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Q9UNH5

- CC14A_HUMAN

UniProt

Q9UNH5 - CC14A_HUMAN

Protein

Dual specificity protein phosphatase CDC14A

Gene

CDC14A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Dual-specificity phosphatase. Required for centrosome separation and productive cytokinesis during cell division. Dephosphorylates SIRT2 around early anaphase. May dephosphorylate the APC subunit FZR1/CDH1, thereby promoting APC-FZR1 dependent degradation of mitotic cyclins and subsequent exit from mitosis.4 Publications

    Catalytic activityi

    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation
    [a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei278 – 2781Phosphocysteine intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. cell division Source: UniProtKB-KW
    3. cell proliferation Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Cell cycle, Cell division

    Enzyme and pathway databases

    ReactomeiREACT_6867. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity protein phosphatase CDC14A (EC:3.1.3.16, EC:3.1.3.48)
    Alternative name(s):
    CDC14 cell division cycle 14 homolog A
    Gene namesi
    Name:CDC14A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:1718. CDC14A.

    Subcellular locationi

    Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonspindle
    Note: Centrosomal during interphase, released into the cytoplasm at the onset of mitosis. Subsequently localizes to the midzone of the mitotic spindle.

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. cytoplasm Source: HPA
    3. nucleus Source: HPA
    4. spindle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi251 – 2511D → A: Loss of phosphatase activity. 1 Publication
    Mutagenesisi278 – 2781C → S: Loss of phosphatase activity. 2 Publications
    Mutagenesisi284 – 2841R → A: Loss of phosphatase activity. 1 Publication
    Mutagenesisi362 – 3621M → A: Inappropriate nucleolar localization; when associated with A-364. 1 Publication
    Mutagenesisi364 – 3641I → A: Inappropriate nucleolar localization; when associated with A-362. 1 Publication

    Organism-specific databases

    PharmGKBiPA26254.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 594594Dual specificity protein phosphatase CDC14APRO_0000094876Add
    BLAST

    Proteomic databases

    PaxDbiQ9UNH5.
    PRIDEiQ9UNH5.

    PTM databases

    PhosphoSiteiQ9UNH5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UNH5.
    BgeeiQ9UNH5.
    CleanExiHS_CDC14A.
    GenevestigatoriQ9UNH5.

    Organism-specific databases

    HPAiHPA023783.

    Interactioni

    Subunit structurei

    Interacts with KIF20A, which is required to localize CDC14 to the midzone of the mitotic spindle.1 Publication

    Protein-protein interaction databases

    BioGridi114126. 10 interactions.
    IntActiQ9UNH5. 1 interaction.
    MINTiMINT-8330048.
    STRINGi9606.ENSP00000354916.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UNH5.
    SMRiQ9UNH5. Positions 15-343.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni7 – 162156AAdd
    BLAST
    Regioni163 – 17614LinkerAdd
    BLAST
    Regioni177 – 343167BAdd
    BLAST

    Domaini

    Composed of two structurally equivalent A and B domains that adopt a dual specificity protein phosphatase (DSP) fold.By similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG2453.
    HOVERGENiHBG050818.
    KOiK06639.
    OMAiNNQYSRS.
    OrthoDBiEOG776SPM.
    PhylomeDBiQ9UNH5.
    TreeFamiTF101053.

    Family and domain databases

    Gene3Di3.90.190.10. 2 hits.
    InterProiIPR029260. DSPn.
    IPR000340. Dual-sp_phosphatase_cat-dom.
    IPR020422. Dual-sp_phosphatase_subgr_cat.
    IPR026068. Dual_Pase_CDC14A.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    [Graphical view]
    PANTHERiPTHR23339:SF62. PTHR23339:SF62. 1 hit.
    PfamiPF00782. DSPc. 1 hit.
    PF14671. DSPn. 1 hit.
    [Graphical view]
    SUPFAMiSSF52799. SSF52799. 2 hits.
    PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UNH5-1) [UniParc]FASTAAdd to Basket

    Also known as: CDC14A1

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAAESGELIG ACEFMKDRLY FATLRNRPKS TVNTHYFSID EELVYENFYA    50
    DFGPLNLAMV YRYCCKLNKK LKSYSLSRKK IVHYTCFDQR KRANAAFLIG 100
    AYAVIYLKKT PEEAYRALLS GSNPPYLPFR DASFGNCTYN LTILDCLQGI 150
    RKGLQHGFFD FETFDVDEYE HYERVENGDF NWIVPGKFLA FSGPHPKSKI 200
    ENGYPLHAPE AYFPYFKKHN VTAVVRLNKK IYEAKRFTDA GFEHYDLFFI 250
    DGSTPSDNIV RRFLNICENT EGAIAVHCKA GLGRTGTLIA CYVMKHYRFT 300
    HAEIIAWIRI CRPGSIIGPQ QHFLEEKQAS LWVQGDIFRS KLKNRPSSEG 350
    SINKILSGLD DMSIGGNLSK TQNMERFGED NLEDDDVEMK NGITQGDKLR 400
    ALKSQRQPRT SPSCAFRSDD TKGHPRAVSQ PFRLSSSLQG SAVTLKTSKM 450
    ALSPSATAKR INRTSLSSGA TVRSFSINSR LASSLGNLNA ATDDPENKKT 500
    SSSSKAGFTA SPFTNLLNGS SQPTTRNYPE LNNNQYNRSS NSNGGNLNSP 550
    PGPHSAKTEE HTTILRPSYT GLSSSSARFL SRSIPSLQSE YVHY 594
    Length:594
    Mass (Da):66,574
    Last modified:May 1, 2000 - v1
    Checksum:iD5552E2BAEEA84DF
    GO
    Isoform 2 (identifier: Q9UNH5-2) [UniParc]FASTAAdd to Basket

    Also known as: CDC14A2

    The sequence of this isoform differs from the canonical sequence as follows:
         586-594: SLQSEYVHY → VSAQTPPPGPQNPECNFCALPSQPRLPPKKFNSAKEAF

    Show »
    Length:623
    Mass (Da):69,543
    Checksum:iCAB2041A59DB3350
    GO
    Isoform 3 (identifier: Q9UNH5-3) [UniParc]FASTAAdd to Basket

    Also known as: CDC14A3

    The sequence of this isoform differs from the canonical sequence as follows:
         380-383: DNLE → VSFP
         384-594: Missing.

    Show »
    Length:383
    Mass (Da):43,908
    Checksum:i28295D04793D00B7
    GO
    Isoform 4 (identifier: Q9UNH5-4) [UniParc]FASTAAdd to Basket

    Also known as: CDC14A4

    The sequence of this isoform differs from the canonical sequence as follows:
         174-191: RVENGDFNWIVPGKFLAF → VILFTPLKPTFLISKSIM
         192-594: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:191
    Mass (Da):22,175
    Checksum:i14E97BCF291E4D81
    GO
    Isoform 5 (identifier: Q9UNH5-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         586-594: SLQSEYVHY → CSCLLLVFRKPFLGSPLLSLPISHL

    Show »
    Length:610
    Mass (Da):68,203
    Checksum:iCA0AC7B44CAE4947
    GO

    Sequence cautioni

    The sequence AAB88277.1 differs from that shown. Reason: Frameshift at position 6.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti164 – 1641F → I in AAB88277. (PubMed:9367992)Curated
    Sequence conflicti182 – 1821W → C in AAB88277. (PubMed:9367992)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti345 – 3451R → Q.1 Publication
    Corresponds to variant rs28364897 [ dbSNP | Ensembl ].
    VAR_019957
    Natural varianti493 – 4931D → Y in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035655
    Natural varianti589 – 5891S → F.1 Publication
    Corresponds to variant rs28364923 [ dbSNP | Ensembl ].
    VAR_019958

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei174 – 19118RVENG…KFLAF → VILFTPLKPTFLISKSIM in isoform 4. 1 PublicationVSP_012322Add
    BLAST
    Alternative sequencei192 – 594403Missing in isoform 4. 1 PublicationVSP_012323Add
    BLAST
    Alternative sequencei380 – 3834DNLE → VSFP in isoform 3. 2 PublicationsVSP_012035
    Alternative sequencei384 – 594211Missing in isoform 3. 2 PublicationsVSP_012036Add
    BLAST
    Alternative sequencei586 – 5949SLQSEYVHY → VSAQTPPPGPQNPECNFCAL PSQPRLPPKKFNSAKEAF in isoform 2. 1 PublicationVSP_012037
    Alternative sequencei586 – 5949SLQSEYVHY → CSCLLLVFRKPFLGSPLLSL PISHL in isoform 5. 1 PublicationVSP_047597

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF000367 mRNA. Translation: AAB88277.1. Frameshift.
    AF122013 mRNA. Translation: AAD49217.1.
    AF064102 mRNA. Translation: AAC16659.1.
    AF064103 mRNA. Translation: AAC16660.1.
    DQ530256 mRNA. Translation: ABF74568.1.
    AY623111 Genomic DNA. Translation: AAT38107.1.
    AL589990, AC104457 Genomic DNA. Translation: CAH70068.1.
    AL589990, AC104457 Genomic DNA. Translation: CAH70069.1.
    AL589990, AC104457 Genomic DNA. Translation: CAH70070.1.
    CH471097 Genomic DNA. Translation: EAW72956.1.
    CH471097 Genomic DNA. Translation: EAW72958.1.
    CH471097 Genomic DNA. Translation: EAW72959.1.
    BC038979 mRNA. Translation: AAH38979.1.
    BC093916 mRNA. Translation: AAH93916.1.
    BC093918 mRNA. Translation: AAH93918.1.
    CCDSiCCDS769.1. [Q9UNH5-1]
    CCDS770.1. [Q9UNH5-2]
    CCDS771.1. [Q9UNH5-3]
    RefSeqiNP_003663.2. NM_003672.3. [Q9UNH5-1]
    NP_201569.1. NM_033312.2. [Q9UNH5-2]
    NP_201570.1. NM_033313.2. [Q9UNH5-3]
    UniGeneiHs.127411.

    Genome annotation databases

    EnsembliENST00000336454; ENSP00000336739; ENSG00000079335. [Q9UNH5-1]
    ENST00000361544; ENSP00000354916; ENSG00000079335. [Q9UNH5-2]
    ENST00000370124; ENSP00000359142; ENSG00000079335. [Q9UNH5-3]
    GeneIDi8556.
    KEGGihsa:8556.
    UCSCiuc001dte.4. human. [Q9UNH5-3]
    uc001dtf.2. human. [Q9UNH5-2]
    uc001dtg.4. human. [Q9UNH5-1]
    uc009wec.1. human. [Q9UNH5-4]

    Polymorphism databases

    DMDMi55976620.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF000367 mRNA. Translation: AAB88277.1 . Frameshift.
    AF122013 mRNA. Translation: AAD49217.1 .
    AF064102 mRNA. Translation: AAC16659.1 .
    AF064103 mRNA. Translation: AAC16660.1 .
    DQ530256 mRNA. Translation: ABF74568.1 .
    AY623111 Genomic DNA. Translation: AAT38107.1 .
    AL589990 , AC104457 Genomic DNA. Translation: CAH70068.1 .
    AL589990 , AC104457 Genomic DNA. Translation: CAH70069.1 .
    AL589990 , AC104457 Genomic DNA. Translation: CAH70070.1 .
    CH471097 Genomic DNA. Translation: EAW72956.1 .
    CH471097 Genomic DNA. Translation: EAW72958.1 .
    CH471097 Genomic DNA. Translation: EAW72959.1 .
    BC038979 mRNA. Translation: AAH38979.1 .
    BC093916 mRNA. Translation: AAH93916.1 .
    BC093918 mRNA. Translation: AAH93918.1 .
    CCDSi CCDS769.1. [Q9UNH5-1 ]
    CCDS770.1. [Q9UNH5-2 ]
    CCDS771.1. [Q9UNH5-3 ]
    RefSeqi NP_003663.2. NM_003672.3. [Q9UNH5-1 ]
    NP_201569.1. NM_033312.2. [Q9UNH5-2 ]
    NP_201570.1. NM_033313.2. [Q9UNH5-3 ]
    UniGenei Hs.127411.

    3D structure databases

    ProteinModelPortali Q9UNH5.
    SMRi Q9UNH5. Positions 15-343.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114126. 10 interactions.
    IntActi Q9UNH5. 1 interaction.
    MINTi MINT-8330048.
    STRINGi 9606.ENSP00000354916.

    Chemistry

    BindingDBi Q9UNH5.
    ChEMBLi CHEMBL1772926.

    PTM databases

    PhosphoSitei Q9UNH5.

    Polymorphism databases

    DMDMi 55976620.

    Proteomic databases

    PaxDbi Q9UNH5.
    PRIDEi Q9UNH5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000336454 ; ENSP00000336739 ; ENSG00000079335 . [Q9UNH5-1 ]
    ENST00000361544 ; ENSP00000354916 ; ENSG00000079335 . [Q9UNH5-2 ]
    ENST00000370124 ; ENSP00000359142 ; ENSG00000079335 . [Q9UNH5-3 ]
    GeneIDi 8556.
    KEGGi hsa:8556.
    UCSCi uc001dte.4. human. [Q9UNH5-3 ]
    uc001dtf.2. human. [Q9UNH5-2 ]
    uc001dtg.4. human. [Q9UNH5-1 ]
    uc009wec.1. human. [Q9UNH5-4 ]

    Organism-specific databases

    CTDi 8556.
    GeneCardsi GC01P100817.
    HGNCi HGNC:1718. CDC14A.
    HPAi HPA023783.
    MIMi 603504. gene.
    neXtProti NX_Q9UNH5.
    PharmGKBi PA26254.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2453.
    HOVERGENi HBG050818.
    KOi K06639.
    OMAi NNQYSRS.
    OrthoDBi EOG776SPM.
    PhylomeDBi Q9UNH5.
    TreeFami TF101053.

    Enzyme and pathway databases

    Reactomei REACT_6867. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.

    Miscellaneous databases

    GeneWikii CDC14A.
    GenomeRNAii 8556.
    NextBioi 32065.
    PROi Q9UNH5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UNH5.
    Bgeei Q9UNH5.
    CleanExi HS_CDC14A.
    Genevestigatori Q9UNH5.

    Family and domain databases

    Gene3Di 3.90.190.10. 2 hits.
    InterProi IPR029260. DSPn.
    IPR000340. Dual-sp_phosphatase_cat-dom.
    IPR020422. Dual-sp_phosphatase_subgr_cat.
    IPR026068. Dual_Pase_CDC14A.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    [Graphical view ]
    PANTHERi PTHR23339:SF62. PTHR23339:SF62. 1 hit.
    Pfami PF00782. DSPc. 1 hit.
    PF14671. DSPn. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52799. SSF52799. 2 hits.
    PROSITEi PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A family of putative tumor suppressors is structurally and functionally conserved in humans and yeast."
      Li L., Ernsting B.R., Wishart M.J., Lohse D.L., Dixon J.E.
      J. Biol. Chem. 272:29403-29406(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION.
    2. "Genomic structure, chromosomal location, and mutation analysis of the human CDC14A gene."
      Wong A.K.C., Chen Y., Lian L., Ha P.C., Petersen K., Laity K., Carillo A., Emerson M., Heichman K., Gupte J., Tavtigian S.V., Teng D.H.-F.
      Genomics 59:248-251(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. Hao L., Baskerville C., Charbonneau H.
      Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
      Tissue: Placenta.
    4. "Human CDC14A splice variant."
      Belyaev A.S., Kolokithas A., Monell C.R.
      Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
    5. NIEHS SNPs program
      Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-345 AND PHE-589.
    6. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
      Tissue: Brain.
    9. "Regulation of the anaphase-promoting complex by the dual specificity phosphatase human Cdc14a."
      Bembenek J., Yu H.
      J. Biol. Chem. 276:48237-48242(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEPHOSPHORYLATION OF FZR1, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-278.
    10. "Disruption of centrosome structure, chromosome segregation, and cytokinesis by misexpression of human Cdc14A phosphatase."
      Kaiser B.K., Zimmerman Z.A., Charbonneau H., Jackson P.K.
      Mol. Biol. Cell 13:2289-2300(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBSTRATE SPECIFICITY, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-251; CYS-278 AND ARG-284.
    11. "Deregulated human Cdc14A phosphatase disrupts centrosome separation and chromosome segregation."
      Mailand N., Lukas C., Kaiser B.K., Jackson P.K., Bartek J., Lukas J.
      Nat. Cell Biol. 4:317-322(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF MET-362 AND ILE-364.
    12. "Relocation of Aurora B from centromeres to the central spindle at the metaphase to anaphase transition requires MKlp2."
      Gruneberg U., Neef R., Honda R., Nigg E.A., Barr F.A.
      J. Cell Biol. 166:167-172(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KIF20A, SUBCELLULAR LOCATION.
    13. "Mitotic regulation of SIRT2 by cyclin-dependent kinase 1-dependent phosphorylation."
      North B.J., Verdin E.
      J. Biol. Chem. 282:19546-19555(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS SIRT2 PHOSPHATASE.
    14. Cited for: VARIANT [LARGE SCALE ANALYSIS] TYR-493.

    Entry informationi

    Entry nameiCC14A_HUMAN
    AccessioniPrimary (citable) accession number: Q9UNH5
    Secondary accession number(s): A6MA65
    , B1AQ14, B1AQ15, O43171, O60727, O60728, Q52LH9, Q8IXX0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 23, 2004
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 121 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3