CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021062
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial 
Protein Synonyms/Alias
 MMSDH; Malonate-semialdehyde dehydrogenase [acylating]; Aldehyde dehydrogenase family 6 member A1 
Gene Name
 Aldh6a1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
41SSSVPTVKLFIDGKFacetylation[1]
47VKLFIDGKFVESKSDacetylation[1, 2, 3, 4, 5, 6, 7, 8]
47VKLFIDGKFVESKSDsuccinylation[7]
47VKLFIDGKFVESKSDubiquitination[9]
52DGKFVESKSDKWIDIacetylation[1, 3, 5, 6, 7, 8]
52DGKFVESKSDKWIDIsuccinylation[7]
55FVESKSDKWIDIHNPacetylation[1, 3, 5, 6, 7, 8, 10, 11]
55FVESKSDKWIDIHNPsuccinylation[7]
76GRVPQSTKAEMDAAVacetylation[1, 5, 7, 8]
76GRVPQSTKAEMDAAVsuccinylation[7]
76GRVPQSTKAEMDAAVubiquitination[9]
87DAAVESCKRAFPAWAacetylation[1]
113LRYQQLIKENLKEIAacetylation[1, 3, 5, 8]
113LRYQQLIKENLKEIAubiquitination[9]
117QLIKENLKEIARLITacetylation[1, 5, 6, 7, 8, 10]
117QLIKENLKEIARLITsuccinylation[7]
129LITLEQGKTLADAEGacetylation[1, 3, 5, 7, 8, 12]
129LITLEQGKTLADAEGsuccinylation[7]
129LITLEQGKTLADAEGubiquitination[9]
298VVMPDANKENTLNQLacetylation[1, 5]
330AILVGEAKKWLPELVacetylation[1]
331ILVGEAKKWLPELVDacetylation[1, 10]
331ILVGEAKKWLPELVDubiquitination[9]
364PLITPQAKERVCNLIacetylation[1, 5, 7, 8, 12]
364PLITPQAKERVCNLIsuccinylation[7]
364PLITPQAKERVCNLIubiquitination[9]
376NLIDSGTKEGASILLacetylation[1, 3, 5, 7, 8]
376NLIDSGTKEGASILLsuccinylation[7]
376NLIDSGTKEGASILLubiquitination[9]
391DGRRIKVKGYENGNFacetylation[7]
391DGRRIKVKGYENGNFsuccinylation[7]
391DGRRIKVKGYENGNFubiquitination[9]
408PTIISNVKPSMTCYKubiquitination[9]
500GDTNFYGKQGIQFYTacetylation[1, 8]
500GDTNFYGKQGIQFYTubiquitination[9]
517KTITSQWKEEDATLSacetylation[5, 7, 8]
517KTITSQWKEEDATLSsuccinylation[7]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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]
 [11] 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]
 [12] 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
Functional Description
 Plays a role in valine and pyrimidine metabolism. Binds fatty acyl-CoA (By similarity). 
Sequence Annotation
 NP_BIND 209 213 NAD (Potential).
 NP_BIND 261 266 NAD (Potential).
 ACT_SITE 317 317 Nucleophile (By similarity).
 BINDING 417 417 NAD (Potential).
 MOD_RES 55 55 N6-acetyllysine.
 MOD_RES 117 117 N6-acetyllysine.
 MOD_RES 331 331 N6-acetyllysine.  
Keyword
 Acetylation; Complete proteome; Mitochondrion; NAD; Oxidoreductase; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 535 AA 
Protein Sequence
MAAAVAAAAA MRSRILQVSS KVNATWYPAS SFSSSSVPTV KLFIDGKFVE SKSDKWIDIH 60
NPATNEVVGR VPQSTKAEMD AAVESCKRAF PAWADTSILS RQQVLLRYQQ LIKENLKEIA 120
RLITLEQGKT LADAEGDVFR GLQVVEHACS VTSLMLGETM PSITKDMDLY SYRLPLGVCA 180
GIAPFNFPAM IPLWMFPMAM VCGNTFLMKP SERVPGATML LAKLLQDSGA PDGTLNIIHG 240
QHDAVNFICD HPDIKAISFV GSNQAGEYIF ERGSRNGKRV QANMGAKNHG VVMPDANKEN 300
TLNQLVGAAF GAAGQRCMAL STAILVGEAK KWLPELVDRA KNLRVNAGDQ PGADLGPLIT 360
PQAKERVCNL IDSGTKEGAS ILLDGRRIKV KGYENGNFVG PTIISNVKPS MTCYKEEIFG 420
PVLVVLETET LDEAIKIVND NPYGNGTAIF TTNGATARKY AHMVDVGQVG VNVPIPVPLP 480
MFSFTGSRSS FRGDTNFYGK QGIQFYTQLK TITSQWKEED ATLSSPAVVM PTMGR 535 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0018478; F:malonate-semialdehyde dehydrogenase (acetylating) activity; IEA:EC.
 GO:0004491; F:methylmalonate-semialdehyde dehydrogenase (acylating) activity; IEA:EC.
 GO:0050873; P:brown fat cell differentiation; IDA:MGI. 
Interpro
 IPR016161; Ald_DH/histidinol_DH.
 IPR016163; Ald_DH_C.
 IPR016160; Ald_DH_CS.
 IPR016162; Ald_DH_N.
 IPR015590; Aldehyde_DH_dom.
 IPR010061; MeMal-semiAld_DH. 
Pfam
 PF00171; Aldedh 
SMART
  
PROSITE
 PS00070; ALDEHYDE_DEHYDR_CYS 
PRINTS