TNKS1_HUMAN - dbPTM
TNKS1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TNKS1_HUMAN
UniProt AC O95271
Protein Name Tankyrase-1
Gene Name TNKS
Organism Homo sapiens (Human).
Sequence Length 1327
Subcellular Localization Cytoplasm. Golgi apparatus membrane
Peripheral membrane protein. Chromosome, centromere. Nucleus, nuclear pore complex. Chromosome, telomere . Cytoplasm, cytoskeleton, spindle pole. Associated with the Golgi and with juxtanuclear SLC2A4/GLUT4-vesicl
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 (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. Stimulates 26S proteasome activity..
Protein Sequence MAASRRSQHHHHHHQQQLQPAPGASAPPPPPPPPLSPGLAPGTTPASPTASGLAPFASPRHGLALPEGDGSRDPPDRPRSPDPVDGTSCCSTTSTICTVAAAPVVPAVSTSSAAGVAPNPAGSGSNNSPSSSSSPTSSSSSSPSSPGSSLAESPEAAGVSSTAPLGPGAAGPGTGVPAVSGALRELLEACRNGDVSRVKRLVDAANVNAKDMAGRKSSPLHFAAGFGRKDVVEHLLQMGANVHARDDGGLIPLHNACSFGHAEVVSLLLCQGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGADPNIRNTDGKSALDLADPSAKAVLTGEYKKDELLEAARSGNEEKLMALLTPLNVNCHASDGRKSTPLHLAAGYNRVRIVQLLLQHGADVHAKDKGGLVPLHNACSYGHYEVTELLLKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSHGADPTLVNCHGKSAVDMAPTPELRERLTYEFKGHSLLQAAREADLAKVKKTLALEIINFKQPQSHETALHCAVASLHPKRKQVTELLLRKGANVNEKNKDFMTPLHVAAERAHNDVMEVLHKHGAKMNALDTLGQTALHRAALAGHLQTCRLLLSYGSDPSIISLQGFTAAQMGNEAVQQILSESTPIRTSDVDYRLLEASKAGDLETVKQLCSSQNVNCRDLEGRHSTPLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVPLHNACSYGHYEVAELLVRHGASVNVADLWKFTPLHEAAAKGKYEICKLLLKHGADPTKKNRDGNTPLDLVKEGDTDIQDLLRGDAALLDAAKKGCLARVQKLCTPENINCRDTQGRNSTPLHLAAGYNNLEVAEYLLEHGADVNAQDKGGLIPLHNAASYGHVDIAALLIKYNTCVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTMKNQEGQTPLDLATADDIRALLIDAMPPEALPTCFKPQATVVSASLISPASTPSCLSAASSIDNLTGPLAELAVGGASNAGDGAAGTERKEGEVAGLDMNISQFLKSLGLEHLRDIFETEQITLDVLADMGHEELKEIGINAYGHRHKLIKGVERLLGGQQGTNPYLTFHCVNQGTILLDLAPEDKEYQSVEEEMQSTIREHRDGGNAGGIFNRYNVIRIQKVVNKKLRERFCHRQKEVSEENHNHHNERMLFHGSPFINAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPTHKDRSCYICHRQMLFCRVTLGKSFLQFSTMKMAHAPPGHHSVIGRPSVNGLAYAEYVIYRGEQAYPEYLITYQIMKPEAPSQTATAAEQKT
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
44PhosphorylationPGLAPGTTPASPTAS
CCCCCCCCCCCCCCC
23.83-
49PhosphorylationGTTPASPTASGLAPF
CCCCCCCCCCCCCCC
30.84-
210UbiquitinationDAANVNAKDMAGRKS
HHHCCCHHHHCCCCC
42.7221890473
210UbiquitinationDAANVNAKDMAGRKS
HHHCCCHHHHCCCCC
42.7222817900
210 (in isoform 1)Ubiquitination-42.7221890473
210 (in isoform 2)Ubiquitination-42.7221890473
217PhosphorylationKDMAGRKSSPLHFAA
HHHCCCCCCCCHHCC
35.5121712546
218PhosphorylationDMAGRKSSPLHFAAG
HHCCCCCCCCHHCCC
34.2225627689
327UbiquitinationDLADPSAKAVLTGEY
HHCCCCCCHHHCCCC
43.2822817900
335AcetylationAVLTGEYKKDELLEA
HHHCCCCCHHHHHHH
49.8219816121
335UbiquitinationAVLTGEYKKDELLEA
HHHCCCCCHHHHHHH
49.8229967540
336UbiquitinationVLTGEYKKDELLEAA
HHCCCCCHHHHHHHH
56.3829967540
345PhosphorylationELLEAARSGNEEKLM
HHHHHHHHCCHHHHH
41.0429514088
350UbiquitinationARSGNEEKLMALLTP
HHHCCHHHHHHHHCC
37.0729967540
365PhosphorylationLNVNCHASDGRKSTP
CCCCCCCCCCCCCCC
19.5522817900
369UbiquitinationCHASDGRKSTPLHLA
CCCCCCCCCCCCHHH
65.3029967540
379PhosphorylationPLHLAAGYNRVRIVQ
CCHHHCCCCHHHHHH
8.62-
411PhosphorylationVPLHNACSYGHYEVT
EECCCCCCCCCHHHH
31.5722817900
412PhosphorylationPLHNACSYGHYEVTE
ECCCCCCCCCHHHHH
14.0622817900
470PhosphorylationLVNCHGKSAVDMAPT
EEECCCCCCCCCCCC
37.8124144214
477PhosphorylationSAVDMAPTPELRERL
CCCCCCCCHHHHHHH
21.6224719451
489UbiquitinationERLTYEFKGHSLLQA
HHHCEEECCHHHHHH
43.7232015554
492PhosphorylationTYEFKGHSLLQAARE
CEEECCHHHHHHHHH
39.17-
507UbiquitinationADLAKVKKTLALEII
HCHHHHHHHHHHEEE
52.32-
536UbiquitinationAVASLHPKRKQVTEL
HHHHHCCCHHHHHHH
62.5729967540
541PhosphorylationHPKRKQVTELLLRKG
CCCHHHHHHHHHHCC
20.58-
579UbiquitinationDVMEVLHKHGAKMNA
HHHHHHHHCCCHHHH
39.3023503661
583 (in isoform 2)Ubiquitination-36.96-
583UbiquitinationVLHKHGAKMNALDTL
HHHHCCCHHHHHHHH
36.9632015554
640PhosphorylationEAVQQILSESTPIRT
HHHHHHHHCCCCCCC
31.00-
659UbiquitinationYRLLEASKAGDLETV
HHHHHHHCCCCHHHH
64.5333845483
667UbiquitinationAGDLETVKQLCSSQN
CCCHHHHHHHHHCCC
45.0029967540
709UbiquitinationYLLHHGADVHAKDKG
HHHHCCCCCCCCCCC
37.0127667366
726PhosphorylationVPLHNACSYGHYEVA
CCCCCCCCCCCHHHH
31.57-
727PhosphorylationPLHNACSYGHYEVAE
CCCCCCCCCCHHHHH
14.06-
742PhosphorylationLLVRHGASVNVADLW
HHHHCCCCCCHHHHH
20.8622817900
750UbiquitinationVNVADLWKFTPLHEA
CCHHHHHHCCHHHHH
46.81-
760UbiquitinationPLHEAAAKGKYEICK
HHHHHHHCCCHHHHH
51.7332015554
762UbiquitinationHEAAAKGKYEICKLL
HHHHHCCCHHHHHHH
38.7222817900
767 (in isoform 1)Ubiquitination-48.0721890473
767UbiquitinationKGKYEICKLLLKHGA
CCCHHHHHHHHHCCC
48.0721890473
767UbiquitinationKGKYEICKLLLKHGA
CCCHHHHHHHHHCCC
48.0722817900
771UbiquitinationEICKLLLKHGADPTK
HHHHHHHHCCCCCCC
39.7122817900
777PhosphorylationLKHGADPTKKNRDGN
HHCCCCCCCCCCCCC
56.02-
778AcetylationKHGADPTKKNRDGNT
HCCCCCCCCCCCCCC
54.1311925781
779AcetylationHGADPTKKNRDGNTP
CCCCCCCCCCCCCCC
60.7411925791
791UbiquitinationNTPLDLVKEGDTDIQ
CCCHHHHHCCCCCHH
64.3832015554
812UbiquitinationAALLDAAKKGCLARV
HHHHHHHHHCHHHHH
51.96-
813UbiquitinationALLDAAKKGCLARVQ
HHHHHHHHCHHHHHH
50.5627667366
821UbiquitinationGCLARVQKLCTPENI
