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P07327

- ADH1A_HUMAN

UniProt

P07327 - ADH1A_HUMAN

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Protein

Alcohol dehydrogenase 1A

Gene
ADH1A, ADH1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 (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
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

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.

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.

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 DB01213. Fomepizole.
DB00157. NADH.

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

« 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: September 3, 2014
This is version 160 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

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