CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023610
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Phospholipase A-2-activating protein 
Protein Synonyms/Alias
 PLA2P; PLAP 
Gene Name
 PLAA 
Gene Synonyms/Alias
 PLAP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
176GSADKTVKLWKAGRCubiquitination[1]
179DKTVKLWKAGRCERTubiquitination[1]
259DRSLRIWKHGECAQTubiquitination[1, 2, 3]
311TASAEEIKAFEKELSubiquitination[1, 2, 4, 5, 6]
315EEIKAFEKELSHATIubiquitination[1, 2, 4, 5, 6, 7]
325SHATIDSKTGDLGDIubiquitination[1, 2, 5]
361RLIRDGEKVEAYQWSubiquitination[1, 2]
376VSEGRWIKIGDVVGSubiquitination[7]
393ANQQTSGKVLYEGKEubiquitination[2, 4, 5, 6, 7]
399GKVLYEGKEFDYVFSubiquitination[8]
436TAYNFLQKNDLNPMFubiquitination[5]
449MFLDQVAKFIIDNTKubiquitination[5]
456KFIIDNTKGQMLGLGubiquitination[1, 2, 4, 5, 6, 7, 9]
529AYRSAASKTMNIYFPacetylation[10]
529AYRSAASKTMNIYFPubiquitination[1, 3, 4, 5, 6, 7]
538MNIYFPKKEAVTFDQubiquitination[1, 2]
554NPTQILGKLKELNGTubiquitination[1]
556TQILGKLKELNGTAPubiquitination[1, 5]
567GTAPEEKKLTEDDLIubiquitination[1]
622DILRLSIKHPSVNENubiquitination[1, 2, 7]
652NLLNPKGKPANQLLAubiquitination[1, 3]
691MSHAIELKSGSNKNIacetylation[11]
691MSHAIELKSGSNKNIubiquitination[1, 2]
773LGVDSQIKKYSSVSEubiquitination[1, 3]
774GVDSQIKKYSSVSEPubiquitination[1, 12]
783SSVSEPAKVSECCRFubiquitination[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] 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]
 [3] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [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] 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]
 [10] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [11] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [12] 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
 Involved in the maintenance of ubiquitin levels (By similarity). 
Sequence Annotation
 REPEAT 17 56 WD 1.
 REPEAT 63 107 WD 2.
 REPEAT 110 148 WD 3.
 REPEAT 149 188 WD 4.
 REPEAT 190 227 WD 5.
 REPEAT 229 268 WD 6.
 REPEAT 270 307 WD 7.
 DOMAIN 366 465 PFU.
 DOMAIN 533 794 PUL.
 REPEAT 546 588 ARM 1.
 REPEAT 589 620 ARM 2.
 REPEAT 621 669 ARM 3.
 REPEAT 670 715 ARM 4.
 REPEAT 716 755 ARM 5.
 REPEAT 756 795 ARM 6.
 MOD_RES 529 529 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Reference proteome; Repeat; WD repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 795 AA 
Protein Sequence
MTSGATRYRL SCSLRGHELD VRGLVCCAYP PGAFVSVSRD RTTRLWAPDS PNRSFTEMHC 60
MSGHSNFVSC VCIIPSSDIY PHGLIATGGN DHNICIFSLD SPMPLYILKG HKNTVCSLSS 120
GKFGTLLSGS WDTTAKVWLN DKCMMTLQGH TAAVWAVKIL PEQGLMLTGS ADKTVKLWKA 180
GRCERTFSGH EDCVRGLAIL SETEFLSCAN DASIRRWQIT GECLEVYYGH TNYIYSISVF 240
PNCRDFVTTA EDRSLRIWKH GECAQTIRLP AQSIWCCCVL DNGDIVVGAS DGIIRVFTES 300
EDRTASAEEI KAFEKELSHA TIDSKTGDLG DINAEQLPGR EHLNEPGTRE GQTRLIRDGE 360
KVEAYQWSVS EGRWIKIGDV VGSSGANQQT SGKVLYEGKE FDYVFSIDVN EGGPSYKLPY 420
NTSDDPWLTA YNFLQKNDLN PMFLDQVAKF IIDNTKGQML GLGNPSFSDP FTGGGRYVPG 480
SSGSSNTLPT ADPFTGAGRY VPGSASMGTT MAGVDPFTGN SAYRSAASKT MNIYFPKKEA 540
VTFDQANPTQ ILGKLKELNG TAPEEKKLTE DDLILLEKIL SLICNSSSEK PTVQQLQILW 600
KAINCPEDIV FPALDILRLS IKHPSVNENF CNEKEGAQFS SHLINLLNPK GKPANQLLAL 660
RTFCNCFVGQ AGQKLMMSQR ESLMSHAIEL KSGSNKNIHI ALATLALNYS VCFHKDHNIE 720
GKAQCLSLIS TILEVVQDLE ATFRLLVALG TLISDDSNAV QLAKSLGVDS QIKKYSSVSE 780
PAKVSECCRF ILNLL 795 
Gene Ontology
 GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
 GO:0016005; F:phospholipase A2 activator activity; TAS:ProtInc.
 GO:0006954; P:inflammatory response; IEA:Compara.
 GO:0006644; P:phospholipid metabolic process; TAS:ProtInc.
 GO:0007165; P:signal transduction; TAS:ProtInc. 
Interpro
 IPR015155; PLAA_fam_Ub-bd_PFU.
 IPR013535; PUL.
 IPR015943; WD40/YVTN_repeat-like_dom.
 IPR001680; WD40_repeat.
 IPR017986; WD40_repeat_dom. 
Pfam
 PF09070; PFU
 PF08324; PUL
 PF00400; WD40 
SMART
 SM00320; WD40 
PROSITE
 PS50176; ARM_REPEAT
 PS51394; PFU
 PS51396; PUL
 PS00678; WD_REPEATS_1
 PS50082; WD_REPEATS_2
 PS50294; WD_REPEATS_REGION 
PRINTS