Q9VD28
Gene name |
PSR (CG5383) |
Protein name |
Bifunctional arginine demethylase and lysyl-hydroxylase PSR |
Names |
|
Species |
Drosophila melanogaster (Fruit fly) |
KEGG Pathway |
dme:Dmel_CG5383 |
EC number |
|
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 Q9VD28
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9VD28-F1 | Predicted | AlphaFoldDB |
No variants for Q9VD28
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9VD28 | |||||
No associated diseases with Q9VD28
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| 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 |
|---|---|
| histone H3-methyl-arginine-2 demethylase activity | Catalysis of the removal of the methyl group from a modified arginine residue at position 2 of the histone H3 protein. This is a dioxygenase reaction that is dependent on Fe(II) and 2-oxoglutarate. |
| histone H3-methyl-arginine-3 demethylase activity | Catalysis of the removal of the methyl group from a modified arginine residue at position 3 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. |
| P-TEFb complex binding | Binding to a P-TEFb complex. |
| peptidyl-lysine 5-dioxygenase activity | Catalysis of the reaction: protein L-lysine + 2-oxoglutarate + O2 = protein 5-hydroxy-L-lysine + succinate + CO2. |
6 GO annotations of biological process
| Name | Definition |
|---|---|
| cell competition in a multicellular organism | Competitive interactions within multicellular organisms between cell populations that differ in growth rates, leading to the elimination of the slowest-growing cells. |
| chromatin organization | The assembly or remodeling of chromatin composed of DNA complexed with histones, other associated proteins, and sometimes RNA. |
| negative regulation of apoptotic process | Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process. |
| negative regulation of JNK cascade | Any process that stops, prevents, or reduces the frequency, rate or extent of signal transduction mediated by the JNK cascade. |
| peptidyl-lysine hydroxylation to 5-hydroxy-L-lysine | The hydroxylation of peptidyl-lysine to peptidyl-5-hydroxy-L-lysine. |
| phagocytosis | A vesicle-mediated transport process that results in the engulfment of external particulate material by phagocytes and their delivery to the lysosome. The particles are initially contained within phagocytic vacuoles (phagosomes), which then fuse with primary lysosomes to effect digestion of the particles. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSEEFKLPKR | SRKRTREVKR | KARPELDGEN | AWSAMRYCEK | FEPFWDFTDN | LERIEESQVP |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ESEFIERFER | PYKPVVIRGC | TDGWLALEKW | TLARLAKKYR | NQKFKCGEDN | EGYSVKMKMK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| YYVEYMQSTR | DDSPLYIFDS | SFGEHHRRRK | LLDDYVVPKY | FRDDLFQYCG | ENRRPPYRWF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VMGPARSGTG | IHIDPLGTSA | WNTLIRGHKR | WCLFPTQTPK | ELLKVTSAMG | GKQRDEAITW |
| 250 | 260 | 270 | 280 | 290 | 300 |
| FSTIYPRTQL | PSWPEQYRPI | EVLQGAGETV | FVPGGWWHVV | LNMDDTIAIT | QNFSSQTNFP |
| 310 | 320 | 330 | 340 | 350 | 360 |
| CVWHKTVRGR | PKLSRKWLRV | LRDQRPELAQ | IADSINLNES | TGFASDSSSN | SSSSSSSSSS |
| 370 | 380 | 390 | 400 | ||
| SSEEEESDDG | GDSNTDSGQE | SLTAKKKKKR | RMAGGGSGSG | SMGGSSRS |