Q66HD0

PR
Gene name
Hsp90b1
Protein name
Endoplasmin
Names
94 kDa glucose-regulated protein, GRP-94, Heat shock protein 90 kDa beta member 1
Species
Rattus norvegicus (Rat)
KEGG Pathway
rno:362862
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

746-804 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q66HD0

Entry ID Method Resolution Chain Position Source
AF-Q66HD0-F1 Predicted AlphaFoldDB

No variants for Q66HD0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q66HD0

No associated diseases with Q66HD0

3 regional properties for Q66HD0

Type Name Position InterPro Accession
domain Histidine kinase/HSP90-like ATPase 96 - 255 IPR003594
conserved_site Heat shock protein Hsp90, conserved site 94 - 103 IPR019805
domain Heat shock protein Hsp90, N-terminal 74 - 279 IPR020575

Functions

Description
EC Number
Subcellular Localization
  • Endoplasmic reticulum lumen
  • Sarcoplasmic reticulum lumen
  • Melanosome
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

13 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
endoplasmic reticulum 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).
endoplasmic reticulum chaperone complex 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.
endoplasmic reticulum lumen The volume enclosed by the membranes of the endoplasmic reticulum.
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
melanosome A tissue-specific, membrane-bounded cytoplasmic organelle within which melanin pigments are synthesized and stored. Melanosomes are synthesized in melanocyte cells.
midbody 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.
perinuclear region of cytoplasm Cytoplasm situated near, or occurring around, the nucleus.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
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.
sarcoplasmic reticulum lumen The volume enclosed by the membranes of the sarcoplasmic reticulum.
smooth endoplasmic reticulum 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.
sperm plasma membrane A plasma membrane that is part of a sperm cell.

7 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 + 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.
ATP-dependent protein folding chaperone Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis.
low-density lipoprotein particle receptor binding Binding to a low-density lipoprotein receptor.
protein phosphatase binding Binding to a protein phosphatase.
RNA binding Binding to an RNA molecule or a portion thereof.
unfolded protein binding Binding to an unfolded protein.

9 GO annotations of biological process

Name Definition
actin rod assembly The assembly of actin rods, a cellular structure consisting of parallel, hexagonally arranged actin tubules.
cellular response to ATP 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 ATP (adenosine 5'-triphosphate) stimulus.
cellular response to manganese ion 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.
negative regulation of apoptotic process Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process.
protein folding The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.
regulation of phosphoprotein phosphatase activity Any process that modulates the frequency, rate or extent of phosphoprotein phosphatase activity, the catalysis of the hydrolysis of phosphate from a phosphoprotein.
response to hypoxia 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.
retrograde protein transport, ER to cytosol The directed movement of unfolded or misfolded proteins from the endoplasmic reticulum to the cytosol through the translocon.
ubiquitin-dependent ERAD pathway The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P14625 HSP90B1 Endoplasmin Homo sapiens (Human) PR
P08113 Hsp90b1 Endoplasmin Mus musculus (Mouse) PR
10 20 30 40 50 60
MRVLWVLGLC CVLLTFGFVR ADDEVDVDGT VEEDLGKSRE GSRTDDEVVQ REEEAIQLDG
70 80 90 100 110 120
LNASQIRELR EKSEKFAFQA EVNRMMKLII NSLYKNKEIF LRELISNASD ALDKIRLISL
130 140 150 160 170 180
TDENALAGNE ELTVKIKCDR EKNLLHVTDT GVGMTREELV KNLGTIAKSG TSEFLNKMTE
190 200 210 220 230 240
AQEDGQSTSE LIGQFGVGFY SAFLVADKVI VTSKHNNDTQ HIWESDSNEF SVIADPRGNT
250 260 270 280 290 300
LGRGTTITLV LKEEASDYLE LDTIKNLVRK YSQFINFPIY VWSSKTETVE EPLEEDETAQ
310 320 330 340 350 360
EEKEEADDEA AVEEEEEEKK PKTKKVEKTV WDWELMNDIK PIWQRPSKEV EEDEYKAFYK
370 380 390 400 410 420
SFSKESDDPM AYIHFTAEGE VTFKSILFVP TSAPRGLFDE YGSKKSDYIK LYVRRVFITD
430 440 450 460 470 480
DFHDMMPKYL NFVKGVVDSD DLPLNVSRET LQQHKLLKVI RKKLVRKTLD MIKKIADEKY
490 500 510 520 530 540
NDTFWKEFGT NIKLGVIEDH SNRTRLAKLL RFQSSHHSTD ITSLDQYVER MKEKQDKIYF
550 560 570 580 590 600
MAGSSRKEAE SSPFVERLLK KGYEVIYLTE PVDEYCIQAL PEFDGKRFQN VAKEGVKFDE
610 620 630 640 650 660
SEKSKESREA TEKEFEPLLN WMKDKALKDK IEKAVVSQRL TESPCALVAS QYGWSGNMER
670 680 690 700 710 720
IMKAQAYQTG KDISTNYYAS QKKTFEINPR HPLIRDMLRR VKEDEDDKTV MDLAVVLFET
730 740 750 760 770 780
ATLRSGYLLP DTKAYGDRIE RMLRLSLNID PEAQVEEEPE EEPEDTTEDT TDDSEQDEEE
790 800
TDAGAEEEEE EQETEKEPTE KDEL