MOUSE:AXIN1

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Species (Taxon ID)	Mus musculus (Mouse). ([1])
Gene Name(s)	Axin1 (synonyms: Axin, Fu)
Protein Name(s)	Axin-1 Axis inhibition protein 1 Protein Fused
External Links
EMBL	AF009011
IPI	IPI00875849 IPI00974688
RefSeq	NP_033863.2
UniGene	Mm.23684
ProteinModelPortal	O35625
SMR	O35625
DIP	DIP-42637N
IntAct	O35625
MINT	MINT-1543084
STRING	O35625
PhosphoSite	O35625
PRIDE	O35625
GeneID	12005
KEGG	mmu:12005
UCSC	uc008bdm.2
CTD	8312
MGI	MGI:1096327
eggNOG	roNOG11401
HOGENOM	HBG714290
HOVERGEN	HBG004324
InParanoid	O35625
OrthoDB	EOG47SSDB
NextBio	280195
ArrayExpress	O35625
Bgee	O35625
CleanEx	MM_AXIN1
Genevestigator	O35625
GermOnline	ENSMUSG00000024182
GO	GO:0034747 GO:0005938 GO:0016023 GO:0005881 GO:0005634 GO:0005886 GO:0044459 GO:0014069 GO:0005625 GO:0070016 GO:0008013 GO:0005096 GO:0070411 GO:0008022 GO:0032947 GO:0019904 GO:0042803 GO:0019901 GO:0043621 GO:0070412 GO:0004871 GO:0031625 GO:0007257 GO:0006915 GO:0048320 GO:0060823 GO:0008219 GO:0071407 GO:0031122 GO:0007368 GO:0009950 GO:0048048 GO:0021797 GO:0071514 GO:0001701 GO:0007275 GO:0055001 GO:0090090 GO:0045599 GO:0051248 GO:0034244 GO:0006913 GO:0030910 GO:0001743 GO:0046330 GO:0032436 GO:0001934 GO:2000060 GO:0045893 GO:0030511 GO:0051443 GO:0030163 GO:0051260 GO:0000209 GO:0035412 GO:0007605 GO:0035121 GO:0016055 GO:0021881 GO:0090244
InterPro	IPR014936 IPR001158 IPR000342 IPR024066 IPR016137
Gene3D	G3DSA:1.10.196.10
KO	K02157
Pfam	PF08833 PF00778 PF00615
PRINTS	PR01301
SMART	SM00021 SM00315
SUPFAM	SSF48097
PROSITE	PS50841 PS50132

Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes	Status
	GO:0000209	protein polyubiquitination	PMID:16601693^[1]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0001701	in utero embryonic development	PMID:19204372^[2]	IGI: Inferred from Genetic Interaction	MGI:MGI:88276	P	Seeded From UniProt
	GO:0001701	in utero embryonic development	PMID:19204372^[2]	IMP: Inferred from Mutant Phenotype	MGI:MGI:3840236	P	Seeded From UniProt
	GO:0001701	in utero embryonic development	PMID:19204372^[2]	IMP: Inferred from Mutant Phenotype	MGI:MGI:3840238	P	Seeded From UniProt
	GO:0001743	optic placode formation	GO_REF:0000033		PANTHER:PTHR10845	P	Seeded From UniProt
	GO:0001932	regulation of protein phosphorylation	PMID:14734535^[3]	IGI: Inferred from Genetic Interaction	MGI:MGI:94941	P	Seeded From UniProt
	GO:0001934	positive regulation of protein phosphorylation	PMID:10330403^[4]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0004871	signal transducer activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000342	F	Seeded From UniProt
	GO:0004871	signal transducer activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR001158	F	Seeded From UniProt
	GO:0005096	GTPase activator activity	GO_REF:0000033		PANTHER:PTHR10845	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:10688669^[5]	IPI: Inferred from Physical Interaction	UniProtKB:Q9PTP2	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:12805222^[6]	IPI: Inferred from Physical Interaction	UniProtKB:P98078	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:12805222^[6]	IPI: Inferred from Physical Interaction	UniProtKB:Q61062	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:12878610^[7]	IPI: Inferred from Physical Interaction	UniProtKB:O08648	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:12878610^[7]	IPI: Inferred from Physical Interaction	UniProtKB:P53349	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:15579909^[8]	IPI: Inferred from Physical Interaction	UniProtKB:Q60838	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:15579909^[8]	IPI: Inferred from Physical Interaction	UniProtKB:Q80Y83	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:17681137^[9]	IPI: Inferred from Physical Interaction	UniProtKB:O08648	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:17681137^[9]	IPI: Inferred from Physical Interaction	UniProtKB:P53349	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:17681137^[9]	IPI: Inferred from Physical Interaction	UniProtKB:Q8C4Q6	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:17681137^[9]	IPI: Inferred from Physical Interaction	UniProtKB:Q8C4Q6	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:18632848^[10]	IPI: Inferred from Physical Interaction	UniProtKB:Q91VN0	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:18632848^[10]	IPI: Inferred from Physical Interaction	UniProtKB:Q9WV60	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:19075000^[11]	IPI: Inferred from Physical Interaction	UniProtKB:Q91VN0	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:19759537^[12]	IPI: Inferred from Physical Interaction	UniProtKB:O95271	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:9920888^[13]	IPI: Inferred from Physical Interaction	UniProtKB:P63330	F	Seeded From UniProt
	GO:0005622	intracellular	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR001158	C	Seeded From UniProt
	GO:0005625	soluble fraction	PMID:16510873^[14]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005634	nucleus	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0539	C	Seeded From UniProt
	GO:0005634	nucleus	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0191	C	Seeded From UniProt
	GO:0005737	cytoplasm	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0963	C	Seeded From UniProt
	GO:0005737	cytoplasm	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0086	C	Seeded From UniProt
	GO:0005737	cytoplasm	PMID:11113207^[15]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005737	cytoplasm	PMID:16601693^[1]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005881	cytoplasmic microtubule	PMID:14734535^[3]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005886	plasma membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-1003	C	Seeded From UniProt
	GO:0005886	plasma membrane	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0039	C	Seeded From UniProt
	GO:0005886	plasma membrane	PMID:16815997^[16]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005938	cell cortex	PMID:10330403^[4]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0006913	nucleocytoplasmic transport	PMID:14981260^[17]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0006915	apoptosis	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0053	P	Seeded From UniProt
	GO:0007257	activation of JUN kinase activity	GO_REF:0000033		PANTHER:PTHR10845	P	Seeded From UniProt
	GO:0007275	multicellular organismal development	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR001158	P	Seeded From UniProt
	GO:0007275	multicellular organismal development	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0217	P	Seeded From UniProt
	GO:0007368	determination of left/right symmetry	GO_REF:0000033		PANTHER:PTHR10845	P	Seeded From UniProt
	GO:0007605	sensory perception of sound	PMID:17247179^[18]	IMP: Inferred from Mutant Phenotype	MGI:MGI:1856035	P	Seeded From UniProt
	GO:0008013	beta-catenin binding	PMID:10318824^[19]	IPI: Inferred from Physical Interaction	UniProtKB:Q02248	F	Seeded From UniProt
	GO:0008013	beta-catenin binding	PMID:10330403^[4]	IPI: Inferred from Physical Interaction	UniProtKB:P35222	F	Seeded From UniProt
	GO:0008013	beta-catenin binding	PMID:10581160^[20]	IMP: Inferred from Mutant Phenotype		F	Seeded From UniProt
	GO:0008013	beta-catenin binding	PMID:18632848^[10]	IPI: Inferred from Physical Interaction	UniProtKB:Q02248	F	Seeded From UniProt
	GO:0008022	protein C-terminus binding	PMID:10318824^[19]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0008022	protein C-terminus binding	PMID:9920888^[13]	IPI: Inferred from Physical Interaction	UniProtKB:P63330	F	Seeded From UniProt
	GO:0008219	cell death	GO_REF:0000033		PANTHER:PTHR10845	P	Seeded From UniProt
	GO:0009950	dorsal/ventral axis specification	PMID:10330403^[4]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0009953	dorsal/ventral pattern formation	PMID:18316368^[21]	IMP: Inferred from Mutant Phenotype	MGI:MGI:1856035	P	Seeded From UniProt
	GO:0014069	postsynaptic density	GO_REF:0000033		PANTHER:PTHR10845	C	Seeded From UniProt
	GO:0016020	membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0472	C	Seeded From UniProt
	GO:0016023	cytoplasmic membrane-bounded vesicle	PMID:11113207^[15]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0016055	Wnt receptor signaling pathway	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0879	P	Seeded From UniProt
	GO:0016055	Wnt receptor signaling pathway	PMID:11113207^[15]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0016055	Wnt receptor signaling pathway	PMID:11113207^[15]	IPI: Inferred from Physical Interaction	UniProtKB:P51141	P	Seeded From UniProt
	GO:0019901	protein kinase binding	PMID:10318824^[19]	IPI: Inferred from Physical Interaction	UniProtKB:P49841	F	Seeded From UniProt
	GO:0019904	protein domain specific binding	PMID:15579909^[8]	IPI: Inferred from Physical Interaction	UniProtKB:Q60838	F	Seeded From UniProt
	GO:0019904	protein domain specific binding	PMID:17681137^[9]	IPI: Inferred from Physical Interaction	UniProtKB:Q8C4Q6	F	Seeded From UniProt
	GO:0021797	forebrain anterior/posterior pattern specification	GO_REF:0000033		PANTHER:PTHR10845	P	Seeded From UniProt
	GO:0021881	Wnt receptor signaling pathway involved in forebrain neuron fate commitment	GO_REF:0000033		PANTHER:PTHR10845	P	Seeded From UniProt
	GO:0030163	protein catabolic process	PMID:12717450^[22]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0030178	negative regulation of Wnt receptor signaling pathway	PMID:10581160^[20]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0030178	negative regulation of Wnt receptor signaling pathway	PMID:12717450^[22]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0030178	negative regulation of Wnt receptor signaling pathway	PMID:17681137^[9]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0030178	negative regulation of Wnt receptor signaling pathway	PMID:9230313^[23]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0030511	positive regulation of transforming growth factor beta receptor signaling pathway	PMID:16601693^[1]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0030511	positive regulation of transforming growth factor beta receptor signaling pathway	PMID:16601693^[1]	IGI: Inferred from Genetic Interaction	MGI:MGI:1934919	P	Seeded From UniProt
	GO:0030910	olfactory placode formation	GO_REF:0000033		PANTHER:PTHR10845	P	Seeded From UniProt
	GO:0031122	cytoplasmic microtubule organization	PMID:14734535^[3]	IGI: Inferred from Genetic Interaction	MGI:MGI:94941	P	Seeded From UniProt
	GO:0031398	positive regulation of protein ubiquitination	PMID:16601693^[1]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0031398	positive regulation of protein ubiquitination	PMID:16601693^[1]	IGI: Inferred from Genetic Interaction	MGI:MGI:1934919	P	Seeded From UniProt
	GO:0031625	ubiquitin protein ligase binding	PMID:16601693^[1]	IPI: Inferred from Physical Interaction	UniProtKB:Q99ML9	F	Seeded From UniProt
	GO:0031625	ubiquitin protein ligase binding	PMID:16601693^[1]	IPI: Inferred from Physical Interaction	UniProtKB:Q99ML9	F	Seeded From UniProt
	GO:0032436	positive regulation of proteasomal ubiquitin-dependent protein catabolic process	PMID:16601693^[1]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0032947	protein complex scaffold	PMID:16601693^[1]	IMP: Inferred from Mutant Phenotype		F	Seeded From UniProt
	GO:0034244	negative regulation of transcription elongation from RNA polymerase II promoter	PMID:10318824^[19]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0034244	negative regulation of transcription elongation from RNA polymerase II promoter	PMID:19204372^[2]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0034747	Axin-APC-beta-catenin-GSK3B complex	PMID:10318824^[19]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0035121	tail morphogenesis	PMID:12601169^[24]	IMP: Inferred from Mutant Phenotype	MGI:MGI:1856035	P	Seeded From UniProt
	GO:0035412	regulation of catenin import into nucleus	PMID:14981260^[17]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0042802	identical protein binding	PMID:9920888^[13]	IPI: Inferred from Physical Interaction	UniProtKB:O35625	F	Seeded From UniProt
	GO:0042803	protein homodimerization activity	PMID:15579909^[8]	IPI: Inferred from Physical Interaction	UniProtKB:O35625	F	Seeded From UniProt
	GO:0042803	protein homodimerization activity	PMID:17681137^[9]	IPI: Inferred from Physical Interaction	UniProtKB:O35625	F	Seeded From UniProt
	GO:0042803	protein homodimerization activity	PMID:18632848^[10]	IPI: Inferred from Physical Interaction	UniProtKB:O35625	F	Seeded From UniProt
	GO:0043234	protein complex	PMID:16601693^[1]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0043507	positive regulation of JUN kinase activity	PMID:12878610^[7]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0043507	positive regulation of JUN kinase activity	PMID:15579909^[8]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0043547	positive regulation of GTPase activity	GO_REF:0000033		PANTHER:PTHR10845	P	Seeded From UniProt
	GO:0043621	protein self-association	PMID:15579909^[8]	IPI: Inferred from Physical Interaction	UniProtKB:O35625	F	Seeded From UniProt
	GO:0044444	cytoplasmic part	PMID:18606656^[25]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0044459	plasma membrane part	PMID:10330403^[4]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0045599	negative regulation of fat cell differentiation	PMID:10937998^[26]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0045893	positive regulation of transcription, DNA-dependent	PMID:16601693^[1]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0046330	positive regulation of JNK cascade	PMID:17681137^[9]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0046330	positive regulation of JNK cascade	PMID:18316368^[21]	IMP: Inferred from Mutant Phenotype	MGI:MGI:1856035	P	Seeded From UniProt
	GO:0048048	embryonic eye morphogenesis	GO_REF:0000033		PANTHER:PTHR10845	P	Seeded From UniProt
	GO:0048318	axial mesoderm development	PMID:9230313^[23]	IMP: Inferred from Mutant Phenotype	MGI:MGI:1857546	P	Seeded From UniProt
	GO:0048320	axial mesoderm formation	PMID:9230313^[23]	IMP: Inferred from Mutant Phenotype	MGI:MGI:1857546	P	Seeded From UniProt
	GO:0051248	negative regulation of protein metabolic process	PMID:10330403^[4]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0051260	protein homooligomerization	PMID:10318824^[19]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0051443	positive regulation of ubiquitin-protein ligase activity	PMID:16601693^[1]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0055001	muscle cell development	GO_REF:0000033		PANTHER:PTHR10845	P	Seeded From UniProt
	GO:0060070	canonical Wnt receptor signaling pathway	PMID:10937998^[26]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0060070	canonical Wnt receptor signaling pathway	PMID:19075000^[11]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0060823	canonical Wnt receptor signaling pathway involved in neural plate anterior/posterior pattern formation	GO_REF:0000033		PANTHER:PTHR10845	P	Seeded From UniProt
	GO:0070016	armadillo repeat domain binding	GO_REF:0000033		PANTHER:PTHR10845	F	Seeded From UniProt
	GO:0070411	I-SMAD binding	PMID:16601693^[1]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0070411	I-SMAD binding	PMID:16601693^[1]	IPI: Inferred from Physical Interaction	UniProtKB:O35182	F	Seeded From UniProt
	GO:0070411	I-SMAD binding	PMID:16601693^[1]	IPI: Inferred from Physical Interaction	UniProtKB:O35253	F	Seeded From UniProt
	GO:0070412	R-SMAD binding	PMID:16601693^[1]	IPI: Inferred from Physical Interaction	UniProtKB:Q8BUN5	F	Seeded From UniProt
	GO:0071407	cellular response to organic cyclic compound	GO_REF:0000033		PANTHER:PTHR10845	P	Seeded From UniProt
	GO:0071514	genetic imprinting	PMID:12601169^[24]	IMP: Inferred from Mutant Phenotype	MGI:MGI:1856035	P	Seeded From UniProt
	GO:0090090	negative regulation of canonical Wnt receptor signaling pathway	PMID:15579909^[8]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0090090	negative regulation of canonical Wnt receptor signaling pathway	PMID:19204372^[2]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0090244	Wnt receptor signaling pathway involved in somitogenesis	GO_REF:0000033		PANTHER:PTHR10845	P	Seeded From UniProt
	GO:2000060	positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process	PMID:16601693^[1]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0045860	positive regulation of protein kinase activity	PMID:15526030^[27]	IDA: Inferred from Direct Assay		P	Figures 4,6,8: Axin activates HIPK2 (homeodomain-interacting protein kinase-2)-mediated p53 phosphorylation and p53-dependent transcription and apoptosis.	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.00 ^1.01 ^1.02 ^1.03 ^1.04 ^1.05 ^1.06 ^1.07 ^1.08 ^1.09 ^1.10 ^1.11 ^1.12 ^1.13 ^1.14 ^1.15 ^1.16 ^1.17 Liu W et al. (2006) Axin is a scaffold protein in TGF-beta signaling that promotes degradation of Smad7 by Arkadia. EMBO J 25: 1646-58 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 Chia IV et al. (2009) Both the RGS domain and the six C-terminal amino acids of mouse Axin are required for normal embryogenesis. Genetics 181: 1359-68 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 Ciani L et al. (2004) A divergent canonical WNT-signaling pathway regulates microtubule dynamics: dishevelled signals locally to stabilize microtubules. J Cell Biol 164: 243-53 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 Fagotto F et al. (1999) Domains of axin involved in protein-protein interactions, Wnt pathway inhibition, and intracellular localization. J Cell Biol 145: 741-56 PubMed GONUTS page
↑ Itoh K et al. (2000) Interaction of dishevelled and Xenopus axin-related protein is required for wnt signal transduction. Mol Cell Biol 20: 2228-38 PubMed GONUTS page
↑ ^6.0 ^6.1 Hocevar BA et al. (2003) Regulation of the Wnt signaling pathway by disabled-2 (Dab2). EMBO J 22: 3084-94 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 Luo W et al. (2003) Axin utilizes distinct regions for competitive MEKK1 and MEKK4 binding and JNK activation. J Biol Chem 278: 37451-8 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 ^8.4 ^8.5 ^8.6 Luo W et al. (2005) Axin contains three separable domains that confer intramolecular, homodimeric, and heterodimeric interactions involved in distinct functions. J Biol Chem 280: 5054-60 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 ^9.3 ^9.4 ^9.5 ^9.6 ^9.7 Rui Y et al. (2007) A beta-catenin-independent dorsalization pathway activated by Axin/JNK signaling and antagonized by aida. Dev Cell 13: 268-82 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 Kim MJ et al. (2008) SUMOylation target sites at the C terminus protect Axin from ubiquitination and confer protein stability. FASEB J 22: 3785-94 PubMed GONUTS page
↑ ^11.0 ^11.1 Haÿ E et al. (2009) N-cadherin interacts with axin and LRP5 to negatively regulate Wnt/beta-catenin signaling, osteoblast function, and bone formation. Mol Cell Biol 29: 953-64 PubMed GONUTS page
↑ Huang SM et al. (2009) Tankyrase inhibition stabilizes axin and antagonizes Wnt signalling. Nature 461: 614-20 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 Hsu W et al. (1999) Identification of a domain of Axin that binds to the serine/threonine protein phosphatase 2A and a self-binding domain. J Biol Chem 274: 3439-45 PubMed GONUTS page
↑ Wu X et al. (2006) Cdc42 controls progenitor cell differentiation and beta-catenin turnover in skin. Genes Dev 20: 571-85 PubMed GONUTS page
↑ ^15.0 ^15.1 ^15.2 ^15.3 Hino S et al. (2001) Inhibition of the Wnt signaling pathway by Idax, a novel Dvl-binding protein. Mol Cell Biol 21: 330-42 PubMed GONUTS page
↑ Chen HJ et al. (2006) The role of microtubule actin cross-linking factor 1 (MACF1) in the Wnt signaling pathway. Genes Dev 20: 1933-45 PubMed GONUTS page
↑ ^17.0 ^17.1 Cong F & Varmus H (2004) Nuclear-cytoplasmic shuttling of Axin regulates subcellular localization of beta-catenin. Proc Natl Acad Sci U S A 101: 2882-7 PubMed GONUTS page
↑ Dunn LC & Caspari E (1945) A Case of Neighboring Loci with Similar Effects. Genetics 30: 543-68 PubMed GONUTS page
↑ ^19.0 ^19.1 ^19.2 ^19.3 ^19.4 ^19.5 Sakanaka C & Williams LT (1999) Functional domains of axin. Importance of the C terminus as an oligomerization domain. J Biol Chem 274: 14090-3 PubMed GONUTS page
↑ ^20.0 ^20.1 Jho E et al. (1999) A GSK3beta phosphorylation site in axin modulates interaction with beta-catenin and Tcf-mediated gene expression. Biochem Biophys Res Commun 266: 28-35 PubMed GONUTS page
↑ ^21.0 ^21.1 Lu Z et al. (2008) 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. J Biol Chem 283: 13132-9 PubMed GONUTS page
↑ ^22.0 ^22.1 Reya T et al. (2003) A role for Wnt signalling in self-renewal of haematopoietic stem cells. Nature 423: 409-14 PubMed GONUTS page
↑ ^23.0 ^23.1 ^23.2 Zeng L et al. (1997) The mouse Fused locus encodes Axin, an inhibitor of the Wnt signaling pathway that regulates embryonic axis formation. Cell 90: 181-92 PubMed GONUTS page
↑ ^24.0 ^24.1 Rakyan VK et al. (2003) Transgenerational inheritance of epigenetic states at the murine Axin(Fu) allele occurs after maternal and paternal transmission. Proc Natl Acad Sci U S A 100: 2538-43 PubMed GONUTS page
↑ Grujic M et al. (2008) Delayed contraction of the CD8+ T cell response toward lymphocytic choriomeningitis virus infection in mice lacking serglycin. J Immunol 181: 1043-51 PubMed GONUTS page
↑ ^26.0 ^26.1 Ross SE et al. (2000) Inhibition of adipogenesis by Wnt signaling. Science 289: 950-3 PubMed GONUTS page
↑ Rui Y et al. (2004) Axin stimulates p53 functions by activation of HIPK2 kinase through multimeric complex formation. EMBO J 23: 4583-94 PubMed GONUTS page

