CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001390
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Putative ATP-dependent Clp protease proteolytic subunit, mitochondrial 
Protein Synonyms/Alias
 Endopeptidase Clp 
Gene Name
 Clpp 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
196IQAEEIMKLKKQLYNacetylation[1]
196IQAEEIMKLKKQLYNsuccinylation[1]
199EEIMKLKKQLYNIYAacetylation[1]
199EEIMKLKKQLYNIYAsuccinylation[1]
207QLYNIYAKHTKQSLQacetylation[2, 3]
210NIYAKHTKQSLQVIEacetylation[2]
Reference
 [1] 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]
 [2] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [3] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753
Functional Description
 Clp cleaves peptides in various proteins in a process that requires ATP hydrolysis. Clp may be responsible for a fairly general and central housekeeping function rather than for the degradation of specific substrates. 
Sequence Annotation
 ACT_SITE 149 149 Probable.
 ACT_SITE 174 174 Probable.
 MOD_RES 207 207 N6-acetyllysine (By similarity).
 MOD_RES 272 272 Phosphothreonine (By similarity).  
Keyword
 Acetylation; ATP-binding; Complete proteome; Hydrolase; Mitochondrion; Nucleotide-binding; Phosphoprotein; Protease; Reference proteome; Serine protease; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 272 AA 
Protein Sequence
MWPRVLLGEA RVAVDGCRAL LSRLAVHFSP PWTAVSCSPL RRSLHGTATR AFPLIPIVVE 60
QTGRGERAYD IYSRLLRERI VCVMGPIDDS VASLVIAQLL FLQSESNKKP IHMYINSPGG 120
VVTAGLAIYD TMQYILNPIC TWCVGQAASM GSLLLAAGSP GMRHSLPNSR IMIHQPSGGA 180
RGQATDIAIQ AEEIMKLKKQ LYNIYAKHTK QSLQVIESAM ERDRYMSPME AQEFGILDKV 240
LVHPPQDGED EPELVQKETA TAPTDPPAPT ST 272 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
 GO:0006515; P:misfolded or incompletely synthesized protein catabolic process; ISA:MGI. 
Interpro
 IPR001907; ClpP.
 IPR023562; ClpP/TepA.
 IPR018215; ClpP_AS. 
Pfam
 PF00574; CLP_protease 
SMART
  
PROSITE
 PS00382; CLP_PROTEASE_HIS
 PS00381; CLP_PROTEASE_SER 
PRINTS
 PR00127; CLPPROTEASEP.