CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017078
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Neuropathy target esterase 
Protein Synonyms/Alias
 Patatin-like phospholipase domain-containing protein 6 
Gene Name
 PNPLA6 
Gene Synonyms/Alias
 NTE 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
192RVLGHFEKPLFLELCubiquitination[1]
298AFSAVFTKYPESLVRubiquitination[2, 3]
394GPTGDPVKPTSLETPubiquitination[4]
500SSIFEAAKQELAKLMubiquitination[1]
600CTFLRISKSDFYEIMubiquitination[1]
893NTAVRALKQLVLLHRubiquitination[1, 5]
946KLHELYEKVFSRRADubiquitination[2, 3]
1093ASAMRVHKDGSLWRYubiquitination[1]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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] 
Functional Description
 Phospholipase B that deacylates intracellular phosphatidylcholine (PtdCho), generating glycerophosphocholine (GroPtdCho). This deacylation occurs at both sn-2 and sn-1 positions of PtdCho. Its specific chemical modification by certain organophosphorus (OP) compounds leads to distal axonopathy. 
Sequence Annotation
 DOMAIN 972 1138 Patatin.
 NP_BIND 186 313 cNMP 1.
 NP_BIND 502 624 cNMP 2.
 NP_BIND 620 740 cNMP 3.
 MOTIF 1003 1007 GXSXG.
 ACT_SITE 1005 1005 By similarity.
 MOD_RES 345 345 Phosphoserine.
 MOD_RES 352 352 Phosphothreonine.
 MOD_RES 353 353 Phosphoserine.
 CARBOHYD 11 11 N-linked (GlcNAc...) (Potential).  
Keyword
 Alternative splicing; Complete proteome; Disease mutation; Endoplasmic reticulum; Glycoprotein; Hereditary spastic paraplegia; Hydrolase; Lipid degradation; Lipid metabolism; Membrane; Neurodegeneration; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1366 AA 
Protein Sequence
MGTSSHGLAT NSSGAKVAER DGFQDVLAPG EGSAGRICGA QPVPFVPQVL GVMIGAGVAV 60
VVTAVLILLV VRRLRVPKTP APDGPRYRFR KRDKVLFYGR KIMRKVSQST SSLVDTSVSA 120
TSRPRMRKKL KMLNIAKKIL RIQKETPTLQ RKEPPPAVLE ADLTEGDLAN SHLPSEVLYM 180
LKNVRVLGHF EKPLFLELCR HMVFQRLGQG DYVFRPGQPD ASIYVVQDGL LELCLPGPDG 240
KECVVKEVVP GDSVNSLLSI LDVITGHQHP QRTVSARAAR DSTVLRLPVE AFSAVFTKYP 300
ESLVRVVQII MVRLQRVTFL ALHNYLGLTN ELFSHEIQPL RLFPSPGLPT RTSPVRGSKR 360
MVSTSATDEP RETPGRPPDP TGAPLPGPTG DPVKPTSLET PSAPLLSRCV SMPGDISGLQ 420
GGPRSDFDMA YERGRISVSL QEEASGGSLA APARTPTQEP REQPAGACEY SYCEDESATG 480
GCPFGPYQGR QTSSIFEAAK QELAKLMRIE DPSLLNSRVL LHHAKAGTII ARQGDQDVSL 540
HFVLWGCLHV YQRMIDKAED VCLFVAQPGE LVGQLAVLTG EPLIFTLRAQ RDCTFLRISK 600
SDFYEIMRAQ PSVVLSAAHT VAARMSPFVR QMDFAIDWTA VEAGRALYRQ GDRSDCTYIV 660
LNGRLRSVIQ RGSGKKELVG EYGRGDLIGV VEALTRQPRA TTVHAVRDTE LAKLPEGTLG 720
HIKRRYPQVV TRLIHLLSQK ILGNLQQLQG PFPAGSGLGV PPHSELTNPA SNLATVAILP 780
VCAEVPMVAF TLELQHALQA IGPTLLLNSD IIRARLGASA LDSIQEFRLS GWLAQQEDAH 840
RIVLYQTDAS LTPWTVRCLR QADCILIVGL GDQEPTLGQL EQMLENTAVR ALKQLVLLHR 900
EEGAGPTRTV EWLNMRSWCS GHLHLRCPRR LFSRRSPAKL HELYEKVFSR RADRHSDFSR 960
LARVLTGNTI ALVLGGGGAR GCSHIGVLKA LEEAGVPVDL VGGTSIGSFI GALYAEERSA 1020
SRTKQRAREW AKSMTSVLEP VLDLTYPVTS MFTGSAFNRS IHRVFQDKQI EDLWLPYFNV 1080
TTDITASAMR VHKDGSLWRY VRASMTLSGY LPPLCDPKDG HLLMDGGYIN NLPADIARSM 1140
GAKTVIAIDV GSQDETDLST YGDSLSGWWL LWKRLNPWAD KVKVPDMAEI QSRLAYVSCV 1200
RQLEVVKSSS YCEYLRPPID CFKTMDFGKF DQIYDVGYQY GKAVFGGWSR GNVIEKMLTD 1260
RRSTDLNESR RADVLAFPSS GFTDLAEIVS RIEPPTSYVS DGCADGEESD CLTEYEEDAG 1320
PDCSRDEGGS PEGASPSTAS EMEEEKSILR QRRCLPQEPP GSATDA 1366 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0004622; F:lysophospholipase activity; IEA:EC.
 GO:0008219; P:cell death; IEA:UniProtKB-KW.
 GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
 GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro. 
Interpro
 IPR016035; Acyl_Trfase/lysoPLipase.
 IPR018490; cNMP-bd-like.
 IPR000595; cNMP-bd_dom.
 IPR001423; LysoPLipase_patatin_CS.
 IPR002641; Patatin/PLipase_A2-rel.
 IPR014710; RmlC-like_jellyroll. 
Pfam
 PF00027; cNMP_binding
 PF01734; Patatin 
SMART
 SM00100; cNMP 
PROSITE
 PS00888; CNMP_BINDING_1
 PS00889; CNMP_BINDING_2
 PS50042; CNMP_BINDING_3
 PS01237; UPF0028 
PRINTS