Q27975
SS
Gene name |
HSPA1A (HSP70-1) |
Protein name |
Heat shock 70 kDa protein 1A |
Names |
Heat shock 70 kDa protein 1 , HSP70.1 |
Species |
Bos taurus (Bovine) |
KEGG Pathway |
bta:282254 |
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 Q27975
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q27975-F1 | Predicted | AlphaFoldDB |
No variants for Q27975
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q27975 | |||||
No associated diseases with Q27975
3 regional properties for Q27975
| 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
7 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. |
| 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. |
| 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. |
| vesicle | Any small, fluid-filled, spherical organelle enclosed by membrane. |
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. |
| disordered domain specific binding | Binding to a disordered domain of a protein. |
| 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. |
| transcription corepressor activity | A transcription coregulator activity that represses or decreases the transcription of specific gene sets via binding to a DNA-bound DNA-binding transcription factor, either on its own or as part of a complex. Corepressors often act by altering chromatin structure and modifications. For example, one class of transcription corepressors modifies chromatin structure through covalent modification of histones. A second class remodels the conformation of chromatin in an ATP-dependent fashion. A third class modulates interactions of DNA-bound DNA-binding transcription factors with other transcription coregulators. |
| ubiquitin protein ligase binding | Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins. |
7 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. |
| lysosomal transport | The directed movement of substances into, out of or within a lysosome. |
| negative regulation of transcription by RNA polymerase II | Any process that stops, prevents, or reduces the frequency, rate or extent of transcription mediated by RNA polymerase II. |
| 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 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. |
54 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P0CB32 | HSPA1L | Heat shock 70 kDa protein 1-like | Bos taurus (Bovine) | SS |
| P19120 | HSPA8 | Heat shock cognate 71 kDa protein | Bos taurus (Bovine) | SS |
| Q2YDD0 | HSPA14 | Heat shock 70 kDa protein 14 | 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 |
| P16627 | Hspa1l | Heat shock 70 kDa protein 1-like | Mus musculus (Mouse) | SS |
| P63017 | Hspa8 | Heat shock cognate 71 kDa protein | Mus musculus (Mouse) | SS |
| Q99M31 | Hspa14 | Heat shock 70 kDa protein 14 | Mus musculus (Mouse) | SS |
| Q8K0U4 | Hspa12a | Heat shock 70 kDa protein 12A | Mus musculus (Mouse) | PR |
| P17156 | Hspa2 | Heat shock-related 70 kDa protein 2 | Mus musculus (Mouse) | SS |
| Q9CZJ2 | Hspa12b | Heat shock 70 kDa protein 12B | Mus musculus (Mouse) | PR |
| P17879 | Hspa1b | Heat shock 70 kDa protein 1B | Mus musculus (Mouse) | SS |
| Q61696 | Hspa1a | Heat shock 70 kDa protein 1A | 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 |
| MAKNMAIGID | LGTTYSCVGV | FQHGKVEIIA | NDQGNRTTPS | YVAFTDTERL | IGDAAKNQVA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LNPQNTVFDA | KRLIGRKFGD | PVVQSDMKHW | PFRVINDGDK | PKVQVSYKGE | TKAFYPEEIS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SMVLTKMKEI | AEAYLGHPVT | NAVITVPAYF | NDSQRQATKD | AGVIAGLNVL | RIINEPTAAA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IAYGLDRTGK | GERNVLIFDL | GGGTFDVSIL | TIDDGIFEVK | ATAGDTHLGG | EDFDNRLVNH |
| 250 | 260 | 270 | 280 | 290 | 300 |
| FVEEFKRKHK | KDISQNKRAV | RRLRTACERA | KRTLSSSTQA | SLEIDSLFEG | IDFYTSITRA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| RFEELCSDLF | RSTLEPVEKA | LRDAKLDKAQ | IHDLVLVGGS | TRIPKVQKLL | QDFFNGRDLN |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KSINPDEAVA | YGAAVQAAIL | MGDKSENVQD | LLLLDVAPLS | LGLETAGGVM | TALIKRNSTI |
| 430 | 440 | 450 | 460 | 470 | 480 |
| PTKQTQIFTT | YSDNQPGVLI | QVYEGERAMT | RDNNLLGRFE | LSGIPPAPRG | VPQIEVTFDI |
| 490 | 500 | 510 | 520 | 530 | 540 |
| DANGILNVTA | TDKSTGKANK | ITITNDKGRL | SKEEIERMVQ | EAEKYKAEDE | VQRERVSAKN |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ALESYAFNMK | SAVEDEGLKG | KISEADKKKV | LDKCQEVISW | LDANTLAEKD | EFEHKRKELE |
| 610 | 620 | 630 | 640 | ||
| QVCNPIISRL | YQGAGGPGAG | GFGAQGPKGG | SGSGPTIEEV | D |