GenomeNet

Database: UniProt/SWISS-PROT
Entry: ALDH2_HUMAN
LinkDB: ALDH2_HUMAN
Original site: ALDH2_HUMAN 
ID   ALDH2_HUMAN             Reviewed;         517 AA.
AC   P05091; B4DW54; E7EUE5; Q03639; Q6IB13; Q6IV71;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 2.
DT   05-DEC-2018, entry version 226.
DE   RecName: Full=Aldehyde dehydrogenase, mitochondrial;
DE            EC=1.2.1.3;
DE   AltName: Full=ALDH class 2;
DE   AltName: Full=ALDH-E2;
DE   AltName: Full=ALDHI;
DE   Flags: Precursor;
GN   Name=ALDH2; Synonyms=ALDM;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Muscle;
RX   PubMed=3582651; DOI=10.1016/0014-5793(87)80152-7;
RA   Braun T., Bober E., Singh S., Agarwal D.P., Goedde H.W.;
RT   "Evidence for a signal peptide at the amino-terminal end of human
RT   mitochondrial aldehyde dehydrogenase.";
RL   FEBS Lett. 215:233-236(1987).
RN   [2]
RP   ERRATUM, AND SEQUENCE REVISION TO N-TERMINUS.
RA   Braun T., Bober E., Singh S., Agarwal D.P., Goedde H.W.;
RL   FEBS Lett. 233:440-440(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Muscle;
RX   PubMed=3562250; DOI=10.1093/nar/15.7.3179;
RA   Braun T., Bober E., Singh S., Agarwal D.P., Goedde H.W.;
RT   "Isolation and sequence analysis of a full length cDNA clone coding
RT   for human mitochondrial aldehyde dehydrogenase.";
RL   Nucleic Acids Res. 15:3179-3179(1987).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2838413; DOI=10.1016/0888-7543(88)90109-7;
RA   Hsu L.C., Bendel R.E., Yoshida A.;
RT   "Genomic structure of the human mitochondrial aldehyde dehydrogenase
RT   gene.";
RL   Genomics 2:57-65(1988).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Lassen N., Estey T., Vasiliou V.;
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Synovium;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA   Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA   Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA   Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA   Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA   Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA   Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA   Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA   Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA   Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA   Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA   Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA   Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA   Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA   Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA   Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA   Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA   Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA   Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA   Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA   Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA   Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA   Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA   Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA   Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA   Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA   Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA   Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA   Kucherlapati R., Weinstock G., Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain, and Lymph;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [10]
RP   PROTEIN SEQUENCE OF 18-517 (ISOFORM 1).
RC   TISSUE=Liver;
RX   PubMed=4065146; DOI=10.1111/j.1432-1033.1985.tb09260.x;
RA   Hempel J., Kaiser R., Joernvall H.;
RT   "Mitochondrial aldehyde dehydrogenase from human liver. Primary
RT   structure, differences in relation to the cytosolic enzyme, and
RT   functional correlations.";
RL   Eur. J. Biochem. 153:13-28(1985).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 119-517 (ISOFORM 1).
RC   TISSUE=Liver;
RX   PubMed=2987944; DOI=10.1073/pnas.82.11.3771;
RA   Hsu L.C., Tani K., Fujiyoshi T., Kurachi K., Yoshida A.;
RT   "Cloning of cDNAs for human aldehyde dehydrogenases 1 and 2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:3771-3775(1985).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 119-517 (ISOFORM 1).
RX   PubMed=4015823; DOI=10.1016/0741-8329(85)90024-2;
RA   Yoshida A., Ikawa M., Hsu L.C., Tani K.;
RT   "Molecular abnormality and cDNA cloning of human aldehyde
RT   dehydrogenases.";
RL   Alcohol 2:103-106(1985).
RN   [13]
RP   PROTEIN SEQUENCE OF 160-172 AND 325-338, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain, and Cajal-Retzius cell;
RA   Lubec G., Vishwanath V.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [14]
RP   PROTEIN SEQUENCE OF 196-226 AND 325-338.
RC   TISSUE=Adipocyte;
RX   PubMed=15242332; DOI=10.1042/BJ20040647;
RA   Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.;
RT   "Vectorial proteomics reveal targeting, phosphorylation and specific
RT   fragmentation of polymerase I and transcript release factor (PTRF) at
RT   the surface of caveolae in human adipocytes.";
RL   Biochem. J. 383:237-248(2004).
RN   [15]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 214-500, AND VARIANT VAL-337.
RC   TISSUE=Liver;
RX   PubMed=3610592;
RA   Agarwal D.P., Goedde H.W.;
RT   "Human aldehyde dehydrogenase isozymes and alcohol sensitivity.";
RL   Isozymes Curr. Top. Biol. Med. Res. 16:21-48(1987).
RN   [16]
RP   DESCRIPTION OF ORIGIN OF CONFLICTS BETWEEN THE SEQUENCE DESCRIBED IN
RP   PUBMED:4065146 AND DNA SEQUENCES.
RX   PubMed=3653404; DOI=10.1016/0014-5793(87)80198-9;
RA   Hempel J., Hoeoeg J.-O., Joernvall H.;
RT   "Mitochondrial aldehyde dehydrogenase. Homology of putative targeting
RT   sequence to that of carbamyl phosphate synthetase I revealed by
RT   correlation of cDNA and protein data.";
RL   FEBS Lett. 222:95-98(1987).
RN   [17]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [18]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (2.58 ANGSTROMS).
RX   PubMed=10631996; DOI=10.1110/ps.8.12.2784;
RA   Ni L., Zhou J., Hurley T.D., Weiner H.;
RT   "Human liver mitochondrial aldehyde dehydrogenase: three-dimensional
RT   structure and the restoration of solubility and activity of chimeric
RT   forms.";
RL   Protein Sci. 8:2784-2790(1999).
RN   [20]
RP   VARIANT LYS-504.
RX   PubMed=6582480; DOI=10.1073/pnas.81.1.258;
RA   Yoshida A., Huang I.-Y., Ikawa M.;
RT   "Molecular abnormality of an inactive aldehyde dehydrogenase variant
RT   commonly found in Orientals.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:258-261(1984).
RN   [21]
RP   VARIANT LYS-496.
RX   PubMed=8561277; DOI=10.1111/j.1530-0277.1995.tb01587.x;
RA   Novoradovsky A., Tsai S.J., Goldfarb L., Peterson R., Long J.C.,
RA   Goldman D.;
RT   "Mitochondrial aldehyde dehydrogenase polymorphism in Asian and
RT   American Indian populations: detection of new ALDH2 alleles.";
RL   Alcohol. Clin. Exp. Res. 19:1105-1110(1995).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) +
CC         NADH; Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.3;
CC   -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from
CC       ethanol: step 2/2.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P05091-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P05091-2; Sequence=VSP_046715;
CC         Note=No experimental confirmation available.;
CC   -!- POLYMORPHISM: Genetic variation in ALDH2 is responsible for
CC       individual differences in responses to drinking alcohol
CC       [MIM:610251]. Allele ALDH2*2 is associated with a very high
CC       incidence of acute alcohol intoxication in Orientals and South
CC       American Indians, as compared to Caucasians.
CC       {ECO:0000269|PubMed:8561277}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA62825.1; Type=Frameshift; Positions=424, 444, 448, 461; Evidence={ECO:0000305};
CC       Sequence=CAA68290.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
CC       Sequence=CAA68290.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/ALDH2ID250.html";
DR   EMBL; X05409; CAA28990.1; -; mRNA.
DR   EMBL; Y00109; CAA68290.1; ALT_SEQ; mRNA.
DR   EMBL; M20456; AAA51693.1; -; Genomic_DNA.
DR   EMBL; M20444; AAA51693.1; JOINED; Genomic_DNA.
DR   EMBL; M20445; AAA51693.1; JOINED; Genomic_DNA.
DR   EMBL; M20446; AAA51693.1; JOINED; Genomic_DNA.
DR   EMBL; M20447; AAA51693.1; JOINED; Genomic_DNA.
DR   EMBL; M20448; AAA51693.1; JOINED; Genomic_DNA.
DR   EMBL; M20449; AAA51693.1; JOINED; Genomic_DNA.
DR   EMBL; M20450; AAA51693.1; JOINED; Genomic_DNA.
DR   EMBL; M20451; AAA51693.1; JOINED; Genomic_DNA.
DR   EMBL; M20452; AAA51693.1; JOINED; Genomic_DNA.
DR   EMBL; M20453; AAA51693.1; JOINED; Genomic_DNA.
DR   EMBL; M20454; AAA51693.1; JOINED; Genomic_DNA.
DR   EMBL; AY621070; AAT41621.1; -; mRNA.
DR   EMBL; CR456991; CAG33272.1; -; mRNA.
DR   EMBL; AK301375; BAG62916.1; -; mRNA.
DR   EMBL; AC002996; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC003029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC002967; AAH02967.1; -; mRNA.
DR   EMBL; BC071839; AAH71839.1; -; mRNA.
DR   EMBL; K03001; AAB59500.1; -; mRNA.
DR   EMBL; M26760; AAA51694.1; -; mRNA.
DR   EMBL; M54931; AAA62825.1; ALT_FRAME; mRNA.
DR   CCDS; CCDS55885.1; -. [P05091-2]
DR   CCDS; CCDS9155.1; -. [P05091-1]
DR   PIR; A29975; DEHUE2.
DR   RefSeq; NP_000681.2; NM_000690.3. [P05091-1]
DR   RefSeq; NP_001191818.1; NM_001204889.1. [P05091-2]
DR   UniGene; Hs.604551; -.
DR   PDB; 1CW3; X-ray; 2.58 A; A/B/C/D/E/F/G/H=24-517.
DR   PDB; 1NZW; X-ray; 2.65 A; A/B/C/D/E/F/G/H=18-517.
DR   PDB; 1NZX; X-ray; 2.45 A; A/B/C/D/E/F/G/H=18-517.
DR   PDB; 1NZZ; X-ray; 2.45 A; A/B/C/D/E/F/G/H=18-517.
DR   PDB; 1O00; X-ray; 2.60 A; A/B/C/D/E/F/G/H=18-517.
DR   PDB; 1O01; X-ray; 2.15 A; A/B/C/D/E/F/G/H=18-517.
DR   PDB; 1O02; X-ray; 1.90 A; A/B/C/D/E/F/G/H=18-517.
DR   PDB; 1O04; X-ray; 1.42 A; A/B/C/D/E/F/G/H=18-517.
DR   PDB; 1O05; X-ray; 2.25 A; A/B/C/D/E/F/G/H=18-517.
DR   PDB; 1ZUM; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L=18-517.
DR   PDB; 2ONM; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=18-517.
DR   PDB; 2ONN; X-ray; 2.75 A; A/B/C/D/E/F/G/H=18-517.
DR   PDB; 2ONO; X-ray; 2.15 A; A/B/C/D/E/F/G/H=18-517.
DR   PDB; 2ONP; X-ray; 2.00 A; A/B/C/D/E/F/G/H=18-517.
DR   PDB; 2VLE; X-ray; 2.40 A; A/B/C/D/E/F/G/H=24-517.
DR   PDB; 3INJ; X-ray; 1.69 A; A/B/C/D/E/F/G/H=18-517.
DR   PDB; 3INL; X-ray; 1.86 A; A/B/C/D/E/F/G/H=18-517.
DR   PDB; 3N80; X-ray; 1.50 A; A/B/C/D/E/F/G/H=18-517.
DR   PDB; 3N81; X-ray; 1.70 A; A/B/C/D/E/F/G/H=18-517.
DR   PDB; 3N82; X-ray; 2.25 A; A/B/C/D/E/F/G/H=18-517.
DR   PDB; 3N83; X-ray; 1.90 A; A/B/C/D/E/F/G/H=18-517.
DR   PDB; 3SZ9; X-ray; 2.10 A; A/B/C/D/E/F/G/H=18-517.
DR   PDB; 4FQF; X-ray; 2.28 A; A/B/C/D=18-517.
DR   PDB; 4FR8; X-ray; 2.20 A; A/B/C/D/E/F/G/H=18-517.
DR   PDB; 4KWF; X-ray; 2.31 A; A/B/C/D/E/F/G/H=24-517.
DR   PDB; 4KWG; X-ray; 2.10 A; A/B/C/D/E/F/G/H=24-517.
DR   PDB; 5L13; X-ray; 2.40 A; A/B/C/D/E/F/G/H=1-517.
DR   PDBsum; 1CW3; -.
DR   PDBsum; 1NZW; -.
DR   PDBsum; 1NZX; -.
DR   PDBsum; 1NZZ; -.
DR   PDBsum; 1O00; -.
DR   PDBsum; 1O01; -.
DR   PDBsum; 1O02; -.
DR   PDBsum; 1O04; -.
DR   PDBsum; 1O05; -.
DR   PDBsum; 1ZUM; -.
DR   PDBsum; 2ONM; -.
DR   PDBsum; 2ONN; -.
DR   PDBsum; 2ONO; -.
DR   PDBsum; 2ONP; -.
DR   PDBsum; 2VLE; -.
DR   PDBsum; 3INJ; -.
DR   PDBsum; 3INL; -.
DR   PDBsum; 3N80; -.
DR   PDBsum; 3N81; -.
DR   PDBsum; 3N82; -.
DR   PDBsum; 3N83; -.
DR   PDBsum; 3SZ9; -.
DR   PDBsum; 4FQF; -.
DR   PDBsum; 4FR8; -.
DR   PDBsum; 4KWF; -.
DR   PDBsum; 4KWG; -.
DR   PDBsum; 5L13; -.
DR   ProteinModelPortal; P05091; -.
DR   SMR; P05091; -.
DR   BioGrid; 106719; 52.
DR   DIP; DIP-40262N; -.
DR   IntAct; P05091; 23.
DR   MINT; P05091; -.
DR   STRING; 9606.ENSP00000261733; -.
DR   BindingDB; P05091; -.
DR   ChEMBL; CHEMBL1935; -.
DR   DrugBank; DB01612; Amyl Nitrite.
DR   DrugBank; DB06770; Benzyl alcohol.
DR   DrugBank; DB04381; Crotonaldehyde.
DR   DrugBank; DB02115; Daidzin.
DR   DrugBank; DB00822; Disulfiram.
DR   DrugBank; DB00536; Guanidine.
DR   DrugBank; DB00157; NADH.
DR   DrugBank; DB00435; Nitric Oxide.
DR   DrugBank; DB00727; Nitroglycerin.
DR   GuidetoPHARMACOLOGY; 2595; -.
DR   iPTMnet; P05091; -.
DR   PhosphoSitePlus; P05091; -.
DR   SwissPalm; P05091; -.
DR   BioMuta; ALDH2; -.
DR   DMDM; 118504; -.
DR   REPRODUCTION-2DPAGE; IPI00006663; -.
DR   REPRODUCTION-2DPAGE; P05091; -.
DR   UCD-2DPAGE; P05091; -.
DR   EPD; P05091; -.
DR   MaxQB; P05091; -.
DR   PaxDb; P05091; -.
DR   PeptideAtlas; P05091; -.
DR   PRIDE; P05091; -.
DR   ProteomicsDB; 51788; -.
DR   DNASU; 217; -.
DR   Ensembl; ENST00000261733; ENSP00000261733; ENSG00000111275. [P05091-1]
DR   Ensembl; ENST00000416293; ENSP00000403349; ENSG00000111275. [P05091-2]
DR   GeneID; 217; -.
DR   KEGG; hsa:217; -.
DR   UCSC; uc001tst.4; human. [P05091-1]
DR   CTD; 217; -.
DR   DisGeNET; 217; -.
DR   EuPathDB; HostDB:ENSG00000111275.12; -.
DR   GeneCards; ALDH2; -.
DR   HGNC; HGNC:404; ALDH2.
DR   HPA; HPA051065; -.
DR   MalaCards; ALDH2; -.
DR   MIM; 100650; gene+phenotype.
DR   MIM; 610251; phenotype.
DR   neXtProt; NX_P05091; -.
DR   OpenTargets; ENSG00000111275; -.
DR   PharmGKB; PA24696; -.
DR   eggNOG; KOG2450; Eukaryota.
DR   eggNOG; COG1012; LUCA.
DR   GeneTree; ENSGT00940000156240; -.
DR   HOGENOM; HOG000271505; -.
DR   HOVERGEN; HBG000097; -.
DR   InParanoid; P05091; -.
DR   KO; K00128; -.
DR   OMA; TFVQEDV; -.
DR   OrthoDB; EOG091G05E8; -.
DR   PhylomeDB; P05091; -.
DR   TreeFam; TF300455; -.
DR   BioCyc; MetaCyc:MONOMER66-302; -.
DR   BRENDA; 1.2.1.3; 2681.
DR   Reactome; R-HSA-380612; Metabolism of serotonin.
DR   Reactome; R-HSA-71384; Ethanol oxidation.
DR   SABIO-RK; P05091; -.
DR   UniPathway; UPA00780; UER00768.
DR   ChiTaRS; ALDH2; human.
DR   EvolutionaryTrace; P05091; -.
DR   GeneWiki; ALDH2; -.
DR   GenomeRNAi; 217; -.
DR   PRO; PR:P05091; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   Bgee; ENSG00000111275; Expressed in 231 organ(s), highest expression level in liver.
DR   CleanEx; HS_ALDH2; -.
DR   ExpressionAtlas; P05091; baseline and differential.
DR   Genevisible; P05091; HS.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD) activity; IDA:CACAO.
DR   GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; TAS:ProtInc.
DR   GO; GO:0009055; F:electron transfer activity; TAS:UniProtKB.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; ISS:CAFA.
DR   GO; GO:0006066; P:alcohol metabolic process; TAS:ProtInc.
DR   GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc.
DR   GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006069; P:ethanol oxidation; TAS:Reactome.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW   Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase;
KW   Polymorphism; Reference proteome; Transit peptide.
FT   TRANSIT       1     17       Mitochondrion.
FT   CHAIN        18    517       Aldehyde dehydrogenase, mitochondrial.
FT                                /FTId=PRO_0000007168.
FT   NP_BIND     262    267       NAD. {ECO:0000250}.
FT   ACT_SITE    285    285       Proton acceptor.
FT   ACT_SITE    319    319       Nucleophile.
FT   SITE        186    186       Transition state stabilizer.
FT                                {ECO:0000250|UniProtKB:P20000}.
FT   MOD_RES      52     52       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES      73     73       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES      78     78       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     159    159       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     368    368       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     383    383       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     426    426       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     428    428       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     451    451       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   VAR_SEQ      74    120       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_046715.
FT   VARIANT     337    337       E -> V (in dbSNP:rs1062136).
FT                                {ECO:0000269|PubMed:3610592}.
FT                                /FTId=VAR_011869.
FT   VARIANT     496    496       E -> K (in allele ALDH2*3;
FT                                dbSNP:rs769724893).
FT                                {ECO:0000269|PubMed:8561277}.
FT                                /FTId=VAR_011302.
FT   VARIANT     504    504       E -> K (in allele ALDH2*2; drastic
FT                                reduction of enzyme activity;
FT                                dbSNP:rs671).
FT                                {ECO:0000269|PubMed:6582480}.
FT                                /FTId=VAR_002248.
FT   CONFLICT      7     12       RFGPRL -> ARAPP (in Ref. 1; CAA28990).
FT                                {ECO:0000305}.
FT   CONFLICT     18     18       S -> A (in Ref. 10; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     60     60       S -> F (in Ref. 6; CAG33272).
FT                                {ECO:0000305}.
FT   CONFLICT     80     85       VKAARA -> REGRPG (in Ref. 1; CAA28990).
FT                                {ECO:0000305}.
FT   CONFLICT    101    101       R -> S (in Ref. 1; CAA28990).
FT                                {ECO:0000305}.
FT   CONFLICT    116    116       R -> Q (in Ref. 5; AAT41621).
FT                                {ECO:0000305}.
FT   CONFLICT    216    216       L -> S (in Ref. 15; AAA62825).
FT                                {ECO:0000305}.
FT   CONFLICT    218    218       A -> R (in Ref. 15; AAA62825).
FT                                {ECO:0000305}.
FT   CONFLICT    247    247       A -> P (in Ref. 15; AAA62825).
FT                                {ECO:0000305}.
FT   CONFLICT    332    332       Y -> C (in Ref. 7; BAG62916).
FT                                {ECO:0000305}.
FT   CONFLICT    362    362       V -> L (in Ref. 6; CAG33272).
FT                                {ECO:0000305}.
FT   CONFLICT    380    380       E -> Q (in Ref. 4; AAA51693).
FT                                {ECO:0000305}.
FT   STRAND       38     41       {ECO:0000244|PDB:1O04}.
FT   STRAND       44     46       {ECO:0000244|PDB:1O04}.
FT   STRAND       53     57       {ECO:0000244|PDB:1O04}.
FT   TURN         59     61       {ECO:0000244|PDB:1O04}.
FT   STRAND       64     69       {ECO:0000244|PDB:1O04}.
FT   HELIX        73     86       {ECO:0000244|PDB:1O04}.
FT   HELIX        92     95       {ECO:0000244|PDB:1O04}.
FT   HELIX        98    114       {ECO:0000244|PDB:1O04}.
FT   HELIX       116    127       {ECO:0000244|PDB:1O04}.
FT   HELIX       131    136       {ECO:0000244|PDB:1O04}.
FT   HELIX       138    152       {ECO:0000244|PDB:1O04}.
FT   TURN        153    155       {ECO:0000244|PDB:1O04}.
FT   STRAND      158    161       {ECO:0000244|PDB:1O04}.
FT   STRAND      164    175       {ECO:0000244|PDB:1O04}.
FT   STRAND      178    182       {ECO:0000244|PDB:1O04}.
FT   STRAND      185    187       {ECO:0000244|PDB:1O04}.
FT   HELIX       188    201       {ECO:0000244|PDB:1O04}.
FT   STRAND      205    209       {ECO:0000244|PDB:1O04}.
FT   STRAND      212    214       {ECO:0000244|PDB:4KWF}.
FT   HELIX       216    228       {ECO:0000244|PDB:1O04}.
FT   STRAND      234    237       {ECO:0000244|PDB:1O04}.
FT   TURN        242    244       {ECO:0000244|PDB:1O04}.
FT   HELIX       245    250       {ECO:0000244|PDB:1O04}.
FT   STRAND      257    262       {ECO:0000244|PDB:1O04}.
FT   HELIX       264    276       {ECO:0000244|PDB:1O04}.
FT   STRAND      281    285       {ECO:0000244|PDB:1O04}.
FT   STRAND      290    294       {ECO:0000244|PDB:1O04}.
FT   HELIX       300    312       {ECO:0000244|PDB:1O04}.
FT   HELIX       313    316       {ECO:0000244|PDB:1O04}.
FT   STRAND      322    328       {ECO:0000244|PDB:1O04}.
FT   HELIX       329    345       {ECO:0000244|PDB:1O04}.
FT   HELIX       364    379       {ECO:0000244|PDB:1O04}.
FT   STRAND      383    386       {ECO:0000244|PDB:1O04}.
FT   STRAND      389    391       {ECO:0000244|PDB:3INL}.
FT   STRAND      393    396       {ECO:0000244|PDB:1O04}.
FT   STRAND      401    405       {ECO:0000244|PDB:1O04}.
FT   HELIX       411    414       {ECO:0000244|PDB:1O04}.
FT   STRAND      419    427       {ECO:0000244|PDB:1O04}.
FT   HELIX       430    438       {ECO:0000244|PDB:1O04}.
FT   STRAND      439    441       {ECO:0000244|PDB:3INL}.
FT   STRAND      444    449       {ECO:0000244|PDB:1O04}.
FT   HELIX       453    462       {ECO:0000244|PDB:1O04}.
FT   STRAND      465    471       {ECO:0000244|PDB:1O04}.
FT   STRAND      478    480       {ECO:0000244|PDB:2ONO}.
FT   HELIX       486    488       {ECO:0000244|PDB:1O04}.
FT   STRAND      489    491       {ECO:0000244|PDB:1O04}.
FT   HELIX       496    502       {ECO:0000244|PDB:1O04}.
FT   STRAND      503    511       {ECO:0000244|PDB:1O04}.
SQ   SEQUENCE   517 AA;  56381 MW;  E8F74D44D285A00E CRC64;
     MLRAAARFGP RLGRRLLSAA ATQAVPAPNQ QPEVFCNQIF INNEWHDAVS RKTFPTVNPS
     TGEVICQVAE GDKEDVDKAV KAARAAFQLG SPWRRMDASH RGRLLNRLAD LIERDRTYLA
     ALETLDNGKP YVISYLVDLD MVLKCLRYYA GWADKYHGKT IPIDGDFFSY TRHEPVGVCG
     QIIPWNFPLL MQAWKLGPAL ATGNVVVMKV AEQTPLTALY VANLIKEAGF PPGVVNIVPG
     FGPTAGAAIA SHEDVDKVAF TGSTEIGRVI QVAAGSSNLK RVTLELGGKS PNIIMSDADM
     DWAVEQAHFA LFFNQGQCCC AGSRTFVQED IYDEFVERSV ARAKSRVVGN PFDSKTEQGP
     QVDETQFKKI LGYINTGKQE GAKLLCGGGI AADRGYFIQP TVFGDVQDGM TIAKEEIFGP
     VMQILKFKTI EEVVGRANNS TYGLAAAVFT KDLDKANYLS QALQAGTVWV NCYDVFGAQS
     PFGGYKMSGS GRELGEYGLQ AYTEVKTVTV KVPQKNS
//
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