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P00325

- ADH1B_HUMAN

UniProt

P00325 - ADH1B_HUMAN

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Protein
Alcohol dehydrogenase 1B
Gene
ADH1B, ADH2
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 activity, zinc-dependent Source: UniProtKB
  2. zinc ion binding Source: UniProtKB

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

BioCyciMetaCyc:MONOMER66-321.
ReactomeiREACT_34. Ethanol oxidation.
SABIO-RKP00325.

Names & Taxonomyi

Protein namesi
Recommended name:
Alcohol dehydrogenase 1B (EC:1.1.1.1)
Alternative name(s):
Alcohol dehydrogenase subunit beta
Gene namesi
Name:ADH1B
Synonyms:ADH2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:250. ADH1B.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

MIMi103720. gene+phenotype.
PharmGKBiPA24571.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 375374Alcohol dehydrogenase 1B
PRO_0000160661Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP00325.
PRIDEiP00325.

PTM databases

PhosphoSiteiP00325.

Expressioni

Gene expression databases

ArrayExpressiP00325.
BgeeiP00325.
CleanExiHS_ADH1B.
GenevestigatoriP00325.

Organism-specific databases

HPAiHPA047814.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi106637. 6 interactions.
IntActiP00325. 7 interactions.
STRINGi9606.ENSP00000306606.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 158
Beta strandi23 – 297
Beta strandi36 – 4510
Helixi48 – 547
Beta strandi56 – 583
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 strandi262 – 2687
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
1DEHX-ray2.20A/B2-375[»]
1HDXX-ray2.50A/B2-375[»]
1HDYX-ray2.50A/B2-375[»]
1HDZX-ray2.50A/B2-375[»]
1HSZX-ray2.20A/B2-375[»]
1HTBX-ray2.40A/B2-375[»]
1U3UX-ray1.60A/B2-375[»]
1U3VX-ray1.65A/B2-375[»]
3HUDX-ray3.20A/B2-375[»]
ProteinModelPortaliP00325.
SMRiP00325. Positions 2-375.

Miscellaneous databases

EvolutionaryTraceiP00325.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1062.
HOGENOMiHOG000294674.
HOVERGENiHBG000195.
InParanoidiP00325.
KOiK13951.
OrthoDBiEOG72NRQ6.
PhylomeDBiP00325.
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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P00325-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MSTAGKVIKC KAAVLWEVKK PFSIEDVEVA PPKAYEVRIK MVAVGICRTD    50
DHVVSGNLVT PLPVILGHEA AGIVESVGEG VTTVKPGDKV IPLFTPQCGK 100
CRVCKNPESN YCLKNDLGNP RGTLQDGTRR FTCRGKPIHH FLGTSTFSQY 150
TVVDENAVAK IDAASPLEKV CLIGCGFSTG YGSAVNVAKV TPGSTCAVFG 200
LGGVGLSAVM GCKAAGAARI IAVDINKDKF AKAKELGATE CINPQDYKKP 250
IQEVLKEMTD GGVDFSFEVI GRLDTMMASL LCCHEACGTS VIVGVPPASQ 300
NLSINPMLLL TGRTWKGAVY GGFKSKEGIP KLVADFMAKK FSLDALITHV 350
LPFEKINEGF DLLHSGKSIR TVLTF 375
Length:375
Mass (Da):39,855
Last modified:January 23, 2007 - v2
Checksum:i6962B9A0F967673B
GO
Isoform 2 (identifier: P00325-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-40: Missing.

Show »
Length:335
Mass (Da):35,412
Checksum:iA92B71F22E3CAFA4
GO

Polymorphismi

Three alleles are known: ADH1B*1 (ADH2*1) corresponding to variant beta-1, ADH1B*2 (ADH2*2) corresponding to variant beta-2, ADH1B*3 (ADH2*3) corresponding to variant beta-3. The sequence shown is that of allele ADH1B*1. The ADH1B*2 allele frequency in orientals is approximately 75%, whereas it is less than 5% in most Caucasian populations. ADH1B variations have been associated with protection against alcohol dependence and alcohol-related aerodigestive tract cancer [MIMi:103720].

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti48 – 481R → H in beta-2; allele ADH1B*2; common in Asian populations; associated with a lower risk of alcoholism. 7 Publications
Corresponds to variant rs1229984 [ dbSNP | Ensembl ].
VAR_000426
Natural varianti57 – 571N → K.2 Publications
Corresponds to variant rs1041969 [ dbSNP | Ensembl ].
VAR_019322
Natural varianti60 – 601T → S.1 Publication
Corresponds to variant rs6413413 [ dbSNP | Ensembl ].
VAR_019323
Natural varianti370 – 3701R → C in beta-3/Indianapolis; allele ADH1B*3; decreased NAD(H) binding. 3 Publications
Corresponds to variant rs2066702 [ dbSNP | Ensembl ].
VAR_000427

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4040Missing in isoform 2.
VSP_054847Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81I → M in AAA51592. 1 Publication
Sequence conflicti130 – 1301Missing AA sequence 1 Publication
Sequence conflicti166 – 1661P → K in AAA51592. 1 Publication
Sequence conflicti190 – 1901V → VV in CAA33487. 1 Publication
Sequence conflicti220 – 2201I → V in BAG62635. 1 Publication
Sequence conflicti230 – 2301F → K in AAA51884. 1 Publication
Sequence conflicti235 – 2351E → V in AAA51592. 1 Publication
Sequence conflicti338 – 3447Missing in BAG62635. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M24317 mRNA. Translation: AAA51884.1.
X03350 mRNA. Translation: CAA27056.1.
M24316
, M24308, M24309, M24310, M24311, M24312, M24313, M24314 Genomic DNA. Translation: AAB59496.1.
D00137 mRNA. Translation: BAA00084.1.
L38290
, L38283, L38284, L38285, L38286, L38287, L38288, L38289 Genomic DNA. Translation: AAB48003.1.
X15447
, X15448, X15449, X15450, X15451, X15452, X15453, X15454, X15455 Genomic DNA. Translation: CAA33487.1.
AF153821 mRNA. Translation: AAD37446.1.
DQ017646 Genomic DNA. Translation: AAY22180.1.
AK301018 mRNA. Translation: BAG62635.1.
AC097530 Genomic DNA. No translation available.
BC033009 mRNA. Translation: AAH33009.1.
M21692 mRNA. Translation: AAA51592.1.
AF040967 Genomic DNA. Translation: AAB96912.1.
CCDSiCCDS34033.1. [P00325-1]
CCDS68761.1. [P00325-2]
PIRiA23607. DEHUAB.
RefSeqiNP_000659.2. NM_000668.5.
NP_001273579.1. NM_001286650.1.
UniGeneiHs.4.

Genome annotation databases

EnsembliENST00000305046; ENSP00000306606; ENSG00000196616.
ENST00000394887; ENSP00000378351; ENSG00000196616.
GeneIDi125.
KEGGihsa:125.
UCSCiuc003hus.4. human. [P00325-1]

Polymorphism databases

DMDMi113394.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M24317 mRNA. Translation: AAA51884.1 .
X03350 mRNA. Translation: CAA27056.1 .
M24316
, M24308 , M24309 , M24310 , M24311 , M24312 , M24313 , M24314 Genomic DNA. Translation: AAB59496.1 .
D00137 mRNA. Translation: BAA00084.1 .
L38290
, L38283 , L38284 , L38285 , L38286 , L38287 , L38288 , L38289 Genomic DNA. Translation: AAB48003.1 .
X15447
, X15448 , X15449 , X15450 , X15451 , X15452 , X15453 , X15454 , X15455 Genomic DNA. Translation: CAA33487.1 .
AF153821 mRNA. Translation: AAD37446.1 .
DQ017646 Genomic DNA. Translation: AAY22180.1 .
AK301018 mRNA. Translation: BAG62635.1 .
AC097530 Genomic DNA. No translation available.
BC033009 mRNA. Translation: AAH33009.1 .
M21692 mRNA. Translation: AAA51592.1 .
AF040967 Genomic DNA. Translation: AAB96912.1 .
CCDSi CCDS34033.1. [P00325-1 ]
CCDS68761.1. [P00325-2 ]
PIRi A23607. DEHUAB.
RefSeqi NP_000659.2. NM_000668.5.
NP_001273579.1. NM_001286650.1.
UniGenei Hs.4.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DEH X-ray 2.20 A/B 2-375 [» ]
1HDX X-ray 2.50 A/B 2-375 [» ]
1HDY X-ray 2.50 A/B 2-375 [» ]
1HDZ X-ray 2.50 A/B 2-375 [» ]
1HSZ X-ray 2.20 A/B 2-375 [» ]
1HTB X-ray 2.40 A/B 2-375 [» ]
1U3U X-ray 1.60 A/B 2-375 [» ]
1U3V X-ray 1.65 A/B 2-375 [» ]
3HUD X-ray 3.20 A/B 2-375 [» ]
ProteinModelPortali P00325.
SMRi P00325. Positions 2-375.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106637. 6 interactions.
IntActi P00325. 7 interactions.
STRINGi 9606.ENSP00000306606.

Chemistry

BindingDBi P00325.
ChEMBLi CHEMBL3284.
DrugBanki DB01213. Fomepizole.
DB00157. NADH.

PTM databases

PhosphoSitei P00325.

Polymorphism databases

DMDMi 113394.

Proteomic databases

PaxDbi P00325.
PRIDEi P00325.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000305046 ; ENSP00000306606 ; ENSG00000196616 .
ENST00000394887 ; ENSP00000378351 ; ENSG00000196616 .
GeneIDi 125.
KEGGi hsa:125.
UCSCi uc003hus.4. human. [P00325-1 ]

Organism-specific databases

CTDi 125.
GeneCardsi GC04M100226.
HGNCi HGNC:250. ADH1B.
HPAi HPA047814.
MIMi 103720. gene+phenotype.
neXtProti NX_P00325.
PharmGKBi PA24571.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1062.
HOGENOMi HOG000294674.
HOVERGENi HBG000195.
InParanoidi P00325.
KOi K13951.
OrthoDBi EOG72NRQ6.
PhylomeDBi P00325.
TreeFami TF300429.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER66-321.
Reactomei REACT_34. Ethanol oxidation.
SABIO-RK P00325.

Miscellaneous databases

EvolutionaryTracei P00325.
GeneWikii ADH1B.
GenomeRNAii 125.
NextBioi 35465058.
PROi P00325.
SOURCEi Search...

Gene expression databases

ArrayExpressi P00325.
Bgeei P00325.
CleanExi HS_ADH1B.
Genevestigatori P00325.

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. "Molecular cloning of a full-length cDNA for human alcohol dehydrogenase."
    Ikuta T., Fujiyoshi T., Kurachi K., Yoshida A.
    Proc. Natl. Acad. Sci. U.S.A. 82:2703-2707(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. Erratum
    Ikuta T., Fujiyoshi T., Kurachi K., Yoshida A.
    Proc. Natl. Acad. Sci. U.S.A. 82:5578-5578(1985)
  3. "cDNA clones coding for the beta-subunit of human liver alcohol dehydrogenase have differently sized 3'-non-coding regions."
    Heden L.-O., Hoeoeg J.-O., Larsson K., Lake M., Lagerholm E., Holmgren A., Vallee B.L., Joernvall H., von Bahr-Lindstroem H.
    FEBS Lett. 194:327-332(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Molecular analysis of the human class I alcohol dehydrogenase gene family and nucleotide sequence of the gene encoding the beta subunit."
    Duester G., Smith M., Bilanchone V., Hatfield G.W.
    J. Biol. Chem. 261:2027-2033(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "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] (ISOFORM 1).
  6. "Molecular characterization of cDNA clones encoding the human alcohol dehydrogenase beta 1 and the evolutionary relationship to the other class I subunits alpha and gamma."
    Yokoyama S., Yokoyama R., Rotwein P.
    Jpn. J. Genet. 62:241-256(1987)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  7. "Nucleotide sequence of the ADH2(3) gene encoding the human alcohol dehydrogenase beta 3 subunit."
    Carr L.G., Xu Y., Ho W.H., Edenberg H.J.
    Alcohol. Clin. Exp. Res. 13:594-596(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-48; LYS-57 AND CYS-370.
    Tissue: Liver.
  8. "The genes for human alcohol dehydrogenases beta 1 and beta 2 differ by only one nucleotide."
    Matsuo Y., Yokoyama R., Yokoyama S.
    Eur. J. Biochem. 183:317-320(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HIS-48.
  9. Polin L., Hey-Chi H.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT HIS-48.
    Tissue: Liver.
  10. NIEHS SNPs program
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-48; SER-60 AND CYS-370.
  11. "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] (ISOFORM 2).
    Tissue: Small intestine.
  12. "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], VARIANT HIS-48.
  13. "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] (ISOFORM 1).
    Tissue: Testis.
  14. "Human liver alcohol dehydrogenase. 1. The primary structure of the beta 1 beta 1 isoenzyme."
    Hempel J., Buhler R., Kaiser R., Holmquist B., de Zalenski C., von Wartburg J.-P., Vallee B.L., Joernvall H.
    Eur. J. Biochem. 145:437-445(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-375, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2.
  15. "Genotyping of human alcohol dehydrogenases at the ADH2 and ADH3 loci following DNA sequence amplification."
    Xu Y.L., Carr L.G., Bosron W.F., Li T.K., Edenberg H.J.
    Genomics 2:209-214(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA], VARIANT LYS-57.
  16. Osier M., Speed W.C., Seaman M.I., Kidd K.K.
    Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-86.
  17. "Human liver alcohol dehydrogenase: amino acid substitution in the beta 2 beta 2 Oriental isozyme explains functional properties, establishes an active site structure, and parallels mutational exchanges in the yeast enzyme."
    Joernvall H., Hempel J., Vallee B.L., Bosron W.F., Li T.-K.
    Proc. Natl. Acad. Sci. U.S.A. 81:3024-3028(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HIS-48.
  18. "The human beta 3 alcohol dehydrogenase subunit differs from beta 1 by a Cys for Arg-369 substitution which decreases NAD(H) binding."
    Burnell J.C., Carr L.G., Dwulet F.E., Edenberg H.J., Li T.-K., Bosron W.F.
    Biochem. Biophys. Res. Commun. 146:1127-1133(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CYS-370.
  19. "Structure of human beta 1 beta 1 alcohol dehydrogenase: catalytic effects of non-active-site substitutions."
    Hurley T.D., Bosron W.F., Hamilton J.A., Amzel L.M.
    Proc. Natl. Acad. Sci. U.S.A. 88:8149-8153(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
  20. "Structures of three human beta alcohol dehydrogenase variants. Correlations with their functional differences."
    Hurley T.D., Bosron W.F., Stone C.L., Amzel L.M.
    J. Mol. Biol. 239:415-429(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
  21. "X-ray structure of human beta3beta3 alcohol dehydrogenase. The contribution of ionic interactions to coenzyme binding."
    Davis G.J., Bosron W.F., Stone C.L., Owusu-Dekyi K., Hurley T.D.
    J. Biol. Chem. 271:17057-17061(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
  22. "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 (2.2 ANGSTROMS).
  23. "Genetic polymorphism of alcohol dehydrogenase in Europeans: the ADH2*2 allele decreases the risk for alcoholism and is associated with ADH3*1."
    Borras E., Coutelle C., Rosell A., Fernandez-Muixi F., Broch M., Crosas B., Hjelmqvist L., Lorenzo A., Gutierrez C., Santos M., Szczepanek M., Heilig M., Quattrocchi P., Farres J., Vidal F., Richart C., Mach T., Bogdal J.
    , Joernvall H., Seitz H.K., Couzigou P., Pares X.
    Hepatology 31:984-989(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION OF VARIANT HIS-48 WITH LOWER RISK OF ALCOHOLISM.

Entry informationi

Entry nameiADH1B_HUMAN
AccessioniPrimary (citable) accession number: P00325
Secondary accession number(s): A8MYN5
, B4DRS9, B4DVC3, Q13711, Q4ZGI9, Q96KI7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 165 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. 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

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