O35465
Gene name |
Fkbp8 (Fkbp38, Sam11) |
Protein name |
Peptidyl-prolyl cis-trans isomerase FKBP8 |
Names |
PPIase FKBP8 , EC 5.2.1.8 , 38 kDa FK506-binding protein , 38 kDa FKBP , FKBP-38 , mFKBP38 , FK506-binding protein 8 , FKBP-8 , FKBPR38 , Rotamase |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:14232 |
EC number |
5.2.1.8: Cis-trans isomerases |
Protein Class |
|

Descriptions
Autoinhibitory domains (AIDs)
Target domain |
105-194 (Peptidyl-prolyl cis-trans isomerase domain) |
Relief mechanism |
Partner binding |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure

Activated structure

1 structures for O35465
Entry ID | Method | Resolution | Chain | Position | Source |
---|---|---|---|---|---|
AF-O35465-F1 | Predicted | AlphaFoldDB |
13 variants for O35465
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
rs3388965222 | 46 | E>V | No | EVA | |
rs3398792321 | 154 | D>A | No | EVA | |
rs3399224373 | 156 | G>S | No | EVA | |
rs3388980250 | 165 | S>F | No | EVA | |
rs3388981106 | 205 | Q>* | No | EVA | |
rs3399224425 | 243 | S>F | No | EVA | |
rs3399221519 | 290 | E>Q | No | EVA | |
rs3399224408 | 292 | Q>L | No | EVA | |
rs3388975262 | 322 | A>V | No | EVA | |
rs3388965203 | 349 | T>I | No | EVA | |
rs3388965204 | 350 | E>D | No | EVA | |
rs3388985693 | 355 | R>L | No | EVA | |
rs3388939710 | 367 | K>M | No | EVA |
No associated diseases with O35465
4 regional properties for O35465
Type | Name | Position | InterPro Accession |
---|---|---|---|
domain | FKBP-type peptidyl-prolyl cis-trans isomerase domain | 105 - 194 | IPR001179 |
repeat | Tetratricopeptide repeat | 211 - 244 | IPR019734-1 |
repeat | Tetratricopeptide repeat | 262 - 295 | IPR019734-2 |
repeat | Tetratricopeptide repeat | 296 - 329 | IPR019734-3 |
Functions
Description | ||
---|---|---|
EC Number | 5.2.1.8 | Cis-trans isomerases |
Subcellular Localization |
|
|
PANTHER Family | ||
PANTHER Subfamily | ||
PANTHER Protein Class | ||
PANTHER Pathway Category | No pathway information available |
8 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. |
endomembrane system | A collection of membranous structures involved in transport within the cell. The main components of the endomembrane system are endoplasmic reticulum, Golgi bodies, vesicles, cell membrane and nuclear envelope. Members of the endomembrane system pass materials through each other or though the use of vesicles. |
endoplasmic reticulum membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. |
mitochondrial envelope | The double lipid bilayer enclosing the mitochondrion and separating its contents from the cell cytoplasm; includes the intermembrane space. |
mitochondrial membrane | Either of the lipid bilayers that surround the mitochondrion and form the mitochondrial envelope. |
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. |
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. |
5 GO annotations of molecular function
Name | Definition |
---|---|
calmodulin binding | Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states. |
disordered domain specific binding | Binding to a disordered domain of a protein. |
identical protein binding | Binding to an identical protein or proteins. |
peptidyl-prolyl cis-trans isomerase activity | Catalysis of the reaction |
protein folding chaperone | Binding to a protein or a protein-containing complex to assist the protein folding process. |
18 GO annotations of biological process
Name | Definition |
---|---|
apoptotic process | A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. |
BMP signaling pathway | The series of molecular signals initiated by the binding of a member of the BMP (bone morphogenetic protein) family to a receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. |
camera-type eye development | The process whose specific outcome is the progression of the camera-type eye over time, from its formation to the mature structure. The camera-type eye is an organ of sight that receives light through an aperture and focuses it through a lens, projecting it on a photoreceptor field. |
cell fate specification | The cellular developmental process involved in cell fate commitment in which the cell is designated to follow a developmental path, unless they receive extrinsic cues that direct an alternative fate. |
dorsal/ventral neural tube patterning | The process in which the neural tube is regionalized in the dorsoventral axis. |
dorsal/ventral pattern formation | The regionalization process in which the areas along the dorsal/ventral axis are established that will lead to differences in cell differentiation. The dorsal/ventral axis is defined by a line that runs orthogonal to both the anterior/posterior and left/right axes. The dorsal end is defined by the upper or back side of an organism. The ventral end is defined by the lower or front side of an organism. |
multicellular organism growth | The increase in size or mass of an entire multicellular organism, as opposed to cell growth. |
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 protein phosphorylation | Any process that stops, prevents or reduces the rate of addition of phosphate groups to amino acids within a protein. |
neural tube development | The process whose specific outcome is the progression of the neural tube over time, from its formation to the mature structure. The mature structure of the neural tube exists when the tube has been segmented into the forebrain, midbrain, hindbrain and spinal cord regions. In addition neural crest has budded away from the epithelium. |
neuron fate specification | The process in which a cell becomes capable of differentiating autonomously into a neuron in an environment that is neutral with respect to the developmental pathway. Upon specification, the cell fate can be reversed. |
positive regulation of BMP signaling pathway | Any process that activates or increases the frequency, rate or extent of BMP signaling pathway activity. |
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 localization to mitochondrion | A process in which a protein is transported to, or maintained in, a location within the mitochondrion. |
regulation of BMP signaling pathway | Any process that modulates the frequency, rate or extent of the activity of any BMP receptor signaling pathway. |
regulation of gene expression | Any process that modulates 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). |
regulation of mitophagy | Any process that modulates the frequency, rate or extent of macromitophagy. |
smoothened signaling pathway | The series of molecular signals generated as a consequence of activation of the transmembrane protein Smoothened. |
6 homologous proteins in AiPD
UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
---|---|---|---|---|
A6QQ71 | FKBP6 | Inactive peptidyl-prolyl cis-trans isomerase FKBP6 | Bos taurus (Bovine) | PR |
Q9W1I9 | shu | Inactive peptidyl-prolyl cis-trans isomerase shutdown | Drosophila melanogaster (Fruit fly) | PR |
Q02790 | FKBP4 | Peptidyl-prolyl cis-trans isomerase FKBP4 | Homo sapiens (Human) | PR |
Q14318 | FKBP8 | Peptidyl-prolyl cis-trans isomerase FKBP8 | Homo sapiens (Human) | EV |
Q3B7U9 | Fkbp8 | Peptidyl-prolyl cis-trans isomerase FKBP8 | Rattus norvegicus (Rat) | SS |
Q7DMA9 | PAS1 | Peptidyl-prolyl cis-trans isomerase PASTICCINO1 | Arabidopsis thaliana (Mouse-ear cress) | PR |
10 | 20 | 30 | 40 | 50 | 60 |
MASWAEPSEP | AALRLPGAPL | LEGFEVLDGV | DDAEEEDDLS | GLPPLEDMGQ | PTVEEAEQPG |
70 | 80 | 90 | 100 | 110 | 120 |
ALAREFLAAT | EPEPAPAPAP | EEWLDILGNG | LLRMKTLVPG | PKGSSRPLKG | QVVTVHLQMS |
130 | 140 | 150 | 160 | 170 | 180 |
LENGTRVQEE | PELAFTLGDC | DVIQALDLSV | PLMDVGETAM | VTADSKYCYG | PQGRSPYIPP |
190 | 200 | 210 | 220 | 230 | 240 |
HAALCLEVTL | KTAEDGPDLE | MLSGQERVAL | ANRKRECGNA | HYQRADFVLA | ANSYDLAIKA |
250 | 260 | 270 | 280 | 290 | 300 |
ITSNTKVDMT | CEEEEELLQL | KVKCLNNLAA | SQLKLDHYRA | ALRSCSQVLE | HQPDNIKALF |
310 | 320 | 330 | 340 | 350 | 360 |
RKGKVLAQQG | EYSEAIPILR | AALKLEPSNK | TIHAELSKLV | KKRAAQRSTE | TALYRKMLGN |
370 | 380 | 390 | 400 | ||
PSRLPAKCPG | KGAWSIPWKW | LFGATAVALG | GVALSVVIAA | RN |