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Q16543

- CDC37_HUMAN

UniProt

Q16543 - CDC37_HUMAN

Protein

Hsp90 co-chaperone Cdc37

Gene

CDC37

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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. protein binding Source: IntAct
    3. 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

    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

    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

    ArrayExpressiQ16543.
    BgeeiQ16543.
    CleanExiHS_CDC37.
    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
    IKBKGQ9Y6K93EBI-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. 116 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.
    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

    MVDYSVWDHI EVSDDEDETH PNIDTASLFR WRHQARVERM EQFQKEKEEL    50
    DRGCRECKRK VAECQRKLKE LEVAEGGKAE LERLQAEAQQ LRKEERSWEQ 100
    KLEEMRKKEK SMPWNVDTLS KDGFSKSMVN TKPEKTEEDS EEVREQKHKT 150
    FVEKYEKQIK HFGMLRRWDD SQKYLSDNVH LVCEETANYL VIWCIDLEVE 200
    EKCALMEQVA HQTIVMQFIL ELAKSLKVDP RACFRQFFTK IKTADRQYME 250
    GFNDELEAFK ERVRGRAKLR IEKAMKEYEE EERKKRLGPG GLDPVEVYES 300
    LPEELQKCFD VKDVQMLQDA ISKMDPTDAK YHMQRCIDSG LWVPNSKASE 350
    AKEGEEAGPG DPLLEAVPKT GDEKDVSV 378
    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. 116 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.
    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

    ArrayExpressi Q16543.
    Bgeei Q16543.
    CleanExi HS_CDC37.
    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

    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 1, 2014
    This is version 136 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