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Q00684 (CDC14_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein phosphatase CDC14

EC=3.1.3.48
Gene names
Name:CDC14
Synonyms:OAF3
Ordered Locus Names:YFR028C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length551 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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 dephosphosprylation 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. Ref.2 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.17 Ref.19 Ref.21 Ref.22 Ref.24 Ref.25 Ref.29 Ref.30 Ref.32 Ref.33 Ref.34 Ref.36 Ref.37 Ref.38 Ref.39 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45 Ref.46

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. Ref.8 Ref.16

Subunit structure

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. Ref.9 Ref.10 Ref.19 Ref.23 Ref.24 Ref.26 Ref.39

Subcellular location

Nucleusnucleolus. 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. Ref.11 Ref.18 Ref.19 Ref.23 Ref.24 Ref.26 Ref.28 Ref.34 Ref.35 Ref.40 Ref.41 Ref.42 Ref.44 Ref.47

Miscellaneous

Present with 8550 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class CDC14 subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=4 mM for p-nitrophenyl phosphate Ref.8

pH dependence:

Optimum pH is 6.9.

Sequence caution

The sequence AAA34477.1 differs from that shown. Reason: Frameshift at positions 116 and 190.

The sequence CAA52971.1 differs from that shown. Reason: Frameshift at position 117.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Meiosis
Mitosis
   Cellular componentCytoplasm
Nucleus
   Molecular functionHydrolase
Protein phosphatase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromosome separation

Inferred from mutant phenotype PubMed 16769819. Source: SGD

meiotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

meiotic spindle disassembly

Inferred from mutant phenotype Ref.11. Source: SGD

mitotic cell cycle

Inferred from mutant phenotype PubMed 6749599. Source: SGD

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

protein dephosphorylation

Inferred from direct assay Ref.8. Source: SGD

regulation of exit from mitosis

Inferred from genetic interaction PubMed 10219244. Source: SGD

   Cellular_componentRENT complex

Inferred from direct assay PubMed 10219244. Source: SGD

cellular bud neck

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from direct assay PubMed 12062061. Source: SGD

spindle pole body

Inferred from direct assay PubMed 12062061. Source: SGD

   Molecular_functionphosphoprotein phosphatase activity

Inferred from direct assay PubMed 24319056Ref.8. Source: SGD

protein binding

Inferred from physical interaction PubMed 11274204PubMed 14734533PubMed 15282295PubMed 16713564PubMed 17043313Ref.24PubMed 18923139Ref.23PubMed 20489023PubMed 21179020Ref.37. Source: IntAct

protein tyrosine phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein tyrosine/serine/threonine phosphatase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 551551Tyrosine-protein phosphatase CDC14
PRO_0000094875

Sites

Active site2831Phosphocysteine intermediate By similarity

Amino acid modifications

Modified residue4671Phosphoserine Ref.20 Ref.31

Experimental info

Mutagenesis2531D → A: Inactivates catalytic activity and leads to substrate retention. Ref.39
Mutagenesis2801A → V: Leads to temperature sensitivity. Ref.38
Mutagenesis2831C → S: Inactivates catalytic activity and leads to substrate retention. Ref.39
Sequence conflict1181A → P in BAA09533. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q00684 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: 4EB3985DFA3FD823

FASTA55161,907
        10         20         30         40         50         60 
MRRSVYLDNT IEFLRGRVYL GAYDYTPEDT DELVFFTVED AIFYNSFHLD FGPMNIGHLY 

        70         80         90        100        110        120 
RFAVIFHEIL NDPENANKAV VFYSSASTRQ RANAACMLCC YMILVQAWTP HQVLQPLAQV 

       130        140        150        160        170        180 
DPPFMPFRDA GYSNADFEIT IQDVVYGVWR AKEKGLIDLH SFNLESYEKY EHVEFGDFNV 

       190        200        210        220        230        240 
LTPDFIAFAS PQEDHPKGYL ATKSSHLNQP FKSVLNFFAN NNVQLVVRLN SHLYNKKHFE 

       250        260        270        280        290        300 
DIGIQHLDLI FEDGTCPDLS IVKNFVGAAE TIIKRGGKIA VHCKAGLGRT GCLIGAHLIY 

       310        320        330        340        350        360 
TYGFTANECI GFLRFIRPGM VVGPQQHWLY LHQNDFREWK YTTRISLKPS EAIGGLYPLI 

       370        380        390        400        410        420 
SLEEYRLQKK KLKDDKRVAQ NNIEGELRDL TMTPPSNGHG ALSARNSSQP STANNGSNSF 

       430        440        450        460        470        480 
KSSAVPQTSP GQPRKGQNGS NTIEDINNNR NPTSHANRKV VIESNNSDDE SMQDTNGTSN 

       490        500        510        520        530        540 
HYPKVSRKKN DISSASSSRM EDNEPSATNI NNAADDTILR QLLPKNRRVT SGRRTTSAAG 

       550 
GIRKISGSIK K 

« Hide

References

« Hide 'large scale' references
[1]"CDC14 of Saccharomyces cerevisiae. Cloning, sequence analysis, and transcription during the cell cycle."
Wan J., Xu H., Grunstein M.
J. Biol. Chem. 267:11274-11280(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Dominant mutant alleles of yeast protein kinase gene CDC15 suppress the lte1 defect in termination of M phase and genetically interact with CDC14."
Shirayama M., Matsui Y., Toh-e A.
Mol. Gen. Genet. 251:176-185(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[3]"Analysis of the nucleotide sequence of chromosome VI from Saccharomyces cerevisiae."
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.
Nat. Genet. 10:261-268(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
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.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Fifteen open reading frames in a 30.8 kb region of the right arm of chromosome VI from Saccharomyces cerevisiae."
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.
Yeast 12:177-190(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[6]Mai B., Lipp M.
Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-421.
[7]"Diploid spore formation and other meiotic effects of two cell-division-cycle mutations of Saccharomyces cerevisiae."
Schild D., Byers B.
Genetics 96:859-876(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"The activity of Cdc14p, an oligomeric dual specificity protein phosphatase from Saccharomyces cerevisiae, is required for cell cycle progression."
Taylor G.S., Liu Y., Baskerville C., Charbonneau H.
J. Biol. Chem. 272:24054-24063(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION.
[9]"The phosphatase Cdc14 triggers mitotic exit by reversal of Cdk-dependent phosphorylation."
Visintin R., Craig K., Hwang E.S., Prinz S., Tyers M., Amon A.
Mol. Cell 2:709-718(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SIC1, FUNCTION IN DEPHOSPHORYLATION OF CDH1; SIC1 AND SWI5.
[10]"Net1 stimulates RNA polymerase I transcription and regulates nucleolar structure independently of controlling mitotic exit."
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.
Mol. Cell 8:45-55(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[11]"The Cdc14 phosphatase and the FEAR network control meiotic spindle disassembly and chromosome segregation."
Marston A.L., Lee B.H., Amon A.
Dev. Cell 4:711-726(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[12]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[13]"Cdc14 and condensin control the dissolution of cohesin-independent chromosome linkages at repeated DNA."
D'Amours D., Stegmeier F., Amon A.
Cell 117:455-469(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"Nucleolar segregation lags behind the rest of the genome and requires Cdc14p activation by the FEAR network."
Torres-Rosell J., Machin F., Jarmuz A., Aragon L.
Cell Cycle 3:496-502(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"Cdc14p/FEAR pathway controls segregation of nucleolus in S. cerevisiae by facilitating condensin targeting to rDNA chromatin in anaphase."
Wang B.D., Yong-Gonzalez V., Strunnikov A.V.
Cell Cycle 3:960-967(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"Kinetic and mechanistic studies of a cell cycle protein phosphatase Cdc14."
Wang W.Q., Bembenek J., Gee K.R., Yu H., Charbonneau H., Zhang Z.Y.
J. Biol. Chem. 279:30459-30468(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY.
[17]"Clb6/Cdc28 and Cdc14 regulate phosphorylation status and cellular localization of Swi6."
Geymonat M., Spanos A., Wells G.P., Smerdon S.J., Sedgwick S.G.
Mol. Cell. Biol. 24:2277-2285(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DEPHOSPHORYLATION OF SWI6.
[18]"Phosphorylation by cyclin B-Cdk underlies release of mitotic exit activator Cdc14 from the nucleolus."
Azzam R., Chen S.L., Shou W., Mah A.S., Alexandru G., Nasmyth K., Annan R.S., Carr S.A., Deshaies R.J.
Science 305:516-519(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[19]"Crm1-mediated nuclear export of Cdc14 is required for the completion of cytokinesis in budding yeast."
Bembenek J., Kang J., Kurischko C., Li B., Raab J.R., Belanger K.D., Luca F.C., Yu H.
Cell Cycle 4:961-971(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CRM1, FUNCTION.
[20]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[21]"Novel role for Cdc14 sequestration: Cdc14 dephosphorylates factors that promote DNA replication."
Bloom J., Cross F.R.
Mol. Cell. Biol. 27:842-853(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DEPHOSPHORYLATION OF DBP2; SIC1 AND SLD2.
[22]"Assembling the spindle midzone in the right place at the right time."
Khmelinskii A., Schiebel E.
Cell Cycle 7:283-286(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DEPHOSPHORYLATION OF ASE1.
[23]"The Polo-like kinase Cdc5 interacts with FEAR network components and Cdc14."
Rahal R., Amon A.
Cell Cycle 7:3262-3272(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CDC5.
[24]"A nucleolus-localized activator of Cdc14 phosphatase supports rDNA segregation in yeast mitosis."
Geil C., Schwab M., Seufert W.
Curr. Biol. 18:1001-1005(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH TOF2.
[25]"Cdc28 and Cdc14 control stability of the anaphase-promoting complex inhibitor Acm1."
Hall M.C., Jeong D.E., Henderson J.T., Choi E., Bremmer S.C., Iliuk A.B., Charbonneau H.
J. Biol. Chem. 283:10396-10407(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DEPHOSPHORYLATION OF ACM1.
[26]"Regulation of Sli15/INCENP, kinetochore, and Cdc14 phosphatase functions by the ribosome biogenesis protein Utp7."
Jwa M., Kim J.H., Chan C.S.
J. Cell Biol. 182:1099-1111(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH UTP7.
[27]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"Dbf2-Mob1 drives relocalization of protein phosphatase Cdc14 to the cytoplasm during exit from mitosis."
Mohl D.A., Huddleston M.J., Collingwood T.S., Annan R.S., Deshaies R.J.
J. Cell Biol. 184:527-539(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[29]"Cdc14 inhibition by the spindle assembly checkpoint prevents unscheduled centrosome separation in budding yeast."
Chiroli E., Rancati G., Catusi I., Lucchini G., Piatti S.
Mol. Biol. Cell 20:2626-2637(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[30]"Cdc14 inhibits transcription by RNA polymerase I during anaphase."
Clemente-Blanco A., Mayan-Santos M., Schneider D.A., Machin F., Jarmuz A., Tschochner H., Aragon L.
Nature 458:219-222(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[31]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[32]"Sli15(INCENP) dephosphorylation prevents mitotic checkpoint reengagement due to loss of tension at anaphase onset."
Mirchenko L., Uhlmann F.
Curr. Biol. 20:1396-1401(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DEPHOSPHORYLATION OF INCENP.
[33]"Cdc14-dependent dephosphorylation of a kinetochore protein prior to anaphase in Saccharomyces cerevisiae."
Akiyoshi B., Biggins S.
Genetics 186:1487-1491(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DEPHOSPHORYLATION OF DSN1.
[34]"Oscillations in Cdc14 release and sequestration reveal a circuit underlying mitotic exit."
Manzoni R., Montani F., Visintin C., Caudron F., Ciliberto A., Visintin R.
J. Cell Biol. 190:209-222(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[35]"The RSC chromatin-remodeling complex influences mitotic exit and adaptation to the spindle assembly checkpoint by controlling the Cdc14 phosphatase."
Rossio V., Galati E., Ferrari M., Pellicioli A., Sutani T., Shirahige K., Lucchini G., Piatti S.
J. Cell Biol. 191:981-997(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[36]"Cdc14p resets the competency of replication licensing by dephosphorylating multiple initiation proteins during mitotic exit in budding yeast."
Zhai Y., Yung P.Y., Huo L., Liang C.
J. Cell Sci. 123:3933-3943(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DEPHOSPHORYLATION OF ORC2; ORC6; CDC6 AND MCM3.
[37]"A quantitative model for ordered Cdk substrate dephosphorylation during mitotic exit."
Bouchoux C., Uhlmann F.
Cell 147:803-814(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[38]"Functions of the mitotic B-type cyclins CLB1, CLB2, and CLB3 at mitotic exit antagonized by the CDC14 phosphatase."
Tzeng Y.W., Huang J.N., Schuyler S.C., Wu C.H., Juang Y.L.
Fungal Genet. Biol. 48:966-978(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ALA-280.
[39]"Global analysis of Cdc14 phosphatase reveals diverse roles in mitotic processes."
Bloom J., Cristea I.M., Procko A.L., Lubkov V., Chait B.T., Snyder M., Cross F.R.
J. Biol. Chem. 286:5434-5445(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASP-253 AND CYS-283, INTERACTION WITH BNI1; BNR1 AND KAR9, FUNCTION IN DEPHOSPHORYLATION OF BNI1; BNR1 AND KAR9.
[40]"Meiotic nuclear divisions in budding yeast require PP2A(Cdc55)-mediated antagonism of Net1 phosphorylation by Cdk."
Kerr G.W., Sarkar S., Tibbles K.L., Petronczki M., Millar J.B., Arumugam P.
J. Cell Biol. 193:1157-1166(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[41]"Cdc55 coordinates spindle assembly and chromosome disjunction during meiosis."
Bizzari F., Marston A.L.
J. Cell Biol. 193:1213-1228(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, FUNCTION.
[42]"The mitotic exit network and Cdc14 phosphatase initiate cytokinesis by counteracting CDK phosphorylations and blocking polarised growth."
Sanchez-Diaz A., Nkosi P.J., Murray S., Labib K.
EMBO J. 31:3620-3634(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[43]"Cdc14 phosphatases preferentially dephosphorylate a subset of cyclin-dependent kinase (Cdk) sites containing phosphoserine."
Bremmer S.C., Hall H., Martinez J.S., Eissler C.L., Hinrichsen T.H., Rossie S., Parker L.L., Hall M.C., Charbonneau H.
J. Biol. Chem. 287:1662-1669(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[44]"Cdc14-dependent dephosphorylation of Inn1 contributes to Inn1-Cyk3 complex formation."
Palani S., Meitinger F., Boehm M.E., Lehmann W.D., Pereira G.
J. Cell Sci. 125:3091-3096(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, FUNCTION IN DEPHOSPHORYLATION OF INN1.
[45]"Dependence of Chs2 ER export on dephosphorylation by cytoplasmic Cdc14 ensures that septum formation follows mitosis."
Chin C.F., Bennett A.M., Ma W.K., Hall M.C., Yeong F.M.
Mol. Biol. Cell 23:45-58(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DEPHOSPHORYLATION OF CHS2.
[46]"Nondisjunction of a single chromosome leads to breakage and activation of DNA damage checkpoint in G2."
Quevedo O., Garcia-Luis J., Matos-Perdomo E., Aragon L., Machin F.
PLoS Genet. 8:E1002509-E1002509(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[47]"The FEAR protein Slk19 restricts Cdc14 phosphatase to the nucleus until the end of anaphase, regulating its participation in mitotic exit in Saccharomyces cerevisiae."
Faust A.M., Wong C.C., Yates Iii J.R., Drubin D.G., Barnes G.
PLoS ONE 8:E73194-E73194(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M61194 Genomic DNA. Translation: AAA34477.1. Frameshift.
D55715 Genomic DNA. Translation: BAA09533.1.
D50617 Genomic DNA. Translation: BAA09267.1.
X75077 Genomic DNA. Translation: CAA52971.1. Frameshift.
BK006940 Genomic DNA. Translation: DAA12468.1.
PIRS56283.
RefSeqNP_116684.3. NM_001179993.3.

3D structure databases

ProteinModelPortalQ00684.
SMRQ00684. Positions 5-336.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31182. 242 interactions.
DIPDIP-5116N.
IntActQ00684. 143 interactions.
MINTMINT-564685.

Proteomic databases

MaxQBQ00684.
PaxDbQ00684.
PeptideAtlasQ00684.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYFR028C; YFR028C; YFR028C.
GeneID850585.
KEGGsce:YFR028C.

Organism-specific databases

CYGDYFR028c.
SGDS000001924. CDC14.

Phylogenomic databases

eggNOGCOG2453.
GeneTreeENSGT00390000010254.
HOGENOMHOG000198341.
KOK06639.
OMAYLHQNDF.
OrthoDBEOG7JQBXJ.

Enzyme and pathway databases

BioCycYEAST:G3O-30477-MONOMER.
SABIO-RKQ00684.

Gene expression databases

GenevestigatorQ00684.

Family and domain databases

Gene3D3.90.190.10. 2 hits.
InterProIPR026070. CDC14.
IPR029260. DSPn.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERPTHR23339:SF27. PTHR23339:SF27. 1 hit.
PfamPF00782. DSPc. 1 hit.
PF14671. DSPn. 1 hit.
[Graphical view]
SMARTSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMSSF52799. SSF52799. 2 hits.
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio966423.
PROQ00684.

Entry information

Entry nameCDC14_YEAST
AccessionPrimary (citable) accession number: Q00684
Secondary accession number(s): D6VTQ8, Q05180, Q05673
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VI

Yeast (Saccharomyces cerevisiae) chromosome VI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families