CDC37

Summary

CDC37 (cell division cycle 37, HSP90 cochaperone, HGNC:1735) is a protein-coding gene on chromosome 19p13.2, encoding Hsp90 co-chaperone Cdc37 (Q16543). Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity. It is a common-essential gene (DepMap: required in 97.1% of cancer cell lines).

The protein encoded by this gene is highly similar to Cdc 37, a cell division cycle control protein of Sacchromyces cerevisiae. This protein is a molecular chaperone with specific function in cell signal transduction. It has been shown to form complex with Hsp90 and a variety of protein kinases including CDK4, CDK6, SRC, RAF-1, MOK, as well as eIF2 alpha kinases. It is thought to play a critical role in directing Hsp90 to its target kinases.

Source: NCBI Gene 11140 — RefSeq curated summary.

At a glance

• GWAS associations: 6
• Clinical variants (ClinVar): 52 total
• Druggable target: yes
• Cancer dependency (DepMap): dependent in 97.1% of screened cell lines (common-essential)
• MANE Select transcript: NM_007065

Identifiers

Gene identifiers

Field	Value
HGNC ID	HGNC:1735
Approved symbol	CDC37
Name	cell division cycle 37, HSP90 cochaperone
Location	19p13.2
Locus type	gene with protein product
Status	Approved
Aliases	P50CDC37
Ensembl gene	ENSG00000105401
Ensembl biotype	protein_coding
OMIM	605065
Entrez	11140

Gene structure

Transcript identifiers

Ensembl transcripts: 25 — 20 protein_coding, 4 retained_intron, 1 nonsense_mediated_decay

ENST00000222005, ENST00000588498, ENST00000588869, ENST00000589331, ENST00000589625, ENST00000589629, ENST00000589755, ENST00000590632, ENST00000591248, ENST00000593124, ENST00000870150, ENST00000870151, ENST00000937013, ENST00000937014, ENST00000937015, ENST00000937016, ENST00000937017, ENST00000937018, ENST00000963714, ENST00000963715, ENST00000963716, ENST00000963717, ENST00000963718, ENST00000963719, ENST00000963720

RefSeq mRNA: 1 — MANE Select: NM_007065 NM_007065

CCDS: CCDS12237

Canonical transcript exons

ENST00000222005 — 8 exons

Exon	Start	End
ENSE00000676214	10395435	10395543
ENSE00000954374	10391133	10391706
ENSE00002828633	10403378	10403542
ENSE00003465362	10393086	10393157
ENSE00003485924	10395928	10396203
ENSE00003514734	10395021	10395143
ENSE00003590935	10395228	10395343
ENSE00003623103	10393259	10393441

Expression profiles

Bgee: expression breadth ubiquitous, 293 present calls, max score 99.09.

FANTOM5 (CAGE): breadth broad, TPM avg 0.7996 / max 28.7072, expressed in 330 samples.

FANTOM5 promoters (6 alternative TSS)

Promoter ID	TPM avg	Samples expressed
179128	132.7402	1828
179132	0.2808	144
179134	0.2561	113
179133	0.1789	78
179126	0.0590	28
179127	0.0249	15

Top tissues by expression

303 total, by Bgee expression score (0-100, higher = more expressed):

Tissue	Anatomy ID	Expression score	Quality
sural nerve	UBERON:0015488	99.09	gold quality
apex of heart	UBERON:0002098	99.06	gold quality
granulocyte	CL:0000094	98.75	gold quality
lower esophagus mucosa	UBERON:0035834	98.73	gold quality
body of uterus	UBERON:0009853	98.70	gold quality
omental fat pad	UBERON:0010414	98.68	gold quality
left uterine tube	UBERON:0001303	98.67	gold quality
metanephros cortex	UBERON:0010533	98.66	gold quality
upper lobe of left lung	UBERON:0008952	98.65	gold quality
left lobe of thyroid gland	UBERON:0001120	98.63	gold quality
peritoneum	UBERON:0002358	98.62	gold quality
mucosa of stomach	UBERON:0001199	98.59	gold quality
right uterine tube	UBERON:0001302	98.58	gold quality
endocervix	UBERON:0000458	98.56	gold quality
right lobe of thyroid gland	UBERON:0001119	98.56	gold quality
nerve	UBERON:0001021	98.55	gold quality
tibial nerve	UBERON:0001323	98.55	gold quality
right atrium auricular region	UBERON:0006631	98.55	gold quality
stromal cell of endometrium	CL:0002255	98.53	gold quality
right hemisphere of cerebellum	UBERON:0014890	98.53	gold quality
transverse colon	UBERON:0001157	98.50	gold quality
lower esophagus	UBERON:0013473	98.50	gold quality
lower esophagus muscularis layer	UBERON:0035833	98.50	gold quality
esophagogastric junction muscularis propria	UBERON:0035841	98.50	gold quality
right frontal lobe	UBERON:0002810	98.49	gold quality
left ovary	UBERON:0002119	98.47	gold quality
body of stomach	UBERON:0001161	98.45	gold quality
hindlimb stylopod muscle	UBERON:0004252	98.44	gold quality
muscle layer of sigmoid colon	UBERON:0035805	98.44	gold quality
right ovary	UBERON:0002118	98.42	gold quality

Single-cell (SCXA)

Detected in 4 experiment(s), a significant marker in 2.

Experiment	Marker?	Max mean expression
E-HCAD-11	yes	41.84
E-MTAB-6524	no	168.80
E-GEOD-86618	no	147.08
E-ANND-3	no	0.00

Regulation

Is transcription factor: no

Upstream regulators (CollecTRI, top): ETS1

miRNA regulators (miRDB)

14 targeting CDC37, top 30 by miRDB confidence (max_score; target_count = how many genes the miRNA targets in total — lower means more specific):

miRNA	Max score	Avg score	miRNA target_count
HSA-MIR-4776-3P	100.00	68.73	1340
HSA-MIR-8075	99.97	67.20	962
HSA-MIR-4688	99.48	64.68	828
HSA-MIR-6743-5P	99.48	63.60	721
HSA-MIR-1324	99.46	66.57	1302
HSA-MIR-330-3P	99.41	69.95	2521
HSA-MIR-4505	99.27	67.81	2678
HSA-MIR-5787	99.22	67.86	2628
HSA-MIR-503-5P	97.87	66.83	575
HSA-MIR-10526-3P	97.86	64.97	1342
HSA-MIR-6793-3P	97.66	65.78	1084
HSA-MIR-4642	97.52	67.60	916
HSA-MIR-12115	94.19	66.37	738
HSA-MIR-4767	86.06	61.02	43

Functional genomics

DepMap (CRISPR cell-line fitness): dependent in 97.1% of screened cell lines, common-essential.

