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Tyrosine-protein phosphatase CDC14 (EC 3.1.3.48)

 CDC14_YEAST             Reviewed;         551 AA.
Q00684; D6VTQ8; Q05180; Q05673;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 2.
28-MAR-2018, entry version 177.
RecName: Full=Tyrosine-protein phosphatase CDC14;
EC=3.1.3.48;
Name=CDC14; Synonyms=OAF3; OrderedLocusNames=YFR028C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1597462;
Wan J., Xu H., Grunstein M.;
"CDC14 of Saccharomyces cerevisiae. Cloning, sequence analysis, and
transcription during the cell cycle.";
J. Biol. Chem. 267:11274-11280(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
PubMed=8668128; DOI=10.1007/BF02172916;
Shirayama M., Matsui Y., Toh-e A.;
"Dominant mutant alleles of yeast protein kinase gene CDC15 suppress
the lte1 defect in termination of M phase and genetically interact
with CDC14.";
Mol. Gen. Genet. 251:176-185(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7670463; DOI=10.1038/ng0795-261;
Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M.,
Sasanuma S., Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K.,
Yamazaki M., Tashiro H., Eki T.;
"Analysis of the nucleotide sequence of chromosome VI from
Saccharomyces cerevisiae.";
Nat. Genet. 10:261-268(1995).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=8686381;
DOI=10.1002/(SICI)1097-0061(199602)12:2<177::AID-YEA896>3.0.CO;2-A;
Eki T., Naitou M., Hagiwara H., Abe M., Ozawa M., Sasanuma S.,
Sasanuma M., Tsuchiya Y., Shibata T., Watanabe K., Ono A.,
Yamazaki M., Tashiro H., Hanaoka F., Murakami Y.;
"Fifteen open reading frames in a 30.8 kb region of the right arm of
chromosome VI from Saccharomyces cerevisiae.";
Yeast 12:177-190(1996).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-421.
Mai B., Lipp M.;
Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
[7]
FUNCTION.
PubMed=7021319;
Schild D., Byers B.;
"Diploid spore formation and other meiotic effects of two cell-
division-cycle mutations of Saccharomyces cerevisiae.";
Genetics 96:859-876(1980).
[8]
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND FUNCTION.
PubMed=9295359; DOI=10.1074/jbc.272.38.24054;
Taylor G.S., Liu Y., Baskerville C., Charbonneau H.;
"The activity of Cdc14p, an oligomeric dual specificity protein
phosphatase from Saccharomyces cerevisiae, is required for cell cycle
progression.";
J. Biol. Chem. 272:24054-24063(1997).
[9]
INTERACTION WITH SIC1, AND FUNCTION IN DEPHOSPHORYLATION OF CDH1; SIC1
AND SWI5.
PubMed=9885559; DOI=10.1016/S1097-2765(00)80286-5;
Visintin R., Craig K., Hwang E.S., Prinz S., Tyers M., Amon A.;
"The phosphatase Cdc14 triggers mitotic exit by reversal of Cdk-
dependent phosphorylation.";
Mol. Cell 2:709-718(1998).
[10]
FUNCTION, AND SUBUNIT.
PubMed=11511359; DOI=10.1016/S1097-2765(01)00291-X;
Shou W., Sakamoto K.M., Keener J., Morimoto K.W., Traverso E.E.,
Azzam R., Hoppe G.J., Feldman R.M.R., DeModena J., Moazed D.,
Charbonneau H., Nomura M., Deshaies R.J.;
"Net1 stimulates RNA polymerase I transcription and regulates
nucleolar structure independently of controlling mitotic exit.";
Mol. Cell 8:45-55(2001).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12737806; DOI=10.1016/S1534-5807(03)00130-8;
Marston A.L., Lee B.H., Amon A.;
"The Cdc14 phosphatase and the FEAR network control meiotic spindle
disassembly and chromosome segregation.";
Dev. Cell 4:711-726(2003).
[12]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[13]
FUNCTION.
PubMed=15137939; DOI=10.1016/S0092-8674(04)00413-1;
D'Amours D., Stegmeier F., Amon A.;
"Cdc14 and condensin control the dissolution of cohesin-independent
chromosome linkages at repeated DNA.";
Cell 117:455-469(2004).
[14]
FUNCTION.
PubMed=15004526;
Torres-Rosell J., Machin F., Jarmuz A., Aragon L.;
"Nucleolar segregation lags behind the rest of the genome and requires
Cdc14p activation by the FEAR network.";
Cell Cycle 3:496-502(2004).
[15]
FUNCTION.
PubMed=15190202; DOI=10.4161/cc.3.7.1003;
Wang B.D., Yong-Gonzalez V., Strunnikov A.V.;
"Cdc14p/FEAR pathway controls segregation of nucleolus in S.
cerevisiae by facilitating condensin targeting to rDNA chromatin in
anaphase.";
Cell Cycle 3:960-967(2004).
[16]
CATALYTIC ACTIVITY.
PubMed=15128740; DOI=10.1074/jbc.M402217200;
Wang W.Q., Bembenek J., Gee K.R., Yu H., Charbonneau H., Zhang Z.Y.;
"Kinetic and mechanistic studies of a cell cycle protein phosphatase
Cdc14.";
J. Biol. Chem. 279:30459-30468(2004).
[17]
FUNCTION IN DEPHOSPHORYLATION OF SWI6.
PubMed=14993267; DOI=10.1128/MCB.24.6.2277-2285.2004;
Geymonat M., Spanos A., Wells G.P., Smerdon S.J., Sedgwick S.G.;
"Clb6/Cdc28 and Cdc14 regulate phosphorylation status and cellular
localization of Swi6.";
Mol. Cell. Biol. 24:2277-2285(2004).
[18]
SUBCELLULAR LOCATION.
PubMed=15273393; DOI=10.1126/science.1099402;
Azzam R., Chen S.L., Shou W., Mah A.S., Alexandru G., Nasmyth K.,
Annan R.S., Carr S.A., Deshaies R.J.;
"Phosphorylation by cyclin B-Cdk underlies release of mitotic exit
activator Cdc14 from the nucleolus.";
Science 305:516-519(2004).
[19]
SUBCELLULAR LOCATION, INTERACTION WITH CRM1, AND FUNCTION.
PubMed=15917648; DOI=10.4161/cc.4.7.1798;
Bembenek J., Kang J., Kurischko C., Li B., Raab J.R., Belanger K.D.,
Luca F.C., Yu H.;
"Crm1-mediated nuclear export of Cdc14 is required for the completion
of cytokinesis in budding yeast.";
Cell Cycle 4:961-971(2005).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[21]
FUNCTION IN DEPHOSPHORYLATION OF DBP2; SIC1 AND SLD2.
PubMed=17116692; DOI=10.1128/MCB.01069-06;
Bloom J., Cross F.R.;
"Novel role for Cdc14 sequestration: Cdc14 dephosphorylates factors
that promote DNA replication.";
Mol. Cell. Biol. 27:842-853(2007).
[22]
FUNCTION IN DEPHOSPHORYLATION OF ASE1.
PubMed=18235228; DOI=10.4161/cc.7.3.5349;
Khmelinskii A., Schiebel E.;
"Assembling the spindle midzone in the right place at the right
time.";
Cell Cycle 7:283-286(2008).
[23]
SUBCELLULAR LOCATION, AND INTERACTION WITH CDC5.
PubMed=18927509; DOI=10.4161/cc.7.20.6852;
Rahal R., Amon A.;
"The Polo-like kinase Cdc5 interacts with FEAR network components and
Cdc14.";
Cell Cycle 7:3262-3272(2008).
[24]
SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH TOF2.
PubMed=18595708; DOI=10.1016/j.cub.2008.06.025;
Geil C., Schwab M., Seufert W.;
"A nucleolus-localized activator of Cdc14 phosphatase supports rDNA
segregation in yeast mitosis.";
Curr. Biol. 18:1001-1005(2008).
[25]
FUNCTION IN DEPHOSPHORYLATION OF ACM1.
PubMed=18287090; DOI=10.1074/jbc.M710011200;
Hall M.C., Jeong D.E., Henderson J.T., Choi E., Bremmer S.C.,
Iliuk A.B., Charbonneau H.;
"Cdc28 and Cdc14 control stability of the anaphase-promoting complex
inhibitor Acm1.";
J. Biol. Chem. 283:10396-10407(2008).
[26]
SUBCELLULAR LOCATION, AND INTERACTION WITH UTP7.
PubMed=18794331; DOI=10.1083/jcb.200802085;
Jwa M., Kim J.H., Chan C.S.;
"Regulation of Sli15/INCENP, kinetochore, and Cdc14 phosphatase
functions by the ribosome biogenesis protein Utp7.";
J. Cell Biol. 182:1099-1111(2008).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[28]
SUBCELLULAR LOCATION.
PubMed=19221193; DOI=10.1083/jcb.200812022;
Mohl D.A., Huddleston M.J., Collingwood T.S., Annan R.S.,
Deshaies R.J.;
"Dbf2-Mob1 drives relocalization of protein phosphatase Cdc14 to the
cytoplasm during exit from mitosis.";
J. Cell Biol. 184:527-539(2009).
[29]
FUNCTION.
PubMed=19339280; DOI=10.1091/mbc.E08-11-1150;
Chiroli E., Rancati G., Catusi I., Lucchini G., Piatti S.;
"Cdc14 inhibition by the spindle assembly checkpoint prevents
unscheduled centrosome separation in budding yeast.";
Mol. Biol. Cell 20:2626-2637(2009).
[30]
FUNCTION.
PubMed=19158678; DOI=10.1038/nature07652;
Clemente-Blanco A., Mayan-Santos M., Schneider D.A., Machin F.,
Jarmuz A., Tschochner H., Aragon L.;
"Cdc14 inhibits transcription by RNA polymerase I during anaphase.";
Nature 458:219-222(2009).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[32]
FUNCTION IN DEPHOSPHORYLATION OF INCENP.
PubMed=20619650; DOI=10.1016/j.cub.2010.06.023;
Mirchenko L., Uhlmann F.;
"Sli15(INCENP) dephosphorylation prevents mitotic checkpoint
reengagement due to loss of tension at anaphase onset.";
Curr. Biol. 20:1396-1401(2010).
[33]
FUNCTION IN DEPHOSPHORYLATION OF DSN1.
PubMed=20923974; DOI=10.1534/genetics.110.123653;
Akiyoshi B., Biggins S.;
"Cdc14-dependent dephosphorylation of a kinetochore protein prior to
anaphase in Saccharomyces cerevisiae.";
Genetics 186:1487-1491(2010).
[34]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20660629; DOI=10.1083/jcb.201002026;
Manzoni R., Montani F., Visintin C., Caudron F., Ciliberto A.,
Visintin R.;
"Oscillations in Cdc14 release and sequestration reveal a circuit
underlying mitotic exit.";
J. Cell Biol. 190:209-222(2010).
[35]
SUBCELLULAR LOCATION.
PubMed=21098112; DOI=10.1083/jcb.201007025;
Rossio V., Galati E., Ferrari M., Pellicioli A., Sutani T.,
Shirahige K., Lucchini G., Piatti S.;
"The RSC chromatin-remodeling complex influences mitotic exit and
adaptation to the spindle assembly checkpoint by controlling the Cdc14
phosphatase.";
J. Cell Biol. 191:981-997(2010).
[36]
FUNCTION IN DEPHOSPHORYLATION OF ORC2; ORC6; CDC6 AND MCM3.
