CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013076
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Alanine--glyoxylate aminotransferase 2, mitochondrial 
Protein Synonyms/Alias
 AGT 2; (R)-3-amino-2-methylpropionate--pyruvate transaminase; Beta-ALAAT II; Beta-alanine-pyruvate aminotransferase; D-AIBAT 
Gene Name
 Agxt2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
56PCDFSPEKYQSLAYSacetylation[1]
70SRVLAIHKQHLSPVDacetylation[1]
127PKVSAVAKKQIDRLWacetylation[1]
261APDCCQAKERYIEQFacetylation[1, 2, 3, 4, 5, 6]
261APDCCQAKERYIEQFsuccinylation[5]
261APDCCQAKERYIEQFubiquitination[7]
303QYPKEFLKEAFALVRacetylation[1]
303QYPKEFLKEAFALVRubiquitination[7]
368VTTPEIAKSLAKRLLubiquitination[7]
416VGTYMLLKFAKLRDEacetylation[1]
419YMLLKFAKLRDEFDIacetylation[1]
453ISRQPLPKTEVNQIHacetylation[1]
464NQIHEDCKDMGLLVGacetylation[1]
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] 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] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
 Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
 Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]
 [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] 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]
 [6] 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]
 [7] 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
Functional Description
 Can metabolize asymmetric dimethylarginine (ADMA) via transamination to alpha-keto-delta-(NN-dimethylguanidino) valeric acid (DMGV). ADMA is a potent inhibitor of nitric-oxide (NO) synthase, and this activity provides mechanism through which the kidney regulates blood pressure. 
Sequence Annotation
 MOD_RES 349 349 N6-(pyridoxal phosphate)lysine (By  
Keyword
 Aminotransferase; Complete proteome; Mitochondrion; Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 513 AA 
Protein Sequence
MSLAWRNLQK PFYLETSLRI LQMRPSLSLG ASRIAVPKLT LHTKHSMPPC DFSPEKYQSL 60
AYSRVLAIHK QHLSPVDTAY FRKPLLLHQG HMEWLFDSEG NRYLDFFSGI VTVSVGHCHP 120
KVSAVAKKQI DRLWHTSSVF FHSPMHEYAE KLSALLPEPL KVIFLVNSGS EANDLAMVMA 180
RAHSNHTDII SFRGAYHGCS PYTLGLTNVG IYKMEVPGGI GCQSTMCPDV FRGPWGGIHC 240
RDSPVQTVRD CSCAPDCCQA KERYIEQFKD TLNTSVATSI AGFFAEPIQG VNGVVQYPKE 300
FLKEAFALVR ERGGVCIADE VQTGFGRLGS HFWGFQTHDV LPDIVTMAKG IGNGFPMAAV 360
VTTPEIAKSL AKRLLHFSTF GGNPLACAIG SAVLEVIEEE NLQRNSQEVG TYMLLKFAKL 420
RDEFDIVGDV RGKGLMVGIE MVQDKISRQP LPKTEVNQIH EDCKDMGLLV GRGGNFSQTF 480
RIVPPMCVTK MEVDFAYEVF RAALIQHMER RAK 513 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0047305; F:(R)-3-amino-2-methylpropionate-pyruvate transaminase activity; IEA:EC.
 GO:0008453; F:alanine-glyoxylate transaminase activity; IEA:EC.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0008152; P:metabolic process; IEA:GOC. 
Interpro
 IPR005814; Aminotrans_3.
 IPR015424; PyrdxlP-dep_Trfase.
 IPR015421; PyrdxlP-dep_Trfase_major_sub1.
 IPR015422; PyrdxlP-dep_Trfase_major_sub2. 
Pfam
 PF00202; Aminotran_3 
SMART
  
PROSITE
 PS00600; AA_TRANSFER_CLASS_3 
PRINTS