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P00325 (ADH1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 161. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alcohol dehydrogenase 1B

EC=1.1.1.1
Alternative name(s):
Alcohol dehydrogenase subunit beta
Gene names
Name:ADH1B
Synonyms:ADH2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length375 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

An alcohol + NAD+ = an aldehyde or ketone + NADH.

Cofactor

Binds 2 zinc ions per subunit.

Subunit structure

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. ADH1B variations have been associated with protection against alcohol dependence and alcohol-related aerodigestive tract cancer [MIM:103720].

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.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12
Chain2 – 375374Alcohol dehydrogenase 1B
PRO_0000160661

Regions

Nucleotide binding200 – 2056NAD
Nucleotide binding293 – 2953NAD

Sites

Metal binding471Zinc 1; catalytic
Metal binding681Zinc 1; catalytic
Metal binding981Zinc 2
Metal binding1011Zinc 2
Metal binding1041Zinc 2
Metal binding1121Zinc 2
Metal binding1751Zinc 1; catalytic
Binding site2241NAD
Binding site2291NAD
Binding site3701NAD

Amino acid modifications

Modified residue21N-acetylserine Ref.12

Natural variations

Natural variant481R → H in beta-2; allele ADH1B*2; common in Asian populations; associated with a lower risk of alcoholism. Ref.7 Ref.8 Ref.9 Ref.10 Ref.15 Ref.21
Corresponds to variant rs1229984 [ dbSNP | Ensembl ].
VAR_000426
Natural variant571N → K. Ref.7 Ref.13
Corresponds to variant rs1041969 [ dbSNP | Ensembl ].
VAR_019322
Natural variant601T → S. Ref.10
Corresponds to variant rs6413413 [ dbSNP | Ensembl ].
VAR_019323
Natural variant3701R → C in beta-3/Indianapolis; allele ADH1B*3; decreased NAD(H) binding. Ref.7 Ref.10 Ref.16
Corresponds to variant rs2066702 [ dbSNP | Ensembl ].
VAR_000427

Experimental info

Sequence conflict81I → M in AAA51592. Ref.13
Sequence conflict1301Missing AA sequence Ref.12
Sequence conflict1661P → K in AAA51592. Ref.13
Sequence conflict1901V → VV in CAA33487. Ref.8
Sequence conflict2301F → K in AAA51884. Ref.1
Sequence conflict2351E → V in AAA51592. Ref.13

Secondary structure

.............................................................................. 375
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00325 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 6962B9A0F967673B

FASTA37539,855
        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 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of a full-length cDNA for human alcohol dehydrogenase."
Ikuta T., Fujiyoshi T., Kurachi K., Yoshida A.
Proc. Natl. Acad. Sci. U.S.A. 82:2703-2707(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Erratum
Ikuta T., Fujiyoshi T., Kurachi K., Yoshida A.
Proc. Natl. Acad. Sci. U.S.A. 82:5578-5578(1985)
[3]"cDNA clones coding for the beta-subunit of human liver alcohol dehydrogenase have differently sized 3'-non-coding regions."
Heden L.-O., Hoeoeg J.-O., Larsson K., Lake M., Lagerholm E., Holmgren A., Vallee B.L., Joernvall H., von Bahr-Lindstroem H.
FEBS Lett. 194:327-332(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Molecular analysis of the human class I alcohol dehydrogenase gene family and nucleotide sequence of the gene encoding the beta subunit."
Duester G., Smith M., Bilanchone V., Hatfield G.W.
J. Biol. Chem. 261:2027-2033(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence."
Ikuta T., Szeto S., Yoshida A.
Proc. Natl. Acad. Sci. U.S.A. 83:634-638(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]"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."
Yokoyama S., Yokoyama R., Rotwein P.
Jpn. J. Genet. 62:241-256(1987)
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[7]"Nucleotide sequence of the ADH2(3) gene encoding the human alcohol dehydrogenase beta 3 subunit."
Carr L.G., Xu Y., Ho W.H., Edenberg H.J.
Alcohol. Clin. Exp. Res. 13:594-596(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-48; LYS-57 AND CYS-370.
Tissue: Liver.
[8]"The genes for human alcohol dehydrogenases beta 1 and beta 2 differ by only one nucleotide."
Matsuo Y., Yokoyama R., Yokoyama S.
Eur. J. Biochem. 183:317-320(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HIS-48.
[9]Polin L., Hey-Chi H.
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT HIS-48.
Tissue: Liver.
[10]NIEHS SNPs program
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-48; SER-60 AND CYS-370.
[11]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[12]"Human liver alcohol dehydrogenase. 1. The primary structure of the beta 1 beta 1 isoenzyme."
Hempel J., Buhler R., Kaiser R., Holmquist B., de Zalenski C., von Wartburg J.-P., Vallee B.L., Joernvall H.
Eur. J. Biochem. 145:437-445(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-375.
[13]"Genotyping of human alcohol dehydrogenases at the ADH2 and ADH3 loci following DNA sequence amplification."
Xu Y.L., Carr L.G., Bosron W.F., Li T.K., Edenberg H.J.
Genomics 2:209-214(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA], VARIANT LYS-57.
[14]Osier M., Speed W.C., Seaman M.I., Kidd K.K.
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-86.
[15]"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."
Joernvall H., Hempel J., Vallee B.L., Bosron W.F., Li T.-K.
Proc. Natl. Acad. Sci. U.S.A. 81:3024-3028(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HIS-48.
[16]"The human beta 3 alcohol dehydrogenase subunit differs from beta 1 by a Cys for Arg-369 substitution which decreases NAD(H) binding."
Burnell J.C., Carr L.G., Dwulet F.E., Edenberg H.J., Li T.-K., Bosron W.F.
Biochem. Biophys. Res. Commun. 146:1127-1133(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CYS-370.
[17]"Structure of human beta 1 beta 1 alcohol dehydrogenase: catalytic effects of non-active-site substitutions."
Hurley T.D., Bosron W.F., Hamilton J.A., Amzel L.M.
Proc. Natl. Acad. Sci. U.S.A. 88:8149-8153(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[18]"Structures of three human beta alcohol dehydrogenase variants. Correlations with their functional differences."
Hurley T.D., Bosron W.F., Stone C.L., Amzel L.M.
J. Mol. Biol. 239:415-429(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
[19]"X-ray structure of human beta3beta3 alcohol dehydrogenase. The contribution of ionic interactions to coenzyme binding."
Davis G.J., Bosron W.F., Stone C.L., Owusu-Dekyi K., Hurley T.D.
J. Biol. Chem. 271:17057-17061(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[20]"Three-dimensional structures of the three human class I alcohol dehydrogenases."
Niederhut M.S., Gibbons B.J., Perez-Miller S., Hurley T.D.
Protein Sci. 10:697-706(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[21]"Genetic polymorphism of alcohol dehydrogenase in Europeans: the ADH2*2 allele decreases the risk for alcoholism and is associated with ADH3*1."
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. expand/collapse author list , Joernvall H., Seitz H.K., Couzigou P., Pares X.
Hepatology 31:984-989(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION OF VARIANT HIS-48 WITH LOWER RISK OF ALCOHOLISM.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M24317 mRNA. Translation: AAA51884.1.
X03350 mRNA. Translation: CAA27056.1.
M24316 expand/collapse EMBL AC list , M24308, M24309, M24310, M24311, M24312, M24313, M24314 Genomic DNA. Translation: AAB59496.1.
D00137 mRNA. Translation: BAA00084.1.
L38290 expand/collapse EMBL AC list , L38283, L38284, L38285, L38286, L38287, L38288, L38289 Genomic DNA. Translation: AAB48003.1.
X15447 expand/collapse EMBL AC list , X15448, X15449, X15450, X15451, X15452, X15453, X15454, X15455 Genomic DNA. Translation: CAA33487.1.
AF153821 mRNA. Translation: AAD37446.1.
DQ017646 Genomic DNA. Translation: AAY22180.1.
BC033009 mRNA. Translation: AAH33009.1.
M21692 mRNA. Translation: AAA51592.1.
AF040967 Genomic DNA. Translation: AAB96912.1.
PIRDEHUAB. A23607.
RefSeqNP_000659.2. NM_000668.5.
NP_001273579.1. NM_001286650.1.
UniGeneHs.4.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DEHX-ray2.20A/B2-375[»]
1HDXX-ray2.50A/B2-375[»]
1HDYX-ray2.50A/B2-375[»]
1HDZX-ray2.50A/B2-375[»]
1HSZX-ray2.20A/B2-375[»]
1HTBX-ray2.40A/B2-375[»]
1U3UX-ray1.60A/B2-374[»]
1U3VX-ray1.65A/B2-374[»]
3HUDX-ray3.20A/B2-375[»]
ProteinModelPortalP00325.
SMRP00325. Positions 2-375.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106637. 6 interactions.
IntActP00325. 7 interactions.
STRING9606.ENSP00000306606.

Chemistry

BindingDBP00325.
ChEMBLCHEMBL3284.
DrugBankDB01213. Fomepizole.
DB00157. NADH.

PTM databases

PhosphoSiteP00325.

Polymorphism databases

DMDM113394.

Proteomic databases

PaxDbP00325.
PRIDEP00325.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000305046; ENSP00000306606; ENSG00000196616.
GeneID125.
KEGGhsa:125.
UCSCuc003hus.4. human.

Organism-specific databases

CTD125.
GeneCardsGC04M100226.
HGNCHGNC:250. ADH1B.
HPAHPA047814.
MIM103720. gene+phenotype.
neXtProtNX_P00325.
PharmGKBPA24571.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1062.
HOGENOMHOG000294674.
HOVERGENHBG000195.
InParanoidP00325.
KOK13951.
OrthoDBEOG72NRQ6.
PhylomeDBP00325.
TreeFamTF300429.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER66-321.
ReactomeREACT_111217. Metabolism.
SABIO-RKP00325.

Gene expression databases

ArrayExpressP00325.
BgeeP00325.
CleanExHS_ADH1B.
GenevestigatorP00325.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProIPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR11695. PTHR11695. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMSSF50129. SSF50129. 2 hits.
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00325.
GeneWikiADH1B.
GenomeRNAi125.
NextBio499.
PROP00325.
SOURCESearch...

Entry information

Entry nameADH1B_HUMAN
AccessionPrimary (citable) accession number: P00325
Secondary accession number(s): Q13711, Q4ZGI9, Q96KI7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 161 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM