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P05091

- ALDH2_HUMAN

UniProt

P05091 - ALDH2_HUMAN

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Protein
Aldehyde dehydrogenase, mitochondrial
Gene
ALDH2, ALDM
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 2676NAD By 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
Complete GO annotation...

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
Complete GO annotation...

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
Complete GO annotation...

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 – 1717Mitochondrion1 Publication
Add
BLAST
Chaini18 – 517500Aldehyde dehydrogenase, mitochondrial
PRO_0000007168Add
BLAST

Amino acid modifications

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

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.

Miscellaneous databases

EvolutionaryTraceiP05091.

Family & Domainsi

Sequence similaritiesi

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.

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.
VSP_046715Add
BLAST

Sequence conflict

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

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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 186 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

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