CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016389
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Zinc-binding alcohol dehydrogenase domain-containing protein 2 
Protein Synonyms/Alias
  
Gene Name
 Zadh2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
35AIPRTMQKLVVTRLSacetylation[1, 2, 3, 4, 5, 6]
35AIPRTMQKLVVTRLSubiquitination[7]
214DEKAAFLKSIGCDRPacetylation[3]
214DEKAAFLKSIGCDRPubiquitination[7]
292KAGVLPTKLLKKSASacetylation[3, 5, 6]
295VLPTKLLKKSASLRGacetylation[3]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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
Functional Description
  
Sequence Annotation
 NP_BIND 303 305 NADP (By similarity).
 BINDING 185 185 NADP; via amide nitrogen (By similarity).
 BINDING 205 205 NADP (By similarity).
 BINDING 209 209 NADP (By similarity).
 BINDING 224 224 NADP (By similarity).
 BINDING 247 247 NADP (By similarity).
 BINDING 269 269 NADP; via carbonyl oxygen (By
 BINDING 275 275 NADP (By similarity).
 BINDING 361 361 NADP (By similarity).  
Keyword
 Complete proteome; NADP; Oxidoreductase; Peroxisome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 377 AA 
Protein Sequence
MLRLAAAGAR AIVDMSYARH FLDFQGSAIP RTMQKLVVTR LSPNFHEAVT LRRDCPVPLP 60
GDGDLLVRNR FVGINASDIN YSAGRYDPSL KPPFDIGFEG IGEVVALGLS ASARYTVGQA 120
VAYMAPGSFA EYTVVPASIA IPMPSVKPEY LTMLVSGTTA YLSLEELGEL SEGKKVLVTA 180
AAGGTGQFAV QLSKIAKCHV IGTCSSDEKA AFLKSIGCDR PINYRTEPVE TVLKQEYPEG 240
VDVVYESVGG AMFDLAVDAL ATKGRLIVIG FISGYQSPTG LSPIKAGVLP TKLLKKSASL 300
RGFFLNHYFS KYQAAMERLL ELYARGDLVC EVDLGHLAPD GRFIGLESVF QAVDYMYTGK 360
NTGKLVVELP HPVSSKL 377 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005777; C:peroxisome; IDA:UniProtKB.
 GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR013149; ADH_C.
 IPR013154; ADH_GroES-like.
 IPR002085; ADH_SF_Zn-type.
 IPR011032; GroES-like.
 IPR016040; NAD(P)-bd_dom.
 IPR002364; Quin_OxRdtase/zeta-crystal_CS. 
Pfam
 PF08240; ADH_N
 PF00107; ADH_zinc_N 
SMART
  
PROSITE
 PS01162; QOR_ZETA_CRYSTAL 
PRINTS