O35625 (AXIN1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Axin-1

Alternative name(s):
Axis inhibition protein 1
Protein Fused

Gene names

Name:	Axin1
Synonyms:	Axin, Fu

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	863 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the beta-catenin destruction complex required for regulating CTNNB1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling By similarity. Controls dorsoventral patterning via two opposing effects; down-regulates CTNNB1 to inhibit the Wnt signaling pathway and ventralize embryos, but also dorsalizes embryos by activating a Wnt-independent JNK signaling pathway. In Wnt signaling, probably facilitates the phosphorylation of CTNNB1 and APC by GSK3B. Likely to function as a tumor suppressor. Facilitates the phosphorylation of TP53 by HIPK2 upon ultraviolet irradiation. Enhances TGF-beta signaling by recruiting the RNF111 E3 ubiquitin ligase and promoting the degradation of inhibitory SMAD7 By similarity. Also component of the AXIN1-HIPK2-TP53 complex which controls cell growth, apoptosis and development. Ref.5 Ref.7 Ref.10
Subunit structure	Homodimer. Component of the beta-catenin destruction complex, containing at least CTNNB1, an axin and GSK3B, that regulates CTNNB1 protein levels through phosphorylation and ubiquitination By similarity. Interacts with GSK3B; the interaction hyperphosphorylates CTNNB1 leading to its ubiquitination and destruction. Interacts with DAXX; the interaction stimulates the interaction of DAXX with TP53, stimulates 'Ser-46' phosphorylation of TP53 and induces cell death on UV irradiation. Also interacts with APC, RNF111, SMAD6 and SMAD7. Interacts (via the C-terminal) with PPP1CA; the interaction dephosphorylates AXIN1 and regulates interaction with GSK3B. Interacts with PPP2CA; the interaction dephosphorylates AXIN1. Interacts with MDFI; the interaction decreases AXIN1-mediated JUN N-terminal kinase (JNK) activation. Interacts with MDFIC; the interaction inhibits beta-cateninin-mediated signaling and AXIN1-mediated JUN N-terminal kinase (JNK) activation By similarity. Binds ANKRD6, PIAS1, PIAS2, PIAS4, SUMO1, MAP3K1 and MAP3K4. Component of the AXIN1-HIPK2-TP53 complex. Interacts directly in the complex with TP53 and HIPK2. Interacts with DIXDC1; the interaction prevents interaction with MAP3K1. Interacts with AIDA; the interaction blocks the AXIN1-mediated JNK activation through disrupting AXIN1 homodimerization and Wnt signaling. Interacts with LRP5 (via its phosphorylated PPPSP motifs); the interaction is stimulated by WNT1 and GSK3B and activates beta-catenin signaling. Interacts with CTNNB1 (via the armadillo repeats 2-7). Interacts with MACF1 By similarity. Found in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B By similarity. Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.10
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Cell membrane. Note: On UV irradiation, translocates to the nucleus and colocalizes with DAAX By similarity. MACF1 is required for its translocation to cell membrane. Ref.9
Tissue specificity	Expressed in embryonic stem cells.
Developmental stage	Widely expressed at E10.5 to E16.5 day.
Domain	The tankyrase-binding motif (also named TBD) is required for interaction with tankyrase TNKS and TNKS2 By similarity.
Post-translational modification	Phosphorylation and dephosphorylation of AXIN1 regulates assembly and function of the beta-catenin complex. Phosphorylated by CK1 and GSK3B. Dephosphorylated by PPP1CA and PPP2CA. Phosphorylation by CK1 enhances binding of GSK3B to AXIN1 By similarity. Also phosphorylated by CDK2 which regulates interaction with CTNBB1. Ref.2 Ref.6 Ref.12 ADP-ribosylated by tankyrase TNKS and TNKS2. Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination and subsequent activation of the Wnt signaling pathway By similarity. Ubiquitinated by RNF146 when poly-ADP-ribosylated, leading to its degradation and subsequent activation of the Wnt signaling pathway. Deubiquitinated by USP34, deubiquitinated downstream of beta-catenin stabilization step: deubiquitination is important for nuclear accumulation during Wnt signaling to positively regulate beta-catenin (CTNBB1)-mediated transcription By similarity. Sumoylation at Lys-858 and Lys-861 prevents ubiquitination and degradation. Sumoylation is required for AXIN1-mediated JNK activation.
Sequence similarities	Contains 1 DIX domain. Contains 1 RGS domain.
Sequence caution	The sequence AAC53285.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Apoptosis Wnt signaling pathway
Cellular component	Cell membrane Cytoplasm Membrane Nucleus
Coding sequence diversity	Alternative splicing
Disease	Tumor suppressor
Molecular function	Developmental protein
PTM	ADP-ribosylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	Wnt receptor signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW Wnt receptor signaling pathway involved in forebrain neuron fate commitment Inferred from Biological aspect of Ancestor. Source: RefGenome Wnt receptor signaling pathway involved in somitogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome activation of JUN kinase activity Inferred from Biological aspect of Ancestor. Source: RefGenome apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW axial mesoderm formation Inferred from mutant phenotype Ref.1. Source: MGI canonical Wnt receptor signaling pathway involved in neural plate anterior/posterior pattern formation Inferred from Biological aspect of Ancestor. Source: RefGenome cell death Inferred from Biological aspect of Ancestor. Source: RefGenome cellular response to organic cyclic compound Inferred from Biological aspect of Ancestor. Source: RefGenome cytoplasmic microtubule organization Inferred from genetic interaction. Source: MGI determination of left/right symmetry Inferred from Biological aspect of Ancestor. Source: RefGenome dorsal/ventral axis specification Inferred from direct assay. Source: MGI embryonic eye morphogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome forebrain anterior/posterior pattern specification Inferred from Biological aspect of Ancestor. Source: RefGenome genetic imprinting Inferred from mutant phenotype. Source: MGI in utero embryonic development Inferred from mutant phenotype. Source: MGI multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW muscle cell development Inferred from Biological aspect of Ancestor. Source: RefGenome negative regulation of canonical Wnt receptor signaling pathway Inferred from direct assay. Source: MGI negative regulation of fat cell differentiation Inferred from direct assay. Source: MGI negative regulation of protein metabolic process Inferred from direct assay. Source: MGI negative regulation of transcription elongation from RNA polymerase II promoter Inferred from direct assay. Source: MGI nucleocytoplasmic transport Inferred from direct assay. Source: MGI olfactory placode formation Inferred from Biological aspect of Ancestor. Source: RefGenome optic placode formation Inferred from Biological aspect of Ancestor. Source: RefGenome positive regulation of JNK cascade Inferred from mutant phenotype Ref.10. Source: UniProtKB positive regulation of proteasomal ubiquitin-dependent protein catabolic process Inferred from direct assay. Source: MGI positive regulation of protein phosphorylation Inferred from direct assay. Source: MGI positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Inferred from direct assay. Source: MGI positive regulation of transcription, DNA-dependent Inferred from direct assay. Source: BHF-UCL positive regulation of transforming growth factor beta receptor signaling pathway Inferred from direct assay. Source: MGI positive regulation of ubiquitin-protein ligase activity Inferred from mutant phenotype. Source: BHF-UCL protein catabolic process Inferred from direct assay. Source: MGI protein homooligomerization Inferred from direct assay. Source: MGI protein polyubiquitination Inferred from direct assay. Source: MGI regulation of catenin import into nucleus Inferred from direct assay. Source: MGI sensory perception of sound Inferred from mutant phenotype. Source: MGI tail morphogenesis Inferred from mutant phenotype. Source: MGI
Cellular component	Axin-APC-beta-catenin-GSK3B complex Inferred from direct assay. Source: MGI cell cortex Inferred from direct assay. Source: MGI cytoplasmic membrane-bounded vesicle Inferred from direct assay. Source: MGI cytoplasmic microtubule Inferred from direct assay. Source: MGI nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay Ref.9. Source: UniProtKB plasma membrane part Inferred from direct assay. Source: MGI postsynaptic density Inferred from Biological aspect of Ancestor. Source: RefGenome soluble fraction Inferred from direct assay. Source: MGI
Molecular function	GTPase activator activity Inferred from Biological aspect of Ancestor. Source: RefGenome I-SMAD binding Inferred from direct assay. Source: BHF-UCL R-SMAD binding Inferred from physical interaction. Source: MGI armadillo repeat domain binding Inferred from Biological aspect of Ancestor. Source: RefGenome beta-catenin binding Inferred from physical interaction Ref.11. Source: MGI protein C-terminus binding Inferred from direct assay. Source: MGI protein complex scaffold Inferred from mutant phenotype. Source: BHF-UCL protein domain specific binding Inferred from physical interaction Ref.10. Source: MGI protein homodimerization activity Inferred from physical interaction Ref.10. Source: UniProtKB protein kinase binding Inferred from physical interaction. Source: MGI protein self-association Inferred from physical interaction. Source: MGI signal transducer activity Inferred from electronic annotation. Source: InterPro ubiquitin protein ligase binding Inferred from physical interaction. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TNKS	O95271	4	EBI-2365912,EBI-1105254	From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O35625-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: O35625-2)

The sequence of this isoform differs from the canonical sequence as follows:
     731-766: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 863	863	Axin-1		PRO_0000220889
Regions
	Domain	88 – 211	124	RGS
	Domain	781 – 863	83	DIX
	Region	209 – 338	130	Interaction with TP53
	Region	348 – 432	85	Interaction with GSK3B By similarity
	Region	433 – 501	69	Interaction with beta-catenin By similarity
	Region	505 – 758	254	Interaction with RNF111 By similarity
	Region	572 – 790	219	Interaction with PPP2CA By similarity
	Region	678 – 753	76	Interaction with HIPK2
	Motif	20 – 29	10	Tankyrase-binding motif
Amino acid modifications
	Modified residue	75	1	Phosphoserine; by CK1 By similarity
	Modified residue	77	1	Phosphoserine; by CK1 By similarity
	Modified residue	217	1	Phosphoserine; by CK1 By similarity
	Modified residue	468	1	Phosphoserine; by CK1 By similarity
	Modified residue	480	1	Phosphothreonine; by GSK3-beta Probable
	Modified residue	485	1	Phosphoserine; by GSK3-beta Ref.2
	Modified residue	492	1	Phosphoserine Ref.2 Ref.12
	Cross-link	858		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.5 Ref.11
	Cross-link	861		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.5 Ref.11
Natural variations
	Alternative sequence	731 – 766	36	Missing in isoform 2.		VSP_000452
Experimental info
	Mutagenesis	480	1	T → A: Greatly reduced GSK3B-mediated phosphorylation; when associated with A-485 and A-492. Ref.2
	Mutagenesis	485	1	S → A: Greatly reduced GSK3B-mediated phosphorylation and large effect on the inhibitory activity in Wnt-signaling; when associated with A-480 and A-492. Ref.2
	Mutagenesis	492	1	S → A: Greatly reduced GSK3B-mediated phosphorylation; when associated with A-480 and A-485. Ref.2
	Mutagenesis	492	1	S → I: Little effect on inhibitory activity on Wnt-signaling. Ref.2
	Mutagenesis	495	1	S → A: No effect on phosphorylation. Little effect on inhibitory activity on Wnt-signaling. Ref.2
	Mutagenesis	858 – 863	6	Missing: Abolishes binding of PIAS1 and PIAS2. Dramatically reduces sumoylation and abolishes AXIN1-mediated JNK activation. No effect on homodimerization nor on Wnt-signaling. Ref.5 Ref.11
	Mutagenesis	858	1	K → A: Decreased sumoylation followed by increased ubiquitination; when associated with A-861. Ref.11
	Mutagenesis	861	1	K → A: Decreased sumoylation followed by increased ubiquitination; when associated with A-858. Ref.11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 10, 2002. Version 2. Checksum: AD419D685411E9FB	FASTA	863	96,314
	10 20 30 40 50 60 MNVQEQGFPL DLGASFTEDA PRPPVPGEEG ELVSTDSRPV NHSFCSGKGT SIKSETSTAT 70 80 90 100 110 120 PRRSDLDLGY EPEGSASPTP PYLRWAESLH SLLDDQDGIS LFRTFLKQEG CADLLDFWFA 130 140 150 160 170 180 CSGFRKLEPC DSNEEKRLKL ARAIYRKYIL DSNGIVSRQT KPATKSFIKD CVMKQQIDPA 190 200 210 220 230 240 MFDQAQTEIQ STMEENTYPS FLKSDIYLEY TRTGSESPKV CSDQSSGSGT GKGMSGYLPT 250 260 270 280 290 300 LNEDEEWKCD QDADEDDGRD PLPPSRLTQK LLLETAAPRA PSSRRYNEGR ELRYGSWREP 310 320 330 340 350 360 VNPYYVNSGY ALAPATSAND SEQQSLSSDA DTLSLTDSSV DGIPPYRIRK QHRREMQESI 370 380 390 400 410 420 QVNGRVPLPH IPRTYRMPKE IRVEPQKFAE ELIHRLEAVQ RTREAEEKLE ERLKRVRMEE 430 440 450 460 470 480 EGEDGEMPSG PMASHKLPSV PAWHHFPPRY VDMGCSGLRD AHEENPESIL DEHVQRVMRT 490 500 510 520 530 540 PGCQSPGPGH RSPDSGHVAK TAVLGGTASG HGKHVPKLGL KLDTAGLHHH RHVHHHVHHN 550 560 570 580 590 600 SARPKEQMEA EVARRVQSSF SWGPETHGHA KPRSYSENAG TTLSAGDLPF GGKTSAPSKR 610 620 630 640 650 660 NTKKAESGKN ANAEVPSTTE DAEKNQKIMQ WIIEGEKEIS RHRKAGHGSS GLRKQQAHES 670 680 690 700 710 720 SRPLSIERPG AVHPWVSAQL RNSVQPSHLF IQDPTMPPNP APNPLTQLEE ARRRLEEEEK 730 740 750 760 770 780 RANKLPSKQR YVQAVMQRGR TCVRPACAPV LSVVPAVSDL ELSETETKSQ RKAGGGSAPP 790 800 810 820 830 840 CDSIVVGYYF CGEPIPYRTL VRGRAVTLGQ FKELLTKKGS YRYYFKKVSD EFDCGVVFEE 850 860 VREDEPVLPV FEEKIIGKVE KVD
	Isoform 2 [UniParc]. Checksum: 091354285F9EAF9E	FASTA	827	92,456
	10 20 30 40 50 60 MNVQEQGFPL DLGASFTEDA PRPPVPGEEG ELVSTDSRPV NHSFCSGKGT SIKSETSTAT 70 80 90 100 110 120 PRRSDLDLGY EPEGSASPTP PYLRWAESLH SLLDDQDGIS LFRTFLKQEG CADLLDFWFA 130 140 150 160 170 180 CSGFRKLEPC DSNEEKRLKL ARAIYRKYIL DSNGIVSRQT KPATKSFIKD CVMKQQIDPA 190 200 210 220 230 240 MFDQAQTEIQ STMEENTYPS FLKSDIYLEY TRTGSESPKV CSDQSSGSGT GKGMSGYLPT 250 260 270 280 290 300 LNEDEEWKCD QDADEDDGRD PLPPSRLTQK LLLETAAPRA PSSRRYNEGR ELRYGSWREP 310 320 330 340 350 360 VNPYYVNSGY ALAPATSAND SEQQSLSSDA DTLSLTDSSV DGIPPYRIRK QHRREMQESI 370 380 390 400 410 420 QVNGRVPLPH IPRTYRMPKE IRVEPQKFAE ELIHRLEAVQ RTREAEEKLE ERLKRVRMEE 430 440 450 460 470 480 EGEDGEMPSG PMASHKLPSV PAWHHFPPRY VDMGCSGLRD AHEENPESIL DEHVQRVMRT 490 500 510 520 530 540 PGCQSPGPGH RSPDSGHVAK TAVLGGTASG HGKHVPKLGL KLDTAGLHHH RHVHHHVHHN 550 560 570 580 590 600 SARPKEQMEA EVARRVQSSF SWGPETHGHA KPRSYSENAG TTLSAGDLPF GGKTSAPSKR 610 620 630 640 650 660 NTKKAESGKN ANAEVPSTTE DAEKNQKIMQ WIIEGEKEIS RHRKAGHGSS GLRKQQAHES 670 680 690 700 710 720 SRPLSIERPG AVHPWVSAQL RNSVQPSHLF IQDPTMPPNP APNPLTQLEE ARRRLEEEEK 730 740 750 760 770 780 RANKLPSKQR TKSQRKAGGG SAPPCDSIVV GYYFCGEPIP YRTLVRGRAV TLGQFKELLT 790 800 810 820 KKGSYRYYFK KVSDEFDCGV VFEEVREDEP VLPVFEEKII GKVEKVD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 9230313] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[2]	"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: 10581160] [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.
[3]	"Low-density lipoprotein receptor-related protein-5 binds to Axin and regulates the canonical Wnt signaling pathway." Mao J., Wang J., Liu B., Pan W., Farr G.H. III, Flynn C., Yuan H., Takada S., Kimelman D., Li L., Wu D. Mol. Cell 7:801-809(2001) [PubMed: 11336703] [Abstract] Cited for: INTERACTION WITH LRP5.
[4]	"The ankyrin repeat protein diversin recruits casein kinase Iepsilon to the beta-catenin degradation complex and acts in both canonical Wnt and Wnt/JNK signaling." Schwarz-Romond T., Asbrand C., Bakkers J., Kuehl M., Schaeffer H.J., Huelsken J., Behrens J., Hammerschmidt M., Birchmeier W. Genes Dev. 16:2073-2084(2002) [PubMed: 12183362] [Abstract] Cited for: INTERACTION WITH ANKRD6.
[5]	"SUMO-1 modification of the C-terminal KVEKVD of Axin is required for JNK activation but has no effect on Wnt signaling." Rui H.L., Fan E., Zhou H.M., Xu Z., Zhang Y., Lin S.C. J. Biol. Chem. 277:42981-42986(2002) [PubMed: 12223491] [Abstract] Cited for: SUMOYLATION AT LYS-858 AND LYS-861, INTERACTION WITH MAP3K1; SUMO1; PIAS1; PIAS2 AND PIAS4, FUNCTION, HOMODIMERIZATION, MUTAGENESIS OF 858-LYS--ASP-863.
[6]	"Cyclin-dependent kinase 2 regulates the interaction of Axin with beta-catenin." Kim S.I., Park C.S., Lee M.S., Kwon M.S., Jho E.H., Song W.K. Biochem. Biophys. Res. Commun. 317:478-483(2004) [PubMed: 15063782] [Abstract] Cited for: PHOSPHORYLATION, INTERACTION WITH CTNNB1.
[7]	"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: 15526030] [Abstract] Cited for: FUNCTION, INTERACTION WITH TP53 AND HIPK2, IDENTIFICATION IN A COMPLEX WITH TP53 AND HIPK2.
[8]	"The DIX domain protein coiled-coil-DIX1 inhibits c-Jun N-terminal kinase activation by Axin and dishevelled through distinct mechanisms." Wong C.K., Luo W., Deng Y., Zou H., Ye Z., Lin S.-C. J. Biol. Chem. 279:39366-39373(2004) [PubMed: 15262978] [Abstract] Cited for: INTERACTION WITH DIXDC1; MAP3K1 AND MAP3K4.
[9]	"The role of microtubule actin cross-linking factor 1 (MACF1) in the Wnt signaling pathway." Chen H.J., Lin C.M., Lin C.S., Perez-Olle R., Leung C.L., Liem R.K. Genes Dev. 20:1933-1945(2006) [PubMed: 16815997] [Abstract] Cited for: SUBCELLULAR LOCATION.
[10]	"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: 17681137] [Abstract] Cited for: FUNCTION, HOMODIMERIZATION, INTERACTION WITH AIDA.
[11]	"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: 18632848] [Abstract] Cited for: SUMOYLATION AT LYS-858 AND LYS-861, MUTAGENESIS OF LYS-858 AND LYS-861.
[12]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 19367708] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492, MASS SPECTROMETRY. Tissue: Melanoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF009011 mRNA. Translation: AAC53285.1. Different initiation.
IPI	IPI00875849. IPI00974688.
RefSeq	NP_033863.2. NM_009733.2.
UniGene	Mm.23684.
3D structure databases
ProteinModelPortal	O35625.
SMR	O35625. Positions 74-220, 780-863.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-42637N.
IntAct	O35625. 4 interactions.
MINT	MINT-1543084.
STRING	O35625.
PTM databases
PhosphoSite	O35625.
Proteomic databases
PRIDE	O35625.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	12005.
KEGG	mmu:12005.
UCSC	uc008bdm.2. mouse.
Organism-specific databases
CTD	8312.
MGI	MGI:1096327. Axin1.
Phylogenomic databases
eggNOG	roNOG11401.
HOGENOM	HBG714290.
HOVERGEN	HBG004324.
InParanoid	O35625.
OrthoDB	EOG47SSDB.
Gene expression databases
ArrayExpress	O35625.
Bgee	O35625.
CleanEx	MM_AXIN1.
Genevestigator	O35625.
GermOnline	ENSMUSG00000024182. Mus musculus.
Family and domain databases
InterPro	IPR014936. Axin_b-cat-bd. IPR001158. DIX. IPR000342. Regulat_G_prot_signal. IPR024066. Regulat_G_prot_signal_dom1. IPR016137. Regulat_G_prot_signal_superfam. [Graphical view]
Gene3D	G3DSA:1.10.196.10. G3DSA:1.10.196.10. 2 hits.
KO	K02157.
Pfam	PF08833. Axin_b-cat_bind. 1 hit. PF00778. DIX. 1 hit. PF00615. RGS. 1 hit. [Graphical view]
PRINTS	PR01301. RGSPROTEIN.
SMART	SM00021. DAX. 1 hit. SM00315. RGS. 1 hit. [Graphical view]
SUPFAM	SSF48097. Regulat_G_prot_signal_superfam. 1 hit.
PROSITE	PS50841. DIX. 1 hit. PS50132. RGS. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	280195.
SOURCE	Search...

Entry information

Entry name

AXIN1_MOUSE

Accession

Primary (citable) accession number: O35625

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 10, 2002
Last modified:	December 14, 2011
This is version 116 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program