Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P07327

- ADH1A_HUMAN

UniProt

P07327 - ADH1A_HUMAN

Protein

Alcohol dehydrogenase 1A

Gene

ADH1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 – 2241NAD2 Publications
    Binding sitei229 – 2291NAD2 Publications
    Binding sitei370 – 3701NAD2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi200 – 2056NAD2 Publications
    Nucleotide bindingi293 – 2953NAD2 Publications

    GO - Molecular functioni

    1. alcohol dehydrogenase (NAD) activity Source: Reactome
    2. alcohol dehydrogenase activity, zinc-dependent Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. alcohol metabolic process Source: UniProtKB
    2. drug metabolic process Source: Reactome
    3. ethanol oxidation Source: Reactome
    4. small molecule metabolic process Source: Reactome
    5. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Metal-binding, NAD, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_121388. Abacavir metabolism.
    REACT_34. Ethanol oxidation.
    SABIO-RKP07327.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alcohol dehydrogenase 1A (EC:1.1.1.1)
    Alternative name(s):
    Alcohol dehydrogenase subunit alpha
    Gene namesi
    Name:ADH1A
    Synonyms:ADH1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:249. ADH1A.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24570.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 375374Alcohol dehydrogenase 1APRO_0000160658Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP07327.
    PRIDEiP07327.

    PTM databases

    PhosphoSiteiP07327.

    Expressioni

    Gene expression databases

    BgeeiP07327.
    CleanExiHS_ADH1A.
    GenevestigatoriP07327.

    Organism-specific databases

    HPAiCAB009562.
    HPA047814.

    Interactioni

    Subunit structurei

    Dimer of identical or non-identical chains of three types; alpha, beta and gamma.2 Publications

    Protein-protein interaction databases

    BioGridi106636. 2 interactions.
    IntActiP07327. 2 interactions.

    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 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 strandi263 – 2686
    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
    1HSOX-ray2.50A/B2-375[»]
    1U3TX-ray2.49A/B2-375[»]
    ProteinModelPortaliP07327.
    SMRiP07327. Positions 2-375.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07327.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1062.
    HOGENOMiHOG000294674.
    HOVERGENiHBG000195.
    InParanoidiP07327.
    KOiK13951.
    OMAiINATEND.
    OrthoDBiEOG72NRQ6.
    PhylomeDBiP07327.
    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]

    Sequencei

    Sequence statusi: Complete.

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

    P07327-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTAGKVIKC KAAVLWELKK PFSIEEVEVA PPKAHEVRIK MVAVGICGTD    50
    DHVVSGTMVT PLPVILGHEA AGIVESVGEG VTTVKPGDKV IPLAIPQCGK 100
    CRICKNPESN YCLKNDVSNP QGTLQDGTSR FTCRRKPIHH FLGISTFSQY 150
    TVVDENAVAK IDAASPLEKV CLIGCGFSTG YGSAVNVAKV TPGSTCAVFG 200
    LGGVGLSAIM GCKAAGAARI IAVDINKDKF AKAKELGATE CINPQDYKKP 250
    IQEVLKEMTD GGVDFSFEVI GRLDTMMASL LCCHEACGTS VIVGVPPDSQ 300
    NLSMNPMLLL TGRTWKGAIL GGFKSKECVP KLVADFMAKK FSLDALITHV 350
    LPFEKINEGF DLLHSGKSIR TILMF 375
    Length:375
    Mass (Da):39,859
    Last modified:January 23, 2007 - v2
    Checksum:iB6DF4D57080D9BC1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12963 mRNA. Translation: AAA51590.1.
    M12271 mRNA. Translation: AAA68131.1.
    BT019812 mRNA. Translation: AAV38615.1.
    AY948115 Genomic DNA. Translation: AAX20115.1.
    AK290558 mRNA. Translation: BAF83247.1.
    CH471057 Genomic DNA. Translation: EAX06094.1.
    BC074738 mRNA. Translation: AAH74738.1.
    BC117442 mRNA. Translation: AAI17443.1.
    BC126306 mRNA. Translation: AAI26307.1.
    M37066 Genomic DNA. Translation: AAA51591.1.
    CCDSiCCDS3648.1.
    PIRiS02265. DEHUAA.
    RefSeqiNP_000658.1. NM_000667.3.
    UniGeneiHs.654433.

