by elevated levels of beta-migrating very low density lipoproteins, and abnormally triglyceride-rich low and high density lipoproteins. Belongs to the AB hydrolase superfamily. Lipase family. Note: This description may include information from UniProtKB.
Protein type: EC 3.1.1.3; Secreted, signal peptide; Phospholipase; Secreted; Lipid Metabolism - glycerolipid
Cellular Component: extracellular space
Molecular Function: heparin binding; triacylglycerol lipase activity; low-density lipoprotein binding; apolipoprotein binding; phospholipase activity
Biological Process: cholesterol metabolic process; cholesterol homeostasis; reverse cholesterol transport; triacylglycerol catabolic process; fatty acid biosynthetic process
Reference #:  P11150 (UniProtKB)
Alt. Names/Synonyms: HDLCQ12; Hepatic lipase; Hepatic triacylglycerol lipase; HL; HTGL; Lipase member C; lipase, hepatic; LIPC; LIPH
Gene Symbols: LIPC
Molecular weight: 55,914 Da
Basal Isoelectric point: 9.22  Predict pI for various phosphorylation states
Select Structure to View Below

LIPC

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 S347-p FLVTRAQsPFKVYHY
0 3 K486-ac TQEKIFVkCEIKSKT
  mouse

 
S348 FLITRAQSPFKVYHY
N487 SQEKVFVNCEVKSKR
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