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O95271

- TNKS1_HUMAN

UniProt

O95271 - TNKS1_HUMAN

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Protein
Tankyrase-1
Gene
TNKS, PARP5A, PARPL, TIN1, TINF1, TNKS1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.7 Publications

Catalytic activityi

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

Enzyme regulationi

Specifically inhibited by XAV939, a small molecule, leading to inhibit the Wnt signaling pathway by stabilizing AXIN1 and AXIN2.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1234 – 12341Zinc
Metal bindingi1237 – 12371Zinc
Metal bindingi1242 – 12421Zinc
Metal bindingi1245 – 12451Zinc

GO - Molecular functioni

  1. NAD+ ADP-ribosyltransferase activity Source: UniProtKB
  2. protein binding Source: UniProtKB
  3. zinc ion binding Source: BHF-UCL

GO - Biological processi

  1. Wnt signaling pathway Source: UniProtKB-KW
  2. mRNA transport Source: UniProtKB-KW
  3. mitotic nuclear division Source: UniProtKB-KW
  4. mitotic spindle organization Source: BHF-UCL
  5. negative regulation of DNA binding Source: BHF-UCL
  6. peptidyl-serine phosphorylation Source: MGI
  7. peptidyl-threonine phosphorylation Source: MGI
  8. positive regulation of canonical Wnt signaling pathway Source: UniProtKB
  9. positive regulation of telomere maintenance via telomerase Source: BHF-UCL
  10. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  11. protein ADP-ribosylation Source: BHF-UCL
  12. protein auto-ADP-ribosylation Source: UniProtKB
  13. protein localization to chromosome, telomeric region Source: BHF-UCL
  14. protein poly-ADP-ribosylation Source: BHF-UCL
  15. protein polyubiquitination Source: UniProtKB
  16. protein transport Source: UniProtKB-KW
  17. regulation of telomere maintenance via telomerase Source: BHF-UCL
  18. spindle assembly Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, mRNA transport, Protein transport, Translocation, Transport, Wnt signaling pathway

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

BRENDAi2.4.2.30. 2681.
ReactomeiREACT_200766. degradation of AXIN.
REACT_200777. TCF dependent signaling in response to WNT.

Names & Taxonomyi

Protein namesi
Recommended name:
Tankyrase-1 (EC:2.4.2.30)
Short name:
TANK1
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 namesi
Name:TNKS
Synonyms:PARP5A, PARPL, TIN1, TINF1, TNKS1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:11941. TNKS.

Subcellular locationi

Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Chromosomecentromere. Nucleusnuclear pore complex. Chromosometelomere Reviewed prediction. 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 NUMA1.4 Publications

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB
  2. Golgi membrane Source: UniProtKB-SubCell
  3. chromosome, centromeric region Source: UniProtKB-SubCell
  4. chromosome, telomeric region Source: UniProtKB
  5. nuclear chromosome, telomeric region Source: BHF-UCL
  6. nuclear membrane Source: BHF-UCL
  7. nuclear pore Source: BHF-UCL
  8. nucleus Source: HPA
  9. pericentriolar material Source: BHF-UCL
  10. spindle pole Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Golgi apparatus, Membrane, Nuclear pore complex, Nucleus, Telomere

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1184 – 11841H → A: Loss of activity; when associated with A-1291. 1 Publication
Mutagenesisi1291 – 12911E → A: Loss of activity; when associated with A-1184. 1 Publication

Organism-specific databases

PharmGKBiPA36631.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13271327Tankyrase-1
PRO_0000211333Add
BLAST

Post-translational modificationi

Phosphorylated on serine residues by MAPK kinases upon insulin stimulation. Phosphorylated during mitosis.1 Publication
Ubiquitinated by RNF146 when auto-poly-ADP-ribosylated, leading to its degradation.1 Publication
ADP-ribosylated (-auto). Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination.

Keywords - PTMi

ADP-ribosylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO95271.
PaxDbiO95271.
PRIDEiO95271.

PTM databases

PhosphoSiteiO95271.

Expressioni

Tissue specificityi

Ubiquitous; highest levels in testis.

Gene expression databases

ArrayExpressiO95271.
BgeeiO95271.
CleanExiHS_TNKS.
GenevestigatoriO95271.

Organism-specific databases

HPAiHPA025690.

Interactioni

Subunit structurei

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 CASC3.4 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi114207. 20 interactions.
DIPiDIP-36652N.
IntActiO95271. 14 interactions.
MINTiMINT-7026707.
STRINGi9606.ENSP00000311579.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1107 – 11104
Helixi1116 – 112611
Turni1133 – 11397
Beta strandi1143 – 115412
Helixi1156 – 117116
Turni1172 – 11754
Beta strandi1179 – 11846
Helixi1189 – 11957
Helixi1199 – 12013
Turni1203 – 12053
Beta strandi1210 – 12178
Helixi1218 – 12225
Turni1223 – 12264
Helixi1228 – 12303
Turni1235 – 12373
Beta strandi1243 – 12453
Beta strandi1247 – 12559
Beta strandi1258 – 12636
Beta strandi1268 – 12703
Beta strandi1276 – 12805
Beta strandi1284 – 12863
Beta strandi1287 – 12893
Beta strandi1291 – 12966
Helixi1297 – 12993
Beta strandi1300 – 131112

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliO95271.
SMRiO95271. Positions 144-986, 1030-1089, 1105-1314.

Miscellaneous databases

EvolutionaryTraceiO95271.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati215 – 24733ANK 1
Add
BLAST
Repeati248 – 28033ANK 2
Add
BLAST
Repeati281 – 31333ANK 3
Add
BLAST
Repeati368 – 40033ANK 4
Add
BLAST
Repeati401 – 43333ANK 5
Add
BLAST
Repeati434 – 46633ANK 6
Add
BLAST
Repeati521 – 55636ANK 7
Add
BLAST
Repeati557 – 58933ANK 8
Add
BLAST
Repeati590 – 62233ANK 9
Add
BLAST
Repeati683 – 71533ANK 10
Add
BLAST
Repeati716 – 74833ANK 11
Add
BLAST
Repeati749 – 78133ANK 12
Add
BLAST
Repeati836 – 86833ANK 13
Add
BLAST
Repeati869 – 90133ANK 14
Add
BLAST
Repeati902 – 93433ANK 15
Add
BLAST
Domaini1030 – 108960SAM
Add
BLAST
Domaini1112 – 1317206PARP catalytic
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi9 – 146Poly-His
Compositional biasi27 – 348Poly-Pro
Compositional biasi128 – 1347Poly-Ser
Compositional biasi137 – 1459Poly-Ser

Sequence similaritiesi

Contains 15 ANK repeats.

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiCOG0666.
HOGENOMiHOG000246964.
HOVERGENiHBG059472.
InParanoidiO95271.
KOiK10799.
OMAiDDKEYQS.
PhylomeDBiO95271.
TreeFamiTF326036.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
1.25.40.20. 8 hits.
3.90.228.10. 1 hit.
InterProiIPR002110. 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]
PANTHERiPTHR24180:SF3. PTHR24180:SF3. 1 hit.
PfamiPF00023. Ank. 12 hits.
PF12796. Ank_2. 1 hit.
PF00644. PARP. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 17 hits.
SM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF48403. SSF48403. 4 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 15 hits.
PS51059. PARP_CATALYTIC. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O95271-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MAASRRSQHH HHHHQQQLQP APGASAPPPP PPPPLSPGLA PGTTPASPTA     50
SGLAPFASPR HGLALPEGDG SRDPPDRPRS PDPVDGTSCC STTSTICTVA 100
AAPVVPAVST SSAAGVAPNP AGSGSNNSPS SSSSPTSSSS SSPSSPGSSL 150
AESPEAAGVS STAPLGPGAA GPGTGVPAVS GALRELLEAC RNGDVSRVKR 200
LVDAANVNAK DMAGRKSSPL HFAAGFGRKD VVEHLLQMGA NVHARDDGGL 250
IPLHNACSFG HAEVVSLLLC QGADPNARDN WNYTPLHEAA IKGKIDVCIV 300
LLQHGADPNI RNTDGKSALD LADPSAKAVL TGEYKKDELL EAARSGNEEK 350
LMALLTPLNV NCHASDGRKS TPLHLAAGYN RVRIVQLLLQ HGADVHAKDK 400
GGLVPLHNAC SYGHYEVTEL LLKHGACVNA MDLWQFTPLH EAASKNRVEV 450
CSLLLSHGAD PTLVNCHGKS AVDMAPTPEL RERLTYEFKG HSLLQAAREA 500
DLAKVKKTLA LEIINFKQPQ SHETALHCAV ASLHPKRKQV TELLLRKGAN 550
VNEKNKDFMT PLHVAAERAH NDVMEVLHKH GAKMNALDTL GQTALHRAAL 600
AGHLQTCRLL LSYGSDPSII SLQGFTAAQM GNEAVQQILS ESTPIRTSDV 650
DYRLLEASKA GDLETVKQLC SSQNVNCRDL EGRHSTPLHF AAGYNRVSVV 700
EYLLHHGADV HAKDKGGLVP LHNACSYGHY EVAELLVRHG ASVNVADLWK 750
FTPLHEAAAK GKYEICKLLL KHGADPTKKN RDGNTPLDLV KEGDTDIQDL 800
LRGDAALLDA AKKGCLARVQ KLCTPENINC RDTQGRNSTP LHLAAGYNNL 850
EVAEYLLEHG ADVNAQDKGG LIPLHNAASY GHVDIAALLI KYNTCVNATD 900
KWAFTPLHEA AQKGRTQLCA LLLAHGADPT MKNQEGQTPL DLATADDIRA 950
LLIDAMPPEA LPTCFKPQAT VVSASLISPA STPSCLSAAS SIDNLTGPLA 1000
ELAVGGASNA GDGAAGTERK EGEVAGLDMN ISQFLKSLGL EHLRDIFETE 1050
QITLDVLADM GHEELKEIGI NAYGHRHKLI KGVERLLGGQ QGTNPYLTFH 1100
CVNQGTILLD LAPEDKEYQS VEEEMQSTIR EHRDGGNAGG IFNRYNVIRI 1150
QKVVNKKLRE RFCHRQKEVS EENHNHHNER MLFHGSPFIN AIIHKGFDER 1200
HAYIGGMFGA GIYFAENSSK SNQYVYGIGG GTGCPTHKDR SCYICHRQML 1250
FCRVTLGKSF LQFSTMKMAH APPGHHSVIG RPSVNGLAYA EYVIYRGEQA 1300
YPEYLITYQI MKPEAPSQTA TAAEQKT 1327
Length:1,327
Mass (Da):142,039
Last modified:April 14, 2009 - v2
Checksum:i44BDE985C715BEFF
GO
Isoform 2 (identifier: O95271-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:643
Mass (Da):67,203
Checksum:iFA67DE30C2A2F3B8
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei641 – 6433EST → GHS in isoform 2.
VSP_004538
Alternative sequencei644 – 1327684Missing in isoform 2.
VSP_004539Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti83 – 831P → Q in AAH98394. 1 Publication
Sequence conflicti802 – 8021R → K in AAC79841. 1 Publication
Sequence conflicti802 – 8021R → K in AAC79842. 1 Publication
Sequence conflicti1001 – 10011E → G in AAH98394. 1 Publication
Sequence conflicti1266 – 12661M → I in AAH98394. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS5974.1. [O95271-1]
RefSeqiNP_003738.2. NM_003747.2. [O95271-1]
UniGeneiHs.370267.

Genome annotation databases

EnsembliENST00000310430; ENSP00000311579; ENSG00000173273. [O95271-1]
ENST00000518635; ENSP00000431098; ENSG00000173273.
GeneIDi8658.
KEGGihsa:8658.
UCSCiuc003wss.3. human. [O95271-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS5974.1. [O95271-1 ]
RefSeqi NP_003738.2. NM_003747.2. [O95271-1 ]
UniGenei Hs.370267.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
4K4E X-ray 2.30 A/B 1104-1314 [» ]
4K4F X-ray 2.90 A/B 1104-1314 [» ]
4KRS X-ray 2.29 A/B 1105-1327 [» ]
4LI6 X-ray 2.05 A/B 1105-1327 [» ]
4LI7 X-ray 2.20 A/B 1105-1327 [» ]
4LI8 X-ray 2.52 A/B 1105-1327 [» ]
4MSG X-ray 1.80 A/B 1104-1314 [» ]
4MSK X-ray 2.30 A/B/C/D 1104-1314 [» ]
4MT9 X-ray 2.00 A/B 1104-1314 [» ]
4N3R X-ray 1.90 A/B 1104-1314 [» ]
4N4V X-ray 2.00 A/B 1104-1314 [» ]
ProteinModelPortali O95271.
SMRi O95271. Positions 144-986, 1030-1089, 1105-1314.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114207. 20 interactions.
DIPi DIP-36652N.
IntActi O95271. 14 interactions.
MINTi MINT-7026707.
STRINGi 9606.ENSP00000311579.

Chemistry

BindingDBi O95271.
ChEMBLi CHEMBL6164.

PTM databases

PhosphoSitei O95271.

Proteomic databases

MaxQBi O95271.
PaxDbi O95271.
PRIDEi O95271.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000310430 ; ENSP00000311579 ; ENSG00000173273 . [O95271-1 ]
ENST00000518635 ; ENSP00000431098 ; ENSG00000173273 .
GeneIDi 8658.
KEGGi hsa:8658.
UCSCi uc003wss.3. human. [O95271-1 ]

Organism-specific databases

CTDi 8658.
GeneCardsi GC08P009450.
H-InvDB HIX0034248.
HGNCi HGNC:11941. TNKS.
HPAi HPA025690.
MIMi 603303. gene.
neXtProti NX_O95271.
PharmGKBi PA36631.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0666.
HOGENOMi HOG000246964.
HOVERGENi HBG059472.
InParanoidi O95271.
KOi K10799.
OMAi DDKEYQS.
PhylomeDBi O95271.
TreeFami TF326036.

Enzyme and pathway databases

BRENDAi 2.4.2.30. 2681.
Reactomei REACT_200766. degradation of AXIN.
REACT_200777. TCF dependent signaling in response to WNT.

Miscellaneous databases

ChiTaRSi TNKS. human.
EvolutionaryTracei O95271.
GeneWikii TNKS.
GenomeRNAii 8658.
NextBioi 32469.
PROi O95271.
SOURCEi Search...

Gene expression databases

ArrayExpressi O95271.
Bgeei O95271.
CleanExi HS_TNKS.
Genevestigatori O95271.

Family and domain databases

Gene3Di 1.10.150.50. 1 hit.
1.25.40.20. 8 hits.
3.90.228.10. 1 hit.
InterProi IPR002110. 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 ]
PANTHERi PTHR24180:SF3. PTHR24180:SF3. 1 hit.
Pfami PF00023. Ank. 12 hits.
PF12796. Ank_2. 1 hit.
PF00644. PARP. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view ]
PRINTSi PR01415. ANKYRIN.
SMARTi SM00248. ANK. 17 hits.
SM00454. SAM. 1 hit.
[Graphical view ]
SUPFAMi SSF47769. SSF47769. 1 hit.
SSF48403. SSF48403. 4 hits.
PROSITEi PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 15 hits.
PS51059. PARP_CATALYTIC. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1091-1325, ZINC-BINDING SITES.

Entry informationi

Entry nameiTNKS1_HUMAN
AccessioniPrimary (citable) accession number: O95271
Secondary accession number(s): O95272, Q4G0F2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: April 14, 2009
Last modified: September 3, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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