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Protein

Tankyrase-1

Gene

TNKS

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.PROSITE-ProRule annotation1 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)DescriptionActionsGraphical viewLength
Metal bindingi1234ZincCombined sources1 Publication1
Metal bindingi1237ZincCombined sources1 Publication1
Metal bindingi1242ZincCombined sources1 Publication1
Metal bindingi1245ZincCombined sources1 Publication1

GO - Molecular functioni

  • histone binding Source: BHF-UCL
  • NAD+ ADP-ribosyltransferase activity Source: UniProtKB
  • zinc ion binding Source: BHF-UCL

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • mitotic nuclear division Source: UniProtKB-KW
  • mitotic spindle organization Source: BHF-UCL
  • mRNA transport Source: UniProtKB-KW
  • negative regulation of maintenance of mitotic sister chromatid cohesion, telomeric Source: BHF-UCL
  • negative regulation of telomere maintenance via telomere lengthening Source: BHF-UCL
  • negative regulation of telomeric DNA binding Source: BHF-UCL
  • peptidyl-serine phosphorylation Source: MGI
  • peptidyl-threonine phosphorylation Source: MGI
  • positive regulation of canonical Wnt signaling pathway Source: UniProtKB
  • positive regulation of telomerase activity Source: BHF-UCL
  • positive regulation of telomere capping Source: BHF-UCL
  • positive regulation of telomere maintenance via telomerase Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • protein ADP-ribosylation Source: BHF-UCL
  • protein auto-ADP-ribosylation Source: UniProtKB
  • protein localization to chromosome, telomeric region Source: BHF-UCL
  • protein poly-ADP-ribosylation Source: BHF-UCL
  • protein polyubiquitination Source: UniProtKB
  • protein transport Source: UniProtKB-KW
  • regulation of telomere maintenance via telomerase Source: BHF-UCL
  • spindle assembly Source: BHF-UCL
  • Wnt signaling pathway Source: Reactome
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

BioCyciZFISH:HS10642-MONOMER.
BRENDAi2.4.2.30. 2681.
ReactomeiR-HSA-201681. TCF dependent signaling in response to WNT.
R-HSA-4641257. Degradation of AXIN.
R-HSA-5545619. XAV939 inhibits tankyrase, stabilizing AXIN.
R-HSA-5689880. Ub-specific processing proteases.
SIGNORiO95271.

Protein family/group databases

TCDBi1.I.1.1.3. the nuclear pore complex (npc) family.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:11941. TNKS.

Subcellular locationi

GO - Cellular componenti

  • chromosome, centromeric region Source: UniProtKB-SubCell
  • chromosome, telomeric region Source: UniProtKB
  • cytosol Source: Reactome
  • Golgi apparatus Source: UniProtKB
  • Golgi membrane Source: UniProtKB-SubCell
  • nuclear chromosome, telomeric region Source: BHF-UCL
  • nuclear membrane Source: BHF-UCL
  • nuclear pore Source: BHF-UCL
  • pericentriolar material Source: BHF-UCL
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi1184H → A: Loss of activity; when associated with A-1291. 1 Publication1
Mutagenesisi1291E → A: Loss of activity; when associated with A-1184. 1 Publication1

Organism-specific databases

DisGeNETi8658.
OpenTargetsiENSG00000173273.
PharmGKBiPA36631.

Chemistry databases

ChEMBLiCHEMBL6164.

Polymorphism and mutation databases

BioMutaiTNKS.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002113331 – 1327Tankyrase-1Add BLAST1327

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.1 Publication

Keywords - PTMi

ADP-ribosylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO95271.
MaxQBiO95271.
PaxDbiO95271.
PeptideAtlasiO95271.
PRIDEiO95271.

PTM databases

iPTMnetiO95271.
PhosphoSitePlusiO95271.

Expressioni

Tissue specificityi

Ubiquitous; highest levels in testis.

Gene expression databases

BgeeiENSG00000173273.
CleanExiHS_TNKS.
ExpressionAtlasiO95271. baseline and differential.
GenevisibleiO95271. HS.

Organism-specific databases

HPAiHPA025690.
HPA062936.

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
H2AFYO75367-26EBI-1105254,EBI-6249599
HIF1ANQ9NWT63EBI-1105254,EBI-745632
TERF1P542744EBI-1105254,EBI-710997

GO - Molecular functioni

  • histone binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi114207. 44 interactors.
DIPiDIP-36652N.
IntActiO95271. 20 interactors.
MINTiMINT-7026707.
STRINGi9606.ENSP00000311579.

Chemistry databases

BindingDBiO95271.

Structurei

Secondary structure

11327
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi182 – 192Combined sources11
Helixi195 – 201Combined sources7
Turni204 – 208Combined sources5
Turni212 – 215Combined sources4
Helixi219 – 225Combined sources7
Helixi229 – 237Combined sources9
Helixi252 – 258Combined sources7
Helixi262 – 270Combined sources9
Helixi285 – 291Combined sources7
Helixi295 – 303Combined sources9
Turni318 – 321Combined sources4
Helixi324 – 329Combined sources6
Turni330 – 332Combined sources3
Helixi336 – 345Combined sources10
Helixi348 – 354Combined sources7
Helixi359 – 361Combined sources3
Helixi372 – 378Combined sources7
Helixi382 – 390Combined sources9
Helixi405 – 411Combined sources7
Helixi415 – 423Combined sources9
Helixi438 – 444Combined sources7
Helixi448 – 456Combined sources9
Helixi471 – 474Combined sources4
Helixi478 – 498Combined sources21
Helixi502 – 507Combined sources6
Helixi511 – 514Combined sources4
Turni519 – 521Combined sources3
Helixi525 – 530Combined sources6
Helixi537 – 546Combined sources10
Helixi561 – 567Combined sources7
Helixi572 – 579Combined sources8
Helixi594 – 601Combined sources8
Helixi604 – 613Combined sources10
Helixi627 – 630Combined sources4
Helixi633 – 639Combined sources7
Helixi1031 – 1037Combined sources7
Helixi1041 – 1043Combined sources3
Helixi1044 – 1049Combined sources6
Helixi1054 – 1058Combined sources5
Helixi1062 – 1067Combined sources6
Helixi1073 – 1086Combined sources14
Beta strandi1107 – 1110Combined sources4
Helixi1116 – 1127Combined sources12
Turni1133 – 1139Combined sources7
Beta strandi1145 – 1154Combined sources10
Helixi1156 – 1172Combined sources17
Turni1173 – 1175Combined sources3
Beta strandi1179 – 1184Combined sources6
Helixi1189 – 1195Combined sources7
Helixi1199 – 1201Combined sources3
Helixi1202 – 1205Combined sources4
Beta strandi1210 – 1217Combined sources8
Helixi1218 – 1222Combined sources5
Turni1223 – 1226Combined sources4
Helixi1228 – 1230Combined sources3
Turni1235 – 1237Combined sources3
Beta strandi1243 – 1245Combined sources3
Beta strandi1247 – 1255Combined sources9
Beta strandi1258 – 1262Combined sources5
Beta strandi1268 – 1270Combined sources3
Beta strandi1276 – 1280Combined sources5
Beta strandi1282 – 1284Combined sources3
Beta strandi1286 – 1289Combined sources4
Beta strandi1291 – 1296Combined sources6
Helixi1297 – 1299Combined sources3
Beta strandi1300 – 1310Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4OA7X-ray2.30A/B/C/D1105-1313[»]
4TORX-ray1.50A/B/C/D1105-1315[»]
4TOSX-ray1.80A/B1105-1315[»]
4U6AX-ray2.37A1091-1325[»]
4UUHX-ray2.52A1091-1325[»]
4UW1X-ray3.37A/B/C/D/E/F/G/H1091-1325[»]
4W5SX-ray2.80A1105-1314[»]
4W6EX-ray1.95A1106-1314[»]
5EBTX-ray2.24A/B/C/D1106-1314[»]
5ECEX-ray2.20A/B/C/D1105-1316[»]
5ETYX-ray2.90A/B/C/D1091-1324[»]
5JHQX-ray3.20A/B/C/D174-649[»]
5JTIX-ray2.90A/B/C/D/E/F1018-1093[»]
5JU5X-ray2.50A/B/C/D/E/F1018-1093[»]
5KNIX-ray2.50A/B/C/D/E/F/G1026-1091[»]
ProteinModelPortaliO95271.
SMRiO95271.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO95271.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati181 – 209ANK 1Sequence analysisAdd BLAST29
Repeati215 – 244ANK 2Sequence analysisAdd BLAST30
Repeati248 – 277ANK 3Sequence analysisAdd BLAST30
Repeati281 – 310ANK 4Sequence analysisAdd BLAST30
Repeati335 – 364ANK 5Sequence analysisAdd BLAST30
Repeati368 – 397ANK 6Sequence analysisAdd BLAST30
Repeati401 – 430ANK 7Sequence analysisAdd BLAST30
Repeati434 – 463ANK 8Sequence analysisAdd BLAST30
Repeati521 – 553ANK 9Sequence analysisAdd BLAST33
Repeati557 – 586ANK 10Sequence analysisAdd BLAST30
Repeati590 – 619ANK 11Sequence analysisAdd BLAST30
Repeati621 – 647ANK 12Sequence analysisAdd BLAST27
Repeati649 – 679ANK 13Sequence analysisAdd BLAST31
Repeati683 – 712ANK 14Sequence analysisAdd BLAST30
Repeati716 – 745ANK 15Sequence analysisAdd BLAST30
Repeati749 – 778ANK 16Sequence analysisAdd BLAST30
Repeati782 – 810ANK 17Sequence analysisAdd BLAST29
Repeati836 – 865ANK 18Sequence analysisAdd BLAST30
Repeati869 – 898ANK 19Sequence analysisAdd BLAST30
Repeati902 – 931ANK 20Sequence analysisAdd BLAST30
Repeati935 – 964ANK 21Sequence analysisAdd BLAST30
Domaini1030 – 1089SAMPROSITE-ProRule annotationAdd BLAST60
Domaini1112 – 1317PARP catalyticPROSITE-ProRule annotationAdd BLAST206

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi9 – 14Poly-HisPROSITE-ProRule annotation6
Compositional biasi20 – 83Pro-richPROSITE-ProRule annotationAdd BLAST64
Compositional biasi109 – 161Ser-richPROSITE-ProRule annotationAdd BLAST53

Sequence similaritiesi

Contains 21 ANK repeats.PROSITE-ProRule annotation
Contains 1 PARP catalytic domain.PROSITE-ProRule annotation
Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiKOG4177. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00840000129677.
HOGENOMiHOG000246964.
HOVERGENiHBG059472.
InParanoidiO95271.
KOiK10799.
OMAiVYRGEQS.
OrthoDBiEOG091G00W8.
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.
IPR028731. TNKS.
[Graphical view]
PANTHERiPTHR24180:SF3. PTHR24180:SF3. 1 hit.
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 4 hits.
PF13606. Ank_3. 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. AlignAdd to basket

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

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti83P → Q in AAH98394 (PubMed:15489334).Curated1
Sequence conflicti802R → K in AAC79841 (PubMed:9822378).Curated1
Sequence conflicti802R → K in AAC79842 (PubMed:9822378).Curated1
Sequence conflicti1001E → G in AAH98394 (PubMed:15489334).Curated1
Sequence conflicti1266M → I in AAH98394 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_004538641 – 643EST → GHS in isoform 2. 1 Publication3
Alternative sequenceiVSP_004539644 – 1327Missing in isoform 2. 1 PublicationAdd BLAST684

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
GeneIDi8658.
KEGGihsa:8658.
UCSCiuc003wss.4. 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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4OA7X-ray2.30A/B/C/D1105-1313[»]
4TORX-ray1.50A/B/C/D1105-1315[»]
4TOSX-ray1.80A/B1105-1315[»]
4U6AX-ray2.37A1091-1325[»]
4UUHX-ray2.52A1091-1325[»]
4UW1X-ray3.37A/B/C/D/E/F/G/H1091-1325[»]
4W5SX-ray2.80A1105-1314[»]
4W6EX-ray1.95A1106-1314[»]
5EBTX-ray2.24A/B/C/D1106-1314[»]
5ECEX-ray2.20A/B/C/D1105-1316[»]
5ETYX-ray2.90A/B/C/D1091-1324[»]
5JHQX-ray3.20A/B/C/D174-649[»]
5JTIX-ray2.90A/B/C/D/E/F1018-1093[»]
5JU5X-ray2.50A/B/C/D/E/F1018-1093[»]
5KNIX-ray2.50A/B/C/D/E/F/G1026-1091[»]
ProteinModelPortaliO95271.
SMRiO95271.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114207. 44 interactors.
DIPiDIP-36652N.
IntActiO95271. 20 interactors.
MINTiMINT-7026707.
STRINGi9606.ENSP00000311579.

Chemistry databases

BindingDBiO95271.
ChEMBLiCHEMBL6164.

Protein family/group databases

TCDBi1.I.1.1.3. the nuclear pore complex (npc) family.

PTM databases

iPTMnetiO95271.
PhosphoSitePlusiO95271.

Polymorphism and mutation databases

BioMutaiTNKS.

Proteomic databases

EPDiO95271.
MaxQBiO95271.
PaxDbiO95271.
PeptideAtlasiO95271.
PRIDEiO95271.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000310430; ENSP00000311579; ENSG00000173273. [O95271-1]
GeneIDi8658.
KEGGihsa:8658.
UCSCiuc003wss.4. human. [O95271-1]

Organism-specific databases

CTDi8658.
DisGeNETi8658.
GeneCardsiTNKS.
H-InvDBHIX0034248.
HGNCiHGNC:11941. TNKS.
HPAiHPA025690.
HPA062936.
MIMi603303. gene.
neXtProtiNX_O95271.
OpenTargetsiENSG00000173273.
PharmGKBiPA36631.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4177. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00840000129677.
HOGENOMiHOG000246964.
HOVERGENiHBG059472.
InParanoidiO95271.
KOiK10799.
OMAiVYRGEQS.
OrthoDBiEOG091G00W8.
PhylomeDBiO95271.
TreeFamiTF326036.

Enzyme and pathway databases

BioCyciZFISH:HS10642-MONOMER.
BRENDAi2.4.2.30. 2681.
ReactomeiR-HSA-201681. TCF dependent signaling in response to WNT.
R-HSA-4641257. Degradation of AXIN.
R-HSA-5545619. XAV939 inhibits tankyrase, stabilizing AXIN.
R-HSA-5689880. Ub-specific processing proteases.
SIGNORiO95271.

Miscellaneous databases

ChiTaRSiTNKS. human.
EvolutionaryTraceiO95271.
GeneWikiiTNKS.
GenomeRNAii8658.
PROiO95271.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000173273.
CleanExiHS_TNKS.
ExpressionAtlasiO95271. baseline and differential.
GenevisibleiO95271. HS.

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.
IPR028731. TNKS.
[Graphical view]
PANTHERiPTHR24180:SF3. PTHR24180:SF3. 1 hit.
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 4 hits.
PF13606. Ank_3. 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 170 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.