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Protein

Hsp90 co-chaperone Cdc37

Gene

Cdc37

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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. Inhibits HSP90AA1 ATPase activity.By similarity

GO - Molecular functioni

  • chaperone binding Source: RGD
  • heat shock protein binding Source: RGD
  • Hsp90 protein binding Source: RGD
  • kinase binding Source: RGD
  • mitogen-activated protein kinase kinase kinase binding Source: RGD
  • protein C-terminus binding Source: RGD
  • protein kinase B binding Source: RGD
  • protein kinase binding Source: RGD
  • protein tyrosine kinase activity Source: RGD
  • unfolded protein binding Source: GO_Central

GO - Biological processi

Keywordsi

Molecular functionChaperone

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi71006. Cdc37.

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004231991 – 379Hsp90 co-chaperone Cdc37Add BLAST379
Initiator methionineiRemoved; alternateBy similarity
ChainiPRO_00001950592 – 379Hsp90 co-chaperone Cdc37, N-terminally processedAdd BLAST378

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei2N-acetylvaline; in Hsp90 co-chaperone Cdc37, N-terminally processedBy similarity1
Modified residuei13PhosphoserineCombined sources1
Modified residuei119PhosphothreonineBy similarity1
Modified residuei121PhosphoserineBy similarity1
Modified residuei155N6-acetyllysineBy similarity1
Modified residuei378PhosphoserineBy similarity1

Post-translational modificationi

Constitutively sumoylated by UBE2I.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ63692.
PRIDEiQ63692.

PTM databases

iPTMnetiQ63692.
PhosphoSitePlusiQ63692.

Expressioni

Gene expression databases

GenevisibleiQ63692. RN.

Interactioni

Subunit structurei

Interacts with HSP90AA1. Forms a complex with Hsp90/HSP90AB1 and CDK6. Interacts with AR, CDK4, CDK6 and EIF2AK1. Interacts with KSR1. Interacts with FLCN, FNIP1 and FNIP2 (By similarity). Interacts with RB1 (PubMed:8945638).By similarity1 Publication

GO - Molecular functioni

  • chaperone binding Source: RGD
  • heat shock protein binding Source: RGD
  • Hsp90 protein binding Source: RGD
  • kinase binding Source: RGD
  • mitogen-activated protein kinase kinase kinase binding Source: RGD
  • protein C-terminus binding Source: RGD
  • protein kinase B binding Source: RGD
  • protein kinase binding Source: RGD
  • unfolded protein binding Source: GO_Central

Protein-protein interaction databases

BioGridi250380. 4 interactors.
IntActiQ63692. 2 interactors.
STRINGi10116.ENSRNOP00000051248.

Structurei

3D structure databases

ProteinModelPortaliQ63692.
SMRiQ63692.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the CDC37 family.Curated

Phylogenomic databases

eggNOGiKOG2260. Eukaryota.
ENOG410XTCZ. LUCA.
HOGENOMiHOG000018180.
HOVERGENiHBG056343.
InParanoidiQ63692.
KOiK09554.
OrthoDBiEOG091G0HL8.
PhylomeDBiQ63692.

Family and domain databases

InterProiView protein in InterPro
IPR004918. Cdc37.
IPR013873. Cdc37_C.
IPR013874. Cdc37_Hsp90-bd.
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.

Q63692-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVDYSVWDHI EVSDDEDETH PNIDTASLFR WRHQARVERM EQFQKEKEEL
60 70 80 90 100
DRGCRECKRK VAECQRKLKE LEVAEGGGQV ELERLRAEAQ QLRKEERSWE
110 120 130 140 150
QKLEDMRKKE KNMPWNVDTL SKDGFSKSMV NTKPEKAEED SEEAREQKHK
160 170 180 190 200
TFVEKYEKQI KHFGMLHRWD DSQKYLSDNV HLVCEETANY LVIWCIDLEV
210 220 230 240 250
EEKCALMEQV AHQTMVMQFI LELAKSLKVD PRACFRQFFT KIKTADQQYM
260 270 280 290 300
EGFKYELEAF KERVRGRAKL RIEKAMKEYE EEERKKRLGP GGLDPVEVYE
310 320 330 340 350
SLPEELQKCF DVKDVQMLQD AISKMDPTDA KYHMQRCIDS GLWVPNSKSG
360 370
EAKEGEEAGP GDPLLEAVPK AGNEKDISA
Length:379
Mass (Da):44,510
Last modified:June 20, 2003 - v2
Checksum:i52D1314C88824CE1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti64C → F in BAA05618 (PubMed:8534368).Curated1
Sequence conflicti98 – 107SWEQKLEDMR → TGSRSWRTCG in BAA05618 (PubMed:8534368).Curated10
Sequence conflicti373N → F in BAA05618 (PubMed:8534368).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26564 mRNA. Translation: BAA05618.1.
AB097113 mRNA. Translation: BAC54286.1.
BC061720 mRNA. Translation: AAH61720.1.
RefSeqiNP_446195.1. NM_053743.1.
UniGeneiRn.17982.

Genome annotation databases

GeneIDi114562.
KEGGirno:114562.
UCSCiRGD:71006. rat.

Similar proteinsi

Entry informationi

Entry nameiCDC37_RAT
AccessioniPrimary (citable) accession number: Q63692
Secondary accession number(s): Q8CH95
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: June 20, 2003
Last modified: November 22, 2017
This is version 127 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families