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Entry version 196 (13 Feb 2019)
Sequence version 2 (23 Jan 2007)
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Protein

Retinal dehydrogenase 1

Gene

ALDH1A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Can convert/oxidize retinaldehyde to retinoic acid. Binds free retinal and cellular retinol-binding protein-bound retinal (By similarity). May have a broader specificity and oxidize other aldehydes in vivo (PubMed:19296407, PubMed:26373694, PubMed:25450233).By similarity3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by citral, disulfiram, and cyanamide. Activated by diethylstilbestrol (PubMed:19296407). Inhibited by duocarmycin analogs (PubMed:26373694).2 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=59.4 µM for NAD (at pH 8.0)1 Publication
  2. KM=238.2 µM for acetaldehyde (at pH 8.0)1 Publication
  3. KM=142.2 µM for benzaldehyde (at pH 8.0)1 Publication
  4. KM=4.8 µM for 4-hydroxynonenal (at pH 8.0)1 Publication
  5. KM=121.4 µM for propionaldehyde (at pH 8.0)1 Publication
  6. KM=15 µM for propionaldehyde (at pH 7.5)1 Publication
  7. KM=3.5 µM for malonaldehyde (at pH 8.0)1 Publication
  8. KM=177.1 µM for trans-2-heptenal (at pH 8.0)1 Publication
  1. Vmax=149.7 nmol/min/mg enzyme with NAD (at pH 8.0)1 Publication
  2. Vmax=631.4 nmol/min/mg enzyme with acetaldehyde (at pH 8.0)1 Publication
  3. Vmax=750.3 nmol/min/mg enzyme with benzaldehyde (at pH 8.0)1 Publication
  4. Vmax=135 nmol/min/mg enzyme with 4-hydroxynonenal (at pH 8.0)1 Publication
  5. Vmax=445.3 nmol/min/mg enzyme with propionaldehyde (at pH 8.0)1 Publication
  6. Vmax=381.6 nmol/min/mg enzyme with malonaldehyde (at pH 8.0)1 Publication
  7. Vmax=155.8 nmol/min/mg enzyme with trans-2-heptenal (at pH 8.0)1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: retinol metabolism

This protein is involved in the pathway retinol metabolism, which is part of Cofactor metabolism.By similarity
View all proteins of this organism that are known to be involved in the pathway retinol metabolism and in Cofactor metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei170Transition state stabilizerBy similarity1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei269Proton acceptorPROSITE-ProRule annotation1 Publication1
Active sitei303NucleophilePROSITE-ProRule annotation1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi167 – 170NADCombined sources4
Nucleotide bindingi193 – 196NADCombined sources4
Nucleotide bindingi226 – 227NADCombined sources2
Nucleotide bindingi246 – 247NADCombined sources2
Nucleotide bindingi269 – 271NADCombined sources3
Nucleotide bindingi349 – 353NADCombined sources5
Nucleotide bindingi400 – 402NADCombined sources3

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • aldehyde dehydrogenase (NAD) activity Source: UniProtKB
  • androgen binding Source: ProtInc
  • benzaldehyde dehydrogenase (NAD+) activity Source: GO_Central
  • GTPase activator activity Source: UniProtKB
  • NAD binding Source: CAFA
  • retinal dehydrogenase activity Source: UniProtKB

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase
LigandNAD, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:HS09183-MONOMER

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-5365859 RA biosynthesis pathway
R-HSA-70350 Fructose catabolism
R-HSA-71384 Ethanol oxidation

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P00352

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P00352

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00912

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Retinal dehydrogenase 1Curated (EC:1.2.1.-3 Publications, EC:1.2.1.36By similarity)
Short name:
RALDH 1Curated
Short name:
RalDH1Curated
Alternative name(s):
ALDH-E1
ALHDII
Aldehyde dehydrogenase family 1 member A1Imported
Aldehyde dehydrogenase, cytosolic1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ALDH1A1Imported
Synonyms:ALDC, ALDH1Imported, PUMB1Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 9

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000165092.12

Human Gene Nomenclature Database

More...
HGNCi
HGNC:402 ALDH1A1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
100640 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P00352

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi302C → A or S: Does not prevent inhibition by duocarmycin analogs. 1 Publication1
Mutagenesisi458G → N: No significant effect on aldehyde dehydrogenase activity. Prevents the inhibition by ALDH1A1-specific inhibitors. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
216

Open Targets

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OpenTargetsi
ENSG00000165092

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA24692

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3577

Drug and drug target database

More...
DrugBanki
DB09462 Glycerin
DB00157 NADH
DB00755 Tretinoin
DB00162 Vitamin A

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
ALDH1A1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
118495

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources1 Publication
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000564152 – 501Retinal dehydrogenase 1Add BLAST500

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserineCombined sources1 Publication1
Modified residuei91N6-acetyllysineCombined sources1
Modified residuei128N6-acetyllysineCombined sources1
Modified residuei252N6-acetyllysineCombined sources1
Modified residuei337PhosphothreonineCombined sources1
Modified residuei353N6-acetyllysineCombined sources1
Modified residuei367N6-acetyllysineCombined sources1
Modified residuei410N6-acetyllysineCombined sources1
Modified residuei413PhosphoserineCombined sources1
Modified residuei419N6-acetyllysineCombined sources1
Modified residuei435N6-acetyllysineCombined sources1
Modified residuei495N6-acetyllysineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The N-terminus is blocked most probably by acetylation.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P00352

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P00352

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P00352

PeptideAtlas

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PeptideAtlasi
P00352

PRoteomics IDEntifications database

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PRIDEi
P00352

ProteomicsDB human proteome resource

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ProteomicsDBi
51235

2D gel databases

DOSAC-COBS 2D-PAGE database

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DOSAC-COBS-2DPAGEi
P00352

REPRODUCTION-2DPAGE

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REPRODUCTION-2DPAGEi
IPI00218914
P00352

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
P00352

University College Dublin 2-DE Proteome Database

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UCD-2DPAGEi
P00352

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P00352

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P00352

SwissPalm database of S-palmitoylation events

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SwissPalmi
P00352

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000165092 Expressed in 224 organ(s), highest expression level in nasal cavity epithelium

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P00352 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P00352 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB020690
HPA002123

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
106718, 6 interactors

Protein interaction database and analysis system

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IntActi
P00352, 7 interactors

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000297785

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P00352

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1501
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4WB9X-ray2.07A1-501[»]
4WJ9X-ray1.74A1-501[»]
4WP7X-ray1.80A1-501[»]
4WPNX-ray1.95A1-501[»]
4X4LX-ray1.85A1-501[»]
5AC2X-ray1.85A1-501[»]
5L2MX-ray1.70A1-501[»]
5L2NX-ray1.70A1-501[»]
5L2OX-ray2.05A/B/C/D/E/F/G/H1-501[»]
5TEIX-ray2.10A1-501[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P00352

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P00352

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG2450 Eukaryota
COG1012 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000154609

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000271505

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG000097

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P00352

KEGG Orthology (KO)

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KOi
K07249

Identification of Orthologs from Complete Genome Data

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OMAi
KTIWIAL

Database of Orthologous Groups

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OrthoDBi
153834at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P00352

TreeFam database of animal gene trees

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TreeFami
TF300455

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.40.309.10, 1 hit
3.40.605.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
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

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00171 Aldedh, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF53720 SSF53720, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00070 ALDEHYDE_DEHYDR_CYS, 1 hit
PS00687 ALDEHYDE_DEHYDR_GLU, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB26464DC7168348E
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q5SYQ8Q5SYQ8_HUMAN
Retinal dehydrogenase 1
ALDH1A1
238Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q5SYQ9Q5SYQ9_HUMAN
Retinal dehydrogenase 1
ALDH1A1
230Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q5SYQ7Q5SYQ7_HUMAN
Retinal dehydrogenase 1
ALDH1A1
203Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti162V → I in AAA35518 (PubMed:4015823).Curated1
Sequence conflicti162V → I in AAA51695 (PubMed:2987944).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_048901121N → S1 PublicationCorresponds to variant dbSNP:rs1049981Ensembl.1
Natural variantiVAR_048902125G → R. Corresponds to variant dbSNP:rs11554423Ensembl.1
Natural variantiVAR_017778177I → F1 PublicationCorresponds to variant dbSNP:rs8187929Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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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 No translation available.
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

The Consensus CDS (CCDS) project

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CCDSi
CCDS6644.1

Protein sequence database of the Protein Information Resource

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PIRi
A33371 DEHUE1

NCBI Reference Sequences

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RefSeqi
NP_000680.2, NM_000689.4

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.76392

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000297785; ENSP00000297785; ENSG00000165092

Database of genes from NCBI RefSeq genomes

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GeneIDi
216

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:216

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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 No translation available.
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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4WB9X-ray2.07A1-501[»]
4WJ9X-ray1.74A1-501[»]
4WP7X-ray1.80A1-501[»]
4WPNX-ray1.95A1-501[»]
4X4LX-ray1.85A1-501[»]
5AC2X-ray1.85A1-501[»]
5L2MX-ray1.70A1-501[»]
5L2NX-ray1.70A1-501[»]
5L2OX-ray2.05A/B/C/D/E/F/G/H1-501[»]
5TEIX-ray2.10A1-501[»]
ProteinModelPortaliP00352
SMRiP00352
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106718, 6 interactors
IntActiP00352, 7 interactors
STRINGi9606.ENSP00000297785

Chemistry databases

BindingDBiP00352
ChEMBLiCHEMBL3577
DrugBankiDB09462 Glycerin
DB00157 NADH
DB00755 Tretinoin
DB00162 Vitamin A

PTM databases

iPTMnetiP00352
PhosphoSitePlusiP00352
SwissPalmiP00352

Polymorphism and mutation databases

BioMutaiALDH1A1
DMDMi118495

2D gel databases

DOSAC-COBS-2DPAGEiP00352
REPRODUCTION-2DPAGEiIPI00218914
P00352
SWISS-2DPAGEiP00352
UCD-2DPAGEiP00352

Proteomic databases

EPDiP00352
jPOSTiP00352
PaxDbiP00352
PeptideAtlasiP00352
PRIDEiP00352
ProteomicsDBi51235

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
216
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000297785; ENSP00000297785; ENSG00000165092
GeneIDi216
KEGGihsa:216

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
216
DisGeNETi216
EuPathDBiHostDB:ENSG00000165092.12

GeneCards: human genes, protein and diseases

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GeneCardsi
ALDH1A1
HGNCiHGNC:402 ALDH1A1
HPAiCAB020690
HPA002123
MIMi100640 gene
neXtProtiNX_P00352
OpenTargetsiENSG00000165092
PharmGKBiPA24692

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG2450 Eukaryota
COG1012 LUCA
GeneTreeiENSGT00940000154609
HOGENOMiHOG000271505
HOVERGENiHBG000097
InParanoidiP00352
KOiK07249
OMAiKTIWIAL
OrthoDBi153834at2759
PhylomeDBiP00352
TreeFamiTF300455

Enzyme and pathway databases

UniPathwayi
UPA00912

BioCyciMetaCyc:HS09183-MONOMER
ReactomeiR-HSA-5365859 RA biosynthesis pathway
R-HSA-70350 Fructose catabolism
R-HSA-71384 Ethanol oxidation
SABIO-RKiP00352
SIGNORiP00352

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
ALDH1A1 human

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
ALDH1A1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
216

Protein Ontology

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PROi
PR:P00352

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000165092 Expressed in 224 organ(s), highest expression level in nasal cavity epithelium
ExpressionAtlasiP00352 baseline and differential
GenevisibleiP00352 HS

Family and domain databases

Gene3Di3.40.309.10, 1 hit
3.40.605.10, 1 hit
InterProiView protein in InterPro
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
PfamiView protein in Pfam
PF00171 Aldedh, 1 hit
SUPFAMiSSF53720 SSF53720, 1 hit
PROSITEiView protein in PROSITE
PS00070 ALDEHYDE_DEHYDR_CYS, 1 hit
PS00687 ALDEHYDE_DEHYDR_GLU, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAL1A1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P00352
Secondary accession number(s): O00768, Q5SYR1
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: February 13, 2019
This is version 196 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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