Protein family
Protein sequence
Protein function
Catalytic activity
EC number
EC number description
2.4.2.-
Transferases;
Glycosyltransferases;
Pentosyltransferases;
2.4.2.30
Transferases;
Glycosyltransferases;
Pentosyltransferases;
NAD+ ADP-ribosyltransferase
PDB | Resolution (Å) | PDB name |
---|---|---|
2RF5 | 2.3 | Crystal structure of human tankyrase 1- catalytic PARP domain |
3UDD | 1.95 | Tankyrase-1 in complex with small molecule inhibitor |
3UH2 | 2.0 | Tankyrase-1 in complexed with PJ34 |
3UH4 | 2.0 | TANKYRASE-1 complexed with NVP-XAV939 |
4DVI | 1.9 | Crystal structure of Tankyrase 1 with IWR2 |
4I9I | 2.4 | Crystal structure of tankyrase 1 with compound 4 |
4K4E | 2.3 | Co-crystal structure of tnks1 with compound 52 [N~2-(5-chloro-2-methoxyphenyl)-N-[trans-4-(2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)cyclohexyl]glycinamide] |
4K4F | 2.9 | Co-crystal structure of TNKS1 with compound 18 [4-[(4S)-5,5-dimethyl-2-oxo-4-phenyl-1,3-oxazolidin-3-yl]-N-(quinolin-8-yl)benzamide] |
4KRS | 2.29 | Tankyrase-1 complexed with small molecule inhibitor |
4LI6 | 2.05 | TANKYRASE-1 Complexed with small molecule inhibitor N-[(4-oxo-3,4-dihydroquinazolin-2-yl)methyl]-3-phenyl-N-(thiophen-2-ylmethyl)propanamide |
4LI7 | 2.2 | TANKYRASE-1 complexed with small molecule inhibitor 4-chloro-5-cyano-N-{2-[4-(4-fluorobenzoyl)piperidin-1-yl]ethyl}-2-methoxybenzamide |
4LI8 | 2.521 | TANKYRASE-1 complexed with small molecule inhibitor 2-[4-(4-fluorobenzoyl)piperidin-1-yl]-N-[(4-oxo-3,5,7,8-tetrahydro-4H-pyrano[4,3-d]pyrimidin-2-yl)methyl]-N-(thiophen-2-ylmethyl)acetamide |
4MSG | 1.8 | Crystal structure of tankyrase 1 with compound 22 |
4MSK | 2.3 | Co-crystal structure of tankyrase 1 with compound 34 |
4MT9 | 2.0 | Co-crystal structure of tankyrase 1 with compound 49 |
4N3R | 1.9 | Co-crystal structure of tankyrase 1 with compound 2 (5-(2-aminoquinazolin-6-yl)-N-(4,4-dimethyl-2-oxo-1,2,3,4-tetrahydroquinolin-7-yl)-2-fluorobenzamide) |
4N4V | 2.0 | Co-crystal structure of tankyrase 1 with compound 4 [(4S)-3-{trans-4-[6-amino-5-(pyrimidin-2-yl)pyridin-3-yl]cyclohexyl}-5,5-dimethyl-4-phenyl-1,3-oxazolidin-2-one] |
4OA7 | 2.301 | Crystal structure of Tankyrase1 in complex with IWR1 |
4TOR | 1.501 | Crystal structure of Tankyrase 1 with IWR-8 |
4TOS | 1.802 | Crystal structure of Tankyrase 1 with 355 |
4U6A | 2.37 | X-ray crystal structure of human TNKS in complex with a small molecule inhibitor |
4UUH | 2.52 | X-ray crystal structure of human TNKS in complex with a small molecule inhibitor |
4UW1 | 3.37 | X-ray crystal structure of human TNKS in complex with a small molecule inhibitor |
4W5S | 2.8 | Tankyrase in complex with compound |
4W6E | 1.95 | Human Tankyrase 1 with small molecule inhibitor |
5EBT | 2.24 | Tankyrase 1 with Phthalazinone 2 |
5ECE | 2.2 | Tankyrase 1 with Phthalazinone 1 |
5ETY | 2.9 | Crystal Structure of human Tankyrase-1 bound to K-756 |
5GP7 | 1.502 | Structural basis for the binding between Tankyrase-1 and USP25 |
5JHQ | 3.2 | ARCs 1-3 of human Tankyrase-1 bound to a peptide derived from IRAP |
5JTI | 2.9 | Crystal structure of the human Tankyrase 1 (TNKS) SAM domain (D1055R), crystal form 2 |
5JU5 | 2.5 | Crystal structure of the human Tankyrase 1 (TNKS) SAM domain (D1055R), crystal form 1 |
5KNI | 2.5 | Crystal Structure of the wild-type SAM domain of human Tankyrase-1 |
6QXU | 1.2 | Human TNKS1 in complex with 6,8-Difluoro-2-[4-(1-hydroxy-1-methyl-ethyl)-phenyl]-3H-quinazolin-4-one |
6URQ | 2.05 | Complex structure of human poly-ADP-ribosyltransferase TNKS1 ARC2-ARC3 and P antigen family member 4 (PAGE4) |
7KKM | 1.58 | Structure of the catalytic domain of tankyrase 1 |
7KKN | 1.48 | Structure of the catalytic domain of tankyrase 1 in complex with talazoparib |
7KKO | 1.56 | Structure of the catalytic domain of tankyrase 1 in complex with olaparib |
7KKP | 1.4 | Structure of the catalytic domain of tankyrase 1 in complex with niraparib |
7KKQ | 1.59 | Structure of the catalytic domain of tankyrase 1 in complex with veliparib |
7OCV | 1.432 | Human TNKS1 in complex with 3-[4-(1-Hydroxy-1-methyl-ethyl)-phenyl]-6-methyl-2H-pyrrolo[1,2-a]pyrazin-1-one |
GO ontology | GO term | GO description |
---|---|---|
Biological Process | GO:0016055 | Wnt signaling pathway |
Biological Process | GO:0051301 | cell division |
Biological Process | GO:0051028 | mRNA transport |
Biological Process | GO:0007052 | mitotic spindle organization |
Biological Process | GO:1904908 | negative regulation of maintenance of mitotic sister chromatid cohesion, telomeric |
Biological Process | GO:1904357 | negative regulation of telomere maintenance via telomere lengthening |
Biological Process | GO:1904743 | negative regulation of telomeric DNA binding |
Biological Process | GO:0018105 | peptidyl-serine phosphorylation |
Biological Process | GO:0018107 | peptidyl-threonine phosphorylation |
Biological Process | GO:0090263 | positive regulation of canonical Wnt signaling pathway |
Biological Process | GO:0051973 | positive regulation of telomerase activity |
Biological Process | GO:1904355 | positive regulation of telomere capping |
Biological Process | GO:0032212 | positive regulation of telomere maintenance via telomerase |
Biological Process | GO:0045944 | positive regulation of transcription by RNA polymerase II |
Biological Process | GO:0070213 | protein auto-ADP-ribosylation |
Biological Process | GO:0070198 | protein localization to chromosome, telomeric region |
Biological Process | GO:0070212 | protein poly-ADP-ribosylation |
Biological Process | GO:0000209 | protein polyubiquitination |
Biological Process | GO:0015031 | protein transport |
Biological Process | GO:0032210 | regulation of telomere maintenance via telomerase |
Biological Process | GO:0051225 | spindle assembly |
Molecular Function | GO:0003950 | NAD+ ADP-ribosyltransferase activity |
Molecular Function | GO:1990404 | NAD+-protein ADP-ribosyltransferase activity |
Molecular Function | GO:0042393 | histone binding |
Molecular Function | GO:0016779 | nucleotidyltransferase activity |
Molecular Function | GO:0008270 | zinc ion binding |
Cellular Component | GO:0005794 | Golgi apparatus |
Cellular Component | GO:0000139 | Golgi membrane |
Cellular Component | GO:0000781 | chromosome, telomeric region |
Cellular Component | GO:0005737 | cytoplasm |
Cellular Component | GO:0005829 | cytosol |
Cellular Component | GO:0097431 | mitotic spindle pole |
Cellular Component | GO:0016604 | nuclear body |
Cellular Component | GO:0031965 | nuclear membrane |
Cellular Component | GO:0005643 | nuclear pore |
Cellular Component | GO:0005654 | nucleoplasm |
Cellular Component | GO:0005634 | nucleus |
Cellular Component | GO:0000242 | pericentriolar material |
InterPro | InterPro name |
---|---|
IPR001660 | Sterile alpha motif domain |
IPR002110 | Ankyrin repeat |
IPR012317 | Poly(ADP-ribose) polymerase, catalytic domain |
IPR013761 | Sterile alpha motif/pointed domain superfamily |
IPR036770 | Ankyrin repeat-containing domain superfamily |
Pfam | Pfam name |
---|---|
PF00023 | Ankyrin repeat |
PF00644 | Poly(ADP-ribose) polymerase catalytic domain |
PF07647 | SAM domain (Sterile alpha motif) |
PF12796 | Ankyrin repeats (3 copies) |
PF13606 | Ankyrin repeat |
PF13637 | Ankyrin repeats (many copies) |
PF13857 | Ankyrin repeats (many copies) |
Reactome | Reactome Name | Node type | Reactome Root | Reactome Root Name |
---|---|---|---|---|
R-HSA-201681 | TCF dependent signaling in response to WNT | Internal node | R-HSA-162582 | Signal Transduction |
R-HSA-4641257 | Degradation of AXIN | Leaf | R-HSA-162582 | Signal Transduction |
R-HSA-5545619 | XAV939 stabilizes AXIN | Leaf | R-HSA-1643685 | Disease |
R-HSA-5689880 | Ub-specific processing proteases | Leaf | R-HSA-392499 | Metabolism of proteins |
R-HSA-8948751 | Regulation of PTEN stability and activity | Leaf | R-HSA-162582 | Signal Transduction |
Location | ECO term | Pubmed |
---|---|---|
Chromosome, telomere | ECO:0000305 | PubMed:9822378 |
Cytoplasm | ECO:0000269 | PubMed:10523501 |
Cytoplasm | ECO:0000269 | PubMed:21799911 |
Cytoplasm | ECO:0000269 | PubMed:22864114 |
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome | ECO:0000269 | PubMed:10523501 |
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome | ECO:0000269 | PubMed:21799911 |
Cytoplasm, cytoskeleton, spindle pole | ECO:0000269 | PubMed:16076287 |
Golgi apparatus membrane | ECO:0000269 | PubMed:22864114 |
Nucleus, nuclear pore complex | ECO:0000269 | PubMed:10523501 |