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Axin-1 (Axis inhibition protein 1) (Protein Fused)

 AXIN1_MOUSE             Reviewed;         863 AA.
O35625;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 3.
25-OCT-2017, entry version 174.
RecName: Full=Axin-1;
AltName: Full=Axis inhibition protein 1;
AltName: Full=Protein Fused;
Name=Axin1; Synonyms=Axin, Fu;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
PubMed=9230313; DOI=10.1016/S0092-8674(00)80324-4;
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.;
"The mouse Fused locus encodes Axin, an inhibitor of the Wnt signaling
pathway that regulates embryonic axis formation.";
Cell 90:181-192(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
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.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
PHOSPHORYLATION AT THR-480; SER-485 AND SER-492, INTERACTION WITH
CTNNB1, AND MUTAGENESIS OF THR-480; SER-485; SER-492 AND SER-495.
PubMed=10581160; DOI=10.1006/bbrc.1999.1760;
Jho E., Lomvardas S., Costantini F.;
"A GSK3beta phosphorylation site in axin modulates interaction with
beta-catenin and Tcf-mediated gene expression.";
Biochem. Biophys. Res. Commun. 266:28-35(1999).
[4]
INTERACTION WITH LRP5.
PubMed=11336703; DOI=10.1016/S1097-2765(01)00224-6;
Mao J., Wang J., Liu B., Pan W., Farr G.H. III, Flynn C., Yuan H.,
Takada S., Kimelman D., Li L., Wu D.;
"Low-density lipoprotein receptor-related protein-5 binds to Axin and
regulates the canonical Wnt signaling pathway.";
Mol. Cell 7:801-809(2001).
[5]
INTERACTION WITH ANKRD6.
PubMed=12183362; DOI=10.1101/gad.230402;
Schwarz-Romond T., Asbrand C., Bakkers J., Kuehl M., Schaeffer H.J.,
Huelsken J., Behrens J., Hammerschmidt M., Birchmeier W.;
"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.";
Genes Dev. 16:2073-2084(2002).
[6]
SUMOYLATION AT LYS-858 AND LYS-861, INTERACTION WITH MAP3K1; SUMO1;
PIAS1; PIAS2 AND PIAS4, FUNCTION, HOMODIMERIZATION, AND MUTAGENESIS OF
858-LYS--ASP-863.
PubMed=12223491; DOI=10.1074/jbc.M208099200;
Rui H.L., Fan E., Zhou H.M., Xu Z., Zhang Y., Lin S.C.;
"SUMO-1 modification of the C-terminal KVEKVD of Axin is required for
JNK activation but has no effect on Wnt signaling.";
J. Biol. Chem. 277:42981-42986(2002).
[7]
PHOSPHORYLATION, AND INTERACTION WITH CTNNB1.
PubMed=15063782; DOI=10.1016/j.bbrc.2004.03.065;
Kim S.I., Park C.S., Lee M.S., Kwon M.S., Jho E.H., Song W.K.;
"Cyclin-dependent kinase 2 regulates the interaction of Axin with
beta-catenin.";
Biochem. Biophys. Res. Commun. 317:478-483(2004).
[8]
FUNCTION, INTERACTION WITH TP53 AND HIPK2, AND IDENTIFICATION IN A
COMPLEX WITH TP53 AND HIPK2.
PubMed=15526030; DOI=10.1038/sj.emboj.7600475;
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.;
"Axin stimulates p53 functions by activation of HIPK2 kinase through
multimeric complex formation.";
EMBO J. 23:4583-4594(2004).
[9]
INTERACTION WITH DIXDC1; MAP3K1 AND MAP3K4.
PubMed=15262978; DOI=10.1074/jbc.M404598200;
Wong C.K., Luo W., Deng Y., Zou H., Ye Z., Lin S.-C.;
"The DIX domain protein coiled-coil-DIX1 inhibits c-Jun N-terminal
kinase activation by Axin and dishevelled through distinct
mechanisms.";
J. Biol. Chem. 279:39366-39373(2004).
[10]
SUBCELLULAR LOCATION.
PubMed=16815997; DOI=10.1101/gad.1411206;
Chen H.J., Lin C.M., Lin C.S., Perez-Olle R., Leung C.L., Liem R.K.;
"The role of microtubule actin cross-linking factor 1 (MACF1) in the
Wnt signaling pathway.";
Genes Dev. 20:1933-1945(2006).
[11]
FUNCTION, HOMODIMERIZATION, AND INTERACTION WITH AIDA.
