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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Tankyrase-1''' is an [[enzyme]] that in humans is encoded by the ''TNKS'' [[gene]].<ref name="pmid9822378">{{cite journal | vauthors = Smith S, Giriat I, Schmitt A, de Lange T | title = Tankyrase, a poly(ADP-ribose) polymerase at human telomeres | journal = Science | volume = 282 | issue = 5393 | pages = 1484–7 | date = Dec 1998 | pmid = 9822378 | pmc =  | doi = 10.1126/science.282.5393.1484 }}</ref><ref name="pmid10198177">{{cite journal | vauthors = Zhu L, Smith S, de Lange T, Seldin MF | title = Chromosomal mapping of the tankyrase gene in human and mouse | journal = Genomics | volume = 57 | issue = 2 | pages = 320–1 | date = May 1999 | pmid = 10198177 | pmc = | doi = 10.1006/geno.1999.5771 }}</ref><ref name="entrez">{{Cite web| title = Entrez Gene: TNKS tankyrase, TRF1-interacting ankyrin-related ADP-ribose polymerase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8658| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
==Description<ref>https://www.uniprot.org/uniprot/O95271</ref>==
{{GNF_Protein_box
Tankyrase-1 is a poly-ADP-ribosyltransferase involved in various processes such as Wnt signaling pathway, telomere length and vesicle trafficking. Acts as an activator of the Wnt signaling pathway by mediating poly-[[ADP-ribosylation]] (PARsylation) of [[AXIN1]] and [[AXIN2]], 2 key components of the beta-catenin destruction complex: poly-ADP-ribosylated target proteins are recognized by [[RNF146]], which mediates their ubiquitination and subsequent degradation. Also mediates PARsylation of [[BLZF1]] and [[CASC3]], followed by recruitment of [[RNF146]] and subsequent ubiquitination. Mediates PARsylation of [[TERF1]], thereby contributing to the regulation of telomere length. Involved in centrosome maturation during prometaphase by mediating PARsylation of [[HEPACAM]]2/MIKI. May also regulate vesicle trafficking and modulate the subcellular distribution of [[SLC2A4]]/GLUT4-vesicles. May be involved in spindle pole assembly through PARsylation of [[NUMA1]]. Stimulates 26S proteasome activity.<ref>{{cite journal | pmid = 10872471 | doi=10.1146/annurev.biochem.68.1.1015 | volume=68 | title=The 26S proteasome: a molecular machine designed for controlled proteolysis | year=1999 | journal=Annu. Rev. Biochem. | pages=1015–68 | vauthors=Voges D, Zwickl P, Baumeister W}}</ref>
| image =
| image_source =
| PDB =
| Name = Tankyrase, TRF1-interacting ankyrin-related ADP-ribose polymerase
| HGNCid = 11941
| Symbol = TNKS
| AltSymbols =; PARPL; PARP-5a; PARP5A; TIN1; TINF1; TNKS1
| OMIM = 603303
| ECnumber = 
| Homologene = 18405
| MGIid = 1341087
| GeneAtlas_image1 = PBB_GE_TNKS_202561_at_tn.png
| GeneAtlas_image2 = PBB_GE_TNKS_216695_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003950 |text = NAD+ ADP-ribosyltransferase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016757 |text = transferase activity, transferring glycosyl groups}}
| Component = {{GNF_GO|id=GO:0000781 |text = chromosome, telomeric region}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005694 |text = chromosome}}
| Process = {{GNF_GO|id=GO:0006471 |text = protein amino acid ADP-ribosylation}} {{GNF_GO|id=GO:0007004 |text = telomere maintenance via telomerase}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 8658
    | Hs_Ensembl = ENSG00000173273
    | Hs_RefseqProtein = NP_003738
    | Hs_RefseqmRNA = NM_003747
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 8
    | Hs_GenLoc_start = 9450832
    | Hs_GenLoc_end = 9677266
    | Hs_Uniprot = O95271
    | Mm_EntrezGene = 21951
    | Mm_Ensembl = ENSMUSG00000031529
    | Mm_RefseqmRNA = NM_175091
    | Mm_RefseqProtein = NP_780300
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 8
    | Mm_GenLoc_start = 36297696
    | Mm_GenLoc_end = 36434207
    | Mm_Uniprot = 
  }}
}}
'''Tankyrase, TRF1-interacting ankyrin-related ADP-ribose polymerase''', also known as '''TNKS''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TNKS tankyrase, TRF1-interacting ankyrin-related ADP-ribose polymerase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8658| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Protein interactions ==
{{PBB_Summary
TNKS has been shown to [[Protein-protein interaction|interact]] with:
| section_title =  
{{div col|colwidth=20em}}
| summary_text =  
* [[FNBP1]],<ref name = pmid14596906>{{cite journal | vauthors = Fuchs U, Rehkamp GF, Slany R, Follo M, Borkhardt A | title = The formin-binding protein 17, FBP17, binds via a TNKS binding motif to tankyrase, a protein involved in telomere maintenance | journal = FEBS Lett. | volume = 554 | issue = 1–2 | pages = 10–6 | date = Nov 2003 | pmid = 14596906 | doi = 10.1016/s0014-5793(03)01063-9}}</ref>  
}}
* [[MCL1]],<ref name = pmid12475993>{{cite journal | vauthors = Bae J, Donigian JR, Hsueh AJ | title = Tankyrase 1 interacts with Mcl-1 proteins and inhibits their regulation of apoptosis | journal = J. Biol. Chem. | volume = 278 | issue = 7 | pages = 5195–204 | date = Feb 2003 | pmid = 12475993 | doi = 10.1074/jbc.M201988200 }}</ref>
* [[TERF1]],<ref name = pmid9822378 /><ref name = pmid11854288/><ref name = pmid12080061/><ref name = pmid11739745>{{cite journal | vauthors = Cook BD, Dynek JN, Chang W, Shostak G, Smith S | title = Role for the related poly(ADP-Ribose) polymerases tankyrase 1 and 2 at human telomeres | journal = Mol. Cell. Biol. | volume = 22 | issue = 1 | pages = 332–42 | date = Jan 2002 | pmid = 11739745 | pmc = 134233 | doi =  10.1128/mcb.22.1.332-342.2002}}</ref><ref name = pmid11802774>{{cite journal | vauthors = Sbodio JI, Lodish HF, Chi NW | title = Tankyrase-2 oligomerizes with tankyrase-1 and binds to both TRF1 (telomere-repeat-binding factor 1) and IRAP (insulin-responsive aminopeptidase) | journal = Biochem. J. | volume = 361 | issue = Pt 3 | pages = 451–9 | date = Feb 2002 | pmid = 11802774 | pmc = 1222327 | doi =  10.1042/0264-6021:3610451}}</ref> and
* [[TNKS1BP1]].<ref name = pmid11854288>{{cite journal | vauthors = Seimiya H, Smith S | title = The telomeric poly(ADP-ribose) polymerase, tankyrase 1, contains multiple binding sites for telomeric repeat binding factor 1 (TRF1) and a novel acceptor, 182-kDa tankyrase-binding protein (TAB182) | journal = J. Biol. Chem. | volume = 277 | issue = 16 | pages = 14116–26 | date = Apr 2002 | pmid = 11854288 | doi = 10.1074/jbc.M112266200 }}</ref><ref name = pmid12080061>{{cite journal | vauthors = Sbodio JI, Chi NW | title = Identification of a tankyrase-binding motif shared by IRAP, TAB182, and human TRF1 but not mouse TRF1. NuMA contains this RXXPDG motif and is a novel tankyrase partner | journal = J. Biol. Chem. | volume = 277 | issue = 35 | pages = 31887–92 | date = Aug 2002 | pmid = 12080061 | doi = 10.1074/jbc.M203916200 }}</ref>
{{Div col end}}


==References==
== References ==
{{reflist|2}}
{{Reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal  | author=Andersson B, Wentland MA, Ricafrente JY, ''et al.'' |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107-13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 }}
*{{cite journal  | author=Yu W, Andersson B, Worley KC, ''et al.'' |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353-8 |year= 1997 |pmid= 9110174 |doi=  }}
*{{cite journal  | author=Smith S, Giriat I, Schmitt A, de Lange T |title=Tankyrase, a poly(ADP-ribose) polymerase at human telomeres. |journal=Science |volume=282 |issue= 5393 |pages= 1484-7 |year= 1998 |pmid= 9822378 |doi=  }}
*{{cite journal  | author=Zhu L, Smith S, de Lange T, Seldin MF |title=Chromosomal mapping of the tankyrase gene in human and mouse. |journal=Genomics |volume=57 |issue= 2 |pages= 320-1 |year= 1999 |pmid= 10198177 |doi= 10.1006/geno.1999.5771 }}
*{{cite journal  | author=Smith S, de Lange T |title=Cell cycle dependent localization of the telomeric PARP, tankyrase, to nuclear pore complexes and centrosomes. |journal=J. Cell. Sci. |volume=112 ( Pt 21) |issue=  |pages= 3649-56 |year= 1999 |pmid= 10523501 |doi=  }}
*{{cite journal  | author=Chi NW, Lodish HF |title=Tankyrase is a golgi-associated mitogen-activated protein kinase substrate that interacts with IRAP in GLUT4 vesicles. |journal=J. Biol. Chem. |volume=275 |issue= 49 |pages= 38437-44 |year= 2001 |pmid= 10988299 |doi= 10.1074/jbc.M007635200 }}
*{{cite journal  | author=Lyons RJ, Deane R, Lynch DK, ''et al.'' |title=Identification of a novel human tankyrase through its interaction with the adaptor protein Grb14. |journal=J. Biol. Chem. |volume=276 |issue= 20 |pages= 17172-80 |year= 2001 |pmid= 11278563 |doi= 10.1074/jbc.M009756200 }}
*{{cite journal  | author=Kim BY, Krämer H, Yamamoto A, ''et al.'' |title=Molecular characterization of mammalian homologues of class C Vps proteins that interact with syntaxin-7. |journal=J. Biol. Chem. |volume=276 |issue= 31 |pages= 29393-402 |year= 2001 |pmid= 11382755 |doi= 10.1074/jbc.M101778200 }}
*{{cite journal  | author=Cook BD, Dynek JN, Chang W, ''et al.'' |title=Role for the related poly(ADP-Ribose) polymerases tankyrase 1 and 2 at human telomeres. |journal=Mol. Cell. Biol. |volume=22 |issue= 1 |pages= 332-42 |year= 2002 |pmid= 11739745 |doi=  }}
*{{cite journal  | author=Sbodio JI, Lodish HF, Chi NW |title=Tankyrase-2 oligomerizes with tankyrase-1 and binds to both TRF1 (telomere-repeat-binding factor 1) and IRAP (insulin-responsive aminopeptidase). |journal=Biochem. J. |volume=361 |issue= Pt 3 |pages= 451-9 |year= 2002 |pmid= 11802774 |doi=  }}
*{{cite journal  | author=Seimiya H, Smith S |title=The telomeric poly(ADP-ribose) polymerase, tankyrase 1, contains multiple binding sites for telomeric repeat binding factor 1 (TRF1) and a novel acceptor, 182-kDa tankyrase-binding protein (TAB182). |journal=J. Biol. Chem. |volume=277 |issue= 16 |pages= 14116-26 |year= 2002 |pmid= 11854288 |doi= 10.1074/jbc.M112266200 }}
*{{cite journal  | author=Sbodio JI, Chi NW |title=Identification of a tankyrase-binding motif shared by IRAP, TAB182, and human TRF1 but not mouse TRF1. NuMA contains this RXXPDG motif and is a novel tankyrase partner. |journal=J. Biol. Chem. |volume=277 |issue= 35 |pages= 31887-92 |year= 2002 |pmid= 12080061 |doi= 10.1074/jbc.M203916200 }}
*{{cite journal  | author=Rippmann JF, Damm K, Schnapp A |title=Functional characterization of the poly(ADP-ribose) polymerase activity of tankyrase 1, a potential regulator of telomere length. |journal=J. Mol. Biol. |volume=323 |issue= 2 |pages= 217-24 |year= 2002 |pmid= 12381316 |doi=  }}
*{{cite journal  | author=Bae J, Donigian JR, Hsueh AJ |title=Tankyrase 1 interacts with Mcl-1 proteins and inhibits their regulation of apoptosis. |journal=J. Biol. Chem. |volume=278 |issue= 7 |pages= 5195-204 |year= 2003 |pmid= 12475993 |doi= 10.1074/jbc.M201988200 }}
*{{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=Loayza D, De Lange T |title=POT1 as a terminal transducer of TRF1 telomere length control. |journal=Nature |volume=423 |issue= 6943 |pages= 1013-8 |year= 2003 |pmid= 12768206 |doi= 10.1038/nature01688 }}
*{{cite journal  | author=Fuchs U, Rehkamp GF, Slany R, ''et al.'' |title=The formin-binding protein 17, FBP17, binds via a TNKS binding motif to tankyrase, a protein involved in telomere maintenance. |journal=FEBS Lett. |volume=554 |issue= 1-2 |pages= 10-6 |year= 2003 |pmid= 14596906 |doi=  }}
*{{cite journal  | author=Seimiya H, Muramatsu Y, Smith S, Tsuruo T |title=Functional subdomain in the ankyrin domain of tankyrase 1 required for poly(ADP-ribosyl)ation of TRF1 and telomere elongation. |journal=Mol. Cell. Biol. |volume=24 |issue= 5 |pages= 1944-55 |year= 2004 |pmid= 14966275 |doi=  }}
*{{cite journal  | author=Dynek JN, Smith S |title=Resolution of sister telomere association is required for progression through mitosis. |journal=Science |volume=304 |issue= 5667 |pages= 97-100 |year= 2004 |pmid= 15064417 |doi= 10.1126/science.1094754 }}
*{{cite journal  | author=Ye JZ, de Lange T |title=TIN2 is a tankyrase 1 PARP modulator in the TRF1 telomere length control complex. |journal=Nat. Genet. |volume=36 |issue= 6 |pages= 618-23 |year= 2004 |pmid= 15133513 |doi= 10.1038/ng1360 }}
}}
{{refend}}


{{protein-stub}}
== Further reading ==
{{WikiDoc Sources}}
{{Refbegin| 2}}
* {{cite journal | vauthors = Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA | title = A "double adaptor" method for improved shotgun library construction | journal = Anal. Biochem. | volume = 236 | issue = 1 | pages = 107–13 | year = 1996 | pmid = 8619474 | doi = 10.1006/abio.1996.0138 }}
* {{cite journal | vauthors = Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA | title = Large-scale concatenation cDNA sequencing | journal = Genome Res. | volume = 7 | issue = 4 | pages = 353–8 | year = 1997 | pmid = 9110174 | pmc = 139146 | doi = 10.1101/gr.7.4.353 }}
* {{cite journal | vauthors = Smith S, de Lange T | title = Cell cycle dependent localization of the telomeric PARP, tankyrase, to nuclear pore complexes and centrosomes | journal = J. Cell Sci. | volume = 112 | issue = 21 | pages = 3649–56 | year = 1999 | pmid = 10523501 | doi =  }}
* {{cite journal | vauthors = Chi NW, Lodish HF | title = Tankyrase is a golgi-associated mitogen-activated protein kinase substrate that interacts with IRAP in GLUT4 vesicles | journal = J. Biol. Chem. | volume = 275 | issue = 49 | pages = 38437–44 | year = 2001 | pmid = 10988299 | doi = 10.1074/jbc.M007635200 }}
* {{cite journal | vauthors = Lyons RJ, Deane R, Lynch DK, Ye ZS, Sanderson GM, Eyre HJ, Sutherland GR, Daly RJ | title = Identification of a novel human tankyrase through its interaction with the adaptor protein Grb14 | journal = J. Biol. Chem. | volume = 276 | issue = 20 | pages = 17172–80 | year = 2001 | pmid = 11278563 | doi = 10.1074/jbc.M009756200 }}
* {{cite journal | vauthors = Kim BY, Krämer H, Yamamoto A, Kominami E, Kohsaka S, Akazawa C | title = Molecular characterization of mammalian homologues of class C Vps proteins that interact with syntaxin-7 | journal = J. Biol. Chem. | volume = 276 | issue = 31 | pages = 29393–402 | year = 2001 | pmid = 11382755 | doi = 10.1074/jbc.M101778200 }}
* {{cite journal | vauthors = Cook BD, Dynek JN, Chang W, Shostak G, Smith S | title = Role for the related poly(ADP-Ribose) polymerases tankyrase 1 and 2 at human telomeres | journal = Mol. Cell. Biol. | volume = 22 | issue = 1 | pages = 332–42 | year = 2002 | pmid = 11739745 | pmc = 134233 | doi = 10.1128/MCB.22.1.332-342.2002 }}
* {{cite journal | vauthors = Sbodio JI, Lodish HF, Chi NW | title = Tankyrase-2 oligomerizes with tankyrase-1 and binds to both TRF1 (telomere-repeat-binding factor 1) and IRAP (insulin-responsive aminopeptidase) | journal = Biochem. J. | volume = 361 | issue = Pt 3 | pages = 451–9 | year = 2002 | pmid = 11802774 | pmc = 1222327 | doi = 10.1042/0264-6021:3610451 }}
