CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003969
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Alcohol dehydrogenase class-3 
Protein Synonyms/Alias
 Alcohol dehydrogenase 5; Alcohol dehydrogenase class chi chain; Alcohol dehydrogenase class-III; Glutathione-dependent formaldehyde dehydrogenase; FALDH; FDH; GSH-FDH; S-(hydroxymethyl)glutathione dehydrogenase 
Gene Name
 ADH5 
Gene Synonyms/Alias
 ADHX; FDH 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
7*MANEVIKCKAAVAWubiquitination[1, 2]
9ANEVIKCKAAVAWEAubiquitination[2]
18AVAWEAGKPLSIEEIubiquitination[2]
84GEGVTKLKAGDTVIPubiquitination[2]
101IPQCGECKFCLNPKTubiquitination[2]
107CKFCLNPKTNLCQKIubiquitination[2, 3]
113PKTNLCQKIRVTQGKubiquitination[2, 4, 5]
120KIRVTQGKGLMPDGTubiquitination[2]
226IIGVDINKDKFARAKubiquitination[2]
228GVDINKDKFARAKEFubiquitination[2]
233KDKFARAKEFGATECubiquitination[4, 5]
315LVTGRTWKGTAFGGWubiquitination[1, 2]
323GTAFGGWKSVESVPKubiquitination[2, 4, 5, 6, 7]
339VSEYMSKKIKVDEFVubiquitination[2]
357LSFDEINKAFELMHSacetylation[8]
366FELMHSGKSIRTVVKacetylation[7, 9]
366FELMHSGKSIRTVVKubiquitination[2, 4, 5, 7]
Reference
 [1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [2] 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]
 [3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [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] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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] 
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.
 METAL 67 67 Zinc 1; catalytic.
 METAL 97 97 Zinc 2.
 METAL 100 100 Zinc 2.
 METAL 103 103 Zinc 2.
 METAL 111 111 Zinc 2.
 METAL 174 174 Zinc 1; catalytic.
 MOD_RES 2 2 N-acetylalanine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Metal-binding; NAD; Oxidoreductase; Polymorphism; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 374 AA 
Protein Sequence
MANEVIKCKA AVAWEAGKPL SIEEIEVAPP KAHEVRIKII ATAVCHTDAY TLSGADPEGC 60
FPVILGHEGA GIVESVGEGV TKLKAGDTVI PLYIPQCGEC KFCLNPKTNL CQKIRVTQGK 120
GLMPDGTSRF TCKGKTILHY MGTSTFSEYT VVADISVAKI DPLAPLDKVC LLGCGISTGY 180
GAAVNTAKLE PGSVCAVFGL GGVGLAVIMG CKVAGASRII GVDINKDKFA RAKEFGATEC 240
INPQDFSKPI QEVLIEMTDG GVDYSFECIG NVKVMRAALE ACHKGWGVSV VVGVAASGEE 300
IATRPFQLVT GRTWKGTAFG GWKSVESVPK LVSEYMSKKI KVDEFVTHNL SFDEINKAFE 360
LMHSGKSIRT VVKI 374 
Gene Ontology
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0004022; F:alcohol dehydrogenase (NAD) activity; IEA:EC.
 GO:0009055; F:electron carrier activity; TAS:UniProtKB.
 GO:0005504; F:fatty acid binding; IDA:UniProtKB.
 GO:0018467; F:formaldehyde dehydrogenase activity; IDA:UniProtKB.
 GO:0051903; F:S-(hydroxymethyl)glutathione dehydrogenase activity; TAS:UniProtKB.
 GO:0008270; F:zinc ion binding; IDA:UniProtKB.
 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; IEA:Compara.
 GO:0018119; P:peptidyl-cysteine S-nitrosylation; IEA:Compara.
 GO:0045777; P:positive regulation of blood pressure; IEA:Compara.
 GO:0003016; P:respiratory system process; IEA:Compara.
 GO:0032496; P:response to lipopolysaccharide; IEA:Compara.
 GO:0051409; P:response to nitrosative stress; IEA:Compara.
 GO:0051775; P:response to redox state; IDA:UniProtKB.
 GO:0001523; P:retinoid metabolic process; IEA:Compara. 
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