dbPTM

LCAT_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LCAT_HUMAN
UniProt AC	P04180
Protein Name	Phosphatidylcholine-sterol acyltransferase
Gene Name	LCAT
Organism	Homo sapiens (Human).
Sequence Length	440
Subcellular Localization	Secreted . Secreted into blood plasma (PubMed:3458198, PubMed:8820107, PubMed:10222237). Produced in astrocytes and secreted into cerebral spinal fluid (CSF).
Protein Description	Central enzyme in the extracellular metabolism of plasma lipoproteins. Synthesized mainly in the liver and secreted into plasma where it converts cholesterol and phosphatidylcholines (lecithins) to cholesteryl esters and lysophosphatidylcholines on the surface of high and low density lipoproteins (HDLs and LDLs). [PubMed: 10329423]
Protein Sequence	MGPPGSPWQWVTLLLGLLLPPAAPFWLLNVLFPPHTTPKAELSNHTRPVILVPGCLGNQLEAKLDKPDVVNWMCYRKTEDFFTIWLDLNMFLPLGVDCWIDNTRVVYNRSSGLVSNAPGVQIRVPGFGKTYSVEYLDSSKLAGYLHTLVQNLVNNGYVRDETVRAAPYDWRLEPGQQEEYYRKLAGLVEEMHAAYGKPVFLIGHSLGCLHLLYFLLRQPQAWKDRFIDGFISLGAPWGGSIKPMLVLASGDNQGIPIMSSIKLKEEQRITTTSPWMFPSRMAWPEDHVFISTPSFNYTGRDFQRFFADLHFEEGWYMWLQSRDLLAGLPAPGVEVYCLYGVGLPTPRTYIYDHGFPYTDPVGVLYEDGDDTVATRSTELCGLWQGRQPQPVHLLPLHGIQHLNMVFSNLTLEHINAILLGAYRQGPPASPTASPEPPPPE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
44	N-linked_Glycosylation	TPKAELSNHTRPVIL CCCHHHCCCCCCEEE	53.85	17623646
44	N-linked_Glycosylation	TPKAELSNHTRPVIL CCCHHHCCCCCCEEE	53.85	16335952
108	N-linked_Glycosylation	DNTRVVYNRSSGLVS CCCEEEEECCCCCCC	26.25	26195816
108	N-linked_Glycosylation	DNTRVVYNRSSGLVS CCCEEEEECCCCCCC	26.25	26195816
205	Phosphorylation	PVFLIGHSLGCLHLL CEEEEEHHHHHHHHH	22.65	22817900
213	Phosphorylation	LGCLHLLYFLLRQPQ HHHHHHHHHHHHCCH	9.88	-
296	N-linked_Glycosylation	FISTPSFNYTGRDFQ EEECCCCCCCCHHHH	37.48	26195816
296	N-linked_Glycosylation	FISTPSFNYTGRDFQ EEECCCCCCCCHHHH	37.48	26195816
376	Phosphorylation	DDTVATRSTELCGLW CCCEEEECHHCCCCC	23.14	-
377	Phosphorylation	DTVATRSTELCGLWQ CCEEEECHHCCCCCC	29.68	-
408	N-linked_Glycosylation	HLNMVFSNLTLEHIN HHHHHHCCCCHHHHH	26.11	26195816
408	N-linked_Glycosylation	HLNMVFSNLTLEHIN HHHHHHCCCCHHHHH	26.11	26195816
431	O-linked_Glycosylation	QGPPASPTASPEPPP CCCCCCCCCCCCCCC	36.95	7613477
431	O-linked_Glycosylation	QGPPASPTASPEPPP CCCCCCCCCCCCCCC	36.95	7613477
433	O-linked_Glycosylation	PPASPTASPEPPPPE CCCCCCCCCCCCCCC	32.07	7613477
433	O-linked_Glycosylation	PPASPTASPEPPPPE CCCCCCCCCCCCCCC	32.07	7613477

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 LCAT_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
431	T	Glycosylation	7613477
O-glycosylation on Thr-431 and Ser-433 consists of sialylated galactose beta 1-->3N-acetylgalactosamine structures.
433	S	Glycosylation	7613477
O-glycosylation on Thr-431 and Ser-433 consists of sialylated galactose beta 1-->3N-acetylgalactosamine structures.

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
115	N-linked Glycosylation	123 (8)	R ⇒ H	rs199717050	Total cholesterol levels in HDL	29084231

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
APOA1_HUMAN	APOA1	physical	4335615
APOA1_HUMAN	APOA1	physical	10222237
APOA1_HUMAN	APOA1	physical	15654758
APOE_HUMAN	APOE	physical	15654758
APOA1_HUMAN	APOA1	physical	10026251
FYV1_HUMAN	PIKFYVE	physical	26195816

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
245900	Lecithin-cholesterol acyltransferase deficiency (LCATD)
136120	Fish-eye disease (FED)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of LCAT_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-44 AND ASN-296, AND MASSSPECTROMETRY.	16335952 [Abstract]
"Site-specific detection and structural characterization of theglycosylation of human plasma proteins lecithin:cholesterolacyltransferase and apolipoprotein D using HPLC/electrospray massspectrometry and sequential glycosidase digestion."; Schindler P.A., Settineri C.A., Collet X., Fielding C.J.,Burlingame A.L.; Protein Sci. 4:791-803(1995). Cited for: GLYCOSYLATION AT ASN-44; ASN-108; ASN-296; ASN-408; THR-431 ANDSER-433, STRUCTURE OF CARBOHYDRATES, AND MASS SPECTROMETRY.	7613477 [Abstract]
O-linked Glycosylation
Reference	PubMed
"Site-specific detection and structural characterization of theglycosylation of human plasma proteins lecithin:cholesterolacyltransferase and apolipoprotein D using HPLC/electrospray massspectrometry and sequential glycosidase digestion."; Schindler P.A., Settineri C.A., Collet X., Fielding C.J.,Burlingame A.L.; Protein Sci. 4:791-803(1995). Cited for: GLYCOSYLATION AT ASN-44; ASN-108; ASN-296; ASN-408; THR-431 ANDSER-433, STRUCTURE OF CARBOHYDRATES, AND MASS SPECTROMETRY.	7613477 [Abstract]