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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.

GO - Molecular functioni

  • chaperone 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

GO - Biological processi

  • regulation of cell cycle Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Enzyme and pathway databases

ReactomeiR-RNO-1227986. Signaling by ERBB2.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi71006. Cdc37.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • protein complex Source: RGD
  • ruffle membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 379379Hsp90 co-chaperone Cdc37PRO_0000195059Add
BLAST
Initiator methionineiRemoved; alternateBy similarity
Chaini2 – 379378Hsp90 co-chaperone Cdc37, N-terminally processedPRO_0000423199Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei2 – 21N-acetylvaline; in Hsp90 co-chaperone Cdc37, N-terminally processedBy similarity
Modified residuei13 – 131PhosphoserineCombined sources
Modified residuei155 – 1551N6-acetyllysineBy similarity
Modified residuei378 – 3781PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ63692.
PRIDEiQ63692.

PTM databases

iPTMnetiQ63692.
PhosphoSiteiQ63692.

Expressioni

Gene expression databases

GenevisibleiQ63692. RN.

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • chaperone 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-protein interaction databases

BioGridi250380. 4 interactions.
IntActiQ63692. 2 interactions.
STRINGi10116.ENSRNOP00000051248.

Structurei

3D structure databases

ProteinModelPortaliQ63692.
SMRiQ63692. Positions 149-348.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the CDC37 family.Curated

Phylogenomic databases

eggNOGiKOG2260. Eukaryota.
ENOG410XTCZ. LUCA.
HOGENOMiHOG000018180.
HOVERGENiHBG056343.
InParanoidiQ63692.
KOiK09554.
OMAiMEEKHDL.
OrthoDBiEOG73805G.
PhylomeDBiQ63692.

Family and domain databases

InterProiIPR004918. Cdc37.
IPR013873. Cdc37_C.
IPR013874. Cdc37_Hsp90-bd.
IPR013855. Cdc37_N_dom.
[Graphical view]
PANTHERiPTHR12800. PTHR12800. 1 hit.
PfamiPF08564. CDC37_C. 1 hit.
PF08565. CDC37_M. 1 hit.
PF03234. CDC37_N. 1 hit.
[Graphical view]
SMARTiSM01069. CDC37_C. 1 hit.
SM01070. CDC37_M. 1 hit.
SM01071. CDC37_N. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti64 – 641C → F in BAA05618 (PubMed:8534368).Curated
Sequence conflicti98 – 10710SWEQKLEDMR → TGSRSWRTCG in BAA05618 (PubMed:8534368).Curated
Sequence conflicti373 – 3731N → F in BAA05618 (PubMed:8534368).Curated

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliQ63692.
SMRiQ63692. Positions 149-348.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250380. 4 interactions.
IntActiQ63692. 2 interactions.
STRINGi10116.ENSRNOP00000051248.

PTM databases

iPTMnetiQ63692.
PhosphoSiteiQ63692.

Proteomic databases

PaxDbiQ63692.
PRIDEiQ63692.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi11140.
RGDi71006. Cdc37.

Phylogenomic databases

eggNOGiKOG2260. Eukaryota.
ENOG410XTCZ. LUCA.
HOGENOMiHOG000018180.
HOVERGENiHBG056343.
InParanoidiQ63692.
KOiK09554.
OMAiMEEKHDL.
OrthoDBiEOG73805G.
PhylomeDBiQ63692.

Enzyme and pathway databases

ReactomeiR-RNO-1227986. Signaling by ERBB2.

Miscellaneous databases

NextBioi618723.
PROiQ63692.

Gene expression databases

GenevisibleiQ63692. RN.

Family and domain databases

InterProiIPR004918. Cdc37.
IPR013873. Cdc37_C.
IPR013874. Cdc37_Hsp90-bd.
IPR013855. Cdc37_N_dom.
[Graphical view]
PANTHERiPTHR12800. PTHR12800. 1 hit.
PfamiPF08564. CDC37_C. 1 hit.
PF08565. CDC37_M. 1 hit.
PF03234. CDC37_N. 1 hit.
[Graphical view]
SMARTiSM01069. CDC37_C. 1 hit.
SM01070. CDC37_M. 1 hit.
SM01071. CDC37_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and cell cycle-dependent expression of a novel gene that is homologous to cdc37."
    Ozaki T., Irie K., Sakiyama S.
    DNA Cell Biol. 14:1017-1023(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Coding region of rat Cdc37, a kinase-associated HSP90 co-chaperone."
    Miyata Y.
    Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.
  4. "Interaction of rat Cdc37-related protein with retinoblastoma gene product."
    Ozaki T., Sakiyama S.
    DNA Cell Biol. 15:975-979(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RB1.
  5. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCDC37_RAT
AccessioniPrimary (citable) accession number: Q63692
Secondary accession number(s): Q8CH95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: June 20, 2003
Last modified: May 11, 2016
This is version 116 of the entry and version 2 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.