LIPR2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: LIPR2_HUMAN
• UniProt AC: P54317
• Protein Name: Pancreatic lipase-related protein 2 {ECO:0000312|HGNC:HGNC:9157}
• Gene Name: PNLIPRP2 {ECO:0000312|HGNC:HGNC:9157}
• Organism: Homo sapiens (Human).
• Sequence Length: 469
• Subcellular Localization: Secreted .
• Protein Description: Lipase with broad substrate specificity. Can hydrolyze both phospholipids and galactolipids. Acts preferentially on monoglycerides, phospholipids and galactolipids. Contributes to milk fat hydrolysis..
• Protein Sequence: MLPPWTLGLLLLATVRGKEVCYGQLGCFSDEKPWAGTLQRPVKLLPWSPEDIDTRFLLYTNENPNNFQLITGTEPDTIEASNFQLDRKTRFIIHGFLDKAEDSWPSDMCKKMFEVEKVNCICVDWRHGSRAMYTQAVQNIRVVGAETAFLIQALSTQLGYSLEDVHVIGHSLGAHTAAEAGRRLGGRVGRITGLDPAGPCFQDEPEEVRLDPSDAVFVDVIHTDSSPIVPSLGFGMSQKVGHLDFFPNGGKEMPGCKKNVLSTITDIDGIWEGIGGFVSCNHLRSFEYYSSSVLNPDGFLGYPCASYDEFQESKCFPCPAEGCPKMGHYADQFKGKTSAVEQTFFLNTGESGNFTSWRYKISVTLSGKEKVNGYIRIALYGSNENSKQYEIFKGSLKPDASHTCAIDVDFNVGKIQKVKFLWNKRGINLSEPKLGASQITVQSGEDGTEYNFCSSDTVEENVLQSLYPC

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
6	Phosphorylation	--MLPPWTLGLLLLA --CCCHHHHHHHHHH	19.40	25072903
14	Phosphorylation	LGLLLLATVRGKEVC HHHHHHHHHCCCEEE	15.65	25072903
89	Phosphorylation	NFQLDRKTRFIIHGF CCCCCCCEEEEEEEH	31.54	24719451
90	Phosphorylation	FQLDRKTRFIIHGFL CCCCCCEEEEEEEHH	24.65	24719451
353	N-linked_Glycosylation	LNTGESGNFTSWRYK EECCCCCCEEEEEEE	46.42	18702514
362	Phosphorylation	TSWRYKISVTLSGKE EEEEEEEEEEECCCC	12.77	24719451
363	Phosphorylation	SWRYKISVTLSGKEK EEEEEEEEEECCCCE	7.56	24719451
366	Phosphorylation	YKISVTLSGKEKVNG EEEEEEECCCCEECE	38.15	24719451
367	Phosphorylation	KISVTLSGKEKVNGY EEEEEECCCCEECEE	45.30	24719451
428	N-linked_Glycosylation	LWNKRGINLSEPKLG EEECCCCCCCCCCCC	40.10	UniProtKB CARBOHYD

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

Oops, there are no upstream regulatory protein records of LIPR2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of LIPR2_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 LIPR2_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of LIPR2_HUMAN !!

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.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Structure of human pancreatic lipase-related protein 2 with the lidin an open conformation.";
Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A.,Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.;
Biochemistry 47:9553-9564(2008).
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITHCALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353,MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, MASS SPECTROMETRY,ACTIVE SITE, AND DISULFIDE BONDS.
PubMed: 18702514