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P05091

- ALDH2_HUMAN

UniProt

P05091 - ALDH2_HUMAN

Protein

Aldehyde dehydrogenase, mitochondrial

Gene

ALDH2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 187 (01 Oct 2014)
      Sequence version 2 (01 Jan 1990)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei186 – 1861Transition state stabilizer
    Active sitei285 – 2851Proton acceptor
    Active sitei319 – 3191Nucleophile

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi262 – 2676NADBy similarity

    GO - Molecular functioni

    1. aldehyde dehydrogenase (NAD) activity Source: Reactome
    2. aldehyde dehydrogenase [NAD(P)+] activity Source: ProtInc
    3. electron carrier activity Source: UniProtKB

    GO - Biological processi

    1. alcohol metabolic process Source: ProtInc
    2. carbohydrate metabolic process Source: ProtInc
    3. ethanol catabolic process Source: UniProtKB-UniPathway
    4. ethanol oxidation Source: Reactome
    5. neurotransmitter biosynthetic process Source: Reactome
    6. small molecule metabolic process Source: Reactome
    7. synaptic transmission Source: Reactome
    8. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER66-302.
    ReactomeiREACT_15532. Metabolism of serotonin.
    REACT_34. Ethanol oxidation.
    SABIO-RKP05091.
    UniPathwayiUPA00780; UER00768.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aldehyde dehydrogenase, mitochondrial (EC:1.2.1.3)
    Alternative name(s):
    ALDH class 2
    ALDH-E2
    ALDHI
    Gene namesi
    Name:ALDH2
    Synonyms:ALDM
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:404. ALDH2.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. mitochondrial matrix Source: Reactome

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    MIMi100650. gene+phenotype.
    610251. phenotype.
    PharmGKBiPA24696.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 1717MitochondrionAdd
    BLAST
    Chaini18 – 517500Aldehyde dehydrogenase, mitochondrialPRO_0000007168Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei52 – 521N6-acetyllysineBy similarity
    Modified residuei73 – 731N6-acetyllysineBy similarity
    Modified residuei78 – 781N6-acetyllysineBy similarity
    Modified residuei159 – 1591N6-acetyllysineBy similarity
    Modified residuei368 – 3681N6-acetyllysineBy similarity
    Modified residuei383 – 3831N6-acetyllysineBy similarity
    Modified residuei426 – 4261N6-acetyllysineBy similarity
    Modified residuei428 – 4281N6-acetyllysineBy similarity
    Modified residuei451 – 4511N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP05091.
    PaxDbiP05091.
    PeptideAtlasiP05091.
    PRIDEiP05091.

    2D gel databases

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

    PTM databases

    PhosphoSiteiP05091.

    Expressioni

    Gene expression databases

    ArrayExpressiP05091.
    BgeeiP05091.
    CleanExiHS_ALDH2.
    GenevestigatoriP05091.

    Organism-specific databases

    HPAiHPA051065.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    BioGridi106719. 15 interactions.
    DIPiDIP-40262N.
    IntActiP05091. 15 interactions.
    MINTiMINT-1368102.
    STRINGi9606.ENSP00000261733.

    Structurei

    Secondary structure

    1
    517
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi38 – 414
    Beta strandi44 – 463
    Beta strandi53 – 575
    Turni59 – 613
    Beta strandi64 – 696
    Helixi73 – 8614
    Helixi92 – 954
    Helixi98 – 11417
    Helixi116 – 12712
    Helixi131 – 1366
    Helixi138 – 15215
    Turni153 – 1553
    Beta strandi158 – 1614
    Beta strandi164 – 17512
    Beta strandi178 – 1825
    Beta strandi185 – 1873
    Helixi188 – 20114
    Beta strandi205 – 2095
    Beta strandi212 – 2143
    Helixi216 – 22813
    Beta strandi234 – 2374
    Turni242 – 2443
    Helixi245 – 2506
    Beta strandi257 – 2626
    Helixi264 – 27613
    Beta strandi281 – 2855
    Beta strandi290 – 2945
    Helixi300 – 31213
    Helixi313 – 3164
    Beta strandi322 – 3287
    Helixi329 – 34517
    Helixi364 – 37916
    Beta strandi383 – 3864
    Beta strandi389 – 3913
    Beta strandi393 – 3964
    Beta strandi401 – 4055
    Helixi411 – 4144
    Beta strandi419 – 4279
    Helixi430 – 4389
    Beta strandi439 – 4413
    Beta strandi444 – 4496
    Helixi453 – 46210
    Beta strandi465 – 4717
    Beta strandi478 – 4803
    Helixi486 – 4883
    Beta strandi489 – 4913
    Helixi496 – 5027
    Beta strandi503 – 5119

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    4KWFX-ray2.31A/B/C/D/E/F/G/H24-517[»]
    4KWGX-ray2.10A/B/C/D/E/F/G/H24-517[»]
    DisProtiDP00383.
    ProteinModelPortaliP05091.
    SMRiP05091. Positions 24-517.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05091.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldehyde dehydrogenase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1012.
    HOGENOMiHOG000271505.
    HOVERGENiHBG000097.
    InParanoidiP05091.
    KOiK00128.
    OMAiYINTGKQ.
    OrthoDBiEOG7PS1F7.
    PhylomeDBiP05091.
    TreeFamiTF300455.

    Family and domain databases

    Gene3Di3.40.309.10. 1 hit.
    3.40.605.10. 1 hit.
    InterProiIPR016161. Ald_DH/histidinol_DH.
    IPR016163. Ald_DH_C.
    IPR016160. Ald_DH_CS_CYS.
    IPR029510. Ald_DH_CS_GLU.
    IPR016162. Ald_DH_N.
    IPR015590. Aldehyde_DH_dom.
    [Graphical view]
    PfamiPF00171. Aldedh. 1 hit.
    [Graphical view]
    SUPFAMiSSF53720. SSF53720. 1 hit.
    PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
    PS00687. ALDEHYDE_DEHYDR_GLU. 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: P05091-1) [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

    MLRAAARFGP RLGRRLLSAA ATQAVPAPNQ QPEVFCNQIF INNEWHDAVS    50
    RKTFPTVNPS TGEVICQVAE GDKEDVDKAV KAARAAFQLG SPWRRMDASH 100
    RGRLLNRLAD LIERDRTYLA ALETLDNGKP YVISYLVDLD MVLKCLRYYA 150
    GWADKYHGKT IPIDGDFFSY TRHEPVGVCG QIIPWNFPLL MQAWKLGPAL 200
    ATGNVVVMKV AEQTPLTALY VANLIKEAGF PPGVVNIVPG FGPTAGAAIA 250
    SHEDVDKVAF TGSTEIGRVI QVAAGSSNLK RVTLELGGKS PNIIMSDADM 300
    DWAVEQAHFA LFFNQGQCCC AGSRTFVQED IYDEFVERSV ARAKSRVVGN 350
    PFDSKTEQGP QVDETQFKKI LGYINTGKQE GAKLLCGGGI AADRGYFIQP 400
    TVFGDVQDGM TIAKEEIFGP VMQILKFKTI EEVVGRANNS TYGLAAAVFT 450
    KDLDKANYLS QALQAGTVWV NCYDVFGAQS PFGGYKMSGS GRELGEYGLQ 500
    AYTEVKTVTV KVPQKNS 517
    Length:517
    Mass (Da):56,381
    Last modified:January 1, 1990 - v2
    Checksum:iE8F74D44D285A00E
    GO
    Isoform 2 (identifier: P05091-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         74-120: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:470
    Mass (Da):50,989
    Checksum:i5D232BE0405A5F2E
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti7 – 126RFGPRL → ARAPP in CAA28990. (PubMed:3582651)Curated
    Sequence conflicti18 – 181S → A AA sequence (PubMed:4065146)Curated
    Sequence conflicti60 – 601S → F in CAG33272. 1 PublicationCurated
    Sequence conflicti80 – 856VKAARA → REGRPG in CAA28990. (PubMed:3582651)Curated
    Sequence conflicti101 – 1011R → S in CAA28990. (PubMed:3582651)Curated
    Sequence conflicti116 – 1161R → Q in AAT41621. 1 PublicationCurated
    Sequence conflicti216 – 2161L → S in AAA62825. (PubMed:3610592)Curated
    Sequence conflicti218 – 2181A → R in AAA62825. (PubMed:3610592)Curated
    Sequence conflicti247 – 2471A → P in AAA62825. (PubMed:3610592)Curated
    Sequence conflicti332 – 3321Y → C in BAG62916. (PubMed:14702039)Curated
    Sequence conflicti362 – 3621V → L in CAG33272. 1 PublicationCurated
    Sequence conflicti380 – 3801E → Q in AAA51693. (PubMed:2838413)Curated

    Polymorphismi

    Genetic variation in ALDH2 is responsible for individual differences in responses to drinking alcohol [MIMi: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.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti337 – 3371E → V.1 Publication
    Corresponds to variant rs1062136 [ dbSNP | Ensembl ].
    VAR_011869
    Natural varianti496 – 4961E → K in allele ALDH2*3. 1 Publication
    VAR_011302
    Natural varianti504 – 5041E → K in allele ALDH2*2; drastic reduction of enzyme activity. 1 Publication
    Corresponds to variant rs671 [ dbSNP | Ensembl ].
    VAR_002248

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei74 – 12047Missing in isoform 2. 1 PublicationVSP_046715Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X05409 mRNA. Translation: CAA28990.1.
    Y00109 mRNA. Translation: CAA68290.1. Sequence problems.
    M20456
    , 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.
    CCDSiCCDS55885.1. [P05091-2]
    CCDS9155.1. [P05091-1]
    PIRiA29975. DEHUE2.
    RefSeqiNP_000681.2. NM_000690.3. [P05091-1]
    NP_001191818.1. NM_001204889.1. [P05091-2]
    UniGeneiHs.604551.

    Genome annotation databases

    EnsembliENST00000261733; ENSP00000261733; ENSG00000111275. [P05091-1]
    ENST00000416293; ENSP00000403349; ENSG00000111275. [P05091-2]
    GeneIDi217.
    KEGGihsa:217.
    UCSCiuc001tst.3. human. [P05091-1]

    Polymorphism databases

    DMDMi118504.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X05409 mRNA. Translation: CAA28990.1 .
    Y00109 mRNA. Translation: CAA68290.1 . Sequence problems.
    M20456
    , 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.
    CCDSi CCDS55885.1. [P05091-2 ]
    CCDS9155.1. [P05091-1 ]
    PIRi A29975. DEHUE2.
    RefSeqi NP_000681.2. NM_000690.3. [P05091-1 ]
    NP_001191818.1. NM_001204889.1. [P05091-2 ]
    UniGenei Hs.604551.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CW3 X-ray 2.58 A/B/C/D/E/F/G/H 24-517 [» ]
    1NZW X-ray 2.65 A/B/C/D/E/F/G/H 18-517 [» ]
    1NZX X-ray 2.45 A/B/C/D/E/F/G/H 18-517 [» ]
    1NZZ X-ray 2.45 A/B/C/D/E/F/G/H 18-517 [» ]
    1O00 X-ray 2.60 A/B/C/D/E/F/G/H 18-517 [» ]
    1O01 X-ray 2.15 A/B/C/D/E/F/G/H 18-517 [» ]
    1O02 X-ray 1.90 A/B/C/D/E/F/G/H 18-517 [» ]
    1O04 X-ray 1.42 A/B/C/D/E/F/G/H 18-517 [» ]
    1O05 X-ray 2.25 A/B/C/D/E/F/G/H 18-517 [» ]
    1ZUM X-ray 2.10 A/B/C/D/E/F/G/H/I/J/K/L 18-517 [» ]
    2ONM X-ray 2.50 A/B/C/D/E/F/G/H/I/J/K/L 18-517 [» ]
    2ONN X-ray 2.75 A/B/C/D/E/F/G/H 18-517 [» ]
    2ONO X-ray 2.15 A/B/C/D/E/F/G/H 18-517 [» ]
    2ONP X-ray 2.00 A/B/C/D/E/F/G/H 18-517 [» ]
    2VLE X-ray 2.40 A/B/C/D/E/F/G/H 24-517 [» ]
    3INJ X-ray 1.69 A/B/C/D/E/F/G/H 18-517 [» ]
    3INL X-ray 1.86 A/B/C/D/E/F/G/H 18-517 [» ]
    3N80 X-ray 1.50 A/B/C/D/E/F/G/H 18-517 [» ]
    3N81 X-ray 1.70 A/B/C/D/E/F/G/H 18-517 [» ]
    3N82 X-ray 2.25 A/B/C/D/E/F/G/H 18-517 [» ]
    3N83 X-ray 1.90 A/B/C/D/E/F/G/H 18-517 [» ]
    3SZ9 X-ray 2.10 A/B/C/D/E/F/G/H 18-517 [» ]
    4FQF X-ray 2.28 A/B/C/D 18-517 [» ]
    4FR8 X-ray 2.20 A/B/C/D/E/F/G/H 18-517 [» ]
    4KWF X-ray 2.31 A/B/C/D/E/F/G/H 24-517 [» ]
    4KWG X-ray 2.10 A/B/C/D/E/F/G/H 24-517 [» ]
    DisProti DP00383.
    ProteinModelPortali P05091.
    SMRi P05091. Positions 24-517.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106719. 15 interactions.
    DIPi DIP-40262N.
    IntActi P05091. 15 interactions.
    MINTi MINT-1368102.
    STRINGi 9606.ENSP00000261733.

    Chemistry

    BindingDBi P05091.
    ChEMBLi CHEMBL1935.
    DrugBanki DB00822. Disulfiram.
    DB00536. Guanidine.
    DB00157. NADH.
    DB00727. Nitroglycerin.
    GuidetoPHARMACOLOGYi 2595.

    PTM databases

    PhosphoSitei P05091.

    Polymorphism databases

    DMDMi 118504.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00006663.
    P05091.
    UCD-2DPAGE P05091.

    Proteomic databases

    MaxQBi P05091.
    PaxDbi P05091.
    PeptideAtlasi P05091.
    PRIDEi P05091.

    Protocols and materials databases

    DNASUi 217.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261733 ; ENSP00000261733 ; ENSG00000111275 . [P05091-1 ]
    ENST00000416293 ; ENSP00000403349 ; ENSG00000111275 . [P05091-2 ]
    GeneIDi 217.
    KEGGi hsa:217.
    UCSCi uc001tst.3. human. [P05091-1 ]

    Organism-specific databases

    CTDi 217.
    GeneCardsi GC12P112205.
    HGNCi HGNC:404. ALDH2.
    HPAi HPA051065.
    MIMi 100650. gene+phenotype.
    610251. phenotype.
    neXtProti NX_P05091.
    PharmGKBi PA24696.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1012.
    HOGENOMi HOG000271505.
    HOVERGENi HBG000097.
    InParanoidi P05091.
    KOi K00128.
    OMAi YINTGKQ.
    OrthoDBi EOG7PS1F7.
    PhylomeDBi P05091.
    TreeFami TF300455.

    Enzyme and pathway databases

    UniPathwayi UPA00780 ; UER00768 .
    BioCyci MetaCyc:MONOMER66-302.
    Reactomei REACT_15532. Metabolism of serotonin.
    REACT_34. Ethanol oxidation.
    SABIO-RK P05091.

    Miscellaneous databases

    ChiTaRSi ALDH2. human.
    EvolutionaryTracei P05091.
    GeneWikii ALDH2.
    GenomeRNAii 217.
    NextBioi 878.
    PROi P05091.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P05091.
    Bgeei P05091.
    CleanExi HS_ALDH2.
    Genevestigatori P05091.

    Family and domain databases

    Gene3Di 3.40.309.10. 1 hit.
    3.40.605.10. 1 hit.
    InterProi IPR016161. Ald_DH/histidinol_DH.
    IPR016163. Ald_DH_C.
    IPR016160. Ald_DH_CS_CYS.
    IPR029510. Ald_DH_CS_GLU.
    IPR016162. Ald_DH_N.
    IPR015590. Aldehyde_DH_dom.
    [Graphical view ]
    Pfami PF00171. Aldedh. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53720. SSF53720. 1 hit.
    PROSITEi PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
    PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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. 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.

    Entry informationi

    Entry nameiALDH2_HUMAN
    AccessioniPrimary (citable) accession number: P05091
    Secondary accession number(s): B4DW54
    , E7EUE5, Q03639, Q6IB13, Q6IV71
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: January 1, 1990
    Last modified: October 1, 2014
    This is version 187 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3