2NCA

Structural Model for the N-terminal Domain of Human Cdc37

External Resource: Annotation

Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF03234	e2ncaA1	A: alpha bundles	X: Hsp90 co-chaperone Cdc37 N-terminal domain (From Topology)	H: Hsp90 co-chaperone Cdc37 N-terminal domain (From Topology)	T: Hsp90 co-chaperone Cdc37 N-terminal domain	F: PF03234	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF03234	Cdc37 N terminal kinase binding (CDC37_N)	Cdc37 N terminal kinase binding	Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domain corresponds to the N terminal domain which binds predominantly to protein kinases [2] and is found N terminal to the Hsp (Heat shocked prote ...	Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domain corresponds to the N terminal domain which binds predominantly to protein kinases [2] and is found N terminal to the Hsp (Heat shocked protein) 90-binding domain Pfam:PF08565. Expression of a construct consisting of only the N-terminal domain of Saccharomyces pombe Cdc37 results in cellular viability. This indicates that interactions with the cochaperone Hsp90 may not be essential for Cdc37 function [2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Hsp90 co-chaperone Cdc37	Hsp90 protein binding protein binding binding heat shock protein binding scaffold protein binding protein-folding chaperone binding kinase binding enzyme binding unfolded protein binding protein kinase binding enzyme regulator activity molecular function regulator activity protein kinase regulator activity kinase regulator activity	regulation of protein stability biological regulation regulation of biological quality protein stabilization organonitrogen compound metabolic process cellular biosynthetic process cellular metabolic process primary metabolic process gene expression macromolecule biosynthetic process protein maturation organic substance metabolic process protein folding biosynthetic process regulation of protein stability biological regulation regulation of biological quality protein stabilization organonitrogen compound metabolic process cellular biosynthetic process cellular metabolic process primary metabolic process gene expression macromolecule biosynthetic process protein maturation organic substance metabolic process protein folding biosynthetic process organic substance biosynthetic process metabolic process cellular process protein metabolic process macromolecule metabolic process regulation of biosynthetic process regulation of biological process regulation of cellular process regulation of cellular metabolic process regulation of macromolecule metabolic process regulation of cellular biosynthetic process post-transcriptional regulation of gene expression regulation of gene expression regulation of macromolecule biosynthetic process regulation of metabolic process protein localization localization establishment of protein localization cellular localization protein targeting cellular macromolecule localization macromolecule localization establishment of localization cellular response to stimulus response to organic substance response to stimulus regulation of type I interferon-mediated signaling pathway response to cytokine regulation of signal transduction response to biotic stimulus cell communication interferon-mediated signaling pathway cellular response to type I interferon regulation of immune system process cellular response to cytokine stimulus signal transduction immune response response to other organism regulation of innate immune response response to external stimulus regulation of response to cytokine stimulus regulation of response to stimulus defense response to other organism response to chemical regulation of immune response response to type I interferon regulation of defense response regulation of response to biotic stimulus biological process involved in interspecies interaction between organisms regulation of response to external stimulus signaling cytokine-mediated signaling pathway response to stress regulation of response to stress innate immune response response to external biotic stimulus cellular response to organic substance regulation of signaling cell surface receptor signaling pathway defense response regulation of cytokine-mediated signaling pathway defense response to symbiont cellular response to chemical stimulus immune system process type I interferon-mediated signaling pathway regulation of cell communication catabolic process macroautophagy autophagy cellular catabolic process cellular component organization mitophagy organelle disassembly cellular response to stress cellular component organization or biogenesis process utilizing autophagic mechanism mitochondrion organization cellular component disassembly regulation of autophagy of mitochondrion in response to mitochondrial depolarization organelle organization positive regulation of mitophagy in response to mitochondrial depolarization response to mitochondrial depolarisation positive regulation of autophagy of mitochondrion in response to mitochondrial depolarization autophagy of mitochondrion regulation of protein modification process regulation of catalytic activity regulation of protein phosphorylation regulation of cyclin-dependent protein kinase activity regulation of transferase activity regulation of primary metabolic process regulation of cyclin-dependent protein serine/threonine kinase activity regulation of phosphate metabolic process phosphate-containing compound metabolic process cell cycle phosphorus metabolic process protein modification process regulation of cell cycle protein phosphorylation phosphorylation regulation of protein metabolic process regulation of protein kinase activity regulation of molecular function regulation of kinase activity macromolecule modification regulation of protein serine/threonine kinase activity regulation of phosphorylation regulation of phosphorus metabolic process response to type II interferon regulation of type II interferon-mediated signaling pathway cellular response to type II interferon type II interferon-mediated signaling pathway regulation of response to type II interferon	extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space cellular anatomical entity vesicle extracellular membrane-bounded organelle intracellular anatomical structure cytoplasm cytosol protein-containing complex extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space cellular anatomical entity vesicle extracellular membrane-bounded organelle intracellular anatomical structure cytoplasm cytosol protein-containing complex HSP90-CDC37 chaperone complex protein folding chaperone complex intracellular protein-containing complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR013855	Cdc37, N-terminal domain	Domain
A	IPR004918	Cdc37	Family
A	IPR013874	Cdc37, Hsp90 binding	Domain
A	IPR038189	Cdc37, Hsp90-binding domain superfamily	Homologous Superfamily
A	IPR013873	Cdc37, C-terminal	Domain

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A	Pharos: Q16543	ankylosing spondylitis Hashimoto thyroiditis juvenile idiopathic arthritis ovarian cancer systemic lupus erythematosus Crohn disease hypothyroidism malignant colon neoplasm primary biliary cholangitis systemic sclerosis dermatomyositis inflammatory bowel disease myositis psoriasis ulcerative colitis

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.