P48558
Gene name |
BXI1 (YBH3, YNL305C, N0405) |
Protein name |
Bax inhibitor 1 |
Names |
BH3 domain-containing protein BXI1 |
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YNL305C |
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 P48558
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P48558-F1 | Predicted | AlphaFoldDB |
2 variants for P48558
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s14-59727 | 22 | S>N | No | SGRP | |
| s14-59530 | 88 | L>I | No | SGRP |
No associated diseases with P48558
No regional properties for P48558
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for P48558 | |||
Functions
8 GO annotations of cellular component
| Name | Definition |
|---|---|
| endoplasmic reticulum | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). |
| endoplasmic reticulum membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
| fungal-type vacuole | A vacuole that has both lytic and storage functions. The fungal vacuole is a large, membrane-bounded organelle that functions as a reservoir for the storage of small molecules (including polyphosphate, amino acids, several divalent cations (e.g. calcium), other ions, and other small molecules) as well as being the primary compartment for degradation. It is an acidic compartment, containing an ensemble of acid hydrolases. At least in S. cerevisiae, there are indications that the morphology of the vacuole is variable and correlated with the cell cycle, with logarithmically growing cells having a multilobed, reticulated vacuole, while stationary phase cells contain a single large structure. |
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
| membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
| mitochondrial membrane | Either of the lipid bilayers that surround the mitochondrion and form the mitochondrial envelope. |
| mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
| vacuolar membrane | The lipid bilayer surrounding the vacuole and separating its contents from the cytoplasm of the cell. |
No GO annotations of molecular function
| Name | Definition |
|---|---|
| No GO annotations for molecular function |
3 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. |
| calcium-mediated signaling | Any intracellular signal transduction in which the signal is passed on within the cell via calcium ions. |
| endoplasmic reticulum unfolded protein response | The series of molecular signals generated as a consequence of the presence of unfolded proteins in the endoplasmic reticulum (ER) or other ER-related stress; results in changes in the regulation of transcription and translation. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSGPPPPYEE | QSSHLYGQPA | SSQDGNAFIP | EDFKYSTVVI | SCEPIIRQRF | MHKVYSLLSC |
| 70 | 80 | 90 | 100 | 110 | 120 |
| QLLASLSFCY | WASVSTSLQN | FIMSHIALFY | ICMVVSLVSC | IWLAVSPRPE | DYEASVPEPL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LTGSSEEPAQ | EQRRLPWYVL | SSYKQKLTLL | SIFTLSEAYC | LSLVTLAYDK | DTVLSALLIT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| TIVVVGVSLT | ALSERFENVL | NSATSIYYWL | NWGLWIMIGM | GLTALLFGWN | THSSKFNLLY |
| 250 | 260 | 270 | 280 | 290 | |
| GWLGAILFTA | YLFIDTQLIF | RKVYPDEEVR | CAMMLYLDIV | NLFLSILRIL | ANSNDDN |