UniProt Accession

 AATM_MOUSE; P05202; O09188; Q3TIP6; Q3UD91; Q5HZH5 

Genbank Protein ID

 J02622; X06917; X06918; X06919; X06920; X06921; X06922; X06923; X06924; X06925; X06926; M37259; M37250; M37251; M37252; M37253; M37254; M37255; M37256; M37258; U82470; AK136556; AK147953; AK149886; AK149926; AK150194; AK152921; AK155075; AK167767; BC089015; BC089341 

Genbank Nucleotide ID

 AAA37264.1; CAA30015.1; CAA30015.1; CAA30015.1; CAA30015.1; CAA30015.1; CAA30015.1; CAA30015.1; CAA30015.1; CAA30015.1; CAA30015.1; AAA37265.1; AAA37265.1; AAA37265.1; AAA37265.1; AAA37265.1; AAA37265.1; AAA37265.1; AAA37265.1; AAA37265.1; AAB91426.1; BAE23042.1; BAE28248.1; BAE29146.1; BAE29171.1; BAE29370.1; BAE31596.1; BAE33029.1; BAE39800.1; AAH89015.1; AAH89341.1 

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

 Got-2 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
52	LGVTEAFKRDTNSKK	acetylation	[1]
58	FKRDTNSKKMNLGVG	acetylation	[2]
59	KRDTNSKKMNLGVGA	acetylation	[1, 3]
59	KRDTNSKKMNLGVGA	succinylation	[3]
73	AYRDDNGKPYVLPSV	acetylation	[1, 2, 3, 4, 5, 6, 7, 8, 9]
73	AYRDDNGKPYVLPSV	succinylation	[3]
73	AYRDDNGKPYVLPSV	ubiquitination	[10]
82	YVLPSVRKAEAQIAA	acetylation	[1]
90	AEAQIAAKNLDKEYL	acetylation	[1, 2, 3, 6, 8, 11]
90	AEAQIAAKNLDKEYL	succinylation	[3]
90	AEAQIAAKNLDKEYL	ubiquitination	[10]
94	IAAKNLDKEYLPIGG	acetylation	[7, 8, 12]
107	GGLAEFCKASAELAL	acetylation	[1, 2, 3, 4, 6]
107	GGLAEFCKASAELAL	succinylation	[3]
122	GENNEVLKSGRFVTV	acetylation	[1, 2, 3, 6, 8, 9]
122	GENNEVLKSGRFVTV	succinylation	[3]
122	GENNEVLKSGRFVTV	ubiquitination	[10]
150	SFLQRFFKFSRDVFL	acetylation	[1, 2, 5]
159	SRDVFLPKPSWGNHT	acetylation	[1, 2, 3, 5, 6, 8, 9, 12]
159	SRDVFLPKPSWGNHT	succinylation	[3]
185	GYRYYDPKTCGFDFS	acetylation	[1, 2, 3, 6, 7, 8, 12]
185	GYRYYDPKTCGFDFS	succinylation	[3]
227	DPRPEQWKEIASVVK	acetylation	[1, 2, 3, 6]
227	DPRPEQWKEIASVVK	succinylation	[3]
234	KEIASVVKKKNLFAF	acetylation	[1, 2, 3, 8]
234	KEIASVVKKKNLFAF	succinylation	[3]
235	EIASVVKKKNLFAFF	acetylation	[1]
279	CLCQSYAKNMGLYGE	acetylation	[1]
296	GAFTVVCKDAEEAKR	acetylation	[1, 2, 3, 5, 6, 8, 12]
296	GAFTVVCKDAEEAKR	succinylation	[3]
302	CKDAEEAKRVESQLK	acetylation	[1, 2, 6, 7, 8, 9]
302	CKDAEEAKRVESQLK	ubiquitination	[10]
309	KRVESQLKILIRPLY	acetylation	[1, 2, 3, 5, 6, 7, 8]
309	KRVESQLKILIRPLY	succinylation	[3]
338	LTSPDLRKQWLQEVK	acetylation	[1, 3, 6, 7]
338	LTSPDLRKQWLQEVK	succinylation	[3]
345	KQWLQEVKGMADRII	acetylation	[1, 2, 3, 6, 7, 8, 12]
345	KQWLQEVKGMADRII	succinylation	[3]
345	KQWLQEVKGMADRII	ubiquitination	[10]
363	TQLVSNLKKEGSSHN	acetylation	[1, 2, 3, 6, 7, 8, 12]
363	TQLVSNLKKEGSSHN	succinylation	[3]
363	TQLVSNLKKEGSSHN	ubiquitination	[10]
364	QLVSNLKKEGSSHNW	acetylation	[1]
387	MFCFTGLKPEQVERL	acetylation	[1, 2]
396	EQVERLTKEFSVYMT	acetylation	[1, 2, 3, 6, 7, 8]
396	EQVERLTKEFSVYMT	succinylation	[3]
396	EQVERLTKEFSVYMT	ubiquitination	[10]
404	EFSVYMTKDGRISVA	acetylation	[1, 2, 3, 5, 6, 7, 8, 9, 13]
404	EFSVYMTKDGRISVA	succinylation	[3]
404	EFSVYMTKDGRISVA	ubiquitination	[10]
430	HAIHQVTK*******	acetylation	[2]

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] 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]
 [3] 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]
 [4] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
 [5] Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice.
 Fritz KS, Galligan JJ, Hirschey MD, Verdin E, Petersen DR.
 J Proteome Res. 2012 Mar 2;11(3):1633-43. [PMID: 22309199]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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]
 [11] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [12] 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]
 [13] 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] 

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.
 BINDING 407 407 Substrate.
 MOD_RES 73 73 N6-acetyllysine (By similarity).
 MOD_RES 90 90 N6-acetyllysine (By similarity).
 MOD_RES 94 94 N6-acetyllysine.
 MOD_RES 96 96 Nitrated tyrosine.
 MOD_RES 159 159 N6-acetyllysine.
 MOD_RES 185 185 N6-acetyllysine.
 MOD_RES 234 234 N6-acetyllysine (By similarity).
 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.
 MOD_RES 363 363 N6-acetyllysine.
 MOD_RES 396 396 N6-acetyllysine (By similarity).
 MOD_RES 404 404 N6-acetyllysine (By similarity).  

Keyword

 3D-structure; Acetylation; Aminotransferase; Cell membrane; Complete proteome; Direct protein sequencing; Lipid transport; Membrane; Mitochondrion; Nitration; Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide; Transport. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 430 AA 

Protein Sequence

Gene Ontology

 GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
 GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0016212; F:kynurenine-oxoglutarate transaminase activity; IEA:EC.
 GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; ISS:UniProtKB.
 GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:EC.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0006532; P:aspartate biosynthetic process; IDA:MGI.
 GO:0006533; P:aspartate catabolic process; IEA:Compara.
 GO:0015908; P:fatty acid transport; IEA:Compara.
 GO:0019551; P:glutamate catabolic process to 2-oxoglutarate; IDA:MGI.
 GO:0019550; P:glutamate catabolic process to aspartate; IDA:MGI.
 GO:0006107; P:oxaloacetate metabolic process; IDA:MGI.
 GO:0045471; P:response to ethanol; IEA:Compara. 

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.