Axin-1

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• armadillo repeat domain binding Source: MGI
• beta-catenin binding Source: MGI <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • Ref.3

    "A GSK3beta phosphorylation site in axin modulates interaction with beta-catenin and Tcf-mediated gene expression."
    Jho E., Lomvardas S., Costantini F.
    Biochem. Biophys. Res. Commun. 266:28-35(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: PHOSPHORYLATION AT THR-480; SER-485 AND SER-492, INTERACTION WITH CTNNB1, MUTAGENESIS OF THR-480; SER-485; SER-492 AND SER-495.
• enzyme binding Source: MGI
• identical protein binding Source: MGI <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "Functional domains of axin. Importance of the C terminus as an oligomerization domain."
    Sakanaka C., Williams L.T.
    J Biol Chem 274:14090-14093(1999) [PubMed] [Europe PMC] [Abstract]
  • "Axin contains three separable domains that confer intramolecular, homodimeric, and heterodimeric interactions involved in distinct functions."
    Luo W., Zou H., Jin L., Lin S., Li Q., Ye Z., Rui H., Lin S.C.
    J Biol Chem 280:5054-5060(2005) [PubMed] [Europe PMC] [Abstract]
  • Ref.12

    "SUMOylation target sites at the C terminus protect Axin from ubiquitination and confer protein stability."
    Kim M.J., Chia I.V., Costantini F.
    FASEB J. 22:3785-3794(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUMOYLATION AT LYS-858 AND LYS-861, MUTAGENESIS OF LYS-858 AND LYS-861.
  • "Identification of a domain of Axin that binds to the serine/threonine protein phosphatase 2A and a self-binding domain."
    Hsu W., Zeng L., Costantini F.
    J. Biol. Chem. 274:3439-3445(1999) [PubMed] [Europe PMC] [Abstract]
• I-SMAD binding Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Axin is a scaffold protein in TGF-beta signaling that promotes degradation of Smad7 by Arkadia."
    Liu W., Rui H., Wang J., Lin S., He Y., Chen M., Li Q., Ye Z., Zhang S., Chan S.C., Chen Y.-G., Han J., Lin S.-C.
    EMBO J. 25:1646-1658(2006) [PubMed] [Europe PMC] [Abstract]
• molecular adaptor activity Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "Axin is a scaffold protein in TGF-beta signaling that promotes degradation of Smad7 by Arkadia."
    Liu W., Rui H., Wang J., Lin S., He Y., Chen M., Li Q., Ye Z., Zhang S., Chan S.C., Chen Y.-G., Han J., Lin S.-C.
    EMBO J. 25:1646-1658(2006) [PubMed] [Europe PMC] [Abstract]
• p53 binding Source: MGIInferred from physical interactionⁱ
  • Ref.8

    "Axin stimulates p53 functions by activation of HIPK2 kinase through multimeric complex formation."
    Rui Y., Xu Z., Lin S., Li Q., Rui H., Luo W., Zhou H.-M., Cheung P.-Y., Wu Z., Ye Z., Li P., Han J., Lin S.-C.
    EMBO J. 23:4583-4594(2004) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH TP53 AND HIPK2, IDENTIFICATION IN A COMPLEX WITH TP53 AND HIPK2.
• protein C-terminus binding Source: MGIInferred from direct assayⁱ
  • "Functional domains of axin. Importance of the C terminus as an oligomerization domain."
    Sakanaka C., Williams L.T.
    J Biol Chem 274:14090-14093(1999) [PubMed] [Europe PMC] [Abstract]
• protein domain specific binding Source: MGIInferred from physical interactionⁱ
  • "Axin contains three separable domains that confer intramolecular, homodimeric, and heterodimeric interactions involved in distinct functions."
    Luo W., Zou H., Jin L., Lin S., Li Q., Ye Z., Rui H., Lin S.C.
    J Biol Chem 280:5054-5060(2005) [PubMed] [Europe PMC] [Abstract]
  • Ref.11

    "A beta-catenin-independent dorsalization pathway activated by Axin/JNK signaling and antagonized by aida."
    Rui Y., Xu Z., Xiong B., Cao Y., Lin S., Zhang M., Chan S.-C., Luo W., Han Y., Lu Z., Ye Z., Zhou H.-M., Han J., Meng A., Lin S.-C.
    Dev. Cell 13:268-282(2007) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, HOMODIMERIZATION, INTERACTION WITH AIDA.
• protein homodimerization activity Source: UniProtKBInferred from physical interactionⁱ
  • Ref.11

    "A beta-catenin-independent dorsalization pathway activated by Axin/JNK signaling and antagonized by aida."
    Rui Y., Xu Z., Xiong B., Cao Y., Lin S., Zhang M., Chan S.-C., Luo W., Han Y., Lu Z., Ye Z., Zhou H.-M., Han J., Meng A., Lin S.-C.
    Dev. Cell 13:268-282(2007) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, HOMODIMERIZATION, INTERACTION WITH AIDA.
• protein kinase binding Source: ParkinsonsUK-UCLInferred from physical interactionⁱ
  • "LRRK2 functions as a Wnt signaling scaffold, bridging cytosolic proteins and membrane-localized LRP6."
    Berwick D.C., Harvey K.
    Hum Mol Genet 21:4966-4979(2012) [PubMed] [Europe PMC] [Abstract]
• protein self-association Source: MGIInferred from physical interactionⁱ
  • "Axin contains three separable domains that confer intramolecular, homodimeric, and heterodimeric interactions involved in distinct functions."
    Luo W., Zou H., Jin L., Lin S., Li Q., Ye Z., Rui H., Lin S.C.
    J Biol Chem 280:5054-5060(2005) [PubMed] [Europe PMC] [Abstract]
• R-SMAD binding Source: MGIInferred from physical interactionⁱ
  • "Axin is a scaffold protein in TGF-beta signaling that promotes degradation of Smad7 by Arkadia."
    Liu W., Rui H., Wang J., Lin S., He Y., Chen M., Li Q., Ye Z., Zhang S., Chan S.C., Chen Y.-G., Han J., Lin S.-C.
    EMBO J. 25:1646-1658(2006) [PubMed] [Europe PMC] [Abstract]
• signaling receptor binding Source: MGI
• signaling receptor complex adaptor activity Source: MGI
• SMAD binding Source: MGI
• ubiquitin protein ligase binding Source: BHF-UCLInferred from physical interactionⁱ
  • "Axin is a scaffold protein in TGF-beta signaling that promotes degradation of Smad7 by Arkadia."
    Liu W., Rui H., Wang J., Lin S., He Y., Chen M., Li Q., Ye Z., Zhang S., Chan S.C., Chen Y.-G., Han J., Lin S.-C.
    EMBO J. 25:1646-1658(2006) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• activation of protein kinase activity Source: MGI
• apoptotic process Source: UniProtKB-KW
• axial mesoderm development Source: MGIInferred from mutant phenotypeⁱ
  • Ref.1

    "The mouse Fused locus encodes Axin, an inhibitor of the Wnt signaling pathway that regulates embryonic axis formation."
    Zeng L., Fagotto F., Zhang T., Hsu W., Vasicek T.J., Perry W.L. III, Lee J.J., Tilghman S.M., Gumbiner B.M., Costantini F.
    Cell 90:181-192(1997) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
• axial mesoderm formation Source: MGIInferred from mutant phenotypeⁱ
  • Ref.1

