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 P48204
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P48204-F1 | Predicted | AlphaFoldDB |
No variants for P48204
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P48204 | |||||
No associated diseases with P48204
No regional properties for P48204
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for P48204 | |||
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| adenyl-nucleotide exchange factor activity | Binds to and stimulates the hydrolysis and exchange of adenyl nucleotides by other proteins. |
| chaperone binding | Binding to a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport. |
| protein homodimerization activity | Binding to an identical protein to form a homodimer. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| protein folding | The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSKQEKSNVE | DKSLDIETAA | QVETAQESAS | GALEELSVEE | QLERAKDTIK | ELEDSCDQFK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DEALRAKAEM | ENIRKRAERD | VSNARKFGIE | KFAKELLPVI | DSIEQALKHE | VKLEEAIAMK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EGIELTAKML | VDILKKNGVE | ELDPKGEKFD | PNLHEAMAMI | PNPEFEDNTI | FDVFQKGYML |
| 190 | |||||
| NGRIVRAAKV | VIVKN |