P09435
SS
Gene name |
SSA3 (YBL075C, YBL06.07, YBL0610) |
Protein name |
Heat shock protein SSA3 |
Names |
|
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YBL075C |
EC number |
|
Protein Class |
|
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 |
223-260 (Nucleolar targeting region) |
Relief mechanism |
Others |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for P09435
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P09435-F1 | Predicted | AlphaFoldDB |
3 variants for P09435
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s02-86388 | 20 | S>F | No | SGRP | |
| s02-84588 | 620 | G>A | No | SGRP | |
| s02-84530 | 639 | E>D | No | SGRP |
No associated diseases with P09435
3 regional properties for P09435
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Heat shock protein 70, conserved site | 7 - 14 | IPR018181-1 |
| conserved_site | Heat shock protein 70, conserved site | 195 - 208 | IPR018181-2 |
| conserved_site | Heat shock protein 70, conserved site | 332 - 346 | IPR018181-3 |
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| 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. |
| 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. |
| unfolded protein binding | Binding to an unfolded protein. |
5 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 folding | The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure. |
| protein quality control for misfolded or incompletely synthesized proteins | The chemical reactions and pathways resulting in the breakdown of misfolded or attenuated proteins. |
| 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. |
| SRP-dependent cotranslational protein targeting to membrane, translocation | The process during cotranslational membrane targeting wherein proteins move across a membrane. SRP and its receptor initiate the transfer of the nascent chain across the endoplasmic reticulum (ER) membrane; they then dissociate from the chain, which is transferred to a set of transmembrane proteins, collectively called the translocon. Once the nascent chain translocon complex is assembled, the elongating chain passes directly from the large ribosomal subunit into the centers of the translocon, a protein-lined channel within the membrane. The growing chain is never exposed to the cytosol and does not fold until it reaches the ER lumen. |
27 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P11484 | SSB1 | Ribosome-associated molecular chaperone SSB1 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | SS |
| P40150 | SSB2 | Ribosome-associated molecular chaperone SSB2 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | SS |
| P22202 | SSA4 | Heat shock protein SSA4 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | SS |
| P10591 | SSA1 | Heat shock protein SSA1 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | SS |
| P10592 | SSA2 | Heat shock protein SSA2 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | SS |
| P19120 | HSPA8 | Heat shock cognate 71 kDa protein | Bos taurus (Bovine) | SS |
| O73885 | HSPA8 | Heat shock cognate 71 kDa protein | Gallus gallus (Chicken) | SS |
| P77319 | hscC | Chaperone protein HscC | Escherichia coli (strain K12) | PR |
| P0A6Y8 | dnaK | Chaperone protein DnaK | Escherichia coli (strain K12) | SS |
| P29843 | Hsc70-1 | Heat shock 70 kDa protein cognate 1 | Drosophila melanogaster (Fruit fly) | SS |
| P11147 | Hsc70-4 | Heat shock 70 kDa protein cognate 4 | Drosophila melanogaster (Fruit fly) | SS |
| A2Q0Z1 | HSPA8 | Heat shock cognate 71 kDa protein | Equus caballus (Horse) | SS |
| P11142 | HSPA8 | Heat shock cognate 71 kDa protein | Homo sapiens (Human) | EV |
| P11143 | HSP70 | Heat shock 70 kDa protein | Zea mays (Maize) | SS |
| P63017 | Hspa8 | Heat shock cognate 71 kDa protein | Mus musculus (Mouse) | SS |
| P63018 | Hspa8 | Heat shock cognate 71 kDa protein | Rattus norvegicus (Rat) | SS |
| P09446 | hsp-1 | Heat shock protein hsp-1 | Caenorhabditis elegans | SS |
| P26413 | HSP70 | Heat shock 70 kDa protein | Glycine max (Soybean) (Glycine hispida) | SS |
| Q9S9N1 | HSP70-5 | Heat shock 70 kDa protein 5 | Arabidopsis thaliana (Mouse-ear cress) | SS |
| P22954 | HSP70-2 | Heat shock 70 kDa protein 2 | Arabidopsis thaliana (Mouse-ear cress) | SS |
| Q9C7X7 | HSP70-18 | Heat shock 70 kDa protein 18 | Arabidopsis thaliana (Mouse-ear cress) | SS |
| P22953 | HSP70-1 | Heat shock 70 kDa protein 1 | Arabidopsis thaliana (Mouse-ear cress) | SS |
| O65719 | HSP70-3 | Heat shock 70 kDa protein 3 | Arabidopsis thaliana (Mouse-ear cress) | SS |
| Q9LHA8 | HSP70-4 | Heat shock 70 kDa protein 4 | Arabidopsis thaliana (Mouse-ear cress) | SS |
| P27322 | HSC-2 | Heat shock cognate 70 kDa protein 2 | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) | SS |
| P24629 | HSC-I | Heat shock cognate 70 kDa protein 1 | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) | SS |
| Q90473 | hspa8 | Heat shock cognate 71 kDa protein | Danio rerio (Zebrafish) (Brachydanio rerio) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSRAVGIDLG | TTYSCVAHFS | NDRVEIIAND | QGNRTTPSYV | AFTDTERLIG | DAAKNQAAIN |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PHNTVFDAKR | LIGRKFDDPE | VTTDAKHFPF | KVISRDGKPV | VQVEYKGETK | TFTPEEISSM |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VLSKMKETAE | NYLGTTVNDA | VVTVPAYFND | SQRQATKDAG | TIAGMNVLRI | INEPTAAAIA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| YGLDKKGRAE | HNVLIFDLGG | GTFDVSLLSI | DEGVFEVKAT | AGDTHLGGED | FDNRLVNHLA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TEFKRKTKKD | ISNNQRSLRR | LRTAAERAKR | ALSSSSQTSI | EIDSLFEGMD | FYTSLTRARF |
| 310 | 320 | 330 | 340 | 350 | 360 |
| EELCADLFRS | TLEPVEKVLK | DSKLDKSQID | EIVLVGGSTR | IPKIQKLVSD | FFNGKEPNRS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| INPDEAVAYG | AAVQAAILTG | DQSTKTQDLL | LLDVAPLSLG | IETAGGIMTK | LIPRNSTIPT |
| 430 | 440 | 450 | 460 | 470 | 480 |
| KKSETFSTYA | DNQPGVLIQV | FEGERTRTKD | NNLLGKFELS | GIPPAPRGVP | QIDVTFDIDA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| NGILNVSALE | KGTGKSNKIT | ITNDKGRLSK | DDIDRMVSEA | EKYRADDERE | AERVQAKNQL |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ESYAFTLKNT | INEASFKEKV | GEDDAKRLET | ASQETIDWLD | ASQAASTDEY | KDRQKELEGI |
| 610 | 620 | 630 | 640 | ||
| ANPIMTKFYG | AGAGAGPGAG | ESGGFPGSMP | NSGATGGGED | TGPTVEEVD |