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Protein

Aldehyde dehydrogenase, mitochondrial

Gene

ALDH2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 – 2676NADBy similarity

GO - Molecular functioni

  • aldehyde dehydrogenase (NAD) activity Source: CACAO
  • aldehyde dehydrogenase [NAD(P)+] activity Source: ProtInc
  • electron carrier activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER66-302.
BRENDAi1.2.1.3. 2681.
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 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:404. ALDH2.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • mitochondrial matrix Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

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

Chemistry

DrugBankiDB01612. Amyl Nitrite.
DB06770. Benzyl alcohol.
DB00822. Disulfiram.
DB00536. Guanidine.
DB00435. Nitric Oxide.
DB00727. Nitroglycerin.

Polymorphism and mutation databases

BioMutaiALDH2.
DMDMi118504.

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-acetyllysine; alternateBy similarity
Modified residuei52 – 521N6-succinyllysine; alternateBy similarity
Modified residuei73 – 731N6-acetyllysineBy similarity
Modified residuei78 – 781N6-acetyllysineBy similarity
Modified residuei81 – 811N6-succinyllysineBy similarity
Modified residuei159 – 1591N6-acetyllysineBy similarity
Modified residuei368 – 3681N6-acetyllysineBy similarity
Modified residuei383 – 3831N6-acetyllysine; alternateBy similarity
Modified residuei383 – 3831N6-succinyllysine; alternateBy similarity
Modified residuei414 – 4141N6-acetyllysine; alternateBy similarity
Modified residuei414 – 4141N6-succinyllysine; alternateBy similarity
Modified residuei426 – 4261N6-acetyllysine; alternateBy similarity
Modified residuei426 – 4261N6-succinyllysine; alternateBy 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

BgeeiP05091.
CleanExiHS_ALDH2.
ExpressionAtlasiP05091. baseline and differential.
GenevestigatoriP05091.

Organism-specific databases

HPAiHPA051065.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi106719. 28 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 – 414Combined sources
Beta strandi44 – 463Combined sources
Beta strandi53 – 575Combined sources
Turni59 – 613Combined sources
Beta strandi64 – 696Combined sources
Helixi73 – 8614Combined sources
Helixi92 – 954Combined sources
Helixi98 – 11417Combined sources
Helixi116 – 12712Combined sources
Helixi131 – 1366Combined sources
Helixi138 – 15215Combined sources
Turni153 – 1553Combined sources
Beta strandi158 – 1614Combined sources
Beta strandi164 – 17512Combined sources
Beta strandi178 – 1825Combined sources
Beta strandi185 – 1873Combined sources
Helixi188 – 20114Combined sources
Beta strandi205 – 2095Combined sources
Beta strandi212 – 2143Combined sources
Helixi216 – 22813Combined sources
Beta strandi234 – 2374Combined sources
Turni242 – 2443Combined sources
Helixi245 – 2506Combined sources
Beta strandi257 – 2626Combined sources
Helixi264 – 27613Combined sources
Beta strandi281 – 2855Combined sources
Beta strandi290 – 2945Combined sources
Helixi300 – 31213Combined sources
Helixi313 – 3164Combined sources
Beta strandi322 – 3287Combined sources
Helixi329 – 34517Combined sources
Helixi364 – 37916Combined sources
Beta strandi383 – 3864Combined sources
Beta strandi389 – 3913Combined sources
Beta strandi393 – 3964Combined sources
Beta strandi401 – 4055Combined sources
Helixi411 – 4144Combined sources
Beta strandi419 – 4279Combined sources
Helixi430 – 4389Combined sources
Beta strandi439 – 4413Combined sources
Beta strandi444 – 4496Combined sources
Helixi453 – 46210Combined sources
Beta strandi465 – 4717Combined sources
Beta strandi478 – 4803Combined sources
Helixi486 – 4883Combined sources
Beta strandi489 – 4913Combined sources
Helixi496 – 5027Combined sources
Beta strandi503 – 5119Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000118999.
HOGENOMiHOG000271505.
HOVERGENiHBG000097.
InParanoidiP05091.
KOiK00128.
OMAiHLIMEAA.
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. AlignAdd to basket

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

        10         20         30         40         50
MLRAAARFGP RLGRRLLSAA ATQAVPAPNQ QPEVFCNQIF INNEWHDAVS
60 70 80 90 100
RKTFPTVNPS TGEVICQVAE GDKEDVDKAV KAARAAFQLG SPWRRMDASH
110 120 130 140 150
RGRLLNRLAD LIERDRTYLA ALETLDNGKP YVISYLVDLD MVLKCLRYYA
160 170 180 190 200
GWADKYHGKT IPIDGDFFSY TRHEPVGVCG QIIPWNFPLL MQAWKLGPAL
210 220 230 240 250
ATGNVVVMKV AEQTPLTALY VANLIKEAGF PPGVVNIVPG FGPTAGAAIA
260 270 280 290 300
SHEDVDKVAF TGSTEIGRVI QVAAGSSNLK RVTLELGGKS PNIIMSDADM
310 320 330 340 350
DWAVEQAHFA LFFNQGQCCC AGSRTFVQED IYDEFVERSV ARAKSRVVGN
360 370 380 390 400
PFDSKTEQGP QVDETQFKKI LGYINTGKQE GAKLLCGGGI AADRGYFIQP
410 420 430 440 450
TVFGDVQDGM TIAKEEIFGP VMQILKFKTI EEVVGRANNS TYGLAAAVFT
460 470 480 490 500
KDLDKANYLS QALQAGTVWV NCYDVFGAQS PFGGYKMSGS GRELGEYGLQ
510
AYTEVKTVTV KVPQKNS
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 AAA62825.1 differs from that shown. Reason: Frameshift at positions 424, 444, 448 and 461. Curated
The sequence CAA68290.1 differs from that shown.Curated
The sequence CAA68290.1 differs from that shown. Reason: Frameshift at several positions. Curated

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 (Ref. 6) Curated
Sequence conflicti80 – 856VKAARA → REGRPG in CAA28990 (PubMed:3582651).Curated
Sequence conflicti101 – 1011R → S in CAA28990 (PubMed:3582651).Curated
Sequence conflicti116 – 1161R → Q in AAT41621 (Ref. 5) Curated
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 (Ref. 6) Curated
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:
EMBLi
GenBanki
DDBJi
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]

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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi106719. 28 interactions.
DIPiDIP-40262N.
IntActiP05091. 15 interactions.
MINTiMINT-1368102.
STRINGi9606.ENSP00000261733.

Chemistry

BindingDBiP05091.
ChEMBLiCHEMBL1935.
DrugBankiDB01612. Amyl Nitrite.
DB06770. Benzyl alcohol.
DB00822. Disulfiram.
DB00536. Guanidine.
DB00435. Nitric Oxide.
DB00727. Nitroglycerin.
GuidetoPHARMACOLOGYi2595.

PTM databases

PhosphoSiteiP05091.

Polymorphism and mutation databases

BioMutaiALDH2.
DMDMi118504.

2D gel databases

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

Proteomic databases

MaxQBiP05091.
PaxDbiP05091.
PeptideAtlasiP05091.
PRIDEiP05091.

Protocols and materials databases

DNASUi217.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi217.
GeneCardsiGC12P112205.
HGNCiHGNC:404. ALDH2.
HPAiHPA051065.
MIMi100650. gene+phenotype.
610251. phenotype.
neXtProtiNX_P05091.
PharmGKBiPA24696.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1012.
GeneTreeiENSGT00760000118999.
HOGENOMiHOG000271505.
HOVERGENiHBG000097.
InParanoidiP05091.
KOiK00128.
OMAiHLIMEAA.
OrthoDBiEOG7PS1F7.
PhylomeDBiP05091.
TreeFamiTF300455.

Enzyme and pathway databases

UniPathwayiUPA00780; UER00768.
BioCyciMetaCyc:MONOMER66-302.
BRENDAi1.2.1.3. 2681.
ReactomeiREACT_15532. Metabolism of serotonin.
REACT_34. Ethanol oxidation.
SABIO-RKP05091.

Miscellaneous databases

ChiTaRSiALDH2. human.
EvolutionaryTraceiP05091.
GeneWikiiALDH2.
GenomeRNAii217.
NextBioi878.
PROiP05091.
SOURCEiSearch...

Gene expression databases

BgeeiP05091.
CleanExiHS_ALDH2.
ExpressionAtlasiP05091. baseline and differential.
GenevestigatoriP05091.

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]
ProtoNetiSearch...

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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. "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).
  20. "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.
  21. "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: May 27, 2015
This is version 194 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.