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Protein

Hsp90 co-chaperone Cdc37

Gene

Cdc37

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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.1 Publication

GO - Molecular functioni

  • chaperone binding Source: GO_Central
  • heat shock protein binding Source: MGI
  • Hsp90 protein binding Source: MGI
  • kinase binding Source: ParkinsonsUK-UCL
  • unfolded protein binding Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Enzyme and pathway databases

ReactomeiREACT_348099. 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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:109531. Cdc37.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: MGI
  • extracellular exosome Source: MGI
  • HSP90-CDC37 chaperone complex Source: ParkinsonsUK-UCL
  • ruffle membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 379379Hsp90 co-chaperone Cdc37PRO_0000195058Add
BLAST
Initiator methioninei1 – 11Removed; alternateBy similarity
Chaini2 – 379378Hsp90 co-chaperone Cdc37, N-terminally processedPRO_0000423198Add
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 – 131PhosphoserineBy similarity
Modified residuei155 – 1551N6-acetyllysineBy similarity
Modified residuei378 – 3781PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ61081.
PaxDbiQ61081.
PRIDEiQ61081.

PTM databases

PhosphoSiteiQ61081.

Expressioni

Gene expression databases

BgeeiQ61081.
CleanExiMM_CDC37.
GenevestigatoriQ61081.

Interactioni

Subunit structurei

Forms a complex with Hsp90/HSP90AB1 and CDK6. Interacts with AR, CDK4, CDK6, EIF2AK1 and RB1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi198626. 6 interactions.
IntActiQ61081. 5 interactions.
MINTiMINT-1848189.

Structurei

3D structure databases

ProteinModelPortaliQ61081.
SMRiQ61081. Positions 149-348.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the CDC37 family.Curated

Phylogenomic databases

eggNOGiNOG300020.
GeneTreeiENSGT00390000013443.
HOGENOMiHOG000018180.
HOVERGENiHBG056343.
InParanoidiQ61081.
KOiK09554.
OMAiSKWKNIE.
OrthoDBiEOG73805G.
PhylomeDBiQ61081.
TreeFamiTF101059.

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. 2 hits.
[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.

Q61081-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVDYSVWDHI EVSDDEDETH PNIDTASLFR WRHQARVERM EQFQKEKEEL
60 70 80 90 100
DRGCRECKRK VAECQRKLKE LEVAESDGQV 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 KIKTADHQYM
260 270 280 290 300
EGFKYELEAF KERVRGRAKL RIEKAMKEYE EEERKKRLGP GGLDPVEVYE
310 320 330 340 350
SLPEELQKCF DVKDVQMLQD AISKMDPTDA KYHMQRCIDS GLWVPNSKSG
360 370
EAKEGEEAGP GDPLLEAVPK AGNEKDVSA
Length:379
Mass (Da):44,593
Last modified:November 1, 1996 - v1
Checksum:i847C146B4FE3AAF1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43076 mRNA. Translation: AAB18761.1.
AK010494 mRNA. Translation: BAB26984.1.
AK013255 mRNA. Translation: BAB28749.1.
AK145671 mRNA. Translation: BAE26580.1.
AK168651 mRNA. Translation: BAE40508.1.
BC060079 mRNA. Translation: AAH60079.1.
CCDSiCCDS22894.1.
RefSeqiNP_058022.1. NM_016742.4.
UniGeneiMm.32331.

Genome annotation databases

EnsembliENSMUST00000019615; ENSMUSP00000019615; ENSMUSG00000019471.
GeneIDi12539.
KEGGimmu:12539.
UCSCiuc009okg.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43076 mRNA. Translation: AAB18761.1.
AK010494 mRNA. Translation: BAB26984.1.
AK013255 mRNA. Translation: BAB28749.1.
AK145671 mRNA. Translation: BAE26580.1.
AK168651 mRNA. Translation: BAE40508.1.
BC060079 mRNA. Translation: AAH60079.1.
CCDSiCCDS22894.1.
RefSeqiNP_058022.1. NM_016742.4.
UniGeneiMm.32331.

3D structure databases

ProteinModelPortaliQ61081.
SMRiQ61081. Positions 149-348.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198626. 6 interactions.
IntActiQ61081. 5 interactions.
MINTiMINT-1848189.

PTM databases

PhosphoSiteiQ61081.

Proteomic databases

MaxQBiQ61081.
PaxDbiQ61081.
PRIDEiQ61081.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000019615; ENSMUSP00000019615; ENSMUSG00000019471.
GeneIDi12539.
KEGGimmu:12539.
UCSCiuc009okg.1. mouse.

Organism-specific databases

CTDi11140.
MGIiMGI:109531. Cdc37.

Phylogenomic databases

eggNOGiNOG300020.
GeneTreeiENSGT00390000013443.
HOGENOMiHOG000018180.
HOVERGENiHBG056343.
InParanoidiQ61081.
KOiK09554.
OMAiSKWKNIE.
OrthoDBiEOG73805G.
PhylomeDBiQ61081.
TreeFamiTF101059.

Enzyme and pathway databases

ReactomeiREACT_348099. Signaling by ERBB2.

Miscellaneous databases

ChiTaRSiCdc37. mouse.
NextBioi281578.
PROiQ61081.
SOURCEiSearch...

Gene expression databases

BgeeiQ61081.
CleanExiMM_CDC37.
GenevestigatoriQ61081.

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. 2 hits.
[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. "Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4."
    Stepanova L., Leng X., Parker S.B., Harper J.W.
    Genes Dev. 10:1491-1502(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo, Embryonic stem cell and Kidney.
  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].
    Strain: C57BL/6.
    Tissue: Brain.

Entry informationi

Entry nameiCDC37_MOUSE
AccessioniPrimary (citable) accession number: Q61081
Secondary accession number(s): Q3TGP0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: November 1, 1996
Last modified: May 27, 2015
This is version 111 of the entry and version 1 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.