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UniProtKB/Swiss-Prot entry P05091


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ALDH2_HUMAN
Primary accession number P05091
Secondary accession numbers Q03639 Q6IB13 Q6IV71
Integrated into Swiss-Prot on August 13, 1987
Sequence was last modified on January 1, 1990 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 123)
Name and origin of the protein
Protein name Aldehyde dehydrogenase, mitochondrial [Precursor]
Synonyms EC 1.2.1.3
ALDH class 2
ALDHI
ALDH-E2
Gene name
Name: ALDH2
Synonyms: ALDM
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Muscle;
DOI=10.1016/0014-5793(87)80152-7; PubMed=3582651 [NCBI, ExPASy, EBI, Israel, Japan]
Braun T., Bober E., Singh S., Agarwal D.P., Goedde H.W.;
"Evidence for a signal peptide at the amino-terminal end of human mitochondrial aldehyde dehydrogenase.";
FEBS Lett. 215:233-236(1987).
[2]
ERRATUM, AND SEQUENCE REVISION TO N-TERMINUS.
Braun T., Bober E., Singh S., Agarwal D.P., Goedde H.W.;
FEBS Lett. 233:440-440(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Muscle;
DOI=10.1093/nar/15.7.3179; PubMed=3562250 [NCBI, ExPASy, EBI, Israel, Japan]
Braun T., Bober E., Singh S., Agarwal D.P., Goedde H.W.;
"Isolation and sequence analysis of a full length cDNA clone coding for human mitochondrial aldehyde dehydrogenase.";
Nucleic Acids Res. 15:3179-3179(1987).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0888-7543(88)90109-7; PubMed=2838413 [NCBI, ExPASy, EBI, Israel, Japan]
Hsu L.C., Bendel R.E., Yoshida A.;
"Genomic structure of the human mitochondrial aldehyde dehydrogenase gene.";
Genomics 2:57-65(1988).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
Lassen N., Estey T., Vasiliou V.;
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Lymph;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 18-517.
TISSUE=Liver;
DOI=10.1111/j.1432-1033.1985.tb09260.x; PubMed=4065146 [NCBI, ExPASy, EBI, Israel, Japan]
Hempel J., Kaiser R., Joernvall H.;
"Mitochondrial aldehyde dehydrogenase from human liver. Primary structure, differences in relation to the cytosolic enzyme, and functional correlations.";
Eur. J. Biochem. 153:13-28(1985).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 119-517.
TISSUE=Liver;
PubMed=2987944 [NCBI, ExPASy, EBI, Israel, Japan]
Hsu L.C., Tani K., Fujiyoshi T., Kurachi K., Yoshida A.;
"Cloning of cDNAs for human aldehyde dehydrogenases 1 and 2.";
Proc. Natl. Acad. Sci. U.S.A. 82:3771-3775(1985).
[10]
NUCLEOTIDE SEQUENCE OF 119-517.
DOI=10.1016/0741-8329(85)90024-2; PubMed=4015823 [NCBI, ExPASy, EBI, Israel, Japan]
Yoshida A., Ikawa M., Hsu L.C., Tani K.;
"Molecular abnormality and cDNA cloning of human aldehyde dehydrogenases.";
Alcohol 2:103-106(1985).
[11]
PROTEIN SEQUENCE OF 160-172 AND 325-338, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[12]
PROTEIN SEQUENCE OF 196-226 AND 325-338.
TISSUE=Adipocyte;
DOI=10.1042/BJ20040647; PubMed=15242332 [NCBI, ExPASy, EBI, Israel, Japan]
Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.;
"Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes.";
Biochem. J. 383:237-248(2004).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 214-500, AND VARIANT VAL-337.
TISSUE=Liver;
PubMed=3610592 [NCBI, ExPASy, EBI, Israel, Japan]
Agarwal D.P., Goedde H.W.;
"Human aldehyde dehydrogenase isozymes and alcohol sensitivity.";
Isozymes Curr. Top. Biol. Med. Res. 16:21-48(1987).
[14]
DESCRIPTION OF ORIGIN OF CONFLICTS BETWEEN THE SEQUENCE DESCRIBED IN PUBMED:4065146 AND DNA SEQUENCES.
DOI=10.1016/0014-5793(87)80198-9; PubMed=3653404 [NCBI, ExPASy, EBI, Israel, Japan]
Hempel J., Hoeoeg J.-O., Joernvall H.;
"Mitochondrial aldehyde dehydrogenase. Homology of putative targeting sequence to that of carbamyl phosphate synthetase I revealed by correlation of cDNA and protein data.";
FEBS Lett. 222:95-98(1987).
[15]
X-RAY CRYSTALLOGRAPHY (2.58 ANGSTROMS).
PubMed=10631996 [NCBI, ExPASy, EBI, Israel, Japan]
Ni L., Zhou J., Hurley T.D., Weiner H.;
"Human liver mitochondrial aldehyde dehydrogenase: three-dimensional structure and the restoration of solubility and activity of chimeric forms.";
Protein Sci. 8:2784-2790(1999).
[16]
VARIANT LYS-504.
PubMed=6582480 [NCBI, ExPASy, EBI, Israel, Japan]
Yoshida A., Huang I.-Y., Ikawa M.;
"Molecular abnormality of an inactive aldehyde dehydrogenase variant commonly found in Orientals.";
Proc. Natl. Acad. Sci. U.S.A. 81:258-261(1984).
[17]
VARIANT LYS-496.
PubMed=8561277 [NCBI, ExPASy, EBI, Israel, Japan]
Novoradovsky A., Tsai S.J., Goldfarb L., Peterson R., Long J.C., Goldman D.;
"Mitochondrial aldehyde dehydrogenase polymorphism in Asian and American Indian populations: detection of new ALDH2 alleles.";
Alcohol. Clin. Exp. Res. 19:1105-1110(1995).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X05409; CAA28990.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y00109; CAA68290.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M20456; AAA51693.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M20444; AAA51693.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M20445; AAA51693.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M20446; AAA51693.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M20447; AAA51693.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M20448; AAA51693.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M20449; AAA51693.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M20450; AAA51693.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M20451; AAA51693.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M20452; AAA51693.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M20453; AAA51693.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M20454; AAA51693.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY621070; AAT41621.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR456991; CAG33272.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002967; AAH02967.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC071839; AAH71839.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K03001; AAB59500.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M26760; AAA51694.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M54931; AAA62825.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A29975; DEHUE2.
RefSeq NP_000681.2; -.
UniGene Hs.632733
3D structure databases
PDB
1CW3; X-ray; 2.58 A; A/B/C/D/E/F/G/H=24-517.[ExPASy / RCSB / EBI]
1NZW; X-ray; 2.65 A; A/B/C/D/E/F/G/H=18-517.[ExPASy / RCSB / EBI]
1NZX; X-ray; 2.45 A; A/B/C/D/E/F/G/H=18-517.[ExPASy / RCSB / EBI]
1NZZ; X-ray; 2.45 A; A/B/C/D/E/F/G/H=18-517.[ExPASy / RCSB / EBI]
1O00; X-ray; 2.60 A; A/B/C/D/E/F/G/H=18-517.[ExPASy / RCSB / EBI]
1O01; X-ray; 2.15 A; A/B/C/D/E/F/G/H=18-517.[ExPASy / RCSB / EBI]
1O02; X-ray; 1.90 A; A/B/C/D/E/F/G/H=18-517.[ExPASy / RCSB / EBI]
1O04; X-ray; 1.42 A; A/B/C/D/E/F/G/H=18-517.[ExPASy / RCSB / EBI]
1O05; X-ray; 2.25 A; A/B/C/D/E/F/G/H=18-517.[ExPASy / RCSB / EBI]
1OF7; X-ray; 2.40 A; A/B/C/D/E/F/G/H=18-517.[ExPASy / RCSB / EBI]
1ZUM; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L=18-517.[ExPASy / RCSB / EBI]
2ONM; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=18-517.[ExPASy / RCSB / EBI]
2ONN; X-ray; 2.75 A; A/B/C/D/E/F/G/H=18-517.[ExPASy / RCSB / EBI]
2ONO; X-ray; 2.15 A; A/B/C/D/E/F/G/H=18-517.[ExPASy / RCSB / EBI]
2ONP; X-ray; 2.00 A; A/B/C/D/E/F/G/H=18-517.[ExPASy / RCSB / EBI]
2VLE; X-ray; 2.40 A; A/B/C/D/E/F/G/H=24-517.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1CW3; -.
1NZW; -.
1NZX; -.
1NZZ; -.
1O00; -.
1O01; -.
1O02; -.
1O04; -.
1O05; -.
1OF7; -.
1ZUM; -.
2ONM; -.
2ONN; -.
2ONO; -.
2ONP; -.
2VLE; -.
DisProt DP00383; -.
ModBase P05091.
Protein-protein interaction databases
IntAct P05091; -.
PTM databases
PhosphoSite P05091; -.
Enzyme and pathway databases
BioCyc MetaCyc:MON-39; -.
Reactome REACT_2063; Metabolism of xenobiotics.
2D gel databases
REPRODUCTION-2DPAGE IPI00006663; -.
P05091; -.
Organism-specific databases
H-InvDB HIX0011002; -.
HGNC HGNC:404; ALDH2.
GenAtlas ALDH2.
MIM 100650; gene+phenotype. [NCBI / EBI]
PharmGKB PA24696; -.
GeneCards P05091.
Gene expression databases
ArrayExpress P05091; -.
CleanEx HS_ALDH2; -.
GermOnline ENSG00000111275; Homo sapiens.
Ontologies
GO
GO:0005759; Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004029; Molecular function: aldehyde dehydrogenase (NAD) activity (traceable author statement from ProtInc).