* {{cite journal | vauthors = Seimiya H, Smith S | title = The telomeric poly(ADP-ribose) polymerase, tankyrase 1, contains multiple binding sites for telomeric repeat binding factor 1 (TRF1) and a novel acceptor, 182-kDa tankyrase-binding protein (TAB182) | journal = J. Biol. Chem. | volume = 277 | issue = 16 | pages = 14116–26 | year = 2002 | pmid = 11854288 | doi = 10.1074/jbc.M112266200 }}
* {{cite journal | vauthors = Sbodio JI, Chi NW | title = Identification of a tankyrase-binding motif shared by IRAP, TAB182, and human TRF1 but not mouse TRF1. NuMA contains this RXXPDG motif and is a novel tankyrase partner | journal = J. Biol. Chem. | volume = 277 | issue = 35 | pages = 31887–92 | year = 2002 | pmid = 12080061 | doi = 10.1074/jbc.M203916200 }}
* {{cite journal | vauthors = Rippmann JF, Damm K, Schnapp A | title = Functional characterization of the poly(ADP-ribose) polymerase activity of tankyrase 1, a potential regulator of telomere length | journal = J. Mol. Biol. | volume = 323 | issue = 2 | pages = 217–24 | year = 2002 | pmid = 12381316 | doi = 10.1016/S0022-2836(02)00946-4 }}
* {{cite journal | vauthors = Bae J, Donigian JR, Hsueh AJ | title = Tankyrase 1 interacts with Mcl-1 proteins and inhibits their regulation of apoptosis | journal = J. Biol. Chem. | volume = 278 | issue = 7 | pages = 5195–204 | year = 2003 | pmid = 12475993 | doi = 10.1074/jbc.M201988200 }}
* {{cite journal | vauthors = Loayza D, De Lange T | title = POT1 as a terminal transducer of TRF1 telomere length control | journal = Nature | volume = 423 | issue = 6943 | pages = 1013–8 | year = 2003 | pmid = 12768206 | doi = 10.1038/nature01688 }}
* {{cite journal | vauthors = Fuchs U, Rehkamp GF, Slany R, Follo M, Borkhardt A | title = The formin-binding protein 17, FBP17, binds via a TNKS binding motif to tankyrase, a protein involved in telomere maintenance | journal = FEBS Lett. | volume = 554 | issue = 1–2 | pages = 10–6 | year = 2003 | pmid = 14596906 | doi = 10.1016/S0014-5793(03)01063-9 }}
* {{cite journal | vauthors = Seimiya H, Muramatsu Y, Smith S, Tsuruo T | title = Functional subdomain in the ankyrin domain of tankyrase 1 required for poly(ADP-ribosyl)ation of TRF1 and telomere elongation | journal = Mol. Cell. Biol. | volume = 24 | issue = 5 | pages = 1944–55 | year = 2004 | pmid = 14966275 | pmc = 350561 | doi = 10.1128/MCB.24.5.1944-1955.2004 }}
* {{cite journal | vauthors = Dynek JN, Smith S | title = Resolution of sister telomere association is required for progression through mitosis | journal = Science | volume = 304 | issue = 5667 | pages = 97–100 | year = 2004 | pmid = 15064417 | doi = 10.1126/science.1094754 }}
* {{cite journal | vauthors = Ye JZ, de Lange T | title = TIN2 is a tankyrase 1 PARP modulator in the TRF1 telomere length control complex | journal = Nat. Genet. | volume = 36 | issue = 6 | pages = 618–23 | year = 2004 | pmid = 15133513 | doi = 10.1038/ng1360 }}
{{Refend}}
 
[[Category:Telomeres]]
[[Category:Telomere-related genes]]
[[Category:Aging-related enzymes]]
 
 
{{Gene-8-stub}}

Latest revision as of 08:42, 10 January 2019

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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

Tankyrase-1 is an enzyme that in humans is encoded by the TNKS gene.[1][2][3]

Description[4]

Tankyrase-1 is a poly-ADP-ribosyltransferase involved in various processes such as Wnt signaling pathway, telomere length and vesicle trafficking. Acts as an activator of the Wnt signaling pathway by mediating poly-ADP-ribosylation (PARsylation) of AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex: poly-ADP-ribosylated target proteins are recognized by RNF146, which mediates their ubiquitination and subsequent degradation. Also mediates PARsylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates PARsylation of TERF1, thereby contributing to the regulation of telomere length. Involved in centrosome maturation during prometaphase by mediating PARsylation of HEPACAM2/MIKI. May also regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles. May be involved in spindle pole assembly through PARsylation of NUMA1. Stimulates 26S proteasome activity.[5]

Protein interactions

TNKS has been shown to interact with:

References

  1. ↑ 1.0 1.1 Smith S, Giriat I, Schmitt A, de Lange T (Dec 1998). "Tankyrase, a poly(ADP-ribose) polymerase at human telomeres". Science. 282 (5393): 1484–7. doi:10.1126/science.282.5393.1484. PMID 9822378.
  2. ↑ Zhu L, Smith S, de Lange T, Seldin MF (May 1999). "Chromosomal mapping of the tankyrase gene in human and mouse". Genomics. 57 (2): 320–1. doi:10.1006/geno.1999.5771. PMID 10198177.
  3. ↑ "Entrez Gene: TNKS tankyrase, TRF1-interacting ankyrin-related ADP-ribose polymerase".
  4. ↑ https://www.uniprot.org/uniprot/O95271
  5. ↑ Voges D, Zwickl P, Baumeister W (1999). "The 26S proteasome: a molecular machine designed for controlled proteolysis". Annu. Rev. Biochem. 68: 1015–68. doi:10.1146/annurev.biochem.68.1.1015. PMID 10872471.
  6. ↑ Fuchs U, Rehkamp GF, Slany R, Follo M, Borkhardt A (Nov 2003). "The formin-binding protein 17, FBP17, binds via a TNKS binding motif to tankyrase, a protein involved in telomere maintenance". FEBS Lett. 554 (1–2): 10–6. doi:10.1016/s0014-5793(03)01063-9. PMID 14596906.
  7. ↑ Bae J, Donigian JR, Hsueh AJ (Feb 2003). "Tankyrase 1 interacts with Mcl-1 proteins and inhibits their regulation of apoptosis". J. Biol. Chem. 278 (7): 5195–204. doi:10.1074/jbc.M201988200. PMID 12475993.
  8. ↑ 8.0 8.1 Seimiya H, Smith S (Apr 2002). "The telomeric poly(ADP-ribose) polymerase, tankyrase 1, contains multiple binding sites for telomeric repeat binding factor 1 (TRF1) and a novel acceptor, 182-kDa tankyrase-binding protein (TAB182)". J. Biol. Chem. 277 (16): 14116–26. doi:10.1074/jbc.M112266200. PMID 11854288.
  9. ↑ 9.0 9.1 Sbodio JI, Chi NW (Aug 2002). "Identification of a tankyrase-binding motif shared by IRAP, TAB182, and human TRF1 but not mouse TRF1. NuMA contains this RXXPDG motif and is a novel tankyrase partner". J. Biol. Chem. 277 (35): 31887–92. doi:10.1074/jbc.M203916200. PMID 12080061.
  10. ↑ Cook BD, Dynek JN, Chang W, Shostak G, Smith S (Jan 2002). "Role for the related poly(ADP-Ribose) polymerases tankyrase 1 and 2 at human telomeres". Mol. Cell. Biol. 22 (1): 332–42. doi:10.1128/mcb.22.1.332-342.2002. PMC 134233. PMID 11739745.
  11. ↑ Sbodio JI, Lodish HF, Chi NW (Feb 2002). "Tankyrase-2 oligomerizes with tankyrase-1 and binds to both TRF1 (telomere-repeat-binding factor 1) and IRAP (insulin-responsive aminopeptidase)". Biochem. J. 361 (Pt 3): 451–9. doi:10.1042/0264-6021:3610451. PMC 1222327. PMID 11802774.

Further reading


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