Q9H2K2 (TNKS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tankyrase-2
Short name=TANK2
EC=2.4.2.30

Alternative name(s):
ADP-ribosyltransferase diphtheria toxin-like 6
Short name=ARTD6
Poly [ADP-ribose] polymerase 5B
TNKS-2
TRF1-interacting ankyrin-related ADP-ribose polymerase 2
Tankyrase II
Tankyrase-like protein
Tankyrase-related protein

Gene names

Name:	TNKS2
Synonyms:	PARP5B, TANK2, TNKL

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1166 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.5 Ref.9 Ref.11 Ref.13
Catalytic activity	NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor. Ref.11 Ref.13
Enzyme regulation	Specifically inhibited by XAV939, a small molecule, leading to inhibit the Wnt signaling pathway by stabilizing AXIN1 and AXIN2. Ref.11
Subunit structure	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. Ref.5 Ref.10 Ref.11 Ref.13 Ref.14
Subcellular location	Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Nucleus. Chromosome › telomere Potential. 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. Ref.3 Ref.4 Ref.14
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.
Post-translational modification	Ubiquitinated at 'Lys-48' and 'Lys-63' by RNF146 when auto-poly-ADP-ribosylated; this leads to degradation. Ref.13 Ref.14 ADP-ribosylated (-auto). Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination. The crystallographic evidence suggests that the 3-hydroxyhistidine may be the (3S) stereoisomer.
Sequence similarities	Contains 15 ANK repeats. Contains 1 PARP catalytic domain. Contains 1 SAM (sterile alpha motif) domain.
Sequence caution	The sequence AAG25674.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence BAB14665.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Wnt signaling pathway
Cellular component	Chromosome Cytoplasm Golgi apparatus Membrane Nucleus Telomere
Domain	ANK repeat Repeat
Ligand	Metal-binding NAD Zinc
Molecular function	Glycosyltransferase Transferase
PTM	ADP-ribosylation Hydroxylation Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Wnt receptor signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW multicellular organism growth Inferred from electronic annotation. Source: Compara positive regulation of canonical Wnt receptor signaling pathway Inferred from mutant phenotype Ref.11. Source: UniProtKB positive regulation of telomere maintenance via telomerase Inferred by curator Ref.9. Source: BHF-UCL protein auto-ADP-ribosylation Inferred from direct assay Ref.11Ref.13. Source: UniProtKB protein localization to chromosome, telomeric region Inferred from mutant phenotype Ref.9. Source: BHF-UCL protein polyubiquitination Inferred from direct assay Ref.11Ref.13. Source: UniProtKB regulation of multicellular organism growth Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear chromosome, telomeric region Inferred by curator Ref.9. Source: BHF-UCL nuclear envelope Inferred from direct assay Ref.4. Source: BHF-UCL pericentriolar material Inferred from direct assay Ref.4. Source: BHF-UCL perinuclear region of cytoplasm Inferred from direct assay Ref.4. Source: BHF-UCL
Molecular_function	NAD+ ADP-ribosyltransferase activity Inferred from direct assay Ref.11Ref.13. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ANKRD28	O15084	3	EBI-4398527,EBI-359567
AXIN1	O15169	2	EBI-4398527,EBI-710484
BABAM1	Q9NWV8	4	EBI-4398527,EBI-745725
BCR	P11274	3	EBI-4398527,EBI-712838
FAT4	Q6V0I7	2	EBI-4398527,EBI-948985
RAD54L	Q92698	3	EBI-4398527,EBI-5333483
SH3BP2	P78314	5	EBI-4398527,EBI-727062
Sh3bp2	Q06649	6	EBI-4398527,EBI-5323518	From a different organism.
STRN	O43815	2	EBI-4398527,EBI-1046642
TERF1	P54274	2	EBI-4398527,EBI-710997

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1166

1166

Tankyrase-2

PRO_0000211334

Regions

Repeat

57 – 89

33

ANK 1

Repeat

90 – 122

33

ANK 2

Repeat

123 – 155

33

ANK 3

Repeat

210 – 242

33

ANK 4

Repeat

243 – 275

33

ANK 5

Repeat

276 – 308

33

ANK 6

Repeat

363 – 398

36

ANK 7

Repeat

399 – 431

33

ANK 8

Repeat

432 – 464

33

ANK 9

Repeat

525 – 557

33

ANK 10

Repeat

558 – 590

33

ANK 11

Repeat

591 – 623

33

ANK 12

Repeat

678 – 710

33

ANK 13

Repeat

711 – 743

33

ANK 14

Repeat

744 – 776

33

ANK 15

Domain

873 – 936

64

SAM

Domain

959 – 1164

206

PARP catalytic

Region

545 – 553

9

HIF1AN-binding

Sites

Metal binding

1081

1

Zinc By similarity

Metal binding

1084

1

Zinc By similarity

Metal binding

1089

1

Zinc By similarity

Metal binding

1092

1

Zinc By similarity

Amino acid modifications

Modified residue

203

1

(3S)-3-hydroxyasparagine; by HIF1AN; partial Ref.10

Modified residue

238

1

3-hydroxyhistidine; by HIF1AN; partial

Modified residue

271

1

(3S)-3-hydroxyasparagine; by HIF1AN; partial Ref.10

Modified residue

427

1

(3S)-3-hydroxyasparagine; by HIF1AN; partial Ref.10

Modified residue

518

1

(3S)-3-hydroxyasparagine; by HIF1AN; partial Ref.10

Modified residue

553

1

3-hydroxyhistidine; by HIF1AN; partial

Modified residue

586

1

(3S)-3-hydroxyasparagine; by HIF1AN; partial Ref.10

Modified residue

671

1

(3S)-3-hydroxyasparagine; by HIF1AN; partial Ref.10

Modified residue

706

1

(3S)-3-hydroxyasparagine; by HIF1AN; partial Ref.10

Modified residue

739

1

(3S)-3-hydroxyasparagine; by HIF1AN; partial Ref.10

Experimental info

Mutagenesis

553

1

H → D: Enhanced hydroxylation by HIF1AN. Ref.15

Mutagenesis

553

1

H → N: Enhanced hydroxylation by HIF1AN. Ref.15

Mutagenesis

1054

1

M → V: Loss of activity. Ref.11

Sequence conflict

115

1

A → T in BAG37180. Ref.7

Sequence conflict

331 – 337

7

KGHSLLQ → QRPLVAA in AAG25674. Ref.1

Sequence conflict

357 – 361

5

NFKHP → IQAS in AAG25674. Ref.1

Sequence conflict

966

1

Q → P in BAB14665. Ref.7

Secondary structure

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1166

Helix Strand Turn

Details...

Helix

491 – 502

12

Helix

505 – 511

7

Turn

514 – 518

5

Turn

522 – 525

4

Helix

529 – 535

7

Helix

539 – 547

9

Helix

562 – 568

7

Helix

572 – 580

9

Helix

595 – 601

7

Helix

605 – 613

9

Helix

629 – 631

3

Helix

637 – 644

8

Beta strand

954 – 957

4

Helix

963 – 974

12

Turn

980 – 986

7

Beta strand

992 – 1001

10

Helix

1003 – 1018

16

Turn

1019 – 1022

4

Beta strand

1026 – 1031

6

Helix

1036 – 1042

7

Helix

1046 – 1048

3

Beta strand

1057 – 1064

8

Helix

1065 – 1069

5

Turn

1070 – 1073

4

Helix

1075 – 1077

3

Turn

1082 – 1084

3

Beta strand

1090 – 1092

3

Beta strand

1094 – 1102

9

Beta strand

1105 – 1111

7

Beta strand

1123 – 1131

9

Beta strand

1138 – 1142

5

Helix

1144 – 1146

3

Beta strand

1147 – 1157

11

Sequences

	Sequence		Length	Mass (Da)
	Q9H2K2 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 4C8B3B8D97CEF704	FASTA	1,166	126,918
	10 20 30 40 50 60 MSGRRCAGGG AACASAAAEA VEPAARELFE ACRNGDVERV KRLVTPEKVN SRDTAGRKST 70 80 90 100 110 120 PLHFAAGFGR KDVVEYLLQN GANVQARDDG GLIPLHNACS FGHAEVVNLL LRHGADPNAR 130 140 150 160 170 180 DNWNYTPLHE AAIKGKIDVC IVLLQHGAEP TIRNTDGRTA LDLADPSAKA VLTGEYKKDE 190 200 210 220 230 240 LLESARSGNE EKMMALLTPL NVNCHASDGR KSTPLHLAAG YNRVKIVQLL LQHGADVHAK 250 260 270 280 290 300 DKGDLVPLHN ACSYGHYEVT ELLVKHGACV NAMDLWQFTP LHEAASKNRV EVCSLLLSYG 310 320 330 340 350 360 ADPTLLNCHN KSAIDLAPTP QLKERLAYEF KGHSLLQAAR EADVTRIKKH LSLEMVNFKH 370 380 390 400 410 420 PQTHETALHC AAASPYPKRK QICELLLRKG ANINEKTKEF LTPLHVASEK AHNDVVEVVV 430 440 450 460 470 480 KHEAKVNALD NLGQTSLHRA AYCGHLQTCR LLLSYGCDPN IISLQGFTAL QMGNENVQQL 490 500 510 520 530 540 LQEGISLGNS EADRQLLEAA KAGDVETVKK LCTVQSVNCR DIEGRQSTPL HFAAGYNRVS 550 560 570 580 590 600 VVEYLLQHGA DVHAKDKGGL VPLHNACSYG HYEVAELLVK HGAVVNVADL WKFTPLHEAA 610 620 630 640 650 660 AKGKYEICKL LLQHGADPTK KNRDGNTPLD LVKDGDTDIQ DLLRGDAALL DAAKKGCLAR 670 680 690 700 710 720 VKKLSSPDNV NCRDTQGRHS TPLHLAAGYN NLEVAEYLLQ HGADVNAQDK GGLIPLHNAA 730 740 750 760 770 780 SYGHVDVAAL LIKYNACVNA TDKWAFTPLH EAAQKGRTQL CALLLAHGAD PTLKNQEGQT 790 800 810 820 830 840 PLDLVSADDV SALLTAAMPP SALPSCYKPQ VLNGVRSPGA TADALSSGPS SPSSLSAASS 850 860 870 880 890 900 LDNLSGSFSE LSSVVSSSGT EGASSLEKKE VPGVDFSITQ FVRNLGLEHL MDIFEREQIT 910 920 930 940 950 960 LDVLVEMGHK ELKEIGINAY GHRHKLIKGV ERLISGQQGL NPYLTLNTSG SGTILIDLSP 970 980 990 1000 1010 1020 DDKEFQSVEE EMQSTVREHR DGGHAGGIFN RYNILKIQKV CNKKLWERYT HRRKEVSEEN 1030 1040 1050 1060 1070 1080 HNHANERMLF HGSPFVNAII HKGFDERHAY IGGMFGAGIY FAENSSKSNQ YVYGIGGGTG 1090 1100 1110 1120 1130 1140 CPVHKDRSCY ICHRQLLFCR VTLGKSFLQF SAMKMAHSPP GHHSVTGRPS VNGLALAEYV 1150 1160 IYRGEQAYPE YLITYQIMRP EGMVDG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Novel tankyrase-related gene detected with meningioma-specific sera." Monz D., Munnia A., Comtesse N., Fischer U., Steudel W.-I., Feiden W., Glass B., Meese E.U. Clin. Cancer Res. 7:113-119(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fetal brain.
[2]	"Cloning and characterization of TNKL, a member of tankyrase gene family." Kuimov A.N., Kuprash D.V., Petrov V.N., Vdovichenko K.K., Scanlan M.J., Jongeneel C.V., Lagarkova M.A., Nedospasov S.A. Genes Immun. 2:52-55(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Mammary carcinoma.
[3]	"Identification of a novel human tankyrase through its interaction with the adaptor protein Grb14." Lyons R.J., Deane R., Lynch D.K., Ye Z.-S.J., Sanderson G.M., Eyre H.J., Sutherland G.R., Daly R.J. J. Biol. Chem. 276:17172-17180(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION. Tissue: Liver.
[4]	"TANK2, a new TRF1-associated poly(ADP-ribose) polymerase, causes rapid induction of cell death upon overexpression." Kaminker P.G., Kim S.-H., Taylor R.D., Zebarjadian Y., Funk W.D., Morin G.B., Yaswen P., Campisi J. J. Biol. Chem. 276:35891-35899(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION. Tissue: Placenta.
[5]	"Tankyrase-2 oligomerizes with tankyrase-1 and binds to both TRF1 (telomere-repeat-binding factor 1) and IRAP (insulin-responsive aminopeptidase)." Sbodio J.I., Lodish H.F., Chi N.-W. Biochem. J. 361:451-459(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH TRF1 AND LNPEP/OTASE. Tissue: Skeletal muscle.
[6]	Yin Y., Gelmann E.P. Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[7]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta and Testis.
[8]	"The DNA sequence and comparative analysis of human chromosome 10." 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. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"Role for the related poly(ADP-Ribose) polymerases tankyrase 1 and 2 at human telomeres." Cook B.D., Dynek J.N., Chang W., Shostak G., Smith S. Mol. Cell. Biol. 22:332-342(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ADP-RIBOSYLATION.
[10]	"Proteomics-based identification of novel factor inhibiting hypoxia-inducible factor (FIH) substrates indicates widespread asparaginyl hydroxylation of ankyrin repeat domain-containing proteins." Cockman M.E., Webb J.D., Kramer H.B., Kessler B.M., Ratcliffe P.J. Mol. Cell. Proteomics 8:535-546(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HIF1AN, HYDROXYLATION AT ASN-203; ASN-271; ASN-427; ASN-518; ASN-586; ASN-671; ASN-706 AND ASN-739.
[11]	"Tankyrase inhibition stabilizes axin and antagonizes Wnt signalling." 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. Nature 461:614-620(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, INTERACTION WITH AXIN1 AND AXIN2, MUTAGENESIS OF MET-1054.
[12]	"Toward a unified nomenclature for mammalian ADP-ribosyltransferases." Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F. Trends Biochem. Sci. 35:208-219(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NOMENCLATURE.
[13]	"RNF146 is a poly(ADP-ribose)-directed E3 ligase that regulates axin degradation and Wnt signalling." 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. Nat. Cell Biol. 13:623-629(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH AXIN1; AXIN2; BLZF1 AND CASC3, UBIQUITINATION.
[14]	"Ubiquitin ligase RNF146 regulates tankyrase and Axin to promote Wnt signaling." 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. PLoS ONE 6:E22595-E22595(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RNF146, UBIQUITINATION, SUBCELLULAR LOCATION.
[15]	"Factor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-translational hydroxylation of histidinyl residues within ankyrin repeat domains." 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. FEBS J. 278:1086-1097(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 538-558 IN COMPLEX WITH HIF1AN; IRON AND 2-OXOGLUTARATE, HYDROXYLATION AT HIS-238 AND HIS-553, MUTAGENESIS OF HIS-553.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF305081 mRNA. Translation: AAG25674.1. Different initiation.
AF264912 mRNA. Translation: AAG44694.1.
AF329696 mRNA. Translation: AAK13463.1.
AF342982 mRNA. Translation: AAK25811.1.
AF309033 mRNA. Translation: AAK82330.1.
AF438201 mRNA. Translation: AAL40795.1.
AK023746 mRNA. Translation: BAB14665.1. Different initiation.
AK314612 mRNA. Translation: BAG37180.1.
AL359707 Genomic DNA. Translation: CAC78760.1.

IPI

IPI00019270.

RefSeq

NP_079511.1. NM_025235.3.

UniGene

Hs.329327.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2Y0I	X-ray	2.28	S	538-558	[»]
3KR7	X-ray	1.95	A	946-1162	[»]
3KR8	X-ray	2.10	A/C	946-1162	[»]
3MHJ	X-ray	1.80	A/B	946-1162	[»]
3MHK	X-ray	2.30	A	952-1166	[»]
3P0N	X-ray	1.90	A/C	946-1162	[»]
3P0P	X-ray	2.49	A/C	946-1162	[»]
3P0Q	X-ray	1.90	A/C	946-1162	[»]
3TWQ	X-ray	2.15	A/B	484-655	[»]
3TWR	X-ray	1.55	A/B/C/D	488-649	[»]
3TWS	X-ray	1.70	A/B/C/D	488-649	[»]
3TWT	X-ray	1.85	A/B/C/D	488-649	[»]
3TWU	X-ray	1.80	A	488-649	[»]
3TWV	X-ray	2.30	A/B/C/D	488-649	[»]
3TWW	X-ray	2.00	A/B	488-649	[»]
3TWX	X-ray	1.80	A/B	488-649	[»]
3U9H	X-ray	1.75	A/B	946-1162	[»]
3U9Y	X-ray	2.30	A	946-1162	[»]
3UA9	X-ray	2.15	A/B	946-1162	[»]
4AVU	X-ray	2.40	A/B	946-1162	[»]
4AVW	X-ray	2.15	A/B	946-1162	[»]
4HKI	X-ray	2.15	A/H	946-1113	[»]
			C/D	1114-1162	[»]
4HKK	X-ray	1.95	A/C	946-1113	[»]
			B/D	1114-1162	[»]
4HKN	X-ray	2.05	A	946-1113	[»]
			C	1114-1162	[»]
4HL5	X-ray	2.20	A	946-1113	[»]
			C	1114-1162	[»]
4HLF	X-ray	2.15	A/B	946-1113	[»]
			C/D	1114-1162	[»]
4HLG	X-ray	2.00	A/B	946-1113	[»]
			C/D	1114-1162	[»]
4HLH	X-ray	1.75	A/B	946-1113	[»]
			C/D	1114-1162	[»]
4HLK	X-ray	2.00	A/B	946-1113	[»]
			C/D	1114-1162	[»]
4HLM	X-ray	1.95	A/B	946-1113	[»]
			C/D	1114-1162	[»]
4HMH	X-ray	2.30	A	946-1113	[»]
			C	1114-1162	[»]
4HYF	X-ray	2.80	A/B/C	946-1162	[»]

ProteinModelPortal

Q9H2K2.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-42098N.

IntAct

Q9H2K2. 30 interactions.

MINT

MINT-1183420.

STRING

9606.ENSP00000360689.

PTM databases

PhosphoSite

Q9H2K2.

Polymorphism databases

DMDM

20140805.

Proteomic databases

PaxDb

Q9H2K2.

PRIDE

Q9H2K2.

Protocols and materials databases

DNASU

80351.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000371627; ENSP00000360689; ENSG00000107854.

GeneID

80351.

KEGG

hsa:80351.

UCSC

uc001khp.3. human.

Organism-specific databases

CTD

80351.

GeneCards

GC10P093548.

HGNC

HGNC:15677. TNKS2.

HPA

HPA036606.

MIM

607128. gene.

neXtProt

NX_Q9H2K2.

PharmGKB

PA38019.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0666.

HOGENOM

HOG000246964.

HOVERGEN

HBG059472.

InParanoid

Q9H2K2.

KO

K10799.

OMA

NSDADRQ.

OrthoDB

EOG45MN4H.

PhylomeDB

Q9H2K2.

Gene expression databases

Bgee

Q9H2K2.

CleanEx

HS_TNKS2.

Genevestigator

Q9H2K2.

GermOnline

ENSG00000107854. Homo sapiens.

Family and domain databases

Gene3D

1.10.150.50. 1 hit.
1.25.40.20. 7 hits.
3.90.228.10. 1 hit.

InterPro

IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR011510. SAM_2.
[Graphical view]

Pfam

PF00023. Ank. 2 hits.
PF12796. Ank_2. 5 hits.
PF00644. PARP. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view]

PRINTS

PR01415. ANKYRIN.

SMART

SM00248. ANK. 15 hits.
SM00454. SAM. 1 hit.
[Graphical view]

SUPFAM

SSF48403. ANK. 3 hits.
SSF47769. SAM_homology. 1 hit.

PROSITE

PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 15 hits.
PS51059. PARP_CATALYTIC. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q9H2K2.

ChEMBL

CHEMBL6154.

ChiTaRS

TNKS2. human.

EvolutionaryTrace

Q9H2K2.

GenomeRNAi

80351.

NextBio

70966.

SOURCE

Search...

Entry information

Entry name

TNKS2_HUMAN

Accession

Primary (citable) accession number: Q9H2K2
Secondary accession number(s): B2RBD3, Q9H8F2, Q9HAS4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 27, 2002
Last sequence update:	March 1, 2001
Last modified:	May 29, 2013
This is version 124 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.