CDC37_SCHPO
ID CDC37_SCHPO Reviewed; 466 AA.
AC O94740;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Hsp90 co-chaperone Cdc37;
DE AltName: Full=Cell division control protein 37;
DE AltName: Full=Hsp90 chaperone protein kinase-targeting subunit;
GN Name=cdc37; ORFNames=SPBC9B6.10;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND FUNCTION.
RX PubMed=14652737; DOI=10.1007/s00438-003-0958-4;
RA Westwood P.K., Martin I.V., Fantes P.A.;
RT "Fission yeast Cdc37 is required for multiple cell cycle functions.";
RL Mol. Genet. Genomics 271:82-90(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION, SUBUNIT, INTERACTION WITH STY1, AND SUBCELLULAR LOCATION.
RX PubMed=12861001; DOI=10.1128/mcb.23.15.5132-5142.2003;
RA Tatebe H., Shiozaki K.;
RT "Identification of cdc37 as a novel regulator of the stress-responsive
RT mitogen-activated protein kinase.";
RL Mol. Cell. Biol. 23:5132-5142(2003).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Co-chaperone that binds to numerous kinases and promotes
CC their interaction with the Hsp90 complex, resulting in stabilization
CC and promotion of their activity. {ECO:0000269|PubMed:12861001,
CC ECO:0000269|PubMed:14652737}.
CC -!- SUBUNIT: Forms a complex with Hsp90. Interacts with sty1.
CC {ECO:0000269|PubMed:12861001}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=When in the nucleus
CC associated with chromatin.
CC -!- SIMILARITY: Belongs to the CDC37 family. {ECO:0000305}.
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DR EMBL; AJ132377; CAB38758.1; -; Genomic_DNA.
DR EMBL; AJ132376; CAB38757.1; -; mRNA.
DR EMBL; CU329671; CAB42371.2; -; Genomic_DNA.
DR PIR; T43653; T43653.
DR RefSeq; NP_595752.1; NM_001021652.2.
DR AlphaFoldDB; O94740; -.
DR SMR; O94740; -.
DR BioGRID; 277805; 34.
DR IntAct; O94740; 1.
DR STRING; 4896.SPBC9B6.10.1; -.
DR iPTMnet; O94740; -.
DR MaxQB; O94740; -.
DR PaxDb; O94740; -.
DR PRIDE; O94740; -.
DR EnsemblFungi; SPBC9B6.10.1; SPBC9B6.10.1:pep; SPBC9B6.10.
DR GeneID; 2541293; -.
DR KEGG; spo:SPBC9B6.10; -.
DR PomBase; SPBC9B6.10; cdc37.
DR VEuPathDB; FungiDB:SPBC9B6.10; -.
DR eggNOG; KOG2260; Eukaryota.
DR HOGENOM; CLU_033261_0_0_1; -.
DR InParanoid; O94740; -.
DR OMA; YSKWDQL; -.
DR PhylomeDB; O94740; -.
DR Reactome; R-SPO-114608; Platelet degranulation.
DR PRO; PR:O94740; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0031072; F:heat shock protein binding; IPI:PomBase.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IGI:PomBase.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR Gene3D; 1.20.58.610; -; 1.
DR InterPro; IPR004918; Cdc37.
DR InterPro; IPR013873; Cdc37_C.
DR InterPro; IPR013874; Cdc37_Hsp90-bd.
DR InterPro; IPR038189; Cdc37_Hsp90-bd_sf.
DR InterPro; IPR013855; Cdc37_N_dom.
DR PANTHER; PTHR12800; PTHR12800; 1.
DR Pfam; PF08564; CDC37_C; 1.
DR Pfam; PF08565; CDC37_M; 1.
DR Pfam; PF03234; CDC37_N; 1.
DR SMART; SM01069; CDC37_C; 1.
DR SMART; SM01070; CDC37_M; 1.
DR SMART; SM01071; CDC37_N; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Chaperone; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..466
FT /note="Hsp90 co-chaperone Cdc37"
FT /id="PRO_0000195066"
FT REGION 204..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 466 AA; 52554 MW; 647238B34CABB3C5 CRC64;
MAIDYSKWDK LELSDDSDIE VHPNVDKKSF IRWRQRDIHE KRAVRKQKME DIKGAMAMNR
RLLSRISEME TVLEKESPSD PYVLLGSFLE AKKSEDMDSA IPGGMSYHHM LMSLLKVIKD
AEDTTEEKSM DDSDKCLRRL KSHKERLLKL LEDAQKEYDT LEAESKNYIT SEDLHLGFDS
TYVQKKEPEK PKKTKTKKET IQVIESLNNP TPPTDFPGAK EQASTGNAPK NPVNENESED
EEGLSLSEDG KKFANIDFGD YSSSEEFLKE HLNILADEEE SDAILLEAFN AELEGKPSLA
KQYVHQALLI SYCRQLGPNG LSIFFQKIKD PNHQSQRLFL EDVHNTYVRI HERSAAISKE
QAESGEGVEQ IQLCAVDPNT KLSITIPEAG STDPETQKAR AAFESFPPNL QKALMTNDLD
KINVVLGKMA VENAEEVVEK LSSTGMLSIE EGIIDTTKGE TIPQLS
