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O15169 (AXIN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Axin-1
Alternative name(s):
Axis inhibition protein 1
Short name=hAxin
Gene names
Name:AXIN1
Synonyms:AXIN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length862 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. 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. Also component of the AXIN1-HIPK2-TP53 complex which controls cell growth, apoptosis and development. Ref.8 Ref.12 Ref.13

Subunit structure

Homodimer. Interacts with ZBED3; the interaction is direct, enhanced by protein kinase GSK3B and casein kinase CSNK1E activities and decreases GSK3B-induced beta-catenin serine and threonine phosphorylations By similarity. Component of the beta-catenin destruction complex, containing at least, CTNNB1, an axin and GSK3B, that regulates CTNNB1 protein levels through phosphorylation and ubiquitination. Interacts with CTNNB1 (via the armadillo repeats 2-7). Interacts with GSK3B; the interaction hyperphosphorylates CTNNB1 leading to its ubiquitination and destruction. Component of the AXIN1-HIPK2-TP53 complex. Interacts directly in the complex with TP53 and HIPK2. 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 binds APC, SMAD6, SMAD7 and RNF111. Interacts with DIXDC1; prevents interaction with MAP3K1. Interacts with MAP3K4. Interacts with ANKRD6 and AIDA By similarity. 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. Interacts with LRP5 (via its phosphorylated PPPSP motifs); the interaction is stimulated by WNT1 and GSK3B and activates beta-catenin signaling. 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 MACF1 By similarity. Found in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B By similarity. Interacts with TNKS. Interacts with DAB2; the interaction is mutually exclusive with the AXIN1:PPP1CA interaction. Ref.5 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.17 Ref.19 Ref.20

Subcellular location

Cytoplasm. Nucleus. Membrane By similarity. Cell membrane By similarity. Note: MACF1 is required for its translocation to cell membrane By similarity. On UV irradiation, translocates to the nucleus and colocalizes with DAAX. Ref.12 Ref.13 Ref.18

Tissue specificity

Ubiquitously expressed.

Domain

The tankyrase-binding motif (also named TBD) is required for interaction with tankyrase TNKS and TNKS2. Ref.17

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. Ref.5 Ref.14

ADP-ribosylated by tankyrase TNKS and TNKS2. Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination at 'Lys-48' and subsequent activation of the Wnt signaling pathway.

Ubiquitinated by RNF146 when poly-ADP-ribosylated, leading to its degradation and subsequent activation of the Wnt signaling pathway. Sumoylation at Lys-857 and Lys-860 prevents ubiquitination and degradation. Sumoylation is required for AXIN1-mediated JNK activation. 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. Ref.17 Ref.18 Ref.19 Ref.20

Involvement in disease

Hepatocellular carcinoma (HCC) [MIM:114550]: A primary malignant neoplasm of epithelial liver cells. The major risk factors for HCC are chronic hepatitis B virus (HBV) infection, chronic hepatitis C virus (HCV) infection, prolonged dietary aflatoxin exposure, alcoholic cirrhosis, and cirrhosis due to other causes.
Note: The gene represented in this entry is involved in disease pathogenesis. Ref.6 Ref.23

Caudal duplication anomaly (CADUA) [MIM:607864]: A condition characterized by the occurrence of duplications of different organs in the caudal region.
Note: The disease is caused by mutations affecting the gene represented in this entry. Caudal duplication anomaly is associated with hypermethylation of the AXIN1 promoter. Ref.6

Sequence similarities

Contains 1 DIX domain.

Contains 1 RGS domain.

Sequence caution

The sequence AAC51624.1 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
   DiseaseDisease mutation
Tumor 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 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

activation of protein kinase activity

Inferred from direct assay PubMed 9601641. Source: BHF-UCL

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

axial mesoderm formation

Inferred from Biological aspect of Ancestor. Source: RefGenome

canonical Wnt signaling pathway

Inferred by curator PubMed 9601641. Source: UniProtKB

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 direct assay Ref.12. Source: BHF-UCL

cellular response to organic cyclic compound

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytoplasmic microtubule organization

Inferred from Biological aspect of Ancestor. Source: RefGenome

determination of left/right symmetry

Inferred from Biological aspect of Ancestor. Source: RefGenome

dorsal/ventral axis specification

Inferred from Biological aspect of Ancestor. Source: RefGenome

embryonic eye morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

embryonic skeletal joint 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 electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

muscle cell development

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of Wnt signaling pathway

Inferred from direct assay PubMed 10644691. Source: BHF-UCL

negative regulation of canonical Wnt signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of fat cell differentiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of protein metabolic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription elongation from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

nucleocytoplasmic transport

Inferred from electronic annotation. Source: Ensembl

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 sequence or structural similarity. Source: UniProtKB

positive regulation of peptidyl-serine phosphorylation

Non-traceable author statement PubMed 18593713. Source: BHF-UCL

positive regulation of peptidyl-threonine phosphorylation

Non-traceable author statement PubMed 18593713. Source: BHF-UCL

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein catabolic process

Inferred from direct assay PubMed 9601641. Source: BHF-UCL

positive regulation of protein phosphorylation

Inferred from direct assay PubMed 9601641. Source: BHF-UCL

positive regulation of protein ubiquitination

Non-traceable author statement PubMed 18593713. Source: BHF-UCL

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

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.12. Source: BHF-UCL

positive regulation of transforming growth factor beta receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of ubiquitin-protein ligase activity

Inferred from mutant phenotype Ref.12. Source: BHF-UCL

post-anal tail morphogenesis

Inferred from electronic annotation. Source: Ensembl

protein catabolic process

Inferred from electronic annotation. Source: Ensembl

protein homooligomerization

Inferred from electronic annotation. Source: Ensembl

protein polyubiquitination

Inferred from electronic annotation. Source: Ensembl

regulation of catenin import into nucleus

Inferred from Biological aspect of Ancestor. Source: RefGenome

sensory perception of sound

Inferred from electronic annotation. Source: Ensembl

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 16188939PubMed 9601641. Source: UniProtKB

cell cortex

Inferred from Biological aspect of Ancestor. Source: RefGenome

cell periphery

Inferred from direct assay PubMed 19038973. Source: BHF-UCL

cytoplasm

Inferred from direct assay Ref.18. Source: UniProtKB

cytoplasmic membrane-bounded vesicle

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytoplasmic microtubule

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytoplasmic vesicle

Inferred from sequence or structural similarity. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

lateral plasma membrane

Inferred from direct assay PubMed 12072559. Source: MGI

nucleus

Inferred from direct assay Ref.18. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay PubMed 19038973. Source: BHF-UCL

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 Ref.12PubMed 18593713. Source: BHF-UCL

SMAD binding

Inferred from physical interaction PubMed 18593713. Source: BHF-UCL

armadillo repeat domain binding

Inferred from sequence or structural similarity. Source: BHF-UCL

beta-catenin binding

Inferred from direct assay PubMed 10644691. Source: BHF-UCL

enzyme binding

Inferred from physical interaction Ref.17Ref.18Ref.19. Source: UniProtKB

identical protein binding

Inferred from sequence or structural similarity. Source: BHF-UCL

protein complex scaffold

Inferred from direct assay PubMed 9601641. Source: BHF-UCL

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein kinase binding

Inferred from sequence or structural similarity. Source: BHF-UCL

signal transducer activity

Inferred from direct assay PubMed 9601641. Source: BHF-UCL

ubiquitin protein ligase binding

Inferred from physical interaction Ref.19. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O15169-1)

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: O15169-2)

The sequence of this isoform differs from the canonical sequence as follows:
     730-765: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 862862Axin-1
PRO_0000220888

Regions

Domain88 – 211124RGS
Domain780 – 86283DIX
Region209 – 338130Interaction with TP53 By similarity
Region348 – 43386Interaction with GSK3B By similarity
Region434 – 50269Interaction with CTNNB1 By similarity
Region507 – 757251Interaction with RNF111
Region575 – 789215Interaction with PPP2CA
Region677 – 75276Interaction with HIPK2 By similarity
Motif20 – 2910Tankyrase-binding motif

Amino acid modifications

Modified residue751Phosphoserine; by CK1 Ref.14
Modified residue771Phosphoserine; by CK1 Ref.14
Modified residue2171Phosphoserine; by CK1 Ref.14
Modified residue4691Phosphoserine; by CK1 Ref.14
Modified residue4811Phosphothreonine; by GSK3-beta Probable
Modified residue4861Phosphoserine; by GSK3-beta By similarity
Modified residue4931Phosphoserine By similarity
Cross-link857Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link860Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence730 – 76536Missing in isoform 2.
VSP_019398
Natural variant1061L → R in HCC. Ref.23
VAR_015589
Natural variant3451P → L in HCC. Ref.23
VAR_015590
Natural variant4251G → S in HCC. Ref.23
Corresponds to variant rs116350678 [ dbSNP | Ensembl ].
VAR_015591
Natural variant6501G → S in HCC and in hepatoblastoma. Ref.23
Corresponds to variant rs117208012 [ dbSNP | Ensembl ].
VAR_015592
Natural variant8411R → Q in hepatoblastoma. Ref.23
Corresponds to variant rs34015754 [ dbSNP | Ensembl ].
VAR_015593

Experimental info

Sequence conflict3601V → A in AAC51624. Ref.1
Sequence conflict451 – 4555CVDMG → LCWTWA in AAC51624. Ref.1
Sequence conflict4821P → T in AAC51624. Ref.1

Secondary structure

........................... 862
Helix Strand Turn

Details...

Sequences

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

Last modified May 10, 2002. Version 2.
Checksum: 10779173F5092F3F

FASTA86295,635
        10         20         30         40         50         60 
MNIQEQGFPL DLGASFTEDA PRPPVPGEEG ELVSTDPRPA SYSFCSGKGV GIKGETSTAT 

        70         80         90        100        110        120 
PRRSDLDLGY EPEGSASPTP PYLKWAESLH SLLDDQDGIS LFRTFLKQEG CADLLDFWFA 

       130        140        150        160        170        180 
CTGFRKLEPC DSNEEKRLKL ARAIYRKYIL DNNGIVSRQT KPATKSFIKG CIMKQLIDPA 

       190        200        210        220        230        240 
MFDQAQTEIQ ATMEENTYPS FLKSDIYLEY TRTGSESPKV CSDQSSGSGT GKGISGYLPT 

       250        260        270        280        290        300 
LNEDEEWKCD QDMDEDDGRD AAPPGRLPQK LLLETAAPRV SSSRRYSEGR EFRYGSWREP 

       310        320        330        340        350        360 
VNPYYVNAGY ALAPATSAND SEQQSLSSDA DTLSLTDSSV DGIPPYRIRK QHRREMQESV 

       370        380        390        400        410        420 
QVNGRVPLPH IPRTYRVPKE VRVEPQKFAE ELIHRLEAVQ RTREAEEKLE ERLKRVRMEE 

       430        440        450        460        470        480 
EGEDGDPSSG PPGPCHKLPP APAWHHFPPR CVDMGCAGLR DAHEENPESI LDEHVQRVLR 

       490        500        510        520        530        540 
TPGRQSPGPG HRSPDSGHVA KMPVALGGAA SGHGKHVPKS GAKLDAAGLH HHRHVHHHVH 

       550        560        570        580        590        600 
HSTARPKEQV EAEATRRAQS SFAWGLEPHS HGARSRGYSE SVGAAPNASD GLAHSGKVGV 

       610        620        630        640        650        660 
ACKRNAKKAE SGKSASTEVP GASEDAEKNQ KIMQWIIEGE KEISRHRRTG HGSSGTRKPQ 

       670        680        690        700        710        720 
PHENSRPLSL EHPWAGPQLR TSVQPSHLFI QDPTMPPHPA PNPLTQLEEA RRRLEEEEKR 

       730        740        750        760        770        780 
ASRAPSKQRY VQEVMRRGRA CVRPACAPVL HVVPAVSDME LSETETRSQR KVGGGSAQPC 

       790        800        810        820        830        840 
DSIVVAYYFC GEPIPYRTLV RGRAVTLGQF KELLTKKGSY RYYFKKVSDE FDCGVVFEEV 

       850        860 
REDEAVLPVF EEKIIGKVEK VD 

« Hide

Isoform 2 [UniParc].

Checksum: 4AA4187D70A5863D
Show »

FASTA82691,653

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] (ISOFORM 1).
[2]"Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16."
Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.
Hum. Mol. Genet. 10:339-352(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 471-862 (ISOFORM 1).
Tissue: Lymphoma and Renal cell carcinoma.
[5]"Identification of a domain of Axin that binds to the serine/threonine protein phosphatase 2A and a self-binding domain."
Hsu W., Zeng L., Costantini F.
J. Biol. Chem. 274:3439-3445(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GSK3B AND PPP2CA, PHOSPHORYLATION, DEPHOSPHORYLATION.
[6]"AXIN1 mutations in hepatocellular carcinomas, and growth suppression in cancer cells by virus-mediated transfer of AXIN1."
Satoh S., Daigo Y., Furukawa Y., Kato T., Miwa N., Nishiwaki T., Kawasoe T., Ishiguro H., Fujita M., Tokino T., Sasaki Y., Imaoka S., Murata M., Shimano T., Yamaoka Y., Nakamura Y.
Nat. Genet. 24:245-250(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: DISEASE.
[7]"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.
[8]"I-mfa domain proteins interact with Axin and affect its regulation of the Wnt and c-Jun N-terminal kinase signaling pathways."
Kusano S., Raab-Traub N.
Mol. Cell. Biol. 22:6393-6405(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MDFI AND MDFIC, FUNCTION.
[9]"Regulation of the Wnt signaling pathway by disabled-2 (Dab2)."
Howe P.H.
EMBO J. 22:3084-3094(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DAB2.
[10]"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.
[11]"Increased DNA methylation at the AXIN1 gene in a monozygotic twin from a pair discordant for a caudal duplication anomaly."
Oates N.A., van Vliet J., Duffy D.L., Kroes H.Y., Martin N.G., Boomsma D.I., Campbell M., Coulthard M.G., Whitelaw E., Chong S.
Am. J. Hum. Genet. 79:155-162(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CAUDAL DUPLICATION ANOMALY.
[12]"Axin is a scaffold protein in TGF-beta signaling that promotes degradation of Smad7 by Arkadia."
Liu W., Rui H., Wang J., Lin S., He Y., Chen M., Li Q., Ye Z., Zhang S., Chan S.C., Chen Y.-G., Han J., Lin S.-C.
EMBO J. 25:1646-1658(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SMAD6; SMAD7 AND RNF111, FUNCTION, SUBCELLULAR LOCATION.
[13]"Daxx cooperates with the Axin/HIPK2/p53 complex to induce cell death."
Li Q., Wang X., Wu X., Rui Y., Liu W., Wang J., Wang X., Liou Y.C., Ye Z., Lin S.C.
Cancer Res. 67:66-74(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DAXX, IDENTIFICATION AS A COMPONENT OF THE AXIN1-HIPK2-TP53 COMPLEX, SUBCELLULAR LOCATION, FUNCTION.
[14]"Protein phosphatase 1 regulates assembly and function of the beta-catenin degradation complex."
Luo W., Peterson A., Garcia B.A., Coombs G., Kofahl B., Heinrich R., Shabanowitz J., Hunt D.F., Yost H.J., Virshup D.M.
EMBO J. 26:1511-1521(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-75; SER-77; SER-217 AND SER-469, INTERACTION WITH GSK3B AND PPP1CA, IDENTIFICATION BY MASS SPECTROMETRY.
[15]"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.
[16]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Tankyrase inhibition stabilizes axin and antagonizes Wnt signalling."
Huang S.M., Mishina Y.M., Liu S., Cheung A., Stegmeier F., Michaud G.A., Charlat O., Wiellette E., Zhang Y., Wiessner S., Hild M., Shi X., Wilson C.J., Mickanin C., Myer V., Fazal A., Tomlinson R., Serluca F. expand/collapse author list , Shao W., Cheng H., Shultz M., Rau C., Schirle M., Schlegl J., Ghidelli S., Fawell S., Lu C., Curtis D., Kirschner M.W., Lengauer C., Finan P.M., Tallarico J.A., Bouwmeester T., Porter J.A., Bauer A., Cong F.
Nature 461:614-620(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ADP-RIBOSYLATION, UBIQUITINATION, DOMAIN TANKYRASE-BINDING MOTIF, INTERACTION WITH TNKS AND TNKS2.
[18]"The Ubiquitin specific protease USP34 regulates Axin stability and Wnt/beta-catenin signaling."
Lui T.T., Lacroix C., Ahmed S.M., Goldenberg S.J., Leach C.A., Daulat A.M., Angers S.
Mol. Cell. Biol. 31:2053-2065(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP34, SUBCELLULAR LOCATION.
[19]"RNF146 is a poly(ADP-ribose)-directed E3 ligase that regulates axin degradation and Wnt signalling."
Zhang Y., Liu S., Mickanin C., Feng Y., Charlat O., Michaud G.A., Schirle M., Shi X., Hild M., Bauer A., Myer V.E., Finan P.M., Porter J.A., Huang S.M., Cong F.
Nat. Cell Biol. 13:623-629(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ADP-RIBOSYLATION, UBIQUITINATION, INTERACTION WITH RNF146; TNKS AND TNKS2.
[20]"Ubiquitin ligase RNF146 regulates tankyrase and Axin to promote Wnt signaling."
Callow M.G., Tran H., Phu L., Lau T., Lee J., Sandoval W.N., Liu P.S., Bheddah S., Tao J., Lill J.R., Hongo J.A., Davis D., Kirkpatrick D.S., Polakis P., Costa M.
PLoS ONE 6:E22595-E22595(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TNKS, UBIQUITINATION.
[21]"Structural basis of the axin-adenomatous polyposis coli interaction."
Spink K.E., Polakis P., Weis W.I.
EMBO J. 19:2270-2279(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 74-220 IN COMPLEX WITH APC.
[22]"Structural basis for recruitment of glycogen synthase kinase 3beta to the axin-APC scaffold complex."
Dajani R., Fraser E., Roe S.M., Yeo M., Good V.M., Thompson V., Dale T.C., Pearl L.H.
EMBO J. 22:494-501(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 383-400 IN COMPLEX WITH GSK3B.
[23]"Mutational spectrum of beta-catenin, AXIN1, and AXIN2 in hepatocellular carcinomas and hepatoblastomas."
Taniguchi K., Roberts L.R., Aderca I.N., Dong X., Qian C., Murphy L.M., Nagorney D.M., Burgart L.J., Roche P.C., Smith D.I., Ross J.A., Liu W.
Oncogene 21:4863-4871(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HCC ARG-106; LEU-345; SER-425 AND SER-650, VARIANT HEPATOBLASTOMA GLN-841.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF009674 mRNA. Translation: AAC51624.1. Different initiation.
AE006463 Genomic DNA. Translation: AAK61224.1.
Z69667, AC005202, Z99754 Genomic DNA. Translation: CAI95589.2.
Z69667, AC005202, Z99754 Genomic DNA. Translation: CAI95590.2.
Z99754, AC005202, Z69667 Genomic DNA. Translation: CAI95600.2.
Z99754, AC005202, Z69667 Genomic DNA. Translation: CAI95601.2.
BC017447 mRNA. Translation: AAH17447.1.
BC044648 mRNA. Translation: AAH44648.1.
RefSeqNP_003493.1. NM_003502.3.
NP_851393.1. NM_181050.2.
XP_005255666.1. XM_005255609.2.
UniGeneHs.592082.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DK8X-ray1.57A74-220[»]
1EMUX-ray1.90A80-211[»]
1O9UX-ray2.40B383-400[»]
3ZDIX-ray2.64B383-400[»]
4B7TX-ray2.77B383-400[»]
ProteinModelPortalO15169.
SMRO15169. Positions 18-220, 779-862.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113909. 55 interactions.
DIPDIP-34630N.
IntActO15169. 62 interactions.
MINTMINT-100969.
STRING9606.ENSP00000262320.

Chemistry

ChEMBLCHEMBL1255127.

PTM databases

PhosphoSiteO15169.

Proteomic databases

PaxDbO15169.
PRIDEO15169.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262320; ENSP00000262320; ENSG00000103126. [O15169-1]
ENST00000354866; ENSP00000346935; ENSG00000103126. [O15169-2]
GeneID8312.
KEGGhsa:8312.
UCSCuc002cgp.2. human. [O15169-1]
uc002cgq.2. human. [O15169-2]

Organism-specific databases

CTD8312.
GeneCardsGC16M000338.
HGNCHGNC:903. AXIN1.
HPACAB012987.
MIM114550. phenotype.
603816. gene.
607864. phenotype.
neXtProtNX_O15169.
PharmGKBPA25195.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG238205.
HOVERGENHBG004324.
InParanoidO15169.
KOK02157.
OMAIMQWIIE.
OrthoDBEOG79PJQ0.
PhylomeDBO15169.
TreeFamTF315454.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkO15169.

Gene expression databases

ArrayExpressO15169.
BgeeO15169.
CleanExHS_AXIN1.
GenevestigatorO15169.

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

EvolutionaryTraceO15169.
GeneWikiAXIN1.
GenomeRNAi8312.
NextBio31127.
PROO15169.
SOURCESearch...

Entry information

Entry nameAXIN1_HUMAN
AccessionPrimary (citable) accession number: O15169
Secondary accession number(s): Q4TT26 expand/collapse secondary AC list , Q4TT27, Q86YA7, Q8WVW6, Q96S28
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 10, 2002
Last modified: April 16, 2014
This is version 159 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM