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 Q5BJR4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5BJR4-F1 | Predicted | AlphaFoldDB |
No variants for Q5BJR4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5BJR4 | |||||
No associated diseases with Q5BJR4
1 regional properties for Q5BJR4
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | CRAL-TRIO lipid binding domain | 130 - 291 | IPR001251 |
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. |
No GO annotations of molecular function
| Name | Definition |
|---|---|
| No GO annotations for molecular function |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| apoptotic process | A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MDIHFEEGVL | SPSATDMRPE | PPNSLDLNGS | HPRRIKLTAP | NINLSLDQSE | GSILSDDNLD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SPDEIDINVD | ELDTPDEADS | FEYPGHEDPM | ANRSSGQESE | SIPEYTAEEE | REDNRLWRTV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VIGEQEQRID | MKVIEPYRRV | ISHGGYYGDG | LNAIIVFAAC | FLPDSSRADY | HYVMENLFLY |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VISTLELMVA | EDYMIVYLNG | ATPRRKMPGL | GWMKKCYQMI | DRRLRKNLKS | FIIVHPSWFI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RTILAVTRPF | ISSKFSSKIK | YVSSLSELSG | LIPMDCIHIP | ESIIKYDEEK | SFKRSVRTSC |
| 310 | 320 | ||||
| LYNDPEMTSM | EKDIDMKLKE | KP |