Page last updated: 2024-08-08 00:34:24
Endoplasmin
An endoplasmin that is encoded in the genome of human. [PRO:DAN]
Synonyms
94 kDa glucose-regulated protein;
GRP-94;
Heat shock protein 90 kDa beta member 1;
Tumor rejection antigen 1;
gp96 homolog
Research
Bioassay Publications (12)
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 6 (50.00) | 24.3611 |
| 2020's | 6 (50.00) | 2.80 |
Compounds (22)
Drugs with Inhibition Measurements
Drugs with Activation Measurements
Drugs with Other Measurements
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|
| adenosine diphosphate | Homo sapiens (human) | Activity | 2.3000 | 1 | 1 |
Design and Synthesis of TRAP1 Selective Inhibitors: H-Bonding with Asn171 Residue in TRAP1 Increases Paralog Selectivity.ACS medicinal chemistry letters, , Jul-08, Volume: 12, Issue:7, 2021
Discovery of 2-((4-resorcinolyl)-5-aryl-1,2,3-triazol-1-yl)acetates as potent Hsp90 inhibitors with selectivity over TRAP1.Bioorganic & medicinal chemistry letters, , 01-15, Volume: 30, Issue:2, 2020
Structure-activity relationship in a purine-scaffold compound series with selectivity for the endoplasmic reticulum Hsp90 paralog Grp94.Journal of medicinal chemistry, , May-14, Volume: 58, Issue:9, 2015
Heat Shock Protein 90 Inhibitors: An Update on Achievements, Challenges, and Future Directions.Journal of medicinal chemistry, , 03-12, Volume: 63, Issue:5, 2020
Correlation between chemotype-dependent binding conformations of HSP90α/β and isoform selectivity-Implications for the structure-based design of HSP90α/β selective inhibitors for treating neurodegenerative diseases.Bioorganic & medicinal chemistry letters, , Jan-01, Volume: 24, Issue:1, 2014
Thermodynamic Dissection of Potency and Selectivity of Cytosolic Hsp90 Inhibitors.Journal of medicinal chemistry, , 03-11, Volume: 64, Issue:5, 2021
Heat Shock Protein 90 Inhibitors: An Update on Achievements, Challenges, and Future Directions.Journal of medicinal chemistry, , 03-12, Volume: 63, Issue:5, 2020
Correlation between chemotype-dependent binding conformations of HSP90α/β and isoform selectivity-Implications for the structure-based design of HSP90α/β selective inhibitors for treating neurodegenerative diseases.Bioorganic & medicinal chemistry letters, , Jan-01, Volume: 24, Issue:1, 2014
Heat shock protein 90: inhibitors in clinical trials.Journal of medicinal chemistry, , Jan-14, Volume: 53, Issue:1, 2010
Enables
This protein enables 9 target(s):
| Target | Category | Definition |
|---|
| RNA binding | molecular function | Binding to an RNA molecule or a portion thereof. [GOC:jl, GOC:mah] |
| calcium ion binding | molecular function | Binding to a calcium ion (Ca2+). [GOC:ai] |
| protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
| ATP binding | molecular function | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. [ISBN:0198506732] |
| ATP hydrolysis activity | molecular function | Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. [RHEA:13065] |
| protein phosphatase binding | molecular function | Binding to a protein phosphatase. [GOC:jl] |
| low-density lipoprotein particle receptor binding | molecular function | Binding to a low-density lipoprotein receptor. [GOC:ai] |
| ATP-dependent protein folding chaperone | molecular function | Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis. [PMID:27365453] |
| unfolded protein binding | molecular function | Binding to an unfolded protein. [GOC:ai] |
Located In
This protein is located in 17 target(s):
| Target | Category | Definition |
|---|
| extracellular region | cellular component | The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. [GOC:go_curators] |
| nucleus | cellular component | 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. [GOC:go_curators] |
| endoplasmic reticulum | cellular component | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). [ISBN:0198506732] |
| endoplasmic reticulum lumen | cellular component | The volume enclosed by the membranes of the endoplasmic reticulum. [ISBN:0198547684] |
| endoplasmic reticulum membrane | cellular component | The lipid bilayer surrounding the endoplasmic reticulum. [GOC:mah] |
| smooth endoplasmic reticulum | cellular component | The smooth endoplasmic reticulum (smooth ER or SER) has no ribosomes attached to it. The smooth ER is the recipient of the proteins synthesized in the rough ER. Those proteins to be exported are passed to the Golgi complex, the resident proteins are returned to the rough ER and the lysosomal proteins after phosphorylation of their mannose residues are passed to the lysosomes. Glycosylation of the glycoproteins also continues. The smooth ER is the site of synthesis of lipids, including the phospholipids. The membranes of the smooth ER also contain enzymes that catalyze a series of reactions to detoxify both lipid-soluble drugs and harmful products of metabolism. Large quantities of certain compounds such as phenobarbital cause an increase in the amount of the smooth ER. [ISBN:0198506732] |
| cytosol | cellular component | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl] |
| focal adhesion | cellular component | A cell-substrate junction that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments. In insects focal adhesion has also been referred to as hemi-adherens junction (HAJ). [GOC:aruk, GOC:bc, ISBN:0124325653, ISBN:0815316208, PMID:10419689, PMID:12191915, PMID:15246682, PMID:1643657, PMID:16805308, PMID:19197329, PMID:23033047, PMID:26923917, PMID:28796323, PMID:8314002] |
| membrane | cellular component | A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. [GOC:dos, GOC:mah, ISBN:0815316194] |
| midbody | cellular component | A thin cytoplasmic bridge formed between daughter cells at the end of cytokinesis. The midbody forms where the contractile ring constricts, and may persist for some time before finally breaking to complete cytokinesis. [ISBN:0815316194] |
| sarcoplasmic reticulum lumen | cellular component | The volume enclosed by the membranes of the sarcoplasmic reticulum. [GOC:rph] |
| melanosome | cellular component | A tissue-specific, membrane-bounded cytoplasmic organelle within which melanin pigments are synthesized and stored. Melanosomes are synthesized in melanocyte cells. [GOC:jl, PMID:11584301] |
| perinuclear region of cytoplasm | cellular component | Cytoplasm situated near, or occurring around, the nucleus. [GOC:jid] |
| collagen-containing extracellular matrix | cellular component | An extracellular matrix consisting mainly of proteins (especially collagen) and glycosaminoglycans (mostly as proteoglycans) that provides not only essential physical scaffolding for the cellular constituents but can also initiate crucial biochemical and biomechanical cues required for tissue morphogenesis, differentiation and homeostasis. The components are secreted by cells in the vicinity and form a sheet underlying or overlying cells such as endothelial and epithelial cells. [GOC:BHF, GOC:rph, PMID:21123617] |
| extracellular exosome | cellular component | 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. [GOC:BHF, GOC:mah, GOC:vesicles, PMID:15908444, PMID:17641064, PMID:19442504, PMID:19498381, PMID:22418571, PMID:24009894] |
| endocytic vesicle lumen | cellular component | The volume enclosed by the membrane of an endocytic vesicle. [GOC:pde] |
| sperm plasma membrane | cellular component | A plasma membrane that is part of a sperm cell. [GOC:cjm] |
Active In
This protein is active in 2 target(s):
| Target | Category | Definition |
|---|
| endoplasmic reticulum | cellular component | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). [ISBN:0198506732] |
| perinuclear region of cytoplasm | cellular component | Cytoplasm situated near, or occurring around, the nucleus. [GOC:jid] |
Part Of
This protein is part of 2 target(s):
| Target | Category | Definition |
|---|
| protein-containing complex | cellular component | 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. [GOC:dos, GOC:mah] |
| endoplasmic reticulum chaperone complex | cellular component | A protein complex that is located in the endoplasmic reticulum and is composed of chaperone proteins, including BiP, GRP94; CaBP1, protein disulfide isomerase (PDI), ERdj3, cyclophilin B, ERp72, GRP170, UDP-glucosyltransferase, and SDF2-L1. [PMID:12475965] |
Involved In
This protein is involved in 10 target(s):
| Target | Category | Definition |
|---|
| response to hypoxia | biological process | 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 stimulus indicating lowered oxygen tension. Hypoxia, defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95%, results in metabolic adaptation at both the cellular and organismal level. [GOC:hjd] |
| protein transport | biological process | The directed movement of proteins into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. [GOC:ai] |
| retrograde protein transport, ER to cytosol | biological process | The directed movement of unfolded or misfolded proteins from the endoplasmic reticulum to the cytosol through the translocon. [PMID:11994744] |
| protein folding in endoplasmic reticulum | biological process | A protein folding process that takes place in the endoplasmic reticulum (ER). Secreted, plasma membrane and organelle proteins are folded in the ER, assisted by chaperones and foldases (protein disulphide isomerases), and additional factors required for optimal folding (ATP, Ca2+ and an oxidizing environment to allow disulfide bond formation). [GOC:mah, GOC:vw] |
| response to endoplasmic reticulum stress | biological process | 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 stress acting at the endoplasmic reticulum. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen. [GOC:cjm, GOC:mah] |
| ERAD pathway | biological process | The protein catabolic pathway which targets endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. It begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein modifications necessary for correct substrate transfer (e.g. ubiquitination), transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome. [GOC:bf, GOC:PARL, PMID:20940304, PMID:21969857] |
| negative regulation of apoptotic process | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process. [GOC:jl, GOC:mtg_apoptosis] |
| sequestering of calcium ion | biological process | The process of binding or confining calcium ions such that they are separated from other components of a biological system. [GOC:ai] |
| cellular response to manganese ion | biological process | 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 manganese ion stimulus. [GOC:mah] |
| protein folding | biological process | The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure. [GOC:go_curators, GOC:rb] |