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O60729

- CC14B_HUMAN

UniProt

O60729 - CC14B_HUMAN

Protein

Dual specificity protein phosphatase CDC14B

Gene

CDC14B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      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.3 Publications

    Catalytic activityi

    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.1 PublicationPROSITE-ProRule annotation
    [a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei314 – 3141Phosphocysteine intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

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

    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. peptidyl-tyrosine dephosphorylation Source: GOC
    5. 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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:1719. CDC14B.

    Subcellular locationi

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

    GO - Cellular componenti

    1. nuclear membrane Source: HPA
    2. nucleolus Source: UniProtKB
    3. nucleoplasm Source: UniProtKB
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26255.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 498498Dual specificity protein phosphatase CDC14BPRO_0000094878Add
    BLAST

    Proteomic databases

    PaxDbiO60729.
    PRIDEiO60729.

    PTM databases

    PhosphoSiteiO60729.

    Expressioni

    Gene expression databases

    ArrayExpressiO60729.
    BgeeiO60729.
    CleanExiHS_CDC14B.
    GenevestigatoriO60729.

    Organism-specific databases

    HPAiHPA013312.

    Interactioni

    Subunit structurei

    Interacts with FZR1/CDH1.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SIRT2Q8IXJ62EBI-970231,EBI-477232

    Protein-protein interaction databases

    BioGridi114125. 3 interactions.
    IntActiO60729. 2 interactions.
    MINTiMINT-4778030.
    STRINGi9606.ENSP00000364389.

    Structurei

    Secondary structure

    1
    498
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi44 – 463
    Beta strandi48 – 6013
    Beta strandi71 – 755
    Turni77 – 793
    Beta strandi85 – 873
    Helixi94 – 10916
    Helixi111 – 1133
    Beta strandi116 – 1227
    Helixi126 – 14318
    Helixi148 – 1558
    Turni156 – 1594
    Beta strandi168 – 1725
    Helixi179 – 19113
    Beta strandi197 – 1993
    Helixi202 – 2098
    Helixi211 – 2133
    Beta strandi216 – 2205
    Turni221 – 2233
    Beta strandi224 – 2274
    Beta strandi237 – 2393
    Helixi246 – 2549
    Beta strandi257 – 2626
    Helixi271 – 2744
    Turni275 – 2773
    Beta strandi279 – 2824
    Helixi293 – 30412
    Beta strandi307 – 3137
    Beta strandi315 – 3184
    Helixi319 – 33315
    Helixi337 – 34711
    Helixi355 – 37723

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1OHCX-ray2.50A39-386[»]
    1OHDX-ray2.60A39-386[»]
    1OHEX-ray2.20A39-386[»]
    ProteinModelPortaliO60729.
    SMRiO60729. Positions 42-379.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO60729.

    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 signalCuratedAdd
    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.
    HOGENOMiHOG000198341.
    HOVERGENiHBG050818.
    InParanoidiO60729.
    KOiK06639.
    OMAiYIPYFKN.
    OrthoDBiEOG776SPM.
    PhylomeDBiO60729.
    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 (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 2 (identifier: O60729-1) [UniParc]FASTAAdd to Basket

    Also known as: CDC14B2

    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

    MKRKSERRSS WAAAPPCSRR CSSTSPGVKK IRSSTQQDPR RRDPQDDVYL    50
    DITDRLCFAI LYSRPKSASN VHYFSIDNEL EYENFYADFG PLNLAMVYRY 100
    CCKINKKLKS ITMLRKKIVH FTGSDQRKQA NAAFLVGCYM VIYLGRTPEE 150
    AYRILIFGET SYIPFRDAAY GSCNFYITLL DCFHAVKKAM QYGFLNFNSF 200
    NLDEYEHYEK AENGDLNWII PDRFIAFCGP HSRARLESGY HQHSPETYIQ 250
    YFKNHNVTTI IRLNKRMYDA KRFTDAGFDH HDLFFADGST PTDAIVKEFL 300
    DICENAEGAI AVHCKAGLGR TGTLIACYIM KHYRMTAAET IAWVRICRPG 350
    SVIGPQQQFL VMKQTNLWLE GDYFRQKLKG QENGQHRAAF SKLLSGVDDI 400
    SINGVENQDQ QEPEPYSDDD EINGVTQGDR LRALKSRRQS KTNAIPLTVI 450
    LQSSVQSCKT SEPNISGSAG ITKRTTRSAS RKSSVKSLSI SRTKTVLR 498
    Length:498
    Mass (Da):56,802
    Last modified:August 1, 1998 - v1
    Checksum:iCEE15EC4DC3B1DC7
    GO
    Isoform 1 (identifier: O60729-2) [UniParc]FASTAAdd to Basket

    Also known as: CDC14B1

    The sequence of this isoform differs from the canonical sequence as follows:
         449-487: Missing.

    Show »
    Length:459
    Mass (Da):52,752
    Checksum:i7E5057E7677B2E61
    GO
    Isoform 3 (identifier: O60729-3) [UniParc]FASTAAdd to Basket

    Also known as: CDC14B3

    The sequence of this isoform differs from the canonical sequence as follows:
         449-498: VILQSSVQSCKTSEPNISGSAGITKRTTRSASRKSSVKSLSISRTKTVLR → DGWLSQAVTFLDRLLIWLGIHKD

    Show »
    Length:471
    Mass (Da):54,176
    Checksum:i7E55AF3DF2B39475
    GO
    Isoform 4 (identifier: O60729-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         449-498: VILQSSVQSC...SISRTKTVLR → CPLAVLTSAL...LFCLDGFRTQ

    Show »
    Length:485
    Mass (Da):55,665
    Checksum:i72641340642F981F
    GO
    Isoform 5 (identifier: O60729-5) [UniParc]FASTAAdd to Basket

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

    Note: No experimental confirmation available.

    Show »
    Length:461
    Mass (Da):52,311
    Checksum:i94244A208280B2CB
    GO

    Sequence cautioni

    The sequence CAI40539.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti302 – 3021I → T.1 Publication
    Corresponds to variant rs16911114 [ dbSNP | Ensembl ].
    VAR_019959
    Natural varianti341 – 3411I → T.1 Publication
    Corresponds to variant rs16911075 [ dbSNP | Ensembl ].
    VAR_019960

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5353MKRKS…YLDIT → MSREGAGAALVAEVIK in isoform 5. 1 PublicationVSP_043576Add
    BLAST
    Alternative sequencei449 – 49850VILQS…KTVLR → DGWLSQAVTFLDRLLIWLGI HKD in isoform 3. 1 PublicationVSP_012039Add
    BLAST
    Alternative sequencei449 – 49850VILQS…KTVLR → CPLAVLTSALCSVVIWWIVC DYILPILLFCLDGFRTQ in isoform 4. 1 PublicationVSP_030720Add
    BLAST
    Alternative sequencei449 – 48739Missing in isoform 1. 1 PublicationVSP_012038Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF023158 mRNA. Translation: AAB88293.1.
    AF064104 mRNA. Translation: AAC16661.1.
    AF064105 mRNA. Translation: AAC16662.2.
    AK126388 mRNA. Translation: BAG54321.1.
    EF611343 mRNA. Translation: ABR12627.1.
    AY675321 Genomic DNA. Translation: AAT70726.1.
    AL133477, AL353578 Genomic DNA. Translation: CAI39616.1.
    AL133477, AL353578 Genomic DNA. Translation: CAI39617.1.
    AL133477, AL353578 Genomic DNA. Translation: CAI39619.1.
    AL353578, AL133477 Genomic DNA. Translation: CAI40536.1.
    AL353578, AL133477 Genomic DNA. Translation: CAI40537.1.
    AL353578 Genomic DNA. Translation: CAI40539.1. Different initiation.
    CH471174 Genomic DNA. Translation: EAW92658.1.
    CH471174 Genomic DNA. Translation: EAW92659.1.
    CCDSiCCDS43853.1. [O60729-5]
    CCDS6721.1. [O60729-2]
    CCDS6722.1. [O60729-1]
    RefSeqiNP_001070649.1. NM_001077181.1. [O60729-5]
    NP_003662.1. NM_003671.3. [O60729-2]
    NP_201588.1. NM_033331.2. [O60729-1]
    XP_005252343.1. XM_005252286.1. [O60729-4]
    XP_005252344.1. XM_005252287.1. [O60729-4]
    UniGeneiHs.40582.

    Genome annotation databases

    EnsembliENST00000375240; ENSP00000364388; ENSG00000081377. [O60729-2]
    ENST00000375241; ENSP00000364389; ENSG00000081377. [O60729-1]
    ENST00000375242; ENSP00000364390; ENSG00000081377. [O60729-5]
    ENST00000463569; ENSP00000420572; ENSG00000081377. [O60729-4]
    ENST00000474602; ENSP00000417897; ENSG00000081377. [O60729-3]
    GeneIDi8555.
    KEGGihsa:8555.
    UCSCiuc004awi.3. human. [O60729-5]
    uc004awj.3. human. [O60729-1]
    uc004awk.3. human. [O60729-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF023158 mRNA. Translation: AAB88293.1 .
    AF064104 mRNA. Translation: AAC16661.1 .
    AF064105 mRNA. Translation: AAC16662.2 .
    AK126388 mRNA. Translation: BAG54321.1 .
    EF611343 mRNA. Translation: ABR12627.1 .
    AY675321 Genomic DNA. Translation: AAT70726.1 .
    AL133477 , AL353578 Genomic DNA. Translation: CAI39616.1 .
    AL133477 , AL353578 Genomic DNA. Translation: CAI39617.1 .
    AL133477 , AL353578 Genomic DNA. Translation: CAI39619.1 .
    AL353578 , AL133477 Genomic DNA. Translation: CAI40536.1 .
    AL353578 , AL133477 Genomic DNA. Translation: CAI40537.1 .
    AL353578 Genomic DNA. Translation: CAI40539.1 . Different initiation.
    CH471174 Genomic DNA. Translation: EAW92658.1 .
    CH471174 Genomic DNA. Translation: EAW92659.1 .
    CCDSi CCDS43853.1. [O60729-5 ]
    CCDS6721.1. [O60729-2 ]
    CCDS6722.1. [O60729-1 ]
    RefSeqi NP_001070649.1. NM_001077181.1. [O60729-5 ]
    NP_003662.1. NM_003671.3. [O60729-2 ]
    NP_201588.1. NM_033331.2. [O60729-1 ]
    XP_005252343.1. XM_005252286.1. [O60729-4 ]
    XP_005252344.1. XM_005252287.1. [O60729-4 ]
    UniGenei Hs.40582.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1OHC X-ray 2.50 A 39-386 [» ]
    1OHD X-ray 2.60 A 39-386 [» ]
    1OHE X-ray 2.20 A 39-386 [» ]
    ProteinModelPortali O60729.
    SMRi O60729. Positions 42-379.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114125. 3 interactions.
    IntActi O60729. 2 interactions.
    MINTi MINT-4778030.
    STRINGi 9606.ENSP00000364389.

    PTM databases

    PhosphoSitei O60729.

    Proteomic databases

    PaxDbi O60729.
    PRIDEi O60729.

    Protocols and materials databases

    DNASUi 8555.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375240 ; ENSP00000364388 ; ENSG00000081377 . [O60729-2 ]
    ENST00000375241 ; ENSP00000364389 ; ENSG00000081377 . [O60729-1 ]
    ENST00000375242 ; ENSP00000364390 ; ENSG00000081377 . [O60729-5 ]
    ENST00000463569 ; ENSP00000420572 ; ENSG00000081377 . [O60729-4 ]
    ENST00000474602 ; ENSP00000417897 ; ENSG00000081377 . [O60729-3 ]
    GeneIDi 8555.
    KEGGi hsa:8555.
    UCSCi uc004awi.3. human. [O60729-5 ]
    uc004awj.3. human. [O60729-1 ]
    uc004awk.3. human. [O60729-2 ]

    Organism-specific databases

    CTDi 8555.
    GeneCardsi GC09M099252.
    HGNCi HGNC:1719. CDC14B.
    HPAi HPA013312.
    MIMi 603505. gene.
    neXtProti NX_O60729.
    PharmGKBi PA26255.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2453.
    HOGENOMi HOG000198341.
    HOVERGENi HBG050818.
    InParanoidi O60729.
    KOi K06639.
    OMAi YIPYFKN.
    OrthoDBi EOG776SPM.
    PhylomeDBi O60729.
    TreeFami TF101053.

    Miscellaneous databases

    EvolutionaryTracei O60729.
    GeneWikii CDC14B.
    GenomeRNAii 8555.
    NextBioi 32057.
    PROi O60729.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60729.
    Bgeei O60729.
    CleanExi HS_CDC14B.
    Genevestigatori O60729.

    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. "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. 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.
    3. Hao L., Baskerville C., Charbonneau H.
      Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION (ISOFORM 3).
    4. "Subcellular adaptation of a hominoid cell cycle protein expressed in the brain."
      Rosso L., Marques A.C., Kaessmann H.
      Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
      Tissue: Uterus.
    6. NIEHS SNPs program
      Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-302 AND THR-341.
    7. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
    10. "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: SUBCELLULAR LOCATION.
    11. "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.
    12. "The Cdc14B-Cdh1-Plk1 axis controls the G2 DNA-damage-response checkpoint."
      Bassermann F., Frescas D., Guardavaccaro D., Busino L., Peschiaroli A., Pagano M.
      Cell 134:256-267(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FZR1.
    13. "The structure of the cell cycle protein Cdc14 reveals a proline-directed protein phosphatase."
      Gray C.H., Good V.M., Tonks N.K., Barford D.
      EMBO J. 22:3524-3535(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 39-386.

    Entry informationi

    Entry nameiCC14B_HUMAN
    AccessioniPrimary (citable) accession number: O60729
    Secondary accession number(s): A6N5X8
    , A8MQ20, B1AL31, B1AL32, O43183, O60730, Q5JU08
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 23, 2004
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 120 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3