CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019910
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Beta-lactamase-like protein 2 
Protein Synonyms/Alias
  
Gene Name
 Lactb2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
102NDTTYCIKKLRRNPQacetylation[1, 2, 3, 4, 5]
102NDTTYCIKKLRRNPQubiquitination[6]
131IENGDVVKTEGATLRubiquitination[6]
191LNNLLKIKANIIYPGubiquitination[6]
234LFRDNFEKSFTVTELubiquitination[6]
247ELRTMIYKDVPENLHacetylation[3, 4, 5, 7]
247ELRTMIYKDVPENLHsuccinylation[7]
255DVPENLHKMAEHNLLacetylation[3, 5]
270LHLRKLEKDGKIFYTacetylation[3]
273RKLEKDGKIFYTTTPacetylation[7]
273RKLEKDGKIFYTTTPsuccinylation[7]
273RKLEKDGKIFYTTTPubiquitination[6]
282FYTTTPVKKWKAVL*acetylation[4, 5, 7]
282FYTTTPVKKWKAVL*succinylation[7]
282FYTTTPVKKWKAVL*ubiquitination[6]
Reference
 [1] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] 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]
 [4] 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]
 [5] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [6] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [7] 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
Functional Description
  
Sequence Annotation
 METAL 77 77 Zinc 1 (By similarity).
 METAL 79 79 Zinc 1 (By similarity).
 METAL 81 81 Zinc 2 (By similarity).
 METAL 82 82 Zinc 2 (By similarity).
 METAL 145 145 Zinc 1 (By similarity).
 METAL 164 164 Zinc 1 (By similarity).
 METAL 164 164 Zinc 2 (By similarity).
 METAL 199 199 Zinc 2 (By similarity).
 MOD_RES 102 102 N6-acetyllysine.  
Keyword
 Acetylation; Complete proteome; Hydrolase; Metal-binding; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 288 AA 
Protein Sequence
MAAALQRIEQ LSSRVVRVLG CNPGPMTLQG TNTYLVGTGS RRILIDTGEP SVPEYISCLK 60
QALVEFDTAI QEILVTHWHS DHSGGIVDIC KNINNDTTYC IKKLRRNPQR EEIIGNGEQQ 120
FIYIENGDVV KTEGATLRVL YTPGHTDDHM ALLLEEENAI FSGDCILGEG TTIFEDLYDY 180
MNSLNNLLKI KANIIYPGHG PVIHNAEAKI LEYISHRNNR EEQIISLFRD NFEKSFTVTE 240
LRTMIYKDVP ENLHKMAEHN LLLHLRKLEK DGKIFYTTTP VKKWKAVL 288 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 
Interpro
 IPR001279; Beta-lactamas-like. 
Pfam
 PF00753; Lactamase_B 
SMART
 SM00849; Lactamase_B 
PROSITE
  
PRINTS