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P00325

- ADH1B_HUMAN

UniProt

P00325 - ADH1B_HUMAN

Protein

Alcohol dehydrogenase 1B

Gene

ADH1B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 166 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

    Binds 2 zinc ions per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi47 – 471Zinc 1; catalytic
    Metal bindingi68 – 681Zinc 1; catalytic
    Metal bindingi98 – 981Zinc 2
    Metal bindingi101 – 1011Zinc 2
    Metal bindingi104 – 1041Zinc 2
    Metal bindingi112 – 1121Zinc 2
    Metal bindingi175 – 1751Zinc 1; catalytic
    Binding sitei224 – 2241NAD
    Binding sitei229 – 2291NAD
    Binding sitei370 – 3701NAD

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi200 – 2056NAD
    Nucleotide bindingi293 – 2953NAD

    GO - Molecular functioni

    1. alcohol dehydrogenase activity, zinc-dependent Source: UniProtKB
    2. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. ethanol oxidation Source: UniProtKB
    2. small molecule metabolic process Source: Reactome
    3. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Metal-binding, NAD, Zinc

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER66-321.
    ReactomeiREACT_34. Ethanol oxidation.
    SABIO-RKP00325.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alcohol dehydrogenase 1B (EC:1.1.1.1)
    Alternative name(s):
    Alcohol dehydrogenase subunit beta
    Gene namesi
    Name:ADH1B
    Synonyms:ADH2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:250. ADH1B.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    MIMi103720. gene+phenotype.
    PharmGKBiPA24571.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 375374Alcohol dehydrogenase 1BPRO_0000160661Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP00325.
    PRIDEiP00325.

    PTM databases

    PhosphoSiteiP00325.

    Expressioni

    Gene expression databases

    ArrayExpressiP00325.
    BgeeiP00325.
    CleanExiHS_ADH1B.
    GenevestigatoriP00325.

    Organism-specific databases

    HPAiHPA047814.

    Interactioni

    Subunit structurei

    Dimer of identical or non-identical chains of three types; alpha, beta and gamma.

    Protein-protein interaction databases

    BioGridi106637. 6 interactions.
    IntActiP00325. 7 interactions.
    STRINGi9606.ENSP00000306606.

    Structurei

    Secondary structure

    1
    375
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 158
    Beta strandi23 – 297
    Beta strandi36 – 4510
    Helixi48 – 547
    Beta strandi56 – 583
    Beta strandi62 – 654
    Beta strandi69 – 779
    Beta strandi89 – 924
    Beta strandi99 – 1013
    Helixi102 – 1054
    Beta strandi116 – 1194
    Beta strandi131 – 1333
    Beta strandi136 – 1394
    Turni142 – 1443
    Beta strandi147 – 1548
    Helixi155 – 1573
    Beta strandi158 – 1603
    Helixi167 – 1704
    Helixi171 – 1744
    Helixi176 – 18510
    Turni186 – 1883
    Beta strandi195 – 1995
    Helixi203 – 21412
    Beta strandi218 – 2236
    Helixi227 – 2293
    Helixi230 – 2356
    Beta strandi239 – 2424
    Helixi244 – 2463
    Helixi251 – 2588
    Turni259 – 2613
    Beta strandi262 – 2687
    Helixi273 – 28210
    Turni285 – 2873
    Beta strandi289 – 2924
    Beta strandi302 – 3043
    Helixi307 – 3104
    Beta strandi314 – 3174
    Helixi320 – 3223
    Helixi325 – 33713
    Helixi344 – 3463
    Beta strandi347 – 3526
    Helixi353 – 3553
    Helixi356 – 3649
    Beta strandi369 – 3746

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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/B2-375[»]
    1U3VX-ray1.65A/B2-375[»]
    3HUDX-ray3.20A/B2-375[»]
    ProteinModelPortaliP00325.
    SMRiP00325. Positions 2-375.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00325.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1062.
    HOGENOMiHOG000294674.
    HOVERGENiHBG000195.
    InParanoidiP00325.
    KOiK13951.
    OrthoDBiEOG72NRQ6.
    PhylomeDBiP00325.
    TreeFamiTF300429.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProiIPR013149. 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]
    PANTHERiPTHR11695. PTHR11695. 1 hit.
    PfamiPF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF50129. SSF50129. 2 hits.
    PROSITEiPS00059. ADH_ZINC. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P00325-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSTAGKVIKC KAAVLWEVKK PFSIEDVEVA PPKAYEVRIK MVAVGICRTD    50
    DHVVSGNLVT PLPVILGHEA AGIVESVGEG VTTVKPGDKV IPLFTPQCGK 100
    CRVCKNPESN YCLKNDLGNP RGTLQDGTRR FTCRGKPIHH FLGTSTFSQY 150
    TVVDENAVAK IDAASPLEKV CLIGCGFSTG YGSAVNVAKV TPGSTCAVFG 200
    LGGVGLSAVM GCKAAGAARI IAVDINKDKF AKAKELGATE CINPQDYKKP 250
    IQEVLKEMTD GGVDFSFEVI GRLDTMMASL LCCHEACGTS VIVGVPPASQ 300
    NLSINPMLLL TGRTWKGAVY GGFKSKEGIP KLVADFMAKK FSLDALITHV 350
    LPFEKINEGF DLLHSGKSIR TVLTF 375
    Length:375
    Mass (Da):39,855
    Last modified:January 23, 2007 - v2
    Checksum:i6962B9A0F967673B
    GO
    Isoform 2 (identifier: P00325-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-40: Missing.

