B5XF11
Gene name |
kdm8 (jmjd5) |
Protein name |
Lysine-specific demethylase 8 |
Names |
JmjC domain-containing protein 5, Jumonji domain-containing protein 5 |
Species |
Salmo salar (Atlantic salmon) |
KEGG Pathway |
|
EC number |
1.14.11.27: With 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors |
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 B5XF11
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B5XF11-F1 | Predicted | AlphaFoldDB |
No variants for B5XF11
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B5XF11 | |||||
No associated diseases with B5XF11
Functions
| Description | ||
|---|---|---|
| EC Number | 1.14.11.27 | With 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| 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. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| chromatin binding | Binding to chromatin, the network of fibers of DNA, protein, and sometimes RNA, that make up the chromosomes of the eukaryotic nucleus during interphase. |
| histone H3-di/monomethyl-lysine-36 demethylase activity | Catalysis of the removal of a methyl group from a di- or a monomethyl-lysine residue at position 36 of the histone H3 protein. This is a dioxygenase reaction that is dependent on Fe(II) and 2-oxoglutarate. |
| histone H3-methyl-lysine-36 demethylase activity | Catalysis of the removal of a methyl group from a modified lysine residue at position 36 of the histone H3 protein. This is a dioxygenase reaction that is dependent on Fe(II) and 2-oxoglutarate. |
| metal ion binding | Binding to a metal ion. |
5 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. |
| circadian regulation of gene expression | Any process that modulates the frequency, rate or extent of gene expression such that an expression pattern recurs with a regularity of approximately 24 hours. |
| G2/M transition of mitotic cell cycle | The mitotic cell cycle transition by which a cell in G2 commits to M phase. The process begins when the kinase activity of M cyclin/CDK complex reaches a threshold high enough for the cell cycle to proceed. This is accomplished by activating a positive feedback loop that results in the accumulation of unphosphorylated and active M cyclin/CDK complex. |
| histone H3-K36 demethylation | The modification of histone H3 by the removal of a methyl group from lysine at position 36 of the histone. |
| positive regulation of DNA-templated transcription | Any process that activates or increases the frequency, rate or extent of cellular DNA-templated transcription. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAELWSAISA | ALPVTEAEFP | LDFSEKVEPS | VVDVLKRCRQ | QLYTGSGRWR | QNAQIILDFS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| WEKLNTGTWR | DVDKEWRCLY | SYGCLFKVAA | LCRDDASPAT | VQEAIRTCDL | GLLMGAAIMD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NILQTFVKIL | QNEIRKRHSN | EENLSEGVSA | KKMKVDCVSV | PVVKQALAVP | RIHCPSLESF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KKDYLDPQKP | VILEGIIDHW | PAFKNHPWSI | EYLQTVAGCR | TVPVEVGSRY | TDEEWSQTLL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TVNEFIDRYI | VVKDASSLGY | LAQHQLFDQV | PELKDDIRIP | DYCCLGEGEE | DDITINAWFG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PGGTVSPLHQ | DPQQNFLAQV | VGRKYIRLYS | PEDTEKLYPH | QLQLLHNTSQ | VEVESPDVVR |
| 370 | 380 | 390 | 400 | ||
| FPEFVKAPYL | ECVLQPGEVL | FIPVKHWHYV | RSLELSFSVS | FWWS |