ID Q6PFX9; PN Poly [ADP-ribose] polymerase tankyrase-1; GN Tnks; OS 10090; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0185; SL Comments: Cytoplasm {ECO:0000250|UniProtKB:O95271}. Golgi apparatus membrane {ECO:0000250|UniProtKB:O95271}; Peripheral membrane protein {ECO:0000250|UniProtKB:O95271}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O95271}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:O95271}. Chromosome, telomere {ECO:0000250|UniProtKB:O95271}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:O95271}. Note=Associated with the Golgi and with juxtanuclear SLC2A4/GLUT4-vesicles. A minor proportion is also found at nuclear pore complexes and around the pericentriolar matrix of mitotic centromeres. During interphase, a small fraction of TNKS is found in the nucleus, associated with TERF1. Localizes to spindle poles at mitosis onset via interaction with NUMA1. {ECO:0000250|UniProtKB:O95271}. DR UNIPROT: Q6PFX9; DR UNIPROT: Q8BX62; DR PDB: 3UTM; DR PDB: 4N4T; DR PDB: 5HKP; DR PDB: 6CF6; DR Pfam: PF00023; DR Pfam: PF12796; DR Pfam: PF13606; DR Pfam: PF13637; DR Pfam: PF13857; DR Pfam: PF00644; DR Pfam: PF07647; DR PROSITE: PS50297; DR PROSITE: PS50088; DR PROSITE: PS51059; DR PROSITE: PS50105; DE Function: 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. {ECO:0000250|UniProtKB:O95271}. DE Reference Proteome: Yes; DE Interaction: Q9C0C2; IntAct: EBI-11025790; Score: 0.35 DE Interaction: Q15018; IntAct: EBI-11025790; Score: 0.35 DE Interaction: E7ESK6; IntAct: EBI-11025790; Score: 0.35 DE Interaction: Q14980; IntAct: EBI-11025790; Score: 0.35 DE Interaction: O95714; IntAct: EBI-11025790; Score: 0.35 DE Interaction: Q9ULU4; IntAct: EBI-11025790; Score: 0.35 DE Interaction: Q99766; IntAct: EBI-11025790; Score: 0.35 DE Interaction: Q96A35; IntAct: EBI-11025790; Score: 0.35 DE Interaction: Q13200; IntAct: EBI-11025790; Score: 0.35 DE Interaction: Q9ULF5; IntAct: EBI-11025790; Score: 0.35 DE Interaction: Q9H2K2; IntAct: EBI-11025790; Score: 0.35 DE Interaction: Q8N1G0; IntAct: EBI-11025790; Score: 0.35 DE Interaction: O60232; IntAct: EBI-11025790; Score: 0.35 DE Interaction: Q6UWP8; IntAct: EBI-11025790; Score: 0.35 DE Interaction: O60239; IntAct: EBI-11025790; Score: 0.35 DE Interaction: O60547; IntAct: EBI-11025790; Score: 0.35 DE Interaction: Q8IY92; IntAct: EBI-11025790; Score: 0.35 DE Interaction: Q9NTX7; IntAct: EBI-16124630; Score: 0.44 DE Interaction: Q9EP53; IntAct: EBI-16734894; Score: 0.35 DE Interaction: Q6NZM9; IntAct: EBI-26473140; Score: 0.35 DE Interaction: P54274; IntAct: EBI-28965117; Score: 0.35 GO GO:0000781; GO GO:0005737; GO GO:0005829; GO GO:0005794; GO GO:0000139; GO GO:0005815; GO GO:0097431; GO GO:0016604; GO GO:0031965; GO GO:0005643; GO GO:0005654; GO GO:0005634; GO GO:0042393; GO GO:0003950; GO GO:1990404; GO GO:0008270; GO GO:0051301; GO GO:0031670; GO GO:0051028; GO GO:1904908; GO GO:1904357; GO GO:1904743; GO GO:0018105; GO GO:0018107; GO GO:0090263; GO GO:0051973; GO GO:1904355; GO GO:0032212; GO GO:0045944; GO GO:0006471; GO GO:0070213; GO GO:0070198; GO GO:0070212; GO GO:0000209; GO GO:0015031; GO GO:0051225; GO GO:0016055; TP Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:O95271}; SQ MAASRRSQHHHHHHQQQLQPAPGASAPPPPPPPPLSPGLAPGPTPASPTAGGLAPFASPRHGLALPEGDGSRDPPDRPRS SQ PDPVDGAVCTVAAPAAVPAASAAVGVAPTPAGGGGGGGNNSASSASSPTSSSSSSPSSPGSSLAESPEAAGVGSTATLGA SQ GAAGLGPGVPAVSGALRELLEACRNGDVSRVKRLVDAANVNAKDMAGRKSSPLHFAAGFGRKDVVEHLLQMGANVHARDD SQ GGLIPLHNACSFGHAEVVSLLLCQGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGADPNIRNTDGKSALDLADPSAK SQ AVLTGEYKKDELLEAARSGNEEKLMALLTPLNVNCHASDGRKSTPLHLAAGYNRVRIVQLLLQHGADVHAKDKGGLVPLH SQ NACSYGHYEVTELLLKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSHGADPTLVNCHGKSAVDMAPTPELRERLTYE SQ FKGHSLLQAAREADLAKVKKTLALEIINFKQPQSHETALHCAVASLHPKRKQVAELLLRKGANVNEKNKDFMTPLHVAAE SQ RAHNDVMEVLHKHGAKMNALDSLGQTALHRAALAGHLQTCRLLLSYGSDPSIISLQGFTAAQMGNEAVQQILSESTPMRT SQ SDVDYRLLEASKAGDLETVKQLCSPQNVNCRDLEGRHSTPLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVPLHNACSY SQ GHYEVAELLVRHGASVNVADLWKFTPLHEAAAKGKYEICKLLLKHGADPTKKNRDGNTPLDLVKEGDTDIQDLLRGDAAL SQ LDAAKKGCLARVQKLCTPENINCRDTQGRNSTPLHLAAGYNNLEVAEYLLEHGADVNAQDKGGLIPLHNAASYGHVDIAA SQ LLIKYNTCVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTMKNQEGQTPLDLATADDIRALLIDAMPPEALPTCFKP SQ QATVVSASLISPASTPSCLSAASSIDNLTGPLTDLAVGGASNAGDGAAGAERKEGEVAGLDMNISQFLKSLGLEHLRDIF SQ ETEQITLDVLADMGHEELKEIGINAYGHRHKLIKGVERLLGGQQGTNPYLTFHCVNQGTILLDLAPEDKEYQSVEEEMQS SQ TIREHRDGGNAGGIFNRYNVIRIQKVVNKKLRERFCHRQKEVSEENHNHHNERMLFHGSPFINAIIHKGFDERHAYIGGM SQ FGAGIYFAENSSKSNQYVYGIGGGTGCPTHKDRSCYICHRQMLFCRVTLGKSFLQFSTMKMAHAPPGHHSVIGRPSVNGL SQ AYAEYVIYRGEQAYPEYLITYQIMKPEAPSQTATAAEQKT //