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Q6PFX9 (TNKS1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·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
TRF1-interacting ankyrin-related ADP-ribose polymerase 1
Short name=Tankyrase I
Gene names
Name:Tnks
Synonyms:Tnks1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1320 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 By similarity.

Catalytic activity

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

Enzyme regulation

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

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 By similarity.

Subcellular location

Cytoplasm By similarity. Golgi apparatus membrane; Peripheral membrane protein By similarity. Chromosomecentromere By similarity. Nucleusnuclear pore complex By similarity. Chromosometelomere Potential. Cytoplasmcytoskeletonspindle pole By similarity. 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 By similarity.

Post-translational modification

Phosphorylated on serine residues by MAPK kinases upon insulin stimulation. Phosphorylated during mitosis By similarity.

Ubiquitinated by RNF146 when auto-poly-ADP-ribosylated, leading to its degradation By similarity.

ADP-ribosylated (-auto). Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination By similarity.

Sequence similarities

Contains 18 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

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of DNA binding

Inferred from electronic annotation. Source: Ensembl

peptidyl-serine phosphorylation

Inferred from sequence orthology PubMed 17026964. Source: MGI

peptidyl-threonine phosphorylation

Inferred from sequence orthology PubMed 17026964. Source: MGI

positive regulation of canonical Wnt signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of telomere maintenance via telomerase

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

protein auto-ADP-ribosylation

Inferred from sequence or structural similarity. Source: UniProtKB

protein localization to chromosome, telomeric region

Inferred from electronic annotation. Source: Ensembl

protein poly-ADP-ribosylation

Inferred from electronic annotation. Source: Ensembl

protein polyubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

spindle assembly

Inferred from electronic annotation. Source: InterPro

   Cellular_componentGolgi apparatus

Inferred from sequence or structural similarity. Source: UniProtKB

Golgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

chromosome, centromeric region

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from direct assay PubMed 23791195. Source: MGI

nuclear chromosome, telomeric region

Inferred from electronic annotation. Source: Ensembl

nuclear pore

Inferred from electronic annotation. Source: UniProtKB-SubCell

spindle pole

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionNAD+ ADP-ribosyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6PFX9-1)

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: Q6PFX9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-344: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13201320Tankyrase-1
PRO_0000409511

Regions

Repeat174 – 20229ANK 1
Repeat208 – 23730ANK 2
Repeat241 – 27030ANK 3
Repeat274 – 30330ANK 4
Repeat361 – 39030ANK 5
Repeat394 – 42330ANK 6
Repeat427 – 45630ANK 7
Repeat514 – 54633ANK 8
Repeat550 – 57930ANK 9
Repeat583 – 61230ANK 10
Repeat676 – 70530ANK 11
Repeat709 – 73830ANK 12
Repeat742 – 77130ANK 13
Repeat775 – 80329ANK 14
Repeat829 – 85830ANK 15
Repeat862 – 89130ANK 16
Repeat895 – 92430ANK 17
Repeat928 – 95730ANK 18
Domain1019 – 108264SAM
Domain1105 – 1310206PARP catalytic
Compositional bias9 – 146Poly-His
Compositional bias20 – 8364Pro-rich
Compositional bias112 – 1187Poly-Gly
Compositional bias121 – 14626Ser-rich

Sites

Metal binding12271Zinc By similarity
Metal binding12301Zinc By similarity
Metal binding12351Zinc By similarity
Metal binding12381Zinc By similarity

Natural variations

Alternative sequence1 – 344344Missing in isoform 2.
VSP_041320

Experimental info

Sequence conflict9691L → V in BAC33475. Ref.1
Sequence conflict10251S → I in BAC33475. Ref.1

Secondary structure

.................................................................................. 1320
Helix Strand Turn

Details...

Sequences

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

Last modified July 5, 2004. Version 1.
Checksum: A90360DC665FFCC0

FASTA1,320140,944
        10         20         30         40         50         60 
MAASRRSQHH HHHHQQQLQP APGASAPPPP PPPPLSPGLA PGPTPASPTA GGLAPFASPR 

        70         80         90        100        110        120 
HGLALPEGDG SRDPPDRPRS PDPVDGAVCT VAAPAAVPAA SAAVGVAPTP AGGGGGGGNN 

       130        140        150        160        170        180 
SASSASSPTS SSSSSPSSPG SSLAESPEAA GVGSTATLGA GAAGLGPGVP AVSGALRELL 

       190        200        210        220        230        240 
EACRNGDVSR VKRLVDAANV NAKDMAGRKS SPLHFAAGFG RKDVVEHLLQ MGANVHARDD 

       250        260        270        280        290        300 
GGLIPLHNAC SFGHAEVVSL LLCQGADPNA RDNWNYTPLH EAAIKGKIDV CIVLLQHGAD 

       310        320        330        340        350        360 
PNIRNTDGKS ALDLADPSAK AVLTGEYKKD ELLEAARSGN EEKLMALLTP LNVNCHASDG 

       370        380        390        400        410        420 
RKSTPLHLAA GYNRVRIVQL LLQHGADVHA KDKGGLVPLH NACSYGHYEV TELLLKHGAC 

       430        440        450        460        470        480 
VNAMDLWQFT PLHEAASKNR VEVCSLLLSH GADPTLVNCH GKSAVDMAPT PELRERLTYE 

       490        500        510        520        530        540 
FKGHSLLQAA READLAKVKK TLALEIINFK QPQSHETALH CAVASLHPKR KQVAELLLRK 

       550        560        570        580        590        600 
GANVNEKNKD FMTPLHVAAE RAHNDVMEVL HKHGAKMNAL DSLGQTALHR AALAGHLQTC 

       610        620        630        640        650        660 
RLLLSYGSDP SIISLQGFTA AQMGNEAVQQ ILSESTPMRT SDVDYRLLEA SKAGDLETVK 

       670        680        690        700        710        720 
QLCSPQNVNC RDLEGRHSTP LHFAAGYNRV SVVEYLLHHG ADVHAKDKGG LVPLHNACSY 

       730        740        750        760        770        780 
GHYEVAELLV RHGASVNVAD LWKFTPLHEA AAKGKYEICK LLLKHGADPT KKNRDGNTPL 

       790        800        810        820        830        840 
DLVKEGDTDI QDLLRGDAAL LDAAKKGCLA RVQKLCTPEN INCRDTQGRN STPLHLAAGY 

       850        860        870        880        890        900 
NNLEVAEYLL EHGADVNAQD KGGLIPLHNA ASYGHVDIAA LLIKYNTCVN ATDKWAFTPL 

       910        920        930        940        950        960 
HEAAQKGRTQ LCALLLAHGA DPTMKNQEGQ TPLDLATADD IRALLIDAMP PEALPTCFKP 

       970        980        990       1000       1010       1020 
QATVVSASLI SPASTPSCLS AASSIDNLTG PLTDLAVGGA SNAGDGAAGA ERKEGEVAGL 

      1030       1040       1050       1060       1070       1080 
DMNISQFLKS LGLEHLRDIF ETEQITLDVL ADMGHEELKE IGINAYGHRH KLIKGVERLL 

      1090       1100       1110       1120       1130       1140 
GGQQGTNPYL TFHCVNQGTI LLDLAPEDKE YQSVEEEMQS TIREHRDGGN AGGIFNRYNV 

      1150       1160       1170       1180       1190       1200 
IRIQKVVNKK LRERFCHRQK EVSEENHNHH NERMLFHGSP FINAIIHKGF DERHAYIGGM 

      1210       1220       1230       1240       1250       1260 
FGAGIYFAEN SSKSNQYVYG IGGGTGCPTH KDRSCYICHR QMLFCRVTLG KSFLQFSTMK 

      1270       1280       1290       1300       1310       1320 
MAHAPPGHHS VIGRPSVNGL AYAEYVIYRG EQAYPEYLIT YQIMKPEAPS QTATAAEQKT 

« Hide

Isoform 2 [UniParc].

Checksum: 8DE71F21652C3D4A
Show »

FASTA976106,651

References

[1]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Cerebellum.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
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. expand/collapse author list , 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.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[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] (ISOFORM 1).
Strain: C57BL/6.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK048860 mRNA. Translation: BAC33475.1.
AC122458 Genomic DNA. No translation available.
BC057370 mRNA. Translation: AAH57370.1.
CCDSCCDS22242.1. [Q6PFX9-1]
RefSeqNP_780300.2. NM_175091.3. [Q6PFX9-1]
UniGeneMm.88364.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3UTMX-ray2.00A/B308-655[»]
4N4TX-ray2.32A/B1097-1307[»]
ProteinModelPortalQ6PFX9.
SMRQ6PFX9. Positions 316-635, 641-940, 1098-1307.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204263. 2 interactions.
STRING10090.ENSMUSP00000033929.

PTM databases

PhosphoSiteQ6PFX9.

Proteomic databases

PaxDbQ6PFX9.
PRIDEQ6PFX9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033929; ENSMUSP00000033929; ENSMUSG00000031529. [Q6PFX9-1]
GeneID21951.
KEGGmmu:21951.
UCSCuc009lku.1. mouse. [Q6PFX9-1]

Organism-specific databases

CTD8658.
MGIMGI:1341087. Tnks.

Phylogenomic databases

eggNOGCOG0666.
GeneTreeENSGT00750000117662.
HOGENOMHOG000246964.
HOVERGENHBG059472.
InParanoidQ8BX62.
KOK10799.
OMADDKEYQS.
OrthoDBEOG7N8ZTP.
PhylomeDBQ6PFX9.
TreeFamTF326036.

Gene expression databases

BgeeQ6PFX9.
GenevestigatorQ6PFX9.

Family and domain databases

Gene3D1.10.150.50. 1 hit.
1.25.40.20. 6 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. 3 hits.
PF12796. Ank_2. 5 hits.
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

NextBio301616.
PROQ6PFX9.
SOURCESearch...

Entry information

Entry nameTNKS1_MOUSE
AccessionPrimary (citable) accession number: Q6PFX9
Secondary accession number(s): Q8BX62
Entry history
Integrated into UniProtKB/Swiss-Prot: May 31, 2011
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot