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P00352

- AL1A1_HUMAN

UniProt

P00352 - AL1A1_HUMAN

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Protein

Retinal dehydrogenase 1

Gene

ALDH1A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Retinal + NAD+ + H2O = retinoate + NADH.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei170 – 1701Transition state stabilizerBy similarity
Active sitei269 – 2691Proton acceptor1 PublicationPROSITE-ProRule annotation
Active sitei303 – 3031Nucleophile1 PublicationPROSITE-ProRule annotation
Binding sitei456 – 4561NAD

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi246 – 2516NADBy similarity

GO - Molecular functioni

  1. aldehyde dehydrogenase (NAD) activity Source: Reactome
  2. androgen binding Source: ProtInc
  3. Ras GTPase activator activity Source: UniProtKB
  4. retinal dehydrogenase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular aldehyde metabolic process Source: ProtInc
  2. ethanol oxidation Source: Reactome
  3. positive regulation of Ras GTPase activity Source: GOC
  4. retinol metabolic process Source: UniProtKB-UniPathway
  5. small molecule metabolic process Source: Reactome
  6. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:HS09183-MONOMER.
ReactomeiREACT_34. Ethanol oxidation.
SABIO-RKP00352.
UniPathwayiUPA00912.

Names & Taxonomyi

Protein namesi
Recommended name:
Retinal dehydrogenase 1 (EC:1.2.1.36)
Short name:
RALDH 1
Short name:
RalDH1
Alternative name(s):
ALDH-E1
ALHDII
Aldehyde dehydrogenase family 1 member A1
Aldehyde dehydrogenase, cytosolic
Gene namesi
Name:ALDH1A1
Synonyms:ALDC, ALDH1, PUMB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:402. ALDH1A1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24692.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 501500Retinal dehydrogenase 1PRO_0000056415Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei91 – 911N6-acetyllysine1 Publication
Modified residuei128 – 1281N6-acetyllysine1 Publication
Modified residuei252 – 2521N6-acetyllysine1 Publication
Modified residuei353 – 3531N6-acetyllysine1 Publication
Modified residuei367 – 3671N6-acetyllysine1 Publication
Modified residuei410 – 4101N6-acetyllysine1 Publication
Modified residuei419 – 4191N6-acetyllysine1 Publication
Modified residuei435 – 4351N6-acetyllysine1 Publication
Modified residuei495 – 4951N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP00352.
PaxDbiP00352.
PeptideAtlasiP00352.
PRIDEiP00352.

2D gel databases

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

PTM databases

PhosphoSiteiP00352.

Expressioni

Gene expression databases

BgeeiP00352.
CleanExiHS_ALDH1A1.
ExpressionAtlasiP00352. baseline and differential.
GenevestigatoriP00352.

Organism-specific databases

HPAiCAB020690.
HPA002123.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi106718. 8 interactions.
IntActiP00352. 6 interactions.
MINTiMINT-4999613.
STRINGi9606.ENSP00000297785.

Structurei

3D structure databases

ProteinModelPortaliP00352.
SMRiP00352. Positions 8-501.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Phylogenomic databases

eggNOGiCOG1012.
HOGENOMiHOG000271505.
HOVERGENiHBG000097.
InParanoidiP00352.
KOiK07249.
OMAiEWHDSAS.
OrthoDBiEOG7PS1F7.
PhylomeDBiP00352.
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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00352-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSSGTPDLP VLLTDLKIQY TKIFINNEWH DSVSGKKFPV FNPATEEELC
60 70 80 90 100
QVEEGDKEDV DKAVKAARQA FQIGSPWRTM DASERGRLLY KLADLIERDR
110 120 130 140 150
LLLATMESMN GGKLYSNAYL NDLAGCIKTL RYCAGWADKI QGRTIPIDGN
160 170 180 190 200
FFTYTRHEPI GVCGQIIPWN FPLVMLIWKI GPALSCGNTV VVKPAEQTPL
210 220 230 240 250
TALHVASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDID KVAFTGSTEV
260 270 280 290 300
GKLIKEAAGK SNLKRVTLEL GGKSPCIVLA DADLDNAVEF AHHGVFYHQG
310 320 330 340 350
QCCIAASRIF VEESIYDEFV RRSVERAKKY ILGNPLTPGV TQGPQIDKEQ
360 370 380 390 400
YDKILDLIES GKKEGAKLEC GGGPWGNKGY FVQPTVFSNV TDEMRIAKEE
410 420 430 440 450
IFGPVQQIMK FKSLDDVIKR ANNTFYGLSA GVFTKDIDKA ITISSALQAG
460 470 480 490 500
TVWVNCYGVV SAQCPFGGFK MSGNGRELGE YGFHEYTEVK TVTVKISQKN

S
Length:501
Mass (Da):54,862
Last modified:January 23, 2007 - v2
Checksum:iB26464DC7168348E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti162 – 1621V → I in AAA35518. (PubMed:4015823)Curated
Sequence conflicti162 – 1621V → I in AAA51695. (PubMed:2987944)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti121 – 1211N → S.1 Publication
Corresponds to variant rs1049981 [ dbSNP | Ensembl ].
VAR_048901
Natural varianti125 – 1251G → R.
Corresponds to variant rs11554423 [ dbSNP | Ensembl ].
VAR_048902
Natural varianti177 – 1771I → F.1 Publication
Corresponds to variant rs8187929 [ dbSNP | Ensembl ].
VAR_017778

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31994
, 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.
CCDSiCCDS6644.1.
PIRiA33371. DEHUE1.
RefSeqiNP_000680.2. NM_000689.4.
UniGeneiHs.76392.

Genome annotation databases

EnsembliENST00000297785; ENSP00000297785; ENSG00000165092.
GeneIDi216.
KEGGihsa:216.
UCSCiuc004ajd.3. human.

Polymorphism databases

DMDMi118495.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31994
, 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 .
CCDSi CCDS6644.1.
PIRi A33371. DEHUE1.
RefSeqi NP_000680.2. NM_000689.4.
UniGenei Hs.76392.

3D structure databases

ProteinModelPortali P00352.
SMRi P00352. Positions 8-501.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106718. 8 interactions.
IntActi P00352. 6 interactions.
MINTi MINT-4999613.
STRINGi 9606.ENSP00000297785.

Chemistry

BindingDBi P00352.
ChEMBLi CHEMBL3577.
DrugBanki DB00755. Tretinoin.
DB00162. Vitamin A.

PTM databases

PhosphoSitei P00352.

Polymorphism databases

DMDMi 118495.

2D gel databases

DOSAC-COBS-2DPAGE P00352.
REPRODUCTION-2DPAGE IPI00218914.
P00352.
SWISS-2DPAGE P00352.
UCD-2DPAGE P00352.

Proteomic databases

MaxQBi P00352.
PaxDbi P00352.
PeptideAtlasi P00352.
PRIDEi P00352.

Protocols and materials databases

DNASUi 216.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000297785 ; ENSP00000297785 ; ENSG00000165092 .
GeneIDi 216.
KEGGi hsa:216.
UCSCi uc004ajd.3. human.

Organism-specific databases

CTDi 216.
GeneCardsi GC09M075515.
HGNCi HGNC:402. ALDH1A1.
HPAi CAB020690.
HPA002123.
MIMi 100640. gene.
neXtProti NX_P00352.
PharmGKBi PA24692.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1012.
HOGENOMi HOG000271505.
HOVERGENi HBG000097.
InParanoidi P00352.
KOi K07249.
OMAi EWHDSAS.
OrthoDBi EOG7PS1F7.
PhylomeDBi P00352.
TreeFami TF300455.

Enzyme and pathway databases

UniPathwayi UPA00912 .
BioCyci MetaCyc:HS09183-MONOMER.
Reactomei REACT_34. Ethanol oxidation.
SABIO-RK P00352.

Miscellaneous databases

ChiTaRSi ALDH1A1. human.
GeneWikii ALDH1A1.
GenomeRNAii 216.
NextBioi 874.
PROi P00352.
SOURCEi Search...

Gene expression databases

Bgeei P00352.
CleanExi HS_ALDH1A1.
ExpressionAtlasi P00352. baseline and differential.
Genevestigatori P00352.

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. "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.
    , 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. 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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 162-501.
    Tissue: Liver.
  13. 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. 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].

Entry informationi

Entry nameiAL1A1_HUMAN
AccessioniPrimary (citable) accession number: P00352
Secondary accession number(s): O00768, Q5SYR1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 160 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3