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O35625 (AXIN1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Axin-1
Alternative name(s):
Axis inhibition protein 1
Protein Fused
Gene names
Name:Axin1
Synonyms:Axin, Fu
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length863 AA.
Sequence statusComplete.
Protein existenceEvidence 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.6 Ref.8 Ref.11

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. Interacts with TNKS By similarity. Interacts with DAB2; the interaction is mutually exclusive with the AXIN1:PPP1CA interaction. Interacts with ZBED3 (via PPPSP motif); the interaction is direct, enhanced by protein kinase GSK3B and casein kinase CSNK1E activities and decreases GSK3B-induced beta-catenin serine and threonine phosphorylations. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.13 Ref.14

Subcellular location

Cytoplasm. Nucleus By similarity. Cell membrane. 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.10 Ref.13

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.3 Ref.7

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. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processApoptosis
Wnt signaling pathway
   Cellular componentCell membrane
Cytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   DiseaseTumor suppressor
   Molecular functionDevelopmental protein
   PTMADP-ribosylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from direct assay PubMed 11113207. Source: MGI

Wnt signaling pathway involved in somitogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

Wnt-activated signaling pathway involved in forebrain neuron fate commitment

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 development

Inferred from mutant phenotype Ref.1. Source: MGI

axial mesoderm formation

Inferred from mutant phenotype Ref.1. Source: MGI

canonical Wnt signaling pathway

Inferred from direct assay PubMed 10937998. Source: MGI

canonical Wnt 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 protein complex assembly

Inferred from electronic annotation. Source: Ensembl

cellular response to organic cyclic compound

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytoplasmic microtubule organization

Inferred from genetic interaction PubMed 14734535. Source: MGI

determination of left/right symmetry

Inferred from Biological aspect of Ancestor. Source: RefGenome

dorsal/ventral axis specification

Inferred from direct assay PubMed 10330403. Source: MGI

dorsal/ventral pattern formation

Inferred from mutant phenotype PubMed 18316368. 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 PubMed 12601169. Source: MGI

in utero embryonic development

Inferred from mutant phenotype PubMed 19204372. Source: MGI

muscle cell development

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of Wnt signaling pathway

Inferred from direct assay Ref.3PubMed 12717450Ref.11Ref.1. Source: MGI

negative regulation of canonical Wnt signaling pathway

Inferred from direct assay PubMed 15579909PubMed 19204372. Source: MGI

negative regulation of fat cell differentiation

Inferred from direct assay PubMed 10937998. Source: MGI

negative regulation of protein metabolic process

Inferred from direct assay PubMed 10330403. Source: MGI

negative regulation of transcription elongation from RNA polymerase II promoter

Inferred from direct assay PubMed 10318824PubMed 19204372. Source: MGI

nucleocytoplasmic transport

Inferred from direct assay PubMed 14981260. 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 GTPase activity

Inferred from Biological aspect of Ancestor. Source: GOC

positive regulation of JNK cascade

Inferred from mutant phenotype. Source: MGI

positive regulation of JUN kinase activity

Inferred from direct assay PubMed 12878610. Source: MGI

positive regulation of peptidyl-serine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-threonine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from direct assay PubMed 16601693. Source: MGI

positive regulation of protein phosphorylation

Inferred from direct assay PubMed 10330403. Source: MGI

positive regulation of protein ubiquitination

Inferred from direct assay PubMed 16601693. Source: MGI

positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process

Inferred from direct assay PubMed 16601693. Source: MGI

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 16601693. Source: BHF-UCL

positive regulation of transforming growth factor beta receptor signaling pathway

Inferred from direct assay PubMed 16601693. Source: MGI

positive regulation of ubiquitin-protein ligase activity

Inferred from mutant phenotype PubMed 16601693. Source: BHF-UCL

post-anal tail morphogenesis

Inferred from mutant phenotype PubMed 12601169. Source: MGI

protein catabolic process

Inferred from direct assay PubMed 12717450. Source: MGI

protein homooligomerization

Inferred from direct assay PubMed 10318824. Source: MGI

protein polyubiquitination

Inferred from direct assay PubMed 16601693. Source: MGI

regulation of catenin import into nucleus

Inferred from direct assay PubMed 14981260. Source: MGI

regulation of protein phosphorylation

Inferred from genetic interaction PubMed 14734535. Source: MGI

sensory perception of sound

Inferred from mutant phenotype PubMed 17247179. Source: MGI

termination of G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: InterPro

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

beta-catenin destruction complex

Inferred from direct assay PubMed 10318824. Source: MGI

cell cortex

Inferred from direct assay PubMed 10330403. Source: MGI

cytoplasm

Inferred from direct assay PubMed 16601693. Source: BHF-UCL

cytoplasmic membrane-bounded vesicle

Inferred from direct assay PubMed 11113207. Source: MGI

cytoplasmic microtubule

Inferred from direct assay PubMed 14734535. Source: MGI

cytoplasmic vesicle

Inferred from electronic annotation. Source: Ensembl

lateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay Ref.10. Source: UniProtKB

postsynaptic density

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein complex

Inferred from direct assay PubMed 16601693. Source: MGI

   Molecular_functionGTPase activator activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

I-SMAD binding

Inferred from direct assay PubMed 16601693. Source: BHF-UCL

R-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 mutant phenotype Ref.3. Source: MGI

identical protein binding

Inferred from physical interaction PubMed 9920888. Source: MGI

p53 binding

Inferred from physical interaction Ref.8. Source: MGI

protein C-terminus binding

Inferred from direct assay PubMed 10318824. Source: MGI

protein complex scaffold

Inferred from mutant phenotype PubMed 16601693. Source: BHF-UCL

protein domain specific binding

Inferred from physical interaction PubMed 15579909Ref.11. Source: MGI

protein homodimerization activity

Inferred from physical interaction. Source: MGI

protein kinase binding

Inferred from physical interaction PubMed 10318824Ref.8. Source: MGI

protein self-association

Inferred from physical interaction PubMed 15579909. Source: MGI

signal transducer activity

Inferred from electronic annotation. Source: Ensembl

ubiquitin protein ligase binding

Inferred from physical interaction PubMed 16601693. Source: BHF-UCL

Complete GO annotation...

