Hsp90 co-chaperone Cdc37 - Homo sapiens (Human)

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Q16543 (CDC37_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 121. History...

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

Documents (6) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	378 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

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/HSP90AB1 and CDK6. Interacts with AR, CDK4, CDK6, EIF2AK1 and RB1. Ref.7 Ref.8 Ref.10 Ref.11
Subcellular location	Cytoplasm Ref.8.
Post-translational modification	Constitutively sumoylated by UBE2I. Ref.13
Sequence similarities	Belongs to the CDC37 family.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Molecular function	Chaperone
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein targeting Traceable author statement Ref.1. Source: ProtInc regulation of cyclin-dependent protein serine/threonine kinase activity Traceable author statement Ref.1. Source: ProtInc regulation of interferon-gamma-mediated signaling pathway Inferred from mutant phenotype PubMed 16280321. Source: MGI regulation of type I interferon-mediated signaling pathway Inferred from mutant phenotype PubMed 16280321. Source: MGI
Cellular_component	cytosol Traceable author statement. Source: Reactome protein complex Inferred from electronic annotation. Source: Compara ruffle membrane Inferred from electronic annotation. Source: Compara
Molecular_function	unfolded protein binding Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P11500	3	EBI-295634,EBI-640126	From a different organism.
AKT1	P31749	2	EBI-295634,EBI-296087
APOE	P02649	3	EBI-295634,EBI-1222467
CDK4	P11802	5	EBI-295634,EBI-295644
CDK6	Q00534	2	EBI-295634,EBI-295663
EIF2AK1	P33279	3	EBI-295634,EBI-640100	From a different organism.
HSP90AB1	P08238	3	EBI-295634,EBI-352572
IFIT3	O14879	4	EBI-295634,EBI-745127
LRRK2	Q5S007	6	EBI-295634,EBI-5323863
NOS3	P29474	4	EBI-295634,EBI-1391623
PPP5C	P53041	2	EBI-295634,EBI-716663
PSEN1	P49768	3	EBI-295634,EBI-297277

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.16

Chain

2 – 378

377

Hsp90 co-chaperone Cdc37

PRO_0000195057

Amino acid modifications

Modified residue

N-acetylvaline Ref.16 Ref.18

Modified residue

Phosphoserine Ref.16 Ref.18

Modified residue

N6-acetyllysine Ref.15

Modified residue

154

N6-acetyllysine Ref.15

Modified residue

377

Phosphoserine Ref.14

Natural variations

Natural variant

360

G → E. Ref.3
Corresponds to variant rs280528 [ dbSNP | Ensembl ].

VAR_022220

Secondary structure

378

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q16543 [UniParc].

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

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

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] [Europe PMC] [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] [Europe PMC] [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]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: Lymph and Placenta.
[7]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CDK4 AND CDK6.
[8]	"Active cdk6 complexes are predominantly nuclear and represent only a minority of the cdk6 in T cells." Mahony D., Parry D.A., Lees E. Oncogene 16:603-611(1998) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CDK6.
[9]	"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] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[10]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EIF2AK1.
[11]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH AR.
[12]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"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] [Europe PMC] [Abstract] Cited for: SUMOYLATION.
[14]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-78 AND LYS-154, MASS SPECTROMETRY.
[16]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE. Tissue: Cervix carcinoma.
[17]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00013122.

PIR

G02313.

RefSeq

NP_008996.1. NM_007065.3.

UniGene

Hs.160958.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q16543.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-27560N.
DIP-395N.

IntAct

Q16543. 86 interactions.

MINT

MINT-99762.

STRING

9606.ENSP00000222005.

PTM databases

PhosphoSite

Q16543.

Polymorphism databases

DMDM

21542000.

Proteomic databases

PaxDb

Q16543.

PeptideAtlas

Q16543.

PRIDE

Q16543.

Protocols and materials databases

DNASU

11140.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000222005; ENSP00000222005; ENSG00000105401.

GeneID

11140.

KEGG

hsa:11140.

UCSC

uc002mof.1. human.

Organism-specific databases

CTD

11140.

GeneCards

GC19M010501.

HGNC

HGNC:1735. CDC37.

HPA

CAB004214.
HPA003928.

MIM

605065. gene.

neXtProt

NX_Q16543.

PharmGKB

PA402.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG300020.

HOGENOM

HOG000018180.

HOVERGEN

HBG056343.

InParanoid

Q16543.

K09554.

OMA

YHMKRCV.

OrthoDB

EOG4CVG75.

PhylomeDB

Q16543.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.
REACT_116125. Disease.

Gene expression databases

Bgee

Q16543.

CleanEx

HS_CDC37.

Genevestigator

Q16543.

GermOnline

ENSG00000105401. Homo sapiens.

Family and domain databases

InterPro

IPR004918. Cdc37.
IPR013873. Cdc37_C.
IPR013874. Cdc37_Hsp90-bd.
IPR013855. Cdc37_N_dom.
[Graphical view]

PANTHER

PTHR12800. PTHR12800. 1 hit.

Pfam

PF08564. CDC37_C. 1 hit.
PF08565. CDC37_M. 1 hit.
PF03234. CDC37_N. 2 hits.
[Graphical view]

SMART

SM01069. CDC37_C. 1 hit.
SM01070. CDC37_M. 1 hit.
SM01071. CDC37_N. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1795123.

ChiTaRS

CDC37. human.

EvolutionaryTrace

Q16543.

GenomeRNAi

11140.

NextBio

42344.

SOURCE

Search...

Entry information

Entry name

CDC37_HUMAN

Accession

Primary (citable) accession number: Q16543
Secondary accession number(s): Q53YA2

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2002
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.

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·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

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

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents