TNKS2_HUMAN - dbPTM
TNKS2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TNKS2_HUMAN
UniProt AC Q9H2K2
Protein Name Tankyrase-2
Gene Name TNKS2
Organism Homo sapiens (Human).
Sequence Length 1166
Subcellular Localization Cytoplasm. Golgi apparatus membrane
Peripheral membrane protein. Nucleus. Chromosome, telomere . Associated with the Golgi and with juxtanuclear SLC2A4/GLUT4-vesicles. Also found around the pericentriolar matrix of mitotic centromeres. During interp
Protein 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. Stimulates 26S proteasome activity..
Protein Sequence MSGRRCAGGGAACASAAAEAVEPAARELFEACRNGDVERVKRLVTPEKVNSRDTAGRKSTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLRHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGRTALDLADPSAKAVLTGEYKKDELLESARSGNEEKMMALLTPLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLQHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSYGADPTLLNCHNKSAIDLAPTPQLKERLAYEFKGHSLLQAAREADVTRIKKHLSLEMVNFKHPQTHETALHCAAASPYPKRKQICELLLRKGANINEKTKEFLTPLHVASEKAHNDVVEVVVKHEAKVNALDNLGQTSLHRAAYCGHLQTCRLLLSYGCDPNIISLQGFTALQMGNENVQQLLQEGISLGNSEADRQLLEAAKAGDVETVKKLCTVQSVNCRDIEGRQSTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLDLVKDGDTDIQDLLRGDAALLDAAKKGCLARVKKLSSPDNVNCRDTQGRHSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPLDLVSADDVSALLTAAMPPSALPSCYKPQVLNGVRSPGATADALSSGPSSPSSLSAASSLDNLSGSFSELSSVVSSSGTEGASSLEKKEVPGVDFSITQFVRNLGLEHLMDIFEREQITLDVLVEMGHKELKEIGINAYGHRHKLIKGVERLISGQQGLNPYLTLNTSGSGTILIDLSPDDKEFQSVEEEMQSTVREHRDGGHAGGIFNRYNILKIQKVCNKKLWERYTHRRKEVSEENHNHANERMLFHGSPFVNAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPVHKDRSCYICHRQLLFCRVTLGKSFLQFSAMKMAHSPPGHHSVTGRPSVNGLALAEYVIYRGEQAYPEYLITYQIMRPEGMVDG
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
38UbiquitinationACRNGDVERVKRLVT
HHHCCCHHHHHHHCC		57.4027667366
39UbiquitinationCRNGDVERVKRLVTP
HHCCCHHHHHHHCCH		38.8227667366
45PhosphorylationERVKRLVTPEKVNSR
HHHHHHCCHHHHCCC		30.2621857030
48UbiquitinationKRLVTPEKVNSRDTA
HHHCCHHHHCCCCCC		48.1733845483
62UbiquitinationAGRKSTPLHFAAGFG
CCCCCCCCHHCCCCC		5.4122053931
71UbiquitinationFAAGFGRKDVVEYLL
HCCCCCCHHHHHHHH		56.08-
109UbiquitinationGHAEVVNLLLRHGAD
CHHHHHHHHHHCCCC		3.0121963094
131UbiquitinationNYTPLHEAAIKGKID
CCCHHHHHHHCCCCE		12.0727667366
151PhosphorylationLQHGAEPTIRNTDGR
ECCCCCCEEECCCCC		24.8724719451
162UbiquitinationTDGRTALDLADPSAK
CCCCCCHHHCCCCCC		37.0322817900
169UbiquitinationDLADPSAKAVLTGEY
HHCCCCCCHHHCCCC		43.2821906983
177AcetylationAVLTGEYKKDELLES
HHHCCCCCHHHHHHH		49.8219816313
177UbiquitinationAVLTGEYKKDELLES
HHHCCCCCHHHHHHH		49.8229967540
178UbiquitinationVLTGEYKKDELLESA
HHCCCCCHHHHHHHH		56.3829967540
184UbiquitinationKKDELLESARSGNEE
CHHHHHHHHHCCCHH		29.0227667366
190UbiquitinationESARSGNEEKMMALL
HHHHCCCHHHHHHHH		63.6222053931
192UbiquitinationARSGNEEKMMALLTP
HHCCCHHHHHHHHCC		28.0029967540
203HydroxylationLLTPLNVNCHASDGR
HHCCCEEECCCCCCC		15.7018936059
204UbiquitinationLTPLNVNCHASDGRK
HCCCEEECCCCCCCC		2.1822817900
206UbiquitinationPLNVNCHASDGRKST
CCEEECCCCCCCCCC		16.1221890473
207PhosphorylationLNVNCHASDGRKSTP
CEEECCCCCCCCCCC		19.5522817900
211UbiquitinationCHASDGRKSTPLHLA
CCCCCCCCCCCCHHH		65.3029967540
216UbiquitinationGRKSTPLHLAAGYNR
CCCCCCCHHHCCCCH		18.0227667366
225UbiquitinationAAGYNRVKIVQLLLQ
HCCCCHHHHHHHHHH		33.64-
229UbiquitinationNRVKIVQLLLQHGAD
CHHHHHHHHHHCCCC		3.4122817900
233UbiquitinationIVQLLLQHGADVHAK
HHHHHHHCCCCCCCC		33.1221890473
238HydroxylationLQHGADVHAKDKGDL
HHCCCCCCCCCCCCC		27.8421251231
242UbiquitinationADVHAKDKGDLVPLH
CCCCCCCCCCCCCCC		54.3329967540
271HydroxylationVKHGACVNAMDLWQF
HHCCCCCCHHHHHHC		29.4518936059
289UbiquitinationHEAASKNRVEVCSLL
HHHHHCCHHHHHHHH		29.7022817900
291UbiquitinationAASKNRVEVCSLLLS
HHHCCHHHHHHHHHH		34.2721890473
314UbiquitinationNCHNKSAIDLAPTPQ
ECCCCCCCCCCCCHH		6.0222817900
318UbiquitinationKSAIDLAPTPQLKER
CCCCCCCCCHHHHHH		52.4921890473
319PhosphorylationSAIDLAPTPQLKERL
CCCCCCCCHHHHHHH		20.3324719451
323UbiquitinationLAPTPQLKERLAYEF
CCCCHHHHHHHHHHC		35.2227667366
331UbiquitinationERLAYEFKGHSLLQA
HHHHHHCCCHHHHHH		43.7232015554
344UbiquitinationQAAREADVTRIKKHL
HHHHHCCHHHHHHHH		5.0927667366
359UbiquitinationSLEMVNFKHPQTHET
CCEEECCCCCCCCHH		49.5329967540
374PhosphorylationALHCAAASPYPKRKQ
HHHHHHCCCCHHHHH		21.9028348404
378UbiquitinationAAASPYPKRKQICEL
HHCCCCHHHHHHHHH		67.4029967540
380UbiquitinationASPYPKRKQICELLL
CCCCHHHHHHHHHHH		50.5729967540
391UbiquitinationELLLRKGANINEKTK
HHHHHCCCCCCHHHH		19.4321963094
396UbiquitinationKGANINEKTKEFLTP
CCCCCCHHHHHHHCH		61.4822817900
398UbiquitinationANINEKTKEFLTPLH
CCCCHHHHHHHCHHH		58.5021890473
398UbiquitinationANINEKTKEFLTPLH
CCCCHHHHHHHCHHH		58.5021906983
402UbiquitinationEKTKEFLTPLHVASE
HHHHHHHCHHHHCCH		29.1727667366
403UbiquitinationKTKEFLTPLHVASEK
HHHHHHCHHHHCCHH		23.7127667366
410UbiquitinationPLHVASEKAHNDVVE
HHHHCCHHCCCCCEE		53.0732015554
413UbiquitinationVASEKAHNDVVEVVV
HCCHHCCCCCEEEEE		48.9427667366
417UbiquitinationKAHNDVVEVVVKHEA
HCCCCCEEEEEECHH		29.4622817900
419UbiquitinationHNDVVEVVVKHEAKV
CCCCEEEEEECHHHH		2.7621890473
421UbiquitinationDVVEVVVKHEAKVNA
CCEEEEEECHHHHCC		24.9033845483
425UbiquitinationVVVKHEAKVNALDNL
EEEECHHHHCCHHHC		32.7921890473
425UbiquitinationVVVKHEAKVNALDNL
EEEECHHHHCCHHHC		32.7922053931
427HydroxylationVKHEAKVNALDNLGQ
EECHHHHCCHHHCCC		33.7918936059
442UbiquitinationTSLHRAAYCGHLQTC
CHHHHHHHCCHHHHH		9.6622817900
444UbiquitinationLHRAAYCGHLQTCRL
HHHHHHCCHHHHHHH		16.3222817900
446UbiquitinationRAAYCGHLQTCRLLL
HHHHCCHHHHHHHHH		2.4721890473
466UbiquitinationPNIISLQGFTALQMG
CCEEEECCCEEHHCC		27.4527667366
473UbiquitinationGFTALQMGNENVQQL
CCEEHHCCCHHHHHH		25.9121963094
476UbiquitinationALQMGNENVQQLLQE
EHHCCCHHHHHHHHH		40.6821963094
495UbiquitinationGNSEADRQLLEAAKA
CCHHHHHHHHHHHHC		51.4527667366
498UbiquitinationEADRQLLEAAKAGDV
HHHHHHHHHHHCCCH		55.9927667366
501UbiquitinationRQLLEAAKAGDVETV
HHHHHHHHCCCHHHH		61.0129967540
509UbiquitinationAGDVETVKKLCTVQS
CCCHHHHHHHHEEEE		47.6633845483
510UbiquitinationGDVETVKKLCTVQSV
CCHHHHHHHHEEEEC		44.4527667366
518HydroxylationLCTVQSVNCRDIEGR
HHEEEECCCCCCCCC		21.9818936059
526UbiquitinationCRDIEGRQSTPLHFA
CCCCCCCCCCCEEEC		63.6122817900
529UbiquitinationIEGRQSTPLHFAAGY
CCCCCCCCEEECCCC		29.1422817900
530UbiquitinationEGRQSTPLHFAAGYN
CCCCCCCEEECCCCC		5.4127667366
531UbiquitinationGRQSTPLHFAAGYNR
CCCCCCEEECCCCCH		16.1127667366
548UbiquitinationVVEYLLQHGADVHAK
HHHHHHHCCCCCCCC		33.1227667366
551UbiquitinationYLLQHGADVHAKDKG
HHHHCCCCCCCCCCC		37.0127667366
553HydroxylationLQHGADVHAKDKGGL
HHCCCCCCCCCCCCC		27.8421251231
555UbiquitinationHGADVHAKDKGGLVP
CCCCCCCCCCCCCCC		45.1329967540
557UbiquitinationADVHAKDKGGLVPLH
CCCCCCCCCCCCCCC		54.9229967540
568PhosphorylationVPLHNACSYGHYEVA
CCCCCCCCCCCHHHH		31.57-
569PhosphorylationPLHNACSYGHYEVAE
CCCCCCCCCCHHHHH		14.06-
580UbiquitinationEVAELLVKHGAVVNV
HHHHHHHHCCCEEEH		35.9721963094
583UbiquitinationELLVKHGAVVNVADL
HHHHHCCCEEEHHHH		11.2121963094
586HydroxylationVKHGAVVNVADLWKF
HHCCCEEEHHHHHHC		19.3618936059
592UbiquitinationVNVADLWKFTPLHEA
EEHHHHHHCCHHHHH		46.8129967540
601UbiquitinationTPLHEAAAKGKYEIC
CHHHHHHHCCCHHHH		28.3421963094
602UbiquitinationPLHEAAAKGKYEICK
HHHHHHHCCCHHHHH		51.7332015554
604UbiquitinationHEAAAKGKYEICKLL
HHHHHCCCHHHHHHH		38.7221963094
605UbiquitinationEAAAKGKYEICKLLL
HHHHCCCHHHHHHHH		21.1327667366
609UbiquitinationKGKYEICKLLLQHGA
CCCHHHHHHHHHCCC		48.0732015554
619PhosphorylationLQHGADPTKKNRDGN
HHCCCCCCCCCCCCC		56.0229116813
620UbiquitinationQHGADPTKKNRDGNT
HCCCCCCCCCCCCCC		54.1329967540
621UbiquitinationHGADPTKKNRDGNTP
CCCCCCCCCCCCCCC		60.74-
623UbiquitinationADPTKKNRDGNTPLD
CCCCCCCCCCCCCCC		63.1927667366
626UbiquitinationTKKNRDGNTPLDLVK
CCCCCCCCCCCCHHC		42.6927667366
633UbiquitinationNTPLDLVKDGDTDIQ
CCCCCHHCCCCCCHH		64.3922817900
636UbiquitinationLDLVKDGDTDIQDLL
CCHHCCCCCCHHHHH		51.8722817900
654UbiquitinationAALLDAAKKGCLARV
HHHHHHHHHCHHHHH		51.9622817900
655UbiquitinationALLDAAKKGCLARVK
HHHHHHHHCHHHHHH		50.5627667366
657UbiquitinationLDAAKKGCLARVKKL
HHHHHHCHHHHHHCC		3.5422817900
658UbiquitinationDAAKKGCLARVKKLS
HHHHHCHHHHHHCCC		4.6827667366
663UbiquitinationGCLARVKKLSSPDNV
CHHHHHHCCCCCCCC		51.2329967540
666PhosphorylationARVKKLSSPDNVNCR
HHHHCCCCCCCCCCC		46.8621815630
671HydroxylationLSSPDNVNCRDTQGR
CCCCCCCCCCCCCCC		22.7418936059
676UbiquitinationNVNCRDTQGRHSTPL
CCCCCCCCCCCCCCC		51.7327667366
679UbiquitinationCRDTQGRHSTPLHLA
CCCCCCCCCCCCCEE		42.7327667366
706HydroxylationLQHGADVNAQDKGGL
HHCCCCCCCCCCCCC		32.2218936059
739HydroxylationIKYNACVNATDKWAF
HHHHHCCCCCCCCCC		36.6918936059
743UbiquitinationACVNATDKWAFTPLH
HCCCCCCCCCCCHHH		35.7529967540
758PhosphorylationEAAQKGRTQLCALLL
HHHHCCHHHHHHHHH		34.26-
869UbiquitinationGASSLEKKEVPGVDF
CCCCCCCCCCCCCCC		55.35-
928UbiquitinationGHRHKLIKGVERLIS
CHHHHHHHHHHHHHH		68.3029967540
996UbiquitinationFNRYNILKIQKVCNK
HHHHCHHHHHHHHCH		39.0229967540
1010PhosphorylationKKLWERYTHRRKEVS
HHHHHHHHHHHHCCC		18.35-
1017PhosphorylationTHRRKEVSEENHNHA
HHHHHCCCHHCCCCC		40.0419651622
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
-KUbiquitinationE3 ubiquitin ligaseRNF146Q9NTX7
PMID:21478859
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
48Kubiquitylation

21478859
63Kubiquitylation

21478859
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of TNKS2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TERF1_HUMANTERF1physical
11739745
TB182_HUMANTNKS1BP1physical
11854288
LCAP_HUMANLNPEPphysical
10988299
GRB14_HUMANGRB14physical
11278563
FTCD_HUMANFTCDphysical
11278563
3BP2_HUMANSH3BP2physical
22153077
3BP2_HUMANSH3BP2physical
22153076
PTEN_HUMANPTENphysical
25547115
TNKS2_HUMANTNKS2physical
25547115
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TNKS2_HUMAN

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Related Literatures of Post-Translational Modification
Hydroxylation
ReferencePubMed
"Proteomics-based identification of novel factor inhibiting hypoxia-inducible factor (FIH) substrates indicates widespread asparaginylhydroxylation 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).
Cited for: INTERACTION WITH HIF1AN, AND HYDROXYLATION AT ASN-203; ASN-271;ASN-427; ASN-518; ASN-586; ASN-671; ASN-706 AND ASN-739.

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