CDC5_YEAST
ID CDC5_YEAST Reviewed; 705 AA.
AC P32562; D6VZH5;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Cell cycle serine/threonine-protein kinase CDC5/MSD2;
DE EC=2.7.11.21 {ECO:0000269|PubMed:11371343, ECO:0000269|PubMed:12056824};
GN Name=CDC5; Synonyms=MSD2, PKX2; OrderedLocusNames=YMR001C;
GN ORFNames=YM8270.03C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 204626 / S288c / A364A;
RX PubMed=8321244; DOI=10.1128/mcb.13.7.4445-4457.1993;
RA Kitada K., Sugino A., Johnston L.H., Johnson A.L.;
RT "A multicopy suppressor gene of the Saccharomyces cerevisiae G1 cell cycle
RT mutant gene dbf4 encodes a protein kinase and is identified as CDC5.";
RL Mol. Cell. Biol. 13:4445-4457(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION IN PHOSPHORYLATION OF SCC1, AND CATALYTIC ACTIVITY.
RX PubMed=11371343; DOI=10.1016/s0092-8674(01)00362-2;
RA Alexandru G., Uhlmann F., Mechtler K., Poupart M.-A., Nasmyth K.;
RT "Phosphorylation of the cohesin subunit Scc1 by Polo/Cdc5 kinase regulates
RT sister chromatid separation in yeast.";
RL Cell 105:459-472(2001).
RN [5]
RP FUNCTION IN PHOSPHORYLATION OF NET1, AND CATALYTIC ACTIVITY.
RX PubMed=12056824; DOI=10.1016/s0006-291x(02)00544-2;
RA Yoshida S., Toh-e A.;
RT "Budding yeast Cdc5 phosphorylates Net1 and assists Cdc14 release from the
RT nucleolus.";
RL Biochem. Biophys. Res. Commun. 294:687-691(2002).
RN [6]
RP FUNCTION AS A COMPONENT OF THE FEAR NETWORK.
RX PubMed=11832211; DOI=10.1016/s0092-8674(02)00618-9;
RA Stegmeier F., Visintin R., Amon A.;
RT "Separase, polo kinase, the kinetochore protein Slk19, and Spo12 function
RT in a network that controls Cdc14 localization during early anaphase.";
RL Cell 108:207-220(2002).
RN [7]
RP INTERACTION WITH CDC48.
RX PubMed=14636562; DOI=10.1016/s0092-8674(03)00815-8;
RA Cao K., Nakajima R., Meyer H.H., Zheng Y.;
RT "The AAA-ATPase Cdc48/p97 regulates spindle disassembly at the end of
RT mitosis.";
RL Cell 115:355-367(2003).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-419, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-23, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Protein kinase required for the cell cycle where it is
CC involved in mitotic exit. A component of the fear (CDC14 early anaphase
CC release) network which promotes CDC14 release from the nucleolus during
CC early anaphase. Phosphorylates SCC1/MCD1 and NET1.
CC {ECO:0000269|PubMed:11371343, ECO:0000269|PubMed:11832211,
CC ECO:0000269|PubMed:12056824}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.21;
CC Evidence={ECO:0000269|PubMed:11371343, ECO:0000269|PubMed:12056824};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.21; Evidence={ECO:0000269|PubMed:11371343,
CC ECO:0000269|PubMed:12056824};
CC -!- SUBUNIT: Interacts with CDC48; the interaction is likely to result in
CC CDC5 degradation. {ECO:0000269|PubMed:14636562}.
CC -!- INTERACTION:
CC P32562; Q00684: CDC14; NbExp=2; IntAct=EBI-4440, EBI-4192;
CC P32562; P06243: CDC7; NbExp=11; IntAct=EBI-4440, EBI-4451;
CC P32562; P41813: FKH2; NbExp=2; IntAct=EBI-4440, EBI-6973;
CC P32562; Q04087: LRS4; NbExp=6; IntAct=EBI-4440, EBI-32189;
CC P32562; P22216: RAD53; NbExp=3; IntAct=EBI-4440, EBI-17843;
CC P32562; P14737: RAD9; NbExp=2; IntAct=EBI-4440, EBI-14788;
CC P32562; P23624: SPO13; NbExp=8; IntAct=EBI-4440, EBI-17719;
CC P32562; P32944: SWE1; NbExp=4; IntAct=EBI-4440, EBI-18607;
CC -!- MISCELLANEOUS: Present with 1480 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDC5/Polo subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; M84220; AAA02576.1; -; Unassigned_DNA.
DR EMBL; Z48613; CAA88516.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09899.1; -; Genomic_DNA.
DR PIR; A48144; A48144.
DR RefSeq; NP_013714.1; NM_001182497.1.
DR PDB; 6MF4; X-ray; 1.80 A; A=418-705.
DR PDB; 6MF5; X-ray; 2.70 A; A/B=418-705.
DR PDB; 6MF6; X-ray; 3.40 A; A/B=418-705.
DR PDBsum; 6MF4; -.
DR PDBsum; 6MF5; -.
DR PDBsum; 6MF6; -.
DR AlphaFoldDB; P32562; -.
DR SMR; P32562; -.
DR BioGRID; 35171; 219.
DR DIP; DIP-2321N; -.
DR IntAct; P32562; 65.
DR MINT; P32562; -.
DR STRING; 4932.YMR001C; -.
DR iPTMnet; P32562; -.
DR MaxQB; P32562; -.
DR PaxDb; P32562; -.
DR PRIDE; P32562; -.
DR EnsemblFungi; YMR001C_mRNA; YMR001C; YMR001C.
DR GeneID; 855013; -.
DR KEGG; sce:YMR001C; -.
DR SGD; S000004603; CDC5.
DR VEuPathDB; FungiDB:YMR001C; -.
DR eggNOG; KOG0575; Eukaryota.
DR GeneTree; ENSGT00940000157752; -.
DR HOGENOM; CLU_000288_46_2_1; -.
DR InParanoid; P32562; -.
DR OMA; LKHFERY; -.
DR BioCyc; YEAST:G3O-32712-MON; -.
DR BRENDA; 2.7.11.21; 984.
DR Reactome; R-SCE-156711; Polo-like kinase mediated events.
DR Reactome; R-SCE-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
DR Reactome; R-SCE-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-SCE-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-SCE-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
DR PRO; PR:P32562; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P32562; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000922; C:spindle pole; IDA:SGD.
DR GO; GO:0005816; C:spindle pole body; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019237; F:centromeric DNA binding; IDA:SGD.
DR GO; GO:0051219; F:phosphoprotein binding; IDA:SGD.
DR GO; GO:0004672; F:protein kinase activity; IDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:SGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0010458; P:exit from mitosis; IGI:SGD.
DR GO; GO:0090306; P:meiotic spindle assembly; IMP:SGD.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:1904750; P:negative regulation of protein localization to nucleolus; IMP:SGD.
DR GO; GO:1905339; P:positive regulation of cohesin unloading; IMP:SGD.
DR GO; GO:0010696; P:positive regulation of mitotic spindle pole body separation; IMP:SGD.
DR GO; GO:0110083; P:positive regulation of protein localization to cell division site involved in mitotic actomyosin contractile ring assembly; IMP:SGD.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
DR GO; GO:1903353; P:regulation of nucleus organization; IMP:SGD.
DR GO; GO:1902542; P:regulation of protein localization to mitotic spindle pole body; IGI:SGD.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IMP:SGD.
DR GO; GO:0070194; P:synaptonemal complex disassembly; IGI:SGD.
DR CDD; cd13118; POLO_box_1; 1.
DR CDD; cd13117; POLO_box_2; 1.
DR Gene3D; 3.30.1120.30; -; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033701; POLO_box_1.
DR InterPro; IPR033695; POLO_box_2.
DR InterPro; IPR000959; POLO_box_dom.
DR InterPro; IPR036947; POLO_box_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00659; POLO_box; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50078; POLO_BOX; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; Cell division; Kinase; Mitosis;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..705
FT /note="Cell cycle serine/threonine-protein kinase
FT CDC5/MSD2"
FT /id="PRO_0000085762"
FT DOMAIN 82..337
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 520..587
FT /note="POLO box 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT DOMAIN 619..692
FT /note="POLO box 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT REGION 41..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 204
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 88..96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 23
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT HELIX 437..450
FT /evidence="ECO:0007829|PDB:6MF5"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:6MF4"
FT HELIX 471..497
FT /evidence="ECO:0007829|PDB:6MF4"
FT STRAND 502..504
FT /evidence="ECO:0007829|PDB:6MF6"
FT STRAND 514..518
FT /evidence="ECO:0007829|PDB:6MF4"
FT STRAND 521..530
FT /evidence="ECO:0007829|PDB:6MF4"
FT STRAND 535..538
FT /evidence="ECO:0007829|PDB:6MF4"
FT STRAND 544..547
FT /evidence="ECO:0007829|PDB:6MF4"
FT STRAND 551..560
FT /evidence="ECO:0007829|PDB:6MF4"
FT TURN 561..563
FT /evidence="ECO:0007829|PDB:6MF4"
FT STRAND 564..571
FT /evidence="ECO:0007829|PDB:6MF4"
FT HELIX 572..574
FT /evidence="ECO:0007829|PDB:6MF4"
FT HELIX 577..579
FT /evidence="ECO:0007829|PDB:6MF4"
FT HELIX 580..593
FT /evidence="ECO:0007829|PDB:6MF4"
FT TURN 607..611
FT /evidence="ECO:0007829|PDB:6MF4"
FT STRAND 615..620
FT /evidence="ECO:0007829|PDB:6MF4"
FT STRAND 622..629
FT /evidence="ECO:0007829|PDB:6MF4"
FT STRAND 634..638
FT /evidence="ECO:0007829|PDB:6MF4"
FT STRAND 643..647
FT /evidence="ECO:0007829|PDB:6MF4"
FT TURN 648..651
FT /evidence="ECO:0007829|PDB:6MF4"
FT STRAND 652..656
FT /evidence="ECO:0007829|PDB:6MF4"
FT STRAND 662..666
FT /evidence="ECO:0007829|PDB:6MF4"
FT HELIX 667..673
FT /evidence="ECO:0007829|PDB:6MF4"
FT HELIX 680..682
FT /evidence="ECO:0007829|PDB:6MF4"
FT HELIX 684..698
FT /evidence="ECO:0007829|PDB:6MF4"
SQ SEQUENCE 705 AA; 81031 MW; B5A25F1BBBEAA3DC CRC64;
MSLGPLKAIN DKQLNTRSKL VHTPIKGNTA DLVGKENHFK QTKRLDPNND HHHQPAQKKK
REKLSALCKT PPSLIKTRGK DYHRGHFLGE GGFARCFQIK DDSGEIFAAK TVAKASIKSE
KTRKKLLSEI QIHKSMSHPN IVQFIDCFED DSNVYILLEI CPNGSLMELL KRRKVLTEPE
VRFFTTQICG AIKYMHSRRV IHRDLKLGNI FFDSNYNLKI GDFGLAAVLA NESERKYTIC
GTPNYIAPEV LMGKHSGHSF EVDIWSLGVM LYALLIGKPP FQARDVNTIY ERIKCRDFSF
PRDKPISDEG KILIRDILSL DPIERPSLTE IMDYVWFRGT FPPSIPSTVM SEAPNFEDIP
EEQSLVNFKD CMEKSLLLES MSSDKIQRQK RDYISSIKSS IDKLEEYHQN RPFLPHSLSP
GGTKQKYKEV VDIEAQRRLN DLAREARIRR AQQAVLRKEL IATSTNVIKS EISLRILASE
CHLTLNGIVE AEAQYKMGGL PKSRLPKIKH PMIVTKWVDY SNKHGFSYQL STEDIGVLFN
NGTTVLRLAD AEEFWYISYD DREGWVASHY LLSEKPRELS RHLEVVDFFA KYMKANLSRV
STFGREEYHK DDVFLRRYTR YKPFVMFELS DGTFQFNFKD HHKMAISDGG KLVTYISPSH
ESTTYPLVEV LKYGEIPGYP ESNFREKLTL IKEGLKQKST IVTVD
