Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P00326

- ADH1G_HUMAN

UniProt

P00326 - ADH1G_HUMAN

(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)

Protein

Alcohol dehydrogenase 1C

Gene

ADH1C

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

Zn2+Note: Binds 2 Zn(2+) 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: UniProtKB
  2. zinc ion binding Source: InterPro

GO - Biological processi

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

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

ReactomeiREACT_34. Ethanol oxidation.
SABIO-RKP00326.

Names & Taxonomyi

Protein namesi
Recommended name:
Alcohol dehydrogenase 1C (EC:1.1.1.1)
Alternative name(s):
Alcohol dehydrogenase subunit gamma
Gene namesi
Name:ADH1C
Synonyms:ADH3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:251. ADH1C.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24572.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 375374Alcohol dehydrogenase 1CPRO_0000160664Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP00326.

PTM databases

PhosphoSiteiP00326.

Expressioni

Gene expression databases

CleanExiHS_ADH1C.
GenevestigatoriP00326.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi106638. 2 interactions.
STRINGi9606.ENSP00000209668.

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 strandi117 – 1193Combined 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 strandi262 – 2687Combined 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
1DDAmodel-A/B1-375[»]
1HT0X-ray2.00A/B2-375[»]
1U3WX-ray1.45A/B2-375[»]
ProteinModelPortaliP00326.
SMRiP00326. Positions 2-375.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00326.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00430000030800.
HOVERGENiHBG000195.
InParanoidiP00326.
KOiK13951.

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.

P00326-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSTAGKVIKC KAAVLWELKK PFSIEEVEVA PPKAHEVRIK MVAAGICRSD
60 70 80 90 100
EHVVSGNLVT PLPVILGHEA AGIVESVGEG VTTVKPGDKV IPLFTPQCGK
110 120 130 140 150
CRICKNPESN YCLKNDLGNP RGTLQDGTRR FTCSGKPIHH FVGVSTFSQY
160 170 180 190 200
TVVDENAVAK IDAASPLEKV CLIGCGFSTG YGSAVKVAKV TPGSTCAVFG
210 220 230 240 250
LGGVGLSVVM GCKAAGAARI IAVDINKDKF AKAKELGATE CINPQDYKKP
260 270 280 290 300
IQEVLKEMTD GGVDFSFEVI GRLDTMMASL LCCHEACGTS VIVGVPPDSQ
310 320 330 340 350
NLSINPMLLL TGRTWKGAIF GGFKSKESVP KLVADFMAKK FSLDALITNI
360 370
LPFEKINEGF DLLRSGKSIR TVLTF
Length:375
Mass (Da):39,868
Last modified:January 23, 2007 - v2
Checksum:i414D73CC4C104C84
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti130 – 1301Missing AA sequence (PubMed:6391921)Curated
Sequence conflicti171 – 1711C → R in AAH67421. (PubMed:15489334)Curated

Polymorphismi

Two main alleles are known, ADH3*1 or gamma-1 has Arg-272/Ile-350 while ADH3*2 or gamma-2 has Gln-272/Val-350. ADH3*1 is associated with a fast rate of ethanol oxidation and ADH3*2 with a slow rate.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti48 – 481R → H.1 Publication
Corresponds to variant rs35385902 [ dbSNP | Ensembl ].
VAR_023992
Natural varianti166 – 1661P → S.1 Publication
VAR_023993
Natural varianti272 – 2721R → Q in allele ADH3*2/gamma-2. 3 Publications
Corresponds to variant rs1693482 [ dbSNP | Ensembl ].
VAR_000428
Natural varianti350 – 3501I → V in allele ADH3*2/gamma-2. 3 Publications
Corresponds to variant rs698 [ dbSNP | Ensembl ].
VAR_000429
Natural varianti352 – 3521P → T.1 Publication
Corresponds to variant rs35719513 [ dbSNP | Ensembl ].
VAR_023994

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04299 mRNA. Translation: CAA27842.1.
X04350 mRNA. Translation: CAA27876.1.
M12272 mRNA. Translation: AAC41757.1.
D11067 Genomic DNA. Translation: BAC06856.1.
DQ088981 Genomic DNA. Translation: AAY68222.1.
AC097530 Genomic DNA. No translation available.
BC062476 mRNA. Translation: AAH62476.1.
BC066227 mRNA. Translation: AAH66227.1.
BC066228 mRNA. Translation: AAH66228.1.
BC067419 mRNA. Translation: AAH67419.1.
BC067420 mRNA. Translation: AAH67420.1.
BC067421 mRNA. Translation: AAH67421.1.
BC067422 mRNA. Translation: AAH67422.1.
BC074771 mRNA. Translation: AAH74771.1.
BC074786 mRNA. Translation: AAH74786.1.
PIRiC25428. DEHUAG.
RefSeqiNP_000660.1. NM_000669.4.
UniGeneiHs.654537.

Genome annotation databases

EnsembliENST00000515683; ENSP00000426083; ENSG00000248144.
GeneIDi126.
KEGGihsa:126.
UCSCiuc031sgp.1. human.

Polymorphism databases

DMDMi113398.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04299 mRNA. Translation: CAA27842.1 .
X04350 mRNA. Translation: CAA27876.1 .
M12272 mRNA. Translation: AAC41757.1 .
D11067 Genomic DNA. Translation: BAC06856.1 .
DQ088981 Genomic DNA. Translation: AAY68222.1 .
AC097530 Genomic DNA. No translation available.
BC062476 mRNA. Translation: AAH62476.1 .
BC066227 mRNA. Translation: AAH66227.1 .
BC066228 mRNA. Translation: AAH66228.1 .
BC067419 mRNA. Translation: AAH67419.1 .
BC067420 mRNA. Translation: AAH67420.1 .
BC067421 mRNA. Translation: AAH67421.1 .
BC067422 mRNA. Translation: AAH67422.1 .
BC074771 mRNA. Translation: AAH74771.1 .
BC074786 mRNA. Translation: AAH74786.1 .
PIRi C25428. DEHUAG.
RefSeqi NP_000660.1. NM_000669.4.
UniGenei Hs.654537.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DDA model - A/B 1-375 [» ]
1HT0 X-ray 2.00 A/B 2-375 [» ]
1U3W X-ray 1.45 A/B 2-375 [» ]
ProteinModelPortali P00326.
SMRi P00326. Positions 2-375.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106638. 2 interactions.
STRINGi 9606.ENSP00000209668.

Chemistry

BindingDBi P00326.
ChEMBLi CHEMBL3285.
DrugBanki DB00898. Ethanol.
DB01213. Fomepizole.

PTM databases

PhosphoSitei P00326.

Polymorphism databases

DMDMi 113398.

Proteomic databases

PRIDEi P00326.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000515683 ; ENSP00000426083 ; ENSG00000248144 .
GeneIDi 126.
KEGGi hsa:126.
UCSCi uc031sgp.1. human.

Organism-specific databases

CTDi 126.
GeneCardsi GC04M100257.
HGNCi HGNC:251. ADH1C.
MIMi 103730. gene.
neXtProti NX_P00326.
PharmGKBi PA24572.
GenAtlasi Search...

Phylogenomic databases

GeneTreei ENSGT00430000030800.
HOVERGENi HBG000195.
InParanoidi P00326.
KOi K13951.

Enzyme and pathway databases

Reactomei REACT_34. Ethanol oxidation.
SABIO-RK P00326.

Miscellaneous databases

ChiTaRSi ADH1C. human.
EvolutionaryTracei P00326.
GeneWikii ADH1C.
GenomeRNAii 126.
NextBioi 503.
PROi P00326.
SOURCEi Search...

Gene expression databases

CleanExi HS_ADH1C.
Genevestigatori P00326.

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. "The gamma 1 and gamma 2 subunits of human liver alcohol dehydrogenase. cDNA structures, two amino acid replacements, and compatibility with changes in the enzymatic properties."
    Hoeoeg J.-O., Heden L.-O., Larsson K., Joernvall H.
    Eur. J. Biochem. 159:215-218(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS GAMMA-2 GLN-272 AND VAL-350.
    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].
    Tissue: Liver.
  3. "Molecular structure of the human alcohol dehydrogenase 3 gene."
    Yokoyama S., Matsuo Y., Rajasekharan S., Yokoyama R.
    Jpn. J. Genet. 67:167-171(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. NIEHS SNPs program
    Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-48; SER-166; GLN-272; VAL-350 AND THR-352.
  5. "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].
  6. "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], VARIANTS GAMMA-2 GLN-272 AND VAL-350.
    Tissue: Brain and Femoral artery.
  7. "Human liver alcohol dehydrogenase. 2. The primary structure of the gamma 1 protein chain."
    Buhler R., Hempel J., Kaiser R., de Zalenski C., von Wartburg J.-P., Joernvall H.
    Eur. J. Biochem. 145:447-453(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-375, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2.
    Tissue: Liver.
  8. "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.
  9. "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.

Entry informationi

Entry nameiADH1G_HUMAN
AccessioniPrimary (citable) accession number: P00326
Secondary accession number(s): Q4PJ18
, Q5WRV0, Q6LBW4, Q6NWV0, Q6NZA7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 153 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.

Caution

The reference genome assembly, GRCh37, describes a non-functional copy of that gene with a stop codon at position 78. However, this premature stop codon is not present in available mRNAs.Curated

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