Q8VHL1 · SETD7_MOUSE
- ProteinHistone-lysine N-methyltransferase SETD7
- GeneSetd7
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids366 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3 (By similarity).
H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation (By similarity).
Plays a central role in the transcriptional activation of genes such as collagenase or insulin (PubMed:12711597).
Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription (By similarity).
Has also methyltransferase activity toward non-histone proteins such as CGAS, p53/TP53, TAF10, and possibly TAF7 by recognizing and binding the [KR]-[STA]-K in substrate proteins (PubMed:35210392).
Monomethylates 'Lys-189' of TAF10, leading to increase the affinity of TAF10 for RNA polymerase II (By similarity).
Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and increasing p53/TP53-mediated transcriptional activation (By similarity).
Monomethylates 'Lys-491' of CGAS, promoting interaction between SGF29 and CGAS (PubMed:35210392).
H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation (By similarity).
Plays a central role in the transcriptional activation of genes such as collagenase or insulin (PubMed:12711597).
Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription (By similarity).
Has also methyltransferase activity toward non-histone proteins such as CGAS, p53/TP53, TAF10, and possibly TAF7 by recognizing and binding the [KR]-[STA]-K in substrate proteins (PubMed:35210392).
Monomethylates 'Lys-189' of TAF10, leading to increase the affinity of TAF10 for RNA polymerase II (By similarity).
Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and increasing p53/TP53-mediated transcriptional activation (By similarity).
Monomethylates 'Lys-491' of CGAS, promoting interaction between SGF29 and CGAS (PubMed:35210392).
Catalytic activity
- L-lysyl4-[histone H3] + S-adenosyl-L-methionine = H+ + N6-methyl-L-lysyl4-[histone H3] + S-adenosyl-L-homocysteine
- L-lysyl-[protein] + S-adenosyl-L-methionine = H+ + N6-methyl-L-lysyl-[protein] + S-adenosyl-L-homocysteineThis reaction proceeds in the forward direction.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 226-228 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: AGE | ||||||
Site | 245 | Histone H3K4 binding | ||||
Sequence: Y | ||||||
Site | 256 | Histone H3K4 binding | ||||
Sequence: D | ||||||
Site | 266 | Histone H3K4 binding | ||||
Sequence: T | ||||||
Binding site | 296 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 297 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Site | 317 | Histone H3K4 binding | ||||
Sequence: K | ||||||
Site | 335 | Histone H3K4 binding | ||||
Sequence: Y | ||||||
Binding site | 356 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chromosome | |
Cellular Component | nucleolus | |
Cellular Component | nucleus | |
Molecular Function | chromatin binding | |
Molecular Function | histone H3K4 monomethyltransferase activity | |
Molecular Function | histone methyltransferase activity | |
Molecular Function | p53 binding | |
Molecular Function | protein-lysine N-methyltransferase activity | |
Biological Process | chromatin organization | |
Biological Process | DNA damage response | |
Biological Process | heterochromatin organization | |
Biological Process | peptidyl-lysine dimethylation | |
Biological Process | peptidyl-lysine monomethylation | |
Biological Process | positive regulation of DNA-templated transcription | |
Biological Process | response to ethanol |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHistone-lysine N-methyltransferase SETD7
- EC number
- Alternative names
Gene names
- Community suggested namesSet7
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ8VHL1
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 297 | Abolishes methyltransferase activity. | ||||
Sequence: H → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 16 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000186055 | 1-366 | Histone-lysine N-methyltransferase SETD7 | |||
Sequence: MDSDDEVVEEAVEGHLDDDGLPHGFCTVTYSSTDRFEGNFVHGEKNGRGKFFFFDGSTLEGYYVDDALQGQGVYTYEDGGVLQGTYVDGELNGPAQEYDSDGRLIFKGQYKDNNRHGVCWIHYPDGGSLVGEVNEDGEMTGEKIAYVYPDQRTALYGKFIDGEMLEGKLATLMATEEGRPHFEVTSGSSVYHFDKSTSSCISSDALLPDPYESERVYVADSLISSAGEGLFSKVAVGPNTVMSFYNGVRITHQEVDSRDWALNGNTLSLDEETVIDVPEPYNHVSKYCASLGHKANHSFTPNCVYDLFVHPRFGPIKCIRTLRAVEAEEELTVAYGYDHSPPGKSGPEAPEWYQVELKAFQATQQK |
Proteomic databases
PTM databases
Expression
Developmental stage
Expressed during all pre-implementation stages in both male and female embryos.
Gene expression databases
Structure
Family & Domains
Features
Showing features for repeat, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 36-58 | MORN 1 | ||||
Sequence: FEGNFVHGEKNGRGKFFFFDGST | ||||||
Repeat | 59-81 | MORN 2 | ||||
Sequence: LEGYYVDDALQGQGVYTYEDGGV | ||||||
Repeat | 106-128 | MORN 3 | ||||
Sequence: FKGQYKDNNRHGVCWIHYPDGGS | ||||||
Domain | 214-336 | SET | ||||
Sequence: ERVYVADSLISSAGEGLFSKVAVGPNTVMSFYNGVRITHQEVDSRDWALNGNTLSLDEETVIDVPEPYNHVSKYCASLGHKANHSFTPNCVYDLFVHPRFGPIKCIRTLRAVEAEEELTVAYG |
Domain
The SET domain is necessary but not sufficient for histone methyltransferase activity.
Sequence similarities
Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SET7 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length366
- Mass (Da)40,506
- Last updated2008-02-05 v2
- ChecksumC826EAFCB4B9D345
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 77 | in Ref. 4; AAH50190 | ||||
Sequence: E → V | ||||||
Sequence conflict | 165 | in Ref. 1; AAL56578 | ||||
Sequence: L → I |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF448509 EMBL· GenBank· DDBJ | AAL56578.1 EMBL· GenBank· DDBJ | mRNA | ||
AK129428 EMBL· GenBank· DDBJ | BAC98238.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK048924 EMBL· GenBank· DDBJ | BAC33493.1 EMBL· GenBank· DDBJ | mRNA | ||
AK147422 EMBL· GenBank· DDBJ | BAE27903.1 EMBL· GenBank· DDBJ | mRNA | ||
AK147413 EMBL· GenBank· DDBJ | BAE27897.1 EMBL· GenBank· DDBJ | mRNA | ||
AK147667 EMBL· GenBank· DDBJ | BAE28059.1 EMBL· GenBank· DDBJ | mRNA | ||
AK170161 EMBL· GenBank· DDBJ | BAE41607.1 EMBL· GenBank· DDBJ | mRNA | ||
BC050190 EMBL· GenBank· DDBJ | AAH50190.1 EMBL· GenBank· DDBJ | mRNA |