CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019038
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Patatin-like phospholipase domain-containing protein 2 
Protein Synonyms/Alias
 Adipose triglyceride lipase; Calcium-independent phospholipase A2; Desnutrin; IPLA2-zeta; Pigment epithelium-derived factor; TTS2.2; Transport-secretion protein 2; TTS2 
Gene Name
 PNPLA2 
Gene Synonyms/Alias
 ATGL; FP17548 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
74AKFIEVSKEARKRFLubiquitination[1, 2, 3]
92HPSFNLVKIIRSFLLubiquitination[2]
100IIRSFLLKVLPADSHubiquitination[1, 2]
179NLPLYELKNTITVSPubiquitination[4]
224RNLYRLSKALFPPEPubiquitination[1, 2, 3, 5, 6, 7]
367PEDIRWMKEQTGSICubiquitination[2]
435SLGDALAKWEECQRQubiquitination[2, 3, 4, 8]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [5] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [6] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [7] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [8] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572] 
Functional Description
 Catalyzes the initial step in triglyceride hydrolysis in adipocyte and non-adipocyte lipid droplets. 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. 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. 
Sequence Annotation
 DOMAIN 10 179 Patatin.
 MOTIF 45 49 GXSXG.
 ACT_SITE 47 47
 MOD_RES 372 372 Phosphoserine; in vitro (By similarity).
 MOD_RES 404 404 Phosphoserine; by PKA.
 MOD_RES 428 428 Phosphoserine.
 CARBOHYD 39 39 N-linked (GlcNAc...) (Potential).  
Keyword
 Alternative splicing; Cell membrane; Complete proteome; Disease mutation; Glycoprotein; Hydrolase; Lipid degradation; Lipid droplet; Lipid metabolism; Membrane; Phosphoprotein; Polymorphism; Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 504 AA 
Protein Sequence
MFPREKTWNI SFAGCGFLGV YYVGVASCLR EHAPFLVANA THIYGASAGA LTATALVTGV 60
CLGEAGAKFI EVSKEARKRF LGPLHPSFNL VKIIRSFLLK VLPADSHEHA SGRLGISLTR 120
VSDGENVIIS HFNSKDELIQ ANVCSGFIPV YCGLIPPSLQ GVRYVDGGIS DNLPLYELKN 180
TITVSPFSGE SDICPQDSST NIHELRVTNT SIQFNLRNLY RLSKALFPPE PLVLREMCKQ 240
GYRDGLRFLQ RNGLLNRPNP LLALPPARPH GPEDKDQAVE SAQAEDYSQL PGEDHILEHL 300
PARLNEALLE ACVEPTDLLT TLSNMLPVRL ATAMMVPYTL PLESALSFTI RLLEWLPDVP 360
EDIRWMKEQT GSICQYLVMR AKRKLGRHLP SRLPEQVELR RVQSLPSVPL SCAAYREALP 420
GWMRNNLSLG DALAKWEECQ RQLLLGLFCT NVAFPPEALR MRAPADPAPA PADPASPQHQ 480
LAGPAPLLST PAPEARPVIG ALGL 504 
Gene Ontology
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005811; C:lipid particle; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0050253; F:retinyl-palmitate esterase activity; IEA:EC.
 GO:0004806; F:triglyceride lipase activity; ISS:UniProtKB.
 GO:0036155; P:acylglycerol acyl-chain remodeling; TAS:Reactome.
 GO:0046474; P:glycerophospholipid biosynthetic process; TAS:Reactome.
 GO:0010891; P:negative regulation of sequestering of triglyceride; IDA:UniProtKB.
 GO:0010898; P:positive regulation of triglyceride catabolic process; IDA:UniProtKB.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome.
 GO:0019433; P:triglyceride catabolic process; IEA:UniProtKB-UniPathway. 
Interpro
 IPR016035; Acyl_Trfase/lysoPLipase.
 IPR002641; Patatin/PLipase_A2-rel. 
Pfam
 PF01734; Patatin 
SMART
  
PROSITE
  
PRINTS