CHHHHHHHHCCCCCC
42.5532015554
839PhosphorylationDTQGRNSTPLHLAAG
CCCCCCCCCCEEECC
33.1621818122
901UbiquitinationTCVNATDKWAFTPLH
CCCCCCCCCCCCHHH
35.7529967540
916PhosphorylationEAAQKGRTQLCALLL
HHHHCCHHHHHHHHH
34.26-
930PhosphorylationLAHGADPTMKNQEGQ
HHCCCCCCCCCCCCC
41.1321818122
932UbiquitinationHGADPTMKNQEGQTP
CCCCCCCCCCCCCCC
58.94-
978PhosphorylationVVSASLISPASTPSC
EEEEHHCCCCCCHHH
21.5122817900
982PhosphorylationSLISPASTPSCLSAA
HHCCCCCCHHHHHHH
22.7122817900
987PhosphorylationASTPSCLSAASSIDN
CCCHHHHHHHHHCCC
26.5622817900
991PhosphorylationSCLSAASSIDNLTGP
HHHHHHHHCCCCCCC
29.2722817900
1020UbiquitinationGAAGTERKEGEVAGL
CCCCCCCCCCCCCCC
64.93-
1081UbiquitinationGHRHKLIKGVERLLG
CHHHHHHHHHHHHHC
68.30-
1128PhosphorylationVEEEMQSTIREHRDG
HHHHHHHHHHHHCCC
13.7321818122
1152UbiquitinationYNVIRIQKVVNKKLR
HCHHHHHHHHCHHHH
45.8629967540
1167UbiquitinationERFCHRQKEVSEENH
HHHHHCHHCCCCCCC
61.1029967540
1195UbiquitinationFINAIIHKGFDERHA
HHHHHHHCCCCHHCC
51.3632015554
1238UbiquitinationGTGCPTHKDRSCYIC
CCCCCCCCCCCEEEE
58.26-
1258UbiquitinationFCRVTLGKSFLQFST
HCHHHCCCCHHHHHH
40.94-
1289PhosphorylationPSVNGLAYAEYVIYR
CCCCCEEEEEEEEEC
12.66-
1292PhosphorylationNGLAYAEYVIYRGEQ
CCEEEEEEEEECCCC
5.5122817900
1308PhosphorylationYPEYLITYQIMKPEA
CCEEEEEEEECCCCC
6.7724260401

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
839TPhosphorylationKinasePLK1P53350
PSP
930TPhosphorylationKinasePLK1P53350
PSP
978SPhosphorylationKinaseGSK3BP49841
PSP
978SPhosphorylationKinasePLK1P53350
PSP
982TPhosphorylationKinaseGSK3BP49841
PSP
982TPhosphorylationKinasePLK1P53350
PSP
987SPhosphorylationKinaseGSK3BP49841
PSP
991SPhosphorylationKinaseGSK3BP49841
PSP
1128TPhosphorylationKinasePLK1P53350
PSP
-KUbiquitinationE3 ubiquitin ligaseRNF146Q9NTX7
PMID:21478859

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TNKS1_HUMAN !!

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 TNKS1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TERF1_HUMANTERF1physical
11739745
TB182_HUMANTNKS1BP1physical
11854288
TERF1_HUMANTERF1physical
11854288
TNKS1_HUMANTNKSphysical
9822378
TERF1_HUMANTERF1physical
9822378
FACD2_HUMANFANCD2physical
21314979
GMDS_HUMANGMDSphysical
22645305
TINF2_HUMANTINF2physical
15133513
TERF1_HUMANTERF1physical
15133513
TNKS1_HUMANTNKSphysical
15133513
AXIN1_HUMANAXIN1physical
25547115
PTEN_HUMANPTENphysical
25547115
TNKS1_HUMANTNKSphysical
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 TNKS1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, AND MASSSPECTROMETRY.

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