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Protein

Hsp90 co-chaperone Cdc37

Gene

CDC37

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity (PubMed:8666233). Inhibits HSP90AA1 ATPase activity (PubMed:23569206).2 Publications

GO - Molecular functioni

  • chaperone binding Source: GO_Central
  • heat shock protein binding Source: UniProtKB
  • Hsp90 protein binding Source: Ensembl
  • kinase binding Source: ParkinsonsUK-UCL
  • protein kinase binding Source: InterPro
  • protein kinase regulator activity Source: Ensembl
  • protein tyrosine kinase activity Source: Reactome
  • scaffold protein binding Source: UniProtKB
  • unfolded protein binding Source: ProtInc

GO - Biological processi

  • ERBB2 signaling pathway Source: Reactome
  • positive regulation of mitophagy in response to mitochondrial depolarization Source: Ensembl
  • posttranscriptional regulation of gene expression Source: Ensembl
  • protein folding Source: GO_Central
  • protein stabilization Source: GO_Central
  • protein targeting Source: ProtInc
  • regulation of cyclin-dependent protein serine/threonine kinase activity Source: ProtInc
  • regulation of interferon-gamma-mediated signaling pathway Source: MGI
  • regulation of type I interferon-mediated signaling pathway Source: MGI

Keywordsi

Molecular functionChaperone

Enzyme and pathway databases

ReactomeiR-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-8863795 Downregulation of ERBB2 signaling
SIGNORiQ16543

Protein family/group databases

MoonDBiQ16543 Predicted

Names & Taxonomyi

Protein namesi
Recommended name:
Hsp90 co-chaperone Cdc37
Alternative name(s):
Hsp90 chaperone protein kinase-targeting subunit
p50Cdc37
Cleaved into the following chain:
Gene namesi
Name:CDC37
Synonyms:CDC37A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

EuPathDBiHostDB:ENSG00000105401.6
HGNCiHGNC:1735 CDC37
MIMi605065 gene
neXtProtiNX_Q16543

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

DisGeNETi11140
OpenTargetsiENSG00000105401
PharmGKBiPA402

Chemistry databases

ChEMBLiCHEMBL1795123

Polymorphism and mutation databases

BioMutaiCDC37
DMDMi21542000

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001950571 – 378Hsp90 co-chaperone Cdc37Add BLAST378
Initiator methionineiRemoved; alternateCombined sources
ChainiPRO_00004231972 – 378Hsp90 co-chaperone Cdc37, N-terminally processedAdd BLAST377

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei2N-acetylvaline; in Hsp90 co-chaperone Cdc37, N-terminally processedCombined sources1
Modified residuei13PhosphoserineCombined sources1
Modified residuei78N6-acetyllysineCombined sources1
Modified residuei118PhosphothreonineCombined sources1
Modified residuei120PhosphoserineCombined sources1
Modified residuei154N6-acetyllysineCombined sources1
Modified residuei377PhosphoserineCombined sources1

Post-translational modificationi

Constitutively sumoylated by UBE2I.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ16543
MaxQBiQ16543
PaxDbiQ16543
PeptideAtlasiQ16543
PRIDEiQ16543
ProteomicsDBi60906
TopDownProteomicsiQ16543

PTM databases

iPTMnetiQ16543
PhosphoSitePlusiQ16543
SwissPalmiQ16543

Expressioni

Gene expression databases

BgeeiENSG00000105401
CleanExiHS_CDC37
ExpressionAtlasiQ16543 baseline and differential
GenevisibleiQ16543 HS

Organism-specific databases

HPAiCAB004214
HPA003928

Interactioni

Subunit structurei

Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and client protein TSC2 (PubMed:29127155). 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 (PubMed:29127155). Forms a complex with Hsp90/HSP90AB1 and CDK6 (PubMed:9482106). Interacts with HSP90AA1 (PubMed:23569206, PubMed:27353360). Interacts with AR, CDK4, CDK6 and EIF2AK1 (PubMed:11036079, PubMed:11085988, PubMed:9150368, PubMed:9482106). Interacts with RB1 (By similarity). Interacts with KSR1 (PubMed:10409742). Interacts with FLCN, FNIP1 and FNIP2 (PubMed:27353360).By similarity8 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • chaperone binding Source: GO_Central
  • heat shock protein binding Source: UniProtKB
  • Hsp90 protein binding Source: Ensembl
  • kinase binding Source: ParkinsonsUK-UCL
  • protein kinase binding Source: InterPro
  • scaffold protein binding Source: UniProtKB
  • unfolded protein binding Source: ProtInc

Protein-protein interaction databases

BioGridi116312, 246 interactors
ComplexPortaliCPX-3285 HSP90B-CDC37 chaperone complex
CPX-3288 HSP90A-CDC37 chaperone complex
CORUMiQ16543
DIPiDIP-27560N
IntActiQ16543, 373 interactors
MINTiQ16543
STRINGi9606.ENSP00000222005

Structurei

Secondary structure

1378
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni13 – 15Combined sources3
Helixi27 – 72Combined sources46
Helixi79 – 109Combined sources31
Helixi113 – 116Combined sources4
Helixi149 – 163Combined sources15
Helixi168 – 177Combined sources10
Helixi179 – 181Combined sources3
Helixi184 – 199Combined sources16
Helixi203 – 226Combined sources24
Helixi230 – 241Combined sources12
Helixi247 – 272Combined sources26
Helixi294 – 300Combined sources7
Helixi303 – 310Combined sources8
Helixi317 – 321Combined sources5
Beta strandi325 – 327Combined sources3
Helixi328 – 338Combined sources11
Beta strandi345 – 347Combined sources3
Beta strandi365 – 367Combined sources3

3D structure databases

ProteinModelPortaliQ16543
SMRiQ16543
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16543

Family & Domainsi

Sequence similaritiesi

Belongs to the CDC37 family.Curated

Phylogenomic databases

eggNOGiKOG2260 Eukaryota
ENOG410XTCZ LUCA
GeneTreeiENSGT00390000013443
HOGENOMiHOG000018180
HOVERGENiHBG056343
InParanoidiQ16543
KOiK09554
OrthoDBiEOG091G0HL8
PhylomeDBiQ16543
TreeFamiTF101059

Family and domain databases

Gene3Di1.20.58.610, 1 hit
InterProiView protein in InterPro
IPR004918 Cdc37
IPR013873 Cdc37_C
IPR013874 Cdc37_Hsp90-bd
IPR038189 Cdc37_Hsp90-bd_sf
IPR013855 Cdc37_N_dom
PANTHERiPTHR12800 PTHR12800, 1 hit
PfamiView protein in Pfam
PF08564 CDC37_C, 1 hit
PF08565 CDC37_M, 1 hit
PF03234 CDC37_N, 1 hit
SMARTiView protein in SMART
SM01069 CDC37_C, 1 hit
SM01070 CDC37_M, 1 hit
SM01071 CDC37_N, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q16543-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVDYSVWDHI EVSDDEDETH PNIDTASLFR WRHQARVERM EQFQKEKEEL
60 70 80 90 100
DRGCRECKRK VAECQRKLKE LEVAEGGKAE LERLQAEAQQ LRKEERSWEQ
110 120 130 140 150
KLEEMRKKEK SMPWNVDTLS KDGFSKSMVN TKPEKTEEDS EEVREQKHKT
160 170 180 190 200
FVEKYEKQIK HFGMLRRWDD SQKYLSDNVH LVCEETANYL VIWCIDLEVE
210 220 230 240 250
EKCALMEQVA HQTIVMQFIL ELAKSLKVDP RACFRQFFTK IKTADRQYME
260 270 280 290 300
GFNDELEAFK ERVRGRAKLR IEKAMKEYEE EERKKRLGPG GLDPVEVYES
310 320 330 340 350
LPEELQKCFD VKDVQMLQDA ISKMDPTDAK YHMQRCIDSG LWVPNSKASE
360 370
AKEGEEAGPG DPLLEAVPKT GDEKDVSV
Length:378
Mass (Da):44,468
Last modified:November 1, 1996 - v1
Checksum:i55BFEFFF3C2A5442
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_022220360G → E1 PublicationCorresponds to variant dbSNP:rs280528Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43077 mRNA Translation: AAB63979.1
U63131 mRNA Translation: AAB04798.1
AY864824 Genomic DNA Translation: AAW34362.1
BT006796 mRNA Translation: AAP35442.1
CH471106 Genomic DNA Translation: EAW84101.1
BC000083 mRNA Translation: AAH00083.1
BC008793 mRNA Translation: AAH08793.1
CCDSiCCDS12237.1
PIRiG02313
RefSeqiNP_008996.1, NM_007065.3
UniGeneiHs.160958

Genome annotation databases

EnsembliENST00000222005; ENSP00000222005; ENSG00000105401
GeneIDi11140
KEGGihsa:11140
UCSCiuc002mof.2 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiCDC37_HUMAN
AccessioniPrimary (citable) accession number: Q16543
Secondary accession number(s): Q53YA2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: November 1, 1996
Last modified: July 18, 2018
This is version 175 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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