LICH_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: LICH_HUMAN
• UniProt AC: P38571
• Protein Name: Lysosomal acid lipase/cholesteryl ester hydrolase
• Gene Name: LIPA
• Organism: Homo sapiens (Human).
• Sequence Length: 399
• Subcellular Localization: Lysosome.
• Protein Description: Crucial for the intracellular hydrolysis of cholesteryl esters and triglycerides that have been internalized via receptor-mediated endocytosis of lipoprotein particles. Important in mediating the effect of LDL (low density lipoprotein) uptake on suppression of hydroxymethylglutaryl-CoA reductase and activation of endogenous cellular cholesteryl ester formation..
• Protein Sequence: MKMRFLGLVVCLVLWTLHSEGSGGKLTAVDPETNMNVSEIISYWGFPSEEYLVETEDGYILCLNRIPHGRKNHSDKGPKPVVFLQHGLLADSSNWVTNLANSSLGFILADAGFDVWMGNSRGNTWSRKHKTLSVSQDEFWAFSYDEMAKYDLPASINFILNKTGQEQVYYVGHSQGTTIGFIAFSQIPELAKRIKMFFALGPVASVAFCTSPMAKLGRLPDHLIKDLFGDKEFLPQSAFLKWLGTHVCTHVILKELCGNLCFLLCGFNERNLNMSRVDVYTTHSPAGTSVQNMLHWSQAVKFQKFQAFDWGSSAKNYFHYNQSYPPTYNVKDMLVPTAVWSGGHDWLADVYDVNILLTQITNLVFHESIPEWEHLDFIWGLDAPWRLYNKIINLMRKYQ

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
36	N-linked_Glycosylation	VDPETNMNVSEIISY ECCCCCCCHHHHHHH	35.91	UniProtKB CARBOHYD
72	N-linked_Glycosylation	RIPHGRKNHSDKGPK CCCCCCCCCCCCCCC	38.24	UniProtKB CARBOHYD
101	N-linked_Glycosylation	NWVTNLANSSLGFIL HHHHHHHHCCCCEEE	34.98	UniProtKB CARBOHYD
161	N-linked_Glycosylation	ASINFILNKTGQEQV EEEEEEECCCCCCEE	34.72	16399764
161	N-linked_Glycosylation	ASINFILNKTGQEQV EEEEEEECCCCCCEE	34.72	16399764
231	2-Hydroxyisobutyrylation	IKDLFGDKEFLPQSA HHHHHCCCCCCCHHH	51.23	-
231	Ubiquitination	IKDLFGDKEFLPQSA HHHHHCCCCCCCHHH	51.23	-
237	Phosphorylation	DKEFLPQSAFLKWLG CCCCCCHHHHHHHHH	21.03	-
248 (in isoform 2)	Ubiquitination	-	1.36	21890473
273	N-linked_Glycosylation	GFNERNLNMSRVDVY CCCCCCCCCCCEEEE	29.90	UniProtKB CARBOHYD
280	Phosphorylation	NMSRVDVYTTHSPAG CCCCEEEEECCCCCC	11.06	23532336
289	Phosphorylation	THSPAGTSVQNMLHW CCCCCCCCHHHHHHH	22.31	23532336
297	Phosphorylation	VQNMLHWSQAVKFQK HHHHHHHHHHHCCCE	9.49	28674151
304	Ubiquitination	SQAVKFQKFQAFDWG HHHHCCCEECCCCCC	42.44	2189047
304 (in isoform 1)	Ubiquitination	-	42.44	21890473
317	Phosphorylation	WGSSAKNYFHYNQSY CCCCCCCCCCCCCCC	7.33	-
320	Phosphorylation	SAKNYFHYNQSYPPT CCCCCCCCCCCCCCC	12.66	-
321	N-linked_Glycosylation	AKNYFHYNQSYPPTY CCCCCCCCCCCCCCC	18.76	19159218
328	Phosphorylation	NQSYPPTYNVKDMLV CCCCCCCCCHHCCCC	24.59	-

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of LICH_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 LICH_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of LICH_HUMAN !!

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 278000: Wolman disease (WOD)
• 278000: Cholesteryl ester storage disease (CESD)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-161 AND ASN-321, AND MASSSPECTROMETRY.
PubMed: 19159218