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P05091 (ALDH2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 182. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aldehyde dehydrogenase, mitochondrial

EC=1.2.1.3
Alternative name(s):
ALDH class 2
ALDH-E2
ALDHI
Gene names
Name:ALDH2
Synonyms:ALDM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length517 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

An aldehyde + NAD+ + H2O = a carboxylate + NADH.

Pathway

Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2.

Subunit structure

Homotetramer.

Subcellular location

Mitochondrion matrix.

Polymorphism

Genetic variation in ALDH2 is responsible for individual differences in responses to drinking alcohol [MIM:610251]. Allele ALDH2*2 is associated with a very high incidence of acute alcohol intoxication in Orientals and South American Indians, as compared to Caucasians.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Sequence caution

The sequence AAA62825.1 differs from that shown. Reason: Frameshift at positions 424, 444, 448 and 461.

The sequence CAA68290.1 differs from that shown. Reason: Frameshift at several positions.

The sequence CAA68290.1 differs from that shown. Reason:

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P05091-1)

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.
Isoform 2 (identifier: P05091-2)

The sequence of this isoform differs from the canonical sequence as follows:
     74-120: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1717Mitochondrion Ref.10
Chain18 – 517500Aldehyde dehydrogenase, mitochondrial
PRO_0000007168

Regions

Nucleotide binding262 – 2676NAD By similarity

Sites

Active site2851Proton acceptor
Active site3191Nucleophile
Site1861Transition state stabilizer

Amino acid modifications

Modified residue521N6-acetyllysine By similarity
Modified residue731N6-acetyllysine By similarity
Modified residue781N6-acetyllysine By similarity
Modified residue1591N6-acetyllysine By similarity
Modified residue3681N6-acetyllysine By similarity
Modified residue3831N6-acetyllysine By similarity
Modified residue4261N6-acetyllysine By similarity
Modified residue4281N6-acetyllysine By similarity
Modified residue4511N6-acetyllysine By similarity

Natural variations

Alternative sequence74 – 12047Missing in isoform 2.
VSP_046715
Natural variant3371E → V. Ref.15
Corresponds to variant rs1062136 [ dbSNP | Ensembl ].
VAR_011869
Natural variant4961E → K in allele ALDH2*3. Ref.20
VAR_011302
Natural variant5041E → K in allele ALDH2*2; drastic reduction of enzyme activity. Ref.19
Corresponds to variant rs671 [ dbSNP | Ensembl ].
VAR_002248

Experimental info

Sequence conflict7 – 126RFGPRL → ARAPP in CAA28990. Ref.1
Sequence conflict181S → A AA sequence Ref.10
Sequence conflict601S → F in CAG33272. Ref.6
Sequence conflict80 – 856VKAARA → REGRPG in CAA28990. Ref.1
Sequence conflict1011R → S in CAA28990. Ref.1
Sequence conflict1161R → Q in AAT41621. Ref.5
Sequence conflict2161L → S in AAA62825. Ref.15
Sequence conflict2181A → R in AAA62825. Ref.15
Sequence conflict2471A → P in AAA62825. Ref.15
Sequence conflict3321Y → C in BAG62916. Ref.7
Sequence conflict3621V → L in CAG33272. Ref.6
Sequence conflict3801E → Q in AAA51693. Ref.4

Secondary structure

......................................................................................... 517
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 1, 1990. Version 2.
Checksum: E8F74D44D285A00E

FASTA51756,381
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 5D232BE0405A5F2E
Show »

FASTA47050,989

References

« Hide 'large scale' references
[1]"Evidence for a signal peptide at the amino-terminal end of human mitochondrial aldehyde dehydrogenase."
Braun T., Bober E., Singh S., Agarwal D.P., Goedde H.W.
FEBS Lett. 215:233-236(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Muscle.
[2]Erratum
Braun T., Bober E., Singh S., Agarwal D.P., Goedde H.W.
FEBS Lett. 233:440-440(1988)
Cited for: SEQUENCE REVISION TO N-TERMINUS.
[3]"Isolation and sequence analysis of a full length cDNA clone coding for human mitochondrial aldehyde dehydrogenase."
Braun T., Bober E., Singh S., Agarwal D.P., Goedde H.W.
Nucleic Acids Res. 15:3179-3179(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Muscle.
[4]"Genomic structure of the human mitochondrial aldehyde dehydrogenase gene."
Hsu L.C., Bendel R.E., Yoshida A.
Genomics 2:57-65(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]Lassen N., Estey T., Vasiliou V.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[6]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[7]"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. expand/collapse author list , 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: Synovium.
[8]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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: Brain and Lymph.
[10]"Mitochondrial aldehyde dehydrogenase from human liver. Primary structure, differences in relation to the cytosolic enzyme, and functional correlations."
Hempel J., Kaiser R., Joernvall H.
Eur. J. Biochem. 153:13-28(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-517 (ISOFORM 1).
Tissue: Liver.
[11]"Cloning of cDNAs for human aldehyde dehydrogenases 1 and 2."
Hsu L.C., Tani K., Fujiyoshi T., Kurachi K., Yoshida A.
Proc. Natl. Acad. Sci. U.S.A. 82:3771-3775(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 119-517 (ISOFORM 1).
Tissue: Liver.
[12]"Molecular abnormality and cDNA cloning of human aldehyde dehydrogenases."
Yoshida A., Ikawa M., Hsu L.C., Tani K.
Alcohol 2:103-106(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 119-517 (ISOFORM 1).
[13]Lubec G., Vishwanath V.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 160-172 AND 325-338, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[14]"Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes."
Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.
Biochem. J. 383:237-248(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 196-226 AND 325-338.
Tissue: Adipocyte.
[15]"Human aldehyde dehydrogenase isozymes and alcohol sensitivity."
Agarwal D.P., Goedde H.W.
Isozymes Curr. Top. Biol. Med. Res. 16:21-48(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 214-500, VARIANT VAL-337.
Tissue: Liver.
[16]"Mitochondrial aldehyde dehydrogenase. Homology of putative targeting sequence to that of carbamyl phosphate synthetase I revealed by correlation of cDNA and protein data."
Hempel J., Hoeoeg J.-O., Joernvall H.
FEBS Lett. 222:95-98(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: DESCRIPTION OF ORIGIN OF CONFLICTS BETWEEN THE SEQUENCE DESCRIBED IN PUBMED:4065146 AND DNA SEQUENCES.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Human liver mitochondrial aldehyde dehydrogenase: three-dimensional structure and the restoration of solubility and activity of chimeric forms."
Ni L., Zhou J., Hurley T.D., Weiner H.
Protein Sci. 8:2784-2790(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.58 ANGSTROMS).
[19]"Molecular abnormality of an inactive aldehyde dehydrogenase variant commonly found in Orientals."
Yoshida A., Huang I.-Y., Ikawa M.
Proc. Natl. Acad. Sci. U.S.A. 81:258-261(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LYS-504.
[20]"Mitochondrial aldehyde dehydrogenase polymorphism in Asian and American Indian populations: detection of new ALDH2 alleles."
Novoradovsky A., Tsai S.J., Goldfarb L., Peterson R., Long J.C., Goldman D.
Alcohol. Clin. Exp. Res. 19:1105-1110(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LYS-496.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X05409 mRNA. Translation: CAA28990.1.
Y00109 mRNA. Translation: CAA68290.1. Sequence problems.
M20456 expand/collapse EMBL AC list , M20444, M20445, M20446, M20447, M20448, M20449, M20450, M20451, M20452, M20453, M20454 Genomic DNA. Translation: AAA51693.1.
AY621070 mRNA. Translation: AAT41621.1.
CR456991 mRNA. Translation: CAG33272.1.
AK301375 mRNA. Translation: BAG62916.1.
AC002996 Genomic DNA. No translation available.
AC003029 Genomic DNA. No translation available.
BC002967 mRNA. Translation: AAH02967.1.
BC071839 mRNA. Translation: AAH71839.1.
K03001 mRNA. Translation: AAB59500.1.
M26760 mRNA. Translation: AAA51694.1.
M54931 mRNA. Translation: AAA62825.1. Frameshift.
PIRDEHUE2. A29975.
RefSeqNP_000681.2. NM_000690.3.
NP_001191818.1. NM_001204889.1.
UniGeneHs.604551.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CW3X-ray2.58A/B/C/D/E/F/G/H24-517[»]
1NZWX-ray2.65A/B/C/D/E/F/G/H18-517[»]
1NZXX-ray2.45A/B/C/D/E/F/G/H18-517[»]
1NZZX-ray2.45A/B/C/D/E/F/G/H18-517[»]
1O00X-ray2.60A/B/C/D/E/F/G/H18-517[»]
1O01X-ray2.15A/B/C/D/E/F/G/H18-517[»]
1O02X-ray1.90A/B/C/D/E/F/G/H18-517[»]
1O04X-ray1.42A/B/C/D/E/F/G/H18-517[»]
1O05X-ray2.25A/B/C/D/E/F/G/H18-517[»]
1ZUMX-ray2.10A/B/C/D/E/F/G/H/I/J/K/L18-517[»]
2ONMX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L18-517[»]
2ONNX-ray2.75A/B/C/D/E/F/G/H18-517[»]
2ONOX-ray2.15A/B/C/D/E/F/G/H18-517[»]
2ONPX-ray2.00A/B/C/D/E/F/G/H18-517[»]
2VLEX-ray2.40A/B/C/D/E/F/G/H24-517[»]
3INJX-ray1.69A/B/C/D/E/F/G/H18-517[»]
3INLX-ray1.86A/B/C/D/E/F/G/H18-517[»]
3N80X-ray1.50A/B/C/D/E/F/G/H18-517[»]
3N81X-ray1.70A/B/C/D/E/F/G/H18-517[»]
3N82X-ray2.25A/B/C/D/E/F/G/H18-517[»]
3N83X-ray1.90A/B/C/D/E/F/G/H18-517[»]
3SZ9X-ray2.10A/B/C/D/E/F/G/H18-517[»]
4FQFX-ray2.28A/B/C/D18-517[»]
4FR8X-ray2.20A/B/C/D/E/F/G/H18-517[»]
DisProtDP00383.
ProteinModelPortalP05091.
SMRP05091. Positions 24-517.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106719. 15 interactions.
DIPDIP-40262N.
IntActP05091. 15 interactions.
MINTMINT-1368102.
STRING9606.ENSP00000261733.

Chemistry

BindingDBP05091.
ChEMBLCHEMBL1935.
DrugBankDB00822. Disulfiram.
DB00536. Guanidine.
DB00157. NADH.
DB00727. Nitroglycerin.
GuidetoPHARMACOLOGY2595.

PTM databases

PhosphoSiteP05091.

Polymorphism databases

DMDM118504.

2D gel databases

REPRODUCTION-2DPAGEIPI00006663.
P05091.
UCD-2DPAGEP05091.

Proteomic databases

PaxDbP05091.
PeptideAtlasP05091.
PRIDEP05091.

Protocols and materials databases

DNASU217.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261733; ENSP00000261733; ENSG00000111275. [P05091-1]
ENST00000416293; ENSP00000403349; ENSG00000111275. [P05091-2]
GeneID217.
KEGGhsa:217.
UCSCuc001tst.3. human. [P05091-1]

Organism-specific databases

CTD217.
GeneCardsGC12P112205.
HGNCHGNC:404. ALDH2.
HPAHPA051065.
MIM100650. gene+phenotype.
610251. phenotype.
neXtProtNX_P05091.
PharmGKBPA24696.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1012.
HOGENOMHOG000271505.
HOVERGENHBG000097.
InParanoidP05091.
KOK00128.
OMAVAYHIYE.
OrthoDBEOG7PS1F7.
PhylomeDBP05091.
TreeFamTF300455.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER66-302.
ReactomeREACT_111217. Metabolism.
REACT_13685. Neuronal System.
SABIO-RKP05091.
UniPathwayUPA00780; UER00768.

Gene expression databases

ArrayExpressP05091.
BgeeP05091.
CleanExHS_ALDH2.
GenevestigatorP05091.

Family and domain databases

Gene3D3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMSSF53720. SSF53720. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSALDH2. human.
EvolutionaryTraceP05091.
GeneWikiALDH2.
GenomeRNAi217.
NextBio878.
PROP05091.
SOURCESearch...

Entry information

Entry nameALDH2_HUMAN
AccessionPrimary (citable) accession number: P05091
Secondary accession number(s): B4DW54 expand/collapse secondary AC list , E7EUE5, Q03639, Q6IB13, Q6IV71
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 1, 1990
Last modified: April 16, 2014
This is version 182 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM