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UniProtKB/Swiss-Prot entry P00325


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ADH1B_HUMAN
Primary accession number P00325
Secondary accession numbers Q13711 Q4ZGI9 Q96KI7
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 117)
Name and origin of the protein
Protein name Alcohol dehydrogenase 1B
Synonyms EC 1.1.1.1
Alcohol dehydrogenase subunit beta
Gene name
Name: ADH1B
Synonyms: ADH2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1073/pnas.82.9.2703; PubMed=2986130 [NCBI, ExPASy, EBI, Israel, Japan]
Ikuta T., Fujiyoshi T., Kurachi K., Yoshida A.;
"Molecular cloning of a full-length cDNA for human alcohol dehydrogenase.";
Proc. Natl. Acad. Sci. U.S.A. 82:2703-2707(1985).
[2]
ERRATUM.
Ikuta T., Fujiyoshi T., Kurachi K., Yoshida A.;
Proc. Natl. Acad. Sci. U.S.A. 82:5578-5578(1985).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/0014-5793(86)80111-9; PubMed=3000832 [NCBI, ExPASy, EBI, Israel, Japan]
Heden L.-O., Hoeoeg J.-O., Larsson K., Lake M., Lagerholm E., Holmgren A., Vallee B.L., Joernvall H., von Bahr-Lindstroem H.;
"cDNA clones coding for the beta-subunit of human liver alcohol dehydrogenase have differently sized 3'-non-coding regions.";
FEBS Lett. 194:327-332(1986).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2935533 [NCBI, ExPASy, EBI, Israel, Japan]
Duester G., Smith M., Bilanchone V., Hatfield G.W.;
"Molecular analysis of the human class I alcohol dehydrogenase gene family and nucleotide sequence of the gene encoding the beta subunit.";
J. Biol. Chem. 261:2027-2033(1986).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1073/pnas.83.3.634; PubMed=2935875 [NCBI, ExPASy, EBI, Israel, Japan]
Ikuta T., Szeto S., Yoshida A.;
"Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence.";
Proc. Natl. Acad. Sci. U.S.A. 83:634-638(1986).
[6]
NUCLEOTIDE SEQUENCE [MRNA].
Yokoyama S., Yokoyama R., Rotwein P.;
"Molecular characterization of cDNA clones encoding the human alcohol dehydrogenase beta 1 and the evolutionary relationship to the other class I subunits alpha and gamma.";
Jpn. J. Genet. 62:241-256(1987).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-48; LYS-57 AND CYS-370.
TISSUE=Liver;
DOI=10.1111/j.1530-0277.1989.tb00383.x; PubMed=2679216 [NCBI, ExPASy, EBI, Israel, Japan]
Carr L.G., Xu Y., Ho W.H., Edenberg H.J.;
"Nucleotide sequence of the ADH2(3) gene encoding the human alcohol dehydrogenase beta 3 subunit.";
Alcohol. Clin. Exp. Res. 13:594-596(1989).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT HIS-48.
DOI=10.1111/j.1432-1033.1989.tb14931.x; PubMed=2547609 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuo Y., Yokoyama R., Yokoyama S.;
"The genes for human alcohol dehydrogenases beta 1 and beta 2 differ by only one nucleotide.";
Eur. J. Biochem. 183:317-320(1989).
[9]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT HIS-48.
TISSUE=Liver;
Polin L., Hey-Chi H.;
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-48; SER-60 AND CYS-370.
NIEHS SNPs program;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
PROTEIN SEQUENCE OF 2-375.
DOI=10.1111/j.1432-1033.1984.tb08573.x; PubMed=6391920 [NCBI, ExPASy, EBI, Israel, Japan]
Hempel J., Buhler R., Kaiser R., Holmquist B., de Zalenski C., von Wartburg J.-P., Vallee B.L., Joernvall H.;
"Human liver alcohol dehydrogenase. 1. The primary structure of the beta 1 beta 1 isoenzyme.";
Eur. J. Biochem. 145:437-445(1984).
[13]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LYS-57.
DOI=10.1016/0888-7543(88)90004-3; PubMed=3397059 [NCBI, ExPASy, EBI, Israel, Japan]
Xu Y.L., Carr L.G., Bosron W.F., Li T.K., Edenberg H.J.;
"Genotyping of human alcohol dehydrogenases at the ADH2 and ADH3 loci following DNA sequence amplification.";
Genomics 2:209-214(1988).
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-86.
Osier M., Speed W.C., Seaman M.I., Kidd K.K.;
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
[15]
VARIANT HIS-48.
DOI=10.1073/pnas.81.10.3024; PubMed=6374651 [NCBI, ExPASy, EBI, Israel, Japan]
Joernvall H., Hempel J., Vallee B.L., Bosron W.F., Li T.-K.;
"Human liver alcohol dehydrogenase: amino acid substitution in the beta 2 beta 2 Oriental isozyme explains functional properties, establishes an active site structure, and parallels mutational exchanges in the yeast enzyme.";
Proc. Natl. Acad. Sci. U.S.A. 81:3024-3028(1984).
[16]
VARIANT CYS-370.
DOI=10.1016/0006-291X(87)90779-0; PubMed=3619918 [NCBI, ExPASy, EBI, Israel, Japan]
Burnell J.C., Carr L.G., Dwulet F.E., Edenberg H.J., Li T.-K., Bosron W.F.;
"The human beta 3 alcohol dehydrogenase subunit differs from beta 1 by a Cys for Arg-369 substitution which decreases NAD(H) binding.";
Biochem. Biophys. Res. Commun. 146:1127-1133(1987).
[17]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
DOI=10.1073/pnas.88.18.8149; PubMed=1896463 [NCBI, ExPASy, EBI, Israel, Japan]
Hurley T.D., Bosron W.F., Hamilton J.A., Amzel L.M.;
"Structure of human beta 1 beta 1 alcohol dehydrogenase: catalytic effects of non-active-site substitutions.";
Proc. Natl. Acad. Sci. U.S.A. 88:8149-8153(1991).
[18]
X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
DOI=10.1006/jmbi.1994.1382; PubMed=8201622 [NCBI, ExPASy, EBI, Israel, Japan]
Hurley T.D., Bosron W.F., Stone C.L., Amzel L.M.;
"Structures of three human beta alcohol dehydrogenase variants. Correlations with their functional differences.";
J. Mol. Biol. 239:415-429(1994).
[19]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
DOI=10.1074/jbc.271.29.17057; PubMed=8663387 [NCBI, ExPASy, EBI, Israel, Japan]
Davis G.J., Bosron W.F., Stone C.L., Owusu-Dekyi K., Hurley T.D.;
"X-ray structure of human beta3beta3 alcohol dehydrogenase. The contribution of ionic interactions to coenzyme binding.";
J. Biol. Chem. 271:17057-17061(1996).
[20]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
DOI=10.1110/ps.45001; PubMed=11274460 [NCBI, ExPASy, EBI, Israel, Japan]
Niederhut M.S., Gibbons B.J., Perez-Miller S., Hurley T.D.;
"Three-dimensional structures of the three human class I alcohol dehydrogenases.";
Protein Sci. 10:697-706(2001).
[21]
ASSOCIATION OF VARIANT HIS-48 WITH LOWER RISK OF ALCOHOLISM.
DOI=10.1053/he.2000.5978; PubMed=10733556 [NCBI, ExPASy, EBI, Israel, Japan]
Borras E., Coutelle C., Rosell A., Fernandez-Muixi F., Broch M., Crosas B., Hjelmqvist L., Lorenzo A., Gutierrez C., Santos M., Szczepanek M., Heilig M., Quattrocchi P., Farres J., Vidal F., Richart C., Mach T., Bogdal J., Joernvall H., Seitz H.K., Couzigou P., Pares X.;
"Genetic polymorphism of alcohol dehydrogenase in Europeans: the ADH2*2 allele decreases the risk for alcoholism and is associated with ADH3*1.";
Hepatology 31:984-989(2000).
Comments
  • CATALYTIC ACTIVITY: An alcohol + NAD+ = an aldehyde or ketone + NADH.
  • COFACTOR: Binds 2 zinc ions per subunit.
  • SUBUNIT: Dimer of identical or non-identical chains of three types; alpha, beta and gamma.
  • SUBCELLULAR LOCATION: Cytoplasm.
  • POLYMORPHISM: Three alleles are known: ADH1B*1 (ADH2*1) corresponding to variant beta-1, ADH1B*2 (ADH2*2) corresponding to variant beta-2, ADH1B*3 (ADH2*3) corresponding to variant beta-3. The sequence shown is that of allele ADH1B*1. The ADH1B*2 allele frequency in orientals is approximately 75%, whereas it is less than 5% in most Caucasian populations.
  • MISCELLANEOUS: There are 7 different ADH's isozymes in human: three belongs to class-I: alpha, beta, and gamma, one to class-II: pi, one to class-III: chi, one to class-IV: ADH7 and one to class-V: ADH6.
  • SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family.
  • WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/adh1b/";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M24317; AAA51884.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X03350; CAA27056.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M24316; AAB59496.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M24308; AAB59496.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M24309; AAB59496.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M24310; AAB59496.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M24311; AAB59496.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M24312; AAB59496.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M24313; AAB59496.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M24314; AAB59496.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D00137; BAA00084.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L38290; AAB48003.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L38283; AAB48003.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L38284; AAB48003.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L38285; AAB48003.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L38286; AAB48003.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L38287; AAB48003.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L38288; AAB48003.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L38289; AAB48003.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X15447; CAA33487.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X15448; CAA33487.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X15449; CAA33487.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X15450; CAA33487.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X15451; CAA33487.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X15452; CAA33487.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X15453; CAA33487.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X15454; CAA33487.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X15455; CAA33487.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF153821; AAD37446.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ017646; AAY22180.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC033009; AAH33009.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21692; AAA51592.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF040967; AAB96912.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00473031; -.
PIR A23607; DEHUAB.
RefSeq NP_000659.2; -.
UniGene Hs.4
3D structure databases
PDB
1DEH; X-ray; 2.20 A; A/B=2-375.[ExPASy / RCSB / EBI]
1HDX; X-ray; 2.50 A; A/B=2-375.[ExPASy / RCSB / EBI]
1HDY; X-ray; 2.50 A; A/B=2-375.[ExPASy / RCSB / EBI]
1HDZ; X-ray; 2.50 A; A/B=2-375.[ExPASy / RCSB / EBI]
1HSZ; X-ray; 2.20 A; A/B=2-375.[ExPASy / RCSB / EBI]
1HTB; X-ray; 2.40 A; A/B=2-375.[ExPASy / RCSB / EBI]
1U3U; X-ray; 1.60 A; A/B=2-374.[ExPASy / RCSB / EBI]
1U3V; X-ray; 1.65 A; A/B=2-374.[ExPASy / RCSB / EBI]
3HUD; X-ray; 3.20 A; A/B=2-375.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1DEH; -.
1HDX; -.
1HDY; -.
1HDZ; -.
1HSZ; -.
1HTB; -.
1U3U; -.
1U3V; -.
3HUD; -.
ModBase P00325.
PTM databases
PhosphoSite P00325; -.
Enzyme and pathway databases
BRENDA 1.1.1.1; 247.
Reactome REACT_13433; Biological oxidations.
Organism-specific databases
GeneCards GC04M100456; -.
HGNC HGNC:250; ADH1B.
GenAtlas ADH1B.
MIM 103720; gene. [NCBI / EBI]
PharmGKB PA24571; -.
Gene expression databases
ArrayExpress P00325; -.
Bgee P00325; -.
CleanEx HS_ADH1B; -.
GermOnline ENSG00000196616; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004022; Molecular function: alcohol dehydrogenase (NAD) activity (inferred from electronic annotation from EC).
GO:0008270; Molecular function: zinc ion binding (inferred from direct assay from UniProtKB).
GO:0006069; Biological process: ethanol oxidation (inferred from direct assay from UniProtKB).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR013154; ADH_GroES-like.
IPR002085; ADH_SF_Zn.
IPR013149; ADH_Zn-bd.
IPR002328; ADH_Zn_CS.
Graphical view of domain structure.
PANTHER PTHR11695; ADH_Sf_Zn; 1.
Pfam PF08240; ADH_N; 1.
PF00107; ADH_zinc_N; 1.
Pfam graphical view of domain structure.
PROSITE PS00059; ADH_ZINC; 1.
Proteomic databases
PRIDE P00325; -.
Genome annotation databases
Ensembl ENSG00000196616; Homo sapiens. [Contig view]
GeneID 125; -.
KEGG hsa:125; -.
Phylogenomic databases
HOGENOM P00325; -.
HOVERGEN P00325; -.
Other
DrugBank DB01213; Fomepizole.
DB00157; NADH.
NextBio 499; -.
SOURCE ADH1B; Homo sapiens.
ProtoNet P00325.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Metal-binding; NAD; Oxidoreductase; Polymorphism; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   375  374     Alcohol dehydrogenase 1B. PRO_0000160661
NP_BIND   200   205  6     NAD. 
NP_BIND   293   295  3     NAD. 
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. 
BINDING   229   229        NAD. 
BINDING   370   370        NAD. 
MOD_RES   2     2        N-acetylserine. 
VARIANT   48    48  1     R -> H (in beta-2; allele ADH1B*2; common in Asian populations; associated with a lower risk of alcoholism). VAR_000426 [3D]
VARIANT   57    57  1     N -> K (in dbSNP:rs1041969 [NCBI]). VAR_019322 [3D]
VARIANT   60    60  1     T -> S (in dbSNP:rs6413413 [NCBI]). VAR_019323 [3D]
VARIANT   370   370  1     R -> C (in beta-3/Indianapolis; allele ADH1B*3; decreased NAD(H) binding; dbSNP:rs2066702 [NCBI]). VAR_000427 [3D]
CONFLICT   8     8        I -> M (in Ref. 13; AAA51592). 
CONFLICT   130   130        Missing (in Ref. 12; AA sequence). 
CONFLICT   166   166        P -> K (in Ref. 13; AAA51592). 
CONFLICT   190   190        V -> VV (in Ref. 8; CAA33487). 
CONFLICT   230   230        F -> K (in Ref. 1; AAA51884). 
CONFLICT   235   235        E -> V (in Ref. 13; AAA51592). 
STRAND   8    15  8      
STRAND   23    29  7      
STRAND   36    45  10      
HELIX   48    54  7      
STRAND   62    65  4      
STRAND   69    77  9      
STRAND   89    92  4      
STRAND   99   101  3      
HELIX   102   105  4      
STRAND   116   119  4      
STRAND   131   133  3      
STRAND   136   139  4      
TURN   142   144  3      
STRAND   147   154  8      
HELIX   155   157  3      
STRAND   158   160  3      
TURN   167   169  3      
HELIX   170   174  5      
HELIX   176   185  10      
TURN   186   188  3      
STRAND   195   199  5      
HELIX   203   215  13      
STRAND   218   223  6      
HELIX   227   229  3      
HELIX   230   236  7      
STRAND   239   242  4      
HELIX   244   246  3      
HELIX   251   258  8      
STRAND   263   268  6      
HELIX   273   281  9      
TURN   285   287  3      
STRAND   289   292  4      
STRAND   302   304  3      
HELIX   307   310  4      
STRAND   314   317  4      
HELIX   320   322  3      
HELIX   325   337  13      
TURN   344   346  3      
STRAND   347   352  6      
HELIX   353   355  3      
HELIX   356   364  9      
STRAND   369   374  6      
Sequence information
Length: 375 AA [This is the length of the unprocessed precursor] Molecular weight: 39855 Da [This is the MW of the unprocessed precursor] CRC64: 6962B9A0F967673B [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSTAGKVIKC KAAVLWEVKK PFSIEDVEVA PPKAYEVRIK MVAVGICRTD DHVVSGNLVT 

        70         80         90        100        110        120 
PLPVILGHEA AGIVESVGEG VTTVKPGDKV IPLFTPQCGK CRVCKNPESN YCLKNDLGNP 

       130        140        150        160        170        180 
RGTLQDGTRR FTCRGKPIHH FLGTSTFSQY TVVDENAVAK IDAASPLEKV CLIGCGFSTG 

       190        200        210        220        230        240 
YGSAVNVAKV TPGSTCAVFG LGGVGLSAVM GCKAAGAARI IAVDINKDKF AKAKELGATE 

       250        260        270        280        290        300 
CINPQDYKKP IQEVLKEMTD GGVDFSFEVI GRLDTMMASL LCCHEACGTS VIVGVPPASQ 

       310        320        330        340        350        360 
NLSINPMLLL TGRTWKGAVY GGFKSKEGIP KLVADFMAKK FSLDALITHV LPFEKINEGF 

       370 
DLLHSGKSIR TVLTF 

P00325 in FASTA format

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