TNKS

Tankyrase, TRF1-interacting ankyrin-related ADP-ribose polymerase
Rendering based on PDB 2rf5​.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2RF5​, 3UDD​, 3UH2​, 3UH4​, 4DVI​, 4I9I​, 4K4E​, 4K4F​, 4KRS​, 4LI6​, 4LI7​, 4LI8​, 4MSG​, 4MSK​, 4MT9​, 4N3R​, 4N4V​, 4OA7​, 4TOR​, 4TOS​, 4W5S​, 4W6E​
Identifiers
Symbols	TNKS ; ARTD5; PARP-5a; PARP5A; PARPL; TIN1; TINF1; TNKS1; pART5
External IDs	OMIM: 603303 MGI: 1341087 HomoloGene: 18405 ChEMBL: 6164 GeneCards: TNKS Gene
EC number	2.4.2.30
Gene ontology Molecular function • NAD+ ADP-ribosyltransferase activity • protein binding • zinc ion binding Cellular component • Golgi membrane • pericentriolar material • chromosome, centromeric region • chromosome, telomeric region • nuclear chromosome, telomeric region • spindle pole • nuclear pore • Golgi apparatus • cytosol • nuclear membrane Biological process • protein polyubiquitination • protein ADP-ribosylation • mitotic spindle organization • mitotic nuclear division • protein transport • Wnt signaling pathway • peptidyl-serine phosphorylation • peptidyl-threonine phosphorylation • regulation of telomere maintenance via telomerase • positive regulation of telomere maintenance via telomerase • negative regulation of DNA binding • positive regulation of transcription from RNA polymerase II promoter • mRNA transport • spindle assembly • cell division • protein localization to chromosome, telomeric region • protein poly-ADP-ribosylation • protein auto-ADP-ribosylation • positive regulation of canonical Wnt signaling pathway Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	8658	21951
Ensembl	ENSG00000173273	ENSMUSG00000031529
UniProt	O95271	Q6PFX9
RefSeq (mRNA)	NM_003747	NM_175091
RefSeq (protein)	NP_003738	NP_780300
Location (UCSC)	Chr 8: 9.56 – 9.78 Mb	Chr 8: 34.83 – 34.97 Mb
PubMed search

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

Protein Interactions

TNKS has been shown to interact with:

• FNBP1,^[4]
• MCL1,^[5]
• TERF1,^{[1][6][7][8][9]} and
• TNKS1BP1.^[6][7]

References

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. 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.
5. 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.
6. 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.
7. 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.
8. 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.
9. 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

• Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
• Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
• Smith S, de Lange T (1999). "Cell cycle dependent localization of the telomeric PARP, tankyrase, to nuclear pore complexes and centrosomes". J. Cell. Sci. 112 (21): 3649–56. PMID 10523501.
• Chi NW, Lodish HF (2001). "Tankyrase is a golgi-associated mitogen-activated protein kinase substrate that interacts with IRAP in GLUT4 vesicles". J. Biol. Chem. 275 (49): 38437–44. doi:10.1074/jbc.M007635200. PMID 10988299.
• Lyons RJ, Deane R, Lynch DK, Ye ZS, Sanderson GM, Eyre HJ, Sutherland GR, Daly RJ (2001). "Identification of a novel human tankyrase through its interaction with the adaptor protein Grb14". J. Biol. Chem. 276 (20): 17172–80. doi:10.1074/jbc.M009756200. PMID 11278563.
• Kim BY, Krämer H, Yamamoto A, Kominami E, Kohsaka S, Akazawa C (2001). "Molecular characterization of mammalian homologues of class C Vps proteins that interact with syntaxin-7". J. Biol. Chem. 276 (31): 29393–402. doi:10.1074/jbc.M101778200. PMID 11382755.
• Cook BD, Dynek JN, Chang W, Shostak G, Smith S (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.
• Sbodio JI, Lodish HF, Chi NW (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.
• Seimiya H, Smith S (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.
• Sbodio JI, Chi NW (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.
• Rippmann JF, Damm K, Schnapp A (2002). "Functional characterization of the poly(ADP-ribose) polymerase activity of tankyrase 1, a potential regulator of telomere length". J. Mol. Biol. 323 (2): 217–24. doi:10.1016/S0022-2836(02)00946-4. PMID 12381316.
• Bae J, Donigian JR, Hsueh AJ (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.
• Loayza D, De Lange T (2003). "POT1 as a terminal transducer of TRF1 telomere length control". Nature 423 (6943): 1013–8. doi:10.1038/nature01688. PMID 12768206.
• Fuchs U, Rehkamp GF, Slany R, Follo M, Borkhardt A (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.
• Seimiya H, Muramatsu Y, Smith S, Tsuruo T (2004). "Functional subdomain in the ankyrin domain of tankyrase 1 required for poly(ADP-ribosyl)ation of TRF1 and telomere elongation". Mol. Cell. Biol. 24 (5): 1944–55. doi:10.1128/MCB.24.5.1944-1955.2004. PMC 350561. PMID 14966275.
• Dynek JN, Smith S (2004). "Resolution of sister telomere association is required for progression through mitosis". Science 304 (5667): 97–100. doi:10.1126/science.1094754. PMID 15064417.
• Ye JZ, de Lange T (2004). "TIN2 is a tankyrase 1 PARP modulator in the TRF1 telomere length control complex". Nat. Genet. 36 (6): 618–23. doi:10.1038/ng1360. PMID 15133513.