dbPTM

PLPL2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PLPL2_HUMAN
UniProt AC	Q96AD5
Protein Name	Patatin-like phospholipase domain-containing protein 2
Gene Name	PNPLA2
Organism	Homo sapiens (Human).
Sequence Length	504
Subcellular Localization	Lipid droplet. Cell membrane Single-pass type II membrane protein.
Protein Description	Catalyzes the initial step in triglyceride hydrolysis in adipocyte and non-adipocyte lipid droplets. [PubMed: 15550674 Also has acylglycerol transacylase activity. May act coordinately with LIPE/HLS within the lipolytic cascade. Regulates adiposome size and may be involved in the degradation of adiposomes]
Protein Sequence	MFPREKTWNISFAGCGFLGVYYVGVASCLREHAPFLVANATHIYGASAGALTATALVTGVCLGEAGAKFIEVSKEARKRFLGPLHPSFNLVKIIRSFLLKVLPADSHEHASGRLGISLTRVSDGENVIISHFNSKDELIQANVCSGFIPVYCGLIPPSLQGVRYVDGGISDNLPLYELKNTITVSPFSGESDICPQDSSTNIHELRVTNTSIQFNLRNLYRLSKALFPPEPLVLREMCKQGYRDGLRFLQRNGLLNRPNPLLALPPARPHGPEDKDQAVESAQAEDYSQLPGEDHILEHLPARLNEALLEACVEPTDLLTTLSNMLPVRLATAMMVPYTLPLESALSFTIRLLEWLPDVPEDIRWMKEQTGSICQYLVMRAKRKLGRHLPSRLPEQVELRRVQSLPSVPLSCAAYREALPGWMRNNLSLGDALAKWEECQRQLLLGLFCTNVAFPPEALRMRAPADPAPAPADPASPQHQLAGPAPLLSTPAPEARPVIGALGL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
39	N-linked_Glycosylation	HAPFLVANATHIYGA HCCEEEEECCEEECC	37.58	UniProtKB CARBOHYD
74	Ubiquitination	AKFIEVSKEARKRFL HHHHHHCHHHHHHHC	61.64	21906983
74 (in isoform 1)	Ubiquitination	-	61.64	21890473
78	Ubiquitination	EVSKEARKRFLGPLH HHCHHHHHHHCCCCC	55.33	22817900
92	Ubiquitination	HPSFNLVKIIRSFLL CCCHHHHHHHHHHHH	35.27	-
100	Ubiquitination	IIRSFLLKVLPADSH HHHHHHHHHCCCCCC	43.82	21906983
100 (in isoform 1)	Ubiquitination	-	43.82	21890473
117	Phosphorylation	ASGRLGISLTRVSDG CCCCCEEEEEEECCC	23.14	24719451
119	O-linked_Glycosylation	GRLGISLTRVSDGEN CCCEEEEEEECCCCC	23.41	29351928
176	Phosphorylation	ISDNLPLYELKNTIT CCCCCEEEEEECEEE	19.78	27642862
179	Ubiquitination	NLPLYELKNTITVSP CCEEEEEECEEEECC	39.85	21963094
224 (in isoform 1)	Ubiquitination	-	54.42	21890473
224	Ubiquitination	RNLYRLSKALFPPEP HHHHHHHHHHCCCCH	54.42	23000965
239	Ubiquitination	LVLREMCKQGYRDGL HHHHHHHHCCHHHHH	45.51	27667366
287	Phosphorylation	ESAQAEDYSQLPGED HHHHHHCHHHCCCCC	6.99	28796482
288	Phosphorylation	SAQAEDYSQLPGEDH HHHHHCHHHCCCCCC	37.25	28796482
349	Phosphorylation	LESALSFTIRLLEWL HHHHHHHHHHHHHHC	11.21	24719451
367	Ubiquitination	PEDIRWMKEQTGSIC CHHHHHHHHHHHCHH	39.45	-
372	Phosphorylation	WMKEQTGSICQYLVM HHHHHHHCHHHHHHH	24.47	-
391	Phosphorylation	KLGRHLPSRLPEQVE HHHCCCCCCCHHHHH	53.46	24719451
404	Phosphorylation	VELRRVQSLPSVPLS HHHEECCCCCCCCHH	39.11	23927012
407	Phosphorylation	RRVQSLPSVPLSCAA EECCCCCCCCHHHHH	41.48	30266825
411	Phosphorylation	SLPSVPLSCAAYREA CCCCCCHHHHHHHHH	8.81	30266825
415	Phosphorylation	VPLSCAAYREALPGW CCHHHHHHHHHCCHH	7.17	23403867
428	Phosphorylation	GWMRNNLSLGDALAK HHHHCCCCHHHHHHH	32.22	19664994
435	Ubiquitination	SLGDALAKWEECQRQ CHHHHHHHHHHHHHH	56.86	21963094
476	Phosphorylation	PAPADPASPQHQLAG CCCCCCCCCCCCCCC	30.40	29255136
490	Phosphorylation	GPAPLLSTPAPEARP CCCCCCCCCCCCCCC	24.36	21712546

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
404	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot
404	S	Phosphorylation	Kinase	PKA	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
404	S	Phosphorylation	22733971
Phosphorylation at Ser-404 by PKA is increased during fasting and moderate intensity exercise, and moderately increases lipolytic activity (By similarity).
404	S	Phosphorylation	22733971
Phosphorylation at Ser-404 is increased upon beta-adrenergic stimulation.

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 PLPL2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PEDF_HUMAN	SERPINF1	physical	17032652
GBF1_HUMAN	GBF1	physical	21789191
ABHD5_HUMAN	ABHD5	physical	17189257
PEX14_HUMAN	PEX14	physical	28514442
TRXR2_HUMAN	TXNRD2	physical	28514442
TIM29_HUMAN	C19orf52	physical	28514442
RFWD2_HUMAN	RFWD2	physical	27658392

Drug and Disease Associations

Kegg Disease
H01297	Neutral lipid storage disease with myopathy
OMIM Disease
	Note=Genetic variations in PNPLA2 may be associated with risk of diabetes mellitus type 2.
610717
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PLPL2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, AND MASSSPECTROMETRY.	18669648 [Abstract]

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