CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001312
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial 
Protein Synonyms/Alias
  
Gene Name
 CLPX 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
67TPAYFASKDGISKDGubiquitination[1]
80DGSGDGNKKSASEGSubiquitination[1]
81GSGDGNKKSASEGSSubiquitination[1]
89SASEGSSKKSGSGNSubiquitination[1]
98SGSGNSGKGGNQLRCacetylation[2]
178KIYNYLDKYVVGQSFacetylation[3]
239EDEYRFTKLLQIAGIubiquitination[1]
269NQQIPQEKRGGEVLDubiquitination[1]
299LGPTGSGKTLLAQTLubiquitination[1, 4]
349DANYNVEKAQQGIVFubiquitination[1]
386GVQQGLLKLLEGTIVubiquitination[1]
398TIVNVPEKNSRKLRGubiquitination[1]
437ISRRKNEKYLGFGTPacetylation[3]
449GTPSNLGKGRRAAAAubiquitination[4, 5]
475THQDIEEKDRLLRHVacetylation[5]
512PLHSLDEKTLVQILTubiquitination[1]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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
 ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of clpP (By similarity). 
Sequence Annotation
 ZN_FING 105 130 C4-type.
 NP_BIND 293 300 ATP (Potential).
 MOD_RES 437 437 N6-acetyllysine.
 MOD_RES 617 617 Phosphoserine.  
Keyword
 Acetylation; ATP-binding; Chaperone; Complete proteome; Metal-binding; Mitochondrion; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Transit peptide; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 633 AA 
Protein Sequence
MPSCGACTCG AAAVRLITSS LASAQRGISG GRIHMSVLGR LGTFETQILQ RAPLRSFTET 60
PAYFASKDGI SKDGSGDGNK KSASEGSSKK SGSGNSGKGG NQLRCPKCGD LCTHVETFVS 120
STRFVKCEKC HHFFVVLSEA DSKKSIIKEP ESAAEAVKLA FQQKPPPPPK KIYNYLDKYV 180
VGQSFAKKVL SVAVYNHYKR IYNNIPANLR QQAEVEKQTS LTPRELEIRR REDEYRFTKL 240
LQIAGISPHG NALGASMQQQ VNQQIPQEKR GGEVLDSSHD DIKLEKSNIL LLGPTGSGKT 300
LLAQTLAKCL DVPFAICDCT TLTQAGYVGE DIESVIAKLL QDANYNVEKA QQGIVFLDEV 360
DKIGSVPGIH QLRDVGGEGV QQGLLKLLEG TIVNVPEKNS RKLRGETVQV DTTNILFVAS 420
GAFNGLDRII SRRKNEKYLG FGTPSNLGKG RRAAAAADLA NRSGESNTHQ DIEEKDRLLR 480
HVEARDLIEF GMIPEFVGRL PVVVPLHSLD EKTLVQILTE PRNAVIPQYQ ALFSMDKCEL 540
NVTEDALKAI ARLALERKTG ARGLRSIMEK LLLEPMFEVP NSDIVCVEVD KEVVEGKKEP 600
GYIRAPTKES SEEEYDSGVE EEGWPRQADA ANS 633 
Gene Ontology
 GO:0009841; C:mitochondrial endopeptidase Clp complex; IDA:UniProtKB.
 GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
 GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0005524; F:ATP binding; ISS:UniProtKB.
 GO:0016887; F:ATPase activity; ISS:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0016504; F:peptidase activator activity; IDA:UniProtKB.
 GO:0006457; P:protein folding; IEA:InterPro.
 GO:0051603; P:proteolysis involved in cellular protein catabolic process; IDA:UniProtKB. 
Interpro
 IPR003593; AAA+_ATPase.
 IPR013093; ATPase_AAA-2.
 IPR019489; Clp_ATPase_C.
 IPR004487; Clp_protease_ATP-bd_su_ClpX.
 IPR027417; P-loop_NTPase. 
Pfam
 PF07724; AAA_2
 PF10431; ClpB_D2-small 
SMART
 SM00382; AAA
 SM01086; ClpB_D2-small 
PROSITE
  
PRINTS