LIPL_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: LIPL_HUMAN
• UniProt AC: P06858
• Protein Name: Lipoprotein lipase
• Gene Name: LPL
• Organism: Homo sapiens (Human).
• Sequence Length: 475
• 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). [PubMed: 27578112 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]
• Protein Sequence: MESKALLVLTLAVWLQSLTASRGGVAAADQRRDFIDIESKFALRTPEDTAEDTCHLIPGVAESVATCHFNHSSKTFMVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQEHYPVSAGYTKLVGQDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCSSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTESETHTNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMLKLKWKSDSYFSWSDWWSSPGFAIQKIRVKAGETQKKVIFCSREKVSHLQKGKAPAVFVKCHDKSLNKKSG

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
17	Phosphorylation	TLAVWLQSLTASRGG HHHHHHHHHHHHCCC	26.05	-
19	Phosphorylation	AVWLQSLTASRGGVA HHHHHHHHHHCCCCH	28.03	-
21	Phosphorylation	WLQSLTASRGGVAAA HHHHHHHHCCCCHHH	26.65	-
40	Ubiquitination	DFIDIESKFALRTPE CCEECCCCEECCCCC	23.13	-
70	N-linked_Glycosylation	SVATCHFNHSSKTFM HEEEEEEECCCCEEE	15.51	18780401
75	Phosphorylation	HFNHSSKTFMVIHGW EEECCCCEEEEEEEE	20.93	-
121	Nitrated tyrosine	LSRAQEHYPVSAGYT HHHHHHHCCCCCCHH	12.46	-
121	Nitration	LSRAQEHYPVSAGYT HHHHHHHCCCCCCHH	12.46	-
129	Ubiquitination	PVSAGYTKLVGQDVA CCCCCHHHHHCHHHH	32.46	-
180	Phosphorylation	NKKVNRITGLDPAGP CCCHHCCCCCCCCCC	28.58	20068231
191	Nitration	PAGPNFEYAEAPSRL CCCCCCCCCCCCCCC	12.95	-
191	Phosphorylation	PAGPNFEYAEAPSRL CCCCCCCCCCCCCCC	12.95	20068231
191	Nitrated tyrosine	PAGPNFEYAEAPSRL CCCCCCCCCCCCCCC	12.95	-
196	Phosphorylation	FEYAEAPSRLSPDDA CCCCCCCCCCCCCCC	53.56	20068231
265	Ubiquitination	GDVDQLVKCSHERSI CCHHHHHHCCCHHHH	38.32	-
294	Ubiquitination	KAYRCSSKEAFEKGL CCCCCCCHHHHHCCC	36.45	-
299	Ubiquitination	SSKEAFEKGLCLSCR CCHHHHHCCCCHHHC	51.21	-
304	Phosphorylation	FEKGLCLSCRKNRCN HHCCCCHHHCCCCCC	15.75	-
329	Phosphorylation	AKRSSKMYLKTRSQM HHHCCCCEEEEHHCC	14.58	-
343	Nitration	MPYKVFHYQVKIHFS CCCEEEEEEEEEEEC	11.97	-
343	Phosphorylation	MPYKVFHYQVKIHFS CCCEEEEEEEEEEEC	11.97	-
343	Nitrated tyrosine	MPYKVFHYQVKIHFS CCCEEEEEEEEEEEC	11.97	-
386	N-linked_Glycosylation	TLPEVSTNKTYSFLI CCCCCCCCCEEEEEE	27.45	30559189
408	Acetylation	ELLMLKLKWKSDSYF HHEEEEECCCCCCCC	51.49	7396805
411	Phosphorylation	MLKLKWKSDSYFSWS EEEECCCCCCCCCHH	30.58	26074081
413	Phosphorylation	KLKWKSDSYFSWSDW EECCCCCCCCCHHHH	34.86	26074081
414	Phosphorylation	LKWKSDSYFSWSDWW ECCCCCCCCCHHHHH	13.46	26074081
416	Phosphorylation	WKSDSYFSWSDWWSS CCCCCCCCHHHHHCC	19.89	26074081
418	Phosphorylation	SDSYFSWSDWWSSPG CCCCCCHHHHHCCCC	23.35	26074081
438	Phosphorylation	IRVKAGETQKKVIFC EEEECCCCCCEEEEE	44.78	-
469	Phosphorylation	FVKCHDKSLNKKSG- EEEECHHHHCCCCC-	43.14	24719451

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

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

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UBE2Z_HUMAN	UBE2Z	physical	16169070
CSN6_HUMAN	COPS6	physical	16169070
CE126_HUMAN	KIAA1377	physical	16169070
LC7L2_HUMAN	LUC7L2	physical	16169070
VLDLR_HUMAN	VLDLR	physical	7592875
LRP1_HUMAN	LRP1	physical	7510694
LRP1_HUMAN	LRP1	physical	7989348
A4_HUMAN	APP	physical	21832049
LIPL_HUMAN	LPL	physical	12740382
CALR_HUMAN	CALR	physical	12740382
LMF1_HUMAN	LMF1	physical	19783858

Drug and Disease Associations

• Kegg Disease
• H00154: Hyperlipoproteinemia, type I
• OMIM Disease
• 238600: Lipoprotein lipase deficiency (LPL deficiency)
• Kegg Drug
• D03747: Ibrolipim (USAN/INN)
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Identification of N-linked glycoproteins in human milk by hydrophilicinteraction liquid chromatography and mass spectrometry.";
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
Proteomics 8:3833-3847(2008).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70, AND MASS SPECTROMETRY.
PubMed: 18780401