UniProt Accession

 DHE3_MOUSE; P26443; Q8C273 

Genbank Protein ID

 X57024; AK089152; BC052724; BC057347 

Genbank Nucleotide ID

 CAA40341.1; BAC40767.1; AAH52724.1; AAH57347.1 

Protein Name

 Glutamate dehydrogenase 1, mitochondrial 

Protein Synonyms/Alias

 GDH 1 

Gene Name

 Glud1 

Gene Synonyms/Alias

 Glud 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
68	EDDPNFFKMVEGFFD	acetylation	[1, 2, 3]
68	EDDPNFFKMVEGFFD	succinylation	[3]
84	GASIVEDKLVEDLKT	acetylation	[1, 2, 3, 4, 5, 6, 7, 8, 9, 10]
84	GASIVEDKLVEDLKT	succinylation	[3]
90	DKLVEDLKTRESEEQ	acetylation	[1, 2, 3, 5, 6, 7, 8, 9, 10, 11, 12]
90	DKLVEDLKTRESEEQ	succinylation	[3]
90	DKLVEDLKTRESEEQ	ubiquitination	[13]
98	TRESEEQKRNRVRGI	acetylation	[8, 10]
110	RGILRIIKPCNHVLS	acetylation	[2, 7, 8, 10]
147	SQHRTPCKGGIRYST	acetylation	[3]
147	SQHRTPCKGGIRYST	succinylation	[3]
147	SQHRTPCKGGIRYST	ubiquitination	[13]
162	DVSVDEVKALASLMT	acetylation	[1, 2, 3, 6, 8, 10, 12]
162	DVSVDEVKALASLMT	succinylation	[3]
162	DVSVDEVKALASLMT	ubiquitination	[13]
171	LASLMTYKCAVVDVP	acetylation	[2, 10]
171	LASLMTYKCAVVDVP	ubiquitination	[13]
183	DVPFGGAKAGVKINP	acetylation	[3, 8, 10]
183	DVPFGGAKAGVKINP	succinylation	[3]
183	DVPFGGAKAGVKINP	ubiquitination	[13]
187	GGAKAGVKINPKNYT	acetylation	[2, 3, 8, 10]
187	GGAKAGVKINPKNYT	succinylation	[3]
191	AGVKINPKNYTDNEL	acetylation	[1, 2, 3, 8, 10]
191	AGVKINPKNYTDNEL	succinylation	[3]
191	AGVKINPKNYTDNEL	ubiquitination	[13]
200	YTDNELEKITRRFTM	acetylation	[2, 3, 6, 7, 8, 10, 12]
200	YTDNELEKITRRFTM	succinylation	[3]
200	YTDNELEKITRRFTM	ubiquitination	[13]
211	RFTMELAKKGFIGPG	acetylation	[2, 3, 10]
211	RFTMELAKKGFIGPG	succinylation	[3]
212	FTMELAKKGFIGPGI	ubiquitination	[13]
326	YLHRFGAKCVGVGES	acetylation	[8]
326	YLHRFGAKCVGVGES	ubiquitination	[13]
352	PKELEDFKLQHGSIL	acetylation	[8]
352	PKELEDFKLQHGSIL	ubiquitination	[13]
363	GSILGFPKAKVYEGS	acetylation	[8]
363	GSILGFPKAKVYEGS	ubiquitination	[13]
390	ASEKQLTKSNAPRVK	acetylation	[8]
397	KSNAPRVKAKIIAEG	acetylation	[8]
399	NAPRVKAKIIAEGAN	acetylation	[8]
399	NAPRVKAKIIAEGAN	ubiquitination	[13]
415	PTTPEADKIFLERNI	acetylation	[8]
415	PTTPEADKIFLERNI	ubiquitination	[13]
444	VSYFEWLKNLNHVSY	acetylation	[2]
457	SYGRLTFKYERDSNY	acetylation	[1, 2, 5, 6, 7]
457	SYGRLTFKYERDSNY	ubiquitination	[13]
477	VQESLERKFGKHGGT	acetylation	[2, 3, 7, 11]
477	VQESLERKFGKHGGT	succinylation	[3]
477	VQESLERKFGKHGGT	ubiquitination	[13]
480	SLERKFGKHGGTIPV	acetylation	[2, 3, 7, 8, 10]
480	SLERKFGKHGGTIPV	succinylation	[3]
480	SLERKFGKHGGTIPV	ubiquitination	[13]
503	RISGASEKDIVHSGL	acetylation	[1, 2, 3, 4, 6, 7, 8, 9, 10, 12]
503	RISGASEKDIVHSGL	phosphoglycerylation	[14]
503	RISGASEKDIVHSGL	succinylation	[3]
503	RISGASEKDIVHSGL	ubiquitination	[13]
527	QIMRTAMKYNLGLDL	acetylation	[1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12]
527	QIMRTAMKYNLGLDL	succinylation	[3]
545	AYVNAIEKVFKVYNE	acetylation	[1, 2, 3, 5, 6, 7, 8, 9, 10]
545	AYVNAIEKVFKVYNE	succinylation	[3]
545	AYVNAIEKVFKVYNE	ubiquitination	[13]
548	NAIEKVFKVYNEAGV	acetylation	[1, 2, 10]

Reference

 [1] 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]
 [2] 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]
 [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] 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]
 [5] 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]
 [6] 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]
 [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] 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]
 [11] Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation.
 Lombard DB, Alt FW, Cheng HL, Bunkenborg J, Streeper RS, Mostoslavsky R, Kim J, Yancopoulos G, Valenzuela D, Murphy A, Yang Y, Chen Y, Hirschey MD, Bronson RT, Haigis M, Guarente LP, Farese RV Jr, Weissman S, Verdin E, Schwer B.
 Mol Cell Biol. 2007 Dec;27(24):8807-14. [PMID: 17923681]
 [12] 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]
 [13] 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]
 [14] Functional lysine modification by an intrinsically reactive primary glycolytic metabolite.
 Moellering RE, Cravatt BF.
 Science. 2013 Aug 2;341(6145):549-53. [PMID: 23908237] 

Functional Description

 May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (By similarity). 

Sequence Annotation

 NP_BIND 141 143 NAD (By similarity).
 ACT_SITE 183 183 By similarity.
 BINDING 147 147 Substrate (By similarity).
 BINDING 171 171 Substrate (By similarity).
 BINDING 176 176 NAD (By similarity).
 BINDING 252 252 NAD (By similarity).
 BINDING 266 266 GTP (By similarity).
 BINDING 270 270 GTP (By similarity).
 BINDING 319 319 GTP (By similarity).
 BINDING 322 322 GTP (By similarity).
 BINDING 438 438 Substrate (By similarity).
 BINDING 444 444 NAD (By similarity).
 BINDING 450 450 ADP (By similarity).
 BINDING 516 516 ADP (By similarity).
 MOD_RES 84 84 N6-acetyllysine; alternate (Probable).
 MOD_RES 84 84 N6-succinyllysine; alternate (By
 MOD_RES 90 90 N6-acetyllysine (By similarity).
 MOD_RES 110 110 N6-acetyllysine; alternate (By
 MOD_RES 110 110 N6-succinyllysine; alternate (By
 MOD_RES 135 135 Phosphotyrosine.
 MOD_RES 162 162 N6-acetyllysine; alternate (By
 MOD_RES 162 162 N6-succinyllysine; alternate (By
 MOD_RES 172 172 ADP-ribosylcysteine (By similarity).
 MOD_RES 183 183 N6-acetyllysine (By similarity).
 MOD_RES 191 191 N6-acetyllysine (By similarity).
 MOD_RES 227 227 Phosphoserine.
 MOD_RES 363 363 N6-acetyllysine; alternate (By
 MOD_RES 363 363 N6-succinyllysine; alternate (By
 MOD_RES 365 365 N6-acetyllysine (By similarity).
 MOD_RES 386 386 N6-acetyllysine (By similarity).
 MOD_RES 399 399 N6-acetyllysine (By similarity).
 MOD_RES 415 415 N6-acetyllysine; alternate (By
 MOD_RES 415 415 N6-succinyllysine; alternate (By
 MOD_RES 450 450 Phosphoserine.
 MOD_RES 457 457 N6-acetyllysine; alternate (By
 MOD_RES 457 457 N6-malonyllysine; alternate (By
 MOD_RES 457 457 N6-succinyllysine; alternate (By
 MOD_RES 480 480 N6-acetyllysine (By similarity).
 MOD_RES 503 503 N6-acetyllysine; alternate (Probable).
 MOD_RES 503 503 N6-malonyllysine; alternate (By
 MOD_RES 503 503 N6-succinyllysine; alternate (By
 MOD_RES 512 512 Phosphotyrosine.
 MOD_RES 527 527 N6-acetyllysine; alternate (Probable).
 MOD_RES 527 527 N6-malonyllysine; alternate (By
 MOD_RES 527 527 N6-succinyllysine; alternate (By
 MOD_RES 545 545 N6-acetyllysine; alternate (By
 MOD_RES 545 545 N6-succinyllysine; alternate (By  

Keyword

 Acetylation; ADP-ribosylation; ATP-binding; Complete proteome; Direct protein sequencing; GTP-binding; Mitochondrion; NADP; Nucleotide-binding; Oxidoreductase; Phosphoprotein; Reference proteome; Transit peptide. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 558 AA 

Protein Sequence

Gene Ontology

 GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
 GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IEA:Compara.
 GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IDA:MGI.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
 GO:0007616; P:long-term memory; IEA:Compara.
 GO:0032024; P:positive regulation of insulin secretion; IGI:MGI.
 GO:0010044; P:response to aluminum ion; IEA:Compara. 

Interpro

 IPR006095; Glu/Leu/Phe/Val_DH.
 IPR006096; Glu/Leu/Phe/Val_DH_C.
 IPR006097; Glu/Leu/Phe/Val_DH_dimer_dom.
 IPR016040; NAD(P)-bd_dom. 

Pfam

 PF00208; ELFV_dehydrog
 PF02812; ELFV_dehydrog_N 

SMART

 SM00839; ELFV_dehydrog 

PROSITE

 PS00074; GLFV_DEHYDROGENASE 

PRINTS

 PR00082; GLFDHDRGNASE.