CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005687
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Alcohol dehydrogenase class-3 
Protein Synonyms/Alias
 Alcohol dehydrogenase 2; Alcohol dehydrogenase 5; Alcohol dehydrogenase B2; ADH-B2; Alcohol dehydrogenase class-III; Glutathione-dependent formaldehyde dehydrogenase; FALDH; FDH; GSH-FDH; S-(hydroxymethyl)glutathione dehydrogenase 
Gene Name
 Adh5 
Gene Synonyms/Alias
 Adh-2; Adh2 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
9ANQVIRCKAAVAWEAubiquitination[1]
18AVAWEAGKPLSIEEIacetylation[2, 3]
18AVAWEAGKPLSIEEIubiquitination[1]
31EIEVAPPKAHEVRIKacetylation[3]
84GEGVTKLKAGDTVIPacetylation[3]
84GEGVTKLKAGDTVIPubiquitination[1]
107CKFCLNPKTNLCQKIacetylation[3]
107CKFCLNPKTNLCQKIubiquitination[1]
113PKTNLCQKIRVTQGKacetylation[3]
113PKTNLCQKIRVTQGKubiquitination[1]
120KIRVTQGKGLMPDGTacetylation[3]
120KIRVTQGKGLMPDGTubiquitination[1]
168DPSAPLDKVCLLGCGacetylation[3]
226IIGIDINKDKFAKAKacetylation[4, 5]
226IIGIDINKDKFAKAKubiquitination[1]
228GIDINKDKFAKAKEFubiquitination[1]
233KDKFAKAKEFGASECacetylation[3, 4, 6]
233KDKFAKAKEFGASECsuccinylation[6]
233KDKFAKAKEFGASECubiquitination[1]
315LVTGRTWKGTAFGGWacetylation[3, 6]
315LVTGRTWKGTAFGGWsuccinylation[6]
315LVTGRTWKGTAFGGWubiquitination[1]
323GTAFGGWKSVESVPKacetylation[3]
330KSVESVPKLVSEYMSacetylation[2]
330KSVESVPKLVSEYMSubiquitination[1]
338LVSEYMSKKIKVDEFacetylation[3]
338LVSEYMSKKIKVDEFubiquitination[1]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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] 
Functional Description
 Class-III ADH is remarkably ineffective in oxidizing ethanol, but it readily catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione. 
Sequence Annotation
 METAL 45 45 Zinc 1; catalytic (By similarity).
 METAL 67 67 Zinc 1; catalytic (By similarity).
 METAL 97 97 Zinc 2 (By similarity).
 METAL 100 100 Zinc 2 (By similarity).
 METAL 103 103 Zinc 2 (By similarity).
 METAL 111 111 Zinc 2 (By similarity).
 METAL 174 174 Zinc 1; catalytic (By similarity).
 MOD_RES 2 2 N-acetylalanine (By similarity).  
Keyword
 3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 374 AA 
Protein Sequence
MANQVIRCKA AVAWEAGKPL SIEEIEVAPP KAHEVRIKIL ATAVCHTDAY TLSGADPEGC 60
FPVILGHEGA GIVESVGEGV TKLKAGDTVI PLYIPQCGEC KFCLNPKTNL CQKIRVTQGK 120
GLMPDGTSRF TCKGKSVFHF MGTSTFSEYT VVADISVAKI DPSAPLDKVC LLGCGISTGY 180
GAAVNTAKVE PGSTCAVFGL GGVGLAVIMG CKVAGASRII GIDINKDKFA KAKEFGASEC 240
ISPQDFSKSI QEVLVEMTDG GVDYSFECIG NVKVMRSALE AAHKGWGVSV VVGVAASGEE 300
ISTRPFQLVT GRTWKGTAFG GWKSVESVPK LVSEYMSKKI KVDEFVTGNL SFDQINQAFD 360
LMHSGDSIRT VLKM 374 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0004022; F:alcohol dehydrogenase (NAD) activity; IDA:MGI.
 GO:0005504; F:fatty acid binding; IEA:Compara.
 GO:0018467; F:formaldehyde dehydrogenase activity; IEA:Compara.
 GO:0051903; F:S-(hydroxymethyl)glutathione dehydrogenase activity; IMP:MGI.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0007568; P:aging; IEA:Compara.
 GO:0006068; P:ethanol catabolic process; IEA:Compara.
 GO:0006069; P:ethanol oxidation; IEA:InterPro.
 GO:0046294; P:formaldehyde catabolic process; IMP:MGI.
 GO:0018119; P:peptidyl-cysteine S-nitrosylation; IMP:MGI.
 GO:0045777; P:positive regulation of blood pressure; IMP:MGI.
 GO:0003016; P:respiratory system process; IMP:MGI.
 GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
 GO:0051409; P:response to nitrosative stress; IMP:MGI.
 GO:0051775; P:response to redox state; IEA:Compara.
 GO:0001523; P:retinoid metabolic process; IMP:MGI. 
Interpro
 IPR014183; ADH_3.
 IPR013149; ADH_C.
 IPR013154; ADH_GroES-like.
 IPR002085; ADH_SF_Zn-type.
 IPR002328; ADH_Zn_CS.
 IPR011032; GroES-like.
 IPR016040; NAD(P)-bd_dom. 
Pfam
 PF08240; ADH_N
 PF00107; ADH_zinc_N 
SMART
  
PROSITE
 PS00059; ADH_ZINC 
PRINTS