CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021308
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tankyrase-2 
Protein Synonyms/Alias
 TANK2; ADP-ribosyltransferase diphtheria toxin-like 6; 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 Name
 TNKS2 
Gene Synonyms/Alias
 PARP5B; TANK2; TNKL 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
71FAAGFGRKDVVEYLLubiquitination[1]
169DLADPSAKAVLTGEYubiquitination[2, 3, 4, 5]
177AVLTGEYKKDELLESubiquitination[1]
178VLTGEYKKDELLESAubiquitination[1]
192ARSGNEEKMMALLTPubiquitination[1]
225AAGYNRVKIVQLLLQubiquitination[1, 5]
323LAPTPQLKERLAYEFubiquitination[4]
331ERLAYEFKGHSLLQAubiquitination[1]
380ASPYPKRKQICELLLubiquitination[1]
398ANINEKTKEFLTPLHubiquitination[1, 4, 5, 6, 7]
421DVVEVVVKHEAKVNAubiquitination[1]
425VVVKHEAKVNALDNLubiquitination[1, 2, 3, 4, 5, 6, 7]
510GDVETVKKLCTVQSVubiquitination[1, 5]
580EVAELLVKHGAVVNVubiquitination[8]
604HEAAAKGKYEICKLLubiquitination[1]
621HGADPTKKNRDGNTPubiquitination[1]
633NTPLDLVKDGDTDIQubiquitination[2, 4]
663GCLARVKKLSSPDNVubiquitination[1, 5]
869GASSLEKKEVPGVDFubiquitination[1, 5]
Reference
 [1] 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]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [5] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [6] 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]
 [7] 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]
 [8] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094] 
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 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. 
Sequence Annotation
 REPEAT 57 89 ANK 1.
 REPEAT 90 122 ANK 2.
 REPEAT 123 155 ANK 3.
 REPEAT 210 242 ANK 4.
 REPEAT 243 275 ANK 5.
 REPEAT 276 308 ANK 6.
 REPEAT 363 398 ANK 7.
 REPEAT 399 431 ANK 8.
 REPEAT 432 464 ANK 9.
 REPEAT 525 557 ANK 10.
 REPEAT 558 590 ANK 11.
 REPEAT 591 623 ANK 12.
 REPEAT 678 710 ANK 13.
 REPEAT 711 743 ANK 14.
 REPEAT 744 776 ANK 15.
 DOMAIN 873 936 SAM.
 DOMAIN 959 1164 PARP catalytic.
 REGION 545 553 HIF1AN-binding.
 METAL 1081 1081 Zinc (By similarity).
 METAL 1084 1084 Zinc (By similarity).
 METAL 1089 1089 Zinc (By similarity).
 METAL 1092 1092 Zinc (By similarity).
 MOD_RES 203 203 (3S)-3-hydroxyasparagine; by HIF1AN;
 MOD_RES 238 238 (3S)-3-hydroxyhistidine; by HIF1AN;
 MOD_RES 271 271 (3S)-3-hydroxyasparagine; by HIF1AN;
 MOD_RES 427 427 (3S)-3-hydroxyasparagine; by HIF1AN;
 MOD_RES 518 518 (3S)-3-hydroxyasparagine; by HIF1AN;
 MOD_RES 553 553 (3S)-3-hydroxyhistidine; by HIF1AN;
 MOD_RES 586 586 (3S)-3-hydroxyasparagine; by HIF1AN;
 MOD_RES 671 671 (3S)-3-hydroxyasparagine; by HIF1AN;
 MOD_RES 706 706 (3S)-3-hydroxyasparagine; by HIF1AN;
 MOD_RES 739 739 (3S)-3-hydroxyasparagine; by HIF1AN;  
Keyword
 3D-structure; ADP-ribosylation; ANK repeat; Chromosome; Complete proteome; Cytoplasm; Glycosyltransferase; Golgi apparatus; Hydroxylation; Membrane; Metal-binding; NAD; Nucleus; Reference proteome; Repeat; Telomere; Transferase; Ubl conjugation; Wnt signaling pathway; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1166 AA 
Protein Sequence
MSGRRCAGGG AACASAAAEA VEPAARELFE ACRNGDVERV KRLVTPEKVN SRDTAGRKST 60
PLHFAAGFGR KDVVEYLLQN GANVQARDDG GLIPLHNACS FGHAEVVNLL LRHGADPNAR 120
DNWNYTPLHE AAIKGKIDVC IVLLQHGAEP TIRNTDGRTA LDLADPSAKA VLTGEYKKDE 180
LLESARSGNE EKMMALLTPL NVNCHASDGR KSTPLHLAAG YNRVKIVQLL LQHGADVHAK 240
DKGDLVPLHN ACSYGHYEVT ELLVKHGACV NAMDLWQFTP LHEAASKNRV EVCSLLLSYG 300
ADPTLLNCHN KSAIDLAPTP QLKERLAYEF KGHSLLQAAR EADVTRIKKH LSLEMVNFKH 360
PQTHETALHC AAASPYPKRK QICELLLRKG ANINEKTKEF LTPLHVASEK AHNDVVEVVV 420
KHEAKVNALD NLGQTSLHRA AYCGHLQTCR LLLSYGCDPN IISLQGFTAL QMGNENVQQL 480
LQEGISLGNS EADRQLLEAA KAGDVETVKK LCTVQSVNCR DIEGRQSTPL HFAAGYNRVS 540
VVEYLLQHGA DVHAKDKGGL VPLHNACSYG HYEVAELLVK HGAVVNVADL WKFTPLHEAA 600
AKGKYEICKL LLQHGADPTK KNRDGNTPLD LVKDGDTDIQ DLLRGDAALL DAAKKGCLAR 660
VKKLSSPDNV NCRDTQGRHS TPLHLAAGYN NLEVAEYLLQ HGADVNAQDK GGLIPLHNAA 720
SYGHVDVAAL LIKYNACVNA TDKWAFTPLH EAAQKGRTQL CALLLAHGAD PTLKNQEGQT 780
PLDLVSADDV SALLTAAMPP SALPSCYKPQ VLNGVRSPGA TADALSSGPS SPSSLSAASS 840
LDNLSGSFSE LSSVVSSSGT EGASSLEKKE VPGVDFSITQ FVRNLGLEHL MDIFEREQIT 900
LDVLVEMGHK ELKEIGINAY GHRHKLIKGV ERLISGQQGL NPYLTLNTSG SGTILIDLSP 960
DDKEFQSVEE EMQSTVREHR DGGHAGGIFN RYNILKIQKV CNKKLWERYT HRRKEVSEEN 1020
HNHANERMLF HGSPFVNAII HKGFDERHAY IGGMFGAGIY FAENSSKSNQ YVYGIGGGTG 1080
CPVHKDRSCY ICHRQLLFCR VTLGKSFLQF SAMKMAHSPP GHHSVTGRPS VNGLALAEYV 1140
IYRGEQAYPE YLITYQIMRP EGMVDG 1166 
Gene Ontology
 GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
 GO:0000784; C:nuclear chromosome, telomeric region; IC:BHF-UCL.
 GO:0005635; C:nuclear envelope; IDA:BHF-UCL.
 GO:0000242; C:pericentriolar material; IDA:BHF-UCL.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IDA:UniProtKB.
 GO:0035264; P:multicellular organism growth; IEA:Compara.
 GO:0090263; P:positive regulation of canonical Wnt receptor signaling pathway; IMP:UniProtKB.
 GO:0032212; P:positive regulation of telomere maintenance via telomerase; IC:BHF-UCL.
 GO:0070213; P:protein auto-ADP-ribosylation; IDA:UniProtKB.
 GO:0070198; P:protein localization to chromosome, telomeric region; IMP:BHF-UCL.
 GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
 GO:0040014; P:regulation of multicellular organism growth; IEA:Compara.
 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.