CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001735
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Alcohol dehydrogenase 1 
Protein Synonyms/Alias
 ADH-A2; Alcohol dehydrogenase A subunit 
Gene Name
 Adh1 
Gene Synonyms/Alias
 Adh-1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
6**MSTAGKVIKCKAAubiquitination[1]
9STAGKVIKCKAAVLWubiquitination[1]
11AGKVIKCKAAVLWELubiquitination[1]
20AVLWELHKPFTIEDIacetylation[2]
20AVLWELHKPFTIEDIubiquitination[1]
33DIEVAPPKAHEVRIKacetylation[3]
33DIEVAPPKAHEVRIKubiquitination[1]
40KAHEVRIKMVATGVCacetylation[4]
40KAHEVRIKMVATGVCubiquitination[1]
85GEGVTCVKPGDKVIPubiquitination[1]
89TCVKPGDKVIPLFSPubiquitination[1]
105CGECRICKHPESNFCacetylation[3]
105CGECRICKHPESNFCubiquitination[1]
136SRFSCKGKQIHNFISubiquitination[1]
169DGASPLDKVCLIGCGacetylation[3]
169DGASPLDKVCLIGCGubiquitination[1]
186TGYGSAVKVAKVTPGubiquitination[1]
227IIAVDINKDKFAKAKacetylation[2]
227IIAVDINKDKFAKAKubiquitination[1]
229AVDINKDKFAKAKELacetylation[2]
229AVDINKDKFAKAKELubiquitination[1]
232INKDKFAKAKELGATacetylation[2]
234KDKFAKAKELGATECacetylation[5]
234KDKFAKAKELGATECsuccinylation[5]
234KDKFAKAKELGATECubiquitination[1]
316LLLGRTWKGAIFGGFacetylation[5]
316LLLGRTWKGAIFGGFsuccinylation[5]
316LLLGRTWKGAIFGGFubiquitination[1]
324GAIFGGFKSKDSVPKubiquitination[1]
326IFGGFKSKDSVPKLVacetylation[2, 3, 4, 6]
331KSKDSVPKLVADFMAacetylation[2, 3]
331KSKDSVPKLVADFMAubiquitination[1]
339LVADFMAKKFPLDPLacetylation[2]
339LVADFMAKKFPLDPLubiquitination[1]
340VADFMAKKFPLDPLIacetylation[5]
340VADFMAKKFPLDPLIsuccinylation[5]
340VADFMAKKFPLDPLIubiquitination[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] 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] 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] 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]
 [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] 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] 
Functional Description
  
Sequence Annotation
 NP_BIND 200 205 NAD (By similarity).
 NP_BIND 293 295 NAD (By similarity).
 METAL 47 47 Zinc 1; catalytic.
 METAL 68 68 Zinc 1; catalytic.
 METAL 98 98 Zinc 2.
 METAL 101 101 Zinc 2.
 METAL 104 104 Zinc 2.
 METAL 112 112 Zinc 2.
 METAL 175 175 Zinc 1; catalytic.
 BINDING 224 224 NAD (By similarity).
 BINDING 229 229 NAD (By similarity).
 BINDING 370 370 NAD (By similarity).
 MOD_RES 2 2 N-acetylserine (By similarity).  
Keyword
 Acetylation; Complete proteome; Cytoplasm; Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 375 AA 
Protein Sequence
MSTAGKVIKC KAAVLWELHK PFTIEDIEVA PPKAHEVRIK MVATGVCRSD DHVVSGTLVT 60
PLPAVLGHEG AGIVESVGEG VTCVKPGDKV IPLFSPQCGE CRICKHPESN FCSRSDLLMP 120
RGTLREGTSR FSCKGKQIHN FISTSTFSQY TVVDDIAVAK IDGASPLDKV CLIGCGFSTG 180
YGSAVKVAKV TPGSTCAVFG LGGVGLSVII GCKAAGAARI IAVDINKDKF AKAKELGATE 240
CINPQDYSKP IQEVLQEMTD GGVDFSFEVI GRLDTMTSAL LSCHAACGVS VVVGVPPNAQ 300
NLSMNPMLLL LGRTWKGAIF GGFKSKDSVP KLVADFMAKK FPLDPLITHV LPFEKINEAF 360
DLLRSGKSIR TVLTF 375 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0004022; F:alcohol dehydrogenase (NAD) activity; IDA:MGI.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0048149; P:behavioral response to ethanol; IMP:MGI.
 GO:0006068; P:ethanol catabolic process; IDA:MGI.
 GO:0032526; P:response to retinoic acid; IDA:MGI.
 GO:0033574; P:response to testosterone stimulus; IDA:MGI.
 GO:0042573; P:retinoic acid metabolic process; IMP:MGI.
 GO:0042572; P:retinol metabolic process; IMP:MGI. 
Interpro
 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