Hsp90 co-chaperone Cdc37 - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot Q16543 (CDC37_HUMAN)

Last modified July 7, 2009. Version 82. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Hsp90 co-chaperone Cdc37
Alternative name(s):
    Hsp90 chaperone protein kinase-targeting subunit
    p50Cdc37

Gene names

Name:	CDC37
Synonyms:	CDC37A

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	378 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity. Ref.1
Subunit structure	Forms a complex with Hsp90. Interacts with AR, CDK4, CDK6, EIF2AK1 and RB1. Ref.5 Ref.7 Ref.8
Subcellular location	Cytoplasm.
Post-translational modification	Constitutively sumoylated by UBE2I. Ref.10
Sequence similarities	Belongs to the CDC37 family.

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Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Molecular function	Chaperone
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	protein targeting Ref.1 Traceable author statement. Source: ProtInc regulation of cyclin-dependent protein kinase activity Ref.1 Traceable author statement. Source: ProtInc regulation of interferon-gamma-mediated signaling pathway Inferred from mutant phenotype. Source: MGI regulation of type I interferon-mediated signaling pathway Inferred from mutant phenotype. Source: MGI
Molecular function	unfolded protein binding Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P11500	2	EBI-295634,EBI-640126	From a different organism.
AKT1	P31749	1	EBI-295634,EBI-296087
AKT2	P31751	1	EBI-295634,EBI-296058
AKT3	Q9Y243	1	EBI-295634,EBI-296115
CDK4	P11802	4	EBI-295634,EBI-295644
CDK6	Q00534	1	EBI-295634,EBI-295663
EIF2AK1	P33279	1	EBI-295634,EBI-640100	From a different organism.
HSP82	P02829	1	EBI-295634,EBI-8659	From a different organism.
NEK6	Q9HC98	1	EBI-295634,EBI-740364
SGK1	O00141	1	EBI-295634,EBI-1042854
SMYD2	Q9NRG4	1	EBI-295634,EBI-1055671

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 378

378

Hsp90 co-chaperone Cdc37

PRO_0000195057

Amino acid modifications

Modified residue

298

Phosphotyrosine Ref.9

Modified residue

377

Phosphoserine Ref.11

Natural variations

Natural variant

360

G → E: dbSNP rs280528. Ref.3

VAR_022220

Secondary structure

378

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q16543-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 55BFEFFF3C2A5442
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FASTA

378

44,468

        10         20         30         40         50         60 
MVDYSVWDHI EVSDDEDETH PNIDTASLFR WRHQARVERM EQFQKEKEEL DRGCRECKRK 

        70         80         90        100        110        120 
VAECQRKLKE LEVAEGGKAE LERLQAEAQQ LRKEERSWEQ KLEEMRKKEK SMPWNVDTLS 

       130        140        150        160        170        180 
KDGFSKSMVN TKPEKTEEDS EEVREQKHKT FVEKYEKQIK HFGMLRRWDD SQKYLSDNVH 

       190        200        210        220        230        240 
LVCEETANYL VIWCIDLEVE EKCALMEQVA HQTIVMQFIL ELAKSLKVDP RACFRQFFTK 

       250        260        270        280        290        300 
IKTADRQYME GFNDELEAFK ERVRGRAKLR IEKAMKEYEE EERKKRLGPG GLDPVEVYES 

       310        320        330        340        350        360 
LPEELQKCFD VKDVQMLQDA ISKMDPTDAK YHMQRCIDSG LWVPNSKASE AKEGEEAGPG 

       370 
DPLLEAVPKT GDEKDVSV

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8666233] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[2]	"Physical interaction of mammalian CDC37 with CDK4." Dai K., Kobayashi R., Beach D. J. Biol. Chem. 271:22030-22034(1996) [PubMed: 8703009] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	NIEHS SNPs program Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLU-360.
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lymph and Placenta.
[5]	"Interaction between Cdc37 and Cdk4 in human cells." Lamphere L., Fiore F., Xu X., Brizuela L., Keezer S., Sardet C., Draetta G.F., Gyuris J. Oncogene 14:1999-2004(1997) [PubMed: 9150368] [Abstract] Cited for: INTERACTION WITH CDK4 AND CDK6.
[6]	"p50(cdc37) is a nonexclusive Hsp90 cohort which participates intimately in Hsp90-mediated folding of immature kinase molecules." Hartson S.D., Irwin A.D., Shao J., Scroggins B.T., Volk L., Huang W., Matts R.L. Biochemistry 39:7631-7644(2000) [PubMed: 10858314] [Abstract] Cited for: CHARACTERIZATION.
[7]	"Hsp90 regulates p50(cdc37) function during the biogenesis of the active conformation of the heme-regulated eIF2 alpha kinase." Shao J., Grammatikakis N., Scroggins B.T., Uma S., Huang W., Chen J.-J., Hartson S.D., Matts R.L. J. Biol. Chem. 276:206-214(2001) [PubMed: 11036079] [Abstract] Cited for: INTERACTION WITH EIF2AK1.
[8]	"Functional interaction of human Cdc37 with the androgen receptor but not with the glucocorticoid receptor." Rao J., Lee P., Benzeno S., Cardozo C., Albertus J., Robins D.M., Caplan A.J. J. Biol. Chem. 276:5814-5820(2001) [PubMed: 11085988] [Abstract] Cited for: INTERACTION WITH AR.
[9]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-298, MASS SPECTROMETRY.
[10]	"Ubc9 fusion-directed SUMOylation identifies constitutive and inducible SUMOylation." Jakobs A., Himstedt F., Funk M., Korn B., Gaestel M., Niedenthal R. Nucleic Acids Res. 35:E109-E109(2007) [PubMed: 17709345] [Abstract] Cited for: SUMOYLATION.
[11]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, MASS SPECTROMETRY.
[12]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Web resources

NIEHS-SNPs

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Cross-references

Sequence databases

U43077 mRNA. Translation: AAB63979.1.
U63131 mRNA. Translation: AAB04798.1.
AY864824 Genomic DNA. Translation: AAW34362.1.
BC000083 mRNA. Translation: AAH00083.1.
BC008793 mRNA. Translation: AAH08793.1.

IPI

IPI00013122.

PIR

G02313.

RefSeq

NP_008996.1.

UniGene

Hs.160958

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1US7	X-ray	2.30	B	127-378	[»]
2K5B	NMR	-	B	148-276	[»]
2W0G	X-ray	1.88	A	148-276	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:27560N.
DIP:395N.

IntAct

Q16543. 36 interactions.

PTM databases

PhosphoSite

Q16543.

Proteomic databases

PeptideAtlas

Q16543.

PRIDE

Q16543.

Genome annotation databases

Ensembl

ENSG00000105401. Homo sapiens. [Contig view]

GeneID

11140.

KEGG

hsa:11140.

UCSC

uc002mof.1. human.

Organism-specific databases

GeneCards

GC19M010362.

H-InvDB

HIX0014745.

HGNC

HGNC:1735. CDC37.

HPA

CAB004214.
HPA003928.

MIM

605065. gene.

PharmGKB

PA142672192.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q16543.

HOVERGEN

Q16543.

OMA

Q16543. GLWVPNA.

Gene expression databases

ArrayExpress

Q16543.

Bgee

Q16543.

CleanEx

HS_CDC37.

GermOnline

ENSG00000105401. Homo sapiens.

Family and domain databases

InterPro

IPR004918. Cdc37.
IPR013873. Cdc37_C.
IPR013874. Cdc37_Hsp90_bd.
IPR013855. Cdc37_N.
[Graphical view]

PANTHER

PTHR12800. Cdc37. 1 hit.

Pfam

PF08564. CDC37_C. 1 hit.
PF08565. CDC37_M. 1 hit.
PF03234. CDC37_N. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

42344.

SOURCE

Search...

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Entry information

Entry name

CDC37_HUMAN

Accession

Primary (citable) accession number: Q16543

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2002
Last sequence update:	November 1, 1996
Last modified:	July 7, 2009
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Natural variations

Secondary structure

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents