cell division cycle 37 homolog (S. cerevisiae); Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity

cell division cycle 37 homolog (S. cerevisiae)-like 1; Co-chaperone that binds to numerous proteins and promotes their interaction with Hsp70 and Hsp90 (By similarity)

cell division cycle 37 homolog (S. cerevisiae); Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity

cyclin-dependent kinase 14

cell division cycle 37 homolog (S. cerevisiae); Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity

cyclin-dependent kinase 20; Required for high-level Shh responses in the developing neural tube. Together with BROMI, controls the structure of the primary cilium by coordinating assembly of the ciliary membrane and axoneme, allowing GLI2 to be properly activated in response to SHH signaling (By similarity). Involved in cell growth. Activates CDK2, a kinase involved in the control of the cell cycle, by phosphorylating residue ’Thr-160’

cell division cycle 37 homolog (S. cerevisiae); Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity

cyclin-dependent kinase 6; Serine/threonine-protein kinase involved in the control of the cell cycle and differentiation; promotes G1/S transition. Phosphorylates pRB/RB1 and NPM1. Interacts with D-type G1 cyclins during interphase at G1 to form a pRB/RB1 kinase and controls the entrance into the cell cycle. Involved in initiation and maintenance of cell cycle exit during cell differentiation; prevents cell proliferation and regulates negatively cell differentiation, but is required for the proliferation of specific cell types (e.g. erythroid and hematopoietic cells). Essential for cel [...]

cell division cycle 37 homolog (S. cerevisiae); Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity

cyclin-dependent kinase 7; Serine/threonine kinase involved in cell cycle control and in RNA polymerase II-mediated RNA transcription. Cyclin- dependent kinases (CDKs) are activated by the binding to a cyclin and mediate the progression through the cell cycle. Each different complex controls a specific transition between 2 subsequent phases in the cell cycle. Required for both activation and complex formation of CDK1/cyclin-B during G2-M transition, and for activation of CDK2/cyclins during G1-S transition (but not complex formation). CDK7 is the catalytic subunit of the CDK-activating [...]

cell division cycle 37 homolog (S. cerevisiae); Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity

heat shock protein 90kDa alpha (cytosolic), class A member 1; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function

cell division cycle 37 homolog (S. cerevisiae); Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity

heat shock protein 90kDa alpha (cytosolic), class B member 1; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function

cell division cycle 37 homolog (S. cerevisiae); Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity

heat shock protein 90kDa beta (Grp94), member 1; Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity

cell division cycle 37 homolog (S. cerevisiae); Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity

mitogen-activated protein kinase kinase kinase 19

cell division cycle 37 homolog (S. cerevisiae); Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity

mitogen-activated protein kinase kinase kinase 2; Component of a protein kinase signal transduction cascade. Regulates the JNK and ERK5 pathways by phosphorylating and activating MAP2K5 and MAP2K7 (By similarity). Plays a role in caveolae kiss-and-run dynamics

cell division cycle 37 homolog (S. cerevisiae); Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity

mitogen-activated protein kinase kinase kinase 3; Component of a protein kinase signal transduction cascade. Mediates activation of the NF-kappa-B, AP1 and DDIT3 transcriptional regulators

cell division cycle 37 homolog (S. cerevisiae); Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity

membrane-spanning 4-domains, subfamily A, member 13; May be involved in signal transduction as a component of a multimeric receptor complex (By similarity)

cell division cycle 37 homolog (S. cerevisiae); Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity

protein phosphatase 5, catalytic subunit; May play a role in the regulation of RNA biogenesis and/or mitosis. In vitro, dephosphorylates serine residues of skeletal muscle phosphorylase and histone H1

cell division cycle 37 homolog (S. cerevisiae); Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity

stress-induced-phosphoprotein 1; Mediates the association of the molecular chaperones HSC70 and HSP90 (HSPCA and HSPCB)

cell division cycle 37 homolog (S. cerevisiae); Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity

SGT1, suppressor of G2 allele of SKP1 (S. cerevisiae); May play a role in ubiquitination and subsequent proteasomal degradation of target proteins

cell division cycle 37 homolog (S. cerevisiae); Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity

suppressor of G2 allele of SKP1 (S. cerevisiae) pseudogene 3

cell division cycle 37 homolog (S. cerevisiae); Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity

TNF receptor-associated protein 1; Chaperone that expresses an ATPase activity

cell division cycle 37 homolog (S. cerevisiae); Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity

tetratricopeptide repeat domain 12

cell division cycle 37 homolog (S. cerevisiae); Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity

tetratricopeptide repeat domain 28

cell division cycle 37 homolog (S. cerevisiae); Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity

tetratricopeptide repeat domain 31