PubMed=20980394; DOI=10.1242/jcs.075366;
Zhai Y., Yung P.Y., Huo L., Liang C.;
"Cdc14p resets the competency of replication licensing by
dephosphorylating multiple initiation proteins during mitotic exit in
budding yeast.";
J. Cell Sci. 123:3933-3943(2010).
[37]
FUNCTION.
PubMed=22078879; DOI=10.1016/j.cell.2011.09.047;
Bouchoux C., Uhlmann F.;
"A quantitative model for ordered Cdk substrate dephosphorylation
during mitotic exit.";
Cell 147:803-814(2011).
[38]
FUNCTION, AND MUTAGENESIS OF ALA-280.
PubMed=21784165; DOI=10.1016/j.fgb.2011.07.001;
Tzeng Y.W., Huang J.N., Schuyler S.C., Wu C.H., Juang Y.L.;
"Functions of the mitotic B-type cyclins CLB1, CLB2, and CLB3 at
mitotic exit antagonized by the CDC14 phosphatase.";
Fungal Genet. Biol. 48:966-978(2011).
[39]
MUTAGENESIS OF ASP-253 AND CYS-283, INTERACTION WITH BNI1; BNR1 AND
KAR9, AND FUNCTION IN DEPHOSPHORYLATION OF BNI1; BNR1 AND KAR9.
PubMed=21127052; DOI=10.1074/jbc.M110.205054;
Bloom J., Cristea I.M., Procko A.L., Lubkov V., Chait B.T., Snyder M.,
Cross F.R.;
"Global analysis of Cdc14 phosphatase reveals diverse roles in mitotic
processes.";
J. Biol. Chem. 286:5434-5445(2011).
[40]
SUBCELLULAR LOCATION.
PubMed=21690311; DOI=10.1083/jcb.201103019;
Kerr G.W., Sarkar S., Tibbles K.L., Petronczki M., Millar J.B.,
Arumugam P.;
"Meiotic nuclear divisions in budding yeast require PP2A(Cdc55)-
mediated antagonism of Net1 phosphorylation by Cdk.";
J. Cell Biol. 193:1157-1166(2011).
[41]
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=21690308; DOI=10.1083/jcb.201103076;
Bizzari F., Marston A.L.;
"Cdc55 coordinates spindle assembly and chromosome disjunction during
meiosis.";
J. Cell Biol. 193:1213-1228(2011).
[42]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=22872148; DOI=10.1038/emboj.2012.224;
Sanchez-Diaz A., Nkosi P.J., Murray S., Labib K.;
"The mitotic exit network and Cdc14 phosphatase initiate cytokinesis
by counteracting CDK phosphorylations and blocking polarised growth.";
EMBO J. 31:3620-3634(2012).
[43]
FUNCTION.
PubMed=22117071; DOI=10.1074/jbc.M111.281105;
Bremmer S.C., Hall H., Martinez J.S., Eissler C.L., Hinrichsen T.H.,
Rossie S., Parker L.L., Hall M.C., Charbonneau H.;
"Cdc14 phosphatases preferentially dephosphorylate a subset of cyclin-
dependent kinase (Cdk) sites containing phosphoserine.";
J. Biol. Chem. 287:1662-1669(2012).
[44]
SUBCELLULAR LOCATION, AND FUNCTION IN DEPHOSPHORYLATION OF INN1.
PubMed=22454527; DOI=10.1242/jcs.106021;
Palani S., Meitinger F., Boehm M.E., Lehmann W.D., Pereira G.;
"Cdc14-dependent dephosphorylation of Inn1 contributes to Inn1-Cyk3
complex formation.";
J. Cell Sci. 125:3091-3096(2012).
[45]
FUNCTION IN DEPHOSPHORYLATION OF CHS2.
PubMed=22072794; DOI=10.1091/mbc.E11-05-0434;
Chin C.F., Bennett A.M., Ma W.K., Hall M.C., Yeong F.M.;
"Dependence of Chs2 ER export on dephosphorylation by cytoplasmic
Cdc14 ensures that septum formation follows mitosis.";
Mol. Biol. Cell 23:45-58(2012).
[46]
FUNCTION.
PubMed=22363215; DOI=10.1371/journal.pgen.1002509;
Quevedo O., Garcia-Luis J., Matos-Perdomo E., Aragon L., Machin F.;
"Nondisjunction of a single chromosome leads to breakage and
activation of DNA damage checkpoint in G2.";
PLoS Genet. 8:E1002509-E1002509(2012).
[47]
SUBCELLULAR LOCATION.
PubMed=24039885; DOI=10.1371/journal.pone.0073194;
Faust A.M., Wong C.C., Yates Iii J.R., Drubin D.G., Barnes G.;
"The FEAR protein Slk19 restricts Cdc14 phosphatase to the nucleus
until the end of anaphase, regulating its participation in mitotic
exit in Saccharomyces cerevisiae.";
PLoS ONE 8:E73194-E73194(2013).
-!- FUNCTION: Protein phosphatase which antagonizes mitotic cyclin-
dependent kinase CDC28, the inactivation of which is essential for
exit from mitosis. To access its substrates, is released from
nucleolar sequestration during mitosis. Plays an essential in
coordinating the nuclear division cycle with cytokinesis through
the cytokinesis checkpoint. Involved in chromosome segregation,
where it is required for meiosis I spindle dissambly as well as
for establishing two consecutive chromosome segregation phases.
Allows damaged actomyosin rings to be maintained to facilitate
completion of cell division in response to minor perturbation of
the cell division machinery. Inhibits transcription of ribosomal
genes (rDNA) during anaphase and controls segregation of nucleolus
by facilitating condensin targeting to rDNA chromatin in anaphase.
Dephosphorylates SIC1, a CDC28 inhibitor, and SWI5, a
transcription factor for SIC1, and induces degradation of mitotic
cyclins, likely by dephosphorylating the activator of mitotic
cyclin degradation, CDH1. Dephosphorylates the microtubule
bundling factor ASE1 which is required to define a centered and
focused mitotic spindle midzone that can drive continuous spindle
elongation. Dephosphorylates the anaphase-promoting complex
inhibitor ACM1, leading to its degradation. Facilitates INN1-CYK3
complex formation which promotes cytokinesis through the
dephosphorylation of CDC28-phosphosphorylated INN1. Reverts also
the inhibitory CDC28 phosphorylation of CHS2 for endoplasmic
reticulum export, ensuring that septum formation is contingent
upon chromosome separation and exit from mitosis. Additional
substrates for CDC14 are the formins BNI1 and BNR1, as well as
CDC6, DBP2, DSN1, INCENP, KAR9, MCM3, ORC2, ORC6, SLD2, and SWI6.
Activity is inhibited by interaction with NET1 which sequesters it
to the nucleolus. {ECO:0000269|PubMed:11511359,
ECO:0000269|PubMed:12737806, ECO:0000269|PubMed:14993267,
ECO:0000269|PubMed:15004526, ECO:0000269|PubMed:15137939,
ECO:0000269|PubMed:15190202, ECO:0000269|PubMed:15917648,
ECO:0000269|PubMed:17116692, ECO:0000269|PubMed:18235228,
ECO:0000269|PubMed:18287090, ECO:0000269|PubMed:18595708,
ECO:0000269|PubMed:19158678, ECO:0000269|PubMed:19339280,
ECO:0000269|PubMed:20619650, ECO:0000269|PubMed:20660629,
ECO:0000269|PubMed:20923974, ECO:0000269|PubMed:20980394,
ECO:0000269|PubMed:21127052, ECO:0000269|PubMed:21690308,
ECO:0000269|PubMed:21784165, ECO:0000269|PubMed:22072794,
ECO:0000269|PubMed:22078879, ECO:0000269|PubMed:22117071,
ECO:0000269|PubMed:22363215, ECO:0000269|PubMed:22454527,
ECO:0000269|PubMed:22872148, ECO:0000269|PubMed:7021319,
ECO:0000269|PubMed:8668128, ECO:0000269|PubMed:9295359,
ECO:0000269|PubMed:9885559}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044,
ECO:0000269|PubMed:15128740, ECO:0000269|PubMed:9295359}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=4 mM for p-nitrophenyl phosphate
{ECO:0000269|PubMed:9295359};
pH dependence:
Optimum pH is 6.9. {ECO:0000269|PubMed:9295359};
-!- SUBUNIT: Component of the RENT (regulator of nucleolar silencing
and telophase) complex which is composed of at least NET1, CDC14
and SIR2. Interacts with CDC5, CRM1, SIC1, TOF2 and UTP7.
{ECO:0000269|PubMed:11511359, ECO:0000269|PubMed:15917648,
ECO:0000269|PubMed:18595708, ECO:0000269|PubMed:18794331,
ECO:0000269|PubMed:18927509, ECO:0000269|PubMed:21127052,
ECO:0000269|PubMed:9885559}.
-!- INTERACTION:
P35734:ASK1; NbExp=2; IntAct=EBI-4192, EBI-26682;
Q01389:BCK1; NbExp=4; IntAct=EBI-4192, EBI-3470;
P38041:BOI1; NbExp=2; IntAct=EBI-4192, EBI-3719;
P53894:CBK1; NbExp=5; IntAct=EBI-4192, EBI-4110;
P32562:CDC5; NbExp=2; IntAct=EBI-4192, EBI-4440;
P38147:CHK1; NbExp=2; IntAct=EBI-4192, EBI-4593;
P15790:CKA1; NbExp=3; IntAct=EBI-4192, EBI-9533;
P19454:CKA2; NbExp=3; IntAct=EBI-4192, EBI-9548;
P24870:CLB3; NbExp=2; IntAct=EBI-4192, EBI-4522;
Q03898:FIN1; NbExp=2; IntAct=EBI-4192, EBI-32941;
P53233:FMP48; NbExp=2; IntAct=EBI-4192, EBI-9664;
P38785:GIC1; NbExp=2; IntAct=EBI-4192, EBI-7575;
Q12329:HSP42; NbExp=2; IntAct=EBI-4192, EBI-8571;
P21965:MCK1; NbExp=2; IntAct=EBI-4192, EBI-10517;
Q02196:MET14; NbExp=2; IntAct=EBI-4192, EBI-9485;
P47035:NET1; NbExp=13; IntAct=EBI-4192, EBI-25953;
P38826:ORC6; NbExp=2; IntAct=EBI-4192, EBI-12588;
P39940:RSP5; NbExp=2; IntAct=EBI-4192, EBI-16219;
P38990:SAK1; NbExp=2; IntAct=EBI-4192, EBI-12863;
P38634:SIC1; NbExp=2; IntAct=EBI-4192, EBI-17127;
P06700:SIR2; NbExp=5; IntAct=EBI-4192, EBI-17219;
P38283:SLI15; NbExp=2; IntAct=EBI-4192, EBI-20842;
P06782:SNF1; NbExp=2; IntAct=EBI-4192, EBI-17516;
P06784:STE7; NbExp=2; IntAct=EBI-4192, EBI-18389;
P32944:SWE1; NbExp=3; IntAct=EBI-4192, EBI-18607;
Q02208:TOF2; NbExp=8; IntAct=EBI-4192, EBI-27048;
Q03785:VHS1; NbExp=2; IntAct=EBI-4192, EBI-35568;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm. Bud neck.
Note=Sequestered in the nucleolus for most of the cell cycle by
the nucleolar proteins NET1 and TOF2, and is released into the
nucleus and cytoplasm during anaphase. CDC55 maintains CDC14
sequestration in the nucleolus during early meiosis, which is
essential for the assembly of the meiosis I spindle. In anaphase,
the CDC14 early anaphase release (FEAR) network (including CDC5,
ESP1, and SLK19), and the mitotic exit network (including the
DBF2-MOB1 complex) coordinately trigger the release of CDC14 from
the nucleolus.
-!- MISCELLANEOUS: Present with 8550 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
Non-receptor class CDC14 subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA34477.1; Type=Frameshift; Positions=116, 190; Evidence={ECO:0000305};
Sequence=CAA52971.1; Type=Frameshift; Positions=117; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; M61194; AAA34477.1; ALT_FRAME; Genomic_DNA.
EMBL; D55715; BAA09533.1; -; Genomic_DNA.
EMBL; D50617; BAA09267.1; -; Genomic_DNA.
EMBL; X75077; CAA52971.1; ALT_FRAME; Genomic_DNA.
EMBL; BK006940; DAA12468.1; -; Genomic_DNA.
PIR; S56283; S56283.
RefSeq; NP_116684.3; NM_001179993.3.
PDB; 4ZJ7; X-ray; 2.40 A; B=517-551.
PDB; 5XW4; X-ray; 1.85 A; A/B=1-374.
PDB; 5XW5; X-ray; 1.85 A; A/B=1-374.
PDBsum; 4ZJ7; -.
PDBsum; 5XW4; -.
PDBsum; 5XW5; -.
ProteinModelPortal; Q00684; -.
SMR; Q00684; -.
BioGrid; 31182; 493.
DIP; DIP-5116N; -.
IntAct; Q00684; 182.
MINT; Q00684; -.
STRING; 4932.YFR028C; -.
iPTMnet; Q00684; -.
MaxQB; Q00684; -.
PaxDb; Q00684; -.
PRIDE; Q00684; -.
EnsemblFungi; BAA09267; BAA09267; BAA09267.
EnsemblFungi; YFR028C; YFR028C; YFR028C.
GeneID; 850585; -.
KEGG; sce:YFR028C; -.
EuPathDB; FungiDB:YFR028C; -.
SGD; S000001924; CDC14.
GeneTree; ENSGT00390000010254; -.
HOGENOM; HOG000198341; -.
InParanoid; Q00684; -.
KO; K06639; -.
OMA; CCYMVLV; -.
OrthoDB; EOG092C2FOY; -.
BioCyc; YEAST:G3O-30477-MONOMER; -.
Reactome; R-SCE-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
Reactome; R-SCE-5687128; MAPK6/MAPK4 signaling.
SABIO-RK; Q00684; -.
PRO; PR:Q00684; -.
Proteomes; UP000002311; Chromosome VI.
GO; GO:0005935; C:cellular bud neck; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
GO; GO:0005730; C:nucleolus; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0030869; C:RENT complex; IDA:SGD.
GO; GO:0000922; C:spindle pole; IBA:GO_Central.
GO; GO:0005816; C:spindle pole body; IDA:SGD.
GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:SGD.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0071470; P:cellular response to osmotic stress; IMP:SGD.
GO; GO:0007059; P:chromosome segregation; IMP:SGD.
GO; GO:0051229; P:meiotic spindle disassembly; IMP:SGD.
GO; GO:0000278; P:mitotic cell cycle; IMP:SGD.
GO; GO:0071850; P:mitotic cell cycle arrest; IBA:GO_Central.
GO; GO:0051256; P:mitotic spindle midzone assembly; IBA:GO_Central.
GO; GO:0032467; P:positive regulation of cytokinesis; IMP:SGD.
GO; GO:0006470; P:protein dephosphorylation; IDA:SGD.
GO; GO:0007096; P:regulation of exit from mitosis; IGI:SGD.
Gene3D; 3.90.190.10; -; 2.
InterPro; IPR026070; CDC14.
InterPro; IPR029260; DSPn.
InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR016130; Tyr_Pase_AS.
InterPro; IPR003595; Tyr_Pase_cat.
InterPro; IPR000387; TYR_PHOSPHATASE_dom.
InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
PANTHER; PTHR23339:SF27; PTHR23339:SF27; 1.
Pfam; PF00782; DSPc; 1.
Pfam; PF14671; DSPn; 1.
SMART; SM00195; DSPc; 1.
SMART; SM00404; PTPc_motif; 1.
SUPFAM; SSF52799; SSF52799; 2.
PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
1: Evidence at protein level;
3D-structure; Cell cycle; Cell division; Complete proteome; Cytoplasm;
Hydrolase; Meiosis; Mitosis; Nucleus; Phosphoprotein;
Protein phosphatase; Reference proteome.
CHAIN 1 551 Tyrosine-protein phosphatase CDC14.
/FTId=PRO_0000094875.
ACT_SITE 283 283 Phosphocysteine intermediate.
{ECO:0000255|PROSITE-ProRule:PRU10044}.
MOD_RES 467 467 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
MUTAGEN 253 253 D->A: Inactivates catalytic activity and
leads to substrate retention.
{ECO:0000269|PubMed:21127052}.
MUTAGEN 280 280 A->V: Leads to temperature sensitivity.
{ECO:0000269|PubMed:21784165}.
MUTAGEN 283 283 C->S: Inactivates catalytic activity and
leads to substrate retention.
{ECO:0000269|PubMed:21127052}.
CONFLICT 118 118 A -> P (in Ref. 2; BAA09533).
{ECO:0000305}.
STRAND 10 14 {ECO:0000244|PDB:5XW4}.
TURN 15 17 {ECO:0000244|PDB:5XW4}.
STRAND 18 22 {ECO:0000244|PDB:5XW4}.
STRAND 31 36 {ECO:0000244|PDB:5XW4}.
TURN 39 41 {ECO:0000244|PDB:5XW4}.
STRAND 47 49 {ECO:0000244|PDB:5XW4}.
HELIX 56 71 {ECO:0000244|PDB:5XW4}.
HELIX 73 75 {ECO:0000244|PDB:5XW4}.
STRAND 78 84 {ECO:0000244|PDB:5XW4}.
HELIX 88 106 {ECO:0000244|PDB:5XW4}.
HELIX 110 114 {ECO:0000244|PDB:5XW4}.
HELIX 115 117 {ECO:0000244|PDB:5XW4}.
STRAND 130 133 {ECO:0000244|PDB:5XW4}.
HELIX 141 153 {ECO:0000244|PDB:5XW4}.
TURN 159 161 {ECO:0000244|PDB:5XW4}.
HELIX 164 170 {ECO:0000244|PDB:5XW4}.
HELIX 173 175 {ECO:0000244|PDB:5XW4}.
STRAND 178 180 {ECO:0000244|PDB:5XW4}.
STRAND 182 189 {ECO:0000244|PDB:5XW4}.
HELIX 209 220 {ECO:0000244|PDB:5XW4}.
STRAND 223 228 {ECO:0000244|PDB:5XW4}.
HELIX 237 240 {ECO:0000244|PDB:5XW4}.
TURN 241 243 {ECO:0000244|PDB:5XW4}.
STRAND 245 248 {ECO:0000244|PDB:5XW4}.
HELIX 259 274 {ECO:0000244|PDB:5XW4}.
STRAND 278 287 {ECO:0000244|PDB:5XW4}.
HELIX 288 302 {ECO:0000244|PDB:5XW4}.
HELIX 306 316 {ECO:0000244|PDB:5XW4}.
HELIX 324 342 {ECO:0000244|PDB:5XW4}.
STRAND 343 345 {ECO:0000244|PDB:5XW4}.
HELIX 351 353 {ECO:0000244|PDB:5XW4}.
STRAND 359 361 {ECO:0000244|PDB:5XW4}.
HELIX 362 367 {ECO:0000244|PDB:5XW4}.
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


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