LIPL_BOVIN - dbPTM
LIPL_BOVIN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LIPL_BOVIN
UniProt AC P11151
Protein Name Lipoprotein lipase
Gene Name LPL
Organism Bos taurus (Bovine).
Sequence Length 478
Subcellular Localization Cell membrane
Lipid-anchor, GPI-anchor. Secreted. 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.
Protein Description 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..
Protein Sequence MESKALLLLALSVCLQSLTVSRGGLVAADRITGGKDFRDIESKFALRTPEDTAEDTCHLIPGVTESVANCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQQHYPVSAGYTKLVGQDVAKFMNWMADEFNYPLGNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEALRVIAERGLGDVDQLVKCSHERSVHLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNMGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTESNTYTNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLLYTEVDIGELLMLKLKWISDSYFSWSNWWSSPGFDIGKIRVKAGETQKKVIFCSREKMSYLQKGKSPVIFVKCHDKSLNRKSG
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
73N-linked_GlycosylationSVANCHFNHSSKTFV
HHEECEECCCCCEEE
15.512674142
103NitrationPKLVAALYKREPDSN
HHHHHHHHHCCCCCC
11.85-
124Nitrated tyrosineLSRAQQHYPVSAGYT
HHHHHHHCCCCCCCH
10.86-
124NitrationLSRAQQHYPVSAGYT
HHHHHHHCCCCCCCH
10.86-
130NitrationHYPVSAGYTKLVGQD
HCCCCCCCHHHHCHH
10.62-
194Nitrated tyrosinePAGPNFEYAEAPSRL
CCCCCCCCCCCCCCC
12.95-
194NitrationPAGPNFEYAEAPSRL
CCCCCCCCCCCCCCC
12.95-
287N-linked_GlycosylationDSLLNEENPSKAYRC
HHHHCCCCCCCCCCC
39.71-
318NitrationNRCNNMGYEINKVRA
CCCCCCCHHHHHHHH
11.67-
341NitrationKTRSQMPYKVFHYQV
EEHHCCCCEEEEEEE
17.91-
346Nitrated tyrosineMPYKVFHYQVKIHFS
CCCEEEEEEEEEEEC
11.97-
346NitrationMPYKVFHYQVKIHFS
CCCEEEEEEEEEEEC
11.97-
389N-linked_GlycosylationTLPEVSTNKTYSFLL
CCCCCCCCCEEEEEE
27.452674142
455NitrationCSREKMSYLQKGKSP
ECHHHHHHHHCCCCC
15.06-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of LIPL_BOVIN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LIPL_BOVIN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of LIPL_BOVIN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of LIPL_BOVIN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LIPL_BOVIN

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Related Literatures of Post-Translational Modification

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