    Show »
    Length:335
    Mass (Da):35,412
    Checksum:iA92B71F22E3CAFA4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti8 – 81I → M in AAA51592. (PubMed:3397059)Curated
    Sequence conflicti130 – 1301Missing AA sequence (PubMed:6391920)Curated
    Sequence conflicti166 – 1661P → K in AAA51592. (PubMed:3397059)Curated
    Sequence conflicti190 – 1901V → VV in CAA33487. (PubMed:2547609)Curated
    Sequence conflicti220 – 2201I → V in BAG62635. (PubMed:14702039)Curated
    Sequence conflicti230 – 2301F → K in AAA51884. (PubMed:2986130)Curated
    Sequence conflicti235 – 2351E → V in AAA51592. (PubMed:3397059)Curated
    Sequence conflicti338 – 3447Missing in BAG62635. (PubMed:14702039)Curated

    Polymorphismi

    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 [MIMi:103720].

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti48 – 481R → H in beta-2; allele ADH1B*2; common in Asian populations; associated with a lower risk of alcoholism. 6 Publications
    Corresponds to variant rs1229984 [ dbSNP | Ensembl ].
    VAR_000426
    Natural varianti57 – 571N → K.2 Publications
    Corresponds to variant rs1041969 [ dbSNP | Ensembl ].
    VAR_019322
    Natural varianti60 – 601T → S.1 Publication
    Corresponds to variant rs6413413 [ dbSNP | Ensembl ].
    VAR_019323
    Natural varianti370 – 3701R → C in beta-3/Indianapolis; allele ADH1B*3; decreased NAD(H) binding. 3 Publications
    Corresponds to variant rs2066702 [ dbSNP | Ensembl ].
    VAR_000427

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4040Missing in isoform 2. 1 PublicationVSP_054847Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M24317 mRNA. Translation: AAA51884.1.
    X03350 mRNA. Translation: CAA27056.1.
    M24316
    , M24308, M24309, M24310, M24311, M24312, M24313, M24314 Genomic DNA. Translation: AAB59496.1.
    D00137 mRNA. Translation: BAA00084.1.
    L38290
    , L38283, L38284, L38285, L38286, L38287, L38288, L38289 Genomic DNA. Translation: AAB48003.1.
    X15447
    , X15448, X15449, X15450, X15451, X15452, X15453, X15454, X15455 Genomic DNA. Translation: CAA33487.1.
    AF153821 mRNA. Translation: AAD37446.1.
    DQ017646 Genomic DNA. Translation: AAY22180.1.
    AK301018 mRNA. Translation: BAG62635.1.
    AC097530 Genomic DNA. No translation available.
    BC033009 mRNA. Translation: AAH33009.1.
    M21692 mRNA. Translation: AAA51592.1.
    AF040967 Genomic DNA. Translation: AAB96912.1.
    CCDSiCCDS34033.1. [P00325-1]
    CCDS68761.1. [P00325-2]
    PIRiA23607. DEHUAB.
    RefSeqiNP_000659.2. NM_000668.5.
    NP_001273579.1. NM_001286650.1.
    UniGeneiHs.4.

    Genome annotation databases

    EnsembliENST00000305046; ENSP00000306606; ENSG00000196616.
    ENST00000394887; ENSP00000378351; ENSG00000196616.
    GeneIDi125.
    KEGGihsa:125.
    UCSCiuc003hus.4. human. [P00325-1]

    Polymorphism databases

    DMDMi113394.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M24317 mRNA. Translation: AAA51884.1 .
    X03350 mRNA. Translation: CAA27056.1 .
    M24316
    , M24308 , M24309 , M24310 , M24311 , M24312 , M24313 , M24314 Genomic DNA. Translation: AAB59496.1 .
    D00137 mRNA. Translation: BAA00084.1 .
    L38290
    , L38283 , L38284 , L38285 , L38286 , L38287 , L38288 , L38289 Genomic DNA. Translation: AAB48003.1 .
    X15447
    , X15448 , X15449 , X15450 , X15451 , X15452 , X15453 , X15454 , X15455 Genomic DNA. Translation: CAA33487.1 .
    AF153821 mRNA. Translation: AAD37446.1 .
    DQ017646 Genomic DNA. Translation: AAY22180.1 .
    AK301018 mRNA. Translation: BAG62635.1 .
    AC097530 Genomic DNA. No translation available.
    BC033009 mRNA. Translation: AAH33009.1 .
    M21692 mRNA. Translation: AAA51592.1 .
    AF040967 Genomic DNA. Translation: AAB96912.1 .
    CCDSi CCDS34033.1. [P00325-1 ]
    CCDS68761.1. [P00325-2 ]
    PIRi A23607. DEHUAB.
    RefSeqi NP_000659.2. NM_000668.5.
    NP_001273579.1. NM_001286650.1.
    UniGenei Hs.4.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DEH X-ray 2.20 A/B 2-375 [» ]
    1HDX X-ray 2.50 A/B 2-375 [» ]
    1HDY X-ray 2.50 A/B 2-375 [» ]
    1HDZ X-ray 2.50 A/B 2-375 [» ]
    1HSZ X-ray 2.20 A/B 2-375 [» ]
    1HTB X-ray 2.40 A/B 2-375 [» ]
    1U3U X-ray 1.60 A/B 2-375 [» ]
    1U3V X-ray 1.65 A/B 2-375 [» ]
    3HUD X-ray 3.20 A/B 2-375 [» ]
    ProteinModelPortali P00325.
    SMRi P00325. Positions 2-375.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106637. 6 interactions.
    IntActi P00325. 7 interactions.
    STRINGi 9606.ENSP00000306606.

    Chemistry

    BindingDBi P00325.
    ChEMBLi CHEMBL3284.
    DrugBanki DB00898. Ethanol.
    DB01213. Fomepizole.

    PTM databases

    PhosphoSitei P00325.

    Polymorphism databases

    DMDMi 113394.

    Proteomic databases

    PaxDbi P00325.
    PRIDEi P00325.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000305046 ; ENSP00000306606 ; ENSG00000196616 .
    ENST00000394887 ; ENSP00000378351 ; ENSG00000196616 .
    GeneIDi 125.
    KEGGi hsa:125.
    UCSCi uc003hus.4. human. [P00325-1 ]

    Organism-specific databases

    CTDi 125.
    GeneCardsi GC04M100226.
    HGNCi HGNC:250. ADH1B.
    HPAi HPA047814.
    MIMi 103720. gene+phenotype.
    neXtProti NX_P00325.
    PharmGKBi PA24571.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1062.
    HOGENOMi HOG000294674.
    HOVERGENi HBG000195.
    InParanoidi P00325.
    KOi K13951.
    OrthoDBi EOG72NRQ6.
    PhylomeDBi P00325.
    TreeFami TF300429.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER66-321.
    Reactomei REACT_34. Ethanol oxidation.
    SABIO-RK P00325.

    Miscellaneous databases

    EvolutionaryTracei P00325.
    GeneWikii ADH1B.
    GenomeRNAii 125.
    NextBioi 35465058.
    PROi P00325.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P00325.
    Bgeei P00325.
    CleanExi HS_ADH1B.
    Genevestigatori P00325.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProi IPR013149. 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 ]
    PANTHERi PTHR11695. PTHR11695. 1 hit.
    Pfami PF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50129. SSF50129. 2 hits.
    PROSITEi PS00059. ADH_ZINC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] (ISOFORM 1).
    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] (ISOFORM 1).
    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] (ISOFORM 1).
    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] (ISOFORM 1).
    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] (ISOFORM 1), 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. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Small intestine.
    12. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT HIS-48.
    13. "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] (ISOFORM 1).
      Tissue: Testis.
    14. "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, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2.
    15. "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.
    16. 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.
    17. "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.
    18. "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.
    19. "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).
    20. "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).
    21. "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).
    22. "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).
    23. "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.
      , 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.

    Entry informationi

    Entry nameiADH1B_HUMAN
    AccessioniPrimary (citable) accession number: P00325
    Secondary accession number(s): A8MYN5
    , B4DRS9, B4DVC3, Q13711, Q4ZGI9, Q96KI7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 166 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    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.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3