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Q16543 (CDC37_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Cleaved into the following chain:

  1. Hsp90 co-chaperone Cdc37, N-terminally processed
Gene names
Name:CDC37
Synonyms:CDC37A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length378 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 378378Hsp90 co-chaperone Cdc37
PRO_0000195057
Initiator methionine11Removed; alternate Ref.15
Chain2 – 378377Hsp90 co-chaperone Cdc37, N-terminally processed
PRO_0000423197

Amino acid modifications

Modified residue11N-acetylmethionine Ref.15
Modified residue21N-acetylvaline; in Hsp90 co-chaperone Cdc37, N-terminally processed Ref.15 Ref.17 Ref.19
Modified residue131Phosphoserine Ref.17 Ref.19
Modified residue781N6-acetyllysine Ref.16
Modified residue1541N6-acetyllysine Ref.16
Modified residue3771Phosphoserine Ref.14

Natural variations

Natural variant3601G → E. Ref.3
Corresponds to variant rs280528 [ dbSNP | Ensembl ].
VAR_022220

Secondary structure

...................... 378
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q16543 [UniParc].

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

FASTA37844,468
        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' 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. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND VAL-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[16]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"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].
[19]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Web resources

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.
PIRG02313.
RefSeqNP_008996.1. NM_007065.3.
UniGeneHs.160958.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1US7X-ray2.30B127-378[»]
2K5BNMR-B148-276[»]
2W0GX-ray1.88A148-276[»]
ProteinModelPortalQ16543.
SMRQ16543. Positions 148-347.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116312. 133 interactions.
DIPDIP-27560N.
DIP-395N.
IntActQ16543. 140 interactions.
MINTMINT-99762.
STRING9606.ENSP00000222005.

Chemistry

ChEMBLCHEMBL1795123.

PTM databases

PhosphoSiteQ16543.

Polymorphism databases

DMDM21542000.

Proteomic databases

PaxDbQ16543.
PeptideAtlasQ16543.
PRIDEQ16543.

Protocols and materials databases

DNASU11140.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000222005; ENSP00000222005; ENSG00000105401.
GeneID11140.
KEGGhsa:11140.
UCSCuc002mof.1. human.

Organism-specific databases

CTD11140.
GeneCardsGC19M010501.
HGNCHGNC:1735. CDC37.
HPACAB004214.
HPA003928.
MIM605065. gene.
neXtProtNX_Q16543.
PharmGKBPA402.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG300020.
HOGENOMHOG000018180.
HOVERGENHBG056343.
InParanoidQ16543.
KOK09554.
OrthoDBEOG73805G.
PhylomeDBQ16543.
TreeFamTF101059.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.

Gene expression databases

ArrayExpressQ16543.
BgeeQ16543.
CleanExHS_CDC37.
GenevestigatorQ16543.

Family and domain databases

InterProIPR004918. Cdc37.
IPR013873. Cdc37_C.
IPR013874. Cdc37_Hsp90-bd.
IPR013855. Cdc37_N_dom.
[Graphical view]
PANTHERPTHR12800. PTHR12800. 1 hit.
PfamPF08564. CDC37_C. 1 hit.
PF08565. CDC37_M. 1 hit.
PF03234. CDC37_N. 2 hits.
[Graphical view]
SMARTSM01069. CDC37_C. 1 hit.
SM01070. CDC37_M. 1 hit.
SM01071. CDC37_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCDC37. human.
EvolutionaryTraceQ16543.
GeneWikiCDC37.
GenomeRNAi11140.
NextBio42344.
PROQ16543.
SOURCESearch...

Entry information

Entry nameCDC37_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

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