[PMID:16601693-0] 1.00 ^1.01 ^1.02 ^1.03 ^1.04 ^1.05 ^1.06 ^1.07 ^1.08 ^1.09 ^1.10 ^1.11 ^1.12 ^1.13 ^1.14 ^1.15 ^1.16 ^1.17 Liu W et al. (2006) Axin is a scaffold protein in TGF-beta signaling that promotes degradation of Smad7 by Arkadia. EMBO J 25: 1646-58 PubMed GONUTS page

[PMID:19204372-1] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 Chia IV et al. (2009) Both the RGS domain and the six C-terminal amino acids of mouse Axin are required for normal embryogenesis. Genetics 181: 1359-68 PubMed GONUTS page

[PMID:14734535-2] 3.0 ^3.1 ^3.2 Ciani L et al. (2004) A divergent canonical WNT-signaling pathway regulates microtubule dynamics: dishevelled signals locally to stabilize microtubules. J Cell Biol 164: 243-53 PubMed GONUTS page

[PMID:10330403-3] 4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 Fagotto F et al. (1999) Domains of axin involved in protein-protein interactions, Wnt pathway inhibition, and intracellular localization. J Cell Biol 145: 741-56 PubMed GONUTS page

[PMID:10688669-4] Itoh K et al. (2000) Interaction of dishevelled and Xenopus axin-related protein is required for wnt signal transduction. Mol Cell Biol 20: 2228-38 PubMed GONUTS page

[PMID:12805222-5] 6.0 ^6.1 Hocevar BA et al. (2003) Regulation of the Wnt signaling pathway by disabled-2 (Dab2). EMBO J 22: 3084-94 PubMed GONUTS page

[PMID:12878610-6] 7.0 ^7.1 ^7.2 Luo W et al. (2003) Axin utilizes distinct regions for competitive MEKK1 and MEKK4 binding and JNK activation. J Biol Chem 278: 37451-8 PubMed GONUTS page

[PMID:15579909-7] 8.0 ^8.1 ^8.2 ^8.3 ^8.4 ^8.5 ^8.6 Luo W et al. (2005) Axin contains three separable domains that confer intramolecular, homodimeric, and heterodimeric interactions involved in distinct functions. J Biol Chem 280: 5054-60 PubMed GONUTS page

[PMID:17681137-8] 9.0 ^9.1 ^9.2 ^9.3 ^9.4 ^9.5 ^9.6 ^9.7 Rui Y et al. (2007) A beta-catenin-independent dorsalization pathway activated by Axin/JNK signaling and antagonized by aida. Dev Cell 13: 268-82 PubMed GONUTS page

[PMID:18632848-9] 10.0 ^10.1 ^10.2 ^10.3 Kim MJ et al. (2008) SUMOylation target sites at the C terminus protect Axin from ubiquitination and confer protein stability. FASEB J 22: 3785-94 PubMed GONUTS page

[PMID:19075000-10] 11.0 ^11.1 Haÿ E et al. (2009) N-cadherin interacts with axin and LRP5 to negatively regulate Wnt/beta-catenin signaling, osteoblast function, and bone formation. Mol Cell Biol 29: 953-64 PubMed GONUTS page

[PMID:19759537-11] Huang SM et al. (2009) Tankyrase inhibition stabilizes axin and antagonizes Wnt signalling. Nature 461: 614-20 PubMed GONUTS page

[PMID:9920888-12] 13.0 ^13.1 ^13.2 Hsu W et al. (1999) Identification of a domain of Axin that binds to the serine/threonine protein phosphatase 2A and a self-binding domain. J Biol Chem 274: 3439-45 PubMed GONUTS page

[PMID:16510873-13] Wu X et al. (2006) Cdc42 controls progenitor cell differentiation and beta-catenin turnover in skin. Genes Dev 20: 571-85 PubMed GONUTS page

[PMID:11113207-14] 15.0 ^15.1 ^15.2 ^15.3 Hino S et al. (2001) Inhibition of the Wnt signaling pathway by Idax, a novel Dvl-binding protein. Mol Cell Biol 21: 330-42 PubMed GONUTS page

[PMID:16815997-15] Chen HJ et al. (2006) The role of microtubule actin cross-linking factor 1 (MACF1) in the Wnt signaling pathway. Genes Dev 20: 1933-45 PubMed GONUTS page

[PMID:14981260-16] 17.0 ^17.1 Cong F & Varmus H (2004) Nuclear-cytoplasmic shuttling of Axin regulates subcellular localization of beta-catenin. Proc Natl Acad Sci U S A 101: 2882-7 PubMed GONUTS page

[PMID:17247179-17] Dunn LC & Caspari E (1945) A Case of Neighboring Loci with Similar Effects. Genetics 30: 543-68 PubMed GONUTS page

[PMID:10318824-18] 19.0 ^19.1 ^19.2 ^19.3 ^19.4 ^19.5 Sakanaka C & Williams LT (1999) Functional domains of axin. Importance of the C terminus as an oligomerization domain. J Biol Chem 274: 14090-3 PubMed GONUTS page

[PMID:10581160-19] 20.0 ^20.1 Jho E et al. (1999) A GSK3beta phosphorylation site in axin modulates interaction with beta-catenin and Tcf-mediated gene expression. Biochem Biophys Res Commun 266: 28-35 PubMed GONUTS page

[PMID:18316368-20] 21.0 ^21.1 Lu Z et al. (2008) 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. J Biol Chem 283: 13132-9 PubMed GONUTS page

[PMID:12717450-21] 22.0 ^22.1 Reya T et al. (2003) A role for Wnt signalling in self-renewal of haematopoietic stem cells. Nature 423: 409-14 PubMed GONUTS page

[PMID:9230313-22] 23.0 ^23.1 ^23.2 Zeng L et al. (1997) The mouse Fused locus encodes Axin, an inhibitor of the Wnt signaling pathway that regulates embryonic axis formation. Cell 90: 181-92 PubMed GONUTS page

[PMID:12601169-23] 24.0 ^24.1 Rakyan VK et al. (2003) Transgenerational inheritance of epigenetic states at the murine Axin(Fu) allele occurs after maternal and paternal transmission. Proc Natl Acad Sci U S A 100: 2538-43 PubMed GONUTS page

[PMID:18606656-24] Grujic M et al. (2008) Delayed contraction of the CD8+ T cell response toward lymphocytic choriomeningitis virus infection in mice lacking serglycin. J Immunol 181: 1043-51 PubMed GONUTS page

[PMID:10937998-25] 26.0 ^26.1 Ross SE et al. (2000) Inhibition of adipogenesis by Wnt signaling. Science 289: 950-3 PubMed GONUTS page

[PMID:15526030-26] Rui Y et al. (2004) Axin stimulates p53 functions by activation of HIPK2 kinase through multimeric complex formation. EMBO J 23: 4583-94 PubMed GONUTS page

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