CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001780
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Aspartate aminotransferase, mitochondrial 
Protein Synonyms/Alias
 mAspAT; Fatty acid-binding protein; FABP-1; Glutamate oxaloacetate transaminase 2; Kynurenine aminotransferase 4; Kynurenine aminotransferase IV; Kynurenine--oxoglutarate transaminase 4; Kynurenine--oxoglutarate transaminase IV; Plasma membrane-associated fatty acid-binding protein; FABPpm; Transaminase A 
Gene Name
 GOT2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
73AYRDDNGKPYVLPSVacetylation[1]
90AEAQIAAKNLDKEYLacetylation[1, 2, 3]
90AEAQIAAKNLDKEYLubiquitination[4, 5]
94IAAKNLDKEYLPIGGubiquitination[6]
107GGLAEFCKASAELALubiquitination[7]
122GENSEVLKSGRFVTVacetylation[3]
122GENSEVLKSGRFVTVubiquitination[4, 5, 8]
150SFLQRFFKFSRDVFLacetylation[1, 9]
159SRDVFLPKPTWGNHTacetylation[1]
234KEIATVVKKRNLFAFacetylation[1]
296GAFTMVCKDADEAKRacetylation[1]
296GAFTMVCKDADEAKRubiquitination[6]
309KRVESQLKILIRPMYacetylation[9]
338LNTPDLRKQWLQEVKubiquitination[6]
363TQLVSNLKKEGSTHNubiquitination[6]
396EQVERLIKEFSIYMTacetylation[1]
396EQVERLIKEFSIYMTubiquitination[8]
404EFSIYMTKDGRISVAacetylation[1]
404EFSIYMTKDGRISVAubiquitination[10]
Reference
 [1] 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]
 [2] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [3] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [5] 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]
 [6] 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]
 [7] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [8] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [9] 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]
 [10] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 
Functional Description
 Catalyzes the irreversible transamination of the L- tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol. Facilitates cellular uptake of long-chain free fatty acids. 
Sequence Annotation
 BINDING 65 65 Substrate; via amide nitrogen (By
 BINDING 162 162 Substrate (By similarity).
 BINDING 215 215 Substrate (By similarity).
 BINDING 407 407 Substrate (By similarity).
 MOD_RES 73 73 N6-acetyllysine.
 MOD_RES 90 90 N6-acetyllysine.
 MOD_RES 94 94 N6-acetyllysine (By similarity).
 MOD_RES 96 96 Nitrated tyrosine (By similarity).
 MOD_RES 159 159 N6-acetyllysine.
 MOD_RES 185 185 N6-acetyllysine (By similarity).
 MOD_RES 234 234 N6-acetyllysine.
 MOD_RES 279 279 N6-(pyridoxal phosphate)lysine (By
 MOD_RES 296 296 N6-acetyllysine.
 MOD_RES 309 309 N6-succinyllysine (By similarity).
 MOD_RES 345 345 N6-acetyllysine (By similarity).
 MOD_RES 363 363 N6-acetyllysine (By similarity).
 MOD_RES 396 396 N6-acetyllysine.
 MOD_RES 404 404 N6-acetyllysine.  
Keyword
 Acetylation; Aminotransferase; Cell membrane; Complete proteome; Direct protein sequencing; Lipid transport; Membrane; Mitochondrion; Nitration; Polymorphism; Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 430 AA 
Protein Sequence
MALLHSGRVL PGIAAAFHPG LAAAASARAS SWWTHVEMGP PDPILGVTEA FKRDTNSKKM 60
NLGVGAYRDD NGKPYVLPSV RKAEAQIAAK NLDKEYLPIG GLAEFCKASA ELALGENSEV 120
LKSGRFVTVQ TISGTGALRI GASFLQRFFK FSRDVFLPKP TWGNHTPIFR DAGMQLQGYR 180
YYDPKTCGFD FTGAVEDISK IPEQSVLLLH ACAHNPTGVD PRPEQWKEIA TVVKKRNLFA 240
FFDMAYQGFA SGDGDKDAWA VRHFIEQGIN VCLCQSYAKN MGLYGERVGA FTMVCKDADE 300
AKRVESQLKI LIRPMYSNPP LNGARIAAAI LNTPDLRKQW LQEVKVMADR IIGMRTQLVS 360
NLKKEGSTHN WQHITDQIGM FCFTGLKPEQ VERLIKEFSI YMTKDGRISV AGVTSSNVGY 420
LAHAIHQVTK 430 
Gene Ontology
 GO:0005743; C:mitochondrial inner membrane; IEA:Compara.
 GO:0005759; C:mitochondrial matrix; TAS:Reactome.
 GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO:0016212; F:kynurenine-oxoglutarate transaminase activity; IEA:EC.
 GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IDA:UniProtKB.
 GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:EC.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
 GO:0019470; P:4-hydroxyproline catabolic process; TAS:BHF-UCL.
 GO:0006532; P:aspartate biosynthetic process; IEA:Compara.
 GO:0006533; P:aspartate catabolic process; IDA:UniProtKB.
 GO:0008652; P:cellular amino acid biosynthetic process; TAS:Reactome.
 GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
 GO:0015908; P:fatty acid transport; IEP:UniProtKB.
 GO:0006094; P:gluconeogenesis; TAS:Reactome.
 GO:0019551; P:glutamate catabolic process to 2-oxoglutarate; IEA:Compara.
 GO:0019550; P:glutamate catabolic process to aspartate; IEA:Compara.
 GO:0006536; P:glutamate metabolic process; ISS:UniProtKB.
 GO:0006107; P:oxaloacetate metabolic process; IEA:Compara.
 GO:0045471; P:response to ethanol; IDA:UniProtKB. 
Interpro
 IPR004839; Aminotransferase_I/II.
 IPR000796; Asp_trans.
 IPR004838; NHTrfase_class1_PyrdxlP-BS.
 IPR015424; PyrdxlP-dep_Trfase.
 IPR015421; PyrdxlP-dep_Trfase_major_sub1. 
Pfam
 PF00155; Aminotran_1_2 
SMART
  
PROSITE
 PS00105; AA_TRANSFER_CLASS_1 
PRINTS
 PR00799; TRANSAMINASE.