AXIN2_HUMAN
ID AXIN2_HUMAN Reviewed; 843 AA.
AC Q9Y2T1; Q3MJ88; Q9H3M6; Q9UH84;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Axin-2;
DE AltName: Full=Axin-like protein;
DE Short=Axil;
DE AltName: Full=Axis inhibition protein 2;
DE AltName: Full=Conductin;
GN Name=AXIN2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-50.
RX PubMed=10049590; DOI=10.1006/geno.1998.5650;
RA Mai M., Qian C., Yokomizo A., Smith D.I., Liu W.;
RT "Cloning of the human homolog of conductin (AXIN2), a gene mapping to
RT chromosome 17q23-q24.";
RL Genomics 55:341-344(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain, and Lymphoblast;
RA Zhang T., Fagotto F., Hsu W., Zeng L., Gilbert D., Copeland N.G.,
RA Jenkins N.A., Warburton D., Costantini F.;
RT "Properties of mouse Axin2 and human AXIN2: chromosomal location,
RT expression pattern, interaction with Axin and effects on embryonic axis
RT formation.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-50.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 697-843.
RA Takahashi M., Furukawa Y.;
RT "Identification of 3' UTR of Axin2.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INVOLVEMENT IN COLORECTAL CANCER.
RX PubMed=11017067; DOI=10.1038/79859;
RA Liu W., Dong X., Mai M., Seelan R.S., Taniguchi K., Krishnadath K.K.,
RA Halling K.C., Cunningham J.M., Qian C., Christensen E., Roches P.C.,
RA Smith D.I., Thibodeau S.N.;
RT "Mutations in AXIN2 cause colorectal cancer with defective mismatch repair
RT by activating beta-catenin/TCF signalling.";
RL Nat. Genet. 26:146-147(2000).
RN [7]
RP INVOLVEMENT IN ODCRCS.
RX PubMed=15042511; DOI=10.1086/386293;
RA Lammi L., Arte S., Somer M., Jarvinen H., Lahermo P., Thesleff I.,
RA Pirinen S., Nieminen P.;
RT "Mutations in AXIN2 cause familial tooth agenesis and predispose to
RT colorectal cancer.";
RL Am. J. Hum. Genet. 74:1043-1050(2004).
RN [8]
RP INTERACTION WITH SMAD7 AND RNF111.
RX PubMed=16601693; DOI=10.1038/sj.emboj.7601057;
RA Liu W., Rui H., Wang J., Lin S., He Y., Chen M., Li Q., Ye Z., Zhang S.,
RA Chan S.C., Chen Y.-G., Han J., Lin S.-C.;
RT "Axin is a scaffold protein in TGF-beta signaling that promotes degradation
RT of Smad7 by Arkadia.";
RL EMBO J. 25:1646-1658(2006).
RN [9]
RP ADP-RIBOSYLATION, UBIQUITINATION, AND INTERACTION WITH TNKS AND TNKS2.
RX PubMed=19759537; DOI=10.1038/nature08356;
RA Huang S.M., Mishina Y.M., Liu S., Cheung A., Stegmeier F., Michaud G.A.,
RA Charlat O., Wiellette E., Zhang Y., Wiessner S., Hild M., Shi X.,
RA Wilson C.J., Mickanin C., Myer V., Fazal A., Tomlinson R., Serluca F.,
RA Shao W., Cheng H., Shultz M., Rau C., Schirle M., Schlegl J., Ghidelli S.,
RA Fawell S., Lu C., Curtis D., Kirschner M.W., Lengauer C., Finan P.M.,
RA Tallarico J.A., Bouwmeester T., Porter J.A., Bauer A., Cong F.;
RT "Tankyrase inhibition stabilizes axin and antagonizes Wnt signalling.";
RL Nature 461:614-620(2009).
RN [10]
RP UBIQUITINATION, AND DEUBIQUITINATION BY USP34.
RX PubMed=21383061; DOI=10.1128/mcb.01094-10;
RA Lui T.T., Lacroix C., Ahmed S.M., Goldenberg S.J., Leach C.A., Daulat A.M.,
RA Angers S.;
RT "The Ubiquitin specific protease USP34 regulates Axin stability and
RT Wnt/beta-catenin signaling.";
RL Mol. Cell. Biol. 31:2053-2065(2011).
RN [11]
RP ADP-RIBOSYLATION, UBIQUITINATION, AND INTERACTION WITH RNF146; TNKS AND
RP TNKS2.
RX PubMed=21478859; DOI=10.1038/ncb2222;
RA Zhang Y., Liu S., Mickanin C., Feng Y., Charlat O., Michaud G.A.,
RA Schirle M., Shi X., Hild M., Bauer A., Myer V.E., Finan P.M., Porter J.A.,
RA Huang S.M., Cong F.;
RT "RNF146 is a poly(ADP-ribose)-directed E3 ligase that regulates axin
RT degradation and Wnt signalling.";
RL Nat. Cell Biol. 13:623-629(2011).
RN [12]
RP INTERACTION WITH SIAH1 AND SIAH2.
RX PubMed=28546513; DOI=10.1101/gad.300053.117;
RA Ji L., Jiang B., Jiang X., Charlat O., Chen A., Mickanin C., Bauer A.,
RA Xu W., Yan X., Cong F.;
RT "The SIAH E3 ubiquitin ligases promote Wnt/beta-catenin signaling through
RT mediating Wnt-induced Axin degradation.";
RL Genes Dev. 31:904-915(2017).
RN [13]
RP VARIANT SER-50.
RX PubMed=16820935;
RA Kanzaki H., Ouchida M., Hanafusa H., Yano M., Suzuki H., Aoe M., Imai K.,
RA Shimizu N., Nakachi K., Shimizu K.;
RT "Single nucleotide polymorphism of the AXIN2 gene is preferentially
RT associated with human lung cancer risk in a Japanese population.";
RL Int. J. Mol. Med. 18:279-284(2006).
CC -!- FUNCTION: Inhibitor of the Wnt signaling pathway. Down-regulates beta-
CC catenin. Probably facilitate the phosphorylation of beta-catenin and
CC APC by GSK3B. {ECO:0000250|UniProtKB:O15169}.
CC -!- SUBUNIT: Interacts with glycogen synthase kinase-3 beta (GSK3B) and
CC beta-catenin. The interaction between axin and beta-catenin occurs via
CC the armadillo repeats contained in beta-catenin (By similarity).
CC Interacts with SMAD7 and RNF111. Interacts with ANKRD6. Interacts with
CC SIAH1 (PubMed:28546513). Interacts with SIAH2 (PubMed:28546513).
CC {ECO:0000250|UniProtKB:O88566, ECO:0000269|PubMed:16601693,
CC ECO:0000269|PubMed:19759537, ECO:0000269|PubMed:21478859,
CC ECO:0000269|PubMed:28546513}.
CC -!- INTERACTION:
CC Q9Y2T1; Q8N944: AMER3; NbExp=2; IntAct=EBI-4400025, EBI-8869590;
CC Q9Y2T1; A2BDD9: AMOT; NbExp=3; IntAct=EBI-4400025, EBI-17286414;
CC Q9Y2T1; Q9BXS5: AP1M1; NbExp=3; IntAct=EBI-4400025, EBI-541426;
CC Q9Y2T1; Q99728: BARD1; NbExp=3; IntAct=EBI-4400025, EBI-473181;
CC Q9Y2T1; Q9Y297: BTRC; NbExp=3; IntAct=EBI-4400025, EBI-307461;
CC Q9Y2T1; Q13895: BYSL; NbExp=3; IntAct=EBI-4400025, EBI-358049;
CC Q9Y2T1; Q2NKX9: C2orf68; NbExp=3; IntAct=EBI-4400025, EBI-11603468;
CC Q9Y2T1; Q9Y6W3: CAPN7; NbExp=3; IntAct=EBI-4400025, EBI-1765641;
CC Q9Y2T1; Q8NEF3-2: CCDC112; NbExp=3; IntAct=EBI-4400025, EBI-12095166;
CC Q9Y2T1; Q9UKJ5: CHIC2; NbExp=3; IntAct=EBI-4400025, EBI-741528;
CC Q9Y2T1; O75638-2: CTAG2; NbExp=3; IntAct=EBI-4400025, EBI-12265122;
CC Q9Y2T1; P35222: CTNNB1; NbExp=2; IntAct=EBI-4400025, EBI-491549;
CC Q9Y2T1; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-4400025, EBI-5453285;
