P06101
Gene name |
CDC37 (SMO1, YDR168W, YD9489.03) |
Protein name |
Hsp90 co-chaperone Cdc37 |
Names |
Cell division control protein 37, Hsp90 chaperone protein kinase-targeting subunit |
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YDR168W |
EC number |
|
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for P06101
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P06101-F1 | Predicted | AlphaFoldDB |
7 variants for P06101
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s04-790891 | 189 | K>N | No | SGRP | |
| s04-790928 | 202 | A>T | No | SGRP | |
| s04-791133 | 270 | A>V | No | SGRP | |
| s04-791145 | 274 | K>M | No | SGRP | |
| s04-791269 | 315 | M>I | No | SGRP | |
| s04-791528 | 402 | K>E | No | SGRP | |
| s04-791835 | 504 | T>I | No | SGRP |
No associated diseases with P06101
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| chaperone binding | Binding to a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport. |
| heat shock protein binding | Binding to a heat shock protein, a protein synthesized or activated in response to heat shock. |
| protein kinase binding | Binding to a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate. |
| unfolded protein binding | Binding to an unfolded protein. |
7 GO annotations of biological process
| Name | Definition |
|---|---|
| cell division | The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells. |
| osmosensory signaling MAPK cascade | The series of molecular signals in which a stress-activated protein kinase (SAPK) cascade relays a signal, containing at least a Hog1/Sty1 family MAPK, a Pbs2/Wis1 family MAPKK and a Ssk2/Win1 family MAP3K. |
| positive regulation of MAPK cascade | Any process that activates or increases the frequency, rate or extent of signal transduction mediated by the MAPK cascade. |
| 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 stabilization | Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation. |
| regulation of cell cycle | Any process that modulates the rate or extent of progression through the cell cycle. |
| spindle pole body duplication | Construction of a new spindle pole body. |
7 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q5EAC6 | CDC37 | Hsp90 co-chaperone Cdc37 | Bos taurus (Bovine) | PR |
| O57476 | CDC37 | Hsp90 co-chaperone Cdc37 | Gallus gallus (Chicken) | PR |
| Q24276 | Cdc37 | Hsp90 co-chaperone Cdc37 | Drosophila melanogaster (Fruit fly) | PR |
| Q16543 | CDC37 | Hsp90 co-chaperone Cdc37 | Homo sapiens (Human) | PR |
| Q61081 | Cdc37 | Hsp90 co-chaperone Cdc37 | Mus musculus (Mouse) | PR |
| Q63692 | Cdc37 | Hsp90 co-chaperone Cdc37 | Rattus norvegicus (Rat) | PR |
| A7YY97 | cdc37l1 | Hsp90 co-chaperone Cdc37-like 1 | Danio rerio (Zebrafish) (Brachydanio rerio) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAIDYSKWDK | IELSDDSDVE | VHPNVDKKSF | IKWKQQSIHE | QRFKRNQDIK | NLETQVDMYS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| HLNKRVDRIL | SNLPESSLTD | LPAVTKFLNA | NFDKMEKSKG | ENVDPEIATY | NEMVEDLFEQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LAKDLDKEGK | DSKSPSLIRD | AILKHRAKID | SVTVEAKKKL | DELYKEKNAH | ISSEDIHTGF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DSSFMNKQKG | GAKPLEATPS | EALSSAAESN | ILNKLAKSSV | PQTFIDFKDD | PMKLAKETEE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| FGKISINEYS | KSQKFLLEHL | PIISEQQKDA | LMMKAFEYQL | HGDDKMTLQV | IHQSELMAYI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KEIYDMKKIP | YLNPMELSNV | INMFFEKVIF | NKDKPMGKES | FLRSVQEKFL | HIQKRSKILQ |
| 370 | 380 | 390 | 400 | 410 | 420 |
| QEEMDESNAE | GVETIQLKSL | DDSTELEVNL | PDFNSKDPEE | MKKVKVFKTL | IPEKMQEAIM |
| 430 | 440 | 450 | 460 | 470 | 480 |
| TKNLDNINKV | FEDIPIEEAE | KLLEVFNDID | IIGIKAILEN | EKDFQSLKDQ | YEQDHEDATM |
| 490 | 500 | ||||
| ENLSLNDRDG | GGDNHEEVKH | TADTVD |