CPLM-015285

CPLM 1.0 - Compendium of Protein Lysine Modification

Tag

Content

CPLM ID

CPLM-015285

UniProt Accession

TNKS1_MOUSE; Q6PFX9; Q8BX62

Genbank Protein ID

AK048860; AC122458; BC057370

Genbank Nucleotide ID

BAC33475.1; AAH57370.1

Protein Name

Tankyrase-1

Protein Synonyms/Alias

TANK1; ADP-ribosyltransferase diphtheria toxin-like 5; ARTD5; TRF1-interacting ankyrin-related ADP-ribose polymerase 1; Tankyrase I

Gene Name

Tnks

Gene Synonyms/Alias

Tnks1

Created Date

July 27, 2013

Organism

Mus musculus (Mouse)

NCBI Taxa ID

10090

Lysine Modification

Position	Peptide	Type	References
500	ADLAKVKKTLALEII	ubiquitination	[1]

Reference

[1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]

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 (By similarity).

Sequence Annotation

REPEAT 174 202 ANK 1.
REPEAT 208 237 ANK 2.
REPEAT 241 270 ANK 3.
REPEAT 274 303 ANK 4.
REPEAT 361 390 ANK 5.
REPEAT 394 423 ANK 6.
REPEAT 427 456 ANK 7.
REPEAT 514 546 ANK 8.
REPEAT 550 579 ANK 9.
REPEAT 583 612 ANK 10.
REPEAT 676 705 ANK 11.
REPEAT 709 738 ANK 12.
REPEAT 742 771 ANK 13.
REPEAT 775 803 ANK 14.
REPEAT 829 858 ANK 15.
REPEAT 862 891 ANK 16.
REPEAT 895 924 ANK 17.
REPEAT 928 957 ANK 18.
DOMAIN 1019 1082 SAM.
DOMAIN 1105 1310 PARP catalytic.
METAL 1227 1227 Zinc (By similarity).
METAL 1230 1230 Zinc (By similarity).
METAL 1235 1235 Zinc (By similarity).
METAL 1238 1238 Zinc (By similarity).

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

1320 AA

Protein Sequence

MAASRRSQHH HHHHQQQLQP APGASAPPPP PPPPLSPGLA PGPTPASPTA GGLAPFASPR 60
HGLALPEGDG SRDPPDRPRS PDPVDGAVCT VAAPAAVPAA SAAVGVAPTP AGGGGGGGNN 120
SASSASSPTS SSSSSPSSPG SSLAESPEAA GVGSTATLGA GAAGLGPGVP AVSGALRELL 180
EACRNGDVSR VKRLVDAANV NAKDMAGRKS SPLHFAAGFG RKDVVEHLLQ MGANVHARDD 240
GGLIPLHNAC SFGHAEVVSL LLCQGADPNA RDNWNYTPLH EAAIKGKIDV CIVLLQHGAD 300
PNIRNTDGKS ALDLADPSAK AVLTGEYKKD ELLEAARSGN EEKLMALLTP LNVNCHASDG 360
RKSTPLHLAA GYNRVRIVQL LLQHGADVHA KDKGGLVPLH NACSYGHYEV TELLLKHGAC 420
VNAMDLWQFT PLHEAASKNR VEVCSLLLSH GADPTLVNCH GKSAVDMAPT PELRERLTYE 480
FKGHSLLQAA READLAKVKK TLALEIINFK QPQSHETALH CAVASLHPKR KQVAELLLRK 540
GANVNEKNKD FMTPLHVAAE RAHNDVMEVL HKHGAKMNAL DSLGQTALHR AALAGHLQTC 600
RLLLSYGSDP SIISLQGFTA AQMGNEAVQQ ILSESTPMRT SDVDYRLLEA SKAGDLETVK 660
QLCSPQNVNC RDLEGRHSTP LHFAAGYNRV SVVEYLLHHG ADVHAKDKGG LVPLHNACSY 720
GHYEVAELLV RHGASVNVAD LWKFTPLHEA AAKGKYEICK LLLKHGADPT KKNRDGNTPL 780
DLVKEGDTDI QDLLRGDAAL LDAAKKGCLA RVQKLCTPEN INCRDTQGRN STPLHLAAGY 840
NNLEVAEYLL EHGADVNAQD KGGLIPLHNA ASYGHVDIAA LLIKYNTCVN ATDKWAFTPL 900
HEAAQKGRTQ LCALLLAHGA DPTMKNQEGQ TPLDLATADD IRALLIDAMP PEALPTCFKP 960
QATVVSASLI SPASTPSCLS AASSIDNLTG PLTDLAVGGA SNAGDGAAGA ERKEGEVAGL 1020
DMNISQFLKS LGLEHLRDIF ETEQITLDVL ADMGHEELKE IGINAYGHRH KLIKGVERLL 1080
GGQQGTNPYL TFHCVNQGTI LLDLAPEDKE YQSVEEEMQS TIREHRDGGN AGGIFNRYNV 1140
IRIQKVVNKK LRERFCHRQK EVSEENHNHH NERMLFHGSP FINAIIHKGF DERHAYIGGM 1200
FGAGIYFAEN SSKSNQYVYG IGGGTGCPTH KDRSCYICHR QMLFCRVTLG KSFLQFSTMK 1260
MAHAPPGHHS VIGRPSVNGL AYAEYVIYRG EQAYPEYLIT YQIMKPEAPS QTATAAEQKT 1320

Gene Ontology

GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO:0000784; C:nuclear chromosome, telomeric region; IEA:Compara.
GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
GO:0003950; F:NAD+ ADP-ribosyltransferase activity; ISS:UniProtKB.
GO:0008270; F:zinc ion binding; IEA:Compara.
GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO:0007067; P:mitosis; IEA:UniProtKB-KW.
GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
GO:0043392; P:negative regulation of DNA binding; IEA:Compara.
GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
GO:0018107; P:peptidyl-threonine phosphorylation; ISO:MGI.
GO:0090263; P:positive regulation of canonical Wnt receptor signaling pathway; ISS:UniProtKB.
GO:0032212; P:positive regulation of telomere maintenance via telomerase; IEA:Compara.
GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Compara.
GO:0070213; P:protein auto-ADP-ribosylation; ISS:UniProtKB.
GO:0070198; P:protein localization to chromosome, telomeric region; IEA:Compara.
GO:0070212; P:protein poly-ADP-ribosylation; IEA:Compara.
GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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.