Q9NKX1
Gene name |
grp94 (DDB_G0280057) |
Protein name |
Endoplasmin homolog |
Names |
92 kDa phosphoprotein, Glucose-regulated protein 94 homolog, GRP-94 homolog |
Species |
Dictyostelium discoideum (Slime mold) |
KEGG Pathway |
ddi:DDB_G0280057 |
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 Q9NKX1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9NKX1-F1 | Predicted | AlphaFoldDB |
No variants for Q9NKX1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9NKX1 | |||||
No associated diseases with Q9NKX1
Functions
4 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). |
| Golgi apparatus | A membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways. |
| Golgi-associated vesicle | Any vesicle associated with the Golgi complex and involved in mediating transport within the Golgi or between the Golgi and other parts of the cell. |
| perinuclear region of cytoplasm | Cytoplasm situated near, or occurring around, the nucleus. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ATP hydrolysis activity | Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. |
| ATP-dependent protein folding chaperone | Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis. |
| unfolded protein binding | Binding to an unfolded protein. |
2 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. |
| ubiquitin-dependent ERAD pathway | The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKSITKIFLI | LGLFAFLLVA | FAPSSSVATV | NLESDGYTEA | EAKLIEEKGE | KFTFQTEVNK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LMNIIINSLY | SKKEIFLREL | ISNASDALDK | IRFLALTNAD | LLGEGEQSNL | DIHIKIDKAN |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NVLHITDRGV | GMTKDELVRN | LGTIAQSGTK | EFIKKVSDSA | ESSNLIGQFG | VGFYSLFLVA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DSVVVTSKSN | DDDQYVWTSD | SQSSYTIAKD | PKGNTLGRGT | RISLHIKDDS | KEFLDQEVIK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| QLVKKYSQFI | NFPIYLYVSE | EVEIPKEEQE | DSKPITDDQV | EETTTTTEEG | EEETTTEEEG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| QTEEKKTKTV | YKWEELNDSK | PLWMKAAKDV | TKEEYTEFFR | SLSKTQDTPI | TYSHFKTEGD |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TEFRSILYIP | ENPPSNMFDL | EAAGSGLKLF | VRRVFITDNL | KELVPNWLRF | LVGVIDSDDL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| PLNVSREMLQ | QNKILDAIKK | KVILVKFISM | IKELSEDEDK | TKYNEFFKKF | GSSMKLGAIE |
| 490 | 500 | 510 | 520 | 530 | 540 |
| DQANKKRLTK | YLLFPSSKEE | LTTFAGYVER | MKEGQDQIYF | ITGKSKDSVE | ASPLIEQAIK |
| 550 | 560 | 570 | 580 | 590 | 600 |
| KGYEVLFLVD | PIDEYLVPQL | DKFDDKYKFT | NLARSGVKFN | EDKEEEDQRK | QTAEEFKPLL |
| 610 | 620 | 630 | 640 | 650 | 660 |
| SYLKKTLSDK | LEKVVISKVL | ADSPSILVSN | SWGVTANQER | IMKAQAHQAN | AQPQFNSKKI |
| 670 | 680 | 690 | 700 | 710 | 720 |
| MEINPSHPLI | KKLLNRLNEF | GEEDETTKVS | AHVLYETSAL | TAGYSIDNPT | NFADFIYKLM |
| 730 | 740 | 750 | 760 | ||
| MINGDSLAQT | NFETTKNENS | GPSVSFGDDD | ENQQQDFQQP | PQSTHDEL |