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O95271 (TNKS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1327 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Stimulates 26S proteasome activity. Ref.5 Ref.6 Ref.8 Ref.9 Ref.11 Ref.13 Ref.14

Catalytic activity

NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor. Ref.9

Enzyme regulation

Specifically inhibited by XAV939, a small molecule, leading to inhibit the Wnt signaling pathway by stabilizing AXIN1 and AXIN2. Ref.9

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.9 Ref.11 Ref.12

Subcellular location

Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Chromosomecentromere. Nucleusnuclear pore complex. Chromosometelomere Potential. Cytoplasmcytoskeletonspindle 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.12 Ref.13

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.11

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 processCell cycle
Cell division
Mitosis
mRNA transport
Protein transport
Translocation
Transport
Wnt signaling pathway
   Cellular componentCentromere
Chromosome
Cytoplasm
Cytoskeleton
Golgi apparatus
Membrane
Nuclear pore complex
Nucleus
Telomere
   Coding sequence diversityAlternative splicing
   DomainANK repeat
Repeat
   LigandMetal-binding
NAD
Zinc
   Molecular functionGlycosyltransferase
Transferase
   PTMADP-ribosylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

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 signaling pathway

Inferred from mutant phenotype Ref.9. 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 ADP-ribosylation

Inferred from direct assay Ref.1. Source: BHF-UCL

protein auto-ADP-ribosylation

Inferred from direct assay Ref.9Ref.11. 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.9Ref.11. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of telomere maintenance via telomerase

Inferred by curator Ref.1. Source: BHF-UCL

spindle assembly

Traceable author statement PubMed 17026964. Source: BHF-UCL

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.13. Source: UniProtKB

Golgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

chromosome, centromeric region

Inferred from electronic annotation. Source: UniProtKB-SubCell

chromosome, telomeric region

Inferred from direct assay Ref.1. Source: UniProtKB

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

nucleus

Inferred from direct assay. Source: HPA

pericentriolar material

Traceable author statement PubMed 11454873. Source: BHF-UCL

spindle pole

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionNAD+ ADP-ribosyltransferase activity

Inferred from direct assay Ref.9Ref.11Ref.13Ref.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

Axin1O356254EBI-1105254,EBI-2365912From a different organism.
CENPJQ9HC774EBI-1105254,EBI-946194
FNBP1Q96RU34EBI-1105254,EBI-1111248
HIF1ANQ9NWT62EBI-1105254,EBI-745632

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13271327Tankyrase-1
PRO_0000211333

Regions

Repeat215 – 24733ANK 1
Repeat248 – 28033ANK 2
Repeat281 – 31333ANK 3
Repeat368 – 40033ANK 4
Repeat401 – 43333ANK 5
Repeat434 – 46633ANK 6
Repeat521 – 55636ANK 7
Repeat557 – 58933ANK 8
Repeat590 – 62233ANK 9
Repeat683 – 71533ANK 10
Repeat716 – 74833ANK 11
Repeat749 – 78133ANK 12
Repeat836 – 86833ANK 13
Repeat869 – 90133ANK 14
Repeat902 – 93433ANK 15
Domain1030 – 108960SAM
Domain1112 – 1317206PARP catalytic
Compositional bias9 – 146Poly-His
Compositional bias27 – 348Poly-Pro
Compositional bias128 – 1347Poly-Ser
Compositional bias137 – 1459Poly-Ser

Sites

Metal binding12341Zinc
Metal binding12371Zinc
Metal binding12421Zinc
Metal binding12451Zinc

Natural variations

Alternative sequence641 – 6433EST → GHS in isoform 2.
VSP_004538
Alternative sequence644 – 1327684Missing in isoform 2.
VSP_004539

Experimental info

Mutagenesis11841H → A: Loss of activity; when associated with A-1291. Ref.6
Mutagenesis12911E → A: Loss of activity; when associated with A-1184. Ref.6
Sequence conflict831P → Q in AAH98394. Ref.3
Sequence conflict8021R → K in AAC79841. Ref.1
Sequence conflict8021R → K in AAC79842. Ref.1
Sequence conflict10011E → G in AAH98394. Ref.3
Sequence conflict12661M → I in AAH98394. Ref.3

Secondary structure

............................................. 1327
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 14, 2009. Version 2.
Checksum: 44BDE985C715BEFF

FASTA1,327142,039
        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 

« Hide

Isoform 2 [UniParc].

Checksum: FA67DE30C2A2F3B8
Show »

FASTA64367,203

References

« Hide '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. expand/collapse author list , 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]"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. expand/collapse author list , 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.
[10]"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.
[11]"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.
[12]"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.
[13]"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.
[14]"Proteasome regulation by ADP-ribosylation."
Cho-Park P.F., Steller H.
Cell 153:614-627(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[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.
RefSeqNP_003738.2. NM_003747.2.
UniGeneHs.370267.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2RF5X-ray2.30A1091-1325[»]
3UDDX-ray1.95A/B1105-1327[»]
3UH2X-ray2.00A/B1105-1327[»]
3UH4X-ray2.00A/B1105-1327[»]
4DVIX-ray1.90A/B1104-1314[»]
4I9IX-ray2.40A/B/C/D1104-1314[»]
4K4EX-ray2.30A/B1104-1314[»]
4K4FX-ray2.90A/B1104-1314[»]
4KRSX-ray2.29A/B1105-1327[»]
4LI6X-ray2.05A/B1105-1327[»]
4LI7X-ray2.20A/B1105-1327[»]
4LI8X-ray2.52A/B1105-1327[»]
4MSGX-ray1.80A/B1104-1314[»]
4MSKX-ray2.30A/B/C/D1104-1314[»]
4MT9X-ray2.00A/B1104-1314[»]
4N3RX-ray1.90A/B1104-1314[»]
4N4VX-ray2.00A/B1104-1314[»]
ProteinModelPortalO95271.
SMRO95271. Positions 144-986, 1105-1315.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114207. 20 interactions.
DIPDIP-36652N.
IntActO95271. 14 interactions.
MINTMINT-7026707.
STRING9606.ENSP00000311579.

Chemistry

BindingDBO95271.
ChEMBLCHEMBL6164.

PTM databases

PhosphoSiteO95271.

Proteomic databases

PaxDbO95271.
PRIDEO95271.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000310430; ENSP00000311579; ENSG00000173273. [O95271-1]
ENST00000518635; ENSP00000431098; ENSG00000173273.
GeneID8658.
KEGGhsa:8658.
UCSCuc003wss.3. human. [O95271-1]

Organism-specific databases

CTD8658.
GeneCardsGC08P009450.
H-InvDBHIX0034248.
HGNCHGNC:11941. TNKS.
HPAHPA025690.
MIM603303. gene.
neXtProtNX_O95271.
PharmGKBPA36631.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0666.
HOGENOMHOG000246964.
HOVERGENHBG059472.
InParanoidO95271.
KOK10799.
OMADDKEYQS.
PhylomeDBO95271.
TreeFamTF326036.

Enzyme and pathway databases

BRENDA2.4.2.30. 2681.

Gene expression databases

ArrayExpressO95271.
BgeeO95271.
CleanExHS_TNKS.
GenevestigatorO95271.

Family and domain databases

Gene3D1.10.150.50. 1 hit.
1.25.40.20. 8 hits.
3.90.228.10. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR011510. SAM_2.
IPR028731. TNKS.
[Graphical view]
PANTHERPTHR24180:SF3. PTHR24180:SF3. 1 hit.
PfamPF00023. Ank. 12 hits.
PF12796. Ank_2. 1 hit.
PF00644. PARP. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view]
PRINTSPR01415. ANKYRIN.
SMARTSM00248. ANK. 17 hits.
SM00454. SAM. 1 hit.
[Graphical view]
SUPFAMSSF47769. SSF47769. 1 hit.
SSF48403. SSF48403. 4 hits.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 15 hits.
PS51059. PARP_CATALYTIC. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTNKS. human.
EvolutionaryTraceO95271.
GeneWikiTNKS.
GenomeRNAi8658.
NextBio32469.
PROO95271.
SOURCESearch...

Entry information

Entry nameTNKS1_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM