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Protein

Tyrosine-protein phosphatase CDC14

Gene

CDC14

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -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 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.30 Publications

Miscellaneous

Present with 8550 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation2 Publications

Kineticsi

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

    pH dependencei

    Optimum pH is 6.9.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei283Phosphocysteine intermediatePROSITE-ProRule annotation1

    GO - Molecular functioni

    GO - Biological processi

    • cell division Source: UniProtKB-KW
    • cellular response to osmotic stress Source: SGD
    • chromosome segregation Source: SGD
    • meiotic spindle disassembly Source: SGD
    • mitotic cell cycle Source: SGD
    • mitotic cell cycle arrest Source: GO_Central
    • mitotic spindle midzone assembly Source: GO_Central
    • positive regulation of cytokinesis Source: SGD
    • protein dephosphorylation Source: SGD
    • regulation of exit from mitosis Source: SGD

    Keywordsi

    Molecular functionHydrolase, Protein phosphatase
    Biological processCell cycle, Cell division, Meiosis, Mitosis

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30477-MONOMER
    ReactomeiR-SCE-176407 Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase
    R-SCE-5687128 MAPK6/MAPK4 signaling
    SABIO-RKiQ00684

    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
    Proteomesi
    • UP000002311 Componenti: Chromosome VI

    Organism-specific databases

    EuPathDBiFungiDB:YFR028C
    SGDiS000001924 CDC14

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi253D → A: Inactivates catalytic activity and leads to substrate retention. 1 Publication1
    Mutagenesisi280A → V: Leads to temperature sensitivity. 1 Publication1
    Mutagenesisi283C → S: Inactivates catalytic activity and leads to substrate retention. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000948751 – 551Tyrosine-protein phosphatase CDC14Add BLAST551

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei467PhosphoserineCombined sources1

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ00684
    PaxDbiQ00684
    PRIDEiQ00684

    PTM databases

    iPTMnetiQ00684

    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

    Show more details

    Protein-protein interaction databases

    BioGridi31182493 interactors.
    DIPiDIP-5116N
    IntActiQ00684 182 interactors.
    MINTiQ00684
    STRINGi4932.YFR028C

    Structurei

    Secondary structure

    1551
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi10 – 14Combined sources5
    Turni15 – 17Combined sources3
    Beta strandi18 – 22Combined sources5
    Beta strandi31 – 36Combined sources6
    Turni39 – 41Combined sources3
    Beta strandi47 – 49Combined sources3
    Helixi56 – 71Combined sources16
    Helixi73 – 75Combined sources3
    Beta strandi78 – 84Combined sources7
    Helixi88 – 106Combined sources19
    Helixi110 – 114Combined sources5
    Helixi115 – 117Combined sources3
    Beta strandi130 – 133Combined sources4
    Helixi141 – 153Combined sources13
    Turni159 – 161Combined sources3
    Helixi164 – 170Combined sources7
    Helixi173 – 175Combined sources3
    Beta strandi178 – 180Combined sources3
    Beta strandi182 – 189Combined sources8
    Helixi209 – 220Combined sources12
    Beta strandi223 – 228Combined sources6
    Helixi237 – 240Combined sources4
    Turni241 – 243Combined sources3
    Beta strandi245 – 248Combined sources4
    Helixi259 – 274Combined sources16
    Beta strandi278 – 287Combined sources10
    Helixi288 – 302Combined sources15
    Helixi306 – 316Combined sources11
    Helixi324 – 342Combined sources19
    Beta strandi343 – 345Combined sources3
    Helixi351 – 353Combined sources3
    Beta strandi359 – 361Combined sources3
    Helixi362 – 367Combined sources6

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4ZJ7X-ray2.40B517-551[»]
    5XW4X-ray1.85A/B1-374[»]
    5XW5X-ray1.85A/B1-374[»]
    ProteinModelPortaliQ00684
    SMRiQ00684
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    GeneTreeiENSGT00390000010254
    HOGENOMiHOG000198341
    InParanoidiQ00684
    KOiK06639
    OMAiCCYMVLV
    OrthoDBiEOG092C2FOY

    Family and domain databases

    Gene3Di3.90.190.102 hits
    InterProiView protein in InterPro
    IPR026070 CDC14
    IPR029260 DSPn
    IPR000340 Dual-sp_phosphatase_cat-dom
    IPR029021 Prot-tyrosine_phosphatase-like
    IPR016130 Tyr_Pase_AS
    IPR003595 Tyr_Pase_cat
    IPR000387 TYR_PHOSPHATASE_dom
    IPR020422 TYR_PHOSPHATASE_DUAL_dom
    PANTHERiPTHR23339:SF27 PTHR23339:SF27, 1 hit
    PfamiView protein in Pfam
    PF00782 DSPc, 1 hit
    PF14671 DSPn, 1 hit
    SMARTiView protein in SMART
    SM00195 DSPc, 1 hit
    SM00404 PTPc_motif, 1 hit
    SUPFAMiSSF52799 SSF52799, 2 hits
    PROSITEiView protein in PROSITE
    PS00383 TYR_PHOSPHATASE_1, 1 hit
    PS50056 TYR_PHOSPHATASE_2, 1 hit

    Sequencei

    Sequence statusi: Complete.

    Q00684-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRRSVYLDNT IEFLRGRVYL GAYDYTPEDT DELVFFTVED AIFYNSFHLD
    60 70 80 90 100
    FGPMNIGHLY RFAVIFHEIL NDPENANKAV VFYSSASTRQ RANAACMLCC
    110 120 130 140 150
    YMILVQAWTP HQVLQPLAQV DPPFMPFRDA GYSNADFEIT IQDVVYGVWR
    160 170 180 190 200
    AKEKGLIDLH SFNLESYEKY EHVEFGDFNV LTPDFIAFAS PQEDHPKGYL
    210 220 230 240 250
    ATKSSHLNQP FKSVLNFFAN NNVQLVVRLN SHLYNKKHFE DIGIQHLDLI
    260 270 280 290 300
    FEDGTCPDLS IVKNFVGAAE TIIKRGGKIA VHCKAGLGRT GCLIGAHLIY
    310 320 330 340 350
    TYGFTANECI GFLRFIRPGM VVGPQQHWLY LHQNDFREWK YTTRISLKPS
    360 370 380 390 400
    EAIGGLYPLI SLEEYRLQKK KLKDDKRVAQ NNIEGELRDL TMTPPSNGHG
    410 420 430 440 450
    ALSARNSSQP STANNGSNSF KSSAVPQTSP GQPRKGQNGS NTIEDINNNR
    460 470 480 490 500
    NPTSHANRKV VIESNNSDDE SMQDTNGTSN HYPKVSRKKN DISSASSSRM
    510 520 530 540 550
    EDNEPSATNI NNAADDTILR QLLPKNRRVT SGRRTTSAAG GIRKISGSIK

    K
    Length:551
    Mass (Da):61,907
    Last modified:November 1, 1995 - v2
    Checksum:i4EB3985DFA3FD823
    GO

    Sequence cautioni

    The sequence AAA34477 differs from that shown. Reason: Frameshift at positions 116 and 190.Curated
    The sequence CAA52971 differs from that shown. Reason: Frameshift at position 117.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti118A → P in BAA09533 (PubMed:8668128).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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

    EnsemblFungiiBAA09267; BAA09267; BAA09267
    YFR028C; YFR028C; YFR028C
    GeneIDi850585
    KEGGisce:YFR028C

    Similar proteinsi

    Entry informationi

    Entry nameiCDC14_YEAST
    AccessioniPrimary (citable) accession number: Q00684
    Secondary accession number(s): D6VTQ8, Q05180, Q05673
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: November 1, 1995
    Last modified: March 28, 2018
    This is version 177 of the entry and version 2 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome