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Q16543

- CDC37_HUMAN

UniProt

Q16543 - CDC37_HUMAN

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Protein

Hsp90 co-chaperone Cdc37

Gene

CDC37

Organism
Homo sapiens (Human)
Status
Reviewed - 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.1 Publication

GO - Molecular functioni

  1. heat shock protein binding Source: UniProtKB
  2. unfolded protein binding Source: ProtInc

GO - Biological processi

  1. protein targeting Source: ProtInc
  2. regulation of cyclin-dependent protein serine/threonine kinase activity Source: ProtInc
  3. regulation of interferon-gamma-mediated signaling pathway Source: MGI
  4. regulation of type I interferon-mediated signaling pathway Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Enzyme and pathway databases

ReactomeiREACT_115755. Signaling by ERBB2.
REACT_115852. Signaling by constitutively active EGFR.

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
Synonyms:CDC37A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:1735. CDC37.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: LIFEdb
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
  4. protein complex Source: Ensembl
  5. ruffle membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA402.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 378378Hsp90 co-chaperone Cdc37PRO_0000195057Add
BLAST
Initiator methioninei1 – 11Removed; alternate3 Publications
Chaini2 – 378377Hsp90 co-chaperone Cdc37, N-terminally processedPRO_0000423197Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei2 – 21N-acetylvaline; in Hsp90 co-chaperone Cdc37, N-terminally processed3 Publications
Modified residuei13 – 131Phosphoserine2 Publications
Modified residuei78 – 781N6-acetyllysine1 Publication
Modified residuei154 – 1541N6-acetyllysine1 Publication
Modified residuei377 – 3771Phosphoserine1 Publication

Post-translational modificationi

Constitutively sumoylated by UBE2I.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ16543.
PaxDbiQ16543.
PeptideAtlasiQ16543.
PRIDEiQ16543.

PTM databases

PhosphoSiteiQ16543.

Expressioni

Gene expression databases

BgeeiQ16543.
CleanExiHS_CDC37.
ExpressionAtlasiQ16543. baseline and differential.
GenevestigatoriQ16543.

Organism-specific databases

HPAiCAB004214.
HPA003928.

Interactioni

Subunit structurei

Forms a complex with Hsp90/HSP90AB1 and CDK6. Interacts with AR, CDK4, CDK6, EIF2AK1 and RB1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P115003EBI-295634,EBI-640126From a different organism.
AKT1P317492EBI-295634,EBI-296087
AKT3Q9Y2432EBI-295634,EBI-296115
APOEP026493EBI-295634,EBI-1222467
AURKBQ96GD42EBI-295634,EBI-624291
CDK15Q96Q402EBI-295634,EBI-1051975
CDK4P118027EBI-295634,EBI-295644
CDK6Q005343EBI-295634,EBI-295663
CDK9P507503EBI-295634,EBI-1383449
CHUKO151114EBI-295634,EBI-81249
CUL4BQ136202EBI-295634,EBI-456067
EGFRP005339EBI-295634,EBI-297353
EIF2AK1P332793EBI-295634,EBI-640100From a different organism.
ERBB2P046263EBI-295634,EBI-641062
FBXW2Q9UKT82EBI-295634,EBI-914727
FERP165912EBI-295634,EBI-1380661
FKBP4Q027903EBI-295634,EBI-1047444
HSP90AA1P0790013EBI-295634,EBI-296047
HSP90AB1P082386EBI-295634,EBI-352572
IFIT3O148794EBI-295634,EBI-745127
IKBKBO149203EBI-295634,EBI-81266
IKBKEQ141643EBI-295634,EBI-307369
IKBKGQ9Y6K94EBI-295634,EBI-81279
LRRK2Q5S0077EBI-295634,EBI-5323863
MAP3K14Q995582EBI-295634,EBI-358011
MAP3K7O43318-25EBI-295634,EBI-358700
NOS3P294744EBI-295634,EBI-1391623
PPP5CP530414EBI-295634,EBI-716663
PSEN1P497683EBI-295634,EBI-297277
RAF1P040494EBI-295634,EBI-365996
SQSTM1Q135013EBI-295634,EBI-307104
STK11Q158313EBI-295634,EBI-306838
STK38LQ9Y2H12EBI-295634,EBI-991501
ZNF843Q8N4462EBI-295634,EBI-6428016

Protein-protein interaction databases

BioGridi116312. 166 interactions.
DIPiDIP-27560N.
DIP-395N.
IntActiQ16543. 241 interactions.
MINTiMINT-99762.
STRINGi9606.ENSP00000222005.

Structurei

Secondary structure

1
378
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi149 – 16315
Helixi168 – 17710
Helixi179 – 1813
Helixi184 – 19916
Helixi203 – 22624
Helixi230 – 24112
Helixi247 – 27226
Helixi294 – 3007
Helixi317 – 3215
Beta strandi325 – 3273
Helixi328 – 33811

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1US7X-ray2.30B127-378[»]
2K5BNMR-B148-276[»]
2W0GX-ray1.88A148-276[»]
ProteinModelPortaliQ16543.
SMRiQ16543. Positions 148-347.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16543.

Family & Domainsi

Sequence similaritiesi

Belongs to the CDC37 family.Curated

Phylogenomic databases

eggNOGiNOG300020.
GeneTreeiENSGT00390000013443.
HOGENOMiHOG000018180.
HOVERGENiHBG056343.
InParanoidiQ16543.
KOiK09554.
OMAiEEANIKH.
OrthoDBiEOG73805G.
PhylomeDBiQ16543.
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.

Q16543-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVDYSVWDHI EVSDDEDETH PNIDTASLFR WRHQARVERM EQFQKEKEEL
60 70 80 90 100
DRGCRECKRK VAECQRKLKE LEVAEGGKAE LERLQAEAQQ LRKEERSWEQ
110 120 130 140 150
KLEEMRKKEK SMPWNVDTLS KDGFSKSMVN TKPEKTEEDS EEVREQKHKT
160 170 180 190 200
FVEKYEKQIK HFGMLRRWDD SQKYLSDNVH LVCEETANYL VIWCIDLEVE
210 220 230 240 250
EKCALMEQVA HQTIVMQFIL ELAKSLKVDP RACFRQFFTK IKTADRQYME
260 270 280 290 300
GFNDELEAFK ERVRGRAKLR IEKAMKEYEE EERKKRLGPG GLDPVEVYES
310 320 330 340 350
LPEELQKCFD VKDVQMLQDA ISKMDPTDAK YHMQRCIDSG LWVPNSKASE
360 370
AKEGEEAGPG DPLLEAVPKT GDEKDVSV
Length:378
Mass (Da):44,468
Last modified:November 1, 1996 - v1
Checksum:i55BFEFFF3C2A5442
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti360 – 3601G → E.1 Publication
Corresponds to variant rs280528 [ dbSNP | Ensembl ].
VAR_022220

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS12237.1.
PIRiG02313.
RefSeqiNP_008996.1. NM_007065.3.
UniGeneiHs.160958.

Genome annotation databases

EnsembliENST00000222005; ENSP00000222005; ENSG00000105401.
GeneIDi11140.
KEGGihsa:11140.
UCSCiuc002mof.1. human.

Polymorphism databases

DMDMi21542000.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS12237.1.
PIRi G02313.
RefSeqi NP_008996.1. NM_007065.3.
UniGenei Hs.160958.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali Q16543.
SMRi Q16543. Positions 148-347.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116312. 166 interactions.
DIPi DIP-27560N.
DIP-395N.
IntActi Q16543. 241 interactions.
MINTi MINT-99762.
STRINGi 9606.ENSP00000222005.

Chemistry

ChEMBLi CHEMBL1795123.

PTM databases

PhosphoSitei Q16543.

Polymorphism databases

DMDMi 21542000.

Proteomic databases

MaxQBi Q16543.
PaxDbi Q16543.
PeptideAtlasi Q16543.
PRIDEi Q16543.

Protocols and materials databases

DNASUi 11140.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000222005 ; ENSP00000222005 ; ENSG00000105401 .
GeneIDi 11140.
KEGGi hsa:11140.
UCSCi uc002mof.1. human.

Organism-specific databases

CTDi 11140.
GeneCardsi GC19M010501.
HGNCi HGNC:1735. CDC37.
HPAi CAB004214.
HPA003928.
MIMi 605065. gene.
neXtProti NX_Q16543.
PharmGKBi PA402.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG300020.
GeneTreei ENSGT00390000013443.
HOGENOMi HOG000018180.
HOVERGENi HBG056343.
InParanoidi Q16543.
KOi K09554.
OMAi EEANIKH.
OrthoDBi EOG73805G.
PhylomeDBi Q16543.
TreeFami TF101059.

Enzyme and pathway databases

Reactomei REACT_115755. Signaling by ERBB2.
REACT_115852. Signaling by constitutively active EGFR.

Miscellaneous databases

ChiTaRSi CDC37. human.
EvolutionaryTracei Q16543.
GeneWikii CDC37.
GenomeRNAii 11140.
NextBioi 42344.
PROi Q16543.
SOURCEi Search...

Gene expression databases

Bgeei Q16543.
CleanExi HS_CDC37.
ExpressionAtlasi Q16543. baseline and differential.
Genevestigatori Q16543.

Family and domain databases

InterProi IPR004918. Cdc37.
IPR013873. Cdc37_C.
IPR013874. Cdc37_Hsp90-bd.
IPR013855. Cdc37_N_dom.
[Graphical view ]
PANTHERi PTHR12800. PTHR12800. 1 hit.
Pfami PF08564. CDC37_C. 1 hit.
PF08565. CDC37_M. 1 hit.
PF03234. CDC37_N. 2 hits.
[Graphical view ]
SMARTi SM01069. CDC37_C. 1 hit.
SM01070. CDC37_M. 1 hit.
SM01071. CDC37_N. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. "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. 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. 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCDC37_HUMAN
AccessioniPrimary (citable) accession number: Q16543
Secondary accession number(s): Q53YA2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3