Q0VD24
Gene name |
SETMAR |
Protein name |
Histone-lysine N-methyltransferase SETMAR |
Names |
SET domain and mariner transposase fusion protein homolog |
Species |
Bos taurus (Bovine) |
KEGG Pathway |
bta:511299 |
EC number |
2.1.1.357: Methyltransferases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q0VD24
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q0VD24-F1 | Predicted | AlphaFoldDB |
27 variants for Q0VD24
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs453816009 | 2 | A>E | No | EVA | |
| rs471618573 | 7 | V>G | No | EVA | |
| rs437905711 | 11 | L>S | No | EVA | |
| rs469086474 | 13 | G>A | No | EVA | |
| rs449230925 | 20 | G>V | No | EVA | |
| rs435569342 | 21 | L>I | No | EVA | |
| rs466900695 | 21 | L>P | No | EVA | |
| rs446941713 | 22 | E>Q | No | EVA | |
| rs458385631 | 24 | L>R | No | EVA | |
| rs451112701 | 25 | P>H | No | EVA | |
| rs482550980 | 32 | G>R | No | EVA | |
| rs442316472 | 34 | E>D | No | EVA | |
| rs460060264 | 39 | Q>H | No | EVA | |
| rs473833237 | 39 | Q>K | No | EVA | |
| rs448098726 | 50 | A>E | No | EVA | |
| rs133874747 | 52 | A>T | No | EVA | |
| rs445841352 | 53 | D>E | No | EVA | |
| rs801039369 | 78 | R>H | No | EVA | |
| rs443516218 | 88 | C>* | No | EVA | |
| rs463668535 | 88 | C>S | No | EVA | |
| rs517089473 | 92 | I>T | No | EVA | |
| rs135249241 | 99 | T>A | No | EVA | |
| rs876269878 | 119 | V>G | No | EVA | |
| rs876162327 | 122 | W>G | No | EVA | |
| rs441332037 | 159 | V>A | No | EVA | |
| rs447508360 | 227 | M>I | No | EVA | |
| rs382744157 | 300 | T>M | No | EVA |
No associated diseases with Q0VD24
Functions
| Description | ||
|---|---|---|
| EC Number | 2.1.1.357 | Methyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| chromosome | A structure composed of a very long molecule of DNA and associated proteins (e.g. histones) that carries hereditary information. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| double-stranded DNA binding | Binding to double-stranded DNA. |
| histone methyltransferase activity | Catalysis of the reaction: S-adenosyl-L-methionine + histone = S-adenosyl-L-homocysteine + methyl-histone. Histone methylation generally occurs on either an arginine or lysine residue. |
| histone methyltransferase activity (H3-K36 specific) | Catalysis of the reaction: S-adenosyl-L-methionine + histone H3 L-lysine (position 36) = S-adenosyl-L-homocysteine + histone H3 N6-methyl-L-lysine (position 36). This reaction is the addition of a methyl group onto lysine at position 36 of the histone H3 protein. |
| histone methyltransferase activity (H3-K4 specific) | Catalysis of the reaction: S-adenosyl-L-methionine + histone H3 L-lysine (position 4) = S-adenosyl-L-homocysteine + histone H3 N6-methyl-L-lysine (position 4). This reaction is the addition of a methyl group onto lysine at position 4 of the histone H3 protein. |
| zinc ion binding | Binding to a zinc ion (Zn). |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| chromatin organization | The assembly or remodeling of chromatin composed of DNA complexed with histones, other associated proteins, and sometimes RNA. |
| histone H3-K36 methylation | The modification of histone H3 by addition of one or more methyl groups to lysine at position 36 of the histone. |
| histone H3-K4 methylation | The modification of histone H3 by addition of one or more methyl groups to lysine at position 4 of the histone. |
| histone methylation | The modification of histones by addition of methyl groups. |
2 homologous proteins in AiPD
| 10 | 20 | 30 | 40 | 50 | 60 |
| MATCEEVPEA | LKGQLDVARG | LENLPVSAWP | PGAEPEPFQY | TPDHVAGPGA | DADPSQITFP |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GCACLKTPCL | PGTCSCLRHE | NNYDDRSCLR | DIGSEAKCTE | PVFECNVLCQ | CSERCRNRVV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| QWGLQFHLQV | FKTDHKGWGL | RTLDFIPKGR | FVCEYAGEVL | GISEVQRRVQ | LQTIHDSNYI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IAIREHVYNG | QVMETFVDPA | SIGNIGRFLN | HSCEPNLLMI | PVRIDSMVPK | LALFAARDIL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PEEELSYDYS | GRFLNLMHSE | DKERLDNGKL | RKPCYCGARS | CAAFLPYDSS | LYCPTEKPDT |
| SEEGRA |