dbPTM

LIPE_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LIPE_HUMAN
UniProt AC	Q9Y5X9
Protein Name	Endothelial lipase
Gene Name	LIPG
Organism	Homo sapiens (Human).
Sequence Length	500
Subcellular Localization	Secreted.
Protein Description	Has phospholipase and triglyceride lipase activities. Hydrolyzes high density lipoproteins (HDL) more efficiently than other lipoproteins. Binds heparin..
Protein Sequence	MSNSVPLLCFWSLCYCFAAGSPVPFGPEGRLEDKLHKPKATQTEVKPSVRFNLRTSKDPEHEGCYLSVGHSQPLEDCSFNMTAKTFFIIHGWTMSGIFENWLHKLVSALHTREKDANVVVVDWLPLAHQLYTDAVNNTRVVGHSIARMLDWLQEKDDFSLGNVHLIGYSLGAHVAGYAGNFVKGTVGRITGLDPAGPMFEGADIHKRLSPDDADFVDVLHTYTRSFGLSIGIQMPVGHIDIYPNGGDFQPGCGLNDVLGSIAYGTITEVVKCEHERAVHLFVDSLVNQDKPSFAFQCTDSNRFKKGICLSCRKNRCNSIGYNAKKMRNKRNSKMYLKTRAGMPFRVYHYQMKIHVFSYKNMGEIEPTFYVTLYGTNADSQTLPLEIVERIEQNATNTFLVYTEEDLGDLLKIQLTWEGASQSWYNLWKEFRSYLSQPRNPGRELNIRRIRVKSGETQRKLTFCTEDPENTSISPGRELWFRKCRDGWRMKNETSPTVELP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSNSVPLLC ------CCCCHHHHH	37.50	28348404
4	Phosphorylation	----MSNSVPLLCFW ----CCCCHHHHHHH	20.15	28348404
12	Phosphorylation	VPLLCFWSLCYCFAA HHHHHHHHHHHHHHC	6.57	28348404
41	O-linked_Glycosylation	KLHKPKATQTEVKPS CCCCCCCCCCCCCCE	41.99	OGP
48	O-linked_Glycosylation	TQTEVKPSVRFNLRT CCCCCCCEEEEECCC	21.87	OGP
80	N-linked_Glycosylation	PLEDCSFNMTAKTFF CCCCCCEECCEEEEE	15.59	UniProtKB CARBOHYD
136	N-linked_Glycosylation	QLYTDAVNNTRVVGH HHHHHHCCCCEECHH	45.97	UniProtKB CARBOHYD
185	Phosphorylation	AGNFVKGTVGRITGL CCCCCCCCCCEECCC	17.67	-
190	Phosphorylation	KGTVGRITGLDPAGP CCCCCEECCCCCCCC	30.26	-
324	Sumoylation	NSIGYNAKKMRNKRN CCCCCCHHHHHCCCC	43.39	-
325	Sumoylation	SIGYNAKKMRNKRNS CCCCCHHHHHCCCCC	40.45	-
332	Phosphorylation	KMRNKRNSKMYLKTR HHHCCCCCCEEEEEC	23.88	23911959
338	Phosphorylation	NSKMYLKTRAGMPFR CCCEEEEECCCCCEE	24.13	23911959
393	N-linked_Glycosylation	IVERIEQNATNTFLV HHHHHHHHCCCEEEE	35.62	16335952
435	Phosphorylation	KEFRSYLSQPRNPGR HHHHHHHCCCCCCCC	29.88	24719451
469	N-linked_Glycosylation	FCTEDPENTSISPGR EECCCCCCCCCCCCC	44.51	UniProtKB CARBOHYD
491	N-linked_Glycosylation	RDGWRMKNETSPTVE CCCCEECCCCCCCCC	48.73	UniProtKB CARBOHYD
496	O-linked_Glycosylation	MKNETSPTVELP--- ECCCCCCCCCCC---	26.78	OGP

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 LIPE_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of LIPE_HUMAN !!

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 LIPE_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LIPE_HUMAN	LIPG	physical	19567873
LIPE_MOUSE	Lipg	physical	15117821
DJC13_HUMAN	DNAJC13	physical	28514442
TMED4_HUMAN	TMED4	physical	28514442
TBB1_HUMAN	TUBB1	physical	28514442
TMED9_HUMAN	TMED9	physical	28514442
TMED5_HUMAN	TMED5	physical	28514442
TRM1_HUMAN	TRMT1	physical	28514442
PLSI_HUMAN	PLS1	physical	28514442
PTPRS_HUMAN	PTPRS	physical	28514442
NRP1_HUMAN	NRP1	physical	28514442
TMEDA_HUMAN	TMED10	physical	28514442
TMED2_HUMAN	TMED2	physical	28514442
CALX_HUMAN	CANX	physical	28514442
ITIH2_HUMAN	ITIH2	physical	28514442
SDC2_HUMAN	SDC2	physical	28514442
1C07_HUMAN	HLA-C	physical	28514442
MK14_HUMAN	MAPK14	physical	28514442
ARL8A_HUMAN	ARL8A	physical	28514442
ABHEA_HUMAN	ABHD14A	physical	28514442
GPC3_HUMAN	GPC3	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of LIPE_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-393, AND MASSSPECTROMETRY.	16335952 [Abstract]