CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019882
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Alpha-aminoadipic semialdehyde synthase, mitochondrial 
Protein Synonyms/Alias
 LKR/SDH; Lysine ketoglutarate reductase; LKR; LOR; Saccharopine dehydrogenase; SDH 
Gene Name
 Aass 
Gene Synonyms/Alias
 Lorsdh 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
23LSRGLHHKPVMALRRacetylation[1]
45RRAPLAPKHIKGITKacetylation[2, 3]
48PLAPKHIKGITKLGYacetylation[1, 2, 3]
52KHIKGITKLGYKVLIacetylation[1, 2, 3, 4, 5]
52KHIKGITKLGYKVLIsuccinylation[5]
56GITKLGYKVLIQPSNacetylation[1, 2, 3, 5]
56GITKLGYKVLIQPSNsuccinylation[5]
70NRRAIHDKEYVRAGGacetylation[1, 2, 3, 5]
70NRRAIHDKEYVRAGGsuccinylation[5]
93ACLILGVKRPPEEKLacetylation[1, 5]
93ACLILGVKRPPEEKLsuccinylation[5]
99VKRPPEEKLMSKKTYacetylation[2, 3]
104EEKLMSKKTYAFFSHacetylation[1]
128NLLDEVLKQEIRLIDacetylation[1, 2, 3]
128NLLDEVLKQEIRLIDubiquitination[6]
138IRLIDYEKMVDHRGSacetylation[1, 2, 3, 4, 5, 7, 8]
138IRLIDYEKMVDHRGSsuccinylation[5]
253HELREVSKTGDLRKVacetylation[2, 3, 5]
253HELREVSKTGDLRKVsuccinylation[5]
259SKTGDLRKVYGTVLSacetylation[1]
259SKTGDLRKVYGTVLSubiquitination[6]
274RHHHLVRKTDGVYDPacetylation[2, 5]
274RHHHLVRKTDGVYDPsuccinylation[5]
286YDPVEYEKYPERYTSacetylation[1, 2, 3, 4, 5, 7, 8]
286YDPVEYEKYPERYTSsuccinylation[5]
333QSLLVPVKSSVVPVEacetylation[5]
333QSLLVPVKSSVVPVEsuccinylation[5]
458SNGLLTDKYKYIQKLacetylation[1, 2, 3, 4, 5, 7]
458SNGLLTDKYKYIQKLsuccinylation[5]
458SNGLLTDKYKYIQKLubiquitination[6]
460GLLTDKYKYIQKLREacetylation[1, 2, 3]
464DKYKYIQKLRESRERacetylation[2]
523QMQQLSKKYNINPVSacetylation[2]
535PVSLTVGKQEAKLQSacetylation[2]
584SYITPAMKELEKSVDacetylation[2]
707YPNRDSIKYAEIYGIacetylation[1, 2, 3, 4, 5]
707YPNRDSIKYAEIYGIsuccinylation[5]
707YPNRDSIKYAEIYGIubiquitination[6]
732LRYKGYSKALNGFVKacetylation[2, 3, 5]
732LRYKGYSKALNGFVKsuccinylation[5]
732LRYKGYSKALNGFVKubiquitination[6]
739KALNGFVKLGLINREacetylation[1]
739KALNGFVKLGLINREubiquitination[6]
761EANPLTWKQLLCDLVacetylation[1, 4, 5]
761EANPLTWKQLLCDLVsuccinylation[5]
778SRSSPCEKLKEVVFTacetylation[1, 2, 3, 5]
778SRSSPCEKLKEVVFTsuccinylation[5]
778SRSSPCEKLKEVVFTubiquitination[6]
780SSPCEKLKEVVFTKLacetylation[1, 2, 3, 4, 5]
780SSPCEKLKEVVFTKLsuccinylation[5]
820SIVDAFSKHLVSKLSacetylation[4]
825FSKHLVSKLSYGPEEubiquitination[6]
833LSYGPEEKDMIVMRDubiquitination[6]
901GLMGPFTKEIYGPILacetylation[2]
901GLMGPFTKEIYGPILubiquitination[6]
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] 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]
 [3] 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]
 [4] 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]
 [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] 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]
 [7] 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]
 [8] 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
 Bifunctional enzyme that catalyzes the first two steps in lysine degradation. The N-terminal and the C-terminal contain lysine-oxoglutarate reductase and saccharopine dehydrogenase activity, respectively. 
Sequence Annotation
 REGION 33 455 Lysine-ketoglutarate reductase.
 REGION 477 926 Saccharopine dehydrogenase.  
Keyword
 Complete proteome; Mitochondrion; Multifunctional enzyme; NAD; NADP; Oxidoreductase; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 926 AA 
Protein Sequence
MLRAQRPRLA RLRACLSRGL HHKPVMALRR EDVNAWERRA PLAPKHIKGI TKLGYKVLIQ 60
PSNRRAIHDK EYVRAGGILQ EDITEACLIL GVKRPPEEKL MSKKTYAFFS HTIKAQEANM 120
NLLDEVLKQE IRLIDYEKMV DHRGSRIVAF GQWAGVAGMI NILHGMGLRL LALGHHTPFM 180
HLGMAHNYRN SSQAVQAVRD AGYEISLGLM PKSIGPLTFV FTGTGNVSKG AQEVFNELPC 240
EYVEPHELRE VSKTGDLRKV YGTVLSRHHH LVRKTDGVYD PVEYEKYPER YTSRFNTDIA 300
PYTTCLINGI YWEQNTPRLL TRQDAQSLLV PVKSSVVPVE GCPELPHKLV AICDISADTG 360
GSIDFMTECT TIERPFCMYD ADQQIIHDSV EGSGILMCSI DNLPAQLPIE ATEYFGDMLY 420
PYVEEMLLSD ASQPLESQNF SPVVRDAVIT SNGLLTDKYK YIQKLRESRE RIQFLSMSTK 480
KKVLVLGSGY VSGPVLEYLS RDNNIEITLG SDMTNQMQQL SKKYNINPVS LTVGKQEAKL 540
QSLVESQDLV ISLLPYVLHP VVAKACIESR VNMVTASYIT PAMKELEKSV DDAGITVIGE 600
LGLDPGLDHM LAMETIDTAK ELGATVESYV SYCGGLPAPE HSDNPLRYKF SWSPVGVLMN 660
IMQPASYLLN GKVVNVTGGV SFLNSVTPMD YFPGLNLEGY PNRDSIKYAE IYGISSAHTL 720
LRGTLRYKGY SKALNGFVKL GLINREAYPA LRPEANPLTW KQLLCDLVGI SRSSPCEKLK 780
EVVFTKLGGD NTQLEAAEWL GLLGDEQVPQ AESIVDAFSK HLVSKLSYGP EEKDMIVMRD 840
SFGIRHPSGH LENKTIDLVV YGDFNGFSAM AKTVGLPTAM AAKMLLDGEI EAKGLMGPFT 900
KEIYGPILER IKAEGIVFNT QSTIKL 926 
Gene Ontology
 GO:0005739; C:mitochondrion; TAS:UniProtKB.
 GO:0047131; F:saccharopine dehydrogenase (NAD+, L-glutamate-forming) activity; IDA:UniProtKB.
 GO:0047130; F:saccharopine dehydrogenase (NADP+, L-lysine-forming) activity; IEA:EC.
 GO:0006091; P:generation of precursor metabolites and energy; TAS:UniProtKB.
 GO:0019477; P:L-lysine catabolic process; IDA:MGI.
 GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway. 
Interpro
 IPR007886; AlaDH/PNT_N.
 IPR007698; AlaDH/PNT_NAD(H)-bd.
 IPR016040; NAD(P)-bd_dom.
 IPR005097; Saccharopine_DH/HSpermid_syn. 
Pfam
 PF01262; AlaDh_PNT_C
 PF05222; AlaDh_PNT_N
 PF03435; Saccharop_dh 
SMART
 SM01002; AlaDh_PNT_C
 SM01003; AlaDh_PNT_N 
PROSITE
 PS00836; ALADH_PNT_1
 PS00837; ALADH_PNT_2 
PRINTS