P17879
SS
Gene name |
Hspa1b (Hcp70.1, Hsp70-1, Hsp70a1, Hspa1) |
Protein name |
Heat shock 70 kDa protein 1B |
Names |
Heat shock 70 kDa protein 1 , HSP70.1 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:15511 |
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 |
225-262 (Nucleolar targeting region) |
Relief mechanism |
Others |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for P17879
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P17879-F1 | Predicted | AlphaFoldDB |
3 variants for P17879
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3553279258 | 534 | D>E | No | EVA | |
| rs3553187901 | 537 | A>S | No | EVA | |
| rs3552943240 | 562 | L>I | No | EVA |
No associated diseases with P17879
3 regional properties for P17879
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Heat shock protein 70, conserved site | 9 - 16 | IPR018181-1 |
| conserved_site | Heat shock protein 70, conserved site | 197 - 210 | IPR018181-2 |
| conserved_site | Heat shock protein 70, conserved site | 334 - 348 | IPR018181-3 |
Functions
14 GO annotations of cellular component
| Name | Definition |
|---|---|
| apical plasma membrane | The region of the plasma membrane located at the apical end of the cell. |
| basolateral plasma membrane | The region of the plasma membrane that includes the basal end and sides of the cell. Often used in reference to animal polarized epithelial membranes, where the basal membrane is the part attached to the extracellular matrix, or in plant cells, where the basal membrane is defined with respect to the zygotic axis. |
| 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. |
| cell body | The portion of a cell bearing surface projections such as axons, dendrites, cilia, or flagella that includes the nucleus, but excludes all cell projections. |
| centrosome | A structure comprised of a core structure (in most organisms, a pair of centrioles) and peripheral material from which a microtubule-based structure, such as a spindle apparatus, is organized. Centrosomes occur close to the nucleus during interphase in many eukaryotic cells, though in animal cells it changes continually during the cell-division cycle. |
| 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. |
| membrane raft | Any of the small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions. |
| mitochondrial matrix | The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation. |
| 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. |
| 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. |
| 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. |
| vesicle | Any small, fluid-filled, spherical organelle enclosed by membrane. |
| zona pellucida receptor complex | A multisubunit complex comprising the chaperonin-containing T-complex and several other components involved in mediating sperm-oocyte Interaction. |
8 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. |
| NF-kappaB binding | Binding to NF-kappaB, a transcription factor for eukaryotic RNA polymerase II promoters. |
| protease binding | Binding to a protease or a peptidase. |
| 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. |
9 GO annotations of biological process
| Name | Definition |
|---|---|
| binding of sperm to zona pellucida | The process in which the sperm binds to the zona pellucida glycoprotein layer of the egg. The process begins with the attachment of the sperm plasma membrane to the zona pellucida and includes attachment of the acrosome inner membrane to the zona pellucida after the acrosomal reaction takes place. |
| 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. |
| negative regulation of apoptotic process | Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process. |
| positive regulation of microtubule nucleation | Any process that increases the rate, frequency or extent of microtubule nucleation. Microtubule nucleation is the 'de novo' formation of a microtubule, in which tubulin heterodimers form metastable oligomeric aggregates, some of which go on to support formation of a complete microtubule. Microtubule nucleation usually occurs from a specific site within a cell. |
| positive regulation of proteasomal ubiquitin-dependent protein catabolic process | Any process that activates or increases the frequency, rate or extent of the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome. |
| 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 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. |
| regulation of mitotic spindle assembly | Any process that modulates the frequency, rate or extent of mitotic spindle assembly. |
| response to heat | Any process that results in a change in state or activity of a cell or an organism (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. |
54 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P19120 | HSPA8 | Heat shock cognate 71 kDa protein | Bos taurus (Bovine) | SS |
| Q2YDD0 | HSPA14 | Heat shock 70 kDa protein 14 | Bos taurus (Bovine) | SS |
| P0CB32 | HSPA1L | Heat shock 70 kDa protein 1-like | Bos taurus (Bovine) | SS |
| Q27975 | HSPA1A | Heat shock 70 kDa protein 1A | Bos taurus (Bovine) | SS |
| O73885 | HSPA8 | Heat shock cognate 71 kDa protein | Gallus gallus (Chicken) | SS |
| E1C2P3 | HSPA14 | Heat shock 70 kDa protein 14 | Gallus gallus (Chicken) | SS |
| P08106 | Heat shock 70 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 |
| P02825 | Hsp70Ab | Major heat shock 70 kDa protein Ab | Drosophila melanogaster (Fruit fly) | SS |
| P82910 | Hsp70Aa | Major heat shock 70 kDa protein Aa | Drosophila melanogaster (Fruit fly) | SS |
| Q8INI8 | Hsp70Ba | Major heat shock 70 kDa protein Ba | Drosophila melanogaster (Fruit fly) | SS |
| Q9BIR7 | Hsp70Bc | Major heat shock 70 kDa protein Bc | 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 |
| P11146 | Hsc70-2 | Heat shock 70 kDa protein cognate 2 | Drosophila melanogaster (Fruit fly) | SS |
| P11147 | Hsc70-4 | Heat shock 70 kDa protein cognate 4 | Drosophila melanogaster (Fruit fly) | SS |
| Q9VG58 | Hsp70Bbb | Major heat shock 70 kDa protein Bbb | Drosophila melanogaster (Fruit fly) | SS |
| Q96MM6 | HSPA12B | Heat shock 70 kDa protein 12B | Homo sapiens (Human) | PR |
| P17066 | HSPA6 | Heat shock 70 kDa protein 6 | Homo sapiens (Human) | SS |
| O43301 | HSPA12A | Heat shock 70 kDa protein 12A | Homo sapiens (Human) | PR |
| P34931 | HSPA1L | Heat shock 70 kDa protein 1-like | Homo sapiens (Human) | 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 |
| P0DMV9 | HSPA1B | Heat shock 70 kDa protein 1B | Homo sapiens (Human) | SS |
| P0DMV8 | HSPA1A | Heat shock 70 kDa protein 1A | Homo sapiens (Human) | SS |
| P11143 | HSP70 | Heat shock 70 kDa protein | Zea mays (Maize) | SS |
| Q8K0U4 | Hspa12a | Heat shock 70 kDa protein 12A | Mus musculus (Mouse) | PR |
| Q9CZJ2 | Hspa12b | Heat shock 70 kDa protein 12B | Mus musculus (Mouse) | PR |
| P16627 | Hspa1l | Heat shock 70 kDa protein 1-like | Mus musculus (Mouse) | SS |
| P17156 | Hspa2 | Heat shock-related 70 kDa protein 2 | Mus musculus (Mouse) | SS |
| P63017 | Hspa8 | Heat shock cognate 71 kDa protein | Mus musculus (Mouse) | SS |
| Q61696 | Hspa1a | Heat shock 70 kDa protein 1A | Mus musculus (Mouse) | SS |
| Q99M31 | Hspa14 | Heat shock 70 kDa protein 14 | Mus musculus (Mouse) | SS |
| Q6S4N2 | HSPA1B | Heat shock 70 kDa protein 1B | Sus scrofa (Pig) | SS |
| P14659 | Hspa2 | Heat shock-related 70 kDa protein 2 | Rattus norvegicus (Rat) | SS |
| P63018 | Hspa8 | Heat shock cognate 71 kDa protein | Rattus norvegicus (Rat) | SS |
| P55063 | Hspa1l | Heat shock 70 kDa protein 1-like | Rattus norvegicus (Rat) | SS |
| P0DMW0 | Hspa1a | Heat shock 70 kDa protein 1A | Rattus norvegicus (Rat) | SS |
| P0DMW1 | Hspa1b | Heat shock 70 kDa protein 1B | 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 |
| O65719 | HSP70-3 | Heat shock 70 kDa protein 3 | 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 |
| Q9LHA8 | HSP70-4 | Heat shock 70 kDa protein 4 | Arabidopsis thaliana (Mouse-ear cress) | SS |
| Q9S9N1 | HSP70-5 | Heat shock 70 kDa protein 5 | Arabidopsis thaliana (Mouse-ear cress) | SS |
| P22953 | HSP70-1 | Heat shock 70 kDa protein 1 | Arabidopsis thaliana (Mouse-ear cress) | SS |
| P24629 | HSC-I | Heat shock cognate 70 kDa protein 1 | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) | SS |
| P27322 | HSC-2 | Heat shock cognate 70 kDa protein 2 | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) | SS |
| Q5RGE6 | hspa14 | Heat shock 70 kDa protein 14 | Danio rerio (Zebrafish) (Brachydanio rerio) | SS |
| Q90473 | hspa8 | Heat shock cognate 71 kDa protein | Danio rerio (Zebrafish) (Brachydanio rerio) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAKNTAIGID | LGTTYSCVGV | FQHGKVEIIA | NDQGNRTTPS | YVAFTDTERL | IGDAAKNQVA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LNPQNTVFDA | KRLIGRKFGD | AVVQSDMKHW | PFQVVNDGDK | PKVQVNYKGE | SRSFFPEEIS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SMVLTKMKEI | AEAYLGHPVT | NAVITVPAYF | NDSQRQATKD | AGVIAGLNVL | RIINEPTAAA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IAYGLDRTGK | GERNVLIFDL | GGGTFDVSIL | TIDDGIFEVK | ATAGDTHLGG | EDFDNRLVSH |
| 250 | 260 | 270 | 280 | 290 | 300 |
| FVEEFKRKHK | KDISQNKRAV | RRLRTACERA | KRTLSSSTQA | SLEIDSLFEG | IDFYTSITRA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| RFEELCSDLF | RGTLEPVEKA | LRDAKMDKAQ | IHDLVLVGGS | TRIPKVQKLL | QDFFNGRDLN |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KSINPDEAVA | YGAAVQAAIL | MGDKSENVQD | LLLLDVAPLS | LGLETAGGVM | TALIKRNSTI |
| 430 | 440 | 450 | 460 | 470 | 480 |
| PTKQTQTFTT | YSDNQPGVLI | QVYEGERAMT | RDNNLLGRFE | LSGIPPAPRG | VPQIEVTFDI |
| 490 | 500 | 510 | 520 | 530 | 540 |
| DANGILNVTA | TDKSTGKANK | ITITNDKGRL | SKEEIERMVQ | EAERYKAEDE | VQRDRVAAKN |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ALESYAFNMK | SAVEDEGLKG | KLSEADKKKV | LDKCQEVISW | LDSNTLADKE | EFVHKREELE |
| 610 | 620 | 630 | 640 | ||
| RVCSPIISGL | YQGAGAPGAG | GFGAQAPPKG | ASGSGPTIEE | VD |