Literature-anchored findings (GeneRIF, showing 40)

• Tnf-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90. (PMID:11864612)
• role in regulating Hsp90 ATPase activity (PMID:11916974)
• CDC37 binds to Akt and HSP90 in the signal transduction pathway in human tumor cells (PMID:12176997)
• Results show that Cdc37 and heat shock protein 90 bind specifically to the kinase domain of LKB1. (PMID:12489981)
• phosphorylation of Cdc37 on Ser13 is critical for its ability to coordinate Hsp90 nucleotide-mediated conformational switching and kinase binding (PMID:12930845)
• Heteromeric comlpexes containing the molecular chaperones Hsp90 and Cdc37/p50 interacts with the kinase domain of LKB1. (PMID:14668798)
• the interaction of Cdc37 with its client protein kinases requires amino acid residues within a motif that is present in many protein kinases (PMID:14701845)
• Hsp90/p50cdc37 is required for mixed-lineage kinase (MLK) 3 signaling (PMID:15001580)
• the Hsp90.Cdc37 molecular chaperone module has a central role in interleukin-1 receptor-associated-kinase-dependent signaling by toll-like receptors (PMID:15647277)
• Cdc37 is found to heterodimerize with heat-shock protein 90 (Hsp90)-associating relative of Cdc37 (Harc) in vitro. (PMID:15850399)
• Nuclear magnetic resonance study of binding to to HSP90. (PMID:16132836)
• results suggest that a region of Cdc37 other than the client-binding site may be responsible for discriminating client protein kinases from others (PMID:16156789)
• JAK1/2 are client proteins of Hsp90 alpha and beta; Hsp90 and CDC37 play a critical role in types I and II interferon pathways (PMID:16280321)
• N-terminal glycine-rich loop of protein kinases is essential for physically associating with Cdc37. (PMID:16611982)
• The data shows the expression and purification of an Hsp90-Cdc37-Cdk4 complex, defining its stoichiometry, and determining its 3D structure by single-particle electron microscopy. (PMID:16949366)
• these observations support the hypothesis that there is a specific coordination between the activation of the cytosolic Ah receptor and the c-Src- and cdc37-containing HSP90 complex. (PMID:17223712)
• The present data denote Hsp90-Cdc37 as a transiently acting essential regulatory component of IKK signaling. (PMID:17728246)
• identify Pink1 as a novel Cdc37/Hsp90 client kinase (PMID:18003639)
• Cdc37 is essential for maintaining prostate tumor cell growth and may represent a novel target in the search for multitargeted therapies. (PMID:18089825)
• These data reveal a cyclic regulatory mechanism for Cdc37, in which its constitutive phosphorylation is reversed by targeted dephosphorylation in Hsp90 complexes. (PMID:18922470)
• CDC37 in concert with HSP90 plays an essential role in maintaining oncogenic protein kinase clients including ERBB2, CRAF, CDK4, CDK6, & phosphorylated AKT. (PMID:18931700)
• The human Cdc37.Hsp90 complex studied by heteronuclear NMR spectroscopy. (PMID:19073599)
• C-terminal tail and determinants in the alphaE-helix of the catalytic domain allows the chaperones Hsp90 and Cdc37 to bind newly synthesized PKC beta II, a required event in the processing of PKC by phosphorylation (PMID:19091746)
• celastrol may represent a new class of Hsp90 inhibitor by modifying Hsp90 C terminus to allosterically regulate its chaperone activity and disrupt Hsp90-Cdc37 complex. (PMID:19858214)
• Hsp90-Cdc37 complex acta as an endogenous regulator of noncanonical p38alpha activity. (PMID:20299663)
• the Hsp90 kinase co-chaperone Cdc37 regulates tau stability and phosphorylation dynamics (PMID:21367866)
• The primary mechanisms by which apigenin kill multiple myeloma cells is by targeting the trinity of CK2-Cdc37-Hsp90. (PMID:21871133)
• Cdc37-mediated direct interaction between Hsp90/Cdc37 and an IRE1alpha cytosolic motif is important to maintain basal IRE1alpha activity and contributes to normal protein homeostasis and unfolded protein response under physiological stimulation. (PMID:22199355)
• Data show that part of the normal clearance cascade for TDP-43 involves the Cdc37/Hsp90 complex. (PMID:22674575)
• A series of tyrosine phosphorylation events, involving both p50(Cdc37) and Hsp90, are minimally sufficient to provide directionality to the chaperone cycle. (PMID:22727666)
• an essential role for surface Cdc37 in concert with HSP90 on the cell surface during cancer cell invasion processes (PMID:22912728)
• analysis of a novel interaction between the co-chaperone Cdc37 and Rho GTPase exchange factor Vav3 promotes androgen receptor activity and prostate cancer growth (PMID:23281476)
• ERK5 interacts with the Hsp90-Cdc37 chaperone in resting cells, and inhibition of Hsp90 or Cdc37 results in ERK5 ubiquitylation and proteasomal degradation. (PMID:23428871)
• Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein 90) motility by interaction with N-terminal and middle domain binding sites. (PMID:23569206)
• CDC37 is a crucial HSP90-cofactor for KIT oncogenic expression in gastrointestinal stromal tumors (PMID:23584476)
• CDC37 has an important role in chaperoning protein kinases; it stabilizes kinase clients by a mechanism that is not dependent on a substantial direct interaction between CDC37 and HSP90, but requires HSP90 activity (PMID:24292678)
• SGK3 stability and kinase activation are regulated by the Hsp90-Cdc37 chaperone complex. (PMID:24379398)
• Correlation between PDZK1, Cdc37, Akt and breast cancer malignancy: the role of PDZK1 in cell growth through Akt stabilization by increasing and interacting with Cdc37 (PMID:24869908)
• As a novel Hsp90 inhibitor, FW-04-806 binds to the N-terminal of Hsp90 and inhibits Hsp90/Cdc37 interaction, resulting in the disassociation of Hsp90/Cdc37/client complexes and the degradation of Hsp90 client proteins. (PMID:24927996)
• Suppressing expression of the cochaperone CDC37 in hepatocellular carcinoma cells inhibits cell cycle progression and cell growth. (PMID:25098386)

Cross-species orthologs

6 orthologs

Organism	Symbol	Gene ID
danio_rerio	cdc37	ENSDARG00000099301
mus_musculus	Cdc37	ENSMUSG00000019471
rattus_norvegicus	Cdc37	ENSRNOG00000033426
drosophila_melanogaster	Cdc37	FBGN0011573
caenorhabditis_elegans		WBGENE00019497
caenorhabditis_elegans		WBGENE00021097

Paralogs (1): CDC37L1 (ENSG00000106993)

Protein

Protein identifiers

Hsp90 co-chaperone Cdc37 — Q16543 (reviewed: Q16543)

Alternative names: Hsp90 chaperone protein kinase-targeting subunit, p50Cdc37

All UniProt accessions (6): Q16543, K7EIU0, K7EJ06, K7EKQ2, K7EL68, K7EQA9

UniProt curated annotations — full annotation on UniProt →

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.

Subunit / interactions. Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and client protein TSC2. 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. Forms a complex with Hsp90/HSP90AB1 and CDK6. Interacts with HSP90AA1. Interacts with AR, CDK4, CDK6 and EIF2AK1. Interacts with RB1. Interacts with KSR1. Interacts with FLCN, FNIP1 and FNIP2.

Subcellular location. Cytoplasm.

Post-translational modifications. Constitutively sumoylated by UBE2I.

Similarity. Belongs to the CDC37 family.

RefSeq proteins (1): NP_008996* (*=MANE)

Domains & families (InterPro)

ID	Name	Type
IPR004918	Cdc37	Family
IPR013855	Cdc37_N_dom	Domain
IPR013873	Cdc37_C	Domain
IPR013874	Cdc37_Hsp90-bd	Domain
IPR038189	Cdc37_Hsp90-bd_sf	Homologous_superfamily

Pfam: PF03234, PF08564, PF08565

UniProt features (36 total): helix 15, modified residue 8, strand 6, chain 2, region of interest 2, initiator methionine 1, sequence variant 1, turn 1

Structure

Experimental structures (PDB)

19 structures.

PDB	Method	Resolution (Å)
2W0G	X-RAY DIFFRACTION	1.88
5HPE	X-RAY DIFFRACTION	2.27
1US7	X-RAY DIFFRACTION	2.3
9KQN	ELECTRON MICROSCOPY	2.84
7Z38	ELECTRON MICROSCOPY	3.16
8GAE	ELECTRON MICROSCOPY	3.3
7ZR0	ELECTRON MICROSCOPY	3.4
7Z37	ELECTRON MICROSCOPY	3.67
8U1L	ELECTRON MICROSCOPY	3.7
8GFT	ELECTRON MICROSCOPY	3.8
5FWK	ELECTRON MICROSCOPY	3.9
7ZR5	ELECTRON MICROSCOPY	3.9
7ZR6	ELECTRON MICROSCOPY	4.2
5FWP	ELECTRON MICROSCOPY	7.2
5FWM	ELECTRON MICROSCOPY	8
5FWL	ELECTRON MICROSCOPY	9
2K5B	SOLUTION NMR
2N5X	SOLUTION NMR
2NCA	SOLUTION NMR

Predicted structure (AlphaFold)

Model	pLDDT	Fraction very-high
AF-Q16543-F1	81.83	0.38

Functional residue map

Curated UniProt residues grouped by drug-discovery relevance — catalytic, ligand-binding, modification, and mutation-validated positions. Source: UniProtKB sequence features.

Post-translational modifications (8): 120, 154, 377, 1, 2, 13, 78, 118

Function

Pathways and Gene Ontology

Reactome pathways

36 pathways

ID	Pathway
R-HSA-1227986	Signaling by ERBB2
R-HSA-1236382	Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants
R-HSA-5637810	Constitutive Signaling by EGFRvIII
R-HSA-5675482	Regulation of necroptotic cell death
R-HSA-8863795	Downregulation of ERBB2 signaling
R-HSA-9013418	RHOBTB2 GTPase cycle
R-HSA-9634285	Constitutive Signaling by Overexpressed ERBB2
R-HSA-9652282	Drug-mediated inhibition of ERBB2 signaling
R-HSA-9664565	Signaling by ERBB2 KD Mutants
R-HSA-9665233	Resistance of ERBB2 KD mutants to trastuzumab
R-HSA-9665244	Resistance of ERBB2 KD mutants to sapitinib
R-HSA-9665245	Resistance of ERBB2 KD mutants to tesevatinib
R-HSA-9665246	Resistance of ERBB2 KD mutants to neratinib
R-HSA-9665247	Resistance of ERBB2 KD mutants to osimertinib
R-HSA-9665249	Resistance of ERBB2 KD mutants to afatinib
R-HSA-9665250	Resistance of ERBB2 KD mutants to AEE788
R-HSA-9665251	Resistance of ERBB2 KD mutants to lapatinib
R-HSA-9665348	Signaling by ERBB2 ECD mutants
R-HSA-9665686	Signaling by ERBB2 TMD/JMD mutants
R-HSA-9665737	Drug resistance in ERBB2 TMD/JMD mutants
R-HSA-1227990	Signaling by ERBB2 in Cancer
R-HSA-162582	Signal Transduction
R-HSA-1643685	Disease
R-HSA-1643713	Signaling by EGFR in Cancer
R-HSA-194315	Signaling by Rho GTPases
R-HSA-5213460	RIPK1-mediated regulated necrosis
R-HSA-5218859	Regulated Necrosis
R-HSA-5357801	Programmed Cell Death
R-HSA-5637812	Signaling by EGFRvIII in Cancer
R-HSA-5637815	Signaling by Ligand-Responsive EGFR Variants in Cancer

MSigDB gene sets: 234 (showing top): GSE45365_NK_CELL_VS_BCELL_DN, GOBP_REGULATION_OF_AUTOPHAGY, GOBP_REGULATION_OF_PHOSPHORYLATION, GOBP_RESPONSE_TO_PEPTIDE, MODULE_151, ENK_UV_RESPONSE_KERATINOCYTE_UP, CGGAARNGGCNG_UNKNOWN, GRAESSMANN_APOPTOSIS_BY_SERUM_DEPRIVATION_DN, GRAESSMANN_RESPONSE_TO_MC_AND_SERUM_DEPRIVATION_DN, MORF_HDAC1, GOBP_RESPONSE_TO_TYPE_I_INTERFERON, GOBP_PROTEIN_TARGETING, GOBP_REGULATION_OF_TRANSFERASE_ACTIVITY, GOBP_MACROAUTOPHAGY, GOBP_POST_TRANSCRIPTIONAL_REGULATION_OF_GENE_EXPRESSION

GO Biological Process (8): regulation of cyclin-dependent protein serine/threonine kinase activity (GO:0000079), protein folding (GO:0006457), protein targeting (GO:0006605), post-transcriptional regulation of gene expression (GO:0010608), protein stabilization (GO:0050821), regulation of type II interferon-mediated signaling pathway (GO:0060334), regulation of type I interferon-mediated signaling pathway (GO:0060338), positive regulation of type 2 mitophagy (GO:1905091)

GO Molecular Function (9): protein kinase regulator activity (GO:0019887), kinase binding (GO:0019900), protein kinase binding (GO:0019901), heat shock protein binding (GO:0031072), obsolete unfolded protein binding (GO:0051082), protein-folding chaperone binding (GO:0051087), Hsp90 protein binding (GO:0051879), scaffold protein binding (GO:0097110), protein binding (GO:0005515)

GO Cellular Component (5): cytoplasm (GO:0005737), cytosol (GO:0005829), extracellular exosome (GO:0070062), protein folding chaperone complex (GO:0101031), HSP90-CDC37 chaperone complex (GO:1990565)

Reactome top-level categories

Rollup of top-8 pathways:

Category	Pathways
Drug resistance in ERBB2 KD mutants	8
Signaling by ERBB2 in Cancer	5
Signaling by ERBB2	2
Signaling by Receptor Tyrosine Kinases	1
Signaling by Ligand-Responsive EGFR Variants in Cancer	1
Signaling by EGFRvIII in Cancer	1
RIPK1-mediated regulated necrosis	1
RHOBTB GTPase Cycle	1

GO top-level categories

Rollup of top GO terms by namespace:

Category	Terms
protein binding	3
regulation of cytokine-mediated signaling pathway	2
cellular anatomical structure	2
cytoplasm	2
cyclin-dependent protein serine/threonine kinase activity	1
regulation of protein serine/threonine kinase activity	1
cellular process	1
protein maturation	1
establishment of protein localization	1
regulation of gene expression	1
regulation of protein stability	1
regulation of response to type II interferon	1
type II interferon-mediated signaling pathway	1
regulation of innate immune response	1
type I interferon-mediated signaling pathway	1
type 2 mitophagy	1
positive regulation of mitophagy	1
regulation of type 2 mitophagy	1
protein kinase activity	1
kinase regulator activity	1
protein kinase binding	1
enzyme binding	1
kinase binding	1
heat shock protein binding	1
binding	1
intracellular anatomical structure	1
extracellular vesicle	1
intracellular protein-containing complex	1
protein folding chaperone complex	1

Protein interactions and networks

STRING

2617 interactions, top by confidence (×1000):

Protein A	Protein B	Partner UniProt	Score
CDC37	HSP90AA1	P07900	999
CDC37	HSP90AB1	P08238	998
CDC37	CDK4	P11802	996
CDC37	HSPA4	P34932	994
CDC37	PTGES3	Q15185	948
CDC37	AHSA1	O95433	935
CDC37	PINK1	Q9BXM7	910
CDC37	DNAJB1	P25685	900
CDC37	CDK6	Q00534	883
CDC37	STIP1	P31948	881
CDC37	CHUK	O15111	871
CDC37	PPID	Q08752	855
CDC37	EZR	P15311	853
CDC37	AKT1	P31749	833
CDC37	PPP5C	P53041	824

IntAct

1028 interactions, top by confidence:

A	B	Type	Score
IKBKG	IKBKB	psi-mi:“MI:0914”(association)	0.980
PRKAA1	PRKAB2	psi-mi:“MI:0914”(association)	0.950
CDC37	HSP90AB1	psi-mi:“MI:0915”(physical association)	0.930
PPP2R1A	STRN	psi-mi:“MI:0914”(association)	0.880
PPP2R1A	STRN	psi-mi:“MI:2364”(proximity)	0.880
MAP2K5	MAPK7	psi-mi:“MI:0914”(association)	0.860
CDC37	IKBKB	psi-mi:“MI:0914”(association)	0.850
CDK8	MED19	psi-mi:“MI:2364”(proximity)	0.850
CDK8	MED19	psi-mi:“MI:0914”(association)	0.850
RAF1	RAF1	psi-mi:“MI:0914”(association)	0.810
SRC	CDC37	psi-mi:“MI:0915”(physical association)	0.710
PPP5C	IRS4	psi-mi:“MI:0914”(association)	0.570
AURKB	SEC16A	psi-mi:“MI:2364”(proximity)	0.570
AURKB	SEC16A	psi-mi:“MI:0914”(association)	0.570
CEP104	CCDC66	psi-mi:“MI:2364”(proximity)	0.540
KSR2	POLR3A	psi-mi:“MI:0914”(association)	0.530
PSKH2	UNC119B	psi-mi:“MI:0914”(association)	0.530
YES1	AIP	psi-mi:“MI:0914”(association)	0.530
ITK	GAPDHS	psi-mi:“MI:0914”(association)	0.530
PTK6	CDC37	psi-mi:“MI:0915”(physical association)	0.500

BioGRID (1128): CDC37 (Affinity Capture-Western), CDC37 (Affinity Capture-Western), CDC37 (Affinity Capture-Western), CDC37 (Affinity Capture-RNA), CDC37 (Affinity Capture-RNA), CDC37 (Reconstituted Complex), CDC37 (Reconstituted Complex), CDC37 (Co-fractionation), CDC37 (Affinity Capture-MS), CDC37 (Affinity Capture-MS), CDC37 (Affinity Capture-MS), CDC37 (Affinity Capture-MS), CDC37 (Affinity Capture-MS), CDC37 (Affinity Capture-MS), CDC37 (Affinity Capture-MS)

ESM2 similar proteins: A0A1S4D1D3, A0A1W2PR95, A1D9I5, A5D796, A7SD85, B0W6N3, D2K8N5, E1C760, E7EXT2, F7AEX0, O08836, O57476, P51951, P54729, P78318, P92948, Q0CU99, Q16543, Q16891, Q173M7, Q1DM35, Q2PIU8, Q2QY04, Q3ZC62, Q4V8E4, Q4W9M7, Q5AXH3, Q5EAC6, Q5M990, Q5PQS7, Q61081, Q61249, Q63692, Q6PID6, Q7SYB2, Q8C6E0, Q8CAQ8, Q8LDQ4, Q8R3N6, Q93VM9

Diamond homologs: A6H754, A7YY97, O57476, Q16543, Q24276, Q24740, Q28HY7, Q5EAC6, Q5RA87, Q5XIC3, Q61081, Q63692, Q7L3B6, Q9CZP7, Q9DGQ7, O02108, O94740, P06101, Q8X1E6

SIGNOR signaling

4 interactions.

A	Effect	B	Mechanism
PPP5C	“down-regulates activity”	CDC37	dephosphorylation
ULK1	“down-regulates activity”	CDC37	phosphorylation
CSNK2A1	“up-regulates activity”	CDC37	phosphorylation
CSNK2A2	“up-regulates activity”	CDC37	phosphorylation

Enriched among interaction partners

Reactome pathways and GO biological processes over-represented among this gene’s 174 IntAct physical interaction partners (hypergeometric vs the genome-wide background, BH-FDR, gene-set size 15–500, ranked by fold). A functional readout of the neighbourhood — distinct from this gene’s own memberships above, and biased toward well-studied / hub proteins, so read it as themes rather than proof.

Reactome pathways:

Pathway	Partners	Fold	FDR
Co-inhibition by CTLA4	5	23.2×	9e-05
Signaling by RAS mutants	6	22.7×	2e-05
Co-stimulation by CD28	6	20.4×	2e-05
Signaling by RAF1 mutants	7	17.4×	2e-05
Signaling by high-kinase activity BRAF mutants	6	17.0×	6e-05
Signaling by moderate kinase activity BRAF mutants	7	15.9×	2e-05
Paradoxical activation of RAF signaling by kinase inactive BRAF	7	15.9×	2e-05
Signaling downstream of RAS mutants	7	15.9×	2e-05

GO biological processes:

GO term	Partners	Fold	FDR
obsolete positive regulation of NF-kappaB transcription factor activity	8	10.5×	4e-04
MAPK cascade	7	6.9×	9e-03
T cell receptor signaling pathway	7	6.8×	9e-03
regulation of apoptotic process	12	6.4×	2e-04
protein phosphorylation	14	6.1×	1e-04
positive regulation of canonical NF-kappaB signal transduction	12	5.6×	5e-04
intracellular signal transduction	15	3.7×	4e-03

Disease & clinical

Clinical variants and AI predictions

ClinVar

52 variants total. Per-class counts are floors (≥ shown; pagination cap):

Classification	Count (floor)
Pathogenic	0
Likely pathogenic	0
Uncertain significance	42
Likely benign	0
Benign	3

Top pathogenic / likely-pathogenic (0)

SpliceAI

843 predictions. Top by Δscore:

Variant	Effect	Δscore
19:10393080:A:AC	donor_gain	1.0000
19:10393080:ACTC:A	donor_loss	1.0000
19:10393081:C:CC	donor_gain	1.0000
19:10393082:TCA:T	donor_loss	1.0000
19:10393083:CACG:C	donor_loss	1.0000
19:10393084:A:AC	donor_gain	1.0000
19:10393084:A:T	donor_loss	1.0000
19:10393085:C:CC	donor_gain	1.0000
19:10393085:CG:C	donor_gain	1.0000
19:10393085:CGG:C	donor_gain	1.0000
19:10393085:CGGT:C	donor_gain	1.0000
19:10393085:CGGTG:C	donor_gain	1.0000
19:10393153:AGTTC:A	acceptor_gain	1.0000
19:10393154:GTTC:G	acceptor_gain	1.0000
19:10393155:TTC:T	acceptor_gain	1.0000
19:10393156:TC:T	acceptor_gain	1.0000
19:10393157:CC:C	acceptor_gain	1.0000
19:10393157:CCTG:C	acceptor_loss	1.0000
19:10393158:C:CC	acceptor_gain	1.0000
19:10393159:T:A	acceptor_loss	1.0000
19:10393164:G:C	acceptor_gain	1.0000
19:10393164:G:GC	acceptor_gain	1.0000
19:10393253:CCCCA:C	donor_loss	1.0000
19:10393438:CTGT:C	acceptor_gain	1.0000
19:10393438:CTGTC:C	acceptor_loss	1.0000
19:10393439:TGT:T	acceptor_gain	1.0000
19:10393441:TC:T	acceptor_loss	1.0000
19:10393442:C:CC	acceptor_gain	1.0000
19:10393442:CTATG:C	acceptor_loss	1.0000
19:10393443:T:A	acceptor_loss	1.0000

AlphaMissense

2546 scored. Top likely-pathogenic:

Variant	Protein change	am_pathogenicity
19:10391662:C:A	W342C	1.000
19:10391662:C:G	W342C	1.000
19:10391664:A:G	W342R	1.000
19:10391664:A:T	W342R	1.000
19:10391666:A:G	L341P	1.000
19:10391666:A:T	L341H	1.000
19:10391669:C:A	G340V	1.000
19:10391669:C:T	G340D	1.000
19:10391670:C:G	G340R	1.000
19:10391672:G:A	S339F	1.000
19:10391673:A:G	S339P	1.000
19:10391680:G:C	C336W	1.000
19:10391681:C:T	C336Y	1.000
19:10391682:A:G	C336R	1.000
19:10391684:C:G	R335P	1.000
19:10393105:A:T	I321N	1.000
19:10393117:A:G	L317P	1.000
19:10393117:A:T	L317Q	1.000
19:10393140:G:C	F309L	1.000
19:10393140:G:T	F309L	1.000
19:10393141:A:C	F309C	1.000
19:10393141:A:G	F309S	1.000
19:10393142:A:G	F309L	1.000
19:10393266:A:G	L301P	1.000
19:10393266:A:T	L301H	1.000
19:10393368:G:T	A267D	1.000
19:10393380:A:T	V263E	1.000
19:10393384:G:T	R262S	1.000
19:10393401:A:G	L256P	1.000
19:10393412:G:C	F252L	1.000

dbSNP variants (sampled 300 via entrez): RS1000169834 (19:10402298 C>T), RS1000430938 (19:10399568 G>A), RS1000888151 (19:10401998 T>C,G), RS1001004712 (19:10395831 G>A,C,T), RS1001005806 (19:10401637 G>T), RS1001243346 (19:10401127 C>A,T), RS1001388512 (19:10396864 T>G), RS1001482629 (19:10396064 A>C), RS1001515305 (19:10390709 T>C,G), RS1001621897 (19:10403268 G>A,C,T), RS1001898304 (19:10391380 C>T), RS1002231736 (19:10400610 G>A,C), RS1002865562 (19:10394573 G>A,T), RS1002901089 (19:10397580 T>C), RS1002902363 (19:10404705 G>A,C)

Disease associations

OMIM: gene MIM:605065 | disease phenotypes: MIM:611521

GenCC curated gene-disease

Mondo (1): immunodeficiency 35 (MONDO:0012682)

Orphanet (1): Susceptibility to infection due to TYK2 deficiency (Orphanet:331226)

HPO phenotypes

0 total (0 of 0 shown, HPO-id order):

GWAS associations

6 associations (top):

Study	Trait	p-value
GCST001198_11	Multiple sclerosis	1.000000e-06
GCST004131_88	Inflammatory bowel disease	2.000000e-11
GCST004132_111	Crohn’s disease	3.000000e-13
GCST011741_22	LDL cholesterol levels in HIV infection	9.000000e-06
GCST011741_6	LDL cholesterol levels in HIV infection	9.000000e-06
GCST90002407_361	White blood cell count	1.000000e-13

EFO canonical traits (1, from GWAS)

EFO ID	Trait name
EFO:0004611	low density lipoprotein cholesterol measurement

MeSH disease descriptors (1)

Descriptor	Name	Tree numbers
C566928	Tyrosine Kinase 2 Deficiency (supp.)

Drugs & pharmacology

Drug and pharmacology data

Is drug target: yes

ChEMBL targets (3): CHEMBL1795123 (SINGLE PROTEIN), CHEMBL4296080 (PROTEIN COMPLEX), CHEMBL4296081 (PROTEIN COMPLEX)

PharmGKB: 1 entry (VIP=true, CPIC=false)

Binding affinities (BindingDB)

33 measured of 35 human assays (35 total across all organisms); most potent 33 below. Values come from heterogeneous assays and are not directly comparable.

Ligand	Measure	Value	Patent
2-fluoro-8-[(6-iodo-1,3-benzodioxol-5-yl)methyl]-9-[2-(2-methylpropylamino)ethyl]purin-6-amine	EC50	19.6 nM	US-10336757: Treatment of neurodegenerative diseases through inhibition of HSP90
9-[2-(2,2-dimethylpropylamino)ethyl]-2-fluoro-8-[(6-iodo-1,3-benzodioxol-5-yl)methyl]purin-6-amine	EC50	23.5 nM	US-10336757: Treatment of neurodegenerative diseases through inhibition of HSP90
8-[(6-IODO-1,3-BENZODIOXOL-5-YL)THIO]-9-[3-(ISOPROPYLAMINO)PROPYL]-9H-PURIN-6-AMINE	EC50	30.8 nM	US-10336757: Treatment of neurodegenerative diseases through inhibition of HSP90
9-[2-(cyclopropylmethylamino)ethyl]-2-fluoro-8-[(6-iodo-1,3-benzodioxol-5-yl)methyl]purin-6-amine	EC50	35.6 nM	US-10336757: Treatment of neurodegenerative diseases through inhibition of HSP90
2-fluoro-8-[(6-iodo-1,3-benzodioxol-5-yl)methyl]-9-[3-[methyl(propan-2-yl)amino]propyl]purin-6-amine	EC50	39.4 nM	US-10336757: Treatment of neurodegenerative diseases through inhibition of HSP90
9-[3-[cyclopropyl(propyl)amino]propyl]-2-fluoro-8-[(6-iodo-1,3-benzodioxol-5-yl)methyl]purin-6-amine	EC50	42.8 nM	US-10336757: Treatment of neurodegenerative diseases through inhibition of HSP90
2-fluoro-8-[(6-iodo-1,3-benzodioxol-5-yl)methyl]-9-[3-[methyl(prop-2-enyl)amino]propyl]purin-6-amine	EC50	44.5 nM	US-10336757: Treatment of neurodegenerative diseases through inhibition of HSP90
2-fluoro-8-(6-iodo-benzo[1,3]dioxol-5-ylmethyl)-9-(3-isopropylamino-propyl)adenine	EC50	60.7 nM	US-10336757: Treatment of neurodegenerative diseases through inhibition of HSP90
2-[3-[6-amino-2-fluoro-8-[(6-iodo-1,3-benzodioxol-5-yl)methyl]purin-9-yl]propyl-propan-2-ylamino]ethanol	EC50	60.8 nM	US-10336757: Treatment of neurodegenerative diseases through inhibition of HSP90
2-fluoro-8-[(6-iodo-1,3-benzodioxol-5-yl)methyl]-9-(3-piperidin-1-ylpropyl)purin-6-amine	EC50	68.2 nM	US-10336757: Treatment of neurodegenerative diseases through inhibition of HSP90
2-fluoro-8-[(6-iodo-1,3-benzodioxol-5-yl)methyl]-9-[2-[methyl(propan-2-yl)amino]ethyl]purin-6-amine	EC50	92.3 nM	US-10336757: Treatment of neurodegenerative diseases through inhibition of HSP90
3-[6-amino-2-fluoro-8-[(6-iodo-1,3-benzodioxol-5-yl)methyl]purin-9-yl]propyl-trimethylazanium	EC50	95.3 nM	US-10336757: Treatment of neurodegenerative diseases through inhibition of HSP90
2-fluoro-8-[(6-iodo-1,3-benzodioxol-5-yl)methyl]-9-[3-(2-methylaziridin-1-yl)propyl]purin-6-amine	EC50	105 nM	US-10336757: Treatment of neurodegenerative diseases through inhibition of HSP90
2-[2-[6-amino-2-fluoro-8-[(6-iodo-1,3-benzodioxol-5-yl)methyl]purin-9-yl]ethyl-methylamino]acetonitrile	EC50	107 nM	US-10336757: Treatment of neurodegenerative diseases through inhibition of HSP90
8-(6-bromo-benzo[1,3]dioxol-5-ylsulfanyl)-9-(3-isopropylamino-propyl)adenine	EC50	122 nM	US-10336757: Treatment of neurodegenerative diseases through inhibition of HSP90
8-[(6-ethenyl-1,3-benzodioxol-5-yl)methyl]-2-fluoro-9-[3-(propan-2-ylamino)propyl]purin-6-amine	EC50	147 nM	US-10336757: Treatment of neurodegenerative diseases through inhibition of HSP90
9-[2-[ethyl(methyl)amino]ethyl]-2-fluoro-8-[(6-iodo-1,3-benzodioxol-5-yl)methyl]purin-6-amine	EC50	166 nM	US-10336757: Treatment of neurodegenerative diseases through inhibition of HSP90
8-[(6-bromo-1,3-benzodioxol-5-yl)methyl]-2-fluoro-9-[3-(propan-2-ylamino)propyl]purin-6-amine	EC50	193 nM	US-10336757: Treatment of neurodegenerative diseases through inhibition of HSP90
2-[4-[3-[6-amino-2-fluoro-8-[(6-iodo-1,3-benzodioxol-5-yl)methyl]purin-9-yl]propyl]piperazin-1-yl]ethanol	EC50	199 nM	US-10336757: Treatment of neurodegenerative diseases through inhibition of HSP90
2-fluoro-8-[(6-iodo-1,3-benzodioxol-5-yl)methyl]-9-(3-morpholin-4-ylpropyl)purin-6-amine	EC50	202 nM	US-10336757: Treatment of neurodegenerative diseases through inhibition of HSP90
2-fluoro-8-[(6-iodo-1,3-benzodioxol-5-yl)methyl]-9-[3-[methyl(prop-2-ynyl)amino]propyl]purin-6-amine	EC50	210 nM	US-10336757: Treatment of neurodegenerative diseases through inhibition of HSP90
8-[(6-ethenyl-1,3-benzodioxol-5-yl)sulfanyl]-9-[3-(propan-2-ylamino)propyl]purin-6-amine	EC50	213 nM	US-10336757: Treatment of neurodegenerative diseases through inhibition of HSP90
2-fluoro-8-[(6-iodo-1,3-benzodioxol-5-yl)methyl]-9-[2-(propan-2-ylamino)ethyl]purin-6-amine	EC50	219 nM	US-10336757: Treatment of neurodegenerative diseases through inhibition of HSP90
2-[(6-bromo-1,3-benzodioxol-5-yl)sulfanyl]-1-pent-4-ynylimidazo[4,5-c]pyridin-4-amine	IC50	550 nM	US-10035797: Fused amino pyridine as HSP90 inhibitors
2-[(6-chloro-1,3-benzodioxol-5-yl)sulfanyl]-1-pent-4-ynylimidazo[4,5-c]pyridin-4-amine	IC50	550 nM	US-10035797: Fused amino pyridine as HSP90 inhibitors
2-[(6-iodo-1,3-benzodioxol-5-yl)sulfanyl]-1-pent-4-ynylimidazo[4,5-c]pyridin-4-amine	IC50	550 nM	US-10035797: Fused amino pyridine as HSP90 inhibitors
2-(2-iodo-5-methoxyphenyl)sulfanyl-1-pent-4-ynylimidazo[4,5-c]pyridin-4-amine	IC50	550 nM	US-10035797: Fused amino pyridine as HSP90 inhibitors
1-[2-(2,2-dimethylpropylamino)ethyl]-2-[(6-iodo-1,3-benzodioxol-5-yl)sulfanyl]imidazo[4,5-c]pyridin-4-amine	IC50	550 nM	US-10035797: Fused amino pyridine as HSP90 inhibitors
8-[(6-ethyl-1,3-benzodioxol-5-yl)methyl]-2-fluoro-9-[3-(propan-2-ylamino)propyl]purin-6-amine	EC50	813 nM	US-10336757: Treatment of neurodegenerative diseases through inhibition of HSP90
2-(2-bromo-5-methoxyphenyl)sulfanyl-1-pent-4-ynylimidazo[4,5-c]pyridin-4-amine	IC50	5500 nM	US-10035797: Fused amino pyridine as HSP90 inhibitors
2-(2-chloro-5-methoxyphenyl)sulfanyl-1-pent-4-ynylimidazo[4,5-c]pyridin-4-amine	IC50	5500 nM	US-10035797: Fused amino pyridine as HSP90 inhibitors
1-[2-(4-amino-1-pent-4-ynylimidazo[4,5-c]pyridin-2-yl)sulfanyl-4-methoxyphenyl]ethanone	IC50	5500 nM	US-10035797: Fused amino pyridine as HSP90 inhibitors
2-fluoro-9-[3-(propan-2-ylamino)propyl]-8-[(6-prop-2-enyl-1,3-benzodioxol-5-yl)methyl]purin-6-amine	EC50	9560 nM	US-10336757: Treatment of neurodegenerative diseases through inhibition of HSP90

ChEMBL bioactivities

18 potent at pChembl≥5 of 18 total, top 18 by pChembl (potency: 10 = 0.1 nM, 6 = 1 µM).

pChembl	Type	Value	Unit	Molecule
8.06	Kd	8.706	nM	CHEMBL5653589
8.06	ED50	8.706	nM	CHEMBL5653589
6.26	IC50	550	nM	CHEMBL5822873
6.26	IC50	550	nM	CHEMBL5789714
6.26	IC50	550	nM	CHEMBL5980387
6.26	IC50	550	nM	CHEMBL5960149
5.77	IC50	1700	nM	CHEMBL4782984
5.62	IC50	2400	nM	CHEMBL1170915
5.54	IC50	2900	nM	CHEMBL4789502
5.45	Kd	3549	nM	CHEMBL3752910
5.45	ED50	3549	nM	CHEMBL3752910
5.26	IC50	5500	nM	CHEMBL6055898
5.26	IC50	5500	nM	CHEMBL5807031
5.26	IC50	5500	nM	CHEMBL5860304
5.26	IC50	5500	nM	CHEMBL5769227
5.21	IC50	6200	nM	CHEMBL4758598
5.17	IC50	6700	nM	CHEMBL4751648
5.00	IC50	1e+04	nM	CHEMBL4763181

PubChem BioAssay actives

8 with measured affinity, of 111 total; 8 most potent distinct compounds. Largely complementary to BindingDB; screening values are coarse (µM, 4 dp), so sub-nM hits tie at the floor.

Compound	Assay	Type	Value	Unit
4-methyl-3-[(2-methyl-6-pyridin-3-ylpyrazolo[3,4-d]pyrimidin-4-yl)amino]-N-[3-(trifluoromethyl)phenyl]benzamide	2148034: Binding affinity to human CDC37 incubated for 45 mins by Kinobead based pull down assay	kd	0.0087	uM
prop-2-ynyl (2R,4aS,6aR,6aS,14aS,14bR)-10-hydroxy-2,4a,6a,6a,9,14a-hexamethyl-11-oxo-1,3,4,5,6,13,14,14b-octahydropicene-2-carboxylate	1929120: Disruption of His-tagged full length HSP90 (unknown origin)/GST-tagged Cdc37 (unknown origin) measured after 1 hr by HTRF method	ic50	1.7000	uM
benzyl (2R,4aS,6aR,6aS,14aS,14bR)-10-hydroxy-2,4a,6a,6a,9,14a-hexamethyl-11-oxo-1,3,4,5,6,13,14,14b-octahydropicene-2-carboxylate	1929120: Disruption of His-tagged full length HSP90 (unknown origin)/GST-tagged Cdc37 (unknown origin) measured after 1 hr by HTRF method	ic50	2.4000	uM
cyclohexylmethyl (2R,4aS,6aR,6aS,14aS,14bR)-10-hydroxy-2,4a,6a,6a,9,14a-hexamethyl-11-oxo-1,3,4,5,6,13,14,14b-octahydropicene-2-carboxylate	1929120: Disruption of His-tagged full length HSP90 (unknown origin)/GST-tagged Cdc37 (unknown origin) measured after 1 hr by HTRF method	ic50	2.9000	uM
4-methyl-3-[(1-methyl-6-pyridin-3-ylpyrazolo[3,4-d]pyrimidin-4-yl)amino]-N-[3-(trifluoromethyl)phenyl]benzamide	2148034: Binding affinity to human CDC37 incubated for 45 mins by Kinobead based pull down assay	kd	3.5486	uM
(3-methylphenyl)methyl (2R,4aS,6aR,6aS,14aS,14bR)-10-hydroxy-2,4a,6a,6a,9,14a-hexamethyl-11-oxo-1,3,4,5,6,13,14,14b-octahydropicene-2-carboxylate	1929120: Disruption of His-tagged full length HSP90 (unknown origin)/GST-tagged Cdc37 (unknown origin) measured after 1 hr by HTRF method	ic50	6.2000	uM
2-methoxyethyl (2R,4aS,6aR,6aS,14aS,14bR)-10-hydroxy-2,4a,6a,6a,9,14a-hexamethyl-11-oxo-1,3,4,5,6,13,14,14b-octahydropicene-2-carboxylate	1929120: Disruption of His-tagged full length HSP90 (unknown origin)/GST-tagged Cdc37 (unknown origin) measured after 1 hr by HTRF method	ic50	6.7000	uM
(2-methylphenyl)methyl (2R,4aS,6aR,6aS,14aS,14bR)-10-hydroxy-2,4a,6a,6a,9,14a-hexamethyl-11-oxo-1,3,4,5,6,13,14,14b-octahydropicene-2-carboxylate	1929120: Disruption of His-tagged full length HSP90 (unknown origin)/GST-tagged Cdc37 (unknown origin) measured after 1 hr by HTRF method	ic50	10.0000	uM

CTD chemical–gene interactions

61 total (human), top 30 by PubMed support.

Chemical	Actions (top 5)	PubMed papers
Valproic Acid	increases expression, affects expression, affects cotreatment	5
bisphenol A	decreases expression	2
Benzene	decreases expression	2
Copper	affects binding, decreases expression, increases expression	2
Tobacco Smoke Pollution	increases expression, affects expression	2
aristolochic acid I	increases expression	1
ribociclib	affects binding, decreases reaction	1
abemaciclib	affects binding, decreases reaction	1
FR900359	increases phosphorylation	1
moringin	affects cotreatment, increases expression	1
geldanamycin	affects binding, decreases reaction, affects localization	1
2,4,6-tribromophenol	decreases expression	1
triphenyl phosphate	affects expression	1
nobiletin	decreases expression, decreases reaction	1
sodium arsenate	decreases reaction, decreases expression	1
pyrogallol 1,3-dimethyl ether	affects cotreatment, decreases expression	1
sodium arsenite	increases expression	1
cobaltous chloride	decreases expression	1
tetrabromobisphenol A	decreases expression	1
coumarin	increases phosphorylation	1
2-chloroethyl ethyl sulfide	decreases expression	1
M-VAC protocol	decreases response to substance	1
chloropicrin	decreases expression	1
platycodin D	decreases expression	1
4-(5-benzo(1,3)dioxol-5-yl-4-pyridin-2-yl-1H-imidazol-2-yl)benzamide	decreases expression, affects cotreatment	1
bisphenol B	increases expression	1
14-deoxy-11,12-didehydroandrographolide	decreases expression	1
abrine	increases expression	1
palbociclib	affects binding, decreases reaction	1
hexabrominated diphenyl ether 153	decreases expression	1

ChEMBL screening assays

51 unique, capped per target: 51 binding

Representative assays (with source publication via chembl_document):

Assay ID	Type	Description	Source paper
CHEMBL1803252	Binding	Inhibition of Cdc37 interaction with heme-regulated [35S]His-tagged eIF2alpha K199R mutant kinase in reticulocyte lysate assessed as coadsorbed Cdc37 at 80 uM after 40 mins by SDS-PAGE and Western blot analysis	Gambogic acid, a natural product inhibitor of Hsp90. — J Nat Prod

Cellosaurus cell lines

1 cell lines: 1 cancer cell line

First 10 cell lines (id-ordered, not curated):

Cellosaurus	Name	Category	Sex
CVCL_D9ZT	Ubigene HeLa CDC37 KO	Cancer cell line	Female

Clinical trials (associated diseases)

0 trials via MONDO — disease-level, not drug-specific.