| Gene Symbol | PIM1 |
| Aliases | PIM1PROTEIN |
| Function | PIM1 possesses a characteristic kinase domain architecture that distinguishes it from typical serine/threonine kinases. |
| Subcellular Localization | </th><td>Cytoplasm, Nucleus</td></tr> |
| Molecular Weight | 34 kDa |
| GeneCards | PIM1 |
| Human Protein Atlas | PIM1 |
| N-terminal domain | Contains the hinge region connecting the N-lobe and C-lobe of the kinase domain. This region contributes to substrate recognition and binding affinity. |
| Activation loop | Contains key serine/threonine residues that are phosphorylated in other kinases but are constitutively active in PIM1 due to its unique structure. |
| C-terminal domain | Forms the C-lobe of the kinase domain, providing structural stability and substrate positioning. |
| Regulatory domain | No PH domain, SH2 domain, or other regulatory modules found in many signaling kinases |
| Activation segment phosphorylation | The activation loop is not regulated by phosphorylation |
| Autoinhibitory elements | No intramolecular inhibitory interactions |
| Phosphorylation | Can be phosphorylated by other kinases on serine and threonine residues, though its catalytic activity is largely independent of phosphorylation state |
| Ubiquitination | Regulates protein stability and turnover |
| Associated Diseases | Alzheimer's disease, Parkinson's disease |
| Databases | GeneCardsUniProtNCBI GeneHPASTRING |