P0DMW0
SS
Gene name |
Hspa1a (Hsp70-1, Hspa1) |
Protein name |
Heat shock 70 kDa protein 1A |
Names |
Heat shock 70 kDa protein 2 , HSP70-2 , HSP70.2 |
Species |
Rattus norvegicus (Rat) |
KEGG Pathway |
rno:24472 |
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 P0DMW0
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P0DMW0-F1 | Predicted | AlphaFoldDB |
No variants for P0DMW0
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P0DMW0 | |||||
No associated diseases with P0DMW0
3 regional properties for P0DMW0
| 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
21 GO annotations of cellular component
| Name | Definition |
|---|---|
| aggresome | An inclusion body formed by dynein-dependent retrograde transport of an aggregated protein on microtubules. |
| 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. |
| centriole | A cellular organelle, found close to the nucleus in many eukaryotic cells, consisting of a small cylinder with microtubular walls, 300-500 nm long and 150-250 nm in diameter. It contains nine short, parallel, peripheral microtubular fibrils, each fibril consisting of one complete microtubule fused to two incomplete microtubules. Cells usually have two centrioles, lying at right angles to each other. At division, each pair of centrioles generates another pair and the twin pairs form the pole of the mitotic spindle. |
| 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. |
| COP9 signalosome | A protein complex that catalyzes the deneddylation of proteins, including the cullin component of SCF ubiquitin E3 ligase; deneddylation increases the activity of cullin family ubiquitin ligases. The signalosome is involved in many regulatory process, including some which control development, in many species; also regulates photomorphogenesis in plants; in many species its subunits are highly similar to those of the proteasome. |
| 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 space | That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid. |
| inclusion body | A discrete intracellular part formed of aggregated molecules such as proteins or other biopolymers. |
| 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. |
| 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. |
| nuclear speck | A discrete extra-nucleolar subnuclear domain, 20-50 in number, in which splicing factors are seen to be localized by immunofluorescence microscopy. |
| 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. |
| perinuclear region of cytoplasm | Cytoplasm situated near, or occurring around, the nucleus. |
| 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. |
| ribonucleoprotein complex | A macromolecular complex that contains both RNA and protein molecules. |
| 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. |
22 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 disaggregase activity | An ATP-dependent molecular chaperone activity that mediates the solubilization of ordered protein aggregates. |
| ATP-dependent protein folding chaperone | Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis. |
| C3HC4-type RING finger domain binding | Binding to a C3HC4-type zinc finger domain of a protein. The C3HC4-type zinc finger is a variant of RING finger, is a cysteine-rich domain of 40 to 60 residues that coordinates two zinc ions, and has the consensus sequence |
| death receptor agonist activity | Interacting with a death receptor such that the proportion of death receptors in an active form is increased. Ligand binding to a death receptor often induces a conformational change to activate the receptor. |
| denatured protein binding | Binding to a denatured protein. |
| disordered domain specific binding | Binding to a disordered domain of a protein. |
| enzyme binding | Binding to an enzyme, a protein with catalytic activity. |
| G protein-coupled receptor binding | Binding to a G protein-coupled receptor. |
| heat shock protein binding | Binding to a heat shock protein, a protein synthesized or activated in response to heat shock. |
| histone deacetylase binding | Binding to histone deacetylase. |
| misfolded protein binding | Binding to a misfolded protein. |
| 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. |
| receptor ligand activity | The activity of a gene product that interacts with a receptor to effect a change in the activity of the receptor. Ligands may be produced by the same, or different, cell that expresses the receptor. Ligands may diffuse extracellularly from their point of origin to the receiving cell, or remain attached to an adjacent cell surface (e.g. Notch ligands). |
| signaling receptor binding | Binding to one or more specific sites on a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function. |
| 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. |
| transcription regulator inhibitor activity | A molecular function regulator that inhibits the activity of a transcription regulator via direct binding and/or post-translational modification. |
| ubiquitin protein ligase binding | Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins. |
| unfolded protein binding | Binding to an unfolded protein. |
37 GO annotations of biological process
| Name | Definition |
|---|---|
| ATP metabolic process | The chemical reactions and pathways involving ATP, adenosine triphosphate, a universally important coenzyme and enzyme regulator. |
| 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. |
| cellular heat acclimation | Any process that increases heat tolerance of a cell in response to high temperatures. |
| 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. |
| cellular response to unfolded protein | 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 an unfolded protein stimulus. |
| 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. |
| chaperone-mediated protein complex assembly | The aggregation, arrangement and bonding together of a set of components to form a protein complex, mediated by chaperone molecules that do not form part of the finished complex. |
| defense response | Reactions, triggered in response to the presence of a foreign body or the occurrence of an injury, which result in restriction of damage to the organism attacked or prevention/recovery from the infection caused by the attack. |
| lysosomal transport | The directed movement of substances into, out of or within a lysosome. |
| mRNA catabolic process | The chemical reactions and pathways resulting in the breakdown of mRNA, messenger RNA, which is responsible for carrying the coded genetic 'message', transcribed from DNA, to sites of protein assembly at the ribosomes. |
| negative regulation of apoptotic process | Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process. |
| negative regulation of cell growth | Any process that stops, prevents, or reduces the frequency, rate, extent or direction of cell growth. |
| negative regulation of cell population proliferation | Any process that stops, prevents or reduces the rate or extent of cell proliferation. |
| negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway | Any process that stops, prevents or reduces the frequency, rate or extent of an endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway. |
| negative regulation of extrinsic apoptotic signaling pathway in absence of ligand | Any process that stops, prevents or reduces the frequency, rate or extent of extrinsic apoptotic signaling pathway in absence of ligand. |
| negative regulation of inclusion body assembly | Any process that decreases the rate, frequency, or extent of inclusion body assembly. Inclusion body assembly is the aggregation, arrangement and bonding together of a set of components to form an inclusion body. |
| negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway | Any process that stops, prevents or reduces the frequency, rate or extent of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway. |
| negative regulation of protein ubiquitination | Any process that stops, prevents, or reduces the frequency, rate or extent of the addition of ubiquitin groups to a protein. |
| 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. |
| negative regulation of transforming growth factor beta receptor signaling pathway | Any process that stops, prevents, or reduces the frequency, rate or extent of any TGF-beta receptor signaling pathway. |
| negative regulation of vasoconstriction | Any process that stops, prevents, or reduces the frequency, rate or extent of vasoconstriction. |
| positive regulation of erythrocyte differentiation | Any process that activates or increases the frequency, rate or extent of erythrocyte differentiation. |
| positive regulation of gene expression | Any process that increases the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product (protein or RNA). |
| positive regulation of interleukin-8 production | Any process that activates or increases the frequency, rate, or extent of interleukin-8 production. |
| 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 nucleotide-binding oligomerization domain containing 2 signaling pathway | Any process that activates or increases the frequency, rate, or extent of the nucleotide-binding oligomerization domain containing 2 (NOD2) pathway. |
| 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. |
| positive regulation of RNA splicing | Any process that activates or increases the frequency, rate or extent of RNA splicing. |
| positive regulation of T cell mediated cytotoxicity | Any process that activates or increases the frequency, rate or extent of T cell mediated cytotoxicity. |
| positive regulation of tumor necrosis factor-mediated signaling pathway | Any process that activates or increases the frequency, rate or extent of tumor necrosis factor-mediated signaling pathway. |
| 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. |
| protein stabilization | Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation. |
| regulation of mitotic spindle assembly | Any process that modulates the frequency, rate or extent of mitotic spindle assembly. |
| regulation of protein ubiquitination | Any process that modulates the frequency, rate or extent of the addition of ubiquitin groups to a protein. |
| 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. |
| response to unfolded protein | 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 an unfolded protein stimulus. |
55 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 |
| O97125 | Hsp68 | Heat shock protein 68 | Drosophila melanogaster (Fruit fly) | SS |
| P02825 | Hsp70Ab | Major heat shock 70 kDa protein Ab | 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 |
| 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 |
| 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 |
| P0DMV8 | HSPA1A | Heat shock 70 kDa protein 1A | Homo sapiens (Human) | SS |
| P0DMV9 | HSPA1B | Heat shock 70 kDa protein 1B | 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 |
| P0DMW0 | Hspa1a | Heat shock 70 kDa protein 1A | Rattus norvegicus (Rat) | SS |
| P0DMW1 | Hspa1b | Heat shock 70 kDa protein 1B | Rattus norvegicus (Rat) | SS |
| P14659 | Hspa2 | Heat shock-related 70 kDa protein 2 | Rattus norvegicus (Rat) | SS |
| P55063 | Hspa1l | Heat shock 70 kDa protein 1-like | Rattus norvegicus (Rat) | 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 |
| 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 |
| MAKKTAIGID | LGTTYSCVGV | FQHGKVEIIA | NDQGNRTTPS | YVAFTDTERL | IGDAAKNQVA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LNPQNTVFDA | KRLIGRKFGD | PVVQSDMKHW | PFQVVNDGDK | PKVQVNYKGE | NRSFYPEEIS |
| 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 | LRDAKLDKAQ | 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 | VQRERVAAKN |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ALESYAFNMK | SAVEDEGLKG | KISEADKKKV | LDKCQEVISW | LDSNTLAEKE | EFVHKREELE |
| 610 | 620 | 630 | 640 | ||
| RVCNPIISGL | YQGAGAPGAG | GFGAQAPKGG | SGSGPTIEEV | D |