    Genome annotation databases

    EnsembliENST00000209668; ENSP00000209668; ENSG00000187758.
    GeneIDi124.
    KEGGihsa:124.
    UCSCiuc003hur.2. human.

    Polymorphism databases

    DMDMi113390.

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12963 mRNA. Translation: AAA51590.1 .
    M12271 mRNA. Translation: AAA68131.1 .
    BT019812 mRNA. Translation: AAV38615.1 .
    AY948115 Genomic DNA. Translation: AAX20115.1 .
    AK290558 mRNA. Translation: BAF83247.1 .
    CH471057 Genomic DNA. Translation: EAX06094.1 .
    BC074738 mRNA. Translation: AAH74738.1 .
    BC117442 mRNA. Translation: AAI17443.1 .
    BC126306 mRNA. Translation: AAI26307.1 .
    M37066 Genomic DNA. Translation: AAA51591.1 .
    CCDSi CCDS3648.1.
    PIRi S02265. DEHUAA.
    RefSeqi NP_000658.1. NM_000667.3.
    UniGenei Hs.654433.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HSO X-ray 2.50 A/B 2-375 [» ]
    1U3T X-ray 2.49 A/B 2-375 [» ]
    ProteinModelPortali P07327.
    SMRi P07327. Positions 2-375.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106636. 2 interactions.
    IntActi P07327. 2 interactions.

    Chemistry

    BindingDBi P07327.
    ChEMBLi CHEMBL1970.
    DrugBanki DB00898. Ethanol.
    DB01213. Fomepizole.

    PTM databases

    PhosphoSitei P07327.

    Polymorphism databases

    DMDMi 113390.

    Proteomic databases

    PaxDbi P07327.
    PRIDEi P07327.

    Protocols and materials databases

    DNASUi 124.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000209668 ; ENSP00000209668 ; ENSG00000187758 .
    GeneIDi 124.
    KEGGi hsa:124.
    UCSCi uc003hur.2. human.

    Organism-specific databases

    CTDi 124.
    GeneCardsi GC04M100197.
    HGNCi HGNC:249. ADH1A.
    HPAi CAB009562.
    HPA047814.
    MIMi 103700. gene.
    neXtProti NX_P07327.
    PharmGKBi PA24570.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1062.
    HOGENOMi HOG000294674.
    HOVERGENi HBG000195.
    InParanoidi P07327.
    KOi K13951.
    OMAi INATEND.
    OrthoDBi EOG72NRQ6.
    PhylomeDBi P07327.
    TreeFami TF300429.

    Enzyme and pathway databases

    Reactomei REACT_121388. Abacavir metabolism.
    REACT_34. Ethanol oxidation.
    SABIO-RK P07327.

    Miscellaneous databases

    EvolutionaryTracei P07327.
    GeneWikii ADH1A.
    GenomeRNAii 124.
    NextBioi 495.
    PROi P07327.
    SOURCEi Search...

    Gene expression databases

    Bgeei P07327.
    CleanExi HS_ADH1A.
    Genevestigatori P07327.

    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-375, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2.
      Tissue: Liver.
    2. "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].
    3. "Molecular structure of the human alcohol dehydrogenase 1 gene."
      Matsuo Y., Yokoyama S.
      FEBS Lett. 243:57-60(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "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].
      Tissue: Heart.
    6. NIEHS SNPs program
      Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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: Brain.
    9. "The human class I alcohol dehydrogenase gene cluster: three genes are tandemly organized in an 80-kb-long segment of the genome."
      Yasunami M., Kikuchi I., Sarapata D., Yoshida A.
      Genomics 7:152-158(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
    10. "Structure of three class I human alcohol dehydrogenases complexed with isoenzyme specific formamide inhibitors."
      Gibbons B.J., Hurley T.D.
      Biochemistry 43:12555-12562(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) IN COMPLEX WITH NAD AND ZINC IONS.
    11. "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 (2.5 ANGSTROMS) IN COMPLEX WITH NAD AND ZINC IONS.

    Entry informationi

    Entry nameiADH1A_HUMAN
    AccessioniPrimary (citable) accession number: P07327
    Secondary accession number(s): A8K3E3, Q17R68
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 161 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3