PubMed=17681137; DOI=10.1016/j.devcel.2007.07.006;
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.;
"A beta-catenin-independent dorsalization pathway activated by
Axin/JNK signaling and antagonized by aida.";
Dev. Cell 13:268-282(2007).
[12]
SUMOYLATION AT LYS-858 AND LYS-861, AND MUTAGENESIS OF LYS-858 AND
LYS-861.
PubMed=18632848; DOI=10.1096/fj.08-113910;
Kim M.J., Chia I.V., Costantini F.;
"SUMOylation target sites at the C terminus protect Axin from
ubiquitination and confer protein stability.";
FASEB J. 22:3785-3794(2008).
[13]
INTERACTION WITH ZBED3, AND SUBCELLULAR LOCATION.
PubMed=19141611; DOI=10.1074/jbc.M807753200;
Chen T., Li M., Ding Y., Zhang L.S., Xi Y., Pan W.J., Tao D.L.,
Wang J.Y., Li L.;
"Identification of zinc-finger BED domain-containing 3 (Zbed3) as a
novel Axin-interacting protein that activates Wnt/beta-catenin
signaling.";
J. Biol. Chem. 284:6683-6689(2009).
[14]
INTERACTION WITH DAB2.
PubMed=19581931; DOI=10.1038/onc.2009.157;
Jiang Y., Luo W., Howe P.H.;
"Dab2 stabilizes Axin and attenuates Wnt/beta-catenin signaling by
preventing protein phosphatase 1 (PP1)-Axin interactions.";
Oncogene 28:2999-3007(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND SER-217, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, Liver, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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. {ECO:0000250,
ECO:0000269|PubMed:12223491, ECO:0000269|PubMed:15526030,
ECO:0000269|PubMed:17681137}.
-!- SUBUNIT: 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. {ECO:0000250, ECO:0000269|PubMed:10581160,
ECO:0000269|PubMed:11336703, ECO:0000269|PubMed:12183362,
ECO:0000269|PubMed:12223491, ECO:0000269|PubMed:15063782,
ECO:0000269|PubMed:15262978, ECO:0000269|PubMed:15526030,
ECO:0000269|PubMed:17681137, ECO:0000269|PubMed:19141611,
ECO:0000269|PubMed:19581931}.
-!- INTERACTION:
P35222:CTNNB1 (xeno); NbExp=4; IntAct=EBI-2365912, EBI-491549;
P98078:Dab2; NbExp=4; IntAct=EBI-2365912, EBI-1391846;
Q61062:Dvl3; NbExp=2; IntAct=EBI-2365912, EBI-1538450;
P49841:GSK3B (xeno); NbExp=5; IntAct=EBI-2365912, EBI-373586;
O75581:LRP6 (xeno); NbExp=2; IntAct=EBI-2365912, EBI-910915;
P62137:Ppp1ca; NbExp=2; IntAct=EBI-2365912, EBI-357187;
Q99ML9:Rnf111; NbExp=4; IntAct=EBI-2365912, EBI-646015;
Q8BUN5:Smad3; NbExp=2; IntAct=EBI-2365912, EBI-2337983;
O35182:Smad6; NbExp=2; IntAct=EBI-2365912, EBI-4321242;
O35253:Smad7; NbExp=2; IntAct=EBI-2365912, EBI-5274835;
Q15583:TGIF1 (xeno); NbExp=2; IntAct=EBI-2365912, EBI-714215;
O95271:TNKS (xeno); NbExp=4; IntAct=EBI-2365912, EBI-1105254;
Q9EPK5:Wwtr1; NbExp=4; IntAct=EBI-2365912, EBI-1211920;
P46937:YAP1 (xeno); NbExp=3; IntAct=EBI-2365912, EBI-1044059;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16815997,
ECO:0000269|PubMed:19141611}. Nucleus
{ECO:0000250|UniProtKB:O15169}. Cell membrane
{ECO:0000269|PubMed:16815997}. Membrane
{ECO:0000269|PubMed:19141611}. Note=On UV irradiation,
translocates to the nucleus and colocalizes with DAAX (By
similarity). MACF1 is required for its translocation to cell
membrane (PubMed:16815997). {ECO:0000250|UniProtKB:O15169,
ECO:0000269|PubMed:16815997}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O35625-1; Sequence=Displayed;
Name=2;
IsoId=O35625-2; Sequence=VSP_000452;
-!- 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. {ECO:0000250}.
