TNKS2_HUMAN
ID TNKS2_HUMAN Reviewed; 1166 AA.
AC Q9H2K2; B2RBD3; Q9H8F2; Q9HAS4;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Poly [ADP-ribose] polymerase tankyrase-2 {ECO:0000305};
DE EC=2.4.2.30 {ECO:0000269|PubMed:19759537, ECO:0000269|PubMed:21478859};
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 6 {ECO:0000303|PubMed:20106667};
DE Short=ARTD6 {ECO:0000303|PubMed:20106667};
DE AltName: Full=Poly [ADP-ribose] polymerase 5B {ECO:0000303|PubMed:20106667};
DE AltName: Full=Protein poly-ADP-ribosyltransferase tankyrase-2 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000269|PubMed:19759537, ECO:0000269|PubMed:25043379};
DE AltName: Full=TNKS-2;
DE AltName: Full=TRF1-interacting ankyrin-related ADP-ribose polymerase 2;
DE AltName: Full=Tankyrase II;
DE AltName: Full=Tankyrase-2;
DE Short=TANK2;
DE AltName: Full=Tankyrase-like protein;
DE AltName: Full=Tankyrase-related protein;
GN Name=TNKS2 {ECO:0000312|HGNC:HGNC:15677};
GN Synonyms=PARP5B {ECO:0000303|PubMed:20106667}, TANK2, TNKL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetal brain;
RX PubMed=11205898;
RA Monz D., Munnia A., Comtesse N., Fischer U., Steudel W.-I., Feiden W.,
RA Glass B., Meese E.U.;
RT "Novel tankyrase-related gene detected with meningioma-specific sera.";
RL Clin. Cancer Res. 7:113-119(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary carcinoma;
RX PubMed=11294570; DOI=10.1038/sj.gene.6363722;
RA Kuimov A.N., Kuprash D.V., Petrov V.N., Vdovichenko K.K., Scanlan M.J.,
RA Jongeneel C.V., Lagarkova M.A., Nedospasov S.A.;
RT "Cloning and characterization of TNKL, a member of tankyrase gene family.";
RL Genes Immun. 2:52-55(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=11278563; DOI=10.1074/jbc.m009756200;
RA Lyons R.J., Deane R., Lynch D.K., Ye Z.-S.J., Sanderson G.M., Eyre H.J.,
RA Sutherland G.R., Daly R.J.;
RT "Identification of a novel human tankyrase through its interaction with the
RT adaptor protein Grb14.";
RL J. Biol. Chem. 276:17172-17180(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC TISSUE=Placenta;
RX PubMed=11454873; DOI=10.1074/jbc.m105968200;
RA Kaminker P.G., Kim S.-H., Taylor R.D., Zebarjadian Y., Funk W.D.,
RA Morin G.B., Yaswen P., Campisi J.;
RT "TANK2, a new TRF1-associated poly(ADP-ribose) polymerase, causes rapid
RT induction of cell death upon overexpression.";
RL J. Biol. Chem. 276:35891-35899(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH TRF1 AND
RP LNPEP/OTASE.
RC TISSUE=Skeletal muscle;
RX PubMed=11802774; DOI=10.1042/0264-6021:3610451;
RA Sbodio J.I., Lodish H.F., Chi N.-W.;
RT "Tankyrase-2 oligomerizes with tankyrase-1 and binds to both TRF1
RT (telomere-repeat-binding factor 1) and IRAP (insulin-responsive
RT aminopeptidase).";
RL Biochem. J. 361:451-459(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yin Y., Gelmann E.P.;
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [9]
RP INTERACTION WITH NUMA1.
RX PubMed=12080061; DOI=10.1074/jbc.m203916200;
RA Sbodio J.I., Chi N.W.;
RT "Identification of a tankyrase-binding motif shared by IRAP, TAB182, and
RT human TRF1 but not mouse TRF1. NuMA contains this RXXPDG motif and is a
RT novel tankyrase partner.";
RL J. Biol. Chem. 277:31887-31892(2002).
RN [10]
RP FUNCTION, AND ADP-RIBOSYLATION.
RX PubMed=11739745; DOI=10.1128/mcb.22.1.332-342.2002;
RA Cook B.D., Dynek J.N., Chang W., Shostak G., Smith S.;
RT "Role for the related poly(ADP-Ribose) polymerases tankyrase 1 and 2 at
RT human telomeres.";
RL Mol. Cell. Biol. 22:332-342(2002).
RN [11]
RP INTERACTION WITH HIF1AN, AND HYDROXYLATION AT ASN-203; ASN-271; ASN-427;
RP ASN-518; ASN-586; ASN-671; ASN-706 AND ASN-739.
RX PubMed=18936059; DOI=10.1074/mcp.m800340-mcp200;
RA Cockman M.E., Webb J.D., Kramer H.B., Kessler B.M., Ratcliffe P.J.;
RT "Proteomics-based identification of novel factor inhibiting hypoxia-
RT inducible factor (FIH) substrates indicates widespread asparaginyl
RT hydroxylation of ankyrin repeat domain-containing proteins.";
RL Mol. Cell. Proteomics 8:535-546(2009).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH AXIN1
RP AND AXIN2, AND MUTAGENESIS OF MET-1054.
RX PubMed=19759537; DOI=10.1038/nature08356;
RA Huang S.M., Mishina Y.M., Liu S., Cheung A., Stegmeier F., Michaud G.A.,
RA Charlat O., Wiellette E., Zhang Y., Wiessner S., Hild M., Shi X.,
RA Wilson C.J., Mickanin C., Myer V., Fazal A., Tomlinson R., Serluca F.,
RA Shao W., Cheng H., Shultz M., Rau C., Schirle M., Schlegl J., Ghidelli S.,
RA Fawell S., Lu C., Curtis D., Kirschner M.W., Lengauer C., Finan P.M.,
RA Tallarico J.A., Bouwmeester T., Porter J.A., Bauer A., Cong F.;
RT "Tankyrase inhibition stabilizes axin and antagonizes Wnt signalling.";
RL Nature 461:614-620(2009).
RN [13]
RP NOMENCLATURE.
RX PubMed=20106667; DOI=10.1016/j.tibs.2009.12.003;
RA Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.;
RT "Toward a unified nomenclature for mammalian ADP-ribosyltransferases.";
RL Trends Biochem. Sci. 35:208-219(2010).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH AXIN1; AXIN2; BLZF1 AND
RP CASC3, AND UBIQUITINATION.
RX PubMed=21478859; DOI=10.1038/ncb2222;
RA Zhang Y., Liu S., Mickanin C., Feng Y., Charlat O., Michaud G.A.,
RA Schirle M., Shi X., Hild M., Bauer A., Myer V.E., Finan P.M., Porter J.A.,
RA Huang S.M., Cong F.;
RT "RNF146 is a poly(ADP-ribose)-directed E3 ligase that regulates axin
RT degradation and Wnt signalling.";
RL Nat. Cell Biol. 13:623-629(2011).
RN [15]
RP INTERACTION WITH RNF146, UBIQUITINATION, AND SUBCELLULAR LOCATION.
RX PubMed=21799911; DOI=10.1371/journal.pone.0022595;
RA Callow M.G., Tran H., Phu L., Lau T., Lee J., Sandoval W.N., Liu P.S.,
RA Bheddah S., Tao J., Lill J.R., Hongo J.A., Davis D., Kirkpatrick D.S.,
RA Polakis P., Costa M.;
RT "Ubiquitin ligase RNF146 regulates tankyrase and Axin to promote Wnt
RT signaling.";
RL PLoS ONE 6:E22595-E22595(2011).
RN [16]
RP FUNCTION.
RX PubMed=23622245; DOI=10.1016/j.cell.2013.03.040;
RA Cho-Park P.F., Steller H.;
RT "Proteasome regulation by ADP-ribosylation.";
RL Cell 153:614-627(2013).
RN [17]
RP FUNCTION.
RX PubMed=25043379; DOI=10.1038/ncomms5426;
RA Vyas S., Matic I., Uchima L., Rood J., Zaja R., Hay R.T., Ahel I.,
RA Chang P.;
RT "Family-wide analysis of poly(ADP-ribose) polymerase activity.";
RL Nat. Commun. 5:4426-4426(2014).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 538-558 IN COMPLEX WITH HIF1AN;
RP IRON AND 2-OXOGLUTARATE, HYDROXYLATION AT HIS-238 AND HIS-553, AND
RP MUTAGENESIS OF HIS-553.
RX PubMed=21251231; DOI=10.1111/j.1742-4658.2011.08022.x;
RA Yang M., Chowdhury R., Ge W., Hamed R.B., McDonough M.A., Claridge T.D.,
RA Kessler B.M., Cockman M.E., Ratcliffe P.J., Schofield C.J.;
RT "Factor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-
RT translational hydroxylation of histidinyl residues within ankyrin repeat
RT domains.";
RL FEBS J. 278:1086-1097(2011).
CC -!- FUNCTION: Poly-ADP-ribosyltransferase involved in various processes
CC such as Wnt signaling pathway, telomere length and vesicle trafficking
CC (PubMed:11739745, PubMed:11802774, PubMed:19759537, PubMed:21478859,
CC PubMed:23622245, PubMed:25043379). Acts as an activator of the Wnt
CC signaling pathway by mediating poly-ADP-ribosylation of AXIN1 and
CC AXIN2, 2 key components of the beta-catenin destruction complex: poly-
CC ADP-ribosylated target proteins are recognized by RNF146, which
CC mediates their ubiquitination and subsequent degradation
CC (PubMed:19759537, PubMed:21478859). Also mediates poly-ADP-ribosylation
CC of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent
CC ubiquitination (PubMed:21478859). Mediates poly-ADP-ribosylation of
CC TERF1, thereby contributing to the regulation of telomere length
CC (PubMed:11739745). Stimulates 26S proteasome activity
CC (PubMed:23622245). {ECO:0000269|PubMed:11739745,
CC ECO:0000269|PubMed:11802774, ECO:0000269|PubMed:19759537,
CC ECO:0000269|PubMed:21478859, ECO:0000269|PubMed:23622245,
CC ECO:0000269|PubMed:25043379}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-
CC ribosyl)n+1-acceptor + H(+).; EC=2.4.2.30;
CC Evidence={ECO:0000269|PubMed:19759537, ECO:0000269|PubMed:21478859};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartyl-[protein] + NAD(+) = 4-O-(ADP-D-ribosyl)-L-
CC aspartyl-[protein] + nicotinamide; Xref=Rhea:RHEA:54424, Rhea:RHEA-
CC COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:29961, ChEBI:CHEBI:57540, ChEBI:CHEBI:138102;
CC Evidence={ECO:0000305};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54425;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamyl-[protein] + NAD(+) = 5-O-(ADP-D-ribosyl)-L-
CC glutamyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58224, Rhea:RHEA-
CC COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:57540, ChEBI:CHEBI:142540;
CC Evidence={ECO:0000305};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58225;
CC Evidence={ECO:0000305};
CC -!- ACTIVITY REGULATION: Specifically inhibited by XAV939, a small
CC molecule, leading to inhibit the Wnt signaling pathway by stabilizing
CC AXIN1 and AXIN2. {ECO:0000269|PubMed:19759537}.
CC -!- SUBUNIT: Oligomerizes and associates with TNKS. Interacts with the
CC cytoplasmic domain of LNPEP/Otase in SLC2A4/GLUT4-vesicles
CC (PubMed:11802774). Binds to the N-terminus of Grb14 and TRF1 with its
CC ankyrin repeat region (PubMed:11802774). Interacts with HIF1AN
CC (PubMed:18936059, PubMed:21251231). Interacts with RNF146; this
CC interaction leads to ubiquitination and proteasomal degradation
CC (PubMed:21799911). Interacts with NUMA1 (PubMed:12080061).
CC {ECO:0000269|PubMed:11802774, ECO:0000269|PubMed:12080061,
CC ECO:0000269|PubMed:18936059, ECO:0000269|PubMed:19759537,
CC ECO:0000269|PubMed:21251231, ECO:0000269|PubMed:21478859,
CC ECO:0000269|PubMed:21799911}.
CC -!- INTERACTION:
CC Q9H2K2; O15084: ANKRD28; NbExp=3; IntAct=EBI-4398527, EBI-359567;
CC Q9H2K2; Q7Z6K5-1: ARPIN; NbExp=5; IntAct=EBI-4398527, EBI-16079078;
CC Q9H2K2; O15169: AXIN1; NbExp=2; IntAct=EBI-4398527, EBI-710484;
CC Q9H2K2; Q9NWV8: BABAM1; NbExp=5; IntAct=EBI-4398527, EBI-745725;
CC Q9H2K2; P11274: BCR; NbExp=3; IntAct=EBI-4398527, EBI-712838;
CC Q9H2K2; Q13698: CACNA1S; NbExp=2; IntAct=EBI-4398527, EBI-5329490;
CC Q9H2K2; Q9NRI5: DISC1; NbExp=2; IntAct=EBI-4398527, EBI-529989;
CC Q9H2K2; Q6V0I7: FAT4; NbExp=2; IntAct=EBI-4398527, EBI-948985;
CC Q9H2K2; Q9NWT6: HIF1AN; NbExp=5; IntAct=EBI-4398527, EBI-745632;
CC Q9H2K2; P14652: HOXB2; NbExp=3; IntAct=EBI-4398527, EBI-5329558;
CC Q9H2K2; Q9UIQ6: LNPEP; NbExp=3; IntAct=EBI-4398527, EBI-2805360;
CC Q9H2K2; Q14980: NUMA1; NbExp=4; IntAct=EBI-4398527, EBI-521611;
CC Q9H2K2; Q9BZL4: PPP1R12C; NbExp=2; IntAct=EBI-4398527, EBI-721802;
CC Q9H2K2; Q92698: RAD54L; NbExp=3; IntAct=EBI-4398527, EBI-5333483;
CC Q9H2K2; P78314: SH3BP2; NbExp=5; IntAct=EBI-4398527, EBI-727062;
CC Q9H2K2; O43815: STRN; NbExp=2; IntAct=EBI-4398527, EBI-1046642;
CC Q9H2K2; P54274: TERF1; NbExp=4; IntAct=EBI-4398527, EBI-710997;
CC Q9H2K2; Q9C0C2: TNKS1BP1; NbExp=3; IntAct=EBI-4398527, EBI-2104458;
CC Q9H2K2; Q06649: Sh3bp2; Xeno; NbExp=6; IntAct=EBI-4398527, EBI-5323518;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane; Peripheral
CC membrane protein. Nucleus. Chromosome, telomere {ECO:0000305}.
CC Note=Associated with the Golgi and with juxtanuclear SLC2A4/GLUT4-
CC vesicles. Also found around the pericentriolar matrix of mitotic
CC centromeres. During interphase, a small fraction of TNKS2 is found in
CC the nucleus, associated with TRF1.
CC -!- TISSUE SPECIFICITY: Highly expressed in placenta, skeletal muscle,
CC liver, brain, kidney, heart, thymus, spinal cord, lung, peripheral
CC blood leukocytes, pancreas, lymph nodes, spleen, prostate, testis,
CC ovary, small intestine, colon, mammary gland, breast and breast
CC carcinoma, and in common-type meningioma. Highly expressed in fetal
CC liver, heart and brain.
CC -!- PTM: Ubiquitinated at 'Lys-48' and 'Lys-63' by RNF146 when auto-poly-
CC ADP-ribosylated; this leads to degradation.
CC {ECO:0000269|PubMed:21478859, ECO:0000269|PubMed:21799911}.
CC -!- PTM: ADP-ribosylated (-auto). Poly-ADP-ribosylated protein is
CC recognized by RNF146, followed by ubiquitination.
CC {ECO:0000269|PubMed:21478859}.
CC -!- PTM: The crystallographic evidence suggests that the 3-hydroxyhistidine
CC may be the (3S) stereoisomer. {ECO:0000269|PubMed:21251231}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG25674.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14665.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF305081; AAG25674.1; ALT_INIT; mRNA.
DR EMBL; AF264912; AAG44694.1; -; mRNA.
DR EMBL; AF329696; AAK13463.1; -; mRNA.
DR EMBL; AF342982; AAK25811.1; -; mRNA.
DR EMBL; AF309033; AAK82330.1; -; mRNA.
DR EMBL; AF438201; AAL40795.1; -; mRNA.
DR EMBL; AK023746; BAB14665.1; ALT_INIT; mRNA.
DR EMBL; AK314612; BAG37180.1; -; mRNA.
DR EMBL; AL359707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS7417.1; -.
DR RefSeq; NP_079511.1; NM_025235.3.
DR PDB; 2Y0I; X-ray; 2.28 A; S=538-558.
DR PDB; 3KR7; X-ray; 1.95 A; A=946-1162.
DR PDB; 3KR8; X-ray; 2.10 A; A/C=946-1162.
DR PDB; 3MHJ; X-ray; 1.80 A; A/B=946-1162.
DR PDB; 3MHK; X-ray; 2.30 A; A=952-1166.
DR PDB; 3P0N; X-ray; 1.90 A; A/C=946-1162.
DR PDB; 3P0P; X-ray; 2.49 A; A/C=946-1162.
DR PDB; 3P0Q; X-ray; 1.90 A; A/C=946-1162.
DR PDB; 3TWQ; X-ray; 2.15 A; A/B=484-655.
DR PDB; 3TWR; X-ray; 1.55 A; A/B/C/D=488-649.
DR PDB; 3TWS; X-ray; 1.70 A; A/B/C/D=488-649.
DR PDB; 3TWT; X-ray; 1.85 A; A/B/C/D=488-649.
DR PDB; 3TWU; X-ray; 1.80 A; A=488-649.
DR PDB; 3TWV; X-ray; 2.30 A; A/B/C/D=488-649.
DR PDB; 3TWW; X-ray; 2.00 A; A/B=488-649.
DR PDB; 3TWX; X-ray; 1.80 A; A/B=488-649.
DR PDB; 3U9H; X-ray; 1.75 A; A/B=946-1162.
DR PDB; 3U9Y; X-ray; 2.30 A; A=946-1162.
DR PDB; 3UA9; X-ray; 2.15 A; A/B=946-1162.
DR PDB; 3W51; X-ray; 2.00 A; A/B=952-1161.
DR PDB; 4AVU; X-ray; 2.40 A; A/B=946-1162.
DR PDB; 4AVW; X-ray; 2.15 A; A/B=946-1162.
DR PDB; 4BFP; X-ray; 2.40 A; A/B=946-1162.
DR PDB; 4BJ9; X-ray; 2.05 A; A/B=946-1162.
DR PDB; 4BJB; X-ray; 2.30 A; A=946-1162.
DR PDB; 4BJC; X-ray; 2.20 A; A=946-1162.
DR PDB; 4BS4; X-ray; 1.89 A; A/B=946-1162.
DR PDB; 4BU3; X-ray; 2.15 A; A/B=946-1162.
DR PDB; 4BU5; X-ray; 1.80 A; A/B=946-1162.
DR PDB; 4BU6; X-ray; 1.80 A; A/B=946-1162.
DR PDB; 4BU7; X-ray; 2.05 A; A/C=946-1162.
DR PDB; 4BU8; X-ray; 1.85 A; A/C=946-1162.
DR PDB; 4BU9; X-ray; 1.65 A; A/B=946-1162.
DR PDB; 4BUA; X-ray; 1.85 A; A/C=946-1162.
DR PDB; 4BUD; X-ray; 2.50 A; A/C=946-1162.
DR PDB; 4BUE; X-ray; 1.60 A; A/B=946-1162.
DR PDB; 4BUF; X-ray; 2.50 A; A/B=946-1162.
DR PDB; 4BUI; X-ray; 1.95 A; A/C=946-1162.
DR PDB; 4BUS; X-ray; 1.90 A; A/B=946-1162.
DR PDB; 4BUT; X-ray; 1.90 A; A/B=946-1162.
DR PDB; 4BUU; X-ray; 1.60 A; A/B=946-1162.
DR PDB; 4BUV; X-ray; 1.80 A; A/C=946-1162.
DR PDB; 4BUW; X-ray; 1.85 A; A/B=946-1162.
DR PDB; 4BUX; X-ray; 1.95 A; A/C=946-1162.
DR PDB; 4BUY; X-ray; 1.90 A; A/B=946-1162.
DR PDB; 4HKI; X-ray; 2.15 A; A/H=946-1113, C/D=1114-1162.
DR PDB; 4HKK; X-ray; 1.95 A; A/C=946-1113, B/D=1114-1162.
DR PDB; 4HKN; X-ray; 2.05 A; A=946-1113, C=1114-1162.
DR PDB; 4HL5; X-ray; 2.20 A; A=946-1113, C=1114-1162.
DR PDB; 4HLF; X-ray; 2.15 A; A/B=946-1113, C/D=1114-1162.
DR PDB; 4HLG; X-ray; 2.00 A; A/B=946-1113, C/D=1114-1162.
DR PDB; 4HLH; X-ray; 1.75 A; A/B=946-1113, C/D=1114-1162.
DR PDB; 4HLK; X-ray; 2.00 A; A/B=946-1113, C/D=1114-1162.
DR PDB; 4HLM; X-ray; 1.95 A; A/B=946-1113, C/D=1114-1162.
DR PDB; 4HMH; X-ray; 2.30 A; A=946-1113, C=1114-1162.
DR PDB; 4HYF; X-ray; 2.80 A; A/B/C=946-1162.
DR PDB; 4IUE; X-ray; 2.38 A; A=952-1161.
DR PDB; 4J1Z; X-ray; 2.00 A; A/B=952-1161.
DR PDB; 4J21; X-ray; 1.93 A; A=952-1161.
DR PDB; 4J22; X-ray; 2.12 A; A/B=952-1161.
DR PDB; 4J3L; X-ray; 2.09 A; A=952-1161.
DR PDB; 4J3M; X-ray; 1.90 A; A/B=952-1161.
DR PDB; 4KZL; X-ray; 2.00 A; A/B=946-1113, C/D=1114-1162.
DR PDB; 4KZQ; X-ray; 2.25 A; A/B=946-1113, C/D=1114-1162.
DR PDB; 4KZU; X-ray; 2.10 A; A/B=946-1113, C/D=1114-1162.
DR PDB; 4L09; X-ray; 2.05 A; A/B=946-1113, C/D=1114-1162.
DR PDB; 4L0B; X-ray; 1.80 A; A/B=946-1113, C/D=1114-1162.
DR PDB; 4L0I; X-ray; 2.30 A; A/B=946-1113, C/D=1114-1162.
DR PDB; 4L0S; X-ray; 1.90 A; A/B=946-1113, C/D=1114-1162.
DR PDB; 4L0T; X-ray; 2.10 A; A/B=946-1113, C/D=1114-1162.
DR PDB; 4L0V; X-ray; 1.70 A; A/B=946-1113, C/D=1114-1162.
DR PDB; 4L10; X-ray; 1.70 A; A/B=946-1113, C/D=1114-1162.
DR PDB; 4L2F; X-ray; 2.05 A; A/B=946-1113, C/D=1114-1162.
DR PDB; 4L2G; X-ray; 2.05 A; A/B=946-1113, C/D=1114-1162.
DR PDB; 4L2K; X-ray; 2.10 A; A/B=946-1113, C/D=1114-1162.
DR PDB; 4L31; X-ray; 2.00 A; A/B=946-1113, C/D=1114-1162.
DR PDB; 4L32; X-ray; 1.85 A; A/B=946-1113, C/D=1114-1162.
DR PDB; 4L33; X-ray; 2.10 A; A/B=946-1113, C/D=1114-1162.
DR PDB; 4L34; X-ray; 1.80 A; A/B=946-1113, C/D=1114-1162.
DR PDB; 4M7B; X-ray; 1.95 A; A/C=946-1162.
DR PDB; 4PML; X-ray; 1.87 A; A/B/C/D=959-1164.
DR PDB; 4PNL; X-ray; 1.50 A; A/B/C/D=959-1164.
DR PDB; 4PNM; X-ray; 2.19 A; A/B/C/D=959-1164.
DR PDB; 4PNN; X-ray; 1.65 A; A/B/C/D=959-1164.
DR PDB; 4PNQ; X-ray; 1.85 A; A/B/C/D=959-1164.
DR PDB; 4PNR; X-ray; 1.71 A; A/B/C/D=959-1164.
DR PDB; 4PNS; X-ray; 1.65 A; A/B/C/D=959-1164.
DR PDB; 4PNT; X-ray; 1.60 A; A/B/C/D=959-1164.
DR PDB; 4TJU; X-ray; 1.57 A; A/B/C/D=959-1164.
DR PDB; 4TJW; X-ray; 1.70 A; A/B/C/D=959-1164.
DR PDB; 4TJY; X-ray; 1.90 A; A/B/C/D=959-1164.
DR PDB; 4TK0; X-ray; 1.65 A; A/B/C/D=959-1164.
DR PDB; 4TK5; X-ray; 2.02 A; A/B/C/D=959-1164.
DR PDB; 4TKF; X-ray; 2.60 A; A/B/C/D=959-1164.
DR PDB; 4TKG; X-ray; 1.95 A; A/B/C/D=959-1164.
DR PDB; 4TKI; X-ray; 2.15 A; A/B/C/D=959-1164.
DR PDB; 4UFU; X-ray; 2.10 A; A/B=946-1162.
DR PDB; 4UFY; X-ray; 1.70 A; A/B=946-1162.
DR PDB; 4UHG; X-ray; 1.70 A; A/B=946-1162.
DR PDB; 4UI3; X-ray; 2.00 A; A/B=946-1113, C/D=1115-1162.
DR PDB; 4UI4; X-ray; 2.40 A; A/B=946-1113, C/D=1115-1162.
DR PDB; 4UI5; X-ray; 1.65 A; A/B=946-1113, C/D=1115-1162.
DR PDB; 4UI6; X-ray; 1.80 A; A/B=946-1113, C/D=1115-1162.
DR PDB; 4UI7; X-ray; 1.80 A; A/B=946-1113, C/D=1115-1162.
DR PDB; 4UI8; X-ray; 2.05 A; A/B=946-1113, C/D=1115-1162.
DR PDB; 4UVL; X-ray; 2.00 A; A/C=946-1162.
DR PDB; 4UVN; X-ray; 2.20 A; A/B=946-1162.
DR PDB; 4UVO; X-ray; 1.85 A; A/B=946-1162.
DR PDB; 4UVP; X-ray; 1.75 A; A/C=946-1113, B/D=1115-1162.
DR PDB; 4UVS; X-ray; 2.00 A; A/C=946-1162.
DR PDB; 4UVT; X-ray; 1.95 A; A/C=946-1162.
DR PDB; 4UVU; X-ray; 1.95 A; A/B=946-1162.
DR PDB; 4UVV; X-ray; 1.90 A; A/B=946-1162.
DR PDB; 4UVW; X-ray; 2.10 A; A/B=946-1162.
DR PDB; 4UVX; X-ray; 1.95 A; A/B=946-1162.
DR PDB; 4UVY; X-ray; 1.95 A; A/B=946-1162.
DR PDB; 4UVZ; X-ray; 1.60 A; A/C=946-1162.
DR PDB; 4UX4; X-ray; 1.80 A; A/B=946-1162.
DR PDB; 4W5I; X-ray; 1.95 A; A/B=952-1162.
DR PDB; 4Z68; X-ray; 1.86 A; A=490-644.
DR PDB; 5ADQ; X-ray; 2.10 A; A=946-1113, B=1115-1162.
DR PDB; 5ADR; X-ray; 2.10 A; A=946-1113, B=1115-1162.
DR PDB; 5ADS; X-ray; 1.80 A; A=946-1113, B=1115-1162.
DR PDB; 5ADT; X-ray; 2.15 A; A=946-1113, B=1115-1162.
DR PDB; 5AEH; X-ray; 1.85 A; A/B=946-1162.
DR PDB; 5AKU; X-ray; 1.80 A; A/B=946-1162.
DR PDB; 5AKW; X-ray; 2.07 A; A/B=946-1162.
DR PDB; 5AL1; X-ray; 1.75 A; A/B=946-1162.
DR PDB; 5AL2; X-ray; 1.90 A; A/B=946-1162.
DR PDB; 5AL3; X-ray; 1.75 A; A/B=946-1162.
DR PDB; 5AL4; X-ray; 1.90 A; A/B=946-1162.
DR PDB; 5AL5; X-ray; 2.05 A; A/B=946-1162.
DR PDB; 5BXO; X-ray; 1.33 A; A/B=488-649.
DR PDB; 5BXU; X-ray; 1.35 A; A=488-649.
DR PDB; 5C5P; X-ray; 1.75 A; A/B=946-1113, C/D=1114-1162.
DR PDB; 5C5Q; X-ray; 2.00 A; A/B=946-1113, C/D=1114-1162.
DR PDB; 5C5R; X-ray; 1.55 A; A/B=946-1113, C/D=1114-1162.
DR PDB; 5DCZ; X-ray; 2.23 A; A=936-1166.
DR PDB; 5FPF; X-ray; 2.60 A; A/B=946-1113, C/D=1115-1162.
DR PDB; 5FPG; X-ray; 2.75 A; A/B=946-1162.
DR PDB; 5JRT; X-ray; 1.53 A; A=867-940.
DR PDB; 5NOB; X-ray; 1.85 A; A/B=946-1162.
DR PDB; 5NSP; X-ray; 2.30 A; A/B=946-1113, C/D=1114-1162.
DR PDB; 5NUT; X-ray; 1.60 A; A/B=952-1162.
DR PDB; 5OWS; X-ray; 1.80 A; A/B=946-1162.
DR PDB; 5OWT; X-ray; 2.20 A; A/B=946-1162.
DR PDB; 6TG4; X-ray; 2.76 A; AAA/BBB=946-1162.
DR PDB; 6TKM; X-ray; 2.70 A; AAA/BBB=946-1162.
DR PDB; 6TKN; X-ray; 2.50 A; AAA/BBB=946-1162.
DR PDB; 6TKP; X-ray; 2.40 A; AAA/BBB=946-1162.
DR PDB; 6TKQ; X-ray; 2.50 A; AAA/BBB=946-1162.
DR PDB; 6TKR; X-ray; 2.75 A; AAA/BBB=946-1162.
DR PDB; 6TKS; X-ray; 2.50 A; AAA/BBB=946-1162.
DR PDB; 7A1S; X-ray; 2.01 A; B=691-710.
DR PDB; 7O6X; X-ray; 2.20 A; AAA/BBB=946-1162.
DR PDBsum; 2Y0I; -.
DR PDBsum; 3KR7; -.
DR PDBsum; 3KR8; -.
DR PDBsum; 3MHJ; -.
DR PDBsum; 3MHK; -.
DR PDBsum; 3P0N; -.
DR PDBsum; 3P0P; -.
DR PDBsum; 3P0Q; -.
DR PDBsum; 3TWQ; -.
DR PDBsum; 3TWR; -.
DR PDBsum; 3TWS; -.
DR PDBsum; 3TWT; -.
DR PDBsum; 3TWU; -.
DR PDBsum; 3TWV; -.
DR PDBsum; 3TWW; -.
DR PDBsum; 3TWX; -.
DR PDBsum; 3U9H; -.
DR PDBsum; 3U9Y; -.
DR PDBsum; 3UA9; -.
DR PDBsum; 3W51; -.
DR PDBsum; 4AVU; -.
DR PDBsum; 4AVW; -.
DR PDBsum; 4BFP; -.
DR PDBsum; 4BJ9; -.
DR PDBsum; 4BJB; -.
DR PDBsum; 4BJC; -.
DR PDBsum; 4BS4; -.
DR PDBsum; 4BU3; -.
DR PDBsum; 4BU5; -.
DR PDBsum; 4BU6; -.
DR PDBsum; 4BU7; -.
DR PDBsum; 4BU8; -.
DR PDBsum; 4BU9; -.
DR PDBsum; 4BUA; -.
DR PDBsum; 4BUD; -.
DR PDBsum; 4BUE; -.
DR PDBsum; 4BUF; -.
DR PDBsum; 4BUI; -.
DR PDBsum; 4BUS; -.
DR PDBsum; 4BUT; -.
DR PDBsum; 4BUU; -.
DR PDBsum; 4BUV; -.
DR PDBsum; 4BUW; -.
DR PDBsum; 4BUX; -.
DR PDBsum; 4BUY; -.
DR PDBsum; 4HKI; -.
DR PDBsum; 4HKK; -.
DR PDBsum; 4HKN; -.
DR PDBsum; 4HL5; -.
DR PDBsum; 4HLF; -.
DR PDBsum; 4HLG; -.
DR PDBsum; 4HLH; -.
DR PDBsum; 4HLK; -.
DR PDBsum; 4HLM; -.
DR PDBsum; 4HMH; -.
DR PDBsum; 4HYF; -.
DR PDBsum; 4IUE; -.
DR PDBsum; 4J1Z; -.
DR PDBsum; 4J21; -.
DR PDBsum; 4J22; -.
DR PDBsum; 4J3L; -.
DR PDBsum; 4J3M; -.
DR PDBsum; 4KZL; -.
DR PDBsum; 4KZQ; -.
DR PDBsum; 4KZU; -.
DR PDBsum; 4L09; -.
DR PDBsum; 4L0B; -.
DR PDBsum; 4L0I; -.
DR PDBsum; 4L0S; -.
DR PDBsum; 4L0T; -.
DR PDBsum; 4L0V; -.
DR PDBsum; 4L10; -.
DR PDBsum; 4L2F; -.
DR PDBsum; 4L2G; -.
DR PDBsum; 4L2K; -.
DR PDBsum; 4L31; -.
DR PDBsum; 4L32; -.
DR PDBsum; 4L33; -.
DR PDBsum; 4L34; -.
DR PDBsum; 4M7B; -.
DR PDBsum; 4PML; -.
DR PDBsum; 4PNL; -.
DR PDBsum; 4PNM; -.
DR PDBsum; 4PNN; -.
DR PDBsum; 4PNQ; -.
DR PDBsum; 4PNR; -.
DR PDBsum; 4PNS; -.
DR PDBsum; 4PNT; -.
DR PDBsum; 4TJU; -.
DR PDBsum; 4TJW; -.
DR PDBsum; 4TJY; -.
DR PDBsum; 4TK0; -.
DR PDBsum; 4TK5; -.
DR PDBsum; 4TKF; -.
DR PDBsum; 4TKG; -.
DR PDBsum; 4TKI; -.
DR PDBsum; 4UFU; -.
DR PDBsum; 4UFY; -.
DR PDBsum; 4UHG; -.
DR PDBsum; 4UI3; -.
DR PDBsum; 4UI4; -.
DR PDBsum; 4UI5; -.
DR PDBsum; 4UI6; -.
DR PDBsum; 4UI7; -.
DR PDBsum; 4UI8; -.
DR PDBsum; 4UVL; -.
DR PDBsum; 4UVN; -.
DR PDBsum; 4UVO; -.
DR PDBsum; 4UVP; -.
DR PDBsum; 4UVS; -.
DR PDBsum; 4UVT; -.
DR PDBsum; 4UVU; -.
DR PDBsum; 4UVV; -.
DR PDBsum; 4UVW; -.
DR PDBsum; 4UVX; -.
DR PDBsum; 4UVY; -.
DR PDBsum; 4UVZ; -.
DR PDBsum; 4UX4; -.
DR PDBsum; 4W5I; -.
DR PDBsum; 4Z68; -.
DR PDBsum; 5ADQ; -.
DR PDBsum; 5ADR; -.
DR PDBsum; 5ADS; -.
DR PDBsum; 5ADT; -.
DR PDBsum; 5AEH; -.
DR PDBsum; 5AKU; -.
DR PDBsum; 5AKW; -.
DR PDBsum; 5AL1; -.
DR PDBsum; 5AL2; -.
DR PDBsum; 5AL3; -.
DR PDBsum; 5AL4; -.
DR PDBsum; 5AL5; -.
DR PDBsum; 5BXO; -.
DR PDBsum; 5BXU; -.
DR PDBsum; 5C5P; -.
DR PDBsum; 5C5Q; -.
DR PDBsum; 5C5R; -.
DR PDBsum; 5DCZ; -.
DR PDBsum; 5FPF; -.
DR PDBsum; 5FPG; -.
DR PDBsum; 5JRT; -.
DR PDBsum; 5NOB; -.
DR PDBsum; 5NSP; -.
DR PDBsum; 5NUT; -.
DR PDBsum; 5OWS; -.
DR PDBsum; 5OWT; -.
DR PDBsum; 6TG4; -.
DR PDBsum; 6TKM; -.
DR PDBsum; 6TKN; -.
DR PDBsum; 6TKP; -.
DR PDBsum; 6TKQ; -.
DR PDBsum; 6TKR; -.
DR PDBsum; 6TKS; -.
DR PDBsum; 7A1S; -.
DR PDBsum; 7O6X; -.
DR AlphaFoldDB; Q9H2K2; -.
DR SASBDB; Q9H2K2; -.
DR SMR; Q9H2K2; -.
DR BioGRID; 123257; 55.
DR CORUM; Q9H2K2; -.
DR DIP; DIP-42098N; -.
DR ELM; Q9H2K2; -.
DR IntAct; Q9H2K2; 55.
DR MINT; Q9H2K2; -.
DR STRING; 9606.ENSP00000360689; -.
DR BindingDB; Q9H2K2; -.
DR ChEMBL; CHEMBL6154; -.
DR DrugCentral; Q9H2K2; -.
DR GuidetoPHARMACOLOGY; 3109; -.
DR iPTMnet; Q9H2K2; -.
DR PhosphoSitePlus; Q9H2K2; -.
DR BioMuta; TNKS2; -.
DR DMDM; 20140805; -.
DR EPD; Q9H2K2; -.
DR jPOST; Q9H2K2; -.
DR MassIVE; Q9H2K2; -.
DR MaxQB; Q9H2K2; -.
DR PaxDb; Q9H2K2; -.
DR PeptideAtlas; Q9H2K2; -.
DR PRIDE; Q9H2K2; -.
DR ProteomicsDB; 80559; -.
DR ABCD; Q9H2K2; 2 sequenced antibodies.
DR Antibodypedia; 30362; 223 antibodies from 30 providers.
DR DNASU; 80351; -.
DR Ensembl; ENST00000371627.5; ENSP00000360689.4; ENSG00000107854.6.
DR GeneID; 80351; -.
DR KEGG; hsa:80351; -.
DR MANE-Select; ENST00000371627.5; ENSP00000360689.4; NM_025235.4; NP_079511.1.
DR UCSC; uc001khp.4; human.
DR CTD; 80351; -.
DR DisGeNET; 80351; -.
DR GeneCards; TNKS2; -.
DR HGNC; HGNC:15677; TNKS2.
DR HPA; ENSG00000107854; Low tissue specificity.
DR MIM; 607128; gene.
DR neXtProt; NX_Q9H2K2; -.
DR OpenTargets; ENSG00000107854; -.
DR PharmGKB; PA38019; -.
DR VEuPathDB; HostDB:ENSG00000107854; -.
DR eggNOG; KOG4177; Eukaryota.
DR GeneTree; ENSGT00940000159911; -.
DR HOGENOM; CLU_004303_0_0_1; -.
DR InParanoid; Q9H2K2; -.
DR OMA; YQIIKPE; -.
DR OrthoDB; 111565at2759; -.
DR PhylomeDB; Q9H2K2; -.
DR TreeFam; TF326036; -.
DR PathwayCommons; Q9H2K2; -.
DR Reactome; R-HSA-201681; TCF dependent signaling in response to WNT.
DR Reactome; R-HSA-4641257; Degradation of AXIN.
DR Reactome; R-HSA-5545619; XAV939 stabilizes AXIN.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
DR SignaLink; Q9H2K2; -.
DR SIGNOR; Q9H2K2; -.
DR BioGRID-ORCS; 80351; 5 hits in 1081 CRISPR screens.
DR ChiTaRS; TNKS2; human.
DR EvolutionaryTrace; Q9H2K2; -.
DR GeneWiki; TNKS2; -.
DR GenomeRNAi; 80351; -.
DR Pharos; Q9H2K2; Tchem.
DR PRO; PR:Q9H2K2; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9H2K2; protein.
DR Bgee; ENSG00000107854; Expressed in skeletal muscle tissue of rectus abdominis and 207 other tissues.
DR Genevisible; Q9H2K2; HS.
DR GO; GO:0000781; C:chromosome, telomeric region; IC:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005635; C:nuclear envelope; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0000242; C:pericentriolar material; IDA:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IDA:UniProtKB.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:1904357; P:negative regulation of telomere maintenance via telomere lengthening; IMP:BHF-UCL.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:1904355; P:positive regulation of telomere capping; IDA:BHF-UCL.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IC:BHF-UCL.
DR GO; GO:0006471; P:protein ADP-ribosylation; IDA:BHF-UCL.
DR GO; GO:0070213; P:protein auto-ADP-ribosylation; IDA:UniProtKB.
DR GO; GO:0070198; P:protein localization to chromosome, telomeric region; IMP:BHF-UCL.
DR GO; GO:0070212; P:protein poly-ADP-ribosylation; IDA:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 1.25.40.20; -; 5.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR Pfam; PF00023; Ank; 2.
DR Pfam; PF12796; Ank_2; 5.
DR Pfam; PF13637; Ank_4; 2.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF07647; SAM_2; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 15.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF48403; SSF48403; 3.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 15.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ADP-ribosylation; ANK repeat; Chromosome; Cytoplasm;
KW Glycosyltransferase; Golgi apparatus; Hydroxylation; Membrane;
KW Metal-binding; NAD; Nucleotidyltransferase; Nucleus; Reference proteome;
KW Repeat; Telomere; Transferase; Ubl conjugation; Wnt signaling pathway;
KW Zinc.
FT CHAIN 1..1166
FT /note="Poly [ADP-ribose] polymerase tankyrase-2"
FT /id="PRO_0000211334"
FT REPEAT 57..89
FT /note="ANK 1"
FT REPEAT 90..122
FT /note="ANK 2"
FT REPEAT 123..155
FT /note="ANK 3"
FT REPEAT 210..242
FT /note="ANK 4"
FT REPEAT 243..275
FT /note="ANK 5"
FT REPEAT 276..308
FT /note="ANK 6"
FT REPEAT 363..398
FT /note="ANK 7"
FT REPEAT 399..431
FT /note="ANK 8"
FT REPEAT 432..464
FT /note="ANK 9"
FT REPEAT 525..557
FT /note="ANK 10"
FT REPEAT 558..590
FT /note="ANK 11"
FT REPEAT 591..623
FT /note="ANK 12"
FT REPEAT 678..710
FT /note="ANK 13"
FT REPEAT 711..743
FT /note="ANK 14"
FT REPEAT 744..776
FT /note="ANK 15"
FT DOMAIN 873..936
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 959..1164
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT REGION 545..553
FT /note="HIF1AN-binding"
FT /evidence="ECO:0000269|PubMed:21251231"
FT REGION 819..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..839
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1081
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O95271"
FT BINDING 1084
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O95271"
FT BINDING 1089
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O95271"
FT BINDING 1092
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O95271"
FT MOD_RES 203
FT /note="(3S)-3-hydroxyasparagine; by HIF1AN; partial"
FT /evidence="ECO:0000269|PubMed:18936059"
FT MOD_RES 238
FT /note="(3S)-3-hydroxyhistidine; by HIF1AN; partial"
FT /evidence="ECO:0000269|PubMed:21251231"
FT MOD_RES 271
FT /note="(3S)-3-hydroxyasparagine; by HIF1AN; partial"
FT /evidence="ECO:0000269|PubMed:18936059"
FT MOD_RES 427
FT /note="(3S)-3-hydroxyasparagine; by HIF1AN; partial"
FT /evidence="ECO:0000269|PubMed:18936059"
FT MOD_RES 518
FT /note="(3S)-3-hydroxyasparagine; by HIF1AN; partial"
FT /evidence="ECO:0000269|PubMed:18936059"
FT MOD_RES 553
FT /note="(3S)-3-hydroxyhistidine; by HIF1AN; partial"
FT /evidence="ECO:0000269|PubMed:21251231"
FT MOD_RES 586
FT /note="(3S)-3-hydroxyasparagine; by HIF1AN; partial"
FT /evidence="ECO:0000269|PubMed:18936059"
FT MOD_RES 671
FT /note="(3S)-3-hydroxyasparagine; by HIF1AN; partial"
FT /evidence="ECO:0000269|PubMed:18936059"
FT MOD_RES 706
FT /note="(3S)-3-hydroxyasparagine; by HIF1AN; partial"
FT /evidence="ECO:0000269|PubMed:18936059"
FT MOD_RES 739
FT /note="(3S)-3-hydroxyasparagine; by HIF1AN; partial"
FT /evidence="ECO:0000269|PubMed:18936059"
FT MUTAGEN 553
FT /note="H->D: Enhanced hydroxylation by HIF1AN."
FT /evidence="ECO:0000269|PubMed:21251231"
FT MUTAGEN 553
FT /note="H->N: Enhanced hydroxylation by HIF1AN."
FT /evidence="ECO:0000269|PubMed:21251231"
FT MUTAGEN 1054
FT /note="M->V: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19759537"
FT CONFLICT 115
FT /note="A -> T (in Ref. 7; BAG37180)"
FT /evidence="ECO:0000305"
FT CONFLICT 331..337
FT /note="KGHSLLQ -> QRPLVAA (in Ref. 1; AAG25674)"
FT /evidence="ECO:0000305"
FT CONFLICT 357..361
FT /note="NFKHP -> IQAS (in Ref. 1; AAG25674)"
FT /evidence="ECO:0000305"
FT CONFLICT 966
FT /note="Q -> P (in Ref. 7; BAB14665)"
FT /evidence="ECO:0000305"
FT HELIX 488..502
FT /evidence="ECO:0007829|PDB:5BXO"
FT HELIX 505..511
FT /evidence="ECO:0007829|PDB:5BXO"
FT TURN 514..518
FT /evidence="ECO:0007829|PDB:5BXO"
FT TURN 522..525
FT /evidence="ECO:0007829|PDB:5BXO"
FT HELIX 529..535
FT /evidence="ECO:0007829|PDB:5BXO"
FT HELIX 539..547
FT /evidence="ECO:0007829|PDB:5BXO"
FT HELIX 562..568
FT /evidence="ECO:0007829|PDB:5BXO"
FT HELIX 572..580
FT /evidence="ECO:0007829|PDB:5BXO"
FT HELIX 595..602
FT /evidence="ECO:0007829|PDB:5BXO"
FT HELIX 605..613
FT /evidence="ECO:0007829|PDB:5BXO"
FT HELIX 628..631
FT /evidence="ECO:0007829|PDB:5BXO"
FT HELIX 637..644
FT /evidence="ECO:0007829|PDB:5BXO"
FT HELIX 876..884
FT /evidence="ECO:0007829|PDB:5JRT"
FT HELIX 888..890
FT /evidence="ECO:0007829|PDB:5JRT"
FT HELIX 891..896
FT /evidence="ECO:0007829|PDB:5JRT"
FT HELIX 901..904
FT /evidence="ECO:0007829|PDB:5JRT"
FT HELIX 909..914
FT /evidence="ECO:0007829|PDB:5JRT"
FT HELIX 920..936
FT /evidence="ECO:0007829|PDB:5JRT"
FT STRAND 954..957
FT /evidence="ECO:0007829|PDB:5C5R"
FT HELIX 964..974
FT /evidence="ECO:0007829|PDB:4PNL"
FT TURN 980..986
FT /evidence="ECO:0007829|PDB:4PNL"
FT STRAND 990..999
FT /evidence="ECO:0007829|PDB:4PNL"
FT HELIX 1003..1018
FT /evidence="ECO:0007829|PDB:4PNL"
FT TURN 1019..1021
FT /evidence="ECO:0007829|PDB:4PNL"
FT STRAND 1026..1031
FT /evidence="ECO:0007829|PDB:4PNL"
FT HELIX 1036..1042
FT /evidence="ECO:0007829|PDB:4PNL"
FT HELIX 1046..1048
FT /evidence="ECO:0007829|PDB:4PNL"
FT TURN 1053..1055
FT /evidence="ECO:0007829|PDB:4TJW"
FT STRAND 1059..1064
FT /evidence="ECO:0007829|PDB:4PNL"
FT HELIX 1065..1069
FT /evidence="ECO:0007829|PDB:4PNL"
FT TURN 1070..1073
FT /evidence="ECO:0007829|PDB:4PNL"
FT HELIX 1075..1077
FT /evidence="ECO:0007829|PDB:4PNL"
FT TURN 1082..1084
FT /evidence="ECO:0007829|PDB:4PNL"
FT STRAND 1090..1092
FT /evidence="ECO:0007829|PDB:4PNL"
FT STRAND 1094..1102
FT /evidence="ECO:0007829|PDB:4PNL"
FT STRAND 1105..1109
FT /evidence="ECO:0007829|PDB:4PNL"
FT STRAND 1115..1117
FT /evidence="ECO:0007829|PDB:4PNL"
FT STRAND 1123..1127
FT /evidence="ECO:0007829|PDB:4PNL"
FT STRAND 1131..1133
FT /evidence="ECO:0007829|PDB:4PNL"
FT STRAND 1138..1143
FT /evidence="ECO:0007829|PDB:4PNL"
FT HELIX 1144..1146
FT /evidence="ECO:0007829|PDB:4PNL"
FT STRAND 1147..1157
FT /evidence="ECO:0007829|PDB:4PNL"
SQ SEQUENCE 1166 AA; 126918 MW; 4C8B3B8D97CEF704 CRC64;
MSGRRCAGGG AACASAAAEA VEPAARELFE ACRNGDVERV KRLVTPEKVN SRDTAGRKST
PLHFAAGFGR KDVVEYLLQN GANVQARDDG GLIPLHNACS FGHAEVVNLL LRHGADPNAR
DNWNYTPLHE AAIKGKIDVC IVLLQHGAEP TIRNTDGRTA LDLADPSAKA VLTGEYKKDE
LLESARSGNE EKMMALLTPL NVNCHASDGR KSTPLHLAAG YNRVKIVQLL LQHGADVHAK
DKGDLVPLHN ACSYGHYEVT ELLVKHGACV NAMDLWQFTP LHEAASKNRV EVCSLLLSYG
ADPTLLNCHN KSAIDLAPTP QLKERLAYEF KGHSLLQAAR EADVTRIKKH LSLEMVNFKH
PQTHETALHC AAASPYPKRK QICELLLRKG ANINEKTKEF LTPLHVASEK AHNDVVEVVV
KHEAKVNALD NLGQTSLHRA AYCGHLQTCR LLLSYGCDPN IISLQGFTAL QMGNENVQQL
LQEGISLGNS EADRQLLEAA KAGDVETVKK LCTVQSVNCR DIEGRQSTPL HFAAGYNRVS
VVEYLLQHGA DVHAKDKGGL VPLHNACSYG HYEVAELLVK HGAVVNVADL WKFTPLHEAA
AKGKYEICKL LLQHGADPTK KNRDGNTPLD LVKDGDTDIQ DLLRGDAALL DAAKKGCLAR
VKKLSSPDNV NCRDTQGRHS TPLHLAAGYN NLEVAEYLLQ HGADVNAQDK GGLIPLHNAA
SYGHVDVAAL LIKYNACVNA TDKWAFTPLH EAAQKGRTQL CALLLAHGAD PTLKNQEGQT
PLDLVSADDV SALLTAAMPP SALPSCYKPQ VLNGVRSPGA TADALSSGPS SPSSLSAASS
LDNLSGSFSE LSSVVSSSGT EGASSLEKKE VPGVDFSITQ FVRNLGLEHL MDIFEREQIT
LDVLVEMGHK ELKEIGINAY GHRHKLIKGV ERLISGQQGL NPYLTLNTSG SGTILIDLSP
DDKEFQSVEE EMQSTVREHR DGGHAGGIFN RYNILKIQKV CNKKLWERYT HRRKEVSEEN
HNHANERMLF HGSPFVNAII HKGFDERHAY IGGMFGAGIY FAENSSKSNQ YVYGIGGGTG
CPVHKDRSCY ICHRQLLFCR VTLGKSFLQF SAMKMAHSPP GHHSVTGRPS VNGLALAEYV
IYRGEQAYPE YLITYQIMRP EGMVDG
