Q5RHD1 · KDM7A_DANRE
- ProteinLysine-specific demethylase 7A
- Genekdm7a
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids875 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Histone demethylase required for brain development. Specifically demethylates dimethylated 'Lys-9' and 'Lys-27' (H3K9me2 and H3K27me2, respectively) of histone H3 and monomethylated histone H4 'Lys-20' residue (H4K20Me1), thereby playing a central role in histone code (By similarity).
Cofactor
Note: Binds 1 Fe2+ ion per subunit.
Features
Showing features for binding site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Molecular Function | 2-oxoglutarate-dependent dioxygenase activity | |
Molecular Function | histone demethylase activity | |
Molecular Function | histone H3K27me2/H3K27me3 demethylase activity | |
Molecular Function | histone H3K36 demethylase activity | |
Molecular Function | histone H3K9 demethylase activity | |
Molecular Function | histone H4K20 demethylase activity | |
Molecular Function | metal ion binding | |
Molecular Function | transcription coregulator activity | |
Biological Process | midbrain development | |
Biological Process | regulation of transcription by RNA polymerase II |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLysine-specific demethylase 7A
- EC number
- Short namesDrKDM7a
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio
Accessions
- Primary accessionQ5RHD1
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000394249 | 1-875 | Lysine-specific demethylase 7A | |||
Sequence: MAAAPLYCVCRQPYDVNRFMIECDICKDWFHGSCVQVVEHHAADIDVYHCPNCEPIHGPYMMKKHNNWHRHDYTEPNDGTRPVQAGTAVFVKELQARSFASGDILVQMQGNQVTKRFLEKEGFNYPIVVHDLDGLGLKLPPPSFSVSDVEHYVGANKVIDVIDVAKQADSKMKLGEFVKYYYQPERPKVLNVISLEFSDTRMSNLVVVPDIAQKMSWVENYWPDDSFFPKPFVQKYCLMGMKNSYTDFHIDFGGTSVWYHVLWGEKIFYLIKPTKANLALYEAWSSSPNQSEVFFGEKVDKCYKCVVKQGTTILLPTGWIHAVLTSQDSMAFGGNFLHNLNIDMQLRCYEMERRLKTPDLFKFPYFEAICWYVAKNLLETLKELRENKCEAQGFLVNGVKALISSLKMWLRRELTQPNSEVPDNIRPGHLIKALSKEIRHLEDDSNKAVKTQGSAECSLSRSTLEKGDQAQQAARRLQDHHHHRRRHHHHHHHHHHHHHHHHSRKLPSNLDVLELHTLEVLKRLEVGQLKEDSAFSSKVNGKFKKVCPVPAAAVEASHDNALRLVMCNGKIIRERMPITNVAATVNAVEMYHKHRIKLERIPMCPEEKVKKEKCEDEFGVQCTIKKPVSQGESVQTELRTESPHLASSDSDSKAGDSAEKCSLESESSDGEDGGSQRDSGTFVEHLNSHRHSHHKQALKRERPTSPNTDCAIQGMLSMAGLLCPQASGGAADILQQRWWASQGNGSSTSSSSDMWDSSEPCSAPRSPDAEDGSLGEEYSYRESSLSPPLHPSKRHAPNPTPVSNQATKGKRPKKGQATAKQRLGKILKMSRHKGLFLMKPMVFLIPQQGGTPLDPQFLLQSSSICVFPPPLIVSG |
Proteomic databases
Expression
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for zinc finger, domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 5-56 | PHD-type | ||||
Sequence: PLYCVCRQPYDVNRFMIECDICKDWFHGSCVQVVEHHAADIDVYHCPNCEPI | ||||||
Domain | 197-353 | JmjC | ||||
Sequence: FSDTRMSNLVVVPDIAQKMSWVENYWPDDSFFPKPFVQKYCLMGMKNSYTDFHIDFGGTSVWYHVLWGEKIFYLIKPTKANLALYEAWSSSPNQSEVFFGEKVDKCYKCVVKQGTTILLPTGWIHAVLTSQDSMAFGGNFLHNLNIDMQLRCYEMER | ||||||
Region | 442-506 | Disordered | ||||
Sequence: EDDSNKAVKTQGSAECSLSRSTLEKGDQAQQAARRLQDHHHHRRRHHHHHHHHHHHHHHHHSRKL | ||||||
Compositional bias | 450-469 | Polar residues | ||||
Sequence: KTQGSAECSLSRSTLEKGDQ | ||||||
Compositional bias | 477-505 | Basic residues | ||||
Sequence: LQDHHHHRRRHHHHHHHHHHHHHHHHSRK | ||||||
Compositional bias | 629-652 | Polar residues | ||||
Sequence: SQGESVQTELRTESPHLASSDSDS | ||||||
Region | 629-710 | Disordered | ||||
Sequence: SQGESVQTELRTESPHLASSDSDSKAGDSAEKCSLESESSDGEDGGSQRDSGTFVEHLNSHRHSHHKQALKRERPTSPNTDC | ||||||
Compositional bias | 653-673 | Basic and acidic residues | ||||
Sequence: KAGDSAEKCSLESESSDGEDG | ||||||
Compositional bias | 742-759 | Polar residues | ||||
Sequence: QGNGSSTSSSSDMWDSSE | ||||||
Region | 742-820 | Disordered | ||||
Sequence: QGNGSSTSSSSDMWDSSEPCSAPRSPDAEDGSLGEEYSYRESSLSPPLHPSKRHAPNPTPVSNQATKGKRPKKGQATAK | ||||||
Compositional bias | 797-811 | Polar residues | ||||
Sequence: PNPTPVSNQATKGKR |
Domain
The PHD-type zinc finger mediates the binding to H3K4me3. Binding to H3K4me3 prevents its access to H3K9me2 (By similarity).
Sequence similarities
Belongs to the JHDM1 histone demethylase family. JHDM1D subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length875
- Mass (Da)98,827
- Last updated2010-05-18 v2
- ChecksumB257F3649D95AFF4
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2R8RKB3 | A0A2R8RKB3_DANRE | kdm7aa | 837 |
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 182 | in Ref. 2; AAI42783 | ||||
Sequence: Y → H | ||||||
Compositional bias | 450-469 | Polar residues | ||||
Sequence: KTQGSAECSLSRSTLEKGDQ | ||||||
Sequence conflict | 454 | in Ref. 2; AAI42783 | ||||
Sequence: S → R | ||||||
Sequence conflict | 471 | in Ref. 2; AAI42783 | ||||
Sequence: Q → K | ||||||
Compositional bias | 477-505 | Basic residues | ||||
Sequence: LQDHHHHRRRHHHHHHHHHHHHHHHHSRK | ||||||
Sequence conflict | 588 | in Ref. 2; AAI42783 | ||||
Sequence: V → L | ||||||
Sequence conflict | 596 | in Ref. 2; AAI42783 | ||||
Sequence: I → M | ||||||
Compositional bias | 629-652 | Polar residues | ||||
Sequence: SQGESVQTELRTESPHLASSDSDS | ||||||
Compositional bias | 653-673 | Basic and acidic residues | ||||
Sequence: KAGDSAEKCSLESESSDGEDG | ||||||
Compositional bias | 742-759 | Polar residues | ||||
Sequence: QGNGSSTSSSSDMWDSSE | ||||||
Compositional bias | 797-811 | Polar residues | ||||
Sequence: PNPTPVSNQATKGKR |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BX537168 EMBL· GenBank· DDBJ | CAI12074.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
BC142782 EMBL· GenBank· DDBJ | AAI42783.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. |