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Protein

Tankyrase-2

Gene

TNKS2

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 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 poly-ADP-ribosylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates poly-ADP-ribosylation of TERF1, thereby contributing to the regulation of telomere length. May also regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles. Stimulates 26S proteasome activity.5 Publications

Catalytic activityi

NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.PROSITE-ProRule annotation2 Publications

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 bindingi1081ZincBy similarity1
Metal bindingi1084ZincBy similarity1
Metal bindingi1089ZincBy similarity1
Metal bindingi1092ZincBy similarity1

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • NAD+ ADP-ribosyltransferase activity Source: UniProtKB

GO - Biological processi

  • multicellular organism growth Source: Ensembl
  • negative regulation of telomere maintenance via telomere lengthening Source: BHF-UCL
  • positive regulation of canonical Wnt signaling pathway Source: UniProtKB
  • positive regulation of telomere capping Source: BHF-UCL
  • positive regulation of telomere maintenance via telomerase Source: BHF-UCL
  • protein ADP-ribosylation Source: BHF-UCL
  • protein auto-ADP-ribosylation Source: UniProtKB
  • protein localization to chromosome, telomeric region Source: BHF-UCL
  • protein polyubiquitination Source: UniProtKB
  • regulation of multicellular organism growth Source: Ensembl
  • Wnt signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Wnt signaling pathway

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

BioCyciZFISH:HS03037-MONOMER.
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.
SIGNORiQ9H2K2.

Names & Taxonomyi

Protein namesi
Recommended name:
Tankyrase-2 (EC:2.4.2.30)
Short name:
TANK2
Alternative name(s):
ADP-ribosyltransferase diphtheria toxin-like 6
Short name:
ARTD6
Poly [ADP-ribose] polymerase 5B
TNKS-2
TRF1-interacting ankyrin-related ADP-ribose polymerase 2
Tankyrase II
Tankyrase-like protein
Tankyrase-related protein
Gene namesi
Name:TNKS2
Synonyms:PARP5B, TANK2, TNKL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:15677. TNKS2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: BHF-UCL
  • cytosol Source: Reactome
  • Golgi membrane Source: UniProtKB-SubCell
  • nuclear chromosome, telomeric region Source: BHF-UCL
  • nuclear envelope Source: BHF-UCL
  • nucleus Source: BHF-UCL
  • pericentriolar material Source: BHF-UCL
  • perinuclear region of cytoplasm Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Golgi apparatus, Membrane, Nucleus, Telomere

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi553H → D: Enhanced hydroxylation by HIF1AN. 1 Publication1
Mutagenesisi553H → N: Enhanced hydroxylation by HIF1AN. 1 Publication1
Mutagenesisi1054M → V: Loss of activity. 1 Publication1

Organism-specific databases

DisGeNETi80351.
OpenTargetsiENSG00000107854.
PharmGKBiPA38019.

Chemistry databases

ChEMBLiCHEMBL6154.

Polymorphism and mutation databases

BioMutaiTNKS2.
DMDMi20140805.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002113341 – 1166Tankyrase-2Add BLAST1166

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei203(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication1
Modified residuei238(3S)-3-hydroxyhistidine; by HIF1AN; partial1 Publication1
Modified residuei271(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication1
Modified residuei427(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication1
Modified residuei518(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication1
Modified residuei553(3S)-3-hydroxyhistidine; by HIF1AN; partial1 Publication1
Modified residuei586(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication1
Modified residuei671(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication1
Modified residuei706(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication1
Modified residuei739(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication1

Post-translational modificationi

Ubiquitinated at 'Lys-48' and 'Lys-63' by RNF146 when auto-poly-ADP-ribosylated; this leads to degradation.
ADP-ribosylated (-auto). Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination.
The crystallographic evidence suggests that the 3-hydroxyhistidine may be the (3S) stereoisomer.

Keywords - PTMi

ADP-ribosylation, Hydroxylation, Ubl conjugation

Proteomic databases

EPDiQ9H2K2.
MaxQBiQ9H2K2.
PaxDbiQ9H2K2.
PeptideAtlasiQ9H2K2.
PRIDEiQ9H2K2.

PTM databases

iPTMnetiQ9H2K2.
PhosphoSitePlusiQ9H2K2.

Expressioni

Tissue specificityi

Highly expressed in placenta, skeletal muscle, liver, brain, kidney, heart, thymus, spinal cord, lung, peripheral blood leukocytes, pancreas, lymph nodes, spleen, prostate, testis, ovary, small intestine, colon, mammary gland, breast and breast carcinoma, and in common-type meningioma. Highly expressed in fetal liver, heart and brain.

Gene expression databases

BgeeiENSG00000107854.
CleanExiHS_TNKS2.
GenevisibleiQ9H2K2. HS.

Organism-specific databases

HPAiHPA036606.

Interactioni

Subunit structurei

Oligomerizes and associates with TNKS. Interacts with the cytoplasmic domain of LNPEP/Otase in SLC2A4/GLUT4-vesicles. Binds to the N-terminus of Grb14 and TRF1 with its ankyrin repeat region. Interacts with HIF1AN. Interacts with RNF146; this interaction leads to ubiquitination and proteasomal degradation.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ANKRD28O150843EBI-4398527,EBI-359567
AXIN1O151692EBI-4398527,EBI-710484
BABAM1Q9NWV84EBI-4398527,EBI-745725
BCRP112743EBI-4398527,EBI-712838
FAT4Q6V0I72EBI-4398527,EBI-948985
HIF1ANQ9NWT64EBI-4398527,EBI-745632
RAD54LQ926983EBI-4398527,EBI-5333483
SH3BP2P783145EBI-4398527,EBI-727062
Sh3bp2Q066496EBI-4398527,EBI-5323518From a different organism.
STRNO438152EBI-4398527,EBI-1046642
TERF1P542742EBI-4398527,EBI-710997

GO - Molecular functioni

  • enzyme binding Source: UniProtKB

Protein-protein interaction databases

BioGridi123257. 27 interactors.
DIPiDIP-42098N.
IntActiQ9H2K2. 33 interactors.
MINTiMINT-1183420.
STRINGi9606.ENSP00000360689.

Chemistry databases

BindingDBiQ9H2K2.

Structurei

Secondary structure

11166
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi488 – 502Combined sources15
Helixi505 – 511Combined sources7
Turni514 – 518Combined sources5
Turni522 – 525Combined sources4
Helixi529 – 535Combined sources7
Helixi539 – 547Combined sources9
Helixi562 – 568Combined sources7
Helixi572 – 580Combined sources9
Helixi595 – 602Combined sources8
Helixi605 – 613Combined sources9
Helixi628 – 631Combined sources4
Helixi637 – 644Combined sources8
Helixi876 – 884Combined sources9
Helixi888 – 890Combined sources3
Helixi891 – 896Combined sources6
Helixi901 – 904Combined sources4
Helixi909 – 914Combined sources6
Helixi920 – 936Combined sources17
Beta strandi954 – 957Combined sources4
Helixi964 – 974Combined sources11
Turni980 – 986Combined sources7
Beta strandi990 – 999Combined sources10
Helixi1003 – 1018Combined sources16
Turni1019 – 1021Combined sources3
Beta strandi1026 – 1031Combined sources6
Helixi1036 – 1042Combined sources7
Helixi1046 – 1048Combined sources3
Turni1053 – 1055Combined sources3
Beta strandi1059 – 1064Combined sources6
Helixi1065 – 1069Combined sources5
Turni1070 – 1073Combined sources4
Helixi1075 – 1077Combined sources3
Turni1082 – 1084Combined sources3
Beta strandi1090 – 1092Combined sources3
Beta strandi1094 – 1102Combined sources9
Beta strandi1105 – 1109Combined sources5
Beta strandi1115 – 1117Combined sources3
Beta strandi1123 – 1127Combined sources5
Beta strandi1131 – 1133Combined sources3
Beta strandi1138 – 1143Combined sources6
Helixi1144 – 1146Combined sources3
Beta strandi1147 – 1157Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Y0IX-ray2.28S538-558[»]
3KR7X-ray1.95A946-1162[»]
3KR8X-ray2.10A/C946-1162[»]
3MHJX-ray1.80A/B946-1162[»]
3MHKX-ray2.30A952-1166[»]
3P0NX-ray1.90A/C946-1162[»]
3P0PX-ray2.49A/C946-1162[»]
3P0QX-ray1.90A/C946-1162[»]
3TWQX-ray2.15A/B484-655[»]
3TWRX-ray1.55A/B/C/D488-649[»]
3TWSX-ray1.70A/B/C/D488-649[»]
3TWTX-ray1.85A/B/C/D488-649[»]
3TWUX-ray1.80A488-649[»]
3TWVX-ray2.30A/B/C/D488-649[»]
3TWWX-ray2.00A/B488-649[»]
3TWXX-ray1.80A/B488-649[»]
3U9HX-ray1.75A/B946-1162[»]
3U9YX-ray2.30A946-1162[»]
3UA9X-ray2.15A/B946-1162[»]
3W51X-ray2.00A/B952-1161[»]
4AVUX-ray2.40A/B946-1162[»]
4AVWX-ray2.15A/B946-1162[»]
4BFPX-ray2.40A/B946-1162[»]
4BJ9X-ray2.05A/B946-1162[»]
4BJBX-ray2.30A946-1162[»]
4BJCX-ray2.20A946-1162[»]
4BS4X-ray1.89A/B946-1162[»]
4BU3X-ray2.15A/B946-1162[»]
4BU5X-ray1.80A/B946-1162[»]
4BU6X-ray1.80A/B946-1162[»]
4BU7X-ray2.05A/C946-1162[»]
4BU8X-ray1.85A/C946-1162[»]
4BU9X-ray1.65A/B946-1162[»]
4BUAX-ray1.85A/C946-1162[»]
4BUDX-ray2.50A/C946-1162[»]
4BUEX-ray1.60A/B946-1162[»]
4BUFX-ray2.50A/B946-1162[»]
4BUIX-ray1.95A/C946-1162[»]
4BUSX-ray1.90A/B946-1162[»]
4BUTX-ray1.90A/B946-1162[»]
4BUUX-ray1.60A/B946-1162[»]
4BUVX-ray1.80A/C946-1162[»]
4BUWX-ray1.85A/B946-1162[»]
4BUXX-ray1.95A/C946-1162[»]
4BUYX-ray1.90A/B946-1162[»]
4HKIX-ray2.15A/H946-1113[»]
C/D1114-1162[»]
4HKKX-ray1.95A/C946-1113[»]
B/D1114-1162[»]
4HKNX-ray2.05A946-1113[»]
C1114-1162[»]
4HL5X-ray2.20A946-1113[»]
C1114-1162[»]
4HLFX-ray2.15A/B946-1113[»]
C/D1114-1162[»]
4HLGX-ray2.00A/B946-1113[»]
C/D1114-1162[»]
4HLHX-ray1.75A/B946-1113[»]
C/D1114-1162[»]
4HLKX-ray2.00A/B946-1113[»]
C/D1114-1162[»]
4HLMX-ray1.95A/B946-1113[»]
C/D1114-1162[»]
4HMHX-ray2.30A946-1113[»]
C1114-1162[»]
4HYFX-ray2.80A/B/C946-1162[»]
4IUEX-ray2.38A952-1161[»]
4J1ZX-ray2.00A/B952-1161[»]
4J21X-ray1.93A952-1161[»]
4J22X-ray2.12A/B952-1161[»]
4J3LX-ray2.09A952-1161[»]
4J3MX-ray1.90A/B952-1161[»]
4KZLX-ray2.00A/B946-1113[»]
C/D1114-1162[»]
4KZQX-ray2.25A/B946-1113[»]
C/D1114-1162[»]
4KZUX-ray2.10A/B946-1113[»]
C/D1114-1162[»]
4L09X-ray2.05A/B946-1113[»]
C/D1114-1162[»]
4L0BX-ray1.80A/B946-1113[»]
C/D1114-1162[»]
4L0IX-ray2.30A/B946-1113[»]
C/D1114-1162[»]
4L0SX-ray1.90A/B946-1113[»]
C/D1114-1162[»]
4L0TX-ray2.10A/B946-1113[»]
C/D1114-1162[»]
4L0VX-ray1.70A/B946-1113[»]
C/D1114-1162[»]
4L10X-ray1.70A/B946-1113[»]
C/D1114-1162[»]
4L2FX-ray2.05A/B946-1113[»]
C/D1114-1162[»]
4L2GX-ray2.05A/B946-1113[»]
C/D1114-1162[»]
4L2KX-ray2.10A/B946-1113[»]
C/D1114-1162[»]
4L31X-ray2.00A/B946-1113[»]
C/D1114-1162[»]
4L32X-ray1.85A/B946-1113[»]
C/D1114-1162[»]
4L33X-ray2.10A/B946-1113[»]
C/D1114-1162[»]
4L34X-ray1.80A/B946-1113[»]
C/D1114-1162[»]
4M7BX-ray1.95A/C946-1162[»]
4PMLX-ray1.87A/B/C/D959-1164[»]
4PNLX-ray1.50A/B/C/D959-1164[»]
4PNMX-ray2.19A/B/C/D959-1164[»]
4PNNX-ray1.65A/B/C/D959-1164[»]
4PNQX-ray1.85A/B/C/D959-1164[»]
4PNRX-ray1.71A/B/C/D959-1164[»]
4PNSX-ray1.65A/B/C/D959-1164[»]
4PNTX-ray1.60A/B/C/D959-1164[»]
4TJUX-ray1.57A/B/C/D959-1164[»]
4TJWX-ray1.70A/B/C/D959-1164[»]
4TJYX-ray1.90A/B/C/D959-1164[»]
4TK0X-ray1.65A/B/C/D959-1164[»]
4TK5X-ray2.02A/B/C/D959-1164[»]
4TKFX-ray2.60A/B/C/D959-1164[»]
4TKGX-ray1.95A/B/C/D959-1164[»]
4TKIX-ray2.15A/B/C/D959-1164[»]
4UFUX-ray2.10A/B946-1162[»]
4UFYX-ray1.70A/B946-1162[»]
4UHGX-ray1.70A/B946-1162[»]
4UI3X-ray2.00A/B946-1113[»]
C/D1115-1162[»]
4UI4X-ray2.40A/B946-1113[»]
C/D1115-1162[»]
4UI5X-ray1.65A/B946-1113[»]
C/D1115-1162[»]
4UI6X-ray1.80A/B946-1113[»]
C/D1115-1162[»]
4UI7X-ray1.80A/B946-1113[»]
C/D1115-1162[»]
4UI8X-ray2.05A/B946-1113[»]
C/D1115-1162[»]
4UVLX-ray2.00A/C946-1162[»]
4UVNX-ray2.20A/B946-1162[»]
4UVOX-ray1.85A/B946-1162[»]
4UVPX-ray1.75A/C946-1113[»]
B/D1115-1162[»]
4UVSX-ray2.00A/C946-1162[»]
4UVTX-ray1.95A/C946-1162[»]
4UVUX-ray1.95A/B946-1162[»]
4UVVX-ray1.90A/B946-1162[»]
4UVWX-ray2.10A/B946-1162[»]
4UVXX-ray1.95A/B946-1162[»]
4UVYX-ray1.95A/B946-1162[»]
4UVZX-ray1.60A/C946-1162[»]
4UX4X-ray1.80A/B946-1162[»]
4W5IX-ray1.95A/B952-1162[»]
4Z68X-ray1.86A490-644[»]
5ADQX-ray2.10A946-1113[»]
B1115-1162[»]
5ADRX-ray2.10A946-1113[»]
B1115-1162[»]
5ADSX-ray1.80A946-1113[»]
B1115-1162[»]
5ADTX-ray2.15A946-1113[»]
B1115-1162[»]
5AEHX-ray1.85A/B946-1162[»]
5AKUX-ray1.80A/B946-1162[»]
5AKWX-ray2.07A/B946-1162[»]
5AL1X-ray1.75A/B946-1162[»]
5AL2X-ray1.90A/B946-1162[»]
5AL3X-ray1.75A/B946-1162[»]
5AL4X-ray1.90A/B946-1162[»]
5AL5X-ray2.05A/B946-1162[»]
5BXOX-ray1.33A/B488-649[»]
5BXUX-ray1.35A488-649[»]
5C5PX-ray1.75A/B946-1113[»]
C/D1114-1162[»]
5C5QX-ray2.00A/B946-1113[»]
C/D1114-1162[»]
5C5RX-ray1.55A/B946-1113[»]
C/D1114-1162[»]
5DCZX-ray2.23A936-1166[»]
5JRTX-ray1.53A867-940[»]
ProteinModelPortaliQ9H2K2.
SMRiQ9H2K2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H2K2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati57 – 89ANK 1Add BLAST33
Repeati90 – 122ANK 2Add BLAST33
Repeati123 – 155ANK 3Add BLAST33
Repeati210 – 242ANK 4Add BLAST33
Repeati243 – 275ANK 5Add BLAST33
Repeati276 – 308ANK 6Add BLAST33
Repeati363 – 398ANK 7Add BLAST36
Repeati399 – 431ANK 8Add BLAST33
Repeati432 – 464ANK 9Add BLAST33
Repeati525 – 557ANK 10Add BLAST33
Repeati558 – 590ANK 11Add BLAST33
Repeati591 – 623ANK 12Add BLAST33
Repeati678 – 710ANK 13Add BLAST33
Repeati711 – 743ANK 14Add BLAST33
Repeati744 – 776ANK 15Add BLAST33
Domaini873 – 936SAMPROSITE-ProRule annotationAdd BLAST64
Domaini959 – 1164PARP catalyticPROSITE-ProRule annotationAdd BLAST206

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni545 – 553HIF1AN-binding9

Sequence similaritiesi

Contains 15 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.
InParanoidiQ9H2K2.
KOiK10799.
OMAiLSSGCDP.
OrthoDBiEOG091G00W8.
PhylomeDBiQ9H2K2.
TreeFamiTF326036.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
1.25.40.20. 7 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.
[Graphical view]
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 5 hits.
PF00644. PARP. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 15 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]

Sequencei

Sequence statusi: Complete.

Q9H2K2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGRRCAGGG AACASAAAEA VEPAARELFE ACRNGDVERV KRLVTPEKVN
60 70 80 90 100
SRDTAGRKST PLHFAAGFGR KDVVEYLLQN GANVQARDDG GLIPLHNACS
110 120 130 140 150
FGHAEVVNLL LRHGADPNAR DNWNYTPLHE AAIKGKIDVC IVLLQHGAEP
160 170 180 190 200
TIRNTDGRTA LDLADPSAKA VLTGEYKKDE LLESARSGNE EKMMALLTPL
210 220 230 240 250
NVNCHASDGR KSTPLHLAAG YNRVKIVQLL LQHGADVHAK DKGDLVPLHN
260 270 280 290 300
ACSYGHYEVT ELLVKHGACV NAMDLWQFTP LHEAASKNRV EVCSLLLSYG
310 320 330 340 350
ADPTLLNCHN KSAIDLAPTP QLKERLAYEF KGHSLLQAAR EADVTRIKKH
360 370 380 390 400
LSLEMVNFKH PQTHETALHC AAASPYPKRK QICELLLRKG ANINEKTKEF
410 420 430 440 450
LTPLHVASEK AHNDVVEVVV KHEAKVNALD NLGQTSLHRA AYCGHLQTCR
460 470 480 490 500
LLLSYGCDPN IISLQGFTAL QMGNENVQQL LQEGISLGNS EADRQLLEAA
510 520 530 540 550
KAGDVETVKK LCTVQSVNCR DIEGRQSTPL HFAAGYNRVS VVEYLLQHGA
560 570 580 590 600
DVHAKDKGGL VPLHNACSYG HYEVAELLVK HGAVVNVADL WKFTPLHEAA
610 620 630 640 650
AKGKYEICKL LLQHGADPTK KNRDGNTPLD LVKDGDTDIQ DLLRGDAALL
660 670 680 690 700
DAAKKGCLAR VKKLSSPDNV NCRDTQGRHS TPLHLAAGYN NLEVAEYLLQ
710 720 730 740 750
HGADVNAQDK GGLIPLHNAA SYGHVDVAAL LIKYNACVNA TDKWAFTPLH
760 770 780 790 800
EAAQKGRTQL CALLLAHGAD PTLKNQEGQT PLDLVSADDV SALLTAAMPP
810 820 830 840 850
SALPSCYKPQ VLNGVRSPGA TADALSSGPS SPSSLSAASS LDNLSGSFSE
860 870 880 890 900
LSSVVSSSGT EGASSLEKKE VPGVDFSITQ FVRNLGLEHL MDIFEREQIT
910 920 930 940 950
LDVLVEMGHK ELKEIGINAY GHRHKLIKGV ERLISGQQGL NPYLTLNTSG
960 970 980 990 1000
SGTILIDLSP DDKEFQSVEE EMQSTVREHR DGGHAGGIFN RYNILKIQKV
1010 1020 1030 1040 1050
CNKKLWERYT HRRKEVSEEN HNHANERMLF HGSPFVNAII HKGFDERHAY
1060 1070 1080 1090 1100
IGGMFGAGIY FAENSSKSNQ YVYGIGGGTG CPVHKDRSCY ICHRQLLFCR
1110 1120 1130 1140 1150
VTLGKSFLQF SAMKMAHSPP GHHSVTGRPS VNGLALAEYV IYRGEQAYPE
1160
YLITYQIMRP EGMVDG
Length:1,166
Mass (Da):126,918
Last modified:March 1, 2001 - v1
Checksum:i4C8B3B8D97CEF704
GO

Sequence cautioni

The sequence AAG25674 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAB14665 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti115A → T in BAG37180 (PubMed:14702039).Curated1
Sequence conflicti331 – 337KGHSLLQ → QRPLVAA in AAG25674 (PubMed:11205898).Curated7
Sequence conflicti357 – 361NFKHP → IQAS in AAG25674 (PubMed:11205898).Curated5
Sequence conflicti966Q → P in BAB14665 (PubMed:14702039).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF305081 mRNA. Translation: AAG25674.1. Different initiation.
AF264912 mRNA. Translation: AAG44694.1.
AF329696 mRNA. Translation: AAK13463.1.
AF342982 mRNA. Translation: AAK25811.1.
AF309033 mRNA. Translation: AAK82330.1.
AF438201 mRNA. Translation: AAL40795.1.
AK023746 mRNA. Translation: BAB14665.1. Different initiation.
AK314612 mRNA. Translation: BAG37180.1.
AL359707 Genomic DNA. Translation: CAC78760.1.
CCDSiCCDS7417.1.
RefSeqiNP_079511.1. NM_025235.3.
UniGeneiHs.329327.

Genome annotation databases

EnsembliENST00000371627; ENSP00000360689; ENSG00000107854.
GeneIDi80351.
KEGGihsa:80351.
UCSCiuc001khp.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF305081 mRNA. Translation: AAG25674.1. Different initiation.
AF264912 mRNA. Translation: AAG44694.1.
AF329696 mRNA. Translation: AAK13463.1.
AF342982 mRNA. Translation: AAK25811.1.
AF309033 mRNA. Translation: AAK82330.1.
AF438201 mRNA. Translation: AAL40795.1.
AK023746 mRNA. Translation: BAB14665.1. Different initiation.
AK314612 mRNA. Translation: BAG37180.1.
AL359707 Genomic DNA. Translation: CAC78760.1.
CCDSiCCDS7417.1.
RefSeqiNP_079511.1. NM_025235.3.
UniGeneiHs.329327.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Y0IX-ray2.28S538-558[»]
3KR7X-ray1.95A946-1162[»]
3KR8X-ray2.10A/C946-1162[»]
3MHJX-ray1.80A/B946-1162[»]
3MHKX-ray2.30A952-1166[»]
3P0NX-ray1.90A/C946-1162[»]
3P0PX-ray2.49A/C946-1162[»]
3P0QX-ray1.90A/C946-1162[»]
3TWQX-ray2.15A/B484-655[»]
3TWRX-ray1.55A/B/C/D488-649[»]
3TWSX-ray1.70A/B/C/D488-649[»]
3TWTX-ray1.85A/B/C/D488-649[»]
3TWUX-ray1.80A488-649[»]
3TWVX-ray2.30A/B/C/D488-649[»]
3TWWX-ray2.00A/B488-649[»]
3TWXX-ray1.80A/B488-649[»]
3U9HX-ray1.75A/B946-1162[»]
3U9YX-ray2.30A946-1162[»]
3UA9X-ray2.15A/B946-1162[»]
3W51X-ray2.00A/B952-1161[»]
4AVUX-ray2.40A/B946-1162[»]
4AVWX-ray2.15A/B946-1162[»]
4BFPX-ray2.40A/B946-1162[»]
4BJ9X-ray2.05A/B946-1162[»]
4BJBX-ray2.30A946-1162[»]
4BJCX-ray2.20A946-1162[»]
4BS4X-ray1.89A/B946-1162[»]
4BU3X-ray2.15A/B946-1162[»]
4BU5X-ray1.80A/B946-1162[»]
4BU6X-ray1.80A/B946-1162[»]
4BU7X-ray2.05A/C946-1162[»]
4BU8X-ray1.85A/C946-1162[»]
4BU9X-ray1.65A/B946-1162[»]
4BUAX-ray1.85A/C946-1162[»]
4BUDX-ray2.50A/C946-1162[»]
4BUEX-ray1.60A/B946-1162[»]
4BUFX-ray2.50A/B946-1162[»]
4BUIX-ray1.95A/C946-1162[»]
4BUSX-ray1.90A/B946-1162[»]
4BUTX-ray1.90A/B946-1162[»]
4BUUX-ray1.60A/B946-1162[»]
4BUVX-ray1.80A/C946-1162[»]
4BUWX-ray1.85A/B946-1162[»]
4BUXX-ray1.95A/C946-1162[»]
4BUYX-ray1.90A/B946-1162[»]
4HKIX-ray2.15A/H946-1113[»]
C/D1114-1162[»]
4HKKX-ray1.95A/C946-1113[»]
B/D1114-1162[»]
4HKNX-ray2.05A946-1113[»]
C1114-1162[»]
4HL5X-ray2.20A946-1113[»]
C1114-1162[»]
4HLFX-ray2.15A/B946-1113[»]
C/D1114-1162[»]
4HLGX-ray2.00A/B946-1113[»]
C/D1114-1162[»]
4HLHX-ray1.75A/B946-1113[»]
C/D1114-1162[»]
4HLKX-ray2.00A/B946-1113[»]
C/D1114-1162[»]
4HLMX-ray1.95A/B946-1113[»]
C/D1114-1162[»]
4HMHX-ray2.30A946-1113[»]
C1114-1162[»]
4HYFX-ray2.80A/B/C946-1162[»]
4IUEX-ray2.38A952-1161[»]
4J1ZX-ray2.00A/B952-1161[»]
4J21X-ray1.93A952-1161[»]
4J22X-ray2.12A/B952-1161[»]
4J3LX-ray2.09A952-1161[»]
4J3MX-ray1.90A/B952-1161[»]
4KZLX-ray2.00A/B946-1113[»]
C/D1114-1162[»]
4KZQX-ray2.25A/B946-1113[»]
C/D1114-1162[»]
4KZUX-ray2.10A/B946-1113[»]
C/D1114-1162[»]
4L09X-ray2.05A/B946-1113[»]
C/D1114-1162[»]
4L0BX-ray1.80A/B946-1113[»]
C/D1114-1162[»]
4L0IX-ray2.30A/B946-1113[»]
C/D1114-1162[»]
4L0SX-ray1.90A/B946-1113[»]
C/D1114-1162[»]
4L0TX-ray2.10A/B946-1113[»]
C/D1114-1162[»]
4L0VX-ray1.70A/B946-1113[»]
C/D1114-1162[»]
4L10X-ray1.70A/B946-1113[»]
C/D1114-1162[»]
4L2FX-ray2.05A/B946-1113[»]
C/D1114-1162[»]
4L2GX-ray2.05A/B946-1113[»]
C/D1114-1162[»]
4L2KX-ray2.10A/B946-1113[»]
C/D1114-1162[»]
4L31X-ray2.00A/B946-1113[»]
C/D1114-1162[»]
4L32X-ray1.85A/B946-1113[»]
C/D1114-1162[»]
4L33X-ray2.10A/B946-1113[»]
C/D1114-1162[»]
4L34X-ray1.80A/B946-1113[»]
C/D1114-1162[»]
4M7BX-ray1.95A/C946-1162[»]
4PMLX-ray1.87A/B/C/D959-1164[»]
4PNLX-ray1.50A/B/C/D959-1164[»]
4PNMX-ray2.19A/B/C/D959-1164[»]
4PNNX-ray1.65A/B/C/D959-1164[»]
4PNQX-ray1.85A/B/C/D959-1164[»]
4PNRX-ray1.71A/B/C/D959-1164[»]
4PNSX-ray1.65A/B/C/D959-1164[»]
4PNTX-ray1.60A/B/C/D959-1164[»]
4TJUX-ray1.57A/B/C/D959-1164[»]
4TJWX-ray1.70A/B/C/D959-1164[»]
4TJYX-ray1.90A/B/C/D959-1164[»]
4TK0X-ray1.65A/B/C/D959-1164[»]
4TK5X-ray2.02A/B/C/D959-1164[»]
4TKFX-ray2.60A/B/C/D959-1164[»]
4TKGX-ray1.95A/B/C/D959-1164[»]
4TKIX-ray2.15A/B/C/D959-1164[»]
4UFUX-ray2.10A/B946-1162[»]
4UFYX-ray1.70A/B946-1162[»]
4UHGX-ray1.70A/B946-1162[»]
4UI3X-ray2.00A/B946-1113[»]
C/D1115-1162[»]
4UI4X-ray2.40A/B946-1113[»]
C/D1115-1162[»]
4UI5X-ray1.65A/B946-1113[»]
C/D1115-1162[»]
4UI6X-ray1.80A/B946-1113[»]
C/D1115-1162[»]
4UI7X-ray1.80A/B946-1113[»]
C/D1115-1162[»]
4UI8X-ray2.05A/B946-1113[»]
C/D1115-1162[»]
4UVLX-ray2.00A/C946-1162[»]
4UVNX-ray2.20A/B946-1162[»]
4UVOX-ray1.85A/B946-1162[»]
4UVPX-ray1.75A/C946-1113[»]
B/D1115-1162[»]
4UVSX-ray2.00A/C946-1162[»]
4UVTX-ray1.95A/C946-1162[»]
4UVUX-ray1.95A/B946-1162[»]
4UVVX-ray1.90A/B946-1162[»]
4UVWX-ray2.10A/B946-1162[»]
4UVXX-ray1.95A/B946-1162[»]
4UVYX-ray1.95A/B946-1162[»]
4UVZX-ray1.60A/C946-1162[»]
4UX4X-ray1.80A/B946-1162[»]
4W5IX-ray1.95A/B952-1162[»]
4Z68X-ray1.86A490-644[»]
5ADQX-ray2.10A946-1113[»]
B1115-1162[»]
5ADRX-ray2.10A946-1113[»]
B1115-1162[»]
5ADSX-ray1.80A946-1113[»]
B1115-1162[»]
5ADTX-ray2.15A946-1113[»]
B1115-1162[»]
5AEHX-ray1.85A/B946-1162[»]
5AKUX-ray1.80A/B946-1162[»]
5AKWX-ray2.07A/B946-1162[»]
5AL1X-ray1.75A/B946-1162[»]
5AL2X-ray1.90A/B946-1162[»]
5AL3X-ray1.75A/B946-1162[»]
5AL4X-ray1.90A/B946-1162[»]
5AL5X-ray2.05A/B946-1162[»]
5BXOX-ray1.33A/B488-649[»]
5BXUX-ray1.35A488-649[»]
5C5PX-ray1.75A/B946-1113[»]
C/D1114-1162[»]
5C5QX-ray2.00A/B946-1113[»]
C/D1114-1162[»]
5C5RX-ray1.55A/B946-1113[»]
C/D1114-1162[»]
5DCZX-ray2.23A936-1166[»]
5JRTX-ray1.53A867-940[»]
ProteinModelPortaliQ9H2K2.
SMRiQ9H2K2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123257. 27 interactors.
DIPiDIP-42098N.
IntActiQ9H2K2. 33 interactors.
MINTiMINT-1183420.
STRINGi9606.ENSP00000360689.

Chemistry databases

BindingDBiQ9H2K2.
ChEMBLiCHEMBL6154.

PTM databases

iPTMnetiQ9H2K2.
PhosphoSitePlusiQ9H2K2.

Polymorphism and mutation databases

BioMutaiTNKS2.
DMDMi20140805.

Proteomic databases

EPDiQ9H2K2.
MaxQBiQ9H2K2.
PaxDbiQ9H2K2.
PeptideAtlasiQ9H2K2.
PRIDEiQ9H2K2.

Protocols and materials databases

DNASUi80351.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371627; ENSP00000360689; ENSG00000107854.
GeneIDi80351.
KEGGihsa:80351.
UCSCiuc001khp.4. human.

Organism-specific databases

CTDi80351.
DisGeNETi80351.
GeneCardsiTNKS2.
HGNCiHGNC:15677. TNKS2.
HPAiHPA036606.
MIMi607128. gene.
neXtProtiNX_Q9H2K2.
OpenTargetsiENSG00000107854.
PharmGKBiPA38019.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4177. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00840000129677.
HOGENOMiHOG000246964.
HOVERGENiHBG059472.
InParanoidiQ9H2K2.
KOiK10799.
OMAiLSSGCDP.
OrthoDBiEOG091G00W8.
PhylomeDBiQ9H2K2.
TreeFamiTF326036.

Enzyme and pathway databases

BioCyciZFISH:HS03037-MONOMER.
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.
SIGNORiQ9H2K2.

Miscellaneous databases

ChiTaRSiTNKS2. human.
EvolutionaryTraceiQ9H2K2.
GeneWikiiTNKS2.
GenomeRNAii80351.
PROiQ9H2K2.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000107854.
CleanExiHS_TNKS2.
GenevisibleiQ9H2K2. HS.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
1.25.40.20. 7 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.
[Graphical view]
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 5 hits.
PF00644. PARP. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 15 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 nameiTNKS2_HUMAN
AccessioniPrimary (citable) accession number: Q9H2K2
Secondary accession number(s): B2RBD3, Q9H8F2, Q9HAS4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: March 1, 2001
Last modified: November 30, 2016
This is version 164 of the entry and version 1 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 10
    Human chromosome 10: 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.