Descriptions
HSPA8 (or hsc70) is a heat shock cognate protein involved in many cellular processes. During recovery from stress, HSPA8, initially accumulating in the nucleoplasm for folding/refolding of proteins, transiently concentrates in nucleoli for nucleolar morphology and function restoration. The inhibitory region is positioned at one of the three domains of HSPA8 protein, which is the N-terminal ATPase domain, specifically in residues 263-287 of domain IIB. Under normal growth conditions, the constitutive nucleolar targeting function that is provided by residues 225-262 is diminished by the autoinhibitory element located in residues 263-287. When cells recover from stress, the autoinhibitory element is inactivated, and the constitutive nucleolar targeting function restores.
Autoinhibitory domains (AIDs)
Target domain |
227-264 (Nucleolar targeting region) |
Relief mechanism |
Others |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for P48741
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P48741-F1 | Predicted | AlphaFoldDB |
No variants for P48741
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P48741 | |||||
No associated diseases with P48741
2 regional properties for P48741
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Heat shock protein 70, conserved site | 11 - 18 | IPR018181-1 |
| conserved_site | Heat shock protein 70, conserved site | 199 - 212 | IPR018181-2 |
6 GO annotations of cellular component
| Name | Definition |
|---|---|
| blood microparticle | A phospholipid microvesicle that is derived from any of several cell types, such as platelets, blood cells, endothelial cells, or others, and contains membrane receptors as well as other proteins characteristic of the parental cell. Microparticles are heterogeneous in size, and are characterized as microvesicles free of nucleic acids. |
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| extracellular exosome | A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
6 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-dependent protein folding chaperone | Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis. |
| heat shock protein binding | Binding to a heat shock protein, a protein synthesized or activated in response to heat shock. |
| protein folding chaperone | Binding to a protein or a protein-containing complex to assist the protein folding process. |
| ubiquitin protein ligase binding | Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| chaperone cofactor-dependent protein refolding | The process of assisting in the correct posttranslational noncovalent assembly of proteins, which is dependent on additional protein cofactors. This process occurs over one or several cycles of nucleotide hydrolysis-dependent binding and release. |
| protein refolding | The process carried out by a cell that restores the biological activity of an unfolded or misfolded protein, using helper proteins such as chaperones. |
19 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P77319 | hscC | Chaperone protein HscC | Escherichia coli (strain K12) | PR |
| P0A6Y8 | dnaK | Chaperone protein DnaK | Escherichia coli (strain K12) | SS |
| P11146 | Hsc70-2 | Heat shock 70 kDa protein cognate 2 | Drosophila melanogaster (Fruit fly) | SS |
| Q8INI8 | Hsp70Ba | Major heat shock 70 kDa protein Ba | Drosophila melanogaster (Fruit fly) | SS |
| Q9VG58 | Hsp70Bbb | Major heat shock 70 kDa protein Bbb | Drosophila melanogaster (Fruit fly) | SS |
| P02825 | Hsp70Ab | Major heat shock 70 kDa protein Ab | Drosophila melanogaster (Fruit fly) | SS |
| Q9BIR7 | Hsp70Bc | Major heat shock 70 kDa protein Bc | Drosophila melanogaster (Fruit fly) | SS |
| P82910 | Hsp70Aa | Major heat shock 70 kDa protein Aa | Drosophila melanogaster (Fruit fly) | SS |
| Q9BIS2 | Hsp70Bb | Major heat shock 70 kDa protein Bb | Drosophila melanogaster (Fruit fly) | SS |
| O97125 | Hsp68 | Heat shock protein 68 | Drosophila melanogaster (Fruit fly) | SS |
| Q0VDF9 | HSPA14 | Heat shock 70 kDa protein 14 | Homo sapiens (Human) | SS |
| P54652 | HSPA2 | Heat shock-related 70 kDa protein 2 | Homo sapiens (Human) | SS |
| P11142 | HSPA8 | Heat shock cognate 71 kDa protein | Homo sapiens (Human) | EV |
| P38646 | HSPA9 | Stress-70 protein, mitochondrial | Homo sapiens (Human) | SS |
| P11021 | HSPA5 | Endoplasmic reticulum chaperone BiP | Homo sapiens (Human) | SS |
| P34931 | HSPA1L | Heat shock 70 kDa protein 1-like | Homo sapiens (Human) | SS |
| P17066 | HSPA6 | Heat shock 70 kDa protein 6 | Homo sapiens (Human) | SS |
| P0DMV8 | HSPA1A | Heat shock 70 kDa protein 1A | Homo sapiens (Human) | SS |
| P0DMV9 | HSPA1B | Heat shock 70 kDa protein 1B | Homo sapiens (Human) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MQAPRELAVG | IDLGTTYSCV | GVFQQGRVEI | LANDQGNRTT | PSYVAFTDTE | RLVGDAAKSQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AALNPHNTVF | DAKRLIGRKF | ADTTVQSDMK | HWPFQVVSEG | GKPKVRVCYR | GEDKTFYPEE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ISSMVLSKMK | ETAEAYLGQP | VKHAVITVPT | YFSNSQRQAT | KDAGAIAGLK | VLPIINEATA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AAIAYGLDRR | GAGKRNVLIF | DLGGGTFDVS | VLSIDAGVFE | VKATAGDTHL | GGEDFDNRLV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NHFMEEFRRK | HGKDLSGNKR | ALRRLRTACE | RAKRTPSSST | QATLEIDSLF | EGVDFYKSIT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| RARFEELCSD | LFRSTLEPVE | KALRDAKLDK | AQIHDFVLGG | GLHSHPQGAE | VAAGLLQRQG |
| AEQEHQP |