-!- PTM: 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. {ECO:0000250,
ECO:0000269|PubMed:10581160, ECO:0000269|PubMed:15063782}.
-!- PTM: 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). {ECO:0000250}.
-!- PTM: 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. {ECO:0000250, ECO:0000269|PubMed:12223491,
ECO:0000269|PubMed:18632848}.
-!- SEQUENCE CAUTION:
Sequence=AAC53285.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AF009011; AAC53285.1; ALT_INIT; mRNA.
EMBL; AC126438; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC140047; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; NP_033863.2; NM_009733.2.
UniGene; Mm.23684; -.
PDB; 3UTM; X-ray; 2.00 A; C=1-80.
PDBsum; 3UTM; -.
ProteinModelPortal; O35625; -.
SMR; O35625; -.
BioGrid; 198287; 35.
CORUM; O35625; -.
DIP; DIP-42637N; -.
ELM; O35625; -.
IntAct; O35625; 28.
MINT; MINT-1543084; -.
STRING; 10090.ENSMUSP00000073974; -.
iPTMnet; O35625; -.
PhosphoSitePlus; O35625; -.
MaxQB; O35625; -.
PaxDb; O35625; -.
PRIDE; O35625; -.
GeneID; 12005; -.
KEGG; mmu:12005; -.
CTD; 8312; -.
MGI; MGI:1096327; Axin1.
eggNOG; KOG3589; Eukaryota.
eggNOG; ENOG410YMJD; LUCA.
HOVERGEN; HBG004324; -.
InParanoid; O35625; -.
KO; K02157; -.
Reactome; R-MMU-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
ChiTaRS; Axin1; mouse.
PRO; PR:O35625; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_AXIN1; -.
GO; GO:0030877; C:beta-catenin destruction complex; IDA:MGI.
GO; GO:0005938; C:cell cortex; IDA:MGI.
GO; GO:0071944; C:cell periphery; ISO:MGI.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016328; C:lateral plasma membrane; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:MGI.
GO; GO:1990909; C:Wnt signalosome; IDA:ParkinsonsUK-UCL.
GO; GO:0008013; F:beta-catenin binding; IMP:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
GO; GO:0070411; F:I-SMAD binding; IDA:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:MGI.
GO; GO:0002039; F:p53 binding; IPI:MGI.
GO; GO:0008022; F:protein C-terminus binding; IDA:MGI.
GO; GO:0032947; F:protein complex scaffold activity; IMP:BHF-UCL.
GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0043621; F:protein self-association; IPI:MGI.
GO; GO:0070412; F:R-SMAD binding; IPI:MGI.
GO; GO:0030159; F:receptor signaling complex scaffold activity; IEA:InterPro.
GO; GO:0004871; F:signal transducer activity; ISO:MGI.
GO; GO:0046332; F:SMAD binding; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:BHF-UCL.
GO; GO:0007257; P:activation of JUN kinase activity; IBA:GO_Central.
GO; GO:0032147; P:activation of protein kinase activity; ISO:MGI.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0048318; P:axial mesoderm development; IMP:MGI.
GO; GO:0048320; P:axial mesoderm formation; IMP:MGI.
GO; GO:1904886; P:beta-catenin destruction complex disassembly; TAS:Reactome.
GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:MGI.
GO; GO:0060823; P:canonical Wnt signaling pathway involved in neural plate anterior/posterior pattern formation; IBA:GO_Central.
GO; GO:0043623; P:cellular protein complex assembly; ISO:MGI.
GO; GO:0031122; P:cytoplasmic microtubule organization; IGI:MGI.
GO; GO:0007368; P:determination of left/right symmetry; IBA:GO_Central.
GO; GO:0009950; P:dorsal/ventral axis specification; IDA:MGI.
GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:MGI.
GO; GO:0048048; P:embryonic eye morphogenesis; IBA:GO_Central.
GO; GO:0021797; P:forebrain anterior/posterior pattern specification; IBA:GO_Central.
GO; GO:0071514; P:genetic imprinting; IMP:MGI.
GO; GO:0060322; P:head development; IMP:MGI.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0055001; P:muscle cell development; IBA:GO_Central.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:MGI.
GO; GO:0045599; P:negative regulation of fat cell differentiation; IDA:MGI.
GO; GO:0010629; P:negative regulation of gene expression; IDA:MGI.
GO; GO:0051248; P:negative regulation of protein metabolic process; IDA:MGI.
GO; GO:0034244; P:negative regulation of transcription elongation from RNA polymerase II promoter; IDA:MGI.
GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IDA:MGI.
GO; GO:0006913; P:nucleocytoplasmic transport; IDA:MGI.
GO; GO:0030910; P:olfactory placode formation; IBA:GO_Central.
GO; GO:0001743; P:optic placode formation; IBA:GO_Central.
GO; GO:0046330; P:positive regulation of JNK cascade; IMP:UniProtKB.
GO; GO:0043507; P:positive regulation of JUN kinase activity; IDA:MGI.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:MGI.
GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:CACAO.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:MGI.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:MGI.
GO; GO:2000060; P:positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IDA:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IDA:MGI.
GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; IMP:BHF-UCL.
GO; GO:0036342; P:post-anal tail morphogenesis; IMP:MGI.
GO; GO:0030163; P:protein catabolic process; IDA:MGI.
GO; GO:0051260; P:protein homooligomerization; IDA:MGI.
GO; GO:0000209; P:protein polyubiquitination; IDA:MGI.
GO; GO:0035412; P:regulation of catenin import into nucleus; IDA:MGI.
GO; GO:0001932; P:regulation of protein phosphorylation; IGI:MGI.
GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
GO; GO:0016055; P:Wnt signaling pathway; IDA:MGI.
GO; GO:0021881; P:Wnt-activated signaling pathway involved in forebrain neuron fate commitment; IBA:GO_Central.
CDD; cd11582; Axin_TNKS_binding; 1.
Gene3D; 1.10.196.10; -; 2.
InterPro; IPR029797; AXIN1.
InterPro; IPR014936; Axin_b-cat-bd.
InterPro; IPR032101; Axin_TNKS-bd.
InterPro; IPR001158; DIX.
InterPro; IPR016137; RGS.
InterPro; IPR036305; RGS_sf.
InterPro; IPR024066; RGS_subdom1.
InterPro; IPR029071; Ubiquitin-rel_dom.
PANTHER; PTHR10845:SF11; PTHR10845:SF11; 1.
Pfam; PF16646; AXIN1_TNKS_BD; 1.
Pfam; PF08833; Axin_b-cat_bind; 1.
Pfam; PF00778; DIX; 1.
Pfam; PF00615; RGS; 1.
PRINTS; PR01301; RGSPROTEIN.
SMART; SM00021; DAX; 1.
SMART; SM00315; RGS; 1.
SUPFAM; SSF48097; SSF48097; 1.
SUPFAM; SSF54236; SSF54236; 1.
PROSITE; PS50841; DIX; 1.
PROSITE; PS50132; RGS; 1.
1: Evidence at protein level;
3D-structure; ADP-ribosylation; Alternative splicing; Apoptosis;
Cell membrane; Complete proteome; Cytoplasm; Developmental protein;
Isopeptide bond; Membrane; Nucleus; Phosphoprotein;
Reference proteome; Tumor suppressor; Ubl conjugation;
Wnt signaling pathway.
CHAIN 1 863 Axin-1.
/FTId=PRO_0000220889.
DOMAIN 88 211 RGS. {ECO:0000255|PROSITE-
ProRule:PRU00171}.
DOMAIN 781 863 DIX. {ECO:0000255|PROSITE-
ProRule:PRU00069}.
REGION 209 338 Interaction with TP53.
{ECO:0000269|PubMed:15526030}.
REGION 348 432 Interaction with GSK3B. {ECO:0000250}.
REGION 433 501 Interaction with beta-catenin.
{ECO:0000250}.
REGION 505 758 Interaction with RNF111. {ECO:0000250}.
REGION 572 790 Interaction with PPP2CA. {ECO:0000250}.
REGION 678 753 Interaction with HIPK2.
{ECO:0000269|PubMed:15526030}.
MOTIF 20 29 Tankyrase-binding motif.
MOD_RES 75 75 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 77 77 Phosphoserine; by CK1.
{ECO:0000250|UniProtKB:O15169}.
MOD_RES 217 217 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 468 468 Phosphoserine; by CK1.
{ECO:0000250|UniProtKB:O15169}.
MOD_RES 480 480 Phosphothreonine; by GSK3-beta.
{ECO:0000305|PubMed:10581160}.
MOD_RES 485 485 Phosphoserine; by GSK3-beta.
{ECO:0000269|PubMed:10581160}.
MOD_RES 492 492 Phosphoserine.
{ECO:0000269|PubMed:10581160}.
MOD_RES 509 509 Phosphoserine.
