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{{Infobox_gene}}
{{PBB_Controls
'''Dual specificity protein phosphatase CDC14B''' is an [[enzyme]] that in humans is encoded by the ''CDC14B'' [[gene]].<ref name="pmid9367992">{{cite journal | vauthors = Li L, Ernsting BR, Wishart MJ, Lohse DL, Dixon JE | title = A family of putative tumor suppressors is structurally and functionally conserved in humans and yeast | journal = J Biol Chem | volume = 272 | issue = 47 | pages = 29403–29406 |date=December 1997 | pmid = 9367992 | pmc =  | doi =10.1074/jbc.272.47.29403  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: CDC14B CDC14 cell division cycle 14 homolog B (S. cerevisiae)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8555| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CDC14B_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ohc.
| PDB = {{PDB2|1ohc}}, {{PDB2|1ohd}}, {{PDB2|1ohe}}
| Name = CDC14 cell division cycle 14 homolog B (S. cerevisiae)
| HGNCid = 1719
| Symbol = CDC14B
| AltSymbols =; CDC14B3; Cdc14B1; Cdc14B2; hCDC14B
| OMIM = 603505
| ECnumber =
| Homologene = 75343
| MGIid = 2441808
  | Function = {{GNF_GO|id=GO:0004722 |text = protein serine/threonine phosphatase activity}} {{GNF_GO|id=GO:0004725 |text = protein tyrosine phosphatase activity}} {{GNF_GO|id=GO:0008138 |text = protein tyrosine/serine/threonine phosphatase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006470 |text = protein amino acid dephosphorylation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 8555
    | Hs_Ensembl = 
    | Hs_RefseqProtein = NP_001070649
    | Hs_RefseqmRNA = NM_001077181
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 
    | Hs_GenLoc_start = 
    | Hs_GenLoc_end = 
    | Hs_Uniprot = 
    | Mm_EntrezGene = 218294
    | Mm_Ensembl = ENSMUSG00000033102
    | Mm_RefseqmRNA = NM_172587
    | Mm_RefseqProtein = NP_766175
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 13
    | Mm_GenLoc_start = 64204535
    | Mm_GenLoc_end = 64284140
    | Mm_Uniprot = Q6PFY9
  }}
}}
'''CDC14 cell division cycle 14 homolog B (S. cerevisiae)''', also known as '''CDC14B''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CDC14B CDC14 cell division cycle 14 homolog B (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8555| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = The protein encoded by this gene is a member of the dual specificity protein tyrosine phosphatase family. This protein is highly similar to Saccharomyces cerevisiae Cdc14, a protein tyrosine phosphatase involved in the exit of cell mitosis and initiation of DNA replication, which suggests the role in cell cycle control. This protein has been shown to interact with and dephosphorylates tumor suppressor protein p53, and is thought to regulate the function of p53. Alternative splice of this gene results in 3 transcript variants encoding distinct isoforms.<ref name="entrez">{{cite web | title = Entrez Gene: CDC14B CDC14 cell division cycle 14 homolog B (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8555| accessdate = }}</ref>
| summary_text = The protein encoded by this gene is a member of the dual specificity protein tyrosine phosphatase family. This protein is highly similar to Saccharomyces cerevisiae Cdc14, a protein tyrosine phosphatase involved in the exit of cell mitosis and initiation of DNA replication, which suggests the role in cell cycle control. Specifically, it is thought to fulfil this role by bundling and stabilising microtubules. This protein has been shown to interact with and dephosphorylates tumor suppressor protein p53, and is thought to regulate the function of p53. Alternative splicing of this gene results in 3 transcript variants encoding distinct isoforms.<ref name="entrez" />
}}
}}
==Interactions==
CDC14B has been shown to [[Protein-protein interaction|interact]] with [[p53]].<ref name=pmid10644693>{{cite journal |last=Li |first=L |author2=Ljungman M|author3=Dixon J E |date=January 2000  |title=The human Cdc14 phosphatases interact with and dephosphorylate the tumor suppressor protein p53 |journal=J. Biol. Chem. |volume=275 |issue=4 |pages=2410–2414 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 10644693 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1074/jbc.275.4.2410 }}</ref> However, this interaction has not been reported in other studies.


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|CDC14B}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal  | vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides |journal=Gene |volume=138 |issue= 1–2 |pages= 171–174 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
*{{cite journal  | author=Li L, Ernsting BR, Wishart MJ, ''et al.'' |title=A family of putative tumor suppressors is structurally and functionally conserved in humans and yeast. |journal=J. Biol. Chem. |volume=272 |issue= 47 |pages= 29403-6 |year= 1997 |pmid= 9367992 |doi= }}
*{{cite journal  | author=Suzuki Y |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library |journal=Gene |volume=200 |issue= 1–2 |pages= 149–156 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3  |name-list-format=vanc| author2=Yoshitomo-Nakagawa K  | author3=Maruyama K  | display-authors=3  | last4=Suyama  | first4=A  | last5=Sugano  | first5=S }}
*{{cite journal  | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi=  }}
*{{cite journal  | vauthors=Li L, Ljungman M, Dixon JE |title=The human Cdc14 phosphatases interact with and dephosphorylate the tumor suppressor protein p53 |journal=J. Biol. Chem. |volume=275 |issue= 4 |pages= 2410–2414 |year= 2000 |pmid= 10644693 |doi=10.1074/jbc.275.4.2410 }}
*{{cite journal  | author=Li L, Ljungman M, Dixon JE |title=The human Cdc14 phosphatases interact with and dephosphorylate the tumor suppressor protein p53. |journal=J. Biol. Chem. |volume=275 |issue= 4 |pages= 2410-4 |year= 2000 |pmid= 10644693 |doi=  }}
*{{cite journal  | author=Mailand N |title=Deregulated human Cdc14A phosphatase disrupts centrosome separation and chromosome segregation |journal=Nat. Cell Biol. |volume=4 |issue= 4 |pages= 318–322 |year= 2002 |pmid= 11901424 |doi= 10.1038/ncb777 |name-list-format=vanc| author2=Lukas C  | author3=Kaiser BK  | display-authors=3  | last4=Jackson  | first4=Peter K.  | last5=Bartek  | first5=Jiri  | last6=Lukas  | first6=Jiri }}
*{{cite journal  | author=Mailand N, Lukas C, Kaiser BK, ''et al.'' |title=Deregulated human Cdc14A phosphatase disrupts centrosome separation and chromosome segregation. |journal=Nat. Cell Biol. |volume=4 |issue= 4 |pages= 317-22 |year= 2002 |pmid= 11901424 |doi= 10.1038/ncb777 }}
*{{cite journal  | vauthors=Kaiser BK, Zimmerman ZA, Charbonneau H, Jackson PK |title=Disruption of centrosome structure, chromosome segregation, and cytokinesis by misexpression of human Cdc14A phosphatase |journal=Mol. Biol. Cell |volume=13 |issue= 7 |pages= 2289–2300 |year= 2003 |pmid= 12134069 |doi= 10.1091/mbc.01-11-0535 | pmc=117313 }}
*{{cite journal  | author=Kaiser BK, Zimmerman ZA, Charbonneau H, Jackson PK |title=Disruption of centrosome structure, chromosome segregation, and cytokinesis by misexpression of human Cdc14A phosphatase. |journal=Mol. Biol. Cell |volume=13 |issue= 7 |pages= 2289-300 |year= 2003 |pmid= 12134069 |doi= 10.1091/mbc.01-11-0535 }}
*{{cite journal  | author=Strausberg RL |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–16903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241  |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD |bibcode=2002PNAS...9916899M}}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Dryden SC |title=Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle |journal=Mol. Cell. Biol. |volume=23 |issue= 9 |pages= 3173–3185 |year= 2003 |pmid= 12697818 |doi=10.1128/MCB.23.9.3173-3185.2003  | pmc=153197  |name-list-format=vanc| author2=Nahhas FA  | author3=Nowak JE  | display-authors=3  | last4=Goustin  | first4=A.-S.  | last5=Tainsky  | first5=M. A. }}
*{{cite journal  | author=Dryden SC, Nahhas FA, Nowak JE, ''et al.'' |title=Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle. |journal=Mol. Cell. Biol. |volume=23 |issue= 9 |pages= 3173-85 |year= 2003 |pmid= 12697818 |doi=  }}
*{{cite journal  | vauthors=Gray CH, Good VM, Tonks NK, Barford D |title=The structure of the cell cycle protein Cdc14 reveals a proline-directed protein phosphatase |journal=EMBO J. |volume=22 |issue= 14 |pages= 3524–3535 |year= 2003 |pmid= 12853468 |doi= 10.1093/emboj/cdg348 | pmc=165618 }}
*{{cite journal  | author=Gray CH, Good VM, Tonks NK, Barford D |title=The structure of the cell cycle protein Cdc14 reveals a proline-directed protein phosphatase. |journal=EMBO J. |volume=22 |issue= 14 |pages= 3524-35 |year= 2003 |pmid= 12853468 |doi= 10.1093/emboj/cdg348 }}
*{{cite journal  | vauthors=Nalepa G, Harper JW |title=Visualization of a highly organized intranuclear network of filaments in living mammalian cells |journal=Cell Motil. Cytoskeleton |volume=59 |issue= 2 |pages= 94–108 |year= 2005 |pmid= 15362113 |doi= 10.1002/cm.20023 }}
*{{cite journal  | author=Nalepa G, Harper JW |title=Visualization of a highly organized intranuclear network of filaments in living mammalian cells. |journal=Cell Motil. Cytoskeleton |volume=59 |issue= 2 |pages= 94-108 |year= 2005 |pmid= 15362113 |doi= 10.1002/cm.20023 }}
*{{cite journal  | author=Cho HP |title=The dual-specificity phosphatase CDC14B bundles and stabilizes microtubules |journal=Mol. Cell. Biol. |volume=25 |issue= 11 |pages= 4541–4551 |year= 2005 |pmid= 15899858 |doi= 10.1128/MCB.25.11.4541-4551.2005 | pmc=1140622  |name-list-format=vanc| author2=Liu Y  | author3=Gomez M  | display-authors=3  | last4=Dunlap  | first4=J.  | last5=Tyers  | first5=M.  | last6=Wang  | first6=Y. }}
*{{cite journal  | author=Cho HP, Liu Y, Gomez M, ''et al.'' |title=The dual-specificity phosphatase CDC14B bundles and stabilizes microtubules. |journal=Mol. Cell. Biol. |volume=25 |issue= 11 |pages= 4541-51 |year= 2005 |pmid= 15899858 |doi= 10.1128/MCB.25.11.4541-4551.2005 }}
*{{cite journal  | vauthors=Vázquez-Novelle MD, Esteban V, Bueno A, Sacristán MP |title=Functional homology among human and fission yeast Cdc14 phosphatases |journal=J. Biol. Chem. |volume=280 |issue= 32 |pages= 29144–29150 |year= 2005 |pmid= 15911625 |doi= 10.1074/jbc.M413328200 }}
*{{cite journal  | author=Vázquez-Novelle MD, Esteban V, Bueno A, Sacristán MP |title=Functional homology among human and fission yeast Cdc14 phosphatases. |journal=J. Biol. Chem. |volume=280 |issue= 32 |pages= 29144-50 |year= 2005 |pmid= 15911625 |doi= 10.1074/jbc.M413328200 }}
*{{cite journal  | author=Kimura K |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes |journal=Genome Res. |volume=16 |issue= 1 |pages= 55–65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406 | pmc=1356129  |name-list-format=vanc| author2=Wakamatsu A  | author3=Suzuki Y  | display-authors=3  | last4=Ota  | first4=T  | last5=Nishikawa  | first5=T  | last6=Yamashita  | first6=R  | last7=Yamamoto  | first7=J  | last8=Sekine  | first8=M  | last9=Tsuritani  | first9=K }}
*{{cite journal  | author=Kimura K, Wakamatsu A, Suzuki Y, ''et al.'' |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. |journal=Genome Res. |volume=16 |issue= 1 |pages= 55-65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406 }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=8555}}
{{Protein tyrosine phosphatases}}
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Latest revision as of 07:44, 10 January 2019

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Dual specificity protein phosphatase CDC14B is an enzyme that in humans is encoded by the CDC14B gene.[1][2]

The protein encoded by this gene is a member of the dual specificity protein tyrosine phosphatase family. This protein is highly similar to Saccharomyces cerevisiae Cdc14, a protein tyrosine phosphatase involved in the exit of cell mitosis and initiation of DNA replication, which suggests the role in cell cycle control. Specifically, it is thought to fulfil this role by bundling and stabilising microtubules. This protein has been shown to interact with and dephosphorylates tumor suppressor protein p53, and is thought to regulate the function of p53. Alternative splicing of this gene results in 3 transcript variants encoding distinct isoforms.[2]

Interactions

CDC14B has been shown to interact with p53.[3] However, this interaction has not been reported in other studies.

References

  1. Li L, Ernsting BR, Wishart MJ, Lohse DL, Dixon JE (December 1997). "A family of putative tumor suppressors is structurally and functionally conserved in humans and yeast". J Biol Chem. 272 (47): 29403–29406. doi:10.1074/jbc.272.47.29403. PMID 9367992.
  2. 2.0 2.1 "Entrez Gene: CDC14B CDC14 cell division cycle 14 homolog B (S. cerevisiae)".
  3. Li, L; Ljungman M; Dixon J E (January 2000). "The human Cdc14 phosphatases interact with and dephosphorylate the tumor suppressor protein p53". J. Biol. Chem. UNITED STATES. 275 (4): 2410–2414. doi:10.1074/jbc.275.4.2410. ISSN 0021-9258. PMID 10644693.

External links

Further reading