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Q6PFY9

- CC14B_MOUSE

UniProt

Q6PFY9 - CC14B_MOUSE

Protein

Dual specificity protein phosphatase CDC14B

Gene

Cdc14b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Dual-specificity phosphatase involved in DNA damage response. Essential regulator of the G2 DNA damage checkpoint: following DNA damage, translocates to the nucleus and dephosphorylates FZR1/CDH1, a key activator of the anaphase promoting complex/cyclosome (APC/C). Dephosphorylates SIRT2 around early anaphase. Dephosphorylation of FZR1/CDH1 activates the APC/C, leading to the ubiquitination of PLK1, preventing entry into mitosis. Preferentially dephosphorylates proteins modified by proline-directed kinases By similarity.By similarity

    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 sitei314 – 3141Phosphocysteine intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. activation of anaphase-promoting complex activity Source: UniProtKB
    2. DNA repair Source: UniProtKB-KW
    3. G2 DNA damage checkpoint Source: UniProtKB
    4. protein dephosphorylation Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    DNA damage, DNA repair

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity protein phosphatase CDC14B (EC:3.1.3.16, EC:3.1.3.48)
    Alternative name(s):
    CDC14 cell division cycle 14 homolog B
    Gene namesi
    Name:Cdc14b
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:2441808. Cdc14b.

    Subcellular locationi

    Nucleusnucleolus By similarity. Nucleusnucleoplasm By similarity
    Note: Following DNA damage, translocates from the nucleolus to the nucleoplasm and interacts with FZR1/CDH1.By similarity

    GO - Cellular componenti

    1. nuclear membrane Source: Ensembl
    2. nucleolus Source: UniProtKB-SubCell
    3. nucleoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 485485Dual specificity protein phosphatase CDC14BPRO_0000094879Add
    BLAST

    Proteomic databases

    PRIDEiQ6PFY9.

    PTM databases

    PhosphoSiteiQ6PFY9.

    Expressioni

    Gene expression databases

    BgeeiQ6PFY9.
    GenevestigatoriQ6PFY9.

    Interactioni

    Subunit structurei

    Interacts with FZR1/CDH1.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ6PFY9.
    SMRiQ6PFY9. Positions 43-379.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni44 – 198155AAdd
    BLAST
    Regioni199 – 21214LinkerAdd
    BLAST
    Regioni213 – 379167BAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1 – 5454Nucleolar localization signalBy similarityAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG2453.
    GeneTreeiENSGT00390000010254.
    HOGENOMiHOG000198341.
    HOVERGENiHBG050818.
    InParanoidiQ6PFY9.
    KOiK06639.
    OMAiYIPYFKN.
    OrthoDBiEOG776SPM.
    PhylomeDBiQ6PFY9.
    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.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    [Graphical view]
    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 (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q6PFY9-1) [UniParc]FASTAAdd to Basket

    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

    MKRKSERRSA WATAPPCSRR SSSSSPGVKK SRSSTPQELH RLEQQDDLYL    50
    DITDRLCFAI LYSRPKSATN EHYFSIDNEL EYENFYADFG PLNLAMVYRY 100
    CCKINKKLKS ITMLRKKIIH FTGTDQRKQA NAAFLVGCYM VIYLGRTPED 150
    AYRTLIFGDT AYIPFRDAAY GSCSFYITLL DCFHAVKKAM QYGFFNFNSF 200
    NLDEYEHYEK AENGDFNWII PERFLAFCGP HSRSRLESGY HQHSPETYIP 250
    YFKNHNVTTI IRLNKRMYDA KRFTDAGFDH HDLFFPDGST PAESIVQEFL 300
    DICENVKGAI AVHCKAGLGR TGTLIGCYLM KHYRMTAAES IAWLRICRPG 350
    SVIGPQQQFL VMKQSSLWLE GDYFRQKLRG QENGPLREAF SKHLSDADDL 400
    SLNGLENQDN QEPEPYSDDD EVSGMTQGDR LRALKSRRQP KASAIPLTCP 450
    LAVLTSALCS VAIWWIVCDY ILPTLLFCLD GFRTQ 485
    Length:485
    Mass (Da):55,661
    Last modified:July 5, 2004 - v1
    Checksum:i8963E14648FC89DA
    GO
    Isoform 2 (identifier: Q6PFY9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-53: MKRKSERRSAWATAPPCSRRSSSSSPGVKKSRSSTPQELHRLEQQDDLYLDIT → MRREGAGTPLMAEVIR

    Show »
    Length:448
    Mass (Da):51,402
    Checksum:iC18E8112A217EBE6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti136 – 1361V → I in AAH49794. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5353MKRKS…YLDIT → MRREGAGTPLMAEVIR in isoform 2. 1 PublicationVSP_012325Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK041155 mRNA. Translation: BAC30842.1.
    BC049794 mRNA. Translation: AAH49794.1.
    BC057357 mRNA. Translation: AAH57357.1.
    CCDSiCCDS26598.1. [Q6PFY9-1]
    CCDS49292.1. [Q6PFY9-2]
    RefSeqiNP_001116461.1. NM_001122989.1. [Q6PFY9-2]
    NP_766175.3. NM_172587.3. [Q6PFY9-1]
    XP_006517287.1. XM_006517224.1. [Q6PFY9-1]
    UniGeneiMm.25335.

    Genome annotation databases

    EnsembliENSMUST00000039318; ENSMUSP00000046003; ENSMUSG00000033102. [Q6PFY9-1]
    ENSMUST00000109769; ENSMUSP00000105391; ENSMUSG00000033102. [Q6PFY9-2]
    ENSMUST00000109770; ENSMUSP00000105392; ENSMUSG00000033102. [Q6PFY9-1]
    GeneIDi218294.
    KEGGimmu:218294.
    UCSCiuc007qym.2. mouse. [Q6PFY9-1]
    uc007qyo.2. mouse. [Q6PFY9-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK041155 mRNA. Translation: BAC30842.1 .
    BC049794 mRNA. Translation: AAH49794.1 .
    BC057357 mRNA. Translation: AAH57357.1 .
    CCDSi CCDS26598.1. [Q6PFY9-1 ]
    CCDS49292.1. [Q6PFY9-2 ]
    RefSeqi NP_001116461.1. NM_001122989.1. [Q6PFY9-2 ]
    NP_766175.3. NM_172587.3. [Q6PFY9-1 ]
    XP_006517287.1. XM_006517224.1. [Q6PFY9-1 ]
    UniGenei Mm.25335.

    3D structure databases

    ProteinModelPortali Q6PFY9.
    SMRi Q6PFY9. Positions 43-379.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q6PFY9.

    Proteomic databases

    PRIDEi Q6PFY9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000039318 ; ENSMUSP00000046003 ; ENSMUSG00000033102 . [Q6PFY9-1 ]
    ENSMUST00000109769 ; ENSMUSP00000105391 ; ENSMUSG00000033102 . [Q6PFY9-2 ]
    ENSMUST00000109770 ; ENSMUSP00000105392 ; ENSMUSG00000033102 . [Q6PFY9-1 ]
    GeneIDi 218294.
    KEGGi mmu:218294.
    UCSCi uc007qym.2. mouse. [Q6PFY9-1 ]
    uc007qyo.2. mouse. [Q6PFY9-2 ]

    Organism-specific databases

    CTDi 8555.
    MGIi MGI:2441808. Cdc14b.

    Phylogenomic databases

    eggNOGi COG2453.
    GeneTreei ENSGT00390000010254.
    HOGENOMi HOG000198341.
    HOVERGENi HBG050818.
    InParanoidi Q6PFY9.
    KOi K06639.
    OMAi YIPYFKN.
    OrthoDBi EOG776SPM.
    PhylomeDBi Q6PFY9.
    TreeFami TF101053.

    Miscellaneous databases

    NextBioi 376235.
    PROi Q6PFY9.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q6PFY9.
    Genevestigatori Q6PFY9.

    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.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    [Graphical view ]
    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. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Strain: C57BL/6J.
      Tissue: Aorta and Vein.
    2. "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] (ISOFORM 1).
      Strain: C57BL/6.
      Tissue: Brain and Limb.

    Entry informationi

    Entry nameiCC14B_MOUSE
    AccessioniPrimary (citable) accession number: Q6PFY9
    Secondary accession number(s): Q80WC4, Q8BLV5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 23, 2004
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 94 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3