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Q59NH8

- CDC14_CANAL

UniProt

Q59NH8 - CDC14_CANAL

Protein

Tyrosine-protein phosphatase CDC14

Gene

CDC14

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (26 Apr 2005)
      Previous versions | rss
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    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 By similarity. Plays a role in the expression of hydrolase genes such as CHT3 and ENG1 involved in septum degradation after cytokinesis. Also required for ACE2 localization to the daughter nucleus. Required for invasive and hyphal growth.By similarity3 Publications

    Catalytic activityi

    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei227 – 2271Phosphocysteine intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

    1. protein tyrosine/serine/threonine phosphatase activity Source: CGD
    2. protein tyrosine phosphatase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellular response to glucose starvation Source: CGD
    2. cytokinetic cell separation Source: CGD
    3. hyphal growth Source: CGD
    4. invasive growth in response to glucose limitation Source: CGD
    5. meiotic nuclear division Source: UniProtKB-KW
    6. mitotic nuclear division Source: CGD
    7. regulation of exit from mitosis Source: CGD

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Cell cycle, Cell division, Meiosis, Mitosis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein phosphatase CDC14 (EC:3.1.3.48)
    Gene namesi
    Name:CDC14
    ORF Names:CaO19.11669, CaO19.4192
    OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
    Taxonomic identifieri237561 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida
    ProteomesiUP000000559: Unassembled WGS sequence

    Organism-specific databases

    CGDiCAL0073922. CDC14.

    Subcellular locationi

    Nucleusnucleolus. Cytoplasm. Bud neck. Cytoplasmcytoskeletonspindle pole. Cell septum
    Note: Does not accumulate in the nucleolus in interphase cells. At the G1-S transition, starts to accumulate both in the nucleolus and the and the DAPI-staining region of the nucleus. At the S-G2 transition, starts to concentrate as faint foci on the nuclear periphery. In early mitosis, the CDC14 nuclear signal diminishes concentrates to the spindle pole body (SPB). During cytokinesis, the localization at the SPBs gets fainter and the protein is preferentially found at the septum region. In yeast forms, in which cell separation takes place after cytokinesis, CDC14 is present at the bud neck; in hyphal forms, in which cell separation is inhibited, no CDC14 signal is detected.

    GO - Cellular componenti

    1. cell septum Source: CGD
    2. cellular bud neck Source: UniProtKB-SubCell
    3. cytoplasm Source: UniProtKB-SubCell
    4. nucleolus Source: CGD
    5. nucleus Source: CGD
    6. spindle pole body Source: CGD

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Leads to defective cell separation and impairs hyphal growth.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 494494Tyrosine-protein phosphatase CDC14PRO_0000425253Add
    BLAST

    Post-translational modificationi

    Mainly phosphorylated as the cells are passing through mitosis in yeast form cells. Phosphorylation is delayed in hyphal-induced cells, indicating that the timing of cell-cycle progression occurs with different kinetics in hyphae and in yeast cells.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Expressioni

    Inductioni

    Both during budding and hyphal growth, no detectable levels are observed in G1 cells but, as cells passe through S-phase, begins to accumulate with a peak being reached during mitosis.2 Publications

    Interactioni

    Protein-protein interaction databases

    STRINGi5476.CAL0005886.

    Structurei

    3D structure databases

    ProteinModelPortaliQ59NH8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi438 – 4436Poly-Thr

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG2453.
    KOiK06639.
    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.

    Q59NH8-1 [UniParc]FASTAAdd to Basket

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    MDFGPLNIGH LYRFAVLLHK KLNEDSTQGK GLVIYSSTSP KERANLACLL    50
    CCYMILLQNW APHQVLQPIA QITPPLQAFR DAGYSSADYE ITIQDVVYAM 100
    WRAKERGMID LAKFDLDEYE QYERVDQGDF NVISKDFIAF ASPQQSKRGG 150
    LNEPFQKVLE YFVENNVQLV VRLNSHLYDA KEFTKRNIKH IDMIFDDGTC 200
    PTLEYVQKFI GAAECIINKG GKIAVHCKAG LGRTGCLIGA HLIYTHGFTA 250
    NECIAYMRMI RPGMVVGPQQ HWLYLHHDDF RSWRHTMIVD NRPDPLIGNL 300
    FPLCSYEDYK QRLKEAKRKE RLQLQQQLTS PLADSSVINT PIRRRKVSGA 350
    LASKIQTVVP IESPGQPRKY FEDSEDIDEV EMVNNSDDEN TMQDIIQSSP 400
    ARYDSVTPKT KDNSDWRVLR SISTNNVSSQ QSIHIIKTTT TKTVNETLSS 450
    PPGTSPTNVL RVSKARSKNR IASGNSQTSR AHSGGVRKLS GKKH 494
    Length:494
    Mass (Da):55,912
    Last modified:April 26, 2005 - v1
    Checksum:i8B956E794CC0E182
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AACQ01000206 Genomic DNA. Translation: EAK92009.1.
    AACQ01000205 Genomic DNA. Translation: EAK92033.1.
    RefSeqiXP_711244.1. XM_706152.1.
    XP_711268.1. XM_706176.1.

    Genome annotation databases

    GeneIDi3647116.
    3647132.
    KEGGical:CaO19.11669.
    cal:CaO19.4192.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AACQ01000206 Genomic DNA. Translation: EAK92009.1 .
    AACQ01000205 Genomic DNA. Translation: EAK92033.1 .
    RefSeqi XP_711244.1. XM_706152.1.
    XP_711268.1. XM_706176.1.

    3D structure databases

    ProteinModelPortali Q59NH8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5476.CAL0005886.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 3647116.
    3647132.
    KEGGi cal:CaO19.11669.
    cal:CaO19.4192.

    Organism-specific databases

    CGDi CAL0073922. CDC14.

    Phylogenomic databases

    eggNOGi COG2453.
    KOi K06639.
    OrthoDBi EOG7JQBXJ.

    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

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: SC5314 / ATCC MYA-2876.
    2. "A single-copy suppressor of the Saccharomyces cerevisae late-mitotic mutants cdc15 and dbf2 is encoded by the Candida albicans CDC14 gene."
      Jimenez J., Cid V.J., Nombela C., Sanchez M.
      Yeast 18:849-858(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    3. "The Cdc14p phosphatase affects late cell-cycle events and morphogenesis in Candida albicans."
      Clemente-Blanco A., Gonzalez-Novo A., Machin F., Caballero-Lima D., Aragon L., Sanchez M., de Aldana C.R., Jimenez J., Correa-Bordes J.
      J. Cell Sci. 119:1130-1143(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, PHOSPHORYLATION, DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION.
    4. "Sep7 is essential to modify septin ring dynamics and inhibit cell separation during Candida albicans hyphal growth."
      Gonzalez-Novo A., Correa-Bordes J., Labrador L., Sanchez M., Vazquez de Aldana C.R., Jimenez J.
      Mol. Biol. Cell 19:1509-1518(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    5. "Transcriptional analysis of the Candida albicans cell cycle."
      Cote P., Hogues H., Whiteway M.
      Mol. Biol. Cell 20:3363-3373(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.

    Entry informationi

    Entry nameiCDC14_CANAL
    AccessioniPrimary (citable) accession number: Q59NH8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 19, 2014
    Last sequence update: April 26, 2005
    Last modified: October 1, 2014
    This is version 66 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Candida albicans
      Candida albicans: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3