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Protein

Axin-1

Gene

AXIN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

GO - Molecular functioni

  • armadillo repeat domain binding Source: BHF-UCL
  • beta-catenin binding Source: BHF-UCL
  • enzyme binding Source: UniProtKB
  • GTPase activator activity Source: GO_Central
  • identical protein binding Source: BHF-UCL
  • I-SMAD binding Source: BHF-UCL
  • protein complex scaffold Source: BHF-UCL
  • protein homodimerization activity Source: UniProtKB
  • protein kinase binding Source: BHF-UCL
  • signal transducer activity Source: BHF-UCL
  • SMAD binding Source: BHF-UCL
  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Apoptosis, Wnt signaling pathway

Enzyme and pathway databases

ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_11065. Beta-catