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Tankyrase-2 (TANK2) (EC 2.4.2.30) (ADP-ribosyltransferase diphtheria toxin-like 6) (ARTD6) (TNKS-2) (TRF1-interacting ankyrin-related ADP-ribose polymerase 2) (Tankyrase II)

 TNKS2_MOUSE             Reviewed;        1166 AA.
Q3UES3; Q6P537; Q8BXH7;
31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
31-MAY-2011, sequence version 2.
28-FEB-2018, entry version 115.
RecName: Full=Tankyrase-2;
Short=TANK2;
EC=2.4.2.30;
AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 6;
Short=ARTD6;
AltName: Full=TNKS-2;
AltName: Full=TRF1-interacting ankyrin-related ADP-ribose polymerase 2;
AltName: Full=Tankyrase II;
Name=Tnks2; Synonyms=Tank2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Cerebellum, and Liver;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 759-1166.
TISSUE=Embryo;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- 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 (By
similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: NAD(+) + (ADP-D-ribosyl)(n)-acceptor =
nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.
{ECO:0000255|PROSITE-ProRule:PRU00397}.
-!- ENZYME REGULATION: Specifically inhibited by XAV939, a small
molecule, leading to inhibit the Wnt signaling pathway by
stabilizing AXIN1 and AXIN2. {ECO:0000250}.
-!- SUBUNIT: Oligomerizes and associates with TNKS. Interacts with the
cytoplasmic domain of LNPEP/Otase in SLC2A4/GLUT4-vesicles. Binds
to the N-terminus of Grb14 and TRF1 with its ankyrin repeat
region. Interacts with HIF1AN. Interacts with RNF146; this
interaction leads to ubiquitination and proteasomal degradation.
Interacts with NUMA1 (By similarity).
{ECO:0000250|UniProtKB:Q9H2K2}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus
membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
-!- PTM: Ubiquitinated by RNF146 when auto-poly-ADP-ribosylated,
leading to its degradation. {ECO:0000250}.
-!- PTM: ADP-ribosylated (-auto). Poly-ADP-ribosylated protein is
recognized by RNF146, followed by ubiquitination (By similarity).
{ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; AK047094; BAC32960.2; -; mRNA.
EMBL; AK149368; BAE28838.1; -; mRNA.
EMBL; AC116128; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC063101; AAH63101.1; -; mRNA.
CCDS; CCDS50426.1; -.
RefSeq; NP_001157107.1; NM_001163635.1.
UniGene; Mm.249310; -.
ProteinModelPortal; Q3UES3; -.
SMR; Q3UES3; -.
BioGrid; 216798; 18.
CORUM; Q3UES3; -.
IntAct; Q3UES3; 18.
STRING; 10090.ENSMUSP00000025729; -.
BindingDB; Q3UES3; -.
ChEMBL; CHEMBL3232703; -.
iPTMnet; Q3UES3; -.
PhosphoSitePlus; Q3UES3; -.
SwissPalm; Q3UES3; -.
MaxQB; Q3UES3; -.
PaxDb; Q3UES3; -.
PRIDE; Q3UES3; -.
Ensembl; ENSMUST00000025729; ENSMUSP00000025729; ENSMUSG00000024811.
GeneID; 74493; -.
KEGG; mmu:74493; -.
UCSC; uc008hhu.2; mouse.
CTD; 80351; -.
MGI; MGI:1921743; Tnks2.
eggNOG; KOG4177; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00840000129677; -.
HOGENOM; HOG000246964; -.
HOVERGEN; HBG059472; -.
InParanoid; Q3UES3; -.
KO; K10799; -.
OMA; KRKQVCE; -.
OrthoDB; EOG091G00W8; -.
TreeFam; TF326036; -.
Reactome; R-MMU-201681; TCF dependent signaling in response to WNT.
Reactome; R-MMU-4641257; Degradation of AXIN.
Reactome; R-MMU-5689880; Ub-specific processing proteases.
Reactome; R-MMU-8948751; Regulation of PTEN stability and activity.
ChiTaRS; Tnks2; mouse.
PRO; PR:Q3UES3; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000024811; -.
ExpressionAtlas; Q3UES3; baseline and differential.
Genevisible; Q3UES3; MM.
GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0005635; C:nuclear envelope; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0000242; C:pericentriolar material; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; ISS:UniProtKB.
GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
GO; GO:1904357; P:negative regulation of telomere maintenance via telomere lengthening; ISO:MGI.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
GO; GO:1904355; P:positive regulation of telomere capping; ISO:MGI.
GO; GO:0006471; P:protein ADP-ribosylation; ISO:MGI.
GO; GO:0070213; P:protein auto-ADP-ribosylation; ISS:UniProtKB.
GO; GO:0070198; P:protein localization to chromosome, telomeric region; ISO:MGI.
GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
GO; GO:0040014; P:regulation of multicellular organism growth; IMP:MGI.
GO; GO:0000723; P:telomere maintenance; ISS:MGI.
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; 3.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 15.
PROSITE; PS51059; PARP_CATALYTIC; 1.
PROSITE; PS50105; SAM_DOMAIN; 1.
2: Evidence at transcript level;
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_0000409512.
REPEAT 23 52 ANK 1.
REPEAT 57 86 ANK 2.
REPEAT 90 119 ANK 3.
REPEAT 123 152 ANK 4.
REPEAT 210 239 ANK 5.
REPEAT 243 272 ANK 6.
REPEAT 276 305 ANK 7.
REPEAT 363 395 ANK 8.
REPEAT 399 428 ANK 9.
REPEAT 432 461 ANK 10.
REPEAT 463 489 ANK 11.
REPEAT 525 554 ANK 12.
REPEAT 558 587 ANK 13.
REPEAT 591 620 ANK 14.
REPEAT 624 652 ANK 15.
REPEAT 678 707 ANK 16.
REPEAT 711 740 ANK 17.
REPEAT 744 773 ANK 18.
DOMAIN 873 936 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
DOMAIN 959 1164 PARP catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00397}.
REGION 545 553 HIF1AN-binding. {ECO:0000250}.
COMPBIAS 826 858 Ser-rich.
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.
{ECO:0000250}.
MOD_RES 238 238 (3S)-3-hydroxyhistidine; by HIF1AN.
{ECO:0000250}.
MOD_RES 271 271 (3S)-3-hydroxyasparagine; by HIF1AN.
{ECO:0000250}.
MOD_RES 427 427 (3S)-3-hydroxyasparagine; by HIF1AN.
{ECO:0000250}.
MOD_RES 518 518 (3S)-3-hydroxyasparagine; by HIF1AN.
{ECO:0000250}.
MOD_RES 553 553 (3S)-3-hydroxyhistidine; by HIF1AN.
{ECO:0000250}.
MOD_RES 586 586 (3S)-3-hydroxyasparagine; by HIF1AN.
{ECO:0000250}.
MOD_RES 671 671 (3S)-3-hydroxyasparagine; by HIF1AN.
{ECO:0000250}.
MOD_RES 706 706 (3S)-3-hydroxyasparagine; by HIF1AN.
{ECO:0000250}.
MOD_RES 739 739 (3S)-3-hydroxyasparagine; by HIF1AN.
{ECO:0000250}.
CONFLICT 116 116 D -> H (in Ref. 1; BAC32960).
{ECO:0000305}.
CONFLICT 178 178 K -> E (in Ref. 1; BAC32960).
{ECO:0000305}.
CONFLICT 220 220 G -> E (in Ref. 1; BAC32960).
{ECO:0000305}.
CONFLICT 809 809 P -> T (in Ref. 1; BAE28838).
{ECO:0000305}.
SEQUENCE 1166 AA; 126744 MW; 5C1E11B74BB11FC9 CRC64;
MSGRRCAGGG AACASAGAEA VEPSARELFE ACRNGDVERV KRLVTPEKVN SRDTAGRKST
PLHFAAGFGR KDVVEYLLQN GANVQARDDG GLIPLHNACS FGHAEVVNLL LQHGADPNAR
DNWNYTPLHE AAIKGKIDVC IVLLQHGAEP TIRNTDGRTA LDLADPSAKA VLTGDYKKDE
LLESARSGNE EKMMALLTPL NVNCHASDGR KSTPLHLAAG YNRVKIVQLL LHHGADVHAK
DKGDLVPLHN ACSYGHYEVT ELLVKHGACV NAMDLWQFTP LHEAASKNRI EVCSLLLSYG
ADPTLLNCHN KSAIDLAPTA QLKERLSYEF KGHSLLQAAR EADVTRIKKH LSLEMVNFKH
PQTHETALHC AAASPYPKRK QICELLLRKG ANTNEKTKEF LTPLHVASEN AHNDVVEVVV
KHEAKVNALD SLGQTSLHRA AHCGHLQTCR LLLSYGCDPN IISLQGFTAL QMGNENVQQL
LQEGASLGHS 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 SALPTCYKPQ VLSGVRGPGA TADALSSGPS SPSSLSAASS
LDNLSGSFSE LSAVVSSSAA EGATGLQRKE DSGIDFSITQ FIRNLGLEHL MDIFEREQIT
LDVLVEMGHK ELKEIGINAY GHRHKLIKGV ERLISGQQGL NPYLTLNNSG SGTILIDLSP
DDKEFQSVEE EMQSTVREHR DGGHAGGVFN RYNILKIQKV CNKKLWERYT HRRKEVSEEN
HNHANERMLF HGSPFVNAII HKGFDERHAY IGGMFGAGIY FAENSSKSNQ YVYGIGGGTG
CPIHKDRSCY ICHRQLLFCR VTLGKSFLQF SAMKMAHSPP GHHSVTGRPS VNGLALAEYV
IYRGEQAYPE YLITYQIVRP EGMVDG


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