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) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › 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.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.14 Ref.15
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.14
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 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	3D-structure 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 protein complex assembly Inferred from electronic annotation. Source: Compara 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 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 receptor signaling pathway Inferred from electronic annotation. Source: Compara negative regulation of canonical Wnt receptor 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 JNK cascade Inferred from mutant phenotype PubMed 18316368. Source: MGI positive regulation of JUN kinase activity Inferred from mutant phenotype PubMed 12878610PubMed 15579909. Source: MGI positive regulation of peptidyl-serine phosphorylation Inferred from electronic annotation. Source: Compara positive regulation of peptidyl-threonine phosphorylation Inferred from electronic annotation. Source: Compara positive regulation of proteasomal ubiquitin-dependent protein catabolic process 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-dependent 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 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_component	beta-catenin destruction complex Inferred from direct assay PubMed 10318824. Source: MGI cell cortex Inferred from direct assay PubMed 10330403. Source: MGI 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: Compara lateral plasma membrane Inferred from electronic annotation. Source: Compara nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara plasma membrane Inferred from direct assay Ref.10. Source: UniProtKB plasma membrane part Inferred from direct assay PubMed 10330403. Source: MGI postsynaptic density Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	GTPase activator activity Inferred from Biological aspect of Ancestor. Source: RefGenome I-SMAD binding Inferred from direct assay PubMed 16601693. Source: BHF-UCL armadillo repeat domain binding Inferred from Biological aspect of Ancestor. Source: RefGenome beta-catenin binding Inferred from mutant phenotype Ref.3. Source: MGI p53 binding Inferred from sequence orthology 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 kinase binding Inferred from sequence orthology Ref.8. Source: MGI signal transducer activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Dab2	P98078	2	EBI-2365912,EBI-1391846
Dvl3	Q61062	2	EBI-2365912,EBI-1538450
GSK3B	P49841	4	EBI-2365912,EBI-373586	From a different organism.
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.3

Modified residue

492

1

Phosphoserine Ref.3 Ref.13

Cross-link

858

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.6 Ref.12

Cross-link

861

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.6 Ref.12

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.3

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.3

Mutagenesis

492

1

S → A: Greatly reduced GSK3B-mediated phosphorylation; when associated with A-480 and A-485. Ref.3

Mutagenesis

492

1

S → I: Little effect on inhibitory activity on Wnt-signaling. Ref.3

Mutagenesis

495

1

S → A: No effect on phosphorylation. Little effect on inhibitory activity on Wnt-signaling. Ref.3

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.6 Ref.12

Mutagenesis

858

1

K → A: Decreased sumoylation followed by increased ubiquitination; when associated with A-861. Ref.12

Mutagenesis

861

1

K → A: Decreased sumoylation followed by increased ubiquitination; when associated with A-858. Ref.12

Sequence conflict

589

1

A → P in AAC53285. Ref.1

Sequence conflict

787

1

A → G in AAC53285. Ref.1

Sequence conflict

846

1

A → P in AAC53285. Ref.1

Secondary structure

1

.

.

.

863

Helix Strand Turn

Details...

Beta strand

64 – 66

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 3, 2012. Version 3. Checksum: 2216D66E92387B81	FASTA	863	96,276
	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
	Isoform 2 [UniParc]. Checksum: 0D99A235EEDC597E	FASTA	827	92,418
	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 TKSQRKAGGG SAPPCDSIVV AYYFCGEPIP YRTLVRGRAV TLGQFKELLT 790 800 810 820 KKGSYRYYFK KVSDEFDCGV VFEEVREDEA 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] [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. , 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]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492, MASS SPECTROMETRY. Tissue: Melanoma.
[14]	"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.
[15]	"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.

IPI

IPI00875849.
IPI00974688.

RefSeq

NP_033863.2. NM_009733.2.

UniGene

Mm.23684.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3UTM	X-ray	2.00	C	1-80	[»]

ProteinModelPortal

O35625.

SMR

O35625. Positions 74-220, 780-863.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-42637N.

IntAct

O35625. 9 interactions.

MINT

MINT-1543084.

PTM databases

PhosphoSite

O35625.

Proteomic databases

PaxDb

O35625.

PRIDE

O35625.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

12005.

KEGG

mmu:12005.

Organism-specific databases

CTD

8312.

MGI

MGI:1096327. Axin1.

Phylogenomic databases

eggNOG

NOG238205.

HOVERGEN

HBG004324.

InParanoid

O35625.

KO

K02157.

OrthoDB

EOG47SSDB.

Gene expression databases

CleanEx

MM_AXIN1.

Genevestigator

O35625.

GermOnline

ENSMUSG00000024182. Mus musculus.

Family and domain databases

Gene3D

1.10.196.10. 2 hits.

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]

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.
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NextBio

280195.

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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:	October 3, 2012
Last modified:	May 29, 2013
This is version 130 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program