CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005836
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Phosphatidylethanolamine-binding protein 1 
Protein Synonyms/Alias
 PEBP-1; HCNPpp; Neuropolypeptide h3; Prostatic-binding protein; Raf kinase inhibitor protein; RKIP; Hippocampal cholinergic neurostimulating peptide; HCNP 
Gene Name
 PEBP1 
Gene Synonyms/Alias
 PBP; PEBP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
39AAVDELGKVLTPTQVacetylation[1]
47VLTPTQVKNRPTSISubiquitination[2, 3, 4, 5, 6, 7]
113YVGSGPPKGTGLHRYubiquitination[3, 4, 6, 8, 9]
132YEQDRPLKCDEPILSubiquitination[3, 9]
179EWDDYVPKLYEQLSGubiquitination[5]
Reference
 [1] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [2] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [3] 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]
 [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] 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]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [7] 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]
 [8] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [9] 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
Functional Description
 Binds ATP, opioids and phosphatidylethanolamine. Has lower affinity for phosphatidylinositol and phosphatidylcholine. Serine protease inhibitor which inhibits thrombin, neuropsin and chymotrypsin but not trypsin, tissue type plasminogen activator and elastase (By similarity). Inhibits the kinase activity of RAF1 by inhibiting its activation and by dissociating the RAF1/MEK complex and acting as a competitive inhibitor of MEK phosphorylation. 
Sequence Annotation
 REGION 93 134 Interaction with RAF1.
 MOD_RES 42 42 Phosphothreonine.
 MOD_RES 52 52 Phosphoserine.
 MOD_RES 54 54 Phosphoserine (By similarity).  
Keyword
 3D-structure; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Disulfide bond; Lipid-binding; Nucleotide-binding; Phosphoprotein; Protease inhibitor; Reference proteome; Serine protease inhibitor. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 187 AA 
Protein Sequence
MPVDLSKWSG PLSLQEVDEQ PQHPLHVTYA GAAVDELGKV LTPTQVKNRP TSISWDGLDS 60
GKLYTLVLTD PDAPSRKDPK YREWHHFLVV NMKGNDISSG TVLSDYVGSG PPKGTGLHRY 120
VWLVYEQDRP LKCDEPILSN RSGDHRGKFK VASFRKKYEL RAPVAGTCYQ AEWDDYVPKL 180
YEQLSGK 187 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0008429; F:phosphatidylethanolamine binding; TAS:ProtInc.
 GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW. 
Interpro
 IPR001858; Phosphotidylethanolamine-bd_CS.
 IPR008914; PtdEtn-bd_prot_PEBP. 
Pfam
 PF01161; PBP 
SMART
  
PROSITE
 PS01220; PBP 
PRINTS