CDC14_YEAST
ID CDC14_YEAST Reviewed; 551 AA.
AC Q00684; D6VTQ8; Q05180; Q05673;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Tyrosine-protein phosphatase CDC14;
DE EC=3.1.3.48;
GN Name=CDC14; Synonyms=OAF3; OrderedLocusNames=YFR028C;
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 [GENOMIC DNA].
RX PubMed=1597462; DOI=10.1016/s0021-9258(19)49907-9;
RA Wan J., Xu H., Grunstein M.;
RT "CDC14 of Saccharomyces cerevisiae. Cloning, sequence analysis, and
RT transcription during the cell cycle.";
RL J. Biol. Chem. 267:11274-11280(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=8668128; DOI=10.1007/bf02172916;
RA Shirayama M., Matsui Y., Toh-e A.;
RT "Dominant mutant alleles of yeast protein kinase gene CDC15 suppress the
RT lte1 defect in termination of M phase and genetically interact with
RT CDC14.";
RL Mol. Gen. Genet. 251:176-185(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8686381;
RX DOI=10.1002/(sici)1097-0061(199602)12:2<177::aid-yea896>3.0.co;2-a;
RA Eki T., Naitou M., Hagiwara H., Abe M., Ozawa M., Sasanuma S., Sasanuma M.,
RA Tsuchiya Y., Shibata T., Watanabe K., Ono A., Yamazaki M., Tashiro H.,
RA Hanaoka F., Murakami Y.;
RT "Fifteen open reading frames in a 30.8 kb region of the right arm of
RT chromosome VI from Saccharomyces cerevisiae.";
RL Yeast 12:177-190(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-421.
RA Mai B., Lipp M.;
RL Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION.
RX PubMed=7021319; DOI=10.1093/genetics/96.4.859;
RA Schild D., Byers B.;
RT "Diploid spore formation and other meiotic effects of two cell-division-
RT cycle mutations of Saccharomyces cerevisiae.";
RL Genetics 96:859-876(1980).
RN [8]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND FUNCTION.
RX PubMed=9295359; DOI=10.1074/jbc.272.38.24054;
RA Taylor G.S., Liu Y., Baskerville C., Charbonneau H.;
RT "The activity of Cdc14p, an oligomeric dual specificity protein phosphatase
RT from Saccharomyces cerevisiae, is required for cell cycle progression.";
RL J. Biol. Chem. 272:24054-24063(1997).
RN [9]
RP INTERACTION WITH SIC1, AND FUNCTION IN DEPHOSPHORYLATION OF CDH1; SIC1 AND
RP SWI5.
RX PubMed=9885559; DOI=10.1016/s1097-2765(00)80286-5;
RA Visintin R., Craig K., Hwang E.S., Prinz S., Tyers M., Amon A.;
RT "The phosphatase Cdc14 triggers mitotic exit by reversal of Cdk-dependent
RT phosphorylation.";
RL Mol. Cell 2:709-718(1998).
RN [10]
RP FUNCTION, AND SUBUNIT.
RX PubMed=11511359; DOI=10.1016/s1097-2765(01)00291-x;
RA Shou W., Sakamoto K.M., Keener J., Morimoto K.W., Traverso E.E., Azzam R.,
RA Hoppe G.J., Feldman R.M.R., DeModena J., Moazed D., Charbonneau H.,
RA Nomura M., Deshaies R.J.;
RT "Net1 stimulates RNA polymerase I transcription and regulates nucleolar
RT structure independently of controlling mitotic exit.";
RL Mol. Cell 8:45-55(2001).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12737806; DOI=10.1016/s1534-5807(03)00130-8;
RA Marston A.L., Lee B.H., Amon A.;
RT "The Cdc14 phosphatase and the FEAR network control meiotic spindle
RT disassembly and chromosome segregation.";
RL Dev. Cell 4:711-726(2003).
RN [12]
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 [13]
RP FUNCTION.
RX PubMed=15137939; DOI=10.1016/s0092-8674(04)00413-1;
RA D'Amours D., Stegmeier F., Amon A.;
RT "Cdc14 and condensin control the dissolution of cohesin-independent
RT chromosome linkages at repeated DNA.";
RL Cell 117:455-469(2004).
RN [14]
RP FUNCTION.
RX PubMed=15004526;
RA Torres-Rosell J., Machin F., Jarmuz A., Aragon L.;
RT "Nucleolar segregation lags behind the rest of the genome and requires
RT Cdc14p activation by the FEAR network.";
RL Cell Cycle 3:496-502(2004).
RN [15]
RP FUNCTION.
RX PubMed=15190202; DOI=10.4161/cc.3.7.1003;
RA Wang B.D., Yong-Gonzalez V., Strunnikov A.V.;
RT "Cdc14p/FEAR pathway controls segregation of nucleolus in S. cerevisiae by
RT facilitating condensin targeting to rDNA chromatin in anaphase.";
RL Cell Cycle 3:960-967(2004).
RN [16]
RP CATALYTIC ACTIVITY.
RX PubMed=15128740; DOI=10.1074/jbc.m402217200;
RA Wang W.Q., Bembenek J., Gee K.R., Yu H., Charbonneau H., Zhang Z.Y.;
RT "Kinetic and mechanistic studies of a cell cycle protein phosphatase
RT Cdc14.";
RL J. Biol. Chem. 279:30459-30468(2004).
RN [17]
RP FUNCTION IN DEPHOSPHORYLATION OF SWI6.
RX PubMed=14993267; DOI=10.1128/mcb.24.6.2277-2285.2004;
RA Geymonat M., Spanos A., Wells G.P., Smerdon S.J., Sedgwick S.G.;
RT "Clb6/Cdc28 and Cdc14 regulate phosphorylation status and cellular
RT localization of Swi6.";
RL Mol. Cell. Biol. 24:2277-2285(2004).
RN [18]
RP SUBCELLULAR LOCATION.
RX PubMed=15273393; DOI=10.1126/science.1099402;
RA Azzam R., Chen S.L., Shou W., Mah A.S., Alexandru G., Nasmyth K.,
RA Annan R.S., Carr S.A., Deshaies R.J.;
RT "Phosphorylation by cyclin B-Cdk underlies release of mitotic exit
RT activator Cdc14 from the nucleolus.";
RL Science 305:516-519(2004).
RN [19]
RP SUBCELLULAR LOCATION, INTERACTION WITH CRM1, AND FUNCTION.
RX PubMed=15917648; DOI=10.4161/cc.4.7.1798;
RA Bembenek J., Kang J., Kurischko C., Li B., Raab J.R., Belanger K.D.,
RA Luca F.C., Yu H.;
RT "Crm1-mediated nuclear export of Cdc14 is required for the completion of
RT cytokinesis in budding yeast.";
RL Cell Cycle 4:961-971(2005).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [21]
RP FUNCTION IN DEPHOSPHORYLATION OF DBP2; SIC1 AND SLD2.
RX PubMed=17116692; DOI=10.1128/mcb.01069-06;
RA Bloom J., Cross F.R.;
RT "Novel role for Cdc14 sequestration: Cdc14 dephosphorylates factors that
RT promote DNA replication.";
RL Mol. Cell. Biol. 27:842-853(2007).
RN [22]
RP FUNCTION IN DEPHOSPHORYLATION OF ASE1.
RX PubMed=18235228; DOI=10.4161/cc.7.3.5349;
RA Khmelinskii A., Schiebel E.;
RT "Assembling the spindle midzone in the right place at the right time.";
RL Cell Cycle 7:283-286(2008).
RN [23]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CDC5.
RX PubMed=18927509; DOI=10.4161/cc.7.20.6852;
RA Rahal R., Amon A.;
RT "The Polo-like kinase Cdc5 interacts with FEAR network components and
RT Cdc14.";
RL Cell Cycle 7:3262-3272(2008).
RN [24]
RP SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH TOF2.
RX PubMed=18595708; DOI=10.1016/j.cub.2008.06.025;
RA Geil C., Schwab M., Seufert W.;
RT "A nucleolus-localized activator of Cdc14 phosphatase supports rDNA
RT segregation in yeast mitosis.";
RL Curr. Biol. 18:1001-1005(2008).
RN [25]
RP FUNCTION IN DEPHOSPHORYLATION OF ACM1.
RX PubMed=18287090; DOI=10.1074/jbc.m710011200;
RA Hall M.C., Jeong D.E., Henderson J.T., Choi E., Bremmer S.C., Iliuk A.B.,
RA Charbonneau H.;
RT "Cdc28 and Cdc14 control stability of the anaphase-promoting complex
RT inhibitor Acm1.";
RL J. Biol. Chem. 283:10396-10407(2008).
RN [26]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH UTP7.
RX PubMed=18794331; DOI=10.1083/jcb.200802085;
RA Jwa M., Kim J.H., Chan C.S.;
RT "Regulation of Sli15/INCENP, kinetochore, and Cdc14 phosphatase functions
RT by the ribosome biogenesis protein Utp7.";
RL J. Cell Biol. 182:1099-1111(2008).
RN [27]
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 [28]
RP SUBCELLULAR LOCATION.
RX PubMed=19221193; DOI=10.1083/jcb.200812022;
RA Mohl D.A., Huddleston M.J., Collingwood T.S., Annan R.S., Deshaies R.J.;
RT "Dbf2-Mob1 drives relocalization of protein phosphatase Cdc14 to the
RT cytoplasm during exit from mitosis.";
RL J. Cell Biol. 184:527-539(2009).
RN [29]
RP FUNCTION.
RX PubMed=19339280; DOI=10.1091/mbc.e08-11-1150;
RA Chiroli E., Rancati G., Catusi I., Lucchini G., Piatti S.;
RT "Cdc14 inhibition by the spindle assembly checkpoint prevents unscheduled
RT centrosome separation in budding yeast.";
RL Mol. Biol. Cell 20:2626-2637(2009).
RN [30]
RP FUNCTION.
RX PubMed=19158678; DOI=10.1038/nature07652;
RA Clemente-Blanco A., Mayan-Santos M., Schneider D.A., Machin F., Jarmuz A.,
RA Tschochner H., Aragon L.;
RT "Cdc14 inhibits transcription by RNA polymerase I during anaphase.";
RL Nature 458:219-222(2009).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467, 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).
RN [32]
RP FUNCTION IN DEPHOSPHORYLATION OF INCENP.
RX PubMed=20619650; DOI=10.1016/j.cub.2010.06.023;
RA Mirchenko L., Uhlmann F.;
RT "Sli15(INCENP) dephosphorylation prevents mitotic checkpoint reengagement
RT due to loss of tension at anaphase onset.";
RL Curr. Biol. 20:1396-1401(2010).
RN [33]
RP FUNCTION IN DEPHOSPHORYLATION OF DSN1.
RX PubMed=20923974; DOI=10.1534/genetics.110.123653;
RA Akiyoshi B., Biggins S.;
RT "Cdc14-dependent dephosphorylation of a kinetochore protein prior to
RT anaphase in Saccharomyces cerevisiae.";
RL Genetics 186:1487-1491(2010).
RN [34]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20660629; DOI=10.1083/jcb.201002026;
RA Manzoni R., Montani F., Visintin C., Caudron F., Ciliberto A., Visintin R.;
RT "Oscillations in Cdc14 release and sequestration reveal a circuit
RT underlying mitotic exit.";
RL J. Cell Biol. 190:209-222(2010).
RN [35]
RP SUBCELLULAR LOCATION.
RX PubMed=21098112; DOI=10.1083/jcb.201007025;
RA Rossio V., Galati E., Ferrari M., Pellicioli A., Sutani T., Shirahige K.,
RA Lucchini G., Piatti S.;
RT "The RSC chromatin-remodeling complex influences mitotic exit and
RT adaptation to the spindle assembly checkpoint by controlling the Cdc14
RT phosphatase.";
RL J. Cell Biol. 191:981-997(2010).
RN [36]
RP FUNCTION IN DEPHOSPHORYLATION OF ORC2; ORC6; CDC6 AND MCM3.
RX PubMed=20980394; DOI=10.1242/jcs.075366;
RA Zhai Y., Yung P.Y., Huo L., Liang C.;
RT "Cdc14p resets the competency of replication licensing by dephosphorylating
RT multiple initiation proteins during mitotic exit in budding yeast.";
RL J. Cell Sci. 123:3933-3943(2010).
RN [37]
RP FUNCTION.
RX PubMed=22078879; DOI=10.1016/j.cell.2011.09.047;
RA Bouchoux C., Uhlmann F.;
RT "A quantitative model for ordered Cdk substrate dephosphorylation during
RT mitotic exit.";
RL Cell 147:803-814(2011).
RN [38]
RP FUNCTION, AND MUTAGENESIS OF ALA-280.
RX PubMed=21784165; DOI=10.1016/j.fgb.2011.07.001;
RA Tzeng Y.W., Huang J.N., Schuyler S.C., Wu C.H., Juang Y.L.;
RT "Functions of the mitotic B-type cyclins CLB1, CLB2, and CLB3 at mitotic
RT exit antagonized by the CDC14 phosphatase.";
RL Fungal Genet. Biol. 48:966-978(2011).
RN [39]
RP MUTAGENESIS OF ASP-253 AND CYS-283, INTERACTION WITH BNI1; BNR1 AND KAR9,
RP AND FUNCTION IN DEPHOSPHORYLATION OF BNI1; BNR1 AND KAR9.
RX PubMed=21127052; DOI=10.1074/jbc.m110.205054;
RA Bloom J., Cristea I.M., Procko A.L., Lubkov V., Chait B.T., Snyder M.,
RA Cross F.R.;
RT "Global analysis of Cdc14 phosphatase reveals diverse roles in mitotic
RT processes.";
RL J. Biol. Chem. 286:5434-5445(2011).
RN [40]
RP SUBCELLULAR LOCATION.
RX PubMed=21690311; DOI=10.1083/jcb.201103019;
RA Kerr G.W., Sarkar S., Tibbles K.L., Petronczki M., Millar J.B.,
RA Arumugam P.;
RT "Meiotic nuclear divisions in budding yeast require PP2A(Cdc55)-mediated
RT antagonism of Net1 phosphorylation by Cdk.";
RL J. Cell Biol. 193:1157-1166(2011).
RN [41]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=21690308; DOI=10.1083/jcb.201103076;
RA Bizzari F., Marston A.L.;
RT "Cdc55 coordinates spindle assembly and chromosome disjunction during
RT meiosis.";
RL J. Cell Biol. 193:1213-1228(2011).
RN [42]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22872148; DOI=10.1038/emboj.2012.224;
RA Sanchez-Diaz A., Nkosi P.J., Murray S., Labib K.;
RT "The mitotic exit network and Cdc14 phosphatase initiate cytokinesis by
RT counteracting CDK phosphorylations and blocking polarised growth.";
RL EMBO J. 31:3620-3634(2012).
RN [43]
RP FUNCTION.
RX PubMed=22117071; DOI=10.1074/jbc.m111.281105;
RA Bremmer S.C., Hall H., Martinez J.S., Eissler C.L., Hinrichsen T.H.,
RA Rossie S., Parker L.L., Hall M.C., Charbonneau H.;
RT "Cdc14 phosphatases preferentially dephosphorylate a subset of cyclin-
RT dependent kinase (Cdk) sites containing phosphoserine.";
RL J. Biol. Chem. 287:1662-1669(2012).
RN [44]
RP SUBCELLULAR LOCATION, AND FUNCTION IN DEPHOSPHORYLATION OF INN1.
RX PubMed=22454527; DOI=10.1242/jcs.106021;
RA Palani S., Meitinger F., Boehm M.E., Lehmann W.D., Pereira G.;
RT "Cdc14-dependent dephosphorylation of Inn1 contributes to Inn1-Cyk3 complex
RT formation.";
RL J. Cell Sci. 125:3091-3096(2012).
RN [45]
RP FUNCTION IN DEPHOSPHORYLATION OF CHS2.
RX PubMed=22072794; DOI=10.1091/mbc.e11-05-0434;
RA Chin C.F., Bennett A.M., Ma W.K., Hall M.C., Yeong F.M.;
RT "Dependence of Chs2 ER export on dephosphorylation by cytoplasmic Cdc14
RT ensures that septum formation follows mitosis.";
RL Mol. Biol. Cell 23:45-58(2012).
RN [46]
RP FUNCTION.
RX PubMed=22363215; DOI=10.1371/journal.pgen.1002509;
RA Quevedo O., Garcia-Luis J., Matos-Perdomo E., Aragon L., Machin F.;
RT "Nondisjunction of a single chromosome leads to breakage and activation of
RT DNA damage checkpoint in G2.";
RL PLoS Genet. 8:E1002509-E1002509(2012).
RN [47]
RP SUBCELLULAR LOCATION.
RX PubMed=24039885; DOI=10.1371/journal.pone.0073194;
RA Faust A.M., Wong C.C., Yates Iii J.R., Drubin D.G., Barnes G.;
RT "The FEAR protein Slk19 restricts Cdc14 phosphatase to the nucleus until
RT the end of anaphase, regulating its participation in mitotic exit in
RT Saccharomyces cerevisiae.";
RL PLoS ONE 8:E73194-E73194(2013).
CC -!- FUNCTION: Protein phosphatase which antagonizes mitotic cyclin-
CC dependent kinase CDC28, the inactivation of which is essential for exit
CC from mitosis. To access its substrates, is released from nucleolar
CC sequestration during mitosis. Plays an essential in coordinating the
CC nuclear division cycle with cytokinesis through the cytokinesis
CC checkpoint. Involved in chromosome segregation, where it is required
CC for meiosis I spindle dissambly as well as for establishing two
CC consecutive chromosome segregation phases. Allows damaged actomyosin
CC rings to be maintained to facilitate completion of cell division in
CC response to minor perturbation of the cell division machinery. Inhibits
CC transcription of ribosomal genes (rDNA) during anaphase and controls
CC segregation of nucleolus by facilitating condensin targeting to rDNA
CC chromatin in anaphase. Dephosphorylates SIC1, a CDC28 inhibitor, and
CC SWI5, a transcription factor for SIC1, and induces degradation of
CC mitotic cyclins, likely by dephosphorylating the activator of mitotic
CC cyclin degradation, CDH1. Dephosphorylates the microtubule bundling
CC factor ASE1 which is required to define a centered and focused mitotic
CC spindle midzone that can drive continuous spindle elongation.
CC Dephosphorylates the anaphase-promoting complex inhibitor ACM1, leading
CC to its degradation. Facilitates INN1-CYK3 complex formation which
CC promotes cytokinesis through the dephosphorylation of CDC28-
CC phosphosphorylated INN1. Reverts also the inhibitory CDC28
CC phosphorylation of CHS2 for endoplasmic reticulum export, ensuring that
CC septum formation is contingent upon chromosome separation and exit from
CC mitosis. Additional substrates for CDC14 are the formins BNI1 and BNR1,
CC as well as CDC6, DBP2, DSN1, INCENP, KAR9, MCM3, ORC2, ORC6, SLD2, and
CC SWI6. Activity is inhibited by interaction with NET1 which sequesters
CC it to the nucleolus. {ECO:0000269|PubMed:11511359,
CC ECO:0000269|PubMed:12737806, ECO:0000269|PubMed:14993267,
CC ECO:0000269|PubMed:15004526, ECO:0000269|PubMed:15137939,
CC ECO:0000269|PubMed:15190202, ECO:0000269|PubMed:15917648,
CC ECO:0000269|PubMed:17116692, ECO:0000269|PubMed:18235228,
CC ECO:0000269|PubMed:18287090, ECO:0000269|PubMed:18595708,
CC ECO:0000269|PubMed:19158678, ECO:0000269|PubMed:19339280,
CC ECO:0000269|PubMed:20619650, ECO:0000269|PubMed:20660629,
CC ECO:0000269|PubMed:20923974, ECO:0000269|PubMed:20980394,
CC ECO:0000269|PubMed:21127052, ECO:0000269|PubMed:21690308,
CC ECO:0000269|PubMed:21784165, ECO:0000269|PubMed:22072794,
CC ECO:0000269|PubMed:22078879, ECO:0000269|PubMed:22117071,
CC ECO:0000269|PubMed:22363215, ECO:0000269|PubMed:22454527,
CC ECO:0000269|PubMed:22872148, ECO:0000269|PubMed:7021319,
CC ECO:0000269|PubMed:8668128, ECO:0000269|PubMed:9295359,
CC ECO:0000269|PubMed:9885559}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044, ECO:0000269|PubMed:15128740,
CC ECO:0000269|PubMed:9295359};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4 mM for p-nitrophenyl phosphate {ECO:0000269|PubMed:9295359};
CC pH dependence:
CC Optimum pH is 6.9. {ECO:0000269|PubMed:9295359};
CC -!- SUBUNIT: Component of the RENT (regulator of nucleolar silencing and
CC telophase) complex which is composed of at least NET1, CDC14 and SIR2.
CC Interacts with CDC5, CRM1, SIC1, TOF2 and UTP7.
CC {ECO:0000269|PubMed:11511359, ECO:0000269|PubMed:15917648,
CC ECO:0000269|PubMed:18595708, ECO:0000269|PubMed:18794331,
CC ECO:0000269|PubMed:18927509, ECO:0000269|PubMed:21127052,
CC ECO:0000269|PubMed:9885559}.
CC -!- INTERACTION:
CC Q00684; P35734: ASK1; NbExp=2; IntAct=EBI-4192, EBI-26682;
CC Q00684; Q01389: BCK1; NbExp=4; IntAct=EBI-4192, EBI-3470;
CC Q00684; P38041: BOI1; NbExp=2; IntAct=EBI-4192, EBI-3719;
CC Q00684; P53894: CBK1; NbExp=5; IntAct=EBI-4192, EBI-4110;
CC Q00684; P32562: CDC5; NbExp=2; IntAct=EBI-4192, EBI-4440;
CC Q00684; P38147: CHK1; NbExp=2; IntAct=EBI-4192, EBI-4593;
CC Q00684; P15790: CKA1; NbExp=3; IntAct=EBI-4192, EBI-9533;
CC Q00684; P19454: CKA2; NbExp=3; IntAct=EBI-4192, EBI-9548;
CC Q00684; P24870: CLB3; NbExp=2; IntAct=EBI-4192, EBI-4522;
CC Q00684; Q03898: FIN1; NbExp=2; IntAct=EBI-4192, EBI-32941;
CC Q00684; P53233: FMP48; NbExp=2; IntAct=EBI-4192, EBI-9664;
CC Q00684; P38785: GIC1; NbExp=2; IntAct=EBI-4192, EBI-7575;
CC Q00684; Q12329: HSP42; NbExp=2; IntAct=EBI-4192, EBI-8571;
CC Q00684; P21965: MCK1; NbExp=2; IntAct=EBI-4192, EBI-10517;
CC Q00684; Q02196: MET14; NbExp=2; IntAct=EBI-4192, EBI-9485;
CC Q00684; P47035: NET1; NbExp=13; IntAct=EBI-4192, EBI-25953;
CC Q00684; P38826: ORC6; NbExp=2; IntAct=EBI-4192, EBI-12588;
CC Q00684; P39940: RSP5; NbExp=2; IntAct=EBI-4192, EBI-16219;
CC Q00684; P38990: SAK1; NbExp=2; IntAct=EBI-4192, EBI-12863;
CC Q00684; P38634: SIC1; NbExp=2; IntAct=EBI-4192, EBI-17127;
CC Q00684; P06700: SIR2; NbExp=5; IntAct=EBI-4192, EBI-17219;
CC Q00684; P38283: SLI15; NbExp=2; IntAct=EBI-4192, EBI-20842;
CC Q00684; P06782: SNF1; NbExp=2; IntAct=EBI-4192, EBI-17516;
CC Q00684; P06784: STE7; NbExp=2; IntAct=EBI-4192, EBI-18389;
CC Q00684; P32944: SWE1; NbExp=3; IntAct=EBI-4192, EBI-18607;
CC Q00684; Q02208: TOF2; NbExp=8; IntAct=EBI-4192, EBI-27048;
CC Q00684; Q03785: VHS1; NbExp=2; IntAct=EBI-4192, EBI-35568;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm. Bud neck.