    "The mouse Fused locus encodes Axin, an inhibitor of the Wnt signaling pathway that regulates embryonic axis formation."
    Zeng L., Fagotto F., Zhang T., Hsu W., Vasicek T.J., Perry W.L. III, Lee J.J., Tilghman S.M., Gumbiner B.M., Costantini F.
    Cell 90:181-192(1997) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
• canonical Wnt signaling pathway Source: MGIInferred from direct assayⁱ
  • "Inhibition of adipogenesis by Wnt signaling."
    Ross S.E., Hemati N., Longo K.A., Bennett C.N., Lucas P.C., Erickson R.L., MacDougald O.A.
    Science 289:950-953(2000) [PubMed] [Europe PMC] [Abstract]
• cellular protein-containing complex assembly Source: MGI
• cytoplasmic microtubule organization Source: MGI <p>Inferred from Genetic Interaction</p> <p>Used to describe "traditional" genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#igi">GO evidence code guide</a></p> Inferred from genetic interactionⁱ
  • "A divergent canonical WNT-signaling pathway regulates microtubule dynamics: dishevelled signals locally to stabilize microtubules."
    Ciani L., Krylova O., Smalley M.J., Dale T.C., Salinas P.C.
    J Cell Biol 164:243-253(2004) [PubMed] [Europe PMC] [Abstract]
• dorsal/ventral axis specification Source: MGIInferred from direct assayⁱ
  • "Domains of axin involved in protein-protein interactions, Wnt pathway inhibition, and intracellular localization."
    Fagotto F., Jho E.h., Zeng L., Kurth T., Joos T., Kaufmann C., Costantini F.
    J Cell Biol 145:741-756(1999) [PubMed] [Europe PMC] [Abstract]
• dorsal/ventral pattern formation Source: MGIInferred from mutant phenotypeⁱ
  • "Protein encoded by the Axin(Fu) allele effectively down-regulates Wnt signaling but exerts a dominant negative effect on c-Jun N-terminal kinase signaling."
    Lu Z., Liu W., Huang H., He Y., Han Y., Rui Y., Wang Y., Li Q., Ruan K., Ye Z., Low B.C., Meng A., Lin S.C.
    J Biol Chem 283:13132-13139(2008) [PubMed] [Europe PMC] [Abstract]
• genetic imprinting Source: MGIInferred from mutant phenotypeⁱ
  • "Transgenerational inheritance of epigenetic states at the murine Axin(Fu) allele occurs after maternal and paternal transmission."
    Rakyan V.K., Chong S., Champ M.E., Cuthbert P.C., Morgan H.D., Luu K.V., Whitelaw E.
    Proc Natl Acad Sci U S A 100:2538-2543(2003) [PubMed] [Europe PMC] [Abstract]
• head development Source: MGIInferred from mutant phenotypeⁱ
  • "Generation of Axin1 conditional mutant mice."
    Xie R., Jiang R., Chen D.
    Genesis 49:98-102(2011) [PubMed] [Europe PMC] [Abstract]
• in utero embryonic development Source: MGIInferred from mutant phenotypeⁱ
  • "Both the RGS domain and the six C-terminal amino acids of mouse Axin are required for normal embryogenesis."
    Chia I.V., Kim M.J., Itoh K., Sokol S.Y., Costantini F.
    Genetics 181:1359-1368(2009) [PubMed] [Europe PMC] [Abstract]
• negative regulation of canonical Wnt signaling pathway Source: MGIInferred from direct assayⁱ
  • "Axin contains three separable domains that confer intramolecular, homodimeric, and heterodimeric interactions involved in distinct functions."
    Luo W., Zou H., Jin L., Lin S., Li Q., Ye Z., Rui H., Lin S.C.
    J Biol Chem 280:5054-5060(2005) [PubMed] [Europe PMC] [Abstract]
  • "Both the RGS domain and the six C-terminal amino acids of mouse Axin are required for normal embryogenesis."
    Chia I.V., Kim M.J., Itoh K., Sokol S.Y., Costantini F.
    Genetics 181:1359-1368(2009) [PubMed] [Europe PMC] [Abstract]
• negative regulation of fat cell differentiation Source: MGIInferred from direct assayⁱ
  • "Inhibition of adipogenesis by Wnt signaling."
    Ross S.E., Hemati N., Longo K.A., Bennett C.N., Lucas P.C., Erickson R.L., MacDougald O.A.
    Science 289:950-953(2000) [PubMed] [Europe PMC] [Abstract]
• negative regulation of gene expression Source: MGIInferred from direct assayⁱ
  • "Putative tumor suppressor EDD interacts with and up-regulates APC."
    Ohshima R., Ohta T., Wu W., Koike A., Iwatani T., Henderson M., Watts C.K., Otsubo T.
    Genes Cells 12:1339-1345(2007) [PubMed] [Europe PMC] [Abstract]
• negative regulation of protein metabolic process Source: MGIInferred from direct assayⁱ
  • "Domains of axin involved in protein-protein interactions, Wnt pathway inhibition, and intracellular localization."
    Fagotto F., Jho E.h., Zeng L., Kurth T., Joos T., Kaufmann C., Costantini F.
    J Cell Biol 145:741-756(1999) [PubMed] [Europe PMC] [Abstract]
• negative regulation of transcription elongation from RNA polymerase II promoter Source: MGIInferred from direct assayⁱ
  • "Functional domains of axin. Importance of the C terminus as an oligomerization domain."
    Sakanaka C., Williams L.T.
    J Biol Chem 274:14090-14093(1999) [PubMed] [Europe PMC] [Abstract]
  • "Both the RGS domain and the six C-terminal amino acids of mouse Axin are required for normal embryogenesis."
    Chia I.V., Kim M.J., Itoh K., Sokol S.Y., Costantini F.
    Genetics 181:1359-1368(2009) [PubMed] [Europe PMC] [Abstract]
• negative regulation of Wnt signaling pathway Source: MGIInferred from direct assayⁱ
  • "A role for Wnt signalling in self-renewal of haematopoietic stem cells."
    Reya T., Duncan A.W., Ailles L., Domen J., Scherer D.C., Willert K., Hintz L., Nusse R., Weissman I.L.
    Nature 423:409-414(2003) [PubMed] [Europe PMC] [Abstract]
  • Ref.11

    "A beta-catenin-independent dorsalization pathway activated by Axin/JNK signaling and antagonized by aida."
    Rui Y., Xu Z., Xiong B., Cao Y., Lin S., Zhang M., Chan S.-C., Luo W., Han Y., Lu Z., Ye Z., Zhou H.-M., Han J., Meng A., Lin S.-C.
    Dev. Cell 13:268-282(2007) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, HOMODIMERIZATION, INTERACTION WITH AIDA.
  • Ref.1

    "The mouse Fused locus encodes Axin, an inhibitor of the Wnt signaling pathway that regulates embryonic axis formation."
    Zeng L., Fagotto F., Zhang T., Hsu W., Vasicek T.J., Perry W.L. III, Lee J.J., Tilghman S.M., Gumbiner B.M., Costantini F.
    Cell 90:181-192(1997) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
  • Ref.3

    "A GSK3beta phosphorylation site in axin modulates interaction with beta-catenin and Tcf-mediated gene expression."
    Jho E., Lomvardas S., Costantini F.
    Biochem. Biophys. Res. Commun. 266:28-35(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: PHOSPHORYLATION AT THR-480; SER-485 AND SER-492, INTERACTION WITH CTNNB1, MUTAGENESIS OF THR-480; SER-485; SER-492 AND SER-495.
• nucleocytoplasmic transport Source: MGIInferred from direct assayⁱ
  • "Nuclear-cytoplasmic shuttling of Axin regulates subcellular localization of beta-catenin."
    Cong F., Varmus H.
    Proc Natl Acad Sci U S A 101:2882-2887(2004) [PubMed] [Europe PMC] [Abstract]
• positive regulation of JNK cascade Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.11

    "A beta-catenin-independent dorsalization pathway activated by Axin/JNK signaling and antagonized by aida."
    Rui Y., Xu Z., Xiong B., Cao Y., Lin S., Zhang M., Chan S.-C., Luo W., Han Y., Lu Z., Ye Z., Zhou H.-M., Han J., Meng A., Lin S.-C.
    Dev. Cell 13:268-282(2007) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, HOMODIMERIZATION, INTERACTION WITH AIDA.
• positive regulation of JUN kinase activity Source: MGIInferred from direct assayⁱ
  • "Axin utilizes distinct regions for competitive MEKK1 and MEKK4 binding and JNK activation."
    Luo W., Ng W.W., Jin L.H., Ye Z., Han J., Lin S.C.
    J Biol Chem 278:37451-37458(2003) [PubMed] [Europe PMC] [Abstract]
• positive regulation of peptidyl-serine phosphorylation Source: ParkinsonsUK-UCLInferred from direct assayⁱ
  • "Control of beta-catenin phosphorylation/degradation by a dual-kinase mechanism."
    Liu C., Li Y., Semenov M., Han C., Baeg G.-H., Tan Y., Zhang Z., Lin X., He X.
    Cell 108:837-847(2002) [PubMed] [Europe PMC] [Abstract]
• positive regulation of peptidyl-threonine phosphorylation Source: ParkinsonsUK-UCLInferred from direct assayⁱ
  • "Control of beta-catenin phosphorylation/degradation by a dual-kinase mechanism."
    Liu C., Li Y., Semenov M., Han C., Baeg G.-H., Tan Y., Zhang Z., Lin X., He X.
    Cell 108:837-847(2002) [PubMed] [Europe PMC] [Abstract]
• positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: MGIInferred from direct assayⁱ
  • "Axin is a scaffold protein in TGF-beta signaling that promotes degradation of Smad7 by Arkadia."
    Liu W., Rui H., Wang J., Lin S., He Y., Chen M., Li Q., Ye Z., Zhang S., Chan S.C., Chen Y.-G., Han J., Lin S.-C.
    EMBO J. 25:1646-1658(2006) [PubMed] [Europe PMC] [Abstract]
• positive regulation of protein catabolic process Source: MGI
• positive regulation of protein kinase activity Source: CACAOInferred from direct assayⁱ
  • Ref.8

    "Axin stimulates p53 functions by activation of HIPK2 kinase through multimeric complex formation."
    Rui Y., Xu Z., Lin S., Li Q., Rui H., Luo W., Zhou H.-M., Cheung P.-Y., Wu Z., Ye Z., Li P., Han J., Lin S.-C.
    EMBO J. 23:4583-4594(2004) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH TP53 AND HIPK2, IDENTIFICATION IN A COMPLEX WITH TP53 AND HIPK2.
• positive regulation of protein phosphorylation Source: MGIInferred from direct assayⁱ
  • "Domains of axin involved in protein-protein interactions, Wnt pathway inhibition, and intracellular localization."
    Fagotto F., Jho E.h., Zeng L., Kurth T., Joos T., Kaufmann C., Costantini F.
    J Cell Biol 145:741-756(1999) [PubMed] [Europe PMC] [Abstract]
• positive regulation of protein ubiquitination Source: MGIInferred from direct assayⁱ
  • "Axin is a scaffold protein in TGF-beta signaling that promotes degradation of Smad7 by Arkadia."
    Liu W., Rui H., Wang J., Lin S., He Y., Chen M., Li Q., Ye Z., Zhang S., Chan S.C., Chen Y.-G., Han J., Lin S.-C.
    EMBO J. 25:1646-1658(2006) [PubMed] [Europe PMC] [Abstract]
• positive regulation of transcription, DNA-templated Source: BHF-UCLInferred from direct assayⁱ
  • "Axin is a scaffold protein in TGF-beta signaling that promotes degradation of Smad7 by Arkadia."
    Liu W., Rui H., Wang J., Lin S., He Y., Chen M., Li Q., Ye Z., Zhang S., Chan S.C., Chen Y.-G., Han J., Lin S.-C.
    EMBO J. 25:1646-1658(2006) [PubMed] [Europe PMC] [Abstract]
• positive regulation of transforming growth factor beta receptor signaling pathway Source: MGIInferred from direct assayⁱ
  • "Axin is a scaffold protein in TGF-beta signaling that promotes degradation of Smad7 by Arkadia."
    Liu W., Rui H., Wang J., Lin S., He Y., Chen M., Li Q., Ye Z., Zhang S., Chan S.C., Chen Y.-G., Han J., Lin S.-C.
    EMBO J. 25:1646-1658(2006) [PubMed] [Europe PMC] [Abstract]
• positive regulation of ubiquitin-dependent protein catabolic process Source: MGIInferred from direct assayⁱ
  • "Axin is a scaffold protein in TGF-beta signaling that promotes degradation of Smad7 by Arkadia."
    Liu W., Rui H., Wang J., Lin S., He Y., Chen M., Li Q., Ye Z., Zhang S., Chan S.C., Chen Y.-G., Han J., Lin S.-C.
    EMBO J. 25:1646-1658(2006) [PubMed] [Europe PMC] [Abstract]
• positive regulation of ubiquitin-protein transferase activity Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "Axin is a scaffold protein in TGF-beta signaling that promotes degradation of Smad7 by Arkadia."
    Liu W., Rui H., Wang J., Lin S., He Y., Chen M., Li Q., Ye Z., Zhang S., Chan S.C., Chen Y.-G., Han J., Lin S.-C.
    EMBO J. 25:1646-1658(2006) [PubMed] [Europe PMC] [Abstract]
• post-anal tail morphogenesis Source: MGIInferred from mutant phenotypeⁱ
  • "Transgenerational inheritance of epigenetic states at the murine Axin(Fu) allele occurs after maternal and paternal transmission."
    Rakyan V.K., Chong S., Champ M.E., Cuthbert P.C., Morgan H.D., Luu K.V., Whitelaw E.
    Proc Natl Acad Sci U S A 100:2538-2543(2003) [PubMed] [Europe PMC] [Abstract]
• protein catabolic process Source: MGIInferred from direct assayⁱ
  • "A role for Wnt signalling in self-renewal of haematopoietic stem cells."
    Reya T., Duncan A.W., Ailles L., Domen J., Scherer D.C., Willert K., Hintz L., Nusse R., Weissman I.L.
    Nature 423:409-414(2003) [PubMed] [Europe PMC] [Abstract]
• protein polyubiquitination Source: MGIInferred from direct assayⁱ
  • "Axin is a scaffold protein in TGF-beta signaling that promotes degradation of Smad7 by Arkadia."
    Liu W., Rui H., Wang J., Lin S., He Y., Chen M., Li Q., Ye Z., Zhang S., Chan S.C., Chen Y.-G., Han J., Lin S.-C.
    EMBO J. 25:1646-1658(2006) [PubMed] [Europe PMC] [Abstract]
• regulation of canonical Wnt signaling pathway Source: MGIInferred from direct assayⁱ
  • "Nuclear-cytoplasmic shuttling of Axin regulates subcellular localization of beta-catenin."
    Cong F., Varmus H.
    Proc Natl Acad Sci U S A 101:2882-2887(2004) [PubMed] [Europe PMC] [Abstract]
• regulation of protein phosphorylation Source: MGIInferred from genetic interactionⁱ
  • "A divergent canonical WNT-signaling pathway regulates microtubule dynamics: dishevelled signals locally to stabilize microtubules."
    Ciani L., Krylova O., Smalley M.J., Dale T.C., Salinas P.C.
    J Cell Biol 164:243-253(2004) [PubMed] [Europe PMC] [Abstract]
• sensory perception of sound Source: MGIInferred from mutant phenotypeⁱ
  • "A case of neighboring loci with similar effects."
    DUNN L.C., CASPARI E.
    Genetics 30:543-568(1945) [PubMed] [Europe PMC] [Abstract]
• Wnt signaling pathway Source: MGIInferred from direct assayⁱ
  • "Inhibition of the Wnt signaling pathway by Idax, a novel Dvl-binding protein."
    Hino S., Kishida S., Michiue T., Fukui A., Sakamoto I., Takada S., Asashima M., Kikuchi A.
    Mol. Cell. Biol. 21:330-342(2001) [PubMed] [Europe PMC] [Abstract]

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

• UniProt annotation
• GO - Cellular component

Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Mutagenesis

Keywords - Diseaseⁱ

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stageⁱ

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• armadillo repeat domain binding Source: MGI
• beta-catenin binding Source: MGIInferred from mutant phenotypeⁱ
  • Ref.3

    "A GSK3beta phosphorylation site in axin modulates interaction with beta-catenin and Tcf-mediated gene expression."
    Jho E., Lomvardas S., Costantini F.
    Biochem. Biophys. Res. Commun. 266:28-35(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: PHOSPHORYLATION AT THR-480; SER-485 AND SER-492, INTERACTION WITH CTNNB1, MUTAGENESIS OF THR-480; SER-485; SER-492 AND SER-495.
• enzyme binding Source: MGI
• identical protein binding Source: MGIInferred from physical interactionⁱ
  • "Functional domains of axin. Importance of the C terminus as an oligomerization domain."
    Sakanaka C., Williams L.T.
    J Biol Chem 274:14090-14093(1999) [PubMed] [Europe PMC] [Abstract]
  • "Axin contains three separable domains that confer intramolecular, homodimeric, and heterodimeric interactions involved in distinct functions."
    Luo W., Zou H., Jin L., Lin S., Li Q., Ye Z., Rui H., Lin S.C.
    J Biol Chem 280:5054-5060(2005) [PubMed] [Europe PMC] [Abstract]
  • Ref.12

    "SUMOylation target sites at the C terminus protect Axin from ubiquitination and confer protein stability."
    Kim M.J., Chia I.V., Costantini F.
    FASEB J. 22:3785-3794(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUMOYLATION AT LYS-858 AND LYS-861, MUTAGENESIS OF LYS-858 AND LYS-861.
  • "Identification of a domain of Axin that binds to the serine/threonine protein phosphatase 2A and a self-binding domain."
    Hsu W., Zeng L., Costantini F.
    J. Biol. Chem. 274:3439-3445(1999) [PubMed] [Europe PMC] [Abstract]
• I-SMAD binding Source: BHF-UCLInferred from direct assayⁱ
  • "Axin is a scaffold protein in TGF-beta signaling that promotes degradation of Smad7 by Arkadia."
    Liu W., Rui H., Wang J., Lin S., He Y., Chen M., Li Q., Ye Z., Zhang S., Chan S.C., Chen Y.-G., Han J., Lin S.-C.
    EMBO J. 25:1646-1658(2006) [PubMed] [Europe PMC] [Abstract]
• p53 binding Source: MGIInferred from physical interactionⁱ
  • Ref.8

    "Axin stimulates p53 functions by activation of HIPK2 kinase through multimeric complex formation."
    Rui Y., Xu Z., Lin S., Li Q., Rui H., Luo W., Zhou H.-M., Cheung P.-Y., Wu Z., Ye Z., Li P., Han J., Lin S.-C.
    EMBO J. 23:4583-4594(2004) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH TP53 AND HIPK2, IDENTIFICATION IN A COMPLEX WITH TP53 AND HIPK2.
• protein C-terminus binding Source: MGIInferred from direct assayⁱ
  • "Functional domains of axin. Importance of the C terminus as an oligomerization domain."
    Sakanaka C., Williams L.T.
    J Biol Chem 274:14090-14093(1999) [PubMed] [Europe PMC] [Abstract]
• protein domain specific binding Source: MGIInferred from physical interactionⁱ
  • "Axin contains three separable domains that confer intramolecular, homodimeric, and heterodimeric interactions involved in distinct functions."
    Luo W., Zou H., Jin L., Lin S., Li Q., Ye Z., Rui H., Lin S.C.
    J Biol Chem 280:5054-5060(2005) [PubMed] [Europe PMC] [Abstract]
  • Ref.11

    "A beta-catenin-independent dorsalization pathway activated by Axin/JNK signaling and antagonized by aida."
    Rui Y., Xu Z., Xiong B., Cao Y., Lin S., Zhang M., Chan S.-C., Luo W., Han Y., Lu Z., Ye Z., Zhou H.-M., Han J., Meng A., Lin S.-C.
    Dev. Cell 13:268-282(2007) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, HOMODIMERIZATION, INTERACTION WITH AIDA.
• protein homodimerization activity Source: UniProtKBInferred from physical interactionⁱ
  • Ref.11

    "A beta-catenin-independent dorsalization pathway activated by Axin/JNK signaling and antagonized by aida."
    Rui Y., Xu Z., Xiong B., Cao Y., Lin S., Zhang M., Chan S.-C., Luo W., Han Y., Lu Z., Ye Z., Zhou H.-M., Han J., Meng A., Lin S.-C.
    Dev. Cell 13:268-282(2007) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, HOMODIMERIZATION, INTERACTION WITH AIDA.
• protein kinase binding Source: ParkinsonsUK-UCLInferred from physical interactionⁱ
  • "LRRK2 functions as a Wnt signaling scaffold, bridging cytosolic proteins and membrane-localized LRP6."
    Berwick D.C., Harvey K.
    Hum Mol Genet 21:4966-4979(2012) [PubMed] [Europe PMC] [Abstract]
• protein self-association Source: MGIInferred from physical interactionⁱ
  • "Axin contains three separable domains that confer intramolecular, homodimeric, and heterodimeric interactions involved in distinct functions."
    Luo W., Zou H., Jin L., Lin S., Li Q., Ye Z., Rui H., Lin S.C.
    J Biol Chem 280:5054-5060(2005) [PubMed] [Europe PMC] [Abstract]
• R-SMAD binding Source: MGIInferred from physical interactionⁱ
  • "Axin is a scaffold protein in TGF-beta signaling that promotes degradation of Smad7 by Arkadia."
    Liu W., Rui H., Wang J., Lin S., He Y., Chen M., Li Q., Ye Z., Zhang S., Chan S.C., Chen Y.-G., Han J., Lin S.-C.
    EMBO J. 25:1646-1658(2006) [PubMed] [Europe PMC] [Abstract]
• signaling receptor binding Source: MGI
• SMAD binding Source: MGI
• ubiquitin protein ligase binding Source: BHF-UCLInferred from physical interactionⁱ
  • "Axin is a scaffold protein in TGF-beta signaling that promotes degradation of Smad7 by Arkadia."
    Liu W., Rui H., Wang J., Lin S., He Y., Chen M., Li Q., Ye Z., Zhang S., Chan S.C., Chen Y.-G., Han J., Lin S.-C.
    EMBO J. 25:1646-1658(2006) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

Region

Motif

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

This entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MNVQEQGFPL DLGASFTEDA PRPPVPGEEG ELVSTDSRPV NHSFCSGKGT 
        60         70         80         90        100
SIKSETSTAT PRRSDLDLGY EPEGSASPTP PYLRWAESLH SLLDDQDGIS 
       110        120        130        140        150
LFRTFLKQEG CADLLDFWFA CSGFRKLEPC DSNEEKRLKL ARAIYRKYIL 
       160        170        180        190        200
DSNGIVSRQT KPATKSFIKD CVMKQQIDPA MFDQAQTEIQ STMEENTYPS 
       210        220        230        240        250
FLKSDIYLEY TRTGSESPKV CSDQSSGSGT GKGMSGYLPT LNEDEEWKCD 
       260        270        280        290        300
QDADEDDGRD PLPPSRLTQK LLLETAAPRA PSSRRYNEGR ELRYGSWREP 
       310        320        330        340        350
VNPYYVNSGY ALAPATSAND SEQQSLSSDA DTLSLTDSSV DGIPPYRIRK 
       360        370        380        390        400
QHRREMQESI QVNGRVPLPH IPRTYRMPKE IRVEPQKFAE ELIHRLEAVQ 
       410        420        430        440        450
RTREAEEKLE ERLKRVRMEE EGEDGEMPSG PMASHKLPSV PAWHHFPPRY 
       460        470        480        490        500
VDMGCSGLRD AHEENPESIL DEHVQRVMRT PGCQSPGPGH RSPDSGHVAK 
       510        520        530        540        550
TAVLGGTASG HGKHVPKLGL KLDTAGLHHH RHVHHHVHHN SARPKEQMEA 
       560        570        580        590        600
EVARRVQSSF SWGPETHGHA KPRSYSENAG TTLSAGDLAF GGKTSAPSKR 
       610        620        630        640        650
NTKKAESGKN ANAEVPSTTE DAEKNQKIMQ WIIEGEKEIS RHRKAGHGSS 
       660        670        680        690        700
GLRKQQAHES SRPLSIERPG AVHPWVSAQL RNSVQPSHLF IQDPTMPPNP 
       710        720        730        740        750
APNPLTQLEE ARRRLEEEEK RANKLPSKQR YVQAVMQRGR TCVRPACAPV 
       760        770        780        790        800
LSVVPAVSDL ELSETETKSQ RKAGGGSAPP CDSIVVAYYF CGEPIPYRTL 
       810        820        830        840        850
VRGRAVTLGQ FKELLTKKGS YRYYFKKVSD EFDCGVVFEE VREDEAVLPV 
       860 
FEEKIIGKVE KVD                                         

        10         20         30         40         50
MNVQEQGFPL DLGASFTEDA PRPPVPGEEG ELVSTDSRPV NHSFCSGKGT 
        60         70         80         90        100
SIKSETSTAT PRRSDLDLGY EPEGSASPTP PYLRWAESLH SLLDDQDGIS 
       110        120        130        140        150
LFRTFLKQEG CADLLDFWFA CSGFRKLEPC DSNEEKRLKL ARAIYRKYIL 
       160        170        180        190        200
DSNGIVSRQT KPATKSFIKD CVMKQQIDPA MFDQAQTEIQ STMEENTYPS 
       210        220        230        240        250
FLKSDIYLEY TRTGSESPKV CSDQSSGSGT GKGMSGYLPT LNEDEEWKCD 
       260        270        280        290        300
QDADEDDGRD PLPPSRLTQK LLLETAAPRA PSSRRYNEGR ELRYGSWREP 
       310        320        330        340        350
VNPYYVNSGY ALAPATSAND SEQQSLSSDA DTLSLTDSSV DGIPPYRIRK 
       360        370        380        390        400
QHRREMQESI QVNGRVPLPH IPRTYRMPKE IRVEPQKFAE ELIHRLEAVQ 
       410        420        430        440        450
RTREAEEKLE ERLKRVRMEE EGEDGEMPSG PMASHKLPSV PAWHHFPPRY 
       460        470        480        490        500
VDMGCSGLRD AHEENPESIL DEHVQRVMRT PGCQSPGPGH RSPDSGHVAK 
       510        520        530        540        550
TAVLGGTASG HGKHVPKLGL KLDTAGLHHH RHVHHHVHHN SARPKEQMEA 
       560        570        580        590        600
EVARRVQSSF SWGPETHGHA KPRSYSENAG TTLSAGDLAF GGKTSAPSKR 
       610        620        630        640        650
NTKKAESGKN ANAEVPSTTE DAEKNQKIMQ WIIEGEKEIS RHRKAGHGSS 
       660        670        680        690        700
GLRKQQAHES SRPLSIERPG AVHPWVSAQL RNSVQPSHLF IQDPTMPPNP 
       710        720        730        740        750
APNPLTQLEE ARRRLEEEEK RANKLPSKQR TKSQRKAGGG SAPPCDSIVV 
       760        770        780        790        800
AYYFCGEPIP YRTLVRGRAV TLGQFKELLT KKGSYRYYFK KVSDEFDCGV 
       810        820 
VFEEVREDEA VLPVFEEKII GKVEKVD                          

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautionⁱ

Experimental Info

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityⁱ

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. MGD cross-references
   Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
2. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references