Axin-2 - Mus musculus (Mouse)

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Reviewed, UniProtKB/Swiss-Prot O88566 (AXN2_MOUSE)

Last modified January 19, 2010. Version 85. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Axin-2
Alternative name(s):
    Axis inhibition protein 2
    Conductin
    Axin-like protein
      Short name=Axil

Gene names

Name:

Axin2

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

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Protein attributes

Sequence length	840 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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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.3
Subcellular location	Cytoplasm By similarity.
Post-translational modification	Probably phosphorylated by GSK3B and dephosphorylated by PP2A By similarity. Ref.4
Sequence similarities	Contains 1 DIX domain. Contains 1 RGS domain.

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Ontologies

Keywords
Biological process	Wnt signaling pathway
Cellular component	Cytoplasm
Disease	Tumor suppressor
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	Wnt receptor signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW intramembranous ossification Inferred from mutant phenotype. Source: MGI negative regulation of cell proliferation Inferred from mutant phenotype. Source: MGI negative regulation of osteoblast differentiation Inferred from mutant phenotype. Source: MGI somitogenesis Inferred from direct assay. Source: MGI
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	signal transducer activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 840

840

Axin-2

PRO_0000220896

Regions

Domain

81 – 200

120

RGS

Domain

758 – 840

DIX

Region

327 – 413

Interaction with GSK3B By similarity

Region

413 – 478

Interaction with beta-catenin By similarity

Compositional bias

469 – 476

Poly-His

Amino acid modifications

Modified residue

460

Phosphotyrosine Ref.4

Modified residue

464

Phosphoserine Ref.4

Modified residue

628

Phosphoserine By similarity

Modified residue

637

Phosphoserine By similarity

Experimental info

Sequence conflict

101

R → K in AAF22800. Ref.2

Sequence conflict

474

H → Y in AAF22800. Ref.2

Sequence conflict

484

S → P in AAF22800. Ref.2

Sequence conflict

503

F → S in AAF22800. Ref.2

Sequence conflict

603

G → A in AAF22800. Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

O88566-1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: A07D5EFB25DE7277
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FASTA

840

92,935

        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 
TLLSTGGKLP PVAACPLLGG KSFLTKQTTK HVHHHYIHHH AVPKTKEEIE AEATQRVRCL 

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

       610        620        630        640        650        660 
AGGPQLPGEE GDRSQDVWQW MLESERQSKS KPHSAQSIRK SYPLESARAA 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

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References

	« Hide 'large scale' referencesShow '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: 9554852] [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]	"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.
[4]	"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: 18973353] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-460 AND SER-464, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	AF073788 mRNA. Translation: AAC26047.1. AF205889 mRNA. Translation: AAF22800.1.
IPI	IPI00131981.
UniGene	Mm.71710
3D structure databases
SMR	O88566. Positions 67-206, 761-840.
ModBase	Search...
Protein-protein interaction databases
STRING	O88566.
PTM databases
PhosphoSite	O88566.
Proteomic databases
PRIDE	O88566.
Genome annotation databases
Ensembl	ENSMUST00000052915; ENSMUSP00000051331; ENSMUSG00000000142; Mus musculus. [Genome view]
Organism-specific databases
MGI	MGI:1270862. Axin2.
Phylogenomic databases
HOGENOM	HBG714290.
HOVERGEN	O88566.
InParanoid	O88566.
Gene expression databases
ArrayExpress	O88566.
Bgee	O88566.
CleanEx	MM_AXIN2.
Genevestigator	O88566.
GermOnline	ENSMUSG00000000142. Mus musculus.
Family and domain databases
InterPro	IPR014936. Axin_b-cat_bd. IPR001158. DIX. IPR000342. Regulat_G_prot_signal. 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]
PROSITE	PS50841. DIX. 1 hit. PS50132. RGS. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

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Entry information

Entry name

AXN2_MOUSE

Accession

Primary (citable) accession number: O88566
Secondary accession number(s): Q9QXJ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1998
Last modified:	January 19, 2010
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents