This protein domain family is found at the C-terminal end of the Tankyrase binding protein in eukaryotes. The precise function of this protein is still unknown. However, it is known interacts with the enzyme tankyrase, a telomeric poly(ADP-ribose) polymerase, by binding to it. Tankyrin catalyses poly(ADP-ribose) chain formation onto proteins. More specifically, it binds to the ankyrin domain in tankyrase (PMID:11854288). The protein domain is approximately 170 amino acids in length and contains two conserved sequence motifs: FPG and LKA.
This protein domain is found at the C-terminal end of the Tankyrase binding protein in eukaryotes. The precise function of this protein is still unknown. However, it is known that interacts with the enzyme tankyrase, a telomeric poly(ADP-ribose) polymerase, by binding to it. Tankyrin catalyses poly(ADP-ribose) chain formation onto proteins. More specifically, it binds to the ankyrin domain in tankyrase [ (PUBMED:11854288) ]. The protein domain is approximately 170 amino acids in length and contains two conserved sequence motifs: FPG and LKA.
Family alignment:
There are 703 Tankyrase_bdg_C domains in 703 proteins in SMART's nrdb database.
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Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing Tankyrase_bdg_C domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with Tankyrase_bdg_C domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing Tankyrase_bdg_C domain in the selected taxonomic class.
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
The telomeric poly(ADP-ribose) polymerase, tankyrase 1, contains multiple bindingsites for telomeric repeat binding factor 1 (TRF1) and a novel acceptor, 182-kDa tankyrase-binding protein (TAB182).
J Biol Chem. 2002; 277: 14116-26
Display abstract
Tankyrase 1, a human telomeric poly(ADP-ribose) polymerase, was originallyidentified through its interaction with TRF1, a negative regulator of telomerelength. Tankyrase 1 ADP-ribosylates TRF1 in vitro, and its overexpression inducestelomere elongation in human cancer cells. In addition to its telomericlocalization, tankyrase 1 resides at multiple subcellular sites, suggestingadditional functions for this protein. Here we identify TAB182, a novel tankyrase1-binding protein of 182 kDa. TAB182 displays a complex pattern of subcellularlocalization. TAB182 localizes to the nucleus in a heterochromatic stainingpattern and to the cytoplasm, where it co-stains with the cortical actin network.TAB182 coimmunoprecipitates with tankyrase 1 from human cells and serves as anacceptor of poly(ADP-ribosyl)ation by tankyrase 1 in vitro. Like TRF1, TAB182binds to the ankyrin domain (comprising 24 ankyrin repeats) of tankyrase 1.Surprisingly, dissection of this domain reveals multiple discrete and overlappingbinding sites for TRF1 and TAB182. Thus, we demonstrate five well conservedankyrin repeat clusters in tankyrase 1. Although each of the five ankyrin repeat clusters independently binds to TRF1, only three of the five bind toTAB182. Thesefindings suggest that tankyrase 1 may act as a scaffold for large molecular mass complexes made up of multiple binding proteins. We discuss potential roles fortankyrase 1-mediated higher order complexes at telomeres and at other subcellularsites.
Links (links to other resources describing this domain)
