Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P00352 (AL1A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Retinal dehydrogenase 1

Short name=RALDH 1
Short name=RalDH1
EC=1.2.1.36
Alternative name(s):
ALDH-E1
ALHDII
Aldehyde dehydrogenase family 1 member A1
Aldehyde dehydrogenase, cytosolic
Gene names
Name:ALDH1A1
Synonyms:ALDC, ALDH1, PUMB1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length501 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds free retinal and cellular retinol-binding protein-bound retinal. Can convert/oxidize retinaldehyde to retinoic acid By similarity.

Catalytic activity

Retinal + NAD+ + H2O = retinoate + NADH.

Pathway

Cofactor metabolism; retinol metabolism.

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 501500Retinal dehydrogenase 1
PRO_0000056415

Regions

Nucleotide binding246 – 2516NAD By similarity

Sites

Active site2691Proton acceptor Ref.13
Active site3031Nucleophile Ref.13
Binding site4561NAD
Site1701Transition state stabilizer By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.10 Ref.17
Modified residue911N6-acetyllysine Ref.15
Modified residue1281N6-acetyllysine Ref.15
Modified residue2521N6-acetyllysine Ref.15
Modified residue3531N6-acetyllysine Ref.15
Modified residue3671N6-acetyllysine Ref.15
Modified residue4101N6-acetyllysine Ref.15
Modified residue4191N6-acetyllysine Ref.15
Modified residue4351N6-acetyllysine Ref.15
Modified residue4951N6-acetyllysine Ref.15

Natural variations

Natural variant1211N → S. Ref.2
Corresponds to variant rs1049981 [ dbSNP | Ensembl ].
VAR_048901
Natural variant1251G → R.
Corresponds to variant rs11554423 [ dbSNP | Ensembl ].
VAR_048902
Natural variant1771I → F. Ref.5
Corresponds to variant rs8187929 [ dbSNP | Ensembl ].
VAR_017778

Experimental info

Sequence conflict1621V → I in AAA35518. Ref.11
Sequence conflict1621V → I in AAA51695. Ref.12

Sequences

Sequence LengthMass (Da)Tools
P00352 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: B26464DC7168348E

FASTA50154,862
        10         20         30         40         50         60 
MSSSGTPDLP VLLTDLKIQY TKIFINNEWH DSVSGKKFPV FNPATEEELC QVEEGDKEDV 

        70         80         90        100        110        120 
DKAVKAARQA FQIGSPWRTM DASERGRLLY KLADLIERDR LLLATMESMN GGKLYSNAYL 

       130        140        150        160        170        180 
NDLAGCIKTL RYCAGWADKI QGRTIPIDGN FFTYTRHEPI GVCGQIIPWN FPLVMLIWKI 

       190        200        210        220        230        240 
GPALSCGNTV VVKPAEQTPL TALHVASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDID 

       250        260        270        280        290        300 
KVAFTGSTEV GKLIKEAAGK SNLKRVTLEL GGKSPCIVLA DADLDNAVEF AHHGVFYHQG 

       310        320        330        340        350        360 
QCCIAASRIF VEESIYDEFV RRSVERAKKY ILGNPLTPGV TQGPQIDKEQ YDKILDLIES 

       370        380        390        400        410        420 
GKKEGAKLEC GGGPWGNKGY FVQPTVFSNV TDEMRIAKEE IFGPVQQIMK FKSLDDVIKR 

       430        440        450        460        470        480 
ANNTFYGLSA GVFTKDIDKA ITISSALQAG TVWVNCYGVV SAQCPFGGFK MSGNGRELGE 

       490        500 
YGFHEYTEVK TVTVKISQKN S 

« Hide

References

« Hide 'large scale' references
[1]"Genomic structure of the human cytosolic aldehyde dehydrogenase gene."
Hsu L.C., Chang W.-C., Yoshida A.
Genomics 5:857-865(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Cloning and expression of the full-length cDNAs encoding human liver class 1 and class 2 aldehyde dehydrogenase."
Zheng C.F., Wang T.T., Weiner H.
Alcohol. Clin. Exp. Res. 17:828-831(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-121.
Tissue: Liver.
[3]"Cloning and expression of aldehyde dehydrogenase 1 (ALDH1A1) from human lens cDNA library."
Ramana K.V., Xiao T., Ansari N.H.
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lens.
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]NIEHS SNPs program
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PHE-177.
[6]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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].
Tissue: Colon.
[9]"Biological role of human cytosolic aldehyde dehydrogenase 1: hormonal response, retinal oxidation and implication in testicular feminization."
Yoshida A., Hsu L.C., Yanagawa Y.
Adv. Exp. Med. Biol. 328:37-44(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
[10]"Aldehyde dehydrogenase from human liver. Primary structure of the cytoplasmic isoenzyme."
Hempel J., von Bahr-Lindstroem H., Joernvall H.
Eur. J. Biochem. 141:21-35(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-501, ACETYLATION AT SER-2.
Tissue: Liver.
[11]"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 162-501.
[12]"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 162-501.
Tissue: Liver.
[13]"Active site of human liver aldehyde dehydrogenase."
Abriola D.P., Fields R., Stein S., Mackerell A.D. Jr., Pietruszko R.
Biochemistry 26:5679-5684(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 266-273, ACTIVE SITES GLU-269 AND CYS-303, NAD-BINDING SITE CYS-456.
[14]"Aldehyde dehydrogenase from human erythrocytes: structural relationship to the liver cytosolic isozyme."
Agarwal D.P., Cohn P., Goedde H.W., Hempel J.
Enzyme 42:47-52(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
Tissue: Erythrocyte.
[15]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-91; LYS-128; LYS-252; LYS-353; LYS-367; LYS-410; LYS-419; LYS-435 AND LYS-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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].
[17]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M31994 expand/collapse EMBL AC list , M31982, M31983, M31984, M31985, M31986, M31987, M31988, M31989, M31990, M31991, M31992 Genomic DNA. Translation: AAA51692.1.
AF003341 mRNA. Translation: AAC51652.1.
AY390731 mRNA. Translation: AAR92229.1.
BT006921 mRNA. Translation: AAP35567.1.
AY338497 Genomic DNA. Translation: AAP88039.1.
AL591031 Genomic DNA. Translation: CAI12257.1.
CH471089 Genomic DNA. Translation: EAW62543.1.
BC001505 mRNA. Translation: AAH01505.1.
S61235 Genomic DNA. Translation: AAD13925.1.
M26761 mRNA. Translation: AAA35518.1.
K03000 mRNA. Translation: AAA51695.1.
CCDSCCDS6644.1.
PIRDEHUE1. A33371.
RefSeqNP_000680.2. NM_000689.4.
UniGeneHs.76392.

3D structure databases

ProteinModelPortalP00352.
SMRP00352. Positions 8-501.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106718. 6 interactions.
IntActP00352. 6 interactions.
MINTMINT-4999613.
STRING9606.ENSP00000297785.

Chemistry

BindingDBP00352.
ChEMBLCHEMBL3577.
DrugBankDB00157. NADH.
DB00755. Tretinoin.
DB00162. Vitamin A.

PTM databases

PhosphoSiteP00352.

Polymorphism databases

DMDM118495.

2D gel databases

DOSAC-COBS-2DPAGEP00352.
REPRODUCTION-2DPAGEIPI00218914.
P00352.
SWISS-2DPAGEP00352.
UCD-2DPAGEP00352.

Proteomic databases

MaxQBP00352.
PaxDbP00352.
PeptideAtlasP00352.
PRIDEP00352.

Protocols and materials databases

DNASU216.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000297785; ENSP00000297785; ENSG00000165092.
GeneID216.
KEGGhsa:216.
UCSCuc004ajd.3. human.

Organism-specific databases

CTD216.
GeneCardsGC09M075515.
HGNCHGNC:402. ALDH1A1.
HPACAB020690.
HPA002123.
MIM100640. gene.
neXtProtNX_P00352.
PharmGKBPA24692.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1012.
HOGENOMHOG000271505.
HOVERGENHBG000097.
InParanoidP00352.
KOK07249.
OMAEWHDSAS.
OrthoDBEOG7PS1F7.
PhylomeDBP00352.
TreeFamTF300455.

Enzyme and pathway databases

BioCycMetaCyc:HS09183-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP00352.
UniPathwayUPA00912.

Gene expression databases

ArrayExpressP00352.
BgeeP00352.
CleanExHS_ALDH1A1.
GenevestigatorP00352.

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_CYS.
IPR029510. Ald_DH_CS_GLU.
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

ChiTaRSALDH1A1. human.
GeneWikiALDH1A1.
GenomeRNAi216.
NextBio874.
PROP00352.
SOURCESearch...

Entry information

Entry nameAL1A1_HUMAN
AccessionPrimary (citable) accession number: P00352
Secondary accession number(s): O00768, Q5SYR1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 157 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

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 9

Human chromosome 9: entries, gene names and cross-references to MIM