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Protein

Alcohol dehydrogenase 1A

Gene

ADH1A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Zn2+Note: Binds 2 Zn2+ 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. 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
Complete GO annotation...

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
Complete GO annotation...

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

MaxQBiP07327.
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 – 158Combined sources
Beta strandi23 – 297Combined sources
Beta strandi36 – 4510Combined sources
Helixi48 – 547Combined sources
Beta strandi62 – 654Combined sources
Beta strandi69 – 779Combined sources
Beta strandi89 – 924Combined sources
Beta strandi99 – 1013Combined sources
Helixi102 – 1054Combined sources
Beta strandi116 – 1194Combined sources
Beta strandi131 – 1333Combined sources
Beta strandi136 – 1394Combined sources
Turni142 – 1443Combined sources
Beta strandi147 – 1548Combined sources
Helixi155 – 1573Combined sources
Beta strandi158 – 1603Combined sources
Helixi167 – 1704Combined sources
Helixi171 – 1744Combined sources
Helixi176 – 18510Combined sources
Turni186 – 1883Combined sources
Beta strandi195 – 1995Combined sources
Helixi203 – 21412Combined sources
Beta strandi218 – 2236Combined sources
Helixi227 – 2293Combined sources
Helixi230 – 2356Combined sources
Beta strandi239 – 2424Combined sources
Helixi244 – 2463Combined sources
Helixi251 – 2588Combined sources
Turni259 – 2613Combined sources
Beta strandi263 – 2686Combined sources
Helixi273 – 28210Combined sources
Turni285 – 2873Combined sources
Beta strandi289 – 2924Combined sources
Beta strandi302 – 3043Combined sources
Helixi307 – 3104Combined sources
Beta strandi314 – 3174Combined sources
Helixi320 – 3223Combined sources
Helixi325 – 33713Combined sources
Helixi344 – 3463Combined sources
Beta strandi347 – 3526Combined sources
Helixi353 – 3553Combined sources
Helixi356 – 3649Combined sources
Beta strandi369 – 3746Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00430000030800.
HOGENOMiHOG000294674.
HOVERGENiHBG000195.
InParanoidiP07327.
KOiK13951.
OMAiLGPGCTH.
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

        10         20         30         40         50
MSTAGKVIKC KAAVLWELKK PFSIEEVEVA PPKAHEVRIK MVAVGICGTD
60 70 80 90 100
DHVVSGTMVT PLPVILGHEA AGIVESVGEG VTTVKPGDKV IPLAIPQCGK
110 120 130 140 150
CRICKNPESN YCLKNDVSNP QGTLQDGTSR FTCRRKPIHH FLGISTFSQY
160 170 180 190 200
TVVDENAVAK IDAASPLEKV CLIGCGFSTG YGSAVNVAKV TPGSTCAVFG
210 220 230 240 250
LGGVGLSAIM GCKAAGAARI IAVDINKDKF AKAKELGATE CINPQDYKKP
260 270 280 290 300
IQEVLKEMTD GGVDFSFEVI GRLDTMMASL LCCHEACGTS VIVGVPPDSQ
310 320 330 340 350
NLSMNPMLLL TGRTWKGAIL GGFKSKECVP KLVADFMAKK FSLDALITHV
360 370
LPFEKINEGF DLLHSGKSIR TILMF
Length:375
Mass (Da):39,859
Last modified:January 23, 2007 - v2
Checksum:iB6DF4D57080D9BC1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HSOX-ray2.50A/B2-375[»]
1U3TX-ray2.49A/B2-375[»]
ProteinModelPortaliP07327.
SMRiP07327. Positions 2-375.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106636. 2 interactions.
IntActiP07327. 2 interactions.

Chemistry

BindingDBiP07327.
ChEMBLiCHEMBL2363044.
DrugBankiDB00898. Ethanol.
DB01213. Fomepizole.

PTM databases

PhosphoSiteiP07327.

Polymorphism databases

DMDMi113390.

Proteomic databases

MaxQBiP07327.
PaxDbiP07327.
PRIDEiP07327.

Protocols and materials databases

DNASUi124.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi124.
GeneCardsiGC04M100197.
HGNCiHGNC:249. ADH1A.
HPAiCAB009562.
HPA047814.
MIMi103700. gene.
neXtProtiNX_P07327.
PharmGKBiPA24570.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1062.
GeneTreeiENSGT00430000030800.
HOGENOMiHOG000294674.
HOVERGENiHBG000195.
InParanoidiP07327.
KOiK13951.
OMAiLGPGCTH.
OrthoDBiEOG72NRQ6.
PhylomeDBiP07327.
TreeFamiTF300429.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP07327.
GeneWikiiADH1A.
GenomeRNAii124.
NextBioi495.
PROiP07327.
SOURCEiSearch...

Gene expression databases

BgeeiP07327.
CleanExiHS_ADH1A.
GenevestigatoriP07327.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: January 7, 2015
This is version 164 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.