GO:0004030; Molecular function: aldehyde dehydrogenase [NAD(P)+] activity (traceable author statement from ProtInc).
GO:0009055; Molecular function: electron carrier activity (traceable author statement from UniProtKB).
GO:0005975; Biological process: carbohydrate metabolic process (traceable author statement from ProtInc).
GO:0006066; Biological process: cellular alcohol metabolic process (traceable author statement from ProtInc).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR016160; Ald_DHase_CS.
IPR016162; Ald_DHase_N.
IPR015590; Aldehyde_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
PANTHER PTHR11699; Aldehyde_dehyd; 1.
Pfam PF00171; Aldedh; 1.
Pfam graphical view of domain structure.
PROSITE PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PS00687; ALDEHYDE_DEHYDR_GLU; 1.
ProtoNet P05091.
Proteomic databases
PeptideAtlas P05091; -.
Genome annotation databases
Ensembl ENSG00000111275; Homo sapiens. [Contig view]
GeneID 217; -.
KEGG hsa:217; -.
NMPDR fig|9606.3.peg.8268; -.
Phylogenomic databases
HOGENOM P05091; -.
HOVERGEN P05091; -.
Other
DrugBank DB00822; Disulfiram.
DB00536; Guanidine.
DB00157; NADH.
DB00727; Nitroglycerin.
NextBio 878; -.
SOURCE ALDH2; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase; Polymorphism; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    17  17     Mitochondrion. 
CHAIN   18   517  500     Aldehyde dehydrogenase, mitochondrial. PRO_0000007168
NP_BIND   262   267  6     NAD (By similarity). 
ACT_SITE   285   285        Proton acceptor. 
ACT_SITE   319   319        Nucleophile. 
SITE   186   186  1     Transition state stabilizer. 
MOD_RES   368   368        N6-acetyllysine (By similarity). 
VARIANT   337   337  1     E -> V (in dbSNP:rs1062136 [NCBI]). VAR_011869 [3D]
VARIANT   496   496  1     E -> K (in allele ALDH2*3). VAR_011302 [3D]
VARIANT   504   504  1     E -> K (in allele ALDH2*2; drastic reduction of enzyme activity; dbSNP:rs671 [NCBI]). VAR_002248 [3D]
CONFLICT   7    12        RFGPRL -> ARAPP (in Ref. 1; CAA28990). 
CONFLICT   18    18        S -> A (in Ref. 8; AA sequence). 
CONFLICT   60    60        S -> F (in Ref. 6; CAG33272). 
CONFLICT   80    85        VKAARA -> REGRPG (in Ref. 1; CAA28990). 
CONFLICT   101   101        R -> S (in Ref. 1; CAA28990). 
CONFLICT   116   116        R -> Q (in Ref. 5; AAT41621). 
CONFLICT   216   216        L -> S (in Ref. 13; AAA62825). 
CONFLICT   218   218        A -> R (in Ref. 13; AAA62825). 
CONFLICT   247   247        A -> P (in Ref. 13; AAA62825). 
CONFLICT   362   362        V -> L (in Ref. 6; CAG33272). 
CONFLICT   380   380        E -> Q (in Ref. 4; AAA51693). 
STRAND   38    41  4      
STRAND   44    46  3      
STRAND   53    57  5      
TURN   59    61  3      
STRAND   64    69  6      
HELIX   73    86  14      
HELIX   92    95  4      
HELIX   98   114  17      
HELIX   116   127  12      
HELIX   131   136  6      
HELIX   138   152  15      
TURN   153   155  3      
STRAND   158   161  4      
STRAND   164   175  12      
STRAND   178   182  5      
STRAND   185   187  3      
HELIX   188   201  14      
STRAND   205   209  5      
HELIX   216   228  13      
STRAND   234   237  4      
TURN   242   244  3      
HELIX   245   250  6      
STRAND   257   262  6      
HELIX   264   276  13      
STRAND   281   285  5      
STRAND   290   294  5      
HELIX   300   312  13      
HELIX   313   316  4      
STRAND   322   328  7      
HELIX   329   345  17      
HELIX   364   379  16      
STRAND   383   386  4      
STRAND   393   396  4      
STRAND   401   405  5      
HELIX   411   414  4      
STRAND   419   427  9      
HELIX   430   438  9      
STRAND   444   449  6      
HELIX   453   462  10      
STRAND   465   471  7      
HELIX   486   488  3      
STRAND   489   491  3      
HELIX   496   502  7      
STRAND   503   511  9      
Sequence information
Length: 517 AA [This is the length of the unprocessed precursor] Molecular weight: 56381 Da [This is the MW of the unprocessed precursor] CRC64: E8F74D44D285A00E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLRAAARFGP RLGRRLLSAA ATQAVPAPNQ QPEVFCNQIF INNEWHDAVS RKTFPTVNPS 

        70         80         90        100        110        120 
TGEVICQVAE GDKEDVDKAV KAARAAFQLG SPWRRMDASH RGRLLNRLAD LIERDRTYLA 

       130        140        150        160        170        180 
ALETLDNGKP YVISYLVDLD MVLKCLRYYA GWADKYHGKT IPIDGDFFSY TRHEPVGVCG 

       190        200        210        220        230        240 
QIIPWNFPLL MQAWKLGPAL ATGNVVVMKV AEQTPLTALY VANLIKEAGF PPGVVNIVPG 

       250        260        270        280        290        300 
FGPTAGAAIA SHEDVDKVAF TGSTEIGRVI QVAAGSSNLK RVTLELGGKS PNIIMSDADM 

       310        320        330        340        350        360 
DWAVEQAHFA LFFNQGQCCC AGSRTFVQED IYDEFVERSV ARAKSRVVGN PFDSKTEQGP 

       370        380        390        400        410        420 
QVDETQFKKI LGYINTGKQE GAKLLCGGGI AADRGYFIQP TVFGDVQDGM TIAKEEIFGP 

       430        440        450        460        470        480 
VMQILKFKTI EEVVGRANNS TYGLAAAVFT KDLDKANYLS QALQAGTVWV NCYDVFGAQS 

       490        500        510 
PFGGYKMSGS GRELGEYGLQ AYTEVKTVTV KVPQKNS 

P05091 in FASTA format

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View entry in raw text format (no links)
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