CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001436
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial 
Protein Synonyms/Alias
 AKB ligase; Aminoacetone synthase; Glycine acetyltransferase 
Gene Name
 Gcat 
Gene Synonyms/Alias
 Kbl 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
42IRGAGTWKSERVITSacetylation[1]
115IHKNLEAKIAHFHQRubiquitination[2]
167IDGIRLCKAHKYRYRacetylation[1]
170IRLCKAHKYRYRHLDacetylation[1]
184DMADLEAKLKEAQKHacetylation[1]
184DMADLEAKLKEAQKHubiquitination[2]
186ADLEAKLKEAQKHRLacetylation[1]
190AKLKEAQKHRLRLVAacetylation[1]
365QMADDMLKKGIFVIGacetylation[1]
366MADDMLKKGIFVIGFacetylation[1]
380FSYPVVPKGKARIRVacetylation[1, 3, 4, 5]
380FSYPVVPKGKARIRVsuccinylation[4]
382YPVVPKGKARIRVQIacetylation[1, 5]
Reference
 [1] 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]
 [2] 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]
 [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]
 [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
 MOD_RES 262 262 N6-(pyridoxal phosphate)lysine  
Keyword
 Acyltransferase; Complete proteome; Mitochondrion; Nucleus; Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 416 AA 
Protein Sequence
MWASFMWHGA LSPGRRAHSA LAQLRCILDS ELEGIRGAGT WKSERVITSR QGPSIRVDGI 60
SGGILNFCAN NYLGLSSHPA VIQAGLQTLE EFGAGLSSTR FICGTQSIHK NLEAKIAHFH 120
QREDAILYPS CFDANAGLFE ALLTPEDAVL SDELNHASII DGIRLCKAHK YRYRHLDMAD 180
LEAKLKEAQK HRLRLVATDG AFSMDGDIAP LQDICRLAAQ YGALVFVDEC HATGFLGPTG 240
RGTDELLGVM DQVTIINSTL GKALGGASGG YTTGPEPLVS LLRQRSRPYL FSNSLPPAVV 300
GCASKALDLL MESNAIIQSM AAKTRRFRSK MEAAGFTVSG ADHPICPVML GDARLSSQMA 360
DDMLKKGIFV IGFSYPVVPK GKARIRVQIS AVHSEEDIDR CVEAFVEVGR LHGALP 416 
Gene Ontology
 GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0008890; F:glycine C-acetyltransferase activity; IEA:EC.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0009058; P:biosynthetic process; IEA:InterPro.
 GO:0019518; P:L-threonine catabolic process to glycine; IEA:UniProtKB-UniPathway. 
Interpro
 IPR011282; 2am3keto_CoA_ligase.
 IPR001917; Aminotrans_II_pyridoxalP_BS.
 IPR004839; Aminotransferase_I/II.
 IPR015424; PyrdxlP-dep_Trfase.
 IPR015421; PyrdxlP-dep_Trfase_major_sub1.
 IPR015422; PyrdxlP-dep_Trfase_major_sub2. 
Pfam
 PF00155; Aminotran_1_2 
SMART
  
PROSITE
 PS00599; AA_TRANSFER_CLASS_2 
PRINTS