CC Note=Sequestered in the nucleolus for most of the cell cycle by the
CC nucleolar proteins NET1 and TOF2, and is released into the nucleus and
CC cytoplasm during anaphase. CDC55 maintains CDC14 sequestration in the
CC nucleolus during early meiosis, which is essential for the assembly of
CC the meiosis I spindle. In anaphase, the CDC14 early anaphase release
CC (FEAR) network (including CDC5, ESP1, and SLK19), and the mitotic exit
CC network (including the DBF2-MOB1 complex) coordinately trigger the
CC release of CDC14 from the nucleolus.
CC -!- MISCELLANEOUS: Present with 8550 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class CDC14 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA34477.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA52971.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M61194; AAA34477.1; ALT_FRAME; Genomic_DNA.
DR EMBL; D55715; BAA09533.1; -; Genomic_DNA.
DR EMBL; D50617; BAA09267.1; -; Genomic_DNA.
DR EMBL; X75077; CAA52971.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006940; DAA12468.1; -; Genomic_DNA.
DR PIR; S56283; S56283.
DR RefSeq; NP_116684.3; NM_001179993.3.
DR PDB; 4ZJ7; X-ray; 2.40 A; B=517-551.
DR PDB; 5XW4; X-ray; 1.85 A; A/B=1-374.
DR PDB; 5XW5; X-ray; 1.85 A; A/B=1-374.
DR PDB; 6G84; X-ray; 2.47 A; A/B=1-374.
DR PDB; 6G85; X-ray; 1.53 A; A/B=1-374.
DR PDB; 6G86; X-ray; 1.74 A; A/B=1-374.
DR PDBsum; 4ZJ7; -.
DR PDBsum; 5XW4; -.
DR PDBsum; 5XW5; -.
DR PDBsum; 6G84; -.
DR PDBsum; 6G85; -.
DR PDBsum; 6G86; -.
DR AlphaFoldDB; Q00684; -.
DR SMR; Q00684; -.
DR BioGRID; 31182; 539.
DR ComplexPortal; CPX-1669; RENT complex.
DR DIP; DIP-5116N; -.
DR IntAct; Q00684; 179.
DR MINT; Q00684; -.
DR STRING; 4932.YFR028C; -.
DR iPTMnet; Q00684; -.
DR MaxQB; Q00684; -.
DR PaxDb; Q00684; -.
DR PRIDE; Q00684; -.
DR EnsemblFungi; YFR028C_mRNA; YFR028C; YFR028C.
DR GeneID; 850585; -.
DR KEGG; sce:YFR028C; -.
DR SGD; S000001924; CDC14.
DR VEuPathDB; FungiDB:YFR028C; -.
DR eggNOG; KOG1720; Eukaryota.
DR GeneTree; ENSGT00940000170847; -.
DR HOGENOM; CLU_017787_1_2_1; -.
DR InParanoid; Q00684; -.
DR OMA; EWKYTMR; -.
DR BioCyc; YEAST:G3O-30477-MON; -.
DR Reactome; R-SCE-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR Reactome; R-SCE-5687128; MAPK6/MAPK4 signaling.
DR SABIO-RK; Q00684; -.
DR PRO; PR:Q00684; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; Q00684; protein.
DR GO; GO:0005935; C:cellular bud neck; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:1990023; C:mitotic spindle midzone; IBA:GO_Central.
DR GO; GO:0044732; C:mitotic spindle pole body; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0030869; C:RENT complex; IDA:SGD.
DR GO; GO:0000922; C:spindle pole; IBA:GO_Central.
DR GO; GO:0005816; C:spindle pole body; IDA:SGD.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:SGD.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:SGD.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0000422; P:autophagy of mitochondrion; IMP:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071470; P:cellular response to osmotic stress; IMP:SGD.
DR GO; GO:0007059; P:chromosome segregation; IMP:SGD.
DR GO; GO:0051229; P:meiotic spindle disassembly; IMP:SGD.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:SGD.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; IMP:SGD.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IMP:SGD.
DR GO; GO:1903501; P:positive regulation of mitotic actomyosin contractile ring assembly; IMP:SGD.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0000183; P:rDNA heterochromatin assembly; IC:ComplexPortal.
DR GO; GO:0007096; P:regulation of exit from mitosis; IMP:SGD.
DR CDD; cd14499; CDC14_C; 1.
DR CDD; cd17657; CDC14_N; 1.
DR Gene3D; 3.90.190.10; -; 2.
DR InterPro; IPR026070; CDC14.
DR InterPro; IPR044506; CDC14_C.
DR InterPro; IPR029260; DSPn.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR23339:SF27; PTHR23339:SF27; 1.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF14671; DSPn; 1.
DR SMART; SM00195; DSPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 2.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cytoplasm; Hydrolase; Meiosis;
KW Mitosis; Nucleus; Phosphoprotein; Protein phosphatase; Reference proteome.
FT CHAIN 1..551
FT /note="Tyrosine-protein phosphatase CDC14"
FT /id="PRO_0000094875"
FT DOMAIN 190..342
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 384..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 283
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 253
FT /note="D->A: Inactivates catalytic activity and leads to
FT substrate retention."
FT /evidence="ECO:0000269|PubMed:21127052"
FT MUTAGEN 280
FT /note="A->V: Leads to temperature sensitivity."
FT /evidence="ECO:0000269|PubMed:21784165"
FT MUTAGEN 283
FT /note="C->S: Inactivates catalytic activity and leads to
FT substrate retention."
FT /evidence="ECO:0000269|PubMed:21127052"
FT CONFLICT 118
FT /note="A -> P (in Ref. 2; BAA09533)"
FT /evidence="ECO:0000305"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:6G85"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:6G85"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:6G85"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:6G85"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:6G85"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:6G85"
FT HELIX 56..71
FT /evidence="ECO:0007829|PDB:6G85"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:6G85"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:6G85"
FT HELIX 88..105
FT /evidence="ECO:0007829|PDB:6G85"
FT HELIX 110..114
FT /evidence="ECO:0007829|PDB:6G85"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:6G85"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:6G85"
FT HELIX 141..153
FT /evidence="ECO:0007829|PDB:6G85"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:6G85"
FT HELIX 164..171
FT /evidence="ECO:0007829|PDB:6G85"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:6G85"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:6G85"
FT STRAND 182..189
FT /evidence="ECO:0007829|PDB:6G85"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:6G84"
FT HELIX 209..220
FT /evidence="ECO:0007829|PDB:6G85"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:6G85"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:6G85"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:6G85"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:6G85"
FT HELIX 259..274
FT /evidence="ECO:0007829|PDB:6G85"
FT STRAND 278..287
FT /evidence="ECO:0007829|PDB:6G85"
FT HELIX 288..302
FT /evidence="ECO:0007829|PDB:6G85"
FT HELIX 306..316
FT /evidence="ECO:0007829|PDB:6G85"
FT HELIX 324..342
FT /evidence="ECO:0007829|PDB:6G85"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:6G85"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:6G85"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:6G85"
FT HELIX 362..371
FT /evidence="ECO:0007829|PDB:6G85"
SQ SEQUENCE 551 AA; 61907 MW; 4EB3985DFA3FD823 CRC64;
MRRSVYLDNT IEFLRGRVYL GAYDYTPEDT DELVFFTVED AIFYNSFHLD FGPMNIGHLY
RFAVIFHEIL NDPENANKAV VFYSSASTRQ RANAACMLCC YMILVQAWTP HQVLQPLAQV
DPPFMPFRDA GYSNADFEIT IQDVVYGVWR AKEKGLIDLH SFNLESYEKY EHVEFGDFNV
LTPDFIAFAS PQEDHPKGYL ATKSSHLNQP FKSVLNFFAN NNVQLVVRLN SHLYNKKHFE
DIGIQHLDLI FEDGTCPDLS IVKNFVGAAE TIIKRGGKIA VHCKAGLGRT GCLIGAHLIY
TYGFTANECI GFLRFIRPGM VVGPQQHWLY LHQNDFREWK YTTRISLKPS EAIGGLYPLI
SLEEYRLQKK KLKDDKRVAQ NNIEGELRDL TMTPPSNGHG ALSARNSSQP STANNGSNSF
KSSAVPQTSP GQPRKGQNGS NTIEDINNNR NPTSHANRKV VIESNNSDDE SMQDTNGTSN
HYPKVSRKKN DISSASSSRM EDNEPSATNI NNAADDTILR QLLPKNRRVT SGRRTTSAAG
GIRKISGSIK K
