CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011734
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Mitochondrial-processing peptidase subunit alpha 
Protein Synonyms/Alias
 Alpha-MPP; P-55 
Gene Name
 PMPCA 
Gene Synonyms/Alias
 INPP5E; KIAA0123; MPPA 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
53SPLPGVPKPVFATVDubiquitination[1, 2, 3]
64ATVDGQEKFETKVTTubiquitination[4, 5]
68GQEKFETKVTTLDNGubiquitination[2, 4, 5, 6]
103SGSRYEAKYLSGIAHubiquitination[1, 2, 3, 4, 5, 6]
126STARFDSKDEILLTLubiquitination[2, 4, 5, 6, 7]
135EILLTLEKHGGICDCubiquitination[5, 6]
232CPTENVAKINREVLHubiquitination[4, 6, 7, 8]
269HLVDCARKYLLGVQPubiquitination[2, 4, 6]
299QYTGGIAKLERDMSNacetylation[9]
299QYTGGIAKLERDMSNubiquitination[2, 4, 6, 7]
460VLATRSRKLPHELCTubiquitination[6]
473CTLIRNVKPEDVKRVubiquitination[4]
478NVKPEDVKRVASKMLubiquitination[2, 4]
483DVKRVASKMLRGKPAubiquitination[6]
488ASKMLRGKPAVAALGubiquitination[2, 4]
513IQTALSSKDGRLPRTubiquitination[4]
Reference
 [1] 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]
 [2] 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]
 [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] 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] 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]
 [7] 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]
 [8] 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]
 [9] 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] 
Functional Description
 Cleaves presequences (transit peptides) from mitochondrial protein precursors (By similarity). 
Sequence Annotation
 MOD_RES 299 299 N6-acetyllysine.  
Keyword
 Acetylation; Complete proteome; Hydrolase; Metalloprotease; Mitochondrion; Protease; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 525 AA 
Protein Sequence
MAAVVLAATR LLRGSGSWGC SRLRFGPPAY RRFSSGGAYP NIPLSSPLPG VPKPVFATVD 60
GQEKFETKVT TLDNGLRVAS QNKFGQFCTV GILINSGSRY EAKYLSGIAH FLEKLAFSST 120
ARFDSKDEIL LTLEKHGGIC DCQTSRDTTM YAVSADSKGL DTVVALLADV VLQPRLTDEE 180
VEMTRMAVQF ELEDLNLRPD PEPLLTEMIH EAAYRENTVG LHRFCPTENV AKINREVLHS 240
YLRNYYTPDR MVLAGVGVEH EHLVDCARKY LLGVQPAWGS AEAVDIDRSV AQYTGGIAKL 300
ERDMSNVSLG PTPIPELTHI MVGLESCSFL EEDFIPFAVL NMMMGGGGSF SAGGPGKGMF 360
SRLYLNVLNR HHWMYNATSY HHSYEDTGLL CIHASADPRQ VREMVEIITK EFILMGGTVD 420
TVELERAKTQ LTSMLMMNLE SRPVIFEDVG RQVLATRSRK LPHELCTLIR NVKPEDVKRV 480
ASKMLRGKPA VAALGDLTDL PTYEHIQTAL SSKDGRLPRT YRLFR 525 
Gene Ontology
 GO:0005743; C:mitochondrial inner membrane; TAS:UniProtKB.
 GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
 GO:0046872; F:metal ion binding; IEA:InterPro.
 GO:0004222; F:metalloendopeptidase activity; TAS:UniProtKB.
 GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
 GO:0006626; P:protein targeting to mitochondrion; TAS:Reactome.
 GO:0006508; P:proteolysis; TAS:UniProtKB. 
Interpro
 IPR011249; Metalloenz_LuxS/M16.
 IPR011237; Pept_M16_dom.
 IPR011765; Pept_M16_N.
 IPR001431; Pept_M16_Zn_BS.
 IPR007863; Peptidase_M16_C. 
Pfam
 PF00675; Peptidase_M16
 PF05193; Peptidase_M16_C 
SMART
  
PROSITE
 PS00143; INSULINASE 
PRINTS