Q61081 · CDC37_MOUSE
- ProteinHsp90 co-chaperone Cdc37
- GeneCdc37
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids379 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity. Inhibits HSP90AA1 ATPase activity (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHsp90 co-chaperone Cdc37
- Alternative names
- Cleaved into 1 chains
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ61081
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed; alternate | ||||
Sequence: M | ||||||
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000423198 | 1-379 | Hsp90 co-chaperone Cdc37 | |||
Sequence: MVDYSVWDHIEVSDDEDETHPNIDTASLFRWRHQARVERMEQFQKEKEELDRGCRECKRKVAECQRKLKELEVAESDGQVELERLRAEAQQLRKEERSWEQKLEDMRKKEKNMPWNVDTLSKDGFSKSMVNTKPEKAEEDSEEAREQKHKTFVEKYEKQIKHFGMLHRWDDSQKYLSDNVHLVCEETANYLVIWCIDLEVEEKCALMEQVAHQTMVMQFILELAKSLKVDPRACFRQFFTKIKTADHQYMEGFKYELEAFKERVRGRAKLRIEKAMKEYEEEERKKRLGPGGLDPVEVYESLPEELQKCFDVKDVQMLQDAISKMDPTDAKYHMQRCIDSGLWVPNSKSGEAKEGEEAGPGDPLLEAVPKAGNEKDVSA | ||||||
Modified residue | 2 | N-acetylvaline; in Hsp90 co-chaperone Cdc37, N-terminally processed | ||||
Sequence: V | ||||||
Chain | PRO_0000195058 | 2-379 | Hsp90 co-chaperone Cdc37, N-terminally processed | |||
Sequence: VDYSVWDHIEVSDDEDETHPNIDTASLFRWRHQARVERMEQFQKEKEELDRGCRECKRKVAECQRKLKELEVAESDGQVELERLRAEAQQLRKEERSWEQKLEDMRKKEKNMPWNVDTLSKDGFSKSMVNTKPEKAEEDSEEAREQKHKTFVEKYEKQIKHFGMLHRWDDSQKYLSDNVHLVCEETANYLVIWCIDLEVEEKCALMEQVAHQTMVMQFILELAKSLKVDPRACFRQFFTKIKTADHQYMEGFKYELEAFKERVRGRAKLRIEKAMKEYEEEERKKRLGPGGLDPVEVYESLPEELQKCFDVKDVQMLQDAISKMDPTDAKYHMQRCIDSGLWVPNSKSGEAKEGEEAGPGDPLLEAVPKAGNEKDVSA | ||||||
Modified residue | 13 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 119 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 121 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 155 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 378 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Constitutively sumoylated by UBE2I.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and client protein TSC2 (By similarity).
Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones CDC37, PPP5C, TSC1 and client protein TSC2, CDK4, AKT, RAF1 and NR3C1; this complex does not contain co-chaperones STIP1/HOP and PTGES3/p23 (By similarity).
Forms a complex with Hsp90/HSP90AB1 and CDK6 (By similarity).
Interacts with HSP90AA1 (By similarity).
Interacts with AR, CDK4, CDK6 and EIF2AK1 (By similarity).
Interacts with RB1 (By similarity).
Interacts with KSR1 (PubMed:10409742).
Interacts with FLCN, FNIP1 and FNIP2 (By similarity).
Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones CDC37, PPP5C, TSC1 and client protein TSC2, CDK4, AKT, RAF1 and NR3C1; this complex does not contain co-chaperones STIP1/HOP and PTGES3/p23 (By similarity).
Forms a complex with Hsp90/HSP90AB1 and CDK6 (By similarity).
Interacts with HSP90AA1 (By similarity).
Interacts with AR, CDK4, CDK6 and EIF2AK1 (By similarity).
Interacts with RB1 (By similarity).
Interacts with KSR1 (PubMed:10409742).
Interacts with FLCN, FNIP1 and FNIP2 (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 124-146 | Disordered | ||||
Sequence: GFSKSMVNTKPEKAEEDSEEARE | ||||||
Compositional bias | 132-146 | Basic and acidic residues | ||||
Sequence: TKPEKAEEDSEEARE | ||||||
Region | 344-379 | Disordered | ||||
Sequence: VPNSKSGEAKEGEEAGPGDPLLEAVPKAGNEKDVSA |
Sequence similarities
Belongs to the CDC37 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length379
- Mass (Da)44,593
- Last updated1996-11-01 v1
- Checksum847C146B4FE3AAF1
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1L1STC0 | A0A1L1STC0_MOUSE | Cdc37 | 353 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 132-146 | Basic and acidic residues | ||||
Sequence: TKPEKAEEDSEEARE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U43076 EMBL· GenBank· DDBJ | AAB18761.1 EMBL· GenBank· DDBJ | mRNA | ||
AK010494 EMBL· GenBank· DDBJ | BAB26984.1 EMBL· GenBank· DDBJ | mRNA | ||
AK013255 EMBL· GenBank· DDBJ | BAB28749.1 EMBL· GenBank· DDBJ | mRNA | ||
AK145671 EMBL· GenBank· DDBJ | BAE26580.1 EMBL· GenBank· DDBJ | mRNA | ||
AK168651 EMBL· GenBank· DDBJ | BAE40508.1 EMBL· GenBank· DDBJ | mRNA | ||
BC060079 EMBL· GenBank· DDBJ | AAH60079.1 EMBL· GenBank· DDBJ | mRNA |