CC Q9Y2T1; Q14241: ELOA; NbExp=3; IntAct=EBI-4400025, EBI-742350;
CC Q9Y2T1; Q3B820: FAM161A; NbExp=3; IntAct=EBI-4400025, EBI-719941;
CC Q9Y2T1; P09067: HOXB5; NbExp=3; IntAct=EBI-4400025, EBI-3893317;
CC Q9Y2T1; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-4400025, EBI-14069005;
CC Q9Y2T1; P60014: KRTAP10-10; NbExp=3; IntAct=EBI-4400025, EBI-11955579;
CC Q9Y2T1; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-4400025, EBI-10171774;
CC Q9Y2T1; Q9BYR2: KRTAP4-5; NbExp=3; IntAct=EBI-4400025, EBI-11993254;
CC Q9Y2T1; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-4400025, EBI-1044640;
CC Q9Y2T1; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-4400025, EBI-739832;
CC Q9Y2T1; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-4400025, EBI-348259;
CC Q9Y2T1; P53350: PLK1; NbExp=2; IntAct=EBI-4400025, EBI-476768;
CC Q9Y2T1; P62714: PPP2CB; NbExp=4; IntAct=EBI-4400025, EBI-1044367;
CC Q9Y2T1; Q15172: PPP2R5A; NbExp=3; IntAct=EBI-4400025, EBI-641666;
CC Q9Y2T1; P49721: PSMB2; NbExp=3; IntAct=EBI-4400025, EBI-359335;
CC Q9Y2T1; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-4400025, EBI-748391;
CC Q9Y2T1; O75558: STX11; NbExp=3; IntAct=EBI-4400025, EBI-714135;
CC Q9Y2T1; Q15560: TCEA2; NbExp=3; IntAct=EBI-4400025, EBI-710310;
CC Q9Y2T1; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-4400025, EBI-11955057;
CC Q9Y2T1; Q15583: TGIF1; NbExp=5; IntAct=EBI-4400025, EBI-714215;
CC Q9Y2T1; O95985: TOP3B; NbExp=3; IntAct=EBI-4400025, EBI-373403;
CC Q9Y2T1; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-4400025, EBI-744794;
CC Q9Y2T1; P40222: TXLNA; NbExp=3; IntAct=EBI-4400025, EBI-359793;
CC Q9Y2T1; Q8N3L3: TXLNB; NbExp=3; IntAct=EBI-4400025, EBI-6116822;
CC Q9Y2T1; Q15973: ZNF124; NbExp=3; IntAct=EBI-4400025, EBI-2555767;
CC Q9Y2T1; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-4400025, EBI-740727;
CC Q9Y2T1; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-4400025, EBI-6427977;
CC Q9Y2T1; Q5T619: ZNF648; NbExp=3; IntAct=EBI-4400025, EBI-11985915;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21383061}.
CC -!- TISSUE SPECIFICITY: Expressed in brain and lymphoblast.
CC -!- DOMAIN: The tankyrase-binding motif (also named TBD) is required for
CC interaction with tankyrase TNKS and TNKS2. {ECO:0000250}.
CC -!- PTM: Probably phosphorylated by GSK3B and dephosphorylated by PP2A.
CC {ECO:0000250|UniProtKB:O15169}.
CC -!- PTM: ADP-ribosylated by tankyrase TNKS and TNKS2. Poly-ADP-ribosylated
CC protein is recognized by RNF146, followed by ubiquitination and
CC subsequent activation of the Wnt signaling pathway.
CC {ECO:0000269|PubMed:21383061}.
CC -!- PTM: Ubiquitinated by RNF146 when poly-ADP-ribosylated, leading to its
CC degradation and subsequent activation of the Wnt signaling pathway.
CC Deubiquitinated by USP34, deubiquitinated downstream of beta-catenin
CC stabilization step: deubiquitination is important Wnt signaling to
CC positively regulate beta-catenin (CTNBB1)-mediated transcription.
CC {ECO:0000269|PubMed:21383061}.
CC -!- DISEASE: Colorectal cancer (CRC) [MIM:114500]: A complex disease
CC characterized by malignant lesions arising from the inner wall of the
CC large intestine (the colon) and the rectum. Genetic alterations are
CC often associated with progression from premalignant lesion (adenoma) to
CC invasive adenocarcinoma. Risk factors for cancer of the colon and
CC rectum include colon polyps, long-standing ulcerative colitis, and
CC genetic family history. {ECO:0000269|PubMed:11017067}. Note=The gene
CC represented in this entry is involved in disease pathogenesis.
CC -!- DISEASE: Oligodontia-colorectal cancer syndrome (ODCRCS) [MIM:608615]:
CC Affected individuals manifest severe tooth agenesis and colorectal
CC cancer or precancerous lesions of variable types.
CC {ECO:0000269|PubMed:15042511}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/AXIN2ID456ch17q24.html";
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DR EMBL; AF078165; AAD20976.1; -; mRNA.
DR EMBL; AF205888; AAF22799.1; -; mRNA.
DR EMBL; AC115994; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC101533; AAI01534.1; -; mRNA.
DR EMBL; AB052751; BAB19762.1; -; mRNA.
DR CCDS; CCDS11662.1; -.
DR RefSeq; NP_004646.3; NM_004655.3.
DR AlphaFoldDB; Q9Y2T1; -.
DR BioGRID; 113910; 66.
DR ComplexPortal; CPX-439; Beta-catenin destruction core complex, variant 3.
DR ComplexPortal; CPX-440; Beta-catenin destruction core complex, variant 4.
DR ComplexPortal; CPX-441; Beta-catenin destruction core complex, variant 7.
DR ComplexPortal; CPX-443; Beta-catenin destruction core complex, variant 8.
DR DIP; DIP-59293N; -.
DR IntAct; Q9Y2T1; 61.
DR MINT; Q9Y2T1; -.
DR STRING; 9606.ENSP00000302625; -.
DR BindingDB; Q9Y2T1; -.
DR ChEMBL; CHEMBL1255167; -.
DR iPTMnet; Q9Y2T1; -.
DR PhosphoSitePlus; Q9Y2T1; -.
DR BioMuta; AXIN2; -.
DR DMDM; 12643949; -.
DR EPD; Q9Y2T1; -.
DR jPOST; Q9Y2T1; -.
DR MassIVE; Q9Y2T1; -.
DR MaxQB; Q9Y2T1; -.
DR PaxDb; Q9Y2T1; -.
DR PeptideAtlas; Q9Y2T1; -.
DR PRIDE; Q9Y2T1; -.
DR ProteomicsDB; 85888; -.
DR Antibodypedia; 31648; 425 antibodies from 38 providers.
DR DNASU; 8313; -.
DR Ensembl; ENST00000307078.10; ENSP00000302625.5; ENSG00000168646.14.
DR GeneID; 8313; -.
DR KEGG; hsa:8313; -.
DR MANE-Select; ENST00000307078.10; ENSP00000302625.5; NM_004655.4; NP_004646.3.
DR UCSC; uc002jfi.4; human.
DR CTD; 8313; -.
DR DisGeNET; 8313; -.
DR GeneCards; AXIN2; -.
DR HGNC; HGNC:904; AXIN2.
DR HPA; ENSG00000168646; Low tissue specificity.
DR MalaCards; AXIN2; -.
DR MIM; 114500; phenotype.
DR MIM; 604025; gene.
DR MIM; 608615; phenotype.
DR neXtProt; NX_Q9Y2T1; -.
DR OpenTargets; ENSG00000168646; -.
DR Orphanet; 401911; AXIN2-related attenuated familial adenomatous polyposis.
DR Orphanet; 2227; NON RARE IN EUROPE: Hypodontia.
DR Orphanet; 99798; Oligodontia.
DR Orphanet; 300576; Oligodontia-cancer predisposition syndrome.
DR PharmGKB; PA25196; -.
DR VEuPathDB; HostDB:ENSG00000168646; -.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000157338; -.
DR InParanoid; Q9Y2T1; -.
DR OrthoDB; 1481971at2759; -.
DR PhylomeDB; Q9Y2T1; -.
DR TreeFam; TF315454; -.
DR PathwayCommons; Q9Y2T1; -.
DR Reactome; R-HSA-201681; TCF dependent signaling in response to WNT.
DR Reactome; R-HSA-4411364; Binding of TCF/LEF:CTNNB1 to target gene promoters.
DR Reactome; R-HSA-4641257; Degradation of AXIN.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR SignaLink; Q9Y2T1; -.
DR SIGNOR; Q9Y2T1; -.
DR BioGRID-ORCS; 8313; 18 hits in 1086 CRISPR screens.
DR ChiTaRS; AXIN2; human.
DR GeneWiki; AXIN2; -.
DR GenomeRNAi; 8313; -.
DR Pharos; Q9Y2T1; Tchem.
DR PRO; PR:Q9Y2T1; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9Y2T1; protein.
DR Bgee; ENSG00000168646; Expressed in oviduct epithelium and 158 other tissues.
DR ExpressionAtlas; Q9Y2T1; baseline and differential.
DR Genevisible; Q9Y2T1; HS.
DR GO; GO:0030877; C:beta-catenin destruction complex; IBA:GO_Central.
DR GO; GO:0005813; C:centrosome; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008013; F:beta-catenin binding; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0070411; F:I-SMAD binding; IBA:GO_Central.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
DR GO; GO:0008219; P:cell death; IEA:Ensembl.
DR GO; GO:0048468; P:cell development; IBA:GO_Central.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
DR GO; GO:0003413; P:chondrocyte differentiation involved in endochondral bone morphogenesis; IEA:Ensembl.
DR GO; GO:0001957; P:intramembranous ossification; IEA:Ensembl.
DR GO; GO:0043570; P:maintenance of DNA repeat elements; IMP:BHF-UCL.
DR GO; GO:0048255; P:mRNA stabilization; IMP:BHF-UCL.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:BHF-UCL.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:BHF-UCL.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0033689; P:negative regulation of osteoblast proliferation; IEA:Ensembl.
DR GO; GO:2000054; P:negative regulation of Wnt signaling pathway involved in dorsal/ventral axis specification; IEA:Ensembl.
DR GO; GO:0042476; P:odontogenesis; IMP:BHF-UCL.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0033687; P:osteoblast proliferation; IEA:Ensembl.
DR GO; GO:0010942; P:positive regulation of cell death; IMP:BHF-UCL.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:BHF-UCL.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; IEA:Ensembl.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IBA:GO_Central.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:BHF-UCL.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IC:ComplexPortal.
DR GO; GO:0008104; P:protein localization; IDA:BHF-UCL.
DR GO; GO:0070602; P:regulation of centromeric sister chromatid cohesion; IMP:BHF-UCL.
DR GO; GO:0061181; P:regulation of chondrocyte development; IEA:Ensembl.
DR GO; GO:0032423; P:regulation of mismatch repair; IMP:BHF-UCL.
DR GO; GO:0003139; P:secondary heart field specification; IEA:Ensembl.
DR GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
DR GO; GO:0072089; P:stem cell proliferation; IEA:Ensembl.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd11582; Axin_TNKS_binding; 1.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 1.10.196.10; -; 1.
DR Gene3D; 2.40.240.130; -; 1.
DR InterPro; IPR043581; Axin-like.
DR InterPro; IPR014936; Axin_b-cat-bd.
DR InterPro; IPR032101; Axin_TNKS-bd.
DR InterPro; IPR001158; DIX.
DR InterPro; IPR038207; DIX_dom_sf.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR024066; RGS_subdom1/3.
DR InterPro; IPR044926; RGS_subdomain_2.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR46102; PTHR46102; 1.
DR Pfam; PF16646; AXIN1_TNKS_BD; 1.
DR Pfam; PF08833; Axin_b-cat_bind; 1.
DR Pfam; PF00778; DIX; 1.
DR Pfam; PF00615; RGS; 1.
DR PRINTS; PR01301; RGSPROTEIN.
DR SMART; SM00021; DAX; 1.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50841; DIX; 1.
DR PROSITE; PS50132; RGS; 1.
PE 1: Evidence at protein level;
KW ADP-ribosylation; Cytoplasm; Developmental protein; Phosphoprotein;
KW Reference proteome; Ubl conjugation; Wnt signaling pathway.
FT CHAIN 1..843
FT /note="Axin-2"
FT /id="PRO_0000220895"
FT DOMAIN 81..200
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT DOMAIN 761..843
FT /note="DIX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00069"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..413
FT /note="Interaction with GSK3B"
FT /evidence="ECO:0000250"
FT REGION 334..393
FT /note="Interaction with SIAH1 and SIAH2"
FT /evidence="ECO:0000269|PubMed:28546513"
FT REGION 396..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..476
FT /note="Interaction with beta-catenin"
FT /evidence="ECO:0000250"
FT REGION 447..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 21..30
FT /note="Tankyrase-binding motif"
FT COMPBIAS 396..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 50
FT /note="P -> S (in dbSNP:rs2240308)"
FT /evidence="ECO:0000269|PubMed:10049590,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16820935"
FT /id="VAR_054860"
FT CONFLICT 37..62
FT /note="QPGVGKGQVTKPMPVSSNTRRNEDGL -> HHGGQGPGHQTHVCLFQHQAER
FT RWV (in Ref. 2; AAF22799)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="Q -> R (in Ref. 2; AAF22799)"
FT /evidence="ECO:0000305"
FT CONFLICT 572..636
FT /note="Missing (in Ref. 2; AAF22799)"
FT /evidence="ECO:0000305"
FT CONFLICT 687
FT /note="P -> S (in Ref. 2; AAF22799)"
FT /evidence="ECO:0000305"
FT CONFLICT 696
FT /note="Q -> H (in Ref. 2; AAF22799)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 843 AA; 93568 MW; 23E9C72187A9230C CRC64;
MSSAMLVTCL PDPSSSFRED APRPPVPGEE GETPPCQPGV GKGQVTKPMP VSSNTRRNED
GLGEPEGRAS PDSPLTRWTK SLHSLLGDQD GAYLFRTFLE REKCVDTLDF WFACNGFRQM
NLKDTKTLRV AKAIYKRYIE NNSIVSKQLK PATKTYIRDG IKKQQIDSIM FDQAQTEIQS
VMEENAYQMF LTSDIYLEYV RSGGENTAYM SNGGLGSLKV VCGYLPTLNE EEEWTCADFK
CKLSPTVVGL SSKTLRATAS VRSTETVDSG YRSFKRSDPV NPYHIGSGYV FAPATSANDS
EISSDALTDD SMSMTDSSVD GIPPYRVGSK KQLQREMHRS VKANGQVSLP HFPRTHRLPK
EMTPVEPATF AAELISRLEK LKLELESRHS LEERLQQIRE DEEREGSELT LNSREGAPTQ
HPLSLLPSGS YEEDPQTILD DHLSRVLKTP GCQSPGVGRY SPRSRSPDHH HHHHSQYHSL
LPPGGKLPPA AASPGACPLL GGKGFVTKQT TKHVHHHYIH HHAVPKTKEE IEAEATQRVH
CFCPGGSEYY CYSKCKSHSK APETMPSEQF GGSRGSTLPK RNGKGTEPGL ALPAREGGAP
GGAGALQLPR EEGDRSQDVW QWMLESERQS KPKPHSAQST KKAYPLESAR SSPGERASRH
HLWGGNSGHP RTTPRAHLFT QDPAMPPLTP PNTLAQLEEA CRRLAEVSKP PKQRCCVASQ
QRDRNHSATV QTGATPFSNP SLAPEDHKEP KKLAGVHALQ ASELVVTYFF CGEEIPYRRM
LKAQSLTLGH FKEQLSKKGN YRYYFKKASD EFACGAVFEE IWEDETVLPM YEGRILGKVE
RID
