Q0J4P2
Gene name |
HSP81-1 (HSP82) |
Protein name |
Heat shock protein 81-1 |
Names |
HSP81-1, Heat shock protein 82 |
Species |
Oryza sativa subsp japonica (Rice) |
KEGG Pathway |
osa:4345951 |
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 Q0J4P2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q0J4P2-F1 | Predicted | AlphaFoldDB |
No variants for Q0J4P2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q0J4P2 | |||||
No associated diseases with Q0J4P2
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| perinuclear region of cytoplasm | Cytoplasm situated near, or occurring around, the nucleus. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
| protein-containing complex | A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together. |
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. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| cellular response to heat | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a heat stimulus, a temperature stimulus above the optimal temperature for that organism. |
| protein folding | The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure. |
| protein stabilization | Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation. |
5 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P15108 | HSC82 | ATP-dependent molecular chaperone HSC82 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | PR |
| P51818 | HSP90-3 | Heat shock protein 90-3 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| O03986 | HSP90-4 | Heat shock protein 90-4 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| P55737 | HSP90-2 | Heat shock protein 90-2 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| P36181 | HSC80 | Heat shock cognate protein 80 | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MASETETFAF | QAEINQLLSL | IINTFYSNKE | IFLRELISNS | SDALDKIRFE | SLTDKSKLDA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| QPELFIHIVP | DKASNTLSII | DSGIGMTKSD | LVNNLGTIAR | SGTKEFMEAL | AAGADVSMIG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| QFGVGFYSAY | LVAERVVVTT | KHNDDEQYVW | ESQAGGSFTV | TRDTSGEQLG | RGTKITLYLK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DDQLEYLEER | RLKDLIKKHS | EFISYPISLW | TEKTTEKEIS | DDEDEEEKKD | AEEGKVEDVD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EEKEEKEKKK | KKIKEVSHEW | SLVNKQKPIW | MRKPEEITKE | EYAAFYKSLT | NDWEEHLAVK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| HFSVEGQLEF | KAVLFVPKRA | PFDLFDTRKK | LNNIKLYVRR | VFIMDNCEEL | IPEWLSFVKG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| IVDSEDLPLN | ISREMLQQNK | ILKVIRKNLV | KKCVELFFEI | AENKEDYNKF | YEAFSKNLKL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| GIHEDSTNRN | KIAELLRYHS | TKSGDELTSL | KDYVTRMKEG | QNDIYYITGE | SKKAVENSPF |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LEKLKKKGYE | VLYMVDAIDE | YAVGQLKEFE | GKKLVSATKE | GLKLDESEDE | KKRKEELKEK |
| 550 | 560 | 570 | 580 | 590 | 600 |
| FEGLCKVIKE | VLGDKVEKVV | VSDRVVDSPC | CLVTGEYGWT | ANMERIMKAQ | ALRDSSMAGY |
| 610 | 620 | 630 | 640 | 650 | 660 |
| MSSKKTMEIN | PENAIMEELR | KRADADKNDK | SVKDLVLLLF | ETALLTSGFS | LDDPNTFGSR |
| 670 | 680 | 690 | |||
| IHRMLKLGLS | IDEDETAEAD | TDMPPLEDDA | GESKMEEVD |