H0YMG7 · H0YMG7_HUMAN
- ProteinRetinal dehydrogenase 2
- GeneALDH1A2
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids489 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
Catalytic activity
- H2O + NAD+ + retinal = 2 H+ + NADH + retinoateThis reaction proceeds in the forward direction.
- all-trans-13,14-dihydroretinal + H2O + NAD+ = all-trans-13,14-dihydroretinoate + 2 H+ + NADHThis reaction proceeds in the forward direction.
Pathway
Cofactor metabolism; retinol metabolism.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 257 | |||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRetinal dehydrogenase 2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionH0YMG7
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 589 variants from UniProt as well as other sources including ClinVar and dbSNP.
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue (large scale data) | 255 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 322 | PRIDE | Phosphoserine | ||||
Sequence: S |
Proteomic databases
Expression
Gene expression databases
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 17-480 | Aldehyde dehydrogenase | ||||
Sequence: WQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGSVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV |
Sequence similarities
Belongs to the aldehyde dehydrogenase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length489
- Mass (Da)53,762
- Last updated2012-02-22 v1
- Checksum0A2F553360563D90
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC012653 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC018904 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC025431 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC066616 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC084781 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
KF510409 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |