CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001564
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tankyrase-1 
Protein Synonyms/Alias
 TANK1; ADP-ribosyltransferase diphtheria toxin-like 5; ARTD5; Poly [ADP-ribose] polymerase 5A; TNKS-1; TRF1-interacting ankyrin-related ADP-ribose polymerase; Tankyrase I 
Gene Name
 TNKS 
Gene Synonyms/Alias
 PARP5A; PARPL; TIN1; TINF1; TNKS1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
210DAANVNAKDMAGRKSubiquitination[1, 2]
583VLHKHGAKMNALDTLubiquitination[3]
659YRLLEASKAGDLETVubiquitination[3]
667AGDLETVKQLCSSQNubiquitination[3]
750VNVADLWKFTPLHEAubiquitination[3]
762HEAAAKGKYEICKLLubiquitination[3]
767KGKYEICKLLLKHGAubiquitination[1, 2, 3]
771EICKLLLKHGADPTKubiquitination[3]
821GCLARVQKLCTPENIubiquitination[3]
1020GAAGTERKEGEVAGLubiquitination[3]
1238GTGCPTHKDRSCYICubiquitination[3]
1258FCRVTLGKSFLQFSTubiquitination[3]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961] 
Functional Description
 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. 
Sequence Annotation
 REPEAT 215 247 ANK 1.
 REPEAT 248 280 ANK 2.
 REPEAT 281 313 ANK 3.
 REPEAT 368 400 ANK 4.
 REPEAT 401 433 ANK 5.
 REPEAT 434 466 ANK 6.
 REPEAT 521 556 ANK 7.
 REPEAT 557 589 ANK 8.
 REPEAT 590 622 ANK 9.
 REPEAT 683 715 ANK 10.
 REPEAT 716 748 ANK 11.
 REPEAT 749 781 ANK 12.
 REPEAT 836 868 ANK 13.
 REPEAT 869 901 ANK 14.
 REPEAT 902 934 ANK 15.
 DOMAIN 1030 1089 SAM.
 DOMAIN 1112 1317 PARP catalytic.
 METAL 1234 1234 Zinc.
 METAL 1237 1237 Zinc.
 METAL 1242 1242 Zinc.
 METAL 1245 1245 Zinc.  
Keyword
 3D-structure; ADP-ribosylation; Alternative splicing; ANK repeat; Cell cycle; Cell division; Centromere; Chromosome; Complete proteome; Cytoplasm; Cytoskeleton; Glycosyltransferase; Golgi apparatus; Membrane; Metal-binding; Mitosis; mRNA transport; NAD; Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport; Reference proteome; Repeat; Telomere; Transferase; Translocation; Transport; Ubl conjugation; Wnt signaling pathway; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1327 AA 
Protein Sequence
MAASRRSQHH HHHHQQQLQP APGASAPPPP PPPPLSPGLA PGTTPASPTA SGLAPFASPR 60
HGLALPEGDG SRDPPDRPRS PDPVDGTSCC STTSTICTVA AAPVVPAVST SSAAGVAPNP 120
AGSGSNNSPS SSSSPTSSSS SSPSSPGSSL AESPEAAGVS STAPLGPGAA GPGTGVPAVS 180
GALRELLEAC RNGDVSRVKR LVDAANVNAK DMAGRKSSPL HFAAGFGRKD VVEHLLQMGA 240
NVHARDDGGL IPLHNACSFG HAEVVSLLLC QGADPNARDN WNYTPLHEAA IKGKIDVCIV 300
LLQHGADPNI RNTDGKSALD LADPSAKAVL TGEYKKDELL EAARSGNEEK LMALLTPLNV 360
NCHASDGRKS TPLHLAAGYN RVRIVQLLLQ HGADVHAKDK GGLVPLHNAC SYGHYEVTEL 420
LLKHGACVNA MDLWQFTPLH EAASKNRVEV CSLLLSHGAD PTLVNCHGKS AVDMAPTPEL 480
RERLTYEFKG HSLLQAAREA DLAKVKKTLA LEIINFKQPQ SHETALHCAV ASLHPKRKQV 540
TELLLRKGAN VNEKNKDFMT PLHVAAERAH NDVMEVLHKH GAKMNALDTL GQTALHRAAL 600
AGHLQTCRLL LSYGSDPSII SLQGFTAAQM GNEAVQQILS ESTPIRTSDV DYRLLEASKA 660
GDLETVKQLC SSQNVNCRDL EGRHSTPLHF AAGYNRVSVV EYLLHHGADV HAKDKGGLVP 720
LHNACSYGHY EVAELLVRHG ASVNVADLWK FTPLHEAAAK GKYEICKLLL KHGADPTKKN 780
RDGNTPLDLV KEGDTDIQDL LRGDAALLDA AKKGCLARVQ KLCTPENINC RDTQGRNSTP 840
LHLAAGYNNL EVAEYLLEHG ADVNAQDKGG LIPLHNAASY GHVDIAALLI KYNTCVNATD 900
KWAFTPLHEA AQKGRTQLCA LLLAHGADPT MKNQEGQTPL DLATADDIRA LLIDAMPPEA 960
LPTCFKPQAT VVSASLISPA STPSCLSAAS SIDNLTGPLA ELAVGGASNA GDGAAGTERK 1020
EGEVAGLDMN ISQFLKSLGL EHLRDIFETE QITLDVLADM GHEELKEIGI NAYGHRHKLI 1080
KGVERLLGGQ QGTNPYLTFH CVNQGTILLD LAPEDKEYQS VEEEMQSTIR EHRDGGNAGG 1140
IFNRYNVIRI QKVVNKKLRE RFCHRQKEVS EENHNHHNER MLFHGSPFIN AIIHKGFDER 1200
HAYIGGMFGA GIYFAENSSK SNQYVYGIGG GTGCPTHKDR SCYICHRQML FCRVTLGKSF 1260
LQFSTMKMAH APPGHHSVIG RPSVNGLAYA EYVIYRGEQA YPEYLITYQI MKPEAPSQTA 1320
TAAEQKT 1327 
Gene Ontology
 GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
 GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
 GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
 GO:0000784; C:nuclear chromosome, telomeric region; IDA:BHF-UCL.
 GO:0031965; C:nuclear membrane; TAS:BHF-UCL.
 GO:0005643; C:nuclear pore; TAS:BHF-UCL.
 GO:0000242; C:pericentriolar material; TAS:BHF-UCL.
 GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
 GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IDA:BHF-UCL.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0007052; P:mitotic spindle organization; TAS:BHF-UCL.
 GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
 GO:0043392; P:negative regulation of DNA binding; IDA:BHF-UCL.
 GO:0018105; P:peptidyl-serine phosphorylation; IDA:MGI.
 GO:0018107; P:peptidyl-threonine phosphorylation; IDA:MGI.
 GO:0090263; P:positive regulation of canonical Wnt receptor signaling pathway; IMP:UniProtKB.
 GO:0032212; P:positive regulation of telomere maintenance via telomerase; IDA:BHF-UCL.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0070213; P:protein auto-ADP-ribosylation; IDA:UniProtKB.
 GO:0070198; P:protein localization to chromosome, telomeric region; IMP:BHF-UCL.
 GO:0070212; P:protein poly-ADP-ribosylation; IDA:BHF-UCL.
 GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
 GO:0015031; P:protein transport; IEA:UniProtKB-KW.
 GO:0051225; P:spindle assembly; TAS:BHF-UCL.
 GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW. 
Interpro
 IPR002110; Ankyrin_rpt.
 IPR020683; Ankyrin_rpt-contain_dom.
 IPR012317; Poly(ADP-ribose)pol_cat_dom.
 IPR001660; SAM.
 IPR013761; SAM/pointed.
 IPR011510; SAM_2. 
Pfam
 PF00023; Ank
 PF12796; Ank_2
 PF00644; PARP
 PF07647; SAM_2 
SMART
 SM00248; ANK
 SM00454; SAM 
PROSITE
 PS50297; ANK_REP_REGION
 PS50088; ANK_REPEAT
 PS51059; PARP_CATALYTIC
 PS50105; SAM_DOMAIN 
PRINTS
 PR01415; ANKYRIN.