CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002642
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Alcohol dehydrogenase 4 
Protein Synonyms/Alias
 Alcohol dehydrogenase class II pi chain 
Gene Name
 ADH4 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
254LNPRDLHKPIQEVIIacetylation[1]
Reference
 [1] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786
Functional Description
  
Sequence Annotation
 NP_BIND 48 49 NAD.
 NP_BIND 205 210 NAD.
 NP_BIND 298 300 NAD.
 NP_BIND 323 325 NAD.
 METAL 47 47 Zinc 1; catalytic.
 METAL 69 69 Zinc 1; catalytic.
 METAL 99 99 Zinc 2.
 METAL 102 102 Zinc 2.
 METAL 105 105 Zinc 2.
 METAL 113 113 Zinc 2.
 METAL 180 180 Zinc 1; catalytic.
 BINDING 229 229 NAD.
 BINDING 234 234 NAD.
 BINDING 375 375 NAD.  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Metal-binding; NAD; Oxidoreductase; Polymorphism; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 380 AA 
Protein Sequence
MGTKGKVIKC KAAIAWEAGK PLCIEEVEVA PPKAHEVRIQ IIATSLCHTD ATVIDSKFEG 60
LAFPVIVGHE AAGIVESIGP GVTNVKPGDK VIPLYAPLCR KCKFCLSPLT NLCGKISNLK 120
SPASDQQLME DKTSRFTCKG KPVYHFFGTS TFSQYTVVSD INLAKIDDDA NLERVCLLGC 180
GFSTGYGAAI NNAKVTPGST CAVFGLGGVG LSAVMGCKAA GASRIIGIDI NSEKFVKAKA 240
LGATDCLNPR DLHKPIQEVI IELTKGGVDF ALDCAGGSET MKAALDCTTA GWGSCTFIGV 300
AAGSKGLTIF PEELIIGRTI NGTFFGGWKS VDSIPKLVTD YKNKKFNLDA LVTHTLPFDK 360
ISEAFDLMNQ GKSVRTILIF 380 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
 GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; IDA:UniProtKB.
 GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IEA:Compara.
 GO:0005503; F:all-trans retinal binding; IDA:UniProtKB.
 GO:0019115; F:benzaldehyde dehydrogenase activity; IDA:UniProtKB.
 GO:0051287; F:NAD binding; IDA:UniProtKB.
 GO:0003960; F:NADPH:quinone reductase activity; ISS:UniProtKB.
 GO:0019841; F:retinol binding; IDA:UniProtKB.
 GO:0004745; F:retinol dehydrogenase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IDA:UniProtKB.
 GO:0046164; P:alcohol catabolic process; ISS:UniProtKB.
 GO:0006081; P:cellular aldehyde metabolic process; IDA:UniProtKB.
 GO:0006069; P:ethanol oxidation; IDA:UniProtKB.
 GO:0042375; P:quinone cofactor metabolic process; ISS:UniProtKB.
 GO:0042572; P:retinol metabolic process; IDA:UniProtKB.
 GO:0006805; P:xenobiotic metabolic process; TAS:Reactome. 
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