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Q9H2K2

- TNKS2_HUMAN

UniProt

Q9H2K2 - TNKS2_HUMAN

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Protein

Tankyrase-2

Gene

TNKS2

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 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.2 PublicationsPROSITE-ProRule annotation

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 bindingi1081 – 10811ZincBy similarity
Metal bindingi1084 – 10841ZincBy similarity
Metal bindingi1089 – 10891ZincBy similarity
Metal bindingi1092 – 10921ZincBy similarity

GO - Molecular functioni

  1. enzyme binding Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW
  3. NAD+ ADP-ribosyltransferase activity Source: UniProtKB

GO - Biological processi

  1. multicellular organism growth Source: Ensembl
  2. positive regulation of canonical Wnt signaling pathway Source: UniProtKB
  3. positive regulation of telomere maintenance via telomerase Source: BHF-UCL
  4. protein ADP-ribosylation Source: BHF-UCL
  5. protein auto-ADP-ribosylation Source: UniProtKB
  6. protein localization to chromosome, telomeric region Source: BHF-UCL
  7. protein polyubiquitination Source: UniProtKB
  8. regulation of multicellular organism growth Source: Ensembl
  9. Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Wnt signaling pathway

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

ReactomeiREACT_200766. degradation of AXIN.
REACT_200777. TCF dependent signaling in response to WNT.
REACT_228279. XAV939 inhibits tankyrase, stabilizing AXIN.

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
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:15677. TNKS2.

Subcellular locationi

Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Nucleus. Chromosometelomere Curated
Note: Associated with the Golgi and with juxtanuclear SLC2A4/GLUT4-vesicles. Also found around the pericentriolar matrix of mitotic centromeres. During interphase, a small fraction of TNKS2 is found in the nucleus, associated with TRF1.

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. Golgi apparatus Source: UniProtKB-KW
  3. membrane Source: UniProtKB-KW
  4. nuclear chromosome, telomeric region Source: BHF-UCL
  5. nuclear envelope Source: BHF-UCL
  6. nucleus Source: BHF-UCL
  7. pericentriolar material Source: BHF-UCL
  8. 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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi553 – 5531H → D: Enhanced hydroxylation by HIF1AN. 1 Publication
Mutagenesisi553 – 5531H → N: Enhanced hydroxylation by HIF1AN. 1 Publication
Mutagenesisi1054 – 10541M → V: Loss of activity. 1 Publication

Organism-specific databases

PharmGKBiPA38019.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11661166Tankyrase-2PRO_0000211334Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei203 – 2031(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
Modified residuei238 – 2381(3S)-3-hydroxyhistidine; by HIF1AN; partial1 Publication
Modified residuei271 – 2711(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
Modified residuei427 – 4271(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
Modified residuei518 – 5181(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
Modified residuei553 – 5531(3S)-3-hydroxyhistidine; by HIF1AN; partial1 Publication
Modified residuei586 – 5861(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
Modified residuei671 – 6711(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
Modified residuei706 – 7061(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
Modified residuei739 – 7391(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication

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

MaxQBiQ9H2K2.
PaxDbiQ9H2K2.
PRIDEiQ9H2K2.

PTM databases

PhosphoSiteiQ9H2K2.

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

BgeeiQ9H2K2.
CleanExiHS_TNKS2.
GenevestigatoriQ9H2K2.

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
HIF1ANQ9NWT63EBI-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

Protein-protein interaction databases

BioGridi123257. 16 interactions.
DIPiDIP-42098N.
IntActiQ9H2K2. 32 interactions.
MINTiMINT-1183420.
STRINGi9606.ENSP00000360689.

Structurei

Secondary structure

1
1166
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi491 – 50212Combined sources
Helixi505 – 5117Combined sources
Turni514 – 5185Combined sources
Turni522 – 5254Combined sources
Helixi529 – 5357Combined sources
Helixi539 – 5479Combined sources
Helixi562 – 5687Combined sources
Helixi572 – 5809Combined sources
Helixi595 – 6017Combined sources
Helixi605 – 6139Combined sources
Helixi629 – 6313Combined sources
Helixi637 – 6448Combined sources
Beta strandi954 – 9574Combined sources
Helixi963 – 97412Combined sources
Turni980 – 9867Combined sources
Beta strandi992 – 100110Combined sources
Helixi1003 – 101816Combined sources
Turni1019 – 10224Combined sources
Beta strandi1026 – 10316Combined sources
Helixi1036 – 10427Combined sources
Helixi1046 – 10483Combined sources
Beta strandi1057 – 10648Combined sources
Helixi1065 – 10695Combined sources
Turni1070 – 10734Combined sources
Helixi1075 – 10773Combined sources
Turni1082 – 10843Combined sources
Beta strandi1090 – 10923Combined sources
Beta strandi1094 – 11029Combined sources
Beta strandi1105 – 11117Combined sources
Beta strandi1115 – 11173Combined sources
Beta strandi1123 – 11319Combined sources
Beta strandi1138 – 11425Combined sources
Helixi1144 – 11463Combined sources
Beta strandi1147 – 115711Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ9H2K2.
SMRiQ9H2K2. Positions 24-826, 877-936, 952-1161.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H2K2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati57 – 8933ANK 1Add
BLAST
Repeati90 – 12233ANK 2Add
BLAST
Repeati123 – 15533ANK 3Add
BLAST
Repeati210 – 24233ANK 4Add
BLAST
Repeati243 – 27533ANK 5Add
BLAST
Repeati276 – 30833ANK 6Add
BLAST
Repeati363 – 39836ANK 7Add
BLAST
Repeati399 – 43133ANK 8Add
BLAST
Repeati432 – 46433ANK 9Add
BLAST
Repeati525 – 55733ANK 10Add
BLAST
Repeati558 – 59033ANK 11Add
BLAST
Repeati591 – 62333ANK 12Add
BLAST
Repeati678 – 71033ANK 13Add
BLAST
Repeati711 – 74333ANK 14Add
BLAST
Repeati744 – 77633ANK 15Add
BLAST
Domaini873 – 93664SAMPROSITE-ProRule annotationAdd
BLAST
Domaini959 – 1164206PARP catalyticPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni545 – 5539HIF1AN-binding

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

eggNOGiCOG0666.
GeneTreeiENSGT00760000118950.
HOGENOMiHOG000246964.
HOVERGENiHBG059472.
InParanoidiQ9H2K2.
KOiK10799.
OMAiPYLTLNN.
OrthoDBiEOG7N8ZTP.
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.
IPR011510. SAM_2.
[Graphical view]
PfamiPF00023. Ank. 2 hits.
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 AAG25674.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAB14665.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti115 – 1151A → T in BAG37180. (PubMed:14702039)Curated
Sequence conflicti331 – 3377KGHSLLQ → QRPLVAA in AAG25674. (PubMed:11205898)Curated
Sequence conflicti357 – 3615NFKHP → IQAS in AAG25674. (PubMed:11205898)Curated
Sequence conflicti966 – 9661Q → P in BAB14665. (PubMed:14702039)Curated

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.3. human.

Polymorphism databases

DMDMi20140805.

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 .
CCDSi CCDS7417.1.
RefSeqi NP_079511.1. NM_025235.3.
UniGenei Hs.329327.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2Y0I X-ray 2.28 S 538-558 [» ]
3KR7 X-ray 1.95 A 946-1162 [» ]
3KR8 X-ray 2.10 A/C 946-1162 [» ]
3MHJ X-ray 1.80 A/B 946-1162 [» ]
3MHK X-ray 2.30 A 952-1166 [» ]
3P0N X-ray 1.90 A/C 946-1162 [» ]
3P0P X-ray 2.49 A/C 946-1162 [» ]
3P0Q X-ray 1.90 A/C 946-1162 [» ]
3TWQ X-ray 2.15 A/B 484-655 [» ]
3TWR X-ray 1.55 A/B/C/D 488-649 [» ]
3TWS X-ray 1.70 A/B/C/D 488-649 [» ]
3TWT X-ray 1.85 A/B/C/D 488-649 [» ]
3TWU X-ray 1.80 A 488-649 [» ]
3TWV X-ray 2.30 A/B/C/D 488-649 [» ]
3TWW X-ray 2.00 A/B 488-649 [» ]
3TWX X-ray 1.80 A/B 488-649 [» ]
3U9H X-ray 1.75 A/B 946-1162 [» ]
3U9Y X-ray 2.30 A 946-1162 [» ]
3UA9 X-ray 2.15 A/B 946-1162 [» ]
3W51 X-ray 2.00 A/B 952-1161 [» ]
4AVU X-ray 2.40 A/B 946-1162 [» ]
4AVW X-ray 2.15 A/B 946-1162 [» ]
4BFP X-ray 2.40 A/B 946-1162 [» ]
4BJ9 X-ray 2.05 A/B 946-1162 [» ]
4BJB X-ray 2.30 A 946-1162 [» ]
4BJC X-ray 2.20 A 946-1162 [» ]
4BS4 X-ray 1.89 A/B 946-1162 [» ]
4BU3 X-ray 2.15 A/B 946-1162 [» ]
4BU5 X-ray 1.80 A/B 946-1162 [» ]
4BU6 X-ray 1.80 A/B 946-1162 [» ]
4BU7 X-ray 2.05 A/C 946-1162 [» ]
4BU8 X-ray 1.85 A/C 946-1162 [» ]
4BU9 X-ray 1.65 A/B 946-1162 [» ]
4BUA X-ray 1.85 A/C 946-1162 [» ]
4BUD X-ray 2.50 A/C 946-1162 [» ]
4BUE X-ray 1.60 A/B 946-1162 [» ]
4BUF X-ray 2.50 A/B 946-1162 [» ]
4BUI X-ray 1.95 A/C 946-1162 [» ]
4BUS X-ray 1.90 A/B 946-1162 [» ]
4BUT X-ray 1.90 A/B 946-1162 [» ]
4BUU X-ray 1.60 A/B 946-1162 [» ]
4BUV X-ray 1.80 A/C 946-1162 [» ]
4BUW X-ray 1.85 A/B 946-1162 [» ]
4BUX X-ray 1.95 A/C 946-1162 [» ]
4BUY X-ray 1.90 A/B 946-1162 [» ]
4HKI X-ray 2.15 A/H 946-1113 [» ]
C/D 1114-1162 [» ]
4HKK X-ray 1.95 A/C 946-1113 [» ]
B/D 1114-1162 [» ]
4HKN X-ray 2.05 A 946-1113 [» ]
C 1114-1162 [» ]
4HL5 X-ray 2.20 A 946-1113 [» ]
C 1114-1162 [» ]
4HLF X-ray 2.15 A/B 946-1113 [» ]
C/D 1114-1162 [» ]
4HLG X-ray 2.00 A/B 946-1113 [» ]
C/D 1114-1162 [» ]
4HLH X-ray 1.75 A/B 946-1113 [» ]
C/D 1114-1162 [» ]
4HLK X-ray 2.00 A/B 946-1113 [» ]
C/D 1114-1162 [» ]
4HLM X-ray 1.95 A/B 946-1113 [» ]
C/D 1114-1162 [» ]
4HMH X-ray 2.30 A 946-1113 [» ]
C 1114-1162 [» ]
4HYF X-ray 2.80 A/B/C 946-1162 [» ]
4IUE X-ray 2.38 A 952-1161 [» ]
4J1Z X-ray 2.00 A/B 952-1161 [» ]
4J21 X-ray 1.93 A 952-1161 [» ]
4J22 X-ray 2.12 A/B 952-1161 [» ]
4J3L X-ray 2.09 A 952-1161 [» ]
4J3M X-ray 1.90 A/B 952-1161 [» ]
4KZL X-ray 2.00 A/B 946-1113 [» ]
C/D 1114-1162 [» ]
4KZQ X-ray 2.25 A/B 946-1113 [» ]
C/D 1114-1162 [» ]
4KZU X-ray 2.10 A/B 946-1113 [» ]
C/D 1114-1162 [» ]
4L09 X-ray 2.05 A/B 946-1113 [» ]
C/D 1114-1162 [» ]
4L0B X-ray 1.80 A/B 946-1113 [» ]
C/D 1114-1162 [» ]
4L0I X-ray 2.30 A/B 946-1113 [» ]
C/D 1114-1162 [» ]
4L0S X-ray 1.90 A/B 946-1113 [» ]
C/D 1114-1162 [» ]
4L0T X-ray 2.10 A/B 946-1113 [» ]
C/D 1114-1162 [» ]
4L0V X-ray 1.70 A/B 946-1113 [» ]
C/D 1114-1162 [» ]
4L10 X-ray 1.70 A/B 946-1113 [» ]
C/D 1114-1162 [» ]
4L2F X-ray 2.05 A/B 946-1113 [» ]
C/D 1114-1162 [» ]
4L2G X-ray 2.05 A/B 946-1113 [» ]
C/D 1114-1162 [» ]
4L2K X-ray 2.10 A/B 946-1113 [» ]
C/D 1114-1162 [» ]
4L31 X-ray 2.00 A/B 946-1113 [» ]
C/D 1114-1162 [» ]
4L32 X-ray 1.85 A/B 946-1113 [» ]
C/D 1114-1162 [» ]
4L33 X-ray 2.10 A/B 946-1113 [» ]
C/D 1114-1162 [» ]
4L34 X-ray 1.80 A/B 946-1113 [» ]
C/D 1114-1162 [» ]
4M7B X-ray 1.95 A/C 946-1162 [» ]
ProteinModelPortali Q9H2K2.
SMRi Q9H2K2. Positions 24-826, 877-936, 952-1161.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123257. 16 interactions.
DIPi DIP-42098N.
IntActi Q9H2K2. 32 interactions.
MINTi MINT-1183420.
STRINGi 9606.ENSP00000360689.

Chemistry

BindingDBi Q9H2K2.
ChEMBLi CHEMBL3038515.

PTM databases

PhosphoSitei Q9H2K2.

Polymorphism databases

DMDMi 20140805.

Proteomic databases

MaxQBi Q9H2K2.
PaxDbi Q9H2K2.
PRIDEi Q9H2K2.

Protocols and materials databases

DNASUi 80351.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000371627 ; ENSP00000360689 ; ENSG00000107854 .
GeneIDi 80351.
KEGGi hsa:80351.
UCSCi uc001khp.3. human.

Organism-specific databases

CTDi 80351.
GeneCardsi GC10P093548.
HGNCi HGNC:15677. TNKS2.
HPAi HPA036606.
MIMi 607128. gene.
neXtProti NX_Q9H2K2.
PharmGKBi PA38019.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0666.
GeneTreei ENSGT00760000118950.
HOGENOMi HOG000246964.
HOVERGENi HBG059472.
InParanoidi Q9H2K2.
KOi K10799.
OMAi PYLTLNN.
OrthoDBi EOG7N8ZTP.
PhylomeDBi Q9H2K2.
TreeFami TF326036.

Enzyme and pathway databases

Reactomei REACT_200766. degradation of AXIN.
REACT_200777. TCF dependent signaling in response to WNT.
REACT_228279. XAV939 inhibits tankyrase, stabilizing AXIN.

Miscellaneous databases

ChiTaRSi TNKS2. human.
EvolutionaryTracei Q9H2K2.
GeneWikii TNKS2.
GenomeRNAii 80351.
NextBioi 70966.
PROi Q9H2K2.
SOURCEi Search...

Gene expression databases

Bgeei Q9H2K2.
CleanExi HS_TNKS2.
Genevestigatori Q9H2K2.

Family and domain databases

Gene3Di 1.10.150.50. 1 hit.
1.25.40.20. 7 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.
[Graphical view ]
Pfami PF00023. Ank. 2 hits.
PF12796. Ank_2. 5 hits.
PF00644. PARP. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view ]
PRINTSi PR01415. ANKYRIN.
SMARTi SM00248. ANK. 15 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. "Novel tankyrase-related gene detected with meningioma-specific sera."
    Monz D., Munnia A., Comtesse N., Fischer U., Steudel W.-I., Feiden W., Glass B., Meese E.U.
    Clin. Cancer Res. 7:113-119(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fetal brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Mammary carcinoma.
  3. "Identification of a novel human tankyrase through its interaction with the adaptor protein Grb14."
    Lyons R.J., Deane R., Lynch D.K., Ye Z.-S.J., Sanderson G.M., Eyre H.J., Sutherland G.R., Daly R.J.
    J. Biol. Chem. 276:17172-17180(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
    Tissue: Liver.
  4. "TANK2, a new TRF1-associated poly(ADP-ribose) polymerase, causes rapid induction of cell death upon overexpression."
    Kaminker P.G., Kim S.-H., Taylor R.D., Zebarjadian Y., Funk W.D., Morin G.B., Yaswen P., Campisi J.
    J. Biol. Chem. 276:35891-35899(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
    Tissue: Placenta.
  5. "Tankyrase-2 oligomerizes with tankyrase-1 and binds to both TRF1 (telomere-repeat-binding factor 1) and IRAP (insulin-responsive aminopeptidase)."
    Sbodio J.I., Lodish H.F., Chi N.-W.
    Biochem. J. 361:451-459(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH TRF1 AND LNPEP/OTASE.
    Tissue: Skeletal muscle.
  6. Yin Y., Gelmann E.P.
    Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta and Testis.
  8. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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, ADP-RIBOSYLATION.
  10. "Proteomics-based identification of novel factor inhibiting hypoxia-inducible factor (FIH) substrates indicates widespread asparaginyl hydroxylation of ankyrin repeat domain-containing proteins."
    Cockman M.E., Webb J.D., Kramer H.B., Kessler B.M., Ratcliffe P.J.
    Mol. Cell. Proteomics 8:535-546(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIF1AN, HYDROXYLATION AT ASN-203; ASN-271; ASN-427; ASN-518; ASN-586; ASN-671; ASN-706 AND ASN-739.
  11. Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, INTERACTION WITH AXIN1 AND AXIN2, MUTAGENESIS OF MET-1054.
  12. "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.
  13. "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, CATALYTIC ACTIVITY, INTERACTION WITH AXIN1; AXIN2; BLZF1 AND CASC3, UBIQUITINATION.
  14. Cited for: INTERACTION WITH RNF146, UBIQUITINATION, SUBCELLULAR LOCATION.
  15. "Proteasome regulation by ADP-ribosylation."
    Cho-Park P.F., Steller H.
    Cell 153:614-627(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "Factor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-translational hydroxylation of histidinyl residues within ankyrin repeat domains."
    Yang M., Chowdhury R., Ge W., Hamed R.B., McDonough M.A., Claridge T.D., Kessler B.M., Cockman M.E., Ratcliffe P.J., Schofield C.J.
    FEBS J. 278:1086-1097(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 538-558 IN COMPLEX WITH HIF1AN; IRON AND 2-OXOGLUTARATE, HYDROXYLATION AT HIS-238 AND HIS-553, MUTAGENESIS OF HIS-553.

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 26, 2014
This is version 141 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

External Data

Dasty 3