CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001750
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glutamate dehydrogenase 1, mitochondrial 
Protein Synonyms/Alias
 GDH 1 
Gene Name
 GLUD1 
Gene Synonyms/Alias
 GLUD 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
84GASIVEDKLVEDLRTacetylation[1, 2, 3]
84GASIVEDKLVEDLRTubiquitination[3, 4, 5, 6, 7]
162DVSVDEVKALASLMTacetylation[8]
162DVSVDEVKALASLMTubiquitination[4, 5, 7]
183DVPFGGAKAGVKINPubiquitination[6]
187GGAKAGVKINPKNYTubiquitination[7]
191AGVKINPKNYTDNELubiquitination[5, 6, 7]
200YTDNELEKITRRFTMubiquitination[5, 6, 7]
211RFTMELAKKGFIGPGubiquitination[5, 7]
212FTMELAKKGFIGPGIubiquitination[5, 6, 7]
326YLHRFGAKCIAVGESubiquitination[6]
352PKELEDFKLQHGSILubiquitination[5, 7]
365ILGFPKAKPYEGSILubiquitination[4, 6]
399NAPRVKAKIIAEGANubiquitination[5, 6, 7]
415PTTPEADKIFLERNIacetylation[1, 8]
415PTTPEADKIFLERNIubiquitination[4, 5, 6, 7]
457SYGRLTFKYERDSNYacetylation[1]
457SYGRLTFKYERDSNYubiquitination[6]
480SLERKFGKHGGTIPIacetylation[1]
480SLERKFGKHGGTIPIubiquitination[7]
503RISGASEKDIVHSGLacetylation[1, 8]
503RISGASEKDIVHSGLubiquitination[5, 6, 7]
527QIMRTAMKYNLGLDLacetylation[1]
527QIMRTAMKYNLGLDLubiquitination[4]
545AYVNAIEKVFKVYNEacetylation[1]
545AYVNAIEKVFKVYNEubiquitination[4, 5, 6, 7]
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 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]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [4] 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]
 [5] 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]
 [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] 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]
 [8] 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
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
 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.
 MOD_RES 84 84 N6-succinyllysine; alternate (By
 MOD_RES 110 110 N6-acetyllysine; alternate (By
 MOD_RES 110 110 N6-succinyllysine; alternate (By
 MOD_RES 135 135 Phosphotyrosine (By similarity).
 MOD_RES 162 162 N6-acetyllysine; alternate (By
 MOD_RES 162 162 N6-succinyllysine; alternate (By
 MOD_RES 172 172 ADP-ribosylcysteine.
 MOD_RES 183 183 N6-acetyllysine (By similarity).
 MOD_RES 191 191 N6-acetyllysine (By similarity).
 MOD_RES 227 227 Phosphoserine (By similarity).
 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 (By similarity).
 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.
 MOD_RES 503 503 N6-acetyllysine; alternate.
 MOD_RES 503 503 N6-malonyllysine; alternate (By
 MOD_RES 503 503 N6-succinyllysine; alternate (By
 MOD_RES 512 512 Phosphotyrosine (By similarity).
 MOD_RES 527 527 N6-acetyllysine; alternate (By
 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
 3D-structure; Acetylation; ADP-ribosylation; ATP-binding; Complete proteome; Direct protein sequencing; Disease mutation; 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
MYRYLGEALL LSRAGPAALG SASADSAALL GWARGQPAAA PQPGLALAAR RHYSEAVADR 60
EDDPNFFKMV EGFFDRGASI VEDKLVEDLR TRESEEQKRN RVRGILRIIK PCNHVLSLSF 120
PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI RYSTDVSVDE VKALASLMTY KCAVVDVPFG 180
GAKAGVKINP KNYTDNELEK ITRRFTMELA KKGFIGPGID VPAPDMSTGE REMSWIADTY 240
ASTIGHYDIN AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFG 300
DKTFVVQGFG NVGLHSMRYL HRFGAKCIAV GESDGSIWNP DGIDPKELED FKLQHGSILG 360
FPKAKPYEGS ILEADCDILI PAASEKQLTK SNAPRVKAKI IAEGANGPTT PEADKIFLER 420
NIMVIPDLYL NAGGVTVSYF EWLKNLNHVS YGRLTFKYER DSNYHLLMSV QESLERKFGK 480
HGGTIPIVPT AEFQDRISGA SEKDIVHSGL AYTMERSARQ IMRTAMKYNL GLDLRTAAYV 540
NAIEKVFKVY NEAGVTFT 558 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; TAS:Reactome.
 GO:0043531; F:ADP binding; IDA:BHF-UCL.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IDA:UniProtKB.
 GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IDA:BHF-UCL.
 GO:0005525; F:GTP binding; IDA:BHF-UCL.
 GO:0042802; F:identical protein binding; TAS:BHF-UCL.
 GO:0070728; F:leucine binding; IDA:BHF-UCL.
 GO:0070403; F:NAD+ binding; IDA:BHF-UCL.
 GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
 GO:0006537; P:glutamate biosynthetic process; IDA:BHF-UCL.
 GO:0006538; P:glutamate catabolic process; IDA:UniProtKB.
 GO:0032024; P:positive regulation of insulin secretion; IMP:BHF-UCL. 
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.