O95271 (TNKS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tankyrase-1
Short name=TANK1
EC=2.4.2.30

Alternative name(s):
ADP-ribosyltransferase diphtheria toxin-like 5
Short name=ARTD5
Poly [ADP-ribose] polymerase 5A
TNKS-1
TRF1-interacting ankyrin-related ADP-ribose polymerase
Tankyrase I

Gene names

Name:	TNKS
Synonyms:	PARP5A, PARPL, TIN1, TINF1, TNKS1

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	1327 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 (PARsylation) of AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex: poly-ADP-ribosylated target proteins are recognized by RNF146, which mediates their ubiquitination and subsequent degradation. Also mediates PARsylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates PARsylation of TERF1, thereby contributing to the regulation of telomere length. Involved in centrosome maturation during prometaphase by mediating PARsylation of HEPACAM2/MIKI. May also regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles. May be involved in spindle pole assembly through PARsylation of NUMA1. Ref.5 Ref.6 Ref.8 Ref.10 Ref.12 Ref.14
Catalytic activity	NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor. Ref.10
Enzyme regulation	Specifically inhibited by XAV939, a small molecule, leading to inhibit the Wnt signaling pathway by stabilizing AXIN1 and AXIN2. Ref.10
Subunit structure	Oligomerizes and associates with TNKS2. Interacts with the cytoplasmic domain of LNPEP/Otase in SLC2A4/GLUT4-vesicles. Binds to the N-terminus of telomeric TERF1 via the ANK repeats. Found in a complex with POT1; TERF1 and TINF2. Interacts with AXIN1, AXIN2, BLZF1 and CASC3. Ref.7 Ref.10 Ref.12 Ref.13
Subcellular location	Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Chromosome › centromere. Nucleus › nuclear pore complex. Chromosome › telomere Potential. Cytoplasm › cytoskeleton › spindle pole. Note: Associated with the Golgi and with juxtanuclear SLC2A4/GLUT4-vesicles. A minor proportion is also found at nuclear pore complexes and around the pericentriolar matrix of mitotic centromeres. During interphase, a small fraction of TNKS is found in the nucleus, associated with TERF1. Localizes to spindle poles at mitosis onset via interaction with NUMA1. Ref.4 Ref.8 Ref.13 Ref.14
Tissue specificity	Ubiquitous; highest levels in testis.
Post-translational modification	Phosphorylated on serine residues by MAPK kinases upon insulin stimulation. Phosphorylated during mitosis. Ref.5 Ubiquitinated by RNF146 when auto-poly-ADP-ribosylated, leading to its degradation. Ref.12 ADP-ribosylated (-auto). Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination.
Sequence similarities	Contains 15 ANK repeats. Contains 1 PARP catalytic domain. Contains 1 SAM (sterile alpha motif) domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis Protein transport Translocation Transport Wnt signaling pathway mRNA transport
Cellular component	Centromere Chromosome Cytoplasm Cytoskeleton Golgi apparatus Membrane Nuclear pore complex Nucleus Telomere
Coding sequence diversity	Alternative splicing
Domain	ANK repeat Repeat
Ligand	Metal-binding NAD Zinc
Molecular function	Glycosyltransferase Transferase
PTM	ADP-ribosylation Phosphoprotein 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 cell division Inferred from electronic annotation. Source: UniProtKB-KW mRNA transport Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW mitotic spindle organization Traceable author statement PubMed 17026964. Source: BHF-UCL negative regulation of DNA binding Inferred from direct assay Ref.1. Source: BHF-UCL peptidyl-serine phosphorylation Inferred from direct assay PubMed 17026964. Source: MGI peptidyl-threonine phosphorylation Inferred from direct assay PubMed 17026964. Source: MGI positive regulation of canonical Wnt receptor signaling pathway Inferred from mutant phenotype Ref.10. Source: UniProtKB positive regulation of telomere maintenance via telomerase Inferred from direct assay PubMed 18221737. Source: BHF-UCL positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 19245366. Source: UniProtKB protein auto-ADP-ribosylation Inferred from direct assay Ref.10Ref.12. Source: UniProtKB protein localization to chromosome, telomeric region Inferred from mutant phenotype PubMed 18221737. Source: BHF-UCL protein poly-ADP-ribosylation Inferred from direct assay Ref.1. Source: BHF-UCL protein polyubiquitination Inferred from direct assay Ref.10Ref.12. Source: UniProtKB protein transport Inferred from electronic annotation. Source: UniProtKB-KW spindle assembly Traceable author statement PubMed 17026964. Source: BHF-UCL
Cellular_component	Golgi apparatus Inferred from direct assay Ref.14. Source: UniProtKB Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell chromosome, centromeric region Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear chromosome, telomeric region Inferred from direct assay Ref.6. Source: BHF-UCL nuclear membrane Traceable author statement PubMed 11454873. Source: BHF-UCL nuclear pore Traceable author statement PubMed 11454873. Source: BHF-UCL pericentriolar material Traceable author statement PubMed 11454873. Source: BHF-UCL spindle pole Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	NAD+ ADP-ribosyltransferase activity Inferred from direct assay Ref.10Ref.12Ref.14Ref.1. Source: UniProtKB zinc ion binding Inferred from direct assay Ref.15. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Axin1	O35625	4	EBI-1105254,EBI-2365912	From a different organism.
FNBP1	Q96RU3	4	EBI-1105254,EBI-1111248

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O95271-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: O95271-2)

The sequence of this isoform differs from the canonical sequence as follows:
     641-643: EST → GHS
     644-1327: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1327

1327

Tankyrase-1

PRO_0000211333

Regions

Repeat

215 – 247

33

ANK 1

Repeat

248 – 280

33

ANK 2

Repeat

281 – 313

33

ANK 3

Repeat

368 – 400

33

ANK 4

Repeat

401 – 433

33

ANK 5

Repeat

434 – 466

33

ANK 6

Repeat

521 – 556

36

ANK 7

Repeat

557 – 589

33

ANK 8

Repeat

590 – 622

33

ANK 9

Repeat

683 – 715

33

ANK 10

Repeat

716 – 748

33

ANK 11

Repeat

749 – 781

33

ANK 12

Repeat

836 – 868

33

ANK 13

Repeat

869 – 901

33

ANK 14

Repeat

902 – 934

33

ANK 15

Domain

1030 – 1089

60

SAM

Domain

1112 – 1317

206

PARP catalytic

Compositional bias

9 – 14

6

Poly-His

Compositional bias

27 – 34

8

Poly-Pro

Compositional bias

128 – 134

7

Poly-Ser

Compositional bias

137 – 145

9

Poly-Ser

Sites

Metal binding

1234

1

Zinc

Metal binding

1237

1

Zinc

Metal binding

1242

1

Zinc

Metal binding

1245

1

Zinc

Amino acid modifications

Modified residue

365

1

Phosphoserine Ref.9

Natural variations

Alternative sequence

641 – 643

3

EST → GHS in isoform 2.

VSP_004538

Alternative sequence

644 – 1327

684

Missing in isoform 2.

VSP_004539

Experimental info

Mutagenesis

1184

1

H → A: Loss of activity; when associated with A-1291. Ref.6

Mutagenesis

1291

1

E → A: Loss of activity; when associated with A-1184. Ref.6

Sequence conflict

83

1

P → Q in AAH98394. Ref.3

Sequence conflict

802

1

R → K in AAC79841. Ref.1

Sequence conflict

802

1

R → K in AAC79842. Ref.1

Sequence conflict

1001

1

E → G in AAH98394. Ref.3

Sequence conflict

1266

1

M → I in AAH98394. Ref.3

Secondary structure

1

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1327

Helix Strand Turn

Details...

Beta strand

1107 – 1110

4

Helix

1116 – 1127

12

Turn

1133 – 1139

7

Beta strand

1143 – 1154

12

Helix

1159 – 1171

13

Turn

1172 – 1174

3

Beta strand

1179 – 1184

6

Helix

1189 – 1195

7

Helix

1199 – 1201

3

Turn

1203 – 1205

3

Beta strand

1210 – 1217

8

Helix

1218 – 1222

5

Turn

1223 – 1226

4

Helix

1228 – 1230

3

Turn

1235 – 1237

3

Beta strand

1243 – 1245

3

Beta strand

1247 – 1255

9

Beta strand

1258 – 1263

6

Beta strand

1276 – 1280

5

Beta strand

1284 – 1286

3

Beta strand

1287 – 1289

3

Beta strand

1291 – 1295

5

Helix

1297 – 1299

3

Beta strand

1300 – 1311

12

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 14, 2009. Version 2. Checksum: 44BDE985C715BEFF	FASTA	1,327	142,039
	10 20 30 40 50 60 MAASRRSQHH HHHHQQQLQP APGASAPPPP PPPPLSPGLA PGTTPASPTA SGLAPFASPR 70 80 90 100 110 120 HGLALPEGDG SRDPPDRPRS PDPVDGTSCC STTSTICTVA AAPVVPAVST SSAAGVAPNP 130 140 150 160 170 180 AGSGSNNSPS SSSSPTSSSS SSPSSPGSSL AESPEAAGVS STAPLGPGAA GPGTGVPAVS 190 200 210 220 230 240 GALRELLEAC RNGDVSRVKR LVDAANVNAK DMAGRKSSPL HFAAGFGRKD VVEHLLQMGA 250 260 270 280 290 300 NVHARDDGGL IPLHNACSFG HAEVVSLLLC QGADPNARDN WNYTPLHEAA IKGKIDVCIV 310 320 330 340 350 360 LLQHGADPNI RNTDGKSALD LADPSAKAVL TGEYKKDELL EAARSGNEEK LMALLTPLNV 370 380 390 400 410 420 NCHASDGRKS TPLHLAAGYN RVRIVQLLLQ HGADVHAKDK GGLVPLHNAC SYGHYEVTEL 430 440 450 460 470 480 LLKHGACVNA MDLWQFTPLH EAASKNRVEV CSLLLSHGAD PTLVNCHGKS AVDMAPTPEL 490 500 510 520 530 540 RERLTYEFKG HSLLQAAREA DLAKVKKTLA LEIINFKQPQ SHETALHCAV ASLHPKRKQV 550 560 570 580 590 600 TELLLRKGAN VNEKNKDFMT PLHVAAERAH NDVMEVLHKH GAKMNALDTL GQTALHRAAL 610 620 630 640 650 660 AGHLQTCRLL LSYGSDPSII SLQGFTAAQM GNEAVQQILS ESTPIRTSDV DYRLLEASKA 670 680 690 700 710 720 GDLETVKQLC SSQNVNCRDL EGRHSTPLHF AAGYNRVSVV EYLLHHGADV HAKDKGGLVP 730 740 750 760 770 780 LHNACSYGHY EVAELLVRHG ASVNVADLWK FTPLHEAAAK GKYEICKLLL KHGADPTKKN 790 800 810 820 830 840 RDGNTPLDLV KEGDTDIQDL LRGDAALLDA AKKGCLARVQ KLCTPENINC RDTQGRNSTP 850 860 870 880 890 900 LHLAAGYNNL EVAEYLLEHG ADVNAQDKGG LIPLHNAASY GHVDIAALLI KYNTCVNATD 910 920 930 940 950 960 KWAFTPLHEA AQKGRTQLCA LLLAHGADPT MKNQEGQTPL DLATADDIRA LLIDAMPPEA 970 980 990 1000 1010 1020 LPTCFKPQAT VVSASLISPA STPSCLSAAS SIDNLTGPLA ELAVGGASNA GDGAAGTERK 1030 1040 1050 1060 1070 1080 EGEVAGLDMN ISQFLKSLGL EHLRDIFETE QITLDVLADM GHEELKEIGI NAYGHRHKLI 1090 1100 1110 1120 1130 1140 KGVERLLGGQ QGTNPYLTFH CVNQGTILLD LAPEDKEYQS VEEEMQSTIR EHRDGGNAGG 1150 1160 1170 1180 1190 1200 IFNRYNVIRI QKVVNKKLRE RFCHRQKEVS EENHNHHNER MLFHGSPFIN AIIHKGFDER 1210 1220 1230 1240 1250 1260 HAYIGGMFGA GIYFAENSSK SNQYVYGIGG GTGCPTHKDR SCYICHRQML FCRVTLGKSF 1270 1280 1290 1300 1310 1320 LQFSTMKMAH APPGHHSVIG RPSVNGLAYA EYVIYRGEQA YPEYLITYQI MKPEAPSQTA TAAEQKT
	Isoform 2 [UniParc]. Checksum: FA67DE30C2A2F3B8	FASTA	643	67,203
	10 20 30 40 50 60 MAASRRSQHH HHHHQQQLQP APGASAPPPP PPPPLSPGLA PGTTPASPTA SGLAPFASPR 70 80 90 100 110 120 HGLALPEGDG SRDPPDRPRS PDPVDGTSCC STTSTICTVA AAPVVPAVST SSAAGVAPNP 130 140 150 160 170 180 AGSGSNNSPS SSSSPTSSSS SSPSSPGSSL AESPEAAGVS STAPLGPGAA GPGTGVPAVS 190 200 210 220 230 240 GALRELLEAC RNGDVSRVKR LVDAANVNAK DMAGRKSSPL HFAAGFGRKD VVEHLLQMGA 250 260 270 280 290 300 NVHARDDGGL IPLHNACSFG HAEVVSLLLC QGADPNARDN WNYTPLHEAA IKGKIDVCIV 310 320 330 340 350 360 LLQHGADPNI RNTDGKSALD LADPSAKAVL TGEYKKDELL EAARSGNEEK LMALLTPLNV 370 380 390 400 410 420 NCHASDGRKS TPLHLAAGYN RVRIVQLLLQ HGADVHAKDK GGLVPLHNAC SYGHYEVTEL 430 440 450 460 470 480 LLKHGACVNA MDLWQFTPLH EAASKNRVEV CSLLLSHGAD PTLVNCHGKS AVDMAPTPEL 490 500 510 520 530 540 RERLTYEFKG HSLLQAAREA DLAKVKKTLA LEIINFKQPQ SHETALHCAV ASLHPKRKQV 550 560 570 580 590 600 TELLLRKGAN VNEKNKDFMT PLHVAAERAH NDVMEVLHKH GAKMNALDTL GQTALHRAAL 610 620 630 640 AGHLQTCRLL LSYGSDPSII SLQGFTAAQM GNEAVQQILS GHS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Tankyrase, a poly(ADP-ribose) polymerase at human telomeres." Smith S., Giriat I., Schmitt A., de Lange T. Science 282:1484-1487(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). Tissue: Testis.
[2]	"DNA sequence and analysis of human chromosome 8." Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S. Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[4]	"Cell cycle dependent localization of the telomeric PARP, tankyrase, to nuclear pore complexes and centrosomes." Smith S., de Lange T. J. Cell Sci. 112:3649-3656(1999) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[5]	"Tankyrase is a Golgi-associated mitogen-activated protein kinase substrate that interacts with IRAP in GLUT4 vesicles." Chi N.-W., Lodish H.F. J. Biol. Chem. 275:38437-38444(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION.
[6]	"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, MUTAGENESIS OF HIS-1184 AND GLU-1291.
[7]	"POT1 as a terminal transducer of TRF1 telomere length control." Loayza D., De Lange T. Nature 423:1013-1018(2003) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH POT1; TERF1 AND TINF2.
[8]	"NuMA is a major acceptor of poly(ADP-ribosyl)ation by tankyrase 1 in mitosis." Chang W., Dynek J.N., Smith S. Biochem. J. 391:177-184(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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.
[11]	"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.
[12]	"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, INTERACTION WITH AXIN1; AXIN2; BLZF1 AND CASC3, UBIQUITINATION.
[13]	"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 AXIN1, SUBCELLULAR LOCATION.
[14]	"Poly-ADP ribosylation of Miki by tankyrase-1 promotes centrosome maturation." Ozaki Y., Matsui H., Asou H., Nagamachi A., Aki D., Honda H., Yasunaga S., Takihara Y., Yamamoto T., Izumi S., Ohsugi M., Inaba T. Mol. Cell 47:694-706(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[15]	"Zinc binding catalytic domain of human tankyrase 1." Lehtio L., Collins R., van den Berg S., Johansson A., Dahlgren L.G., Hammarstrom M., Helleday T., Holmberg-Schiavone L., Karlberg T., Weigelt J. J. Mol. Biol. 379:136-145(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1091-1325, ZINC-BINDING SITES.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF082556 mRNA. Translation: AAC79841.1.
AF082557 mRNA. Translation: AAC79842.1.
AF082558 mRNA. Translation: AAC79843.1.
AF082559 mRNA. Translation: AAC79844.1.
AC103834 Genomic DNA. No translation available.
AC103877 Genomic DNA. No translation available.
AC104052 Genomic DNA. No translation available.
AC021242 Genomic DNA. No translation available.
BC098394 mRNA. Translation: AAH98394.1.

IPI

IPI00021493.
IPI00221159.

RefSeq

NP_003738.2. NM_003747.2.

UniGene

Hs.370267.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2RF5	X-ray	2.30	A	1091-1325	[»]
3UDD	X-ray	1.95	A/B	1105-1327	[»]
3UH2	X-ray	2.00	A/B	1105-1327	[»]
3UH4	X-ray	2.00	A/B	1105-1327	[»]
4DVI	X-ray	1.90	A/B	1104-1314	[»]
4I9I	X-ray	2.40	A/B/C/D	1104-1314	[»]

ProteinModelPortal

O95271.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-36652N.

IntAct

O95271. 9 interactions.

STRING

9606.ENSP00000311579.

PTM databases

PhosphoSite

O95271.

Proteomic databases

PaxDb

O95271.

PRIDE

O95271.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000310430; ENSP00000311579; ENSG00000173273.
ENST00000518635; ENSP00000431098; ENSG00000173273.

GeneID

8658.

KEGG

hsa:8658.

UCSC

uc003wss.3. human.

Organism-specific databases

CTD

8658.

GeneCards

GC08P009450.

H-InvDB

HIX0034248.

HGNC

HGNC:11941. TNKS.

HPA

HPA025690.

MIM

603303. gene.

neXtProt

NX_O95271.

PharmGKB

PA36631.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0666.

HOGENOM

HOG000246964.

HOVERGEN

HBG059472.

InParanoid

O95271.

KO

K10799.

OMA

DDKEYQS.

OrthoDB

EOG45MN4H.

PhylomeDB

O95271.

Enzyme and pathway databases

BRENDA

2.4.2.30. 2681.

Pathway_Interaction_DB

telomerasepathway. Regulation of Telomerase.

Gene expression databases

ArrayExpress

O95271.

Bgee

O95271.

CleanEx

HS_TNKS.

Genevestigator

O95271.

GermOnline

ENSG00000173273. Homo sapiens.

Family and domain databases

Gene3D

1.10.150.50. 1 hit.
1.25.40.20. 8 hits.

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. 12 hits.
PF12796. Ank_2. 1 hit.
PF00644. PARP. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view]

PRINTS

PR01415. ANKYRIN.

SMART

SM00248. ANK. 17 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

O95271.

ChEMBL

CHEMBL6164.

ChiTaRS

TNKS. human.

EvolutionaryTrace

O95271.

GenomeRNAi

8658.

NextBio

32469.

SOURCE

Search...

Entry information

Entry name

TNKS1_HUMAN

Accession

Primary (citable) accession number: O95271
Secondary accession number(s): O95272, Q4G0F2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 27, 2002
Last sequence update:	April 14, 2009
Last modified:	May 1, 2013
This is version 130 of the entry and version 2 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.