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Q00684

- CDC14_YEAST

UniProt

Q00684 - CDC14_YEAST

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Protein

Tyrosine-protein phosphatase CDC14

Gene
CDC14, OAF3, YFR028C
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.30 Publications

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.2 Publications

Kineticsi

  1. KM=4 mM for p-nitrophenyl phosphate1 Publication

pH dependencei

Optimum pH is 6.9.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei283 – 2831Phosphocysteine intermediate By similarity

GO - Molecular functioni

  1. phosphoprotein phosphatase activity Source: SGD
  2. protein binding Source: IntAct
  3. protein tyrosine/serine/threonine phosphatase activity Source: InterPro
  4. protein tyrosine phosphatase activity Source: UniProtKB-EC

GO - Biological processi

  1. chromosome separation Source: SGD
  2. meiotic nuclear division Source: UniProtKB-KW
  3. meiotic spindle disassembly Source: SGD
  4. mitotic cell cycle Source: SGD
  5. mitotic nuclear division Source: UniProtKB-KW
  6. protein dephosphorylation Source: SGD
  7. regulation of exit from mitosis Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Cell cycle, Cell division, Meiosis, Mitosis

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein phosphatase CDC14 (EC:3.1.3.48)
Gene namesi
Name:CDC14
Synonyms:OAF3
Ordered Locus Names:YFR028C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VI

Organism-specific databases

CYGDiYFR028c.
SGDiS000001924. CDC14.

Subcellular locationi

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.14 Publications

GO - Cellular componenti

  1. cellular bud neck Source: UniProtKB-SubCell
  2. cytoplasm Source: UniProtKB-SubCell
  3. nucleolus Source: SGD
  4. RENT complex Source: SGD
  5. spindle pole body Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi253 – 2531D → A: Inactivates catalytic activity and leads to substrate retention. 1 Publication
Mutagenesisi280 – 2801A → V: Leads to temperature sensitivity. 1 Publication
Mutagenesisi283 – 2831C → S: Inactivates catalytic activity and leads to substrate retention. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 551551Tyrosine-protein phosphatase CDC14PRO_0000094875Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei467 – 4671Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ00684.
PaxDbiQ00684.
PeptideAtlasiQ00684.

Expressioni

Gene expression databases

GenevestigatoriQ00684.

Interactioni

Subunit structurei

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 UTP7.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ASK1P357342EBI-4192,EBI-26682
BCK1Q013894EBI-4192,EBI-3470
BOI1P380412EBI-4192,EBI-3719
CBK1P538942EBI-4192,EBI-4110
CDC5P325622EBI-4192,EBI-4440
CHK1P381472EBI-4192,EBI-4593
CKA1P157903EBI-4192,EBI-9533
CKA2P194543EBI-4192,EBI-9548
CLB3P248702EBI-4192,EBI-4522
FIN1Q038982EBI-4192,EBI-32941
FMP48P532332EBI-4192,EBI-9664
GIC1P387852EBI-4192,EBI-7575
MCK1P219652EBI-4192,EBI-10517
MET14Q021962EBI-4192,EBI-9485
NET1P4703513EBI-4192,EBI-25953
ORC6P388262EBI-4192,EBI-12588
RSP5P399402EBI-4192,EBI-16219
SAK1P389902EBI-4192,EBI-12863
SIC1P386342EBI-4192,EBI-17127
SIR2P067005EBI-4192,EBI-17219
SLI15P382832EBI-4192,EBI-20842
SNF1P067822EBI-4192,EBI-17516
STE7P067842EBI-4192,EBI-18389
SWE1P329443EBI-4192,EBI-18607
TOF2Q022088EBI-4192,EBI-27048
VHS1Q037852EBI-4192,EBI-35568

Protein-protein interaction databases

BioGridi31182. 242 interactions.
DIPiDIP-5116N.
IntActiQ00684. 143 interactions.
MINTiMINT-564685.

Structurei

3D structure databases

ProteinModelPortaliQ00684.
SMRiQ00684. Positions 5-336.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00390000010254.
HOGENOMiHOG000198341.
KOiK06639.
OMAiYLHQNDF.
OrthoDBiEOG7JQBXJ.

Family and domain databases

Gene3Di3.90.190.10. 2 hits.
InterProiIPR026070. 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]
PANTHERiPTHR23339:SF27. PTHR23339:SF27. 1 hit.
PfamiPF00782. DSPc. 1 hit.
PF14671. DSPn. 1 hit.
[Graphical view]
SMARTiSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 2 hits.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q00684-1 [UniParc]FASTAAdd to Basket

« Hide

MRRSVYLDNT IEFLRGRVYL GAYDYTPEDT DELVFFTVED AIFYNSFHLD    50
FGPMNIGHLY RFAVIFHEIL NDPENANKAV VFYSSASTRQ RANAACMLCC 100
YMILVQAWTP HQVLQPLAQV DPPFMPFRDA GYSNADFEIT IQDVVYGVWR 150
AKEKGLIDLH SFNLESYEKY EHVEFGDFNV LTPDFIAFAS PQEDHPKGYL 200
ATKSSHLNQP FKSVLNFFAN NNVQLVVRLN SHLYNKKHFE DIGIQHLDLI 250
FEDGTCPDLS IVKNFVGAAE TIIKRGGKIA VHCKAGLGRT GCLIGAHLIY 300
TYGFTANECI GFLRFIRPGM VVGPQQHWLY LHQNDFREWK YTTRISLKPS 350
EAIGGLYPLI SLEEYRLQKK KLKDDKRVAQ NNIEGELRDL TMTPPSNGHG 400
ALSARNSSQP STANNGSNSF KSSAVPQTSP GQPRKGQNGS NTIEDINNNR 450
NPTSHANRKV VIESNNSDDE SMQDTNGTSN HYPKVSRKKN DISSASSSRM 500
EDNEPSATNI NNAADDTILR QLLPKNRRVT SGRRTTSAAG GIRKISGSIK 550
K 551
Length:551
Mass (Da):61,907
Last modified:November 1, 1995 - v2
Checksum:i4EB3985DFA3FD823
GO

Sequence cautioni

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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti118 – 1181A → P in BAA09533. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiS56283.
RefSeqiNP_116684.3. NM_001179993.3.

Genome annotation databases

EnsemblFungiiYFR028C; YFR028C; YFR028C.
GeneIDi850585.
KEGGisce:YFR028C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi S56283.
RefSeqi NP_116684.3. NM_001179993.3.

3D structure databases

ProteinModelPortali Q00684.
SMRi Q00684. Positions 5-336.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31182. 242 interactions.
DIPi DIP-5116N.
IntActi Q00684. 143 interactions.
MINTi MINT-564685.

Proteomic databases

MaxQBi Q00684.
PaxDbi Q00684.
PeptideAtlasi Q00684.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YFR028C ; YFR028C ; YFR028C .
GeneIDi 850585.
KEGGi sce:YFR028C.

Organism-specific databases

CYGDi YFR028c.
SGDi S000001924. CDC14.

Phylogenomic databases

eggNOGi COG2453.
GeneTreei ENSGT00390000010254.
HOGENOMi HOG000198341.
KOi K06639.
OMAi YLHQNDF.
OrthoDBi EOG7JQBXJ.

Enzyme and pathway databases

BioCyci YEAST:G3O-30477-MONOMER.
SABIO-RK Q00684.

Miscellaneous databases

NextBioi 966423.
PROi Q00684.

Gene expression databases

Genevestigatori Q00684.

Family and domain databases

Gene3Di 3.90.190.10. 2 hits.
InterProi IPR026070. 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 ]
PANTHERi PTHR23339:SF27. PTHR23339:SF27. 1 hit.
Pfami PF00782. DSPc. 1 hit.
PF14671. DSPn. 1 hit.
[Graphical view ]
SMARTi SM00195. DSPc. 1 hit.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 2 hits.
PROSITEi PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. 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. 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. 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.

Entry informationi

Entry nameiCDC14_YEAST
AccessioniPrimary (citable) accession number: Q00684
Secondary accession number(s): D6VTQ8, Q05180, Q05673
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 1, 1995
Last modified: September 3, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome VI
    Yeast (Saccharomyces cerevisiae) chromosome VI: entries and gene names

External Data

Dasty 3

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