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Protein Page:
PNPLA2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
PNPLA2 the rate-limiting lipolytic enzyme in mammals, flies, and yeast. Catalyzes the initial step in triglyceride hydrolysis in adipocyte and non-adipocyte lipid droplets. Upregulated by exercise training in human skeletal muscle. Has acylglycerol transacylase activity. May act coordinately with HSL within the lipolytic cascade. Regulates adiposome size and may be involved in the degradation of adiposomes. May play an important role in energy homeostasis. May play a role in the response of the organism to starvation, enhancing hydrolysis of triglycerides and providing free fatty acids to other tissues to be oxidized in situations of energy depletion. Interacting with ABHD5 stimulates its triglyceride hydrolase activity. Despite a colocalization in lipid droplets, it probably does not interact with perilipin. Transcriptionally regulated by FOXO1A. Defects cause neutral lipid storage disease (NLSD), an autosomal recessive disorder characterized by the excessive accumulation of neutral lipids in multiple tissues. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Membrane protein, integral; EC 3.1.1.3; Lipase
Chromosomal Location of Human Ortholog: 11p15.5
Cellular Component: endoplasmic reticulum membrane; lipid particle
Molecular Function: acylglycerol O-acyltransferase activity; lipoprotein lipase activity; triacylglycerol lipase activity
Disease: Neutral Lipid Storage Disease With Myopathy
Reference #:  Q96AD5 (UniProtKB)
Alt. Names/Synonyms: 1110001C14Rik; Adipose triglyceride lipase; ATGL; Calcium-independent phospholipase A2; Desnutrin; DKFZp667M109; FP17548; IPLA2-zeta; patatin-like phospholipase domain containing 2; Patatin-like phospholipase domain-containing protein 2; PEDF-R; Pigment epithelium-derived factor; PLPL2; PNPLA2; Transport-secretion protein 2; transport-secretion protein 2.2; triglyceride hydrolase; TTS-2.2; TTS2; TTS2.2
Gene Symbols: PNPLA2
Molecular weight: 55,316 Da
Basal Isoelectric point: 6.65  Predict pI for various phosphorylation states
Select Structure to View Below

PNPLA2

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment



 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 2 K74‑ub AKFIEVSkEARKRFL
1 0 S87 FLGPLHPSFNLVKII
0 1 K100‑ub IIRSFLLkVLPADSH
1 0 V101 IRSFLLkVLPADSHE
0 1 E108 VLPADSHEHASGRLG
1 0 T210 HELRVTNTSIQFNLR
0 13 K224‑ub RNLYRLSkALFPPEP
0 8 Y287‑p ESAQAEDySQLPGED
0 1 E293 DySQLPGEDHILEHL
1 0 T370 IRWMKEQTGSICQYL
1 0 Y376 QTGSICQYLVMRAKR
1 1 S391‑p KLGRHLPsRLPEQVE
3 71 S404‑p VELRRVQsLPsVPLS
0 4 S407‑p RRVQsLPsVPLSCAA
0 1 A414 sVPLSCAAYREALPG
0 1 Y415 VPLSCAAYREALPGW
1 41 S428‑p GWMRNNLsLGDALAk
0 1 K435‑ub sLGDALAkWEECQRQ
0 1 D466 LRMRAPADPAPAPAD
0 3 S476‑p PAPADPAsPQHQLAG
0 1 T490‑p GPAPLLStPAPEARP
0 1 - gap
  PNPLA2 iso2  
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
T46 IRWMKEQTGSICQYL
Y52 QTGSICQYLVMRAKR
S67 KLGRHLPSRLPEQVE
S80 VELRRVQSLPSVPLS
S83 RRVQSLPSVPLSCAA
A90 SVPLSCAAYREALPG
Y91 VPLSCAAYREALPGW
S104 GWMRNNLSLGDALAK
K111 SLGDALAKWEECQRQ
D142 LRMRAPADPAPAPAD
S152 PAPADPASPQHQLAG
T166 GPAPLLSTPAPEARP
- gap
  mouse

 
K74 ANIIEVSKEARKRFL
S87‑p FLGPLHPsFNLVKTI
K100 TIRGCLLKtLPADCH
T101‑p IRGCLLKtLPADCHE
E108 tLPADCHERANGRLG
T210‑p HELRVTNtSIQFNLR
K224‑ub RNLYRLSkALFPPEP
Q289 ERAGEEDQLQPYRkD
K295‑ub DQLQPYRkDRILEHL
T372‑p IRWMKEQtGSICQyL
Y378‑p QtGSICQyLVMRAKR
S393‑p KLGDHLPsRLSEQVE
S406‑p VELRRAQsLPsVPLS
S409‑p RRAQsLPsVPLSCAt
T416‑p sVPLSCAtySEALPN
Y417‑p VPLSCAtySEALPNW
S430‑p NWVRNNLsLGDALAK
K437 sLGDALAKWEECQRQ
S468‑p LRMRAPAsPTAADPA
- gap
- gap
T476‑p PTAADPAtPQDPPGL
  rat

 
K74 ANIIEVSKEARKRFL
S87 FLGPLHPSFNLVKTI
K100 TIRGCLLKTLPADCH
T101 IRGCLLKTLPADCHt
T108‑p TLPADCHtRASGRLG
T210 HELRITNTSIQFNLR
K224 RNLYRLSKALFPPEP
- gap
- gap
T364 IRWMKEQTGSICQYL
Y370 QTGSICQYLVMRAKR
S385 KLGDHLPSRLSEQVE
S398‑p VELRRAQsLPSVPLS
S401 RRAQsLPSVPLSCAT
T408 SVPLSCATYSEALPN
Y409 VPLSCATYSEALPNW
S422‑p NWVRNNLsLGDALAK
K429 sLGDALAKWEECQRQ
S460 LRMRAPASPTATDPA
- gap
- gap
T468 PTATDPATPQDPSGL
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