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Tankyrase-2 (TANK2) (EC 2.4.2.30) (ADP-ribosyltransferase diphtheria toxin-like 6) (ARTD6) (Poly [ADP-ribose] polymerase 5B) (TNKS-2) (TRF1-interacting ankyrin-related ADP-ribose polymerase 2) (Tankyrase II) (Tankyrase-like protein) (Tankyrase-related protein)

 TNKS2_HUMAN             Reviewed;        1166 AA.
Q9H2K2; B2RBD3; Q9H8F2; Q9HAS4;
27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
12-SEP-2018, entry version 181.
RecName: Full=Tankyrase-2;
Short=TANK2;
EC=2.4.2.30;
AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 6;
Short=ARTD6;
AltName: Full=Poly [ADP-ribose] polymerase 5B;
AltName: Full=TNKS-2;
AltName: Full=TRF1-interacting ankyrin-related ADP-ribose polymerase 2;
AltName: Full=Tankyrase II;
AltName: Full=Tankyrase-like protein;
AltName: Full=Tankyrase-related protein;
Name=TNKS2; Synonyms=PARP5B, TANK2, TNKL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fetal brain;
PubMed=11205898;
Monz D., Munnia A., Comtesse N., Fischer U., Steudel W.-I., Feiden W.,
Glass B., Meese E.U.;
"Novel tankyrase-related gene detected with meningioma-specific
sera.";
Clin. Cancer Res. 7:113-119(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Mammary carcinoma;
PubMed=11294570; DOI=10.1038/sj.gene.6363722;
Kuimov A.N., Kuprash D.V., Petrov V.N., Vdovichenko K.K.,
Scanlan M.J., Jongeneel C.V., Lagarkova M.A., Nedospasov S.A.;
"Cloning and characterization of TNKL, a member of tankyrase gene
family.";
Genes Immun. 2:52-55(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
TISSUE=Liver;
PubMed=11278563; DOI=10.1074/jbc.M009756200;
Lyons R.J., Deane R., Lynch D.K., Ye Z.-S.J., Sanderson G.M.,
Eyre H.J., Sutherland G.R., Daly R.J.;
"Identification of a novel human tankyrase through its interaction
with the adaptor protein Grb14.";
J. Biol. Chem. 276:17172-17180(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
TISSUE=Placenta;
PubMed=11454873; DOI=10.1074/jbc.M105968200;
Kaminker P.G., Kim S.-H., Taylor R.D., Zebarjadian Y., Funk W.D.,
Morin G.B., Yaswen P., Campisi J.;
"TANK2, a new TRF1-associated poly(ADP-ribose) polymerase, causes
rapid induction of cell death upon overexpression.";
J. Biol. Chem. 276:35891-35899(2001).
[5]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH TRF1 AND
LNPEP/OTASE.
TISSUE=Skeletal muscle;
PubMed=11802774; DOI=10.1042/0264-6021:3610451;
Sbodio J.I., Lodish H.F., Chi N.-W.;
"Tankyrase-2 oligomerizes with tankyrase-1 and binds to both TRF1
(telomere-repeat-binding factor 1) and IRAP (insulin-responsive
aminopeptidase).";
Biochem. J. 361:451-459(2002).
[6]
NUCLEOTIDE SEQUENCE [MRNA].
Yin Y., Gelmann E.P.;
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta, and Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[9]
INTERACTION WITH NUMA1.
PubMed=12080061; DOI=10.1074/jbc.M203916200;
Sbodio J.I., Chi N.W.;
"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. 277:31887-31892(2002).
[10]
FUNCTION, AND ADP-RIBOSYLATION.
PubMed=11739745; DOI=10.1128/MCB.22.1.332-342.2002;
Cook B.D., Dynek J.N., Chang W., Shostak G., Smith S.;
"Role for the related poly(ADP-Ribose) polymerases tankyrase 1 and 2
at human telomeres.";
Mol. Cell. Biol. 22:332-342(2002).
[11]
INTERACTION WITH HIF1AN, AND HYDROXYLATION AT ASN-203; ASN-271;
ASN-427; ASN-518; ASN-586; ASN-671; ASN-706 AND ASN-739.
PubMed=18936059; DOI=10.1074/mcp.M800340-MCP200;
Cockman M.E., Webb J.D., Kramer H.B., Kessler B.M., Ratcliffe P.J.;
"Proteomics-based identification of novel factor inhibiting hypoxia-
inducible factor (FIH) substrates indicates widespread asparaginyl
hydroxylation of ankyrin repeat domain-containing proteins.";
Mol. Cell. Proteomics 8:535-546(2009).
[12]
FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH
AXIN1 AND AXIN2, AND MUTAGENESIS OF MET-1054.
PubMed=19759537; DOI=10.1038/nature08356;
Huang S.M., Mishina Y.M., Liu S., Cheung A., Stegmeier F.,
Michaud G.A., Charlat O., Wiellette E., Zhang Y., Wiessner S.,
Hild M., Shi X., Wilson C.J., Mickanin C., Myer V., Fazal A.,
Tomlinson R., Serluca F., Shao W., Cheng H., Shultz M., Rau C.,
Schirle M., Schlegl J., Ghidelli S., Fawell S., Lu C., Curtis D.,
Kirschner M.W., Lengauer C., Finan P.M., Tallarico J.A.,
Bouwmeester T., Porter J.A., Bauer A., Cong F.;
"Tankyrase inhibition stabilizes axin and antagonizes Wnt
signalling.";
Nature 461:614-620(2009).
[13]
NOMENCLATURE.
PubMed=20106667; DOI=10.1016/j.tibs.2009.12.003;
Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.;
"Toward a unified nomenclature for mammalian ADP-
ribosyltransferases.";
Trends Biochem. Sci. 35:208-219(2010).
[14]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH AXIN1; AXIN2; BLZF1 AND
CASC3, AND UBIQUITINATION.
PubMed=21478859; DOI=10.1038/ncb2222;
Zhang Y., Liu S., Mickanin C., Feng Y., Charlat O., Michaud G.A.,
Schirle M., Shi X., Hild M., Bauer A., Myer V.E., Finan P.M.,
Porter J.A., Huang S.M., Cong F.;
"RNF146 is a poly(ADP-ribose)-directed E3 ligase that regulates axin
degradation and Wnt signalling.";
Nat. Cell Biol. 13:623-629(2011).
[15]
INTERACTION WITH RNF146, UBIQUITINATION, AND SUBCELLULAR LOCATION.
PubMed=21799911; DOI=10.1371/journal.pone.0022595;
Callow M.G., Tran H., Phu L., Lau T., Lee J., Sandoval W.N., Liu P.S.,
Bheddah S., Tao J., Lill J.R., Hongo J.A., Davis D., Kirkpatrick D.S.,
Polakis P., Costa M.;
"Ubiquitin ligase RNF146 regulates tankyrase and Axin to promote Wnt
signaling.";
PLoS ONE 6:E22595-E22595(2011).
[16]
FUNCTION.
PubMed=23622245; DOI=10.1016/j.cell.2013.03.040;
Cho-Park P.F., Steller H.;
"Proteasome regulation by ADP-ribosylation.";
Cell 153:614-627(2013).
[17]
X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 538-558 IN COMPLEX WITH
HIF1AN; IRON AND 2-OXOGLUTARATE, HYDROXYLATION AT HIS-238 AND HIS-553,
AND MUTAGENESIS OF HIS-553.
PubMed=21251231; DOI=10.1111/j.1742-4658.2011.08022.x;
Yang M., Chowdhury R., Ge W., Hamed R.B., McDonough M.A.,
Claridge T.D., Kessler B.M., Cockman M.E., Ratcliffe P.J.,
Schofield C.J.;
"Factor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-
translational hydroxylation of histidinyl residues within ankyrin
repeat domains.";
FEBS J. 278:1086-1097(2011).
-!- 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 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 poly-ADP-ribosylation of BLZF1 and CASC3, followed by
recruitment of RNF146 and subsequent ubiquitination. Mediates
poly-ADP-ribosylation of TERF1, thereby contributing to the
regulation of telomere length. May also regulate vesicle
trafficking and modulate the subcellular distribution of
SLC2A4/GLUT4-vesicles. Stimulates 26S proteasome activity.
{ECO:0000269|PubMed:11739745, ECO:0000269|PubMed:11802774,
ECO:0000269|PubMed:19759537, ECO:0000269|PubMed:21478859,
ECO:0000269|PubMed:23622245}.
-!- CATALYTIC ACTIVITY: NAD(+) + (ADP-D-ribosyl)(n)-acceptor =
nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.
{ECO:0000255|PROSITE-ProRule:PRU00397,
ECO:0000269|PubMed:19759537, ECO:0000269|PubMed:21478859}.
-!- ACTIVITY REGULATION: Specifically inhibited by XAV939, a small
molecule, leading to inhibit the Wnt signaling pathway by
stabilizing AXIN1 and AXIN2. {ECO:0000269|PubMed:19759537}.
-!- SUBUNIT: Oligomerizes and associates with TNKS. Interacts with the
cytoplasmic domain of LNPEP/Otase in SLC2A4/GLUT4-vesicles
(PubMed:11802774). Binds to the N-terminus of Grb14 and TRF1 with
its ankyrin repeat region (PubMed:11802774). Interacts with HIF1AN
(PubMed:18936059, PubMed:21251231). Interacts with RNF146; this
interaction leads to ubiquitination and proteasomal degradation
(PubMed:21799911). Interacts with NUMA1 (PubMed:12080061).
{ECO:0000269|PubMed:11802774, ECO:0000269|PubMed:12080061,
ECO:0000269|PubMed:18936059, ECO:0000269|PubMed:19759537,
ECO:0000269|PubMed:21251231, ECO:0000269|PubMed:21478859,
ECO:0000269|PubMed:21799911}.
-!- INTERACTION:
O15084:ANKRD28; NbExp=3; IntAct=EBI-4398527, EBI-359567;
Q7Z6K5-1:ARPIN; NbExp=5; IntAct=EBI-4398527, EBI-16079078;
O15169:AXIN1; NbExp=2; IntAct=EBI-4398527, EBI-710484;
Q9NWV8:BABAM1; NbExp=4; IntAct=EBI-4398527, EBI-745725;
P11274:BCR; NbExp=3; IntAct=EBI-4398527, EBI-712838;
Q6V0I7:FAT4; NbExp=2; IntAct=EBI-4398527, EBI-948985;
Q9NWT6:HIF1AN; NbExp=4; IntAct=EBI-4398527, EBI-745632;
Q92698:RAD54L; NbExp=3; IntAct=EBI-4398527, EBI-5333483;
P78314:SH3BP2; NbExp=5; IntAct=EBI-4398527, EBI-727062;
Q06649:Sh3bp2 (xeno); NbExp=6; IntAct=EBI-4398527, EBI-5323518;
O43815:STRN; NbExp=2; IntAct=EBI-4398527, EBI-1046642;
P54274:TERF1; NbExp=2; IntAct=EBI-4398527, EBI-710997;
-!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane;
Peripheral membrane protein. Nucleus. Chromosome, telomere
{ECO:0000305}. Note=Associated with the Golgi and with
juxtanuclear SLC2A4/GLUT4-vesicles. Also found around the
pericentriolar matrix of mitotic centromeres. During interphase, a
small fraction of TNKS2 is found in the nucleus, associated with
TRF1.
-!- TISSUE SPECIFICITY: Highly expressed in placenta, skeletal muscle,
liver, brain, kidney, heart, thymus, spinal cord, lung, peripheral
blood leukocytes, pancreas, lymph nodes, spleen, prostate, testis,
ovary, small intestine, colon, mammary gland, breast and breast
carcinoma, and in common-type meningioma. Highly expressed in
fetal liver, heart and brain.
-!- PTM: Ubiquitinated at 'Lys-48' and 'Lys-63' by RNF146 when auto-
poly-ADP-ribosylated; this leads to degradation.
-!- PTM: ADP-ribosylated (-auto). Poly-ADP-ribosylated protein is
recognized by RNF146, followed by ubiquitination.
-!- PTM: The crystallographic evidence suggests that the 3-
hydroxyhistidine may be the (3S) stereoisomer.
-!- SEQUENCE CAUTION:
Sequence=AAG25674.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAB14665.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AF305081; AAG25674.1; ALT_INIT; mRNA.
EMBL; AF264912; AAG44694.1; -; mRNA.
EMBL; AF329696; AAK13463.1; -; mRNA.
EMBL; AF342982; AAK25811.1; -; mRNA.
EMBL; AF309033; AAK82330.1; -; mRNA.
EMBL; AF438201; AAL40795.1; -; mRNA.
EMBL; AK023746; BAB14665.1; ALT_INIT; mRNA.
EMBL; AK314612; BAG37180.1; -; mRNA.
EMBL; AL359707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS7417.1; -.
RefSeq; NP_079511.1; NM_025235.3.
UniGene; Hs.329327; -.
PDB; 2Y0I; X-ray; 2.28 A; S=538-558.
PDB; 3KR7; X-ray; 1.95 A; A=946-1162.
PDB; 3KR8; X-ray; 2.10 A; A/C=946-1162.
PDB; 3MHJ; X-ray; 1.80 A; A/B=946-1162.
PDB; 3MHK; X-ray; 2.30 A; A=952-1166.
PDB; 3P0N; X-ray; 1.90 A; A/C=946-1162.
PDB; 3P0P; X-ray; 2.49 A; A/C=946-1162.
PDB; 3P0Q; X-ray; 1.90 A; A/C=946-1162.
PDB; 3TWQ; X-ray; 2.15 A; A/B=484-655.
PDB; 3TWR; X-ray; 1.55 A; A/B/C/D=488-649.
PDB; 3TWS; X-ray; 1.70 A; A/B/C/D=488-649.
PDB; 3TWT; X-ray; 1.85 A; A/B/C/D=488-649.
PDB; 3TWU; X-ray; 1.80 A; A=488-649.
PDB; 3TWV; X-ray; 2.30 A; A/B/C/D=488-649.
PDB; 3TWW; X-ray; 2.00 A; A/B=488-649.
PDB; 3TWX; X-ray; 1.80 A; A/B=488-649.
PDB; 3U9H; X-ray; 1.75 A; A/B=946-1162.
PDB; 3U9Y; X-ray; 2.30 A; A=946-1162.
PDB; 3UA9; X-ray; 2.15 A; A/B=946-1162.
PDB; 3W51; X-ray; 2.00 A; A/B=952-1161.
PDB; 4AVU; X-ray; 2.40 A; A/B=946-1162.
PDB; 4AVW; X-ray; 2.15 A; A/B=946-1162.
PDB; 4BFP; X-ray; 2.40 A; A/B=946-1162.
PDB; 4BJ9; X-ray; 2.05 A; A/B=946-1162.
PDB; 4BJB; X-ray; 2.30 A; A=946-1162.
PDB; 4BJC; X-ray; 2.20 A; A=946-1162.
PDB; 4BS4; X-ray; 1.89 A; A/B=946-1162.
PDB; 4BU3; X-ray; 2.15 A; A/B=946-1162.
PDB; 4BU5; X-ray; 1.80 A; A/B=946-1162.
PDB; 4BU6; X-ray; 1.80 A; A/B=946-1162.
PDB; 4BU7; X-ray; 2.05 A; A/C=946-1162.
PDB; 4BU8; X-ray; 1.85 A; A/C=946-1162.
PDB; 4BU9; X-ray; 1.65 A; A/B=946-1162.
PDB; 4BUA; X-ray; 1.85 A; A/C=946-1162.
PDB; 4BUD; X-ray; 2.50 A; A/C=946-1162.
PDB; 4BUE; X-ray; 1.60 A; A/B=946-1162.
PDB; 4BUF; X-ray; 2.50 A; A/B=946-1162.
PDB; 4BUI; X-ray; 1.95 A; A/C=946-1162.
PDB; 4BUS; X-ray; 1.90 A; A/B=946-1162.
PDB; 4BUT; X-ray; 1.90 A; A/B=946-1162.
PDB; 4BUU; X-ray; 1.60 A; A/B=946-1162.
PDB; 4BUV; X-ray; 1.80 A; A/C=946-1162.
PDB; 4BUW; X-ray; 1.85 A; A/B=946-1162.
PDB; 4BUX; X-ray; 1.95 A; A/C=946-1162.
PDB; 4BUY; X-ray; 1.90 A; A/B=946-1162.
PDB; 4HKI; X-ray; 2.15 A; A/H=946-1113, C/D=1114-1162.
PDB; 4HKK; X-ray; 1.95 A; A/C=946-1113, B/D=1114-1162.
PDB; 4HKN; X-ray; 2.05 A; A=946-1113, C=1114-1162.
PDB; 4HL5; X-ray; 2.20 A; A=946-1113, C=1114-1162.
PDB; 4HLF; X-ray; 2.15 A; A/B=946-1113, C/D=1114-1162.
PDB; 4HLG; X-ray; 2.00 A; A/B=946-1113, C/D=1114-1162.
PDB; 4HLH; X-ray; 1.75 A; A/B=946-1113, C/D=1114-1162.
PDB; 4HLK; X-ray; 2.00 A; A/B=946-1113, C/D=1114-1162.
PDB; 4HLM; X-ray; 1.95 A; A/B=946-1113, C/D=1114-1162.
PDB; 4HMH; X-ray; 2.30 A; A=946-1113, C=1114-1162.
PDB; 4HYF; X-ray; 2.80 A; A/B/C=946-1162.
PDB; 4IUE; X-ray; 2.38 A; A=952-1161.
PDB; 4J1Z; X-ray; 2.00 A; A/B=952-1161.
PDB; 4J21; X-ray; 1.93 A; A=952-1161.
PDB; 4J22; X-ray; 2.12 A; A/B=952-1161.
PDB; 4J3L; X-ray; 2.09 A; A=952-1161.
PDB; 4J3M; X-ray; 1.90 A; A/B=952-1161.
PDB; 4KZL; X-ray; 2.00 A; A/B=946-1113, C/D=1114-1162.
PDB; 4KZQ; X-ray; 2.25 A; A/B=946-1113, C/D=1114-1162.
PDB; 4KZU; X-ray; 2.10 A; A/B=946-1113, C/D=1114-1162.
PDB; 4L09; X-ray; 2.05 A; A/B=946-1113, C/D=1114-1162.
PDB; 4L0B; X-ray; 1.80 A; A/B=946-1113, C/D=1114-1162.
PDB; 4L0I; X-ray; 2.30 A; A/B=946-1113, C/D=1114-1162.
PDB; 4L0S; X-ray; 1.90 A; A/B=946-1113, C/D=1114-1162.
PDB; 4L0T; X-ray; 2.10 A; A/B=946-1113, C/D=1114-1162.
PDB; 4L0V; X-ray; 1.70 A; A/B=946-1113, C/D=1114-1162.
PDB; 4L10; X-ray; 1.70 A; A/B=946-1113, C/D=1114-1162.
PDB; 4L2F; X-ray; 2.05 A; A/B=946-1113, C/D=1114-1162.
PDB; 4L2G; X-ray; 2.05 A; A/B=946-1113, C/D=1114-1162.
PDB; 4L2K; X-ray; 2.10 A; A/B=946-1113, C/D=1114-1162.
PDB; 4L31; X-ray; 2.00 A; A/B=946-1113, C/D=1114-1162.
PDB; 4L32; X-ray; 1.85 A; A/B=946-1113, C/D=1114-1162.
PDB; 4L33; X-ray; 2.10 A; A/B=946-1113, C/D=1114-1162.
PDB; 4L34; X-ray; 1.80 A; A/B=946-1113, C/D=1114-1162.
PDB; 4M7B; X-ray; 1.95 A; A/C=946-1162.
PDB; 4PML; X-ray; 1.87 A; A/B/C/D=959-1164.
PDB; 4PNL; X-ray; 1.50 A; A/B/C/D=959-1164.
PDB; 4PNM; X-ray; 2.19 A; A/B/C/D=959-1164.
PDB; 4PNN; X-ray; 1.65 A; A/B/C/D=959-1164.
PDB; 4PNQ; X-ray; 1.85 A; A/B/C/D=959-1164.
PDB; 4PNR; X-ray; 1.71 A; A/B/C/D=959-1164.
PDB; 4PNS; X-ray; 1.65 A; A/B/C/D=959-1164.
PDB; 4PNT; X-ray; 1.60 A; A/B/C/D=959-1164.
PDB; 4TJU; X-ray; 1.57 A; A/B/C/D=959-1164.
PDB; 4TJW; X-ray; 1.70 A; A/B/C/D=959-1164.
PDB; 4TJY; X-ray; 1.90 A; A/B/C/D=959-1164.
PDB; 4TK0; X-ray; 1.65 A; A/B/C/D=959-1164.
PDB; 4TK5; X-ray; 2.02 A; A/B/C/D=959-1164.
PDB; 4TKF; X-ray; 2.60 A; A/B/C/D=959-1164.
PDB; 4TKG; X-ray; 1.95 A; A/B/C/D=959-1164.
PDB; 4TKI; X-ray; 2.15 A; A/B/C/D=959-1164.
PDB; 4UFU; X-ray; 2.10 A; A/B=946-1162.
PDB; 4UFY; X-ray; 1.70 A; A/B=946-1162.
PDB; 4UHG; X-ray; 1.70 A; A/B=946-1162.
PDB; 4UI3; X-ray; 2.00 A; A/B=946-1113, C/D=1115-1162.
PDB; 4UI4; X-ray; 2.40 A; A/B=946-1113, C/D=1115-1162.
PDB; 4UI5; X-ray; 1.65 A; A/B=946-1113, C/D=1115-1162.
PDB; 4UI6; X-ray; 1.80 A; A/B=946-1113, C/D=1115-1162.
PDB; 4UI7; X-ray; 1.80 A; A/B=946-1113, C/D=1115-1162.
PDB; 4UI8; X-ray; 2.05 A; A/B=946-1113, C/D=1115-1162.
PDB; 4UVL; X-ray; 2.00 A; A/C=946-1162.
PDB; 4UVN; X-ray; 2.20 A; A/B=946-1162.
PDB; 4UVO; X-ray; 1.85 A; A/B=946-1162.
PDB; 4UVP; X-ray; 1.75 A; A/C=946-1113, B/D=1115-1162.
PDB; 4UVS; X-ray; 2.00 A; A/C=946-1162.
PDB; 4UVT; X-ray; 1.95 A; A/C=946-1162.
PDB; 4UVU; X-ray; 1.95 A; A/B=946-1162.
PDB; 4UVV; X-ray; 1.90 A; A/B=946-1162.
PDB; 4UVW; X-ray; 2.10 A; A/B=946-1162.
PDB; 4UVX; X-ray; 1.95 A; A/B=946-1162.
PDB; 4UVY; X-ray; 1.95 A; A/B=946-1162.
PDB; 4UVZ; X-ray; 1.60 A; A/C=946-1162.
PDB; 4UX4; X-ray; 1.80 A; A/B=946-1162.
PDB; 4W5I; X-ray; 1.95 A; A/B=952-1162.
PDB; 4Z68; X-ray; 1.86 A; A=490-644.
PDB; 5ADQ; X-ray; 2.10 A; A=946-1113, B=1115-1162.
PDB; 5ADR; X-ray; 2.10 A; A=946-1113, B=1115-1162.
PDB; 5ADS; X-ray; 1.80 A; A=946-1113, B=1115-1162.
PDB; 5ADT; X-ray; 2.15 A; A=946-1113, B=1115-1162.
PDB; 5AEH; X-ray; 1.85 A; A/B=946-1162.
PDB; 5AKU; X-ray; 1.80 A; A/B=946-1162.
PDB; 5AKW; X-ray; 2.07 A; A/B=946-1162.
PDB; 5AL1; X-ray; 1.75 A; A/B=946-1162.
PDB; 5AL2; X-ray; 1.90 A; A/B=946-1162.
PDB; 5AL3; X-ray; 1.75 A; A/B=946-1162.
PDB; 5AL4; X-ray; 1.90 A; A/B=946-1162.
PDB; 5AL5; X-ray; 2.05 A; A/B=946-1162.
PDB; 5BXO; X-ray; 1.33 A; A/B=488-649.
PDB; 5BXU; X-ray; 1.35 A; A=488-649.
PDB; 5C5P; X-ray; 1.75 A; A/B=946-1113, C/D=1114-1162.
PDB; 5C5Q; X-ray; 2.00 A; A/B=946-1113, C/D=1114-1162.
PDB; 5C5R; X-ray; 1.55 A; A/B=946-1113, C/D=1114-1162.
PDB; 5DCZ; X-ray; 2.23 A; A=936-1166.
PDB; 5FPF; X-ray; 2.60 A; A/B=946-1113, C/D=1115-1162.
PDB; 5FPG; X-ray; 2.75 A; A/B=946-1162.
PDB; 5JRT; X-ray; 1.53 A; A=867-940.
PDB; 5NOB; X-ray; 1.85 A; A/B=946-1162.
PDB; 5NSP; X-ray; 2.30 A; A/B=946-1113, C/D=1114-1162.
PDB; 5NUT; X-ray; 1.60 A; A/B=952-1162.
PDB; 5OWS; X-ray; 1.80 A; A/B=946-1162.
PDB; 5OWT; X-ray; 2.20 A; A/B=946-1162.
PDBsum; 2Y0I; -.
PDBsum; 3KR7; -.
PDBsum; 3KR8; -.
PDBsum; 3MHJ; -.
PDBsum; 3MHK; -.
PDBsum; 3P0N; -.
PDBsum; 3P0P; -.
PDBsum; 3P0Q; -.
PDBsum; 3TWQ; -.
PDBsum; 3TWR; -.
PDBsum; 3TWS; -.
PDBsum; 3TWT; -.
PDBsum; 3TWU; -.
PDBsum; 3TWV; -.
PDBsum; 3TWW; -.
PDBsum; 3TWX; -.
PDBsum; 3U9H; -.
PDBsum; 3U9Y; -.
PDBsum; 3UA9; -.
PDBsum; 3W51; -.
PDBsum; 4AVU; -.
PDBsum; 4AVW; -.
PDBsum; 4BFP; -.
PDBsum; 4BJ9; -.
PDBsum; 4BJB; -.
PDBsum; 4BJC; -.
PDBsum; 4BS4; -.
PDBsum; 4BU3; -.
PDBsum; 4BU5; -.
PDBsum; 4BU6; -.
PDBsum; 4BU7; -.
PDBsum; 4BU8; -.
PDBsum; 4BU9; -.
PDBsum; 4BUA; -.
PDBsum; 4BUD; -.
PDBsum; 4BUE; -.
PDBsum; 4BUF; -.
PDBsum; 4BUI; -.
PDBsum; 4BUS; -.
PDBsum; 4BUT; -.
PDBsum; 4BUU; -.
PDBsum; 4BUV; -.
PDBsum; 4BUW; -.
PDBsum; 4BUX; -.
PDBsum; 4BUY; -.
PDBsum; 4HKI; -.
PDBsum; 4HKK; -.
PDBsum; 4HKN; -.
PDBsum; 4HL5; -.
PDBsum; 4HLF; -.
PDBsum; 4HLG; -.
PDBsum; 4HLH; -.
PDBsum; 4HLK; -.
PDBsum; 4HLM; -.
PDBsum; 4HMH; -.
PDBsum; 4HYF; -.
PDBsum; 4IUE; -.
PDBsum; 4J1Z; -.
PDBsum; 4J21; -.
PDBsum; 4J22; -.
PDBsum; 4J3L; -.
PDBsum; 4J3M; -.
PDBsum; 4KZL; -.
PDBsum; 4KZQ; -.
PDBsum; 4KZU; -.
PDBsum; 4L09; -.
PDBsum; 4L0B; -.
PDBsum; 4L0I; -.
PDBsum; 4L0S; -.
PDBsum; 4L0T; -.
PDBsum; 4L0V; -.
PDBsum; 4L10; -.
PDBsum; 4L2F; -.
PDBsum; 4L2G; -.
PDBsum; 4L2K; -.
PDBsum; 4L31; -.
PDBsum; 4L32; -.
PDBsum; 4L33; -.
PDBsum; 4L34; -.
PDBsum; 4M7B; -.
PDBsum; 4PML; -.
PDBsum; 4PNL; -.
PDBsum; 4PNM; -.
PDBsum; 4PNN; -.
PDBsum; 4PNQ; -.
PDBsum; 4PNR; -.
PDBsum; 4PNS; -.
PDBsum; 4PNT; -.
PDBsum; 4TJU; -.
PDBsum; 4TJW; -.
PDBsum; 4TJY; -.
PDBsum; 4TK0; -.
PDBsum; 4TK5; -.
PDBsum; 4TKF; -.
PDBsum; 4TKG; -.
PDBsum; 4TKI; -.
PDBsum; 4UFU; -.
PDBsum; 4UFY; -.
PDBsum; 4UHG; -.
PDBsum; 4UI3; -.
PDBsum; 4UI4; -.
PDBsum; 4UI5; -.
PDBsum; 4UI6; -.
PDBsum; 4UI7; -.
PDBsum; 4UI8; -.
PDBsum; 4UVL; -.
PDBsum; 4UVN; -.
PDBsum; 4UVO; -.
PDBsum; 4UVP; -.
PDBsum; 4UVS; -.
PDBsum; 4UVT; -.
PDBsum; 4UVU; -.
PDBsum; 4UVV; -.
PDBsum; 4UVW; -.
PDBsum; 4UVX; -.
PDBsum; 4UVY; -.
PDBsum; 4UVZ; -.
PDBsum; 4UX4; -.
PDBsum; 4W5I; -.
PDBsum; 4Z68; -.
PDBsum; 5ADQ; -.
PDBsum; 5ADR; -.
PDBsum; 5ADS; -.
PDBsum; 5ADT; -.
PDBsum; 5AEH; -.
PDBsum; 5AKU; -.
PDBsum; 5AKW; -.
PDBsum; 5AL1; -.
PDBsum; 5AL2; -.
PDBsum; 5AL3; -.
PDBsum; 5AL4; -.
PDBsum; 5AL5; -.
PDBsum; 5BXO; -.
PDBsum; 5BXU; -.
PDBsum; 5C5P; -.
PDBsum; 5C5Q; -.
PDBsum; 5C5R; -.
PDBsum; 5DCZ; -.
PDBsum; 5FPF; -.
PDBsum; 5FPG; -.
PDBsum; 5JRT; -.
PDBsum; 5NOB; -.
PDBsum; 5NSP; -.
PDBsum; 5NUT; -.
PDBsum; 5OWS; -.
PDBsum; 5OWT; -.
ProteinModelPortal; Q9H2K2; -.
SMR; Q9H2K2; -.
BioGrid; 123257; 30.
CORUM; Q9H2K2; -.
DIP; DIP-42098N; -.
ELM; Q9H2K2; -.
IntAct; Q9H2K2; 34.
MINT; Q9H2K2; -.
STRING; 9606.ENSP00000360689; -.
BindingDB; Q9H2K2; -.
ChEMBL; CHEMBL6154; -.
iPTMnet; Q9H2K2; -.
PhosphoSitePlus; Q9H2K2; -.
BioMuta; TNKS2; -.
DMDM; 20140805; -.
EPD; Q9H2K2; -.
MaxQB; Q9H2K2; -.
PaxDb; Q9H2K2; -.
PeptideAtlas; Q9H2K2; -.
PRIDE; Q9H2K2; -.
ProteomicsDB; 80559; -.
DNASU; 80351; -.
Ensembl; ENST00000371627; ENSP00000360689; ENSG00000107854.
GeneID; 80351; -.
KEGG; hsa:80351; -.
UCSC; uc001khp.4; human.
CTD; 80351; -.
DisGeNET; 80351; -.
EuPathDB; HostDB:ENSG00000107854.5; -.
GeneCards; TNKS2; -.
HGNC; HGNC:15677; TNKS2.
HPA; HPA036606; -.
MIM; 607128; gene.
neXtProt; NX_Q9H2K2; -.
OpenTargets; ENSG00000107854; -.
PharmGKB; PA38019; -.
eggNOG; KOG4177; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00840000129677; -.
HOGENOM; HOG000246964; -.
HOVERGEN; HBG059472; -.
InParanoid; Q9H2K2; -.
KO; K10799; -.
OMA; KRKQVCE; -.
OrthoDB; EOG091G00W8; -.
PhylomeDB; Q9H2K2; -.
TreeFam; TF326036; -.
Reactome; R-HSA-201681; TCF dependent signaling in response to WNT.
Reactome; R-HSA-4641257; Degradation of AXIN.
Reactome; R-HSA-5545619; XAV939 inhibits tankyrase, stabilizing AXIN.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
SIGNOR; Q9H2K2; -.
ChiTaRS; TNKS2; human.
EvolutionaryTrace; Q9H2K2; -.
GeneWiki; TNKS2; -.
GenomeRNAi; 80351; -.
PRO; PR:Q9H2K2; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000107854; Expressed in 233 organ(s), highest expression level in skeletal muscle tissue of rectus abdominis.
CleanEx; HS_TNKS2; -.
Genevisible; Q9H2K2; HS.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IC:BHF-UCL.
GO; GO:0005635; C:nuclear envelope; IDA:BHF-UCL.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0000242; C:pericentriolar material; IDA:BHF-UCL.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IDA:UniProtKB.
GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
GO; GO:1904357; P:negative regulation of telomere maintenance via telomere lengthening; IMP:BHF-UCL.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
GO; GO:1904355; P:positive regulation of telomere capping; IDA:BHF-UCL.
GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IC:BHF-UCL.
GO; GO:0006471; P:protein ADP-ribosylation; IDA:BHF-UCL.
GO; GO:0070213; P:protein auto-ADP-ribosylation; IDA:UniProtKB.
GO; GO:0070198; P:protein localization to chromosome, telomeric region; IMP:BHF-UCL.
GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
CDD; cd00204; ANK; 5.
Gene3D; 1.25.40.20; -; 5.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed_sf.
Pfam; PF00023; Ank; 1.
Pfam; PF12796; Ank_2; 5.
Pfam; PF00644; PARP; 1.
Pfam; PF07647; SAM_2; 1.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 15.
SMART; SM00454; SAM; 1.
SUPFAM; SSF47769; SSF47769; 1.
SUPFAM; SSF48403; SSF48403; 4.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 15.
PROSITE; PS51059; PARP_CATALYTIC; 1.
PROSITE; PS50105; SAM_DOMAIN; 1.
1: Evidence at protein level;
3D-structure; ADP-ribosylation; ANK repeat; Chromosome;
Complete proteome; Cytoplasm; Glycosyltransferase; Golgi apparatus;
Hydroxylation; Membrane; Metal-binding; NAD; Nucleus;
Reference proteome; Repeat; Telomere; Transferase; Ubl conjugation;
Wnt signaling pathway; Zinc.
CHAIN 1 1166 Tankyrase-2.
/FTId=PRO_0000211334.
REPEAT 57 89 ANK 1.
REPEAT 90 122 ANK 2.
REPEAT 123 155 ANK 3.
REPEAT 210 242 ANK 4.
REPEAT 243 275 ANK 5.
REPEAT 276 308 ANK 6.
REPEAT 363 398 ANK 7.
REPEAT 399 431 ANK 8.
REPEAT 432 464 ANK 9.
REPEAT 525 557 ANK 10.
REPEAT 558 590 ANK 11.
REPEAT 591 623 ANK 12.
REPEAT 678 710 ANK 13.
REPEAT 711 743 ANK 14.
REPEAT 744 776 ANK 15.
DOMAIN 873 936 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
DOMAIN 959 1164 PARP catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00397}.
REGION 545 553 HIF1AN-binding.
METAL 1081 1081 Zinc. {ECO:0000250|UniProtKB:O95271}.
METAL 1084 1084 Zinc. {ECO:0000250|UniProtKB:O95271}.
METAL 1089 1089 Zinc. {ECO:0000250|UniProtKB:O95271}.
METAL 1092 1092 Zinc. {ECO:0000250|UniProtKB:O95271}.
MOD_RES 203 203 (3S)-3-hydroxyasparagine; by HIF1AN;
partial. {ECO:0000269|PubMed:18936059}.
MOD_RES 238 238 (3S)-3-hydroxyhistidine; by HIF1AN;
partial. {ECO:0000269|PubMed:21251231}.
MOD_RES 271 271 (3S)-3-hydroxyasparagine; by HIF1AN;
partial. {ECO:0000269|PubMed:18936059}.
MOD_RES 427 427 (3S)-3-hydroxyasparagine; by HIF1AN;
partial. {ECO:0000269|PubMed:18936059}.
MOD_RES 518 518 (3S)-3-hydroxyasparagine; by HIF1AN;
partial. {ECO:0000269|PubMed:18936059}.
MOD_RES 553 553 (3S)-3-hydroxyhistidine; by HIF1AN;
partial. {ECO:0000269|PubMed:21251231}.
MOD_RES 586 586 (3S)-3-hydroxyasparagine; by HIF1AN;
partial. {ECO:0000269|PubMed:18936059}.
MOD_RES 671 671 (3S)-3-hydroxyasparagine; by HIF1AN;
partial. {ECO:0000269|PubMed:18936059}.
MOD_RES 706 706 (3S)-3-hydroxyasparagine; by HIF1AN;
partial. {ECO:0000269|PubMed:18936059}.
MOD_RES 739 739 (3S)-3-hydroxyasparagine; by HIF1AN;
partial. {ECO:0000269|PubMed:18936059}.
MUTAGEN 553 553 H->D: Enhanced hydroxylation by HIF1AN.
{ECO:0000269|PubMed:21251231}.
MUTAGEN 553 553 H->N: Enhanced hydroxylation by HIF1AN.
{ECO:0000269|PubMed:21251231}.
MUTAGEN 1054 1054 M->V: Loss of activity.
{ECO:0000269|PubMed:19759537}.
CONFLICT 115 115 A -> T (in Ref. 7; BAG37180).
{ECO:0000305}.
CONFLICT 331 337 KGHSLLQ -> QRPLVAA (in Ref. 1; AAG25674).
{ECO:0000305}.
CONFLICT 357 361 NFKHP -> IQAS (in Ref. 1; AAG25674).
{ECO:0000305}.
CONFLICT 966 966 Q -> P (in Ref. 7; BAB14665).
{ECO:0000305}.
HELIX 488 502 {ECO:0000244|PDB:5BXO}.
HELIX 505 511 {ECO:0000244|PDB:5BXO}.
TURN 514 518 {ECO:0000244|PDB:5BXO}.
TURN 522 525 {ECO:0000244|PDB:5BXO}.
HELIX 529 535 {ECO:0000244|PDB:5BXO}.
HELIX 539 547 {ECO:0000244|PDB:5BXO}.
HELIX 562 568 {ECO:0000244|PDB:5BXO}.
HELIX 572 580 {ECO:0000244|PDB:5BXO}.
HELIX 595 602 {ECO:0000244|PDB:5BXO}.
HELIX 605 613 {ECO:0000244|PDB:5BXO}.
HELIX 628 631 {ECO:0000244|PDB:5BXO}.
HELIX 637 644 {ECO:0000244|PDB:5BXO}.
HELIX 876 884 {ECO:0000244|PDB:5JRT}.
HELIX 888 890 {ECO:0000244|PDB:5JRT}.
HELIX 891 896 {ECO:0000244|PDB:5JRT}.
HELIX 901 904 {ECO:0000244|PDB:5JRT}.
HELIX 909 914 {ECO:0000244|PDB:5JRT}.
HELIX 920 936 {ECO:0000244|PDB:5JRT}.
STRAND 954 957 {ECO:0000244|PDB:5C5R}.
HELIX 964 974 {ECO:0000244|PDB:4PNL}.
TURN 980 986 {ECO:0000244|PDB:4PNL}.
STRAND 990 999 {ECO:0000244|PDB:4PNL}.
HELIX 1003 1018 {ECO:0000244|PDB:4PNL}.
TURN 1019 1021 {ECO:0000244|PDB:4PNL}.
STRAND 1026 1031 {ECO:0000244|PDB:4PNL}.
HELIX 1036 1042 {ECO:0000244|PDB:4PNL}.
HELIX 1046 1048 {ECO:0000244|PDB:4PNL}.
TURN 1053 1055 {ECO:0000244|PDB:4TJW}.
STRAND 1059 1064 {ECO:0000244|PDB:4PNL}.
HELIX 1065 1069 {ECO:0000244|PDB:4PNL}.
TURN 1070 1073 {ECO:0000244|PDB:4PNL}.
HELIX 1075 1077 {ECO:0000244|PDB:4PNL}.
TURN 1082 1084 {ECO:0000244|PDB:4PNL}.
STRAND 1090 1092 {ECO:0000244|PDB:4PNL}.
STRAND 1094 1102 {ECO:0000244|PDB:4PNL}.
STRAND 1105 1109 {ECO:0000244|PDB:4PNL}.
STRAND 1115 1117 {ECO:0000244|PDB:4PNL}.
STRAND 1123 1127 {ECO:0000244|PDB:4PNL}.
STRAND 1131 1133 {ECO:0000244|PDB:4PNL}.
STRAND 1138 1143 {ECO:0000244|PDB:4PNL}.
HELIX 1144 1146 {ECO:0000244|PDB:4PNL}.
STRAND 1147 1157 {ECO:0000244|PDB:4PNL}.
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


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