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O88566 (AXIN2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Axin-2
Alternative name(s):
Axin-like protein
Short name=Axil
Axis inhibition protein 2
Conductin
Gene names
Name:Axin2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length840 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inhibitor of the Wnt signaling pathway. Down-regulates beta-catenin. Probably facilitate the phosphorylation of beta-catenin and APC by GSK3B By similarity.

Subunit structure

Interacts with glycogen synthase kinase-3 beta (GSK3B) and beta-catenin. The interaction between axin and beta-catenin occurs via the armadillo repeats contained in beta-catenin. Interacts with SMAD7 and RNF111 By similarity. Interacts with ANKRD6. Ref.6

Subcellular location

Cytoplasm By similarity.

Domain

The tankyrase-binding motif (also named TBD) is required for interaction with tankyrase TNKS and TNKS2 By similarity.

Post-translational modification

Probably phosphorylated by GSK3B and dephosphorylated by PP2A By similarity.

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 Wnt signaling to positively regulate beta-catenin (CTNBB1)-mediated transcription By similarity.

Sequence similarities

Contains 1 DIX domain.

Contains 1 RGS domain.

Ontologies

Keywords
   Biological processWnt signaling pathway
   Cellular componentCytoplasm
   DiseaseTumor suppressor
   PTMADP-ribosylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway involved in somitogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

bone mineralization

Inferred from mutant phenotype PubMed 19623616. Source: MGI

cell death

Inferred from Biological aspect of Ancestor. Source: RefGenome

cell proliferation

Inferred from mutant phenotype PubMed 20569694. Source: MGI

cellular protein localization

Inferred from electronic annotation. Source: Ensembl

cellular response to organic cyclic compound

Inferred from Biological aspect of Ancestor. Source: RefGenome

chondrocyte differentiation involved in endochondral bone morphogenesis

Inferred from mutant phenotype PubMed 19623616. Source: MGI

dorsal/ventral axis specification

Inferred from Biological aspect of Ancestor. Source: RefGenome

intramembranous ossification

Inferred from mutant phenotype PubMed 15790973. Source: MGI

mRNA stabilization

Inferred from electronic annotation. Source: Ensembl

maintenance of DNA repeat elements

Inferred from electronic annotation. Source: Ensembl

negative regulation of canonical Wnt signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of catenin import into nucleus

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from mutant phenotype PubMed 15790973. Source: MGI

negative regulation of osteoblast differentiation

Inferred from mutant phenotype PubMed 15790973. Source: MGI

odontogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of GTPase activity

Inferred from Biological aspect of Ancestor. Source: GOC

positive regulation of cell death

Inferred from electronic annotation. Source: Ensembl

positive regulation of epithelial to mesenchymal transition

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

regulation of Wnt signaling pathway

Inferred from direct assay Ref.1. Source: MGI

regulation of catenin import into nucleus

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of centromeric sister chromatid cohesion

Inferred from mutant phenotype PubMed 20300119. Source: BHF-UCL

regulation of chondrocyte development

Inferred from mutant phenotype PubMed 19623616. Source: MGI

regulation of mismatch repair

Inferred from electronic annotation. Source: Ensembl

regulation of transcription, DNA-templated

Inferred from Biological aspect of Ancestor. Source: RefGenome

secondary heart field specification

Inferred from genetic interaction PubMed 22711842. Source: MGI

somitogenesis

Inferred from direct assay PubMed 12636920. Source: MGI

termination of G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: InterPro

   Cellular_componentbeta-catenin destruction complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

cell cortex

Inferred from Biological aspect of Ancestor. Source: RefGenome

centrosome

Inferred from direct assay PubMed 20300119. Source: BHF-UCL

cytoplasmic membrane-bounded vesicle

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytoplasmic microtubule

Inferred from Biological aspect of Ancestor. Source: RefGenome

nucleus

Inferred from direct assay PubMed 21991325. Source: MGI

plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

postsynaptic density

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionGTPase activator activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

I-SMAD binding

Inferred from physical interaction PubMed 16601693. Source: MGI

armadillo repeat domain binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

beta-catenin binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein kinase binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

signal transducer activity

Inferred from electronic annotation. Source: InterPro

ubiquitin protein ligase binding

Inferred from physical interaction PubMed 16601693. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

AMER3Q8N9442EBI-7690990,EBI-8869590From a different organism.
CDC20Q128342EBI-7690990,EBI-367462From a different organism.
CEP250Q9BV733EBI-7690990,EBI-1053100From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 840840Axin-2
PRO_0000220896

Regions

Domain81 – 200120RGS
Domain758 – 84083DIX
Region327 – 41387Interaction with GSK3B By similarity
Region413 – 47866Interaction with beta-catenin By similarity
Motif21 – 3010Tankyrase-binding motif
Compositional bias469 – 4768Poly-His

Experimental info

Sequence conflict1011R → K in AAF22800. Ref.2
Sequence conflict4741H → Y in AAF22800. Ref.2
Sequence conflict4841P → S in AAC26047. Ref.1
Sequence conflict5031F → S in AAF22800. Ref.2
Sequence conflict6031A → G in AAC26047. Ref.1
Sequence conflict6481C → R in AAC26047. Ref.1
Sequence conflict6481C → R in AAF22800. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O88566 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 53D7D33128879298

FASTA84092,906
        10         20         30         40         50         60 
MSSAVLVTLL PDPSSSFRED APRPPVPGEE GETPPCQPSV GKVQSTKPMP VSSNARRNED 

        70         80         90        100        110        120 
GLGEPEGRAS PDSPLTRWTK SLHSLLGDQD GAYLFRTFLE REKCVDTLDF WFACNGFRQM 