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 863863Axin-1
PRO_0000220889

Regions

Domain88 – 211124RGS
Domain781 – 86383DIX
Region209 – 338130Interaction with TP53
Region348 – 43285Interaction with GSK3B By similarity
Region433 – 50169Interaction with beta-catenin By similarity
Region505 – 758254Interaction with RNF111 By similarity
Region572 – 790219Interaction with PPP2CA By similarity
Region678 – 75376Interaction with HIPK2
Motif20 – 2910Tankyrase-binding motif

Amino acid modifications

Modified residue751Phosphoserine; by CK1 By similarity
Modified residue771Phosphoserine; by CK1 By similarity
Modified residue2171Phosphoserine; by CK1 By similarity
Modified residue4681Phosphoserine; by CK1 By similarity
Modified residue4801Phosphothreonine; by GSK3-beta Probable
Modified residue4851Phosphoserine; by GSK3-beta Ref.3
Modified residue4921Phosphoserine Ref.3
Cross-link858Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.6 Ref.12
Cross-link861Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.6 Ref.12

Natural variations

Alternative sequence731 – 76636Missing in isoform 2.
VSP_000452

Experimental info

Mutagenesis4801T → A: Greatly reduced GSK3B-mediated phosphorylation; when associated with A-485 and A-492. Ref.3
Mutagenesis4851S → 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.3
Mutagenesis4921S → A: Greatly reduced GSK3B-mediated phosphorylation; when associated with A-480 and A-485. Ref.3
Mutagenesis4921S → I: Little effect on inhibitory activity on Wnt-signaling. Ref.3
Mutagenesis4951S → A: No effect on phosphorylation. Little effect on inhibitory activity on Wnt-signaling. Ref.3
Mutagenesis858 – 8636Missing: Abolishes binding of PIAS1 and PIAS2. Dramatically reduces sumoylation and abolishes AXIN1-mediated JNK activation. No effect on homodimerization nor on Wnt-signaling. Ref.6 Ref.12
Mutagenesis8581K → A: Decreased sumoylation followed by increased ubiquitination; when associated with A-861. Ref.12
Mutagenesis8611K → A: Decreased sumoylation followed by increased ubiquitination; when associated with A-858. Ref.12
Sequence conflict5891A → P in AAC53285. Ref.1
Sequence conflict7871A → G in AAC53285. Ref.1
Sequence conflict8461A → P in AAC53285. Ref.1

Secondary structure

... 863
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 3, 2012. Version 3.
Checksum: 2216D66E92387B81

FASTA86396,276
        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 TTLSAGDLAF 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 
CDSIVVAYYF CGEPIPYRTL VRGRAVTLGQ FKELLTKKGS YRYYFKKVSD EFDCGVVFEE 

       850        860 
VREDEAVLPV FEEKIIGKVE KVD 

« Hide

Isoform 2 [UniParc].

Checksum: 0D99A235EEDC597E
Show »

FASTA82792,418

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[2]"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.
[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.
[4]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LRP5.
[5]"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.
[6]"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] [Europe PMC] [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.
[7]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, INTERACTION WITH CTNNB1.
[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.
[9]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DIXDC1; MAP3K1 AND MAP3K4.
[10]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[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.
[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.
[13]"Identification of zinc-finger BED domain-containing 3 (Zbed3) as a novel Axin-interacting protein that activates Wnt/beta-catenin signaling."
Chen T., Li M., Ding Y., Zhang L.S., Xi Y., Pan W.J., Tao D.L., Wang J.Y., Li L.
J. Biol. Chem. 284:6683-6689(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZBED3, SUBCELLULAR LOCATION.
[14]"Dab2 stabilizes Axin and attenuates Wnt/beta-catenin signaling by preventing protein phosphatase 1 (PP1)-Axin interactions."
Jiang Y., Luo W., Howe P.H.
Oncogene 28:2999-3007(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DAB2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF009011 mRNA. Translation: AAC53285.1. Different initiation.
AC126438 Genomic DNA. No translation available.
AC140047 Genomic DNA. No translation available.
RefSeqNP_033863.2. NM_009733.2.
UniGeneMm.23684.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3UTMX-ray2.00C1-80[»]
ProteinModelPortalO35625.
SMRO35625. Positions 18-220, 780-863.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198287. 33 interactions.
DIPDIP-42637N.
IntActO35625. 20 interactions.
MINTMINT-1543084.

PTM databases

PhosphoSiteO35625.

Proteomic databases

PaxDbO35625.
PRIDEO35625.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID12005.
KEGGmmu:12005.

Organism-specific databases

CTD8312.
MGIMGI:1096327. Axin1.

Phylogenomic databases

eggNOGNOG238205.
HOVERGENHBG004324.
InParanoidO35625.
KOK02157.

Gene expression databases

CleanExMM_AXIN1.
GenevestigatorO35625.

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

NextBio280195.
PROO35625.
SOURCESearch...

Entry information

Entry nameAXIN1_MOUSE
AccessionPrimary (citable) accession number: O35625
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: October 3, 2012
Last modified: April 16, 2014
This is version 138 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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