Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P07327 (ADH1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 1A

EC=1.1.1.1
Alternative name(s):
Alcohol dehydrogenase subunit alpha
Gene names
Name:ADH1A
Synonyms:ADH1
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.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 375374Alcohol dehydrogenase 1A
PRO_0000160658

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.1

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P07327 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: B6DF4D57080D9BC1

FASTA37539,859
        10         20         30         40         50         60 
MSTAGKVIKC KAAVLWELKK PFSIEEVEVA PPKAHEVRIK MVAVGICGTD DHVVSGTMVT 

        70         80         90        100        110        120 
PLPVILGHEA AGIVESVGEG VTTVKPGDKV IPLAIPQCGK CRICKNPESN YCLKNDVSNP 

       130        140        150        160        170        180 
QGTLQDGTSR FTCRRKPIHH FLGISTFSQY TVVDENAVAK IDAASPLEKV CLIGCGFSTG 

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

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

       310        320        330        340        350        360 
NLSMNPMLLL TGRTWKGAIL GGFKSKECVP KLVADFMAKK FSLDALITHV LPFEKINEGF 

       370 
DLLHSGKSIR TILMF 

« Hide

References

« Hide 'large scale' references
[1]"cDNA and protein structure for the alpha subunit of human liver alcohol dehydrogenase."
von Bahr-Lindstroem H., Hoeoeg J.-O., Heden L.-O., Kaiser R., Fleetwood L., Larsson K., Lake M., Holmquist B., Holmgren A., Hempel J., Vallee B.L., Joernvall H.
Biochemistry 25:2465-2470(1986) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS3648.1.
PIRDEHUAA. S02265.
RefSeqNP_000658.1. NM_000667.3.
UniGeneHs.654433.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HSOX-ray2.50A/B2-375[»]
1U3TX-ray2.49A/B2-375[»]
ProteinModelPortalP07327.
SMRP07327. Positions 2-375.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106636. 2 interactions.
IntActP07327. 2 interactions.

Chemistry

BindingDBP07327.
ChEMBLCHEMBL1970.
DrugBankDB01213. Fomepizole.
DB00157. NADH.

PTM databases

PhosphoSiteP07327.

Polymorphism databases

DMDM113390.

Proteomic databases

PaxDbP07327.
PRIDEP07327.

Protocols and materials databases

DNASU124.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000209668; ENSP00000209668; ENSG00000187758.
GeneID124.
KEGGhsa:124.
UCSCuc003hur.2. human.

Organism-specific databases

CTD124.
GeneCardsGC04M100197.
HGNCHGNC:249. ADH1A.
HPACAB009562.
HPA047814.
MIM103700. gene.
neXtProtNX_P07327.
PharmGKBPA24570.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1062.
HOGENOMHOG000294674.
HOVERGENHBG000195.
InParanoidP07327.
KOK13951.
OMAINATEND.
OrthoDBEOG72NRQ6.
PhylomeDBP07327.
TreeFamTF300429.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
SABIO-RKP07327.

Gene expression databases

BgeeP07327.
CleanExHS_ADH1A.
GenevestigatorP07327.

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

EvolutionaryTraceP07327.
GeneWikiADH1A.
GenomeRNAi124.
NextBio495.
PROP07327.
SOURCESearch...

Entry information

Entry nameADH1A_HUMAN
AccessionPrimary (citable) accession number: P07327
Secondary accession number(s): A8K3E3, Q17R68
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 159 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 chromosome 4

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