       130        140        150        160        170        180 
NLKDTKTLRV AKAIYKRYIE NNSVVSKQLK PATKTYIRDG IKKQQIGSVM FDQAQTEIQA 

       190        200        210        220        230        240 
VMEENAYQVF LTSDIYLEYV RSGGENTAYM SNGGLGSLKV LCGYLPTLNE EEEWTCADLK 

       250        260        270        280        290        300 
CKLSPTVVGL SSKTLRATAS VRSTETAENG FRSFKRSDPV NPYHVGSGYV FAPATSANDS 

       310        320        330        340        350        360 
ELSSDALTDD SMSMTDSSVD GVPPYRMGSK KQLQREMHRS VKANGQVSLP HFPRTHRLPK 

       370        380        390        400        410        420 
EMTPVEPAAF AAELISRLEK LKLELESRHS LEERLQQIRE DEEKEGSEQA LSSRDGAPVQ 

       430        440        450        460        470        480 
HPLALLPSGS YEEDPQTILD DHLSRVLKTP GCQSPGVGRY SPRSRSPDHH HQHHHHQQCH 

       490        500        510        520        530        540 
TLLPTGGKLP PVAACPLLGG KSFLTKQTTK HVHHHYIHHH AVPKTKEEIE AEATQRVRCL 

       550        560        570        580        590        600 
CPGGTDYYCY SKCKSHPKAP EPLPGEQFCG SRGGTLPKRN AKGTEPGLAL SARDGGMSSA 

       610        620        630        640        650        660 
AGAPQLPGEE GDRSQDVWQW MLESERQSKS KPHSAQSIRK SYPLESACAA PGERVSRHHL 

       670        680        690        700        710        720 
LGASGHSRSV ARAHPFTQDP AMPPLTPPNT LAQLEEACRR LAEVSKPQKQ RCCVASQQRD 

       730        740        750        760        770        780 
RNHSAAGQAG ASPFANPSLA PEDHKEPKKL ASVHALQASE LVVTYFFCGE EIPYRRMLKA 

       790        800        810        820        830        840 
QSLTLGHFKE QLSKKGNYRY YFKKASDEFA CGAVFEEIWD DETVLPMYEG RILGKVERID 

« Hide

References

« Hide 'large scale' references
[1]"Functional interaction of an axin homolog, conductin, with beta-catenin, APC, and GSK3beta."
Behrens J., Jerchow B.-A., Wuertele M., Grimm J., Asbrand C., Wirtz R., Kuehl M., Wedlich D., Birchmeier W.
Science 280:596-599(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Properties of mouse Axin2 and human AXIN2: chromosomal location, expression pattern, interaction with Axin and effects on embryonic axis formation."
Zhang T., Fagotto F., Hsu W., Zeng L., Gilbert D., Copeland N.G., Jenkins N.A., Warburton D., Costantini F.
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[6]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ANKRD6.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF073788 mRNA. Translation: AAC26047.1.
AF205889 mRNA. Translation: AAF22800.1.
AL662893 Genomic DNA. Translation: CAM17369.1.
CH466558 Genomic DNA. Translation: EDL34346.1.
BC057338 mRNA. Translation: AAH57338.1.
RefSeqNP_056547.3. NM_015732.4.
XP_006532120.1. XM_006532057.1.
XP_006532121.1. XM_006532058.1.
XP_006532122.1. XM_006532059.1.
XP_006532123.1. XM_006532060.1.
UniGeneMm.71710.

3D structure databases

ProteinModelPortalO88566.
SMRO88566. Positions 74-199, 761-840.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198288. 6 interactions.
IntActO88566. 5 interactions.
MINTMINT-1951339.

Chemistry

ChEMBLCHEMBL1255128.

PTM databases

PhosphoSiteO88566.

Proteomic databases

PRIDEO88566.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000052915; ENSMUSP00000051331; ENSMUSG00000000142.
GeneID12006.
KEGGmmu:12006.
UCSCuc007mbu.2. mouse.

Organism-specific databases

CTD8313.
MGIMGI:1270862. Axin2.

Phylogenomic databases

eggNOGNOG238205.
GeneTreeENSGT00390000010011.
HOGENOMHOG000231228.
HOVERGENHBG004324.
InParanoidQ6PFZ9.
KOK04385.
OMAKHVHHHY.
OrthoDBEOG79PJQ0.
TreeFamTF315454.

Gene expression databases

ArrayExpressO88566.
BgeeO88566.
CleanExMM_AXIN2.
GenevestigatorO88566.

Family and domain databases

Gene3D1.10.196.10. 2 hits.
InterProIPR014936. Axin_b-cat-bd.
IPR001158. DIX.
IPR024066. Regulat_G_prot_signal_dom1.
IPR016137. Regulat_G_prot_signal_superfam.
IPR000342. RGS_dom.
[Graphical view]
PfamPF08833. Axin_b-cat_bind. 1 hit.
PF00778. DIX. 1 hit.
PF00615. RGS. 1 hit.
[Graphical view]
PRINTSPR01301. RGSPROTEIN.
SMARTSM00021. DAX. 1 hit.
SM00315. RGS. 1 hit.
[Graphical view]
SUPFAMSSF48097. SSF48097. 1 hit.
PROSITEPS50841. DIX. 1 hit.
PS50132. RGS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio280199.
PROO88566.
SOURCESearch...

Entry information

Entry nameAXIN2_MOUSE
AccessionPrimary (citable) accession number: O88566
Secondary accession number(s): Q6PFZ9, Q9QXJ6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot