CDC37 | ENSG00000105401 | NCBI 11140

Details for: CDC37

Gene ID: 11140

Symbol: CDC37

Ensembl ID: ENSG00000105401

Description: cell division cycle 37, HSP90 cochaperone

Associated with

Constitutive signaling by egfrviii
(R-HSA-5637810)
Constitutive signaling by ligand-responsive egfr cancer variants
(R-HSA-1236382)
Constitutive signaling by overexpressed erbb2
(R-HSA-9634285)
Disease
(R-HSA-1643685)
Diseases of signal transduction by growth factor receptors and second messengers
(R-HSA-5663202)
Downregulation of erbb2 signaling
(R-HSA-8863795)
Drug-mediated inhibition of erbb2 signaling
(R-HSA-9652282)
Drug resistance in erbb2 kd mutants
(R-HSA-9665230)
Drug resistance in erbb2 tmd/jmd mutants
(R-HSA-9665737)
Programmed cell death
(R-HSA-5357801)
Regulated necrosis
(R-HSA-5218859)
Regulation of necroptotic cell death
(R-HSA-5675482)
Resistance of erbb2 kd mutants to aee788
(R-HSA-9665250)
Resistance of erbb2 kd mutants to afatinib
(R-HSA-9665249)
Resistance of erbb2 kd mutants to lapatinib
(R-HSA-9665251)
Resistance of erbb2 kd mutants to neratinib
(R-HSA-9665246)
Resistance of erbb2 kd mutants to osimertinib
(R-HSA-9665247)
Resistance of erbb2 kd mutants to sapitinib
(R-HSA-9665244)
Resistance of erbb2 kd mutants to tesevatinib
(R-HSA-9665245)
Resistance of erbb2 kd mutants to trastuzumab
(R-HSA-9665233)
Rhobtb2 gtpase cycle
(R-HSA-9013418)
Rhobtb gtpase cycle
(R-HSA-9706574)
Rho gtpase cycle
(R-HSA-9012999)
Ripk1-mediated regulated necrosis
(R-HSA-5213460)
Signaling by egfr in cancer
(R-HSA-1643713)
Signaling by egfrviii in cancer
(R-HSA-5637812)
Signaling by erbb2
(R-HSA-1227986)
Signaling by erbb2 ecd mutants
(R-HSA-9665348)
Signaling by erbb2 in cancer
(R-HSA-1227990)
Signaling by erbb2 kd mutants
(R-HSA-9664565)
Signaling by erbb2 tmd/jmd mutants
(R-HSA-9665686)
Signaling by ligand-responsive egfr variants in cancer
(R-HSA-5637815)
Signaling by receptor tyrosine kinases
(R-HSA-9006934)
Signaling by rho gtpases
(R-HSA-194315)
Signaling by rho gtpases, miro gtpases and rhobtb3
(R-HSA-9716542)
Signal transduction
(R-HSA-162582)
Cytoplasm
(GO:0005737)
Cytosol
(GO:0005829)
Extracellular exosome
(GO:0070062)
Heat shock protein binding
(GO:0031072)
Hsp90 protein binding
(GO:0051879)
Hsp90-cdc37 chaperone complex
(GO:1990565)
Kinase binding
(GO:0019900)
Positive regulation of mitophagy in response to mitochondrial depolarization
(GO:0098779)
Post-transcriptional regulation of gene expression
(GO:0010608)
Protein-folding chaperone binding
(GO:0051087)
Protein binding
(GO:0005515)
Protein folding
(GO:0006457)
Protein folding chaperone complex
(GO:0101031)
Protein kinase binding
(GO:0019901)
Protein kinase regulator activity
(GO:0019887)
Protein stabilization
(GO:0050821)
Protein targeting
(GO:0006605)
Regulation of cyclin-dependent protein serine/threonine kinase activity
(GO:0000079)
Regulation of type ii interferon-mediated signaling pathway
(GO:0060334)
Regulation of type i interferon-mediated signaling pathway
(GO:0060338)
Scaffold protein binding
(GO:0097110)
Unfolded protein binding
(GO:0051082)

Other Information

Proteins

Hsp90 co-chaperone Cdc37

Genular Protein ID: 3603618742

Symbol: CDC37_HUMAN

Name: Hsp90 co-chaperone Cdc37

UniProtKB Accession Codes:

Q16543 Q53YA2

Database IDs:

Citations:

PubMed ID: 8666233

Title: Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4.

PubMed ID: 8666233

DOI: 10.1101/gad.10.12.1491

PubMed ID: 8703009

Title: Physical interaction of mammalian CDC37 with CDK4.

PubMed ID: 8703009

DOI: 10.1074/jbc.271.36.22030

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 9150368

Title: Interaction between Cdc37 and Cdk4 in human cells.

PubMed ID: 9150368

DOI: 10.1038/sj.onc.1201036

PubMed ID: 9482106

Title: Active cdk6 complexes are predominantly nuclear and represent only a minority of the cdk6 in T cells.

PubMed ID: 9482106

DOI: 10.1038/sj.onc.1201570

PubMed ID: 10409742

Title: Kinase suppressor of Ras forms a multiprotein signaling complex and modulates MEK localization.

PubMed ID: 10409742

DOI: 10.1128/mcb.19.8.5523

PubMed ID: 10858314

Title: p50(cdc37) is a nonexclusive Hsp90 cohort which participates intimately in Hsp90-mediated folding of immature kinase molecules.

PubMed ID: 10858314

DOI: 10.1021/bi000315r

PubMed ID: 11036079

Title: Hsp90 regulates p50(cdc37) function during the biogenesis of the active conformation of the heme-regulated eIF2 alpha kinase.

PubMed ID: 11036079

DOI: 10.1074/jbc.m007583200

PubMed ID: 11085988

Title: Functional interaction of human Cdc37 with the androgen receptor but not with the glucocorticoid receptor.

PubMed ID: 11085988

DOI: 10.1074/jbc.m007385200

PubMed ID: 15592455

Title: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.

PubMed ID: 15592455

DOI: 10.1038/nbt1046

PubMed ID: 17709345

Title: Ubc9 fusion-directed SUMOylation identifies constitutive and inducible SUMOylation.

PubMed ID: 17709345

DOI: 10.1093/nar/gkm617

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23569206

Title: Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein 90) motility by interaction with N-terminal and middle domain binding sites.

PubMed ID: 23569206

DOI: 10.1074/jbc.m112.439257

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 27353360

Title: The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding.

PubMed ID: 27353360

DOI: 10.1038/ncomms12037

PubMed ID: 29127155

Title: Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates folding of kinase and non-kinase clients.

PubMed ID: 29127155

DOI: 10.15252/embj.201796700

Sequence Information:

Length: 378
Mass: 44468
Checksum: 55BFEFFF3C2A5442
Sequence:

MVDYSVWDHI EVSDDEDETH PNIDTASLFR WRHQARVERM EQFQKEKEEL DRGCRECKRK 
VAECQRKLKE LEVAEGGKAE LERLQAEAQQ LRKEERSWEQ KLEEMRKKEK SMPWNVDTLS 
KDGFSKSMVN TKPEKTEEDS EEVREQKHKT FVEKYEKQIK HFGMLRRWDD SQKYLSDNVH 
LVCEETANYL VIWCIDLEVE EKCALMEQVA HQTIVMQFIL ELAKSLKVDP RACFRQFFTK 
IKTADRQYME GFNDELEAFK ERVRGRAKLR IEKAMKEYEE EERKKRLGPG GLDPVEVYES 
LPEELQKCFD VKDVQMLQDA ISKMDPTDAK YHMQRCIDSG LWVPNSKASE AKEGEEAGPG 
DPLLEAVPKT GDEKDVSV

The gene details are incomplete or unavailable at the moment.

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: CDC37

Associated with

Other Information

Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4. PubMed ID: 8666233

Physical interaction of mammalian CDC37 with CDK4. PubMed ID: 8703009

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Interaction between Cdc37 and Cdk4 in human cells. PubMed ID: 9150368

Active cdk6 complexes are predominantly nuclear and represent only a minority of the cdk6 in T cells. PubMed ID: 9482106

Kinase suppressor of Ras forms a multiprotein signaling complex and modulates MEK localization. PubMed ID: 10409742

p50(cdc37) is a nonexclusive Hsp90 cohort which participates intimately in Hsp90-mediated folding of immature kinase molecules. PubMed ID: 10858314

Hsp90 regulates p50(cdc37) function during the biogenesis of the active conformation of the heme-regulated eIF2 alpha kinase. PubMed ID: 11036079

Functional interaction of human Cdc37 with the androgen receptor but not with the glucocorticoid receptor. PubMed ID: 11085988

Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. PubMed ID: 15592455

Ubc9 fusion-directed SUMOylation identifies constitutive and inducible SUMOylation. PubMed ID: 17709345

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. PubMed ID: 19413330

Lysine acetylation targets protein complexes and co-regulates major cellular functions. PubMed ID: 19608861

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

Initial characterization of the human central proteome. PubMed ID: 21269460

System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. PubMed ID: 21406692

N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. PubMed ID: 22814378

Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein 90) motility by interaction with N-terminal and middle domain binding sites. PubMed ID: 23569206

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding. PubMed ID: 27353360

Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates folding of kinase and non-kinase clients. PubMed ID: 29127155