UniProt Accession

 CLYBL_MOUSE; Q8R4N0; Q9D7D0 

Genbank Protein ID

 AF428254; AK009345; BC023398 

Genbank Nucleotide ID

 AAL84704.1; BAB26232.1; AAH23398.1 

Protein Name

 Citrate lyase subunit beta-like protein, mitochondrial 

Protein Synonyms/Alias

 Citrate lyase beta-like 

Gene Name

 Clybl 

Gene Synonyms/Alias

 Clb 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
39	YSSLSNHKYVPRRAV	acetylation	[1]
55	YVPGNDEKKIRKIPS	acetylation	[1, 2, 3, 4, 5]
55	YVPGNDEKKIRKIPS	succinylation	[4]
59	NDEKKIRKIPSLKVD	acetylation	[1, 3]
64	IRKIPSLKVDCAVLD	acetylation	[1, 3, 5]
80	EDGVAENKKNEARLR	acetylation	[1, 2, 3, 4, 5]
80	EDGVAENKKNEARLR	succinylation	[4]
90	EARLRIAKTLEDFDL	acetylation	[1, 3, 4, 5]
90	EARLRIAKTLEDFDL	succinylation	[4]
102	FDLGTTEKCVRINSV	acetylation	[5]
215	SIGATSNKDTQDILY	acetylation	[3, 5]
300	EELIAAFKEHQQLGK	acetylation	[1]
307	KEHQQLGKGAFTFRG	acetylation	[1, 3, 4, 5]
307	KEHQQLGKGAFTFRG	succinylation	[4]

Reference

 [1] 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]
 [2] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [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] 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]
 [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] 

Functional Description

  

Sequence Annotation

 METAL 169 169 Magnesium (By similarity).
 METAL 204 204 Magnesium (By similarity).
 BINDING 105 105 Substrate (By similarity).
 BINDING 169 169 Substrate (By similarity).  

Keyword

 Complete proteome; Lyase; Magnesium; Metal-binding; Mitochondrion; Reference proteome; Transit peptide. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 338 AA 

Protein Sequence

Gene Ontology

 GO:0009346; C:citrate lyase complex; IEA:InterPro.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0008815; F:citrate (pro-3S)-lyase activity; IEA:InterPro.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006725; P:cellular aromatic compound metabolic process; IEA:InterPro. 

Interpro

 IPR005000; Aldehyde-lyase_domain.
 IPR011206; Citrate_lyase_beta.
 IPR015813; Pyrv/PenolPyrv_Kinase-like_dom. 

Pfam

 PF03328; HpcH_HpaI 

SMART

  

PROSITE

  

PRINTS