{ECO:0000250|UniProtKB:O15169}.
CROSSLNK 858 858 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:12223491,
ECO:0000269|PubMed:18632848}.
CROSSLNK 861 861 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:12223491,
ECO:0000269|PubMed:18632848}.
VAR_SEQ 731 766 Missing (in isoform 2).
{ECO:0000303|PubMed:9230313}.
/FTId=VSP_000452.
MUTAGEN 480 480 T->A: Greatly reduced GSK3B-mediated
phosphorylation; when associated with A-
485 and A-492.
{ECO:0000269|PubMed:10581160}.
MUTAGEN 485 485 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.
{ECO:0000269|PubMed:10581160}.
MUTAGEN 492 492 S->A: Greatly reduced GSK3B-mediated
phosphorylation; when associated with A-
480 and A-485.
{ECO:0000269|PubMed:10581160}.
MUTAGEN 492 492 S->I: Little effect on inhibitory
activity on Wnt-signaling.
{ECO:0000269|PubMed:10581160}.
MUTAGEN 495 495 S->A: No effect on phosphorylation.
Little effect on inhibitory activity on
Wnt-signaling.
{ECO:0000269|PubMed:10581160}.
MUTAGEN 858 863 Missing: Abolishes binding of PIAS1 and
PIAS2. Dramatically reduces sumoylation
and abolishes AXIN1-mediated JNK
activation. No effect on homodimerization
nor on Wnt-signaling.
{ECO:0000269|PubMed:12223491}.
MUTAGEN 858 858 K->A: Decreased sumoylation followed by
increased ubiquitination; when associated
with A-861.
{ECO:0000269|PubMed:18632848}.
MUTAGEN 861 861 K->A: Decreased sumoylation followed by
increased ubiquitination; when associated
with A-858.
{ECO:0000269|PubMed:18632848}.
CONFLICT 589 589 A -> P (in Ref. 1; AAC53285).
{ECO:0000305}.
CONFLICT 787 787 A -> G (in Ref. 1; AAC53285).
{ECO:0000305}.
CONFLICT 846 846 A -> P (in Ref. 1; AAC53285).
{ECO:0000305}.
STRAND 64 66 {ECO:0000244|PDB:3UTM}.
SEQUENCE 863 AA; 96276 MW; 2216D66E92387B81 CRC64;
MNVQEQGFPL DLGASFTEDA PRPPVPGEEG ELVSTDSRPV NHSFCSGKGT SIKSETSTAT
PRRSDLDLGY EPEGSASPTP PYLRWAESLH SLLDDQDGIS LFRTFLKQEG CADLLDFWFA
CSGFRKLEPC DSNEEKRLKL ARAIYRKYIL DSNGIVSRQT KPATKSFIKD CVMKQQIDPA
MFDQAQTEIQ STMEENTYPS FLKSDIYLEY TRTGSESPKV CSDQSSGSGT GKGMSGYLPT
LNEDEEWKCD QDADEDDGRD PLPPSRLTQK LLLETAAPRA PSSRRYNEGR ELRYGSWREP
VNPYYVNSGY ALAPATSAND SEQQSLSSDA DTLSLTDSSV DGIPPYRIRK QHRREMQESI
QVNGRVPLPH IPRTYRMPKE IRVEPQKFAE ELIHRLEAVQ RTREAEEKLE ERLKRVRMEE
EGEDGEMPSG PMASHKLPSV PAWHHFPPRY VDMGCSGLRD AHEENPESIL DEHVQRVMRT
PGCQSPGPGH RSPDSGHVAK TAVLGGTASG HGKHVPKLGL KLDTAGLHHH RHVHHHVHHN
SARPKEQMEA EVARRVQSSF SWGPETHGHA KPRSYSENAG TTLSAGDLAF GGKTSAPSKR
NTKKAESGKN ANAEVPSTTE DAEKNQKIMQ WIIEGEKEIS RHRKAGHGSS GLRKQQAHES
SRPLSIERPG AVHPWVSAQL RNSVQPSHLF IQDPTMPPNP APNPLTQLEE ARRRLEEEEK
RANKLPSKQR YVQAVMQRGR TCVRPACAPV LSVVPAVSDL ELSETETKSQ RKAGGGSAPP
CDSIVVAYYF CGEPIPYRTL VRGRAVTLGQ FKELLTKKGS YRYYFKKVSD EFDCGVVFEE
VREDEAVLPV FEEKIIGKVE KVD


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