| Gene |
SETMAR
|
| Protein Name |
SETMR_HUMAN |
| Organism |
Homo sapiens (Human) |
| Alternative name(s) |
Histone-lysine N-methyltransferase SETMAR (SET domain and mariner transposase fusion protein) (Metnase) [Includes: Histone-lysine N-methyltransferase (EC 2.1.1.43); Transposon Hsmar1 transposase (EC 3.1.-.-)] |
| Protein Family |
Class V-like SAM-binding methyltransferase superfamily; Mariner transposase family |
| NCBI Gene ID |
6419
|
| UniProt ID |
Q53H47
|
| Enzyme Class |
2.1.1.43; 3.1.-.- |
| Molecular Weight |
78034 |
| Protein Length |
684 |
| Protein Domain |
InterPro |
Pfam
|
| 3D Structure |
PDBe |
PDBj |
RCSB PDB |
DrugPort
ModBase |
SwissModel
|
| Gene Expression |
Gene Expression Atlas
|
| Function and Disease |
OMIM |
| Protein-protein Interaction Database |
STRING |
IntAct |
MINT
|
| Kinase Database |
Phospho.ELM
|
PhosphoSite
| NetworKIN
|
| Catalytic Activity (UniProt annotation) |
S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]. |
| Localization |
Nucleus |
| Function (UniProt annotation) |
Protein derived from the fusion of a methylase with the transposase of an Hsmar1 transposon that plays a role in DNA double-strand break repair, stalled replication fork restart and DNA integration. DNA-binding protein, it is indirectly recruited to sites of DNA damage through protein-protein interactions. Has also kept a sequence-specific DNA-binding activity recognizing the 19-mer core of the 5'-terminal inverted repeats (TIRs) of the Hsmar1 element and displays a DNA nicking and end joining activity (PubMed:16332963, PubMed:16672366, PubMed:17877369, PubMed:17403897, PubMed:18263876, PubMed:22231448, PubMed:24573677, PubMed:20521842). In parallel, has a histone methyltransferase activity and methylates 'Lys-4' and 'Lys-36' of histone H3. Specifically mediates dimethylation of H3 'Lys-36' at sites of DNA double-strand break and may recruit proteins required for efficient DSB repair through non-homologous end-joining (PubMed:16332963, PubMed:21187428, PubMed:22231448). Also regulates replication fork processing, promoting replication fork restart and regulating DNA decatenation through stimulation of the topoisomerase activity of TOP2A (PubMed:18790802, PubMed:20457750). |
| Gene Ontology |
GO:0000014; GO:0000729; GO:0000737; GO:0003677; GO:0003690; GO:0003697; GO:0004519; GO:0005634; GO:0005730; GO:0006303; GO:0008270; GO:0008283; GO:0010452; GO:0015074; GO:0031297; GO:0035861; GO:0042800; GO:0042803; GO:0044547; GO:0044774; GO:0046975; GO:0051568; GO:0071157; GO:0090305; GO:0097676; GO:2000373; GO:2001034; GO:2001251 |
