Q66JG8 · ALKB5_XENTR
- ProteinRNA demethylase ALKBH5
- Genealkbh5
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids358 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
Dioxygenase that specifically demethylates N6-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes. Demethylates RNA by oxidative demethylation, which requires molecular oxygen, alpha-ketoglutarate and iron. Demethylation of m6A mRNA affects mRNA processing, translation and export.
Catalytic activity
- 2-oxoglutarate + an N6-methyladenosine in mRNA + O2 = an adenosine in mRNA + CO2 + formaldehyde + succinateThis reaction proceeds in the forward direction.
Cofactor
Note: Binds 1 Fe2+ ion per subunit.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 105 | |||||
Sequence: Y | ||||||
Binding site | 159 | 2-oxoglutarate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 161 | 2-oxoglutarate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 170 | 2-oxoglutarate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 232 | 2-oxoglutarate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 243 | 2-oxoglutarate (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nuclear speck | |
Cellular Component | nucleus | |
Cellular Component | paraspeckles | |
Molecular Function | 2-oxoglutarate-dependent dioxygenase activity | |
Molecular Function | metal ion binding | |
Molecular Function | molecular condensate scaffold activity | |
Molecular Function | mRNA N6-methyladenosine dioxygenase activity | |
Biological Process | mRNA destabilization | |
Biological Process | mRNA processing | |
Biological Process | non-membrane-bounded organelle assembly | |
Biological Process | regulation of mRNA export from nucleus | |
Biological Process | regulation of mRNA processing | |
Biological Process | regulation of translation | |
Biological Process | response to hypoxia | |
Biological Process | spermatogenesis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRNA demethylase ALKBH5
- EC number
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Amphibia > Batrachia > Anura > Pipoidea > Pipidae > Xenopodinae > Xenopus > Silurana
Accessions
- Primary accessionQ66JG8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000239286 | 1-358 | RNA demethylase ALKBH5 | |||
Sequence: MSATYTDLREKLQSLYRDSPKEVRKRKQPTSDTEEEEAASEPEEEEEARKVRSGIRQVRLFSPDECARIEAKIDEVVSRAEKGLYREHTVDRAPLRNKYFFGEGYTYGAQLQRRGPGQERLYPKGEVDEIPAWVNELVIRRLVEHRVIPEGFVNSAVINDYQPGGCIVSHVDPIHIFERPIVSVSFFSDSALCFGCKFQFKPIRVSEPVFFLPVQRGSVTVLSGYAADEITHCIRPQDIKERRAVVILRKTRTEAPRLEMKSLSSSYQPERLQGSNRQHILKPKRSHRKADPDAAHRPRILEMDKEENRRSVLLPKQRRRSHFSSENYWRRSHDYVDTYTETGEDDGSPVRKVKMRRH | ||||||
Disulfide bond | 196↔233 | |||||
Sequence: CKFQFKPIRVSEPVFFLPVQRGSVTVLSGYAADEITHC |
Keywords
- PTM
Proteomic databases
Expression
Gene expression databases
Interaction
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-50 | Disordered | ||||
Sequence: MSATYTDLREKLQSLYRDSPKEVRKRKQPTSDTEEEEAASEPEEEEEARK | ||||||
Compositional bias | 11-34 | Basic and acidic residues | ||||
Sequence: KLQSLYRDSPKEVRKRKQPTSDTE | ||||||
Compositional bias | 259-275 | Polar residues | ||||
Sequence: EMKSLSSSYQPERLQGS | ||||||
Region | 259-312 | Disordered | ||||
Sequence: EMKSLSSSYQPERLQGSNRQHILKPKRSHRKADPDAAHRPRILEMDKEENRRSV | ||||||
Compositional bias | 286-312 | Basic and acidic residues | ||||
Sequence: SHRKADPDAAHRPRILEMDKEENRRSV | ||||||
Compositional bias | 334-352 | Basic and acidic residues | ||||
Sequence: DYVDTYTETGEDDGSPVRK | ||||||
Region | 334-358 | Disordered | ||||
Sequence: DYVDTYTETGEDDGSPVRKVKMRRH |
Domain
The C-terminal disordered region undergoes liquid-liquid phase separation (LLPS) for the formation of paraspeckle membraneless compartment.
Sequence similarities
Belongs to the alkB family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length358
- Mass (Da)41,677
- Last updated2004-10-11 v1
- Checksum69E3D4E37CC629C5
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 11-34 | Basic and acidic residues | ||||
Sequence: KLQSLYRDSPKEVRKRKQPTSDTE | ||||||
Compositional bias | 259-275 | Polar residues | ||||
Sequence: EMKSLSSSYQPERLQGS | ||||||
Compositional bias | 286-312 | Basic and acidic residues | ||||
Sequence: SHRKADPDAAHRPRILEMDKEENRRSV | ||||||
Compositional bias | 334-352 | Basic and acidic residues | ||||
Sequence: DYVDTYTETGEDDGSPVRK |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AAMC01050884 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AAMC01050885 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC080920 EMBL· GenBank· DDBJ | AAH80920.1 EMBL· GenBank· DDBJ | mRNA |