CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019871
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Lipid phosphate phosphohydrolase 3 
Protein Synonyms/Alias
 PAP2-beta; Phosphatidate phosphohydrolase type 2b; Phosphatidic acid phosphatase 2b; PAP-2b; PAP2b 
Gene Name
 Ppap2b 
Gene Synonyms/Alias
 Lpp3 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
8MQSYKYDKAIVPESKubiquitination[1]
15KAIVPESKNGGSPALubiquitination[1]
74YCNDESIKYPLKVSEacetylation[2, 3]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337
Functional Description
 Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). In addition it hydrolyzes lysophosphatidic acid (LPA), ceramide-1-phosphate (C-1-P) and sphingosine-1- phosphate (S-1-P) (By similarity). Essential to the formation of the chorioallantoic placenta and extraembryonic vasculature. Also mediates gastrulation and axis formation, probably by regulating the Wnt signaling pathway. 
Sequence Annotation
 MOD_RES 19 19 Phosphoserine (By similarity).
 MOD_RES 298 298 Phosphoserine (By similarity).
 CARBOHYD 171 171 N-linked (GlcNAc...) (Potential).  
Keyword
 Complete proteome; Developmental protein; Direct protein sequencing; Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane; Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 312 AA 
Protein Sequence
MQSYKYDKAI VPESKNGGSP ALNNNPRKGG SKRVLLICLD LFCLFMAALP FLIIETSTIK 60
PYRRGFYCND ESIKYPLKVS ETINDAVLCA VGIVIAILAI ITGEFYRIYY LKEKSRSTTQ 120
NPYVAALYKQ VGCFLFGCAI SQSFTDIAKV SIGRLRPHFL SVCDPDFSQI NCSEGYIQNY 180
RCRGEDSKVQ EARKSFFSGH ASFSMFTMLY LVLYLQARFT WRGARLLRPL LQFTLLMMAF 240
YTGLSRVSDY KHHPSDVLAG FAQGALVACC IVFFVSDLFK TKTSLSLPAP AIRREILSPV 300
DIIDRNNHHN MV 312 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005178; F:integrin binding; IDA:MGI.
 GO:0042577; F:lipid phosphatase activity; IMP:MGI.
 GO:0008195; F:phosphatidate phosphatase activity; IEA:EC.
 GO:0001568; P:blood vessel development; IMP:MGI.
 GO:0060070; P:canonical Wnt receptor signaling pathway; IDA:BHF-UCL.
 GO:0044329; P:canonical Wnt receptor signaling pathway involved in positive regulation of cell-cell adhesion; IEA:Compara.
 GO:0044328; P:canonical Wnt receptor signaling pathway involved in positive regulation of endothelial cell migration; IEA:Compara.
 GO:0044330; P:canonical Wnt receptor signaling pathway involved in positive regulation of wound healing; IEA:Compara.
 GO:0016337; P:cell-cell adhesion; IDA:MGI.
 GO:0001702; P:gastrulation with mouth forming second; IMP:MGI.
 GO:0034109; P:homotypic cell-cell adhesion; IEA:Compara.
 GO:0001933; P:negative regulation of protein phosphorylation; IDA:BHF-UCL.
 GO:0006644; P:phospholipid metabolic process; IMP:MGI.
 GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:MGI.
 GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IDA:BHF-UCL.
 GO:0050821; P:protein stabilization; IDA:BHF-UCL.
 GO:0030111; P:regulation of Wnt receptor signaling pathway; IDA:MGI. 
Interpro
 IPR016118; P_Acid_Pase/Cl_peroxidase_N.
 IPR000326; P_Acid_Pase_2/haloperoxidase. 
Pfam
 PF01569; PAP2 
SMART
 SM00014; acidPPc 
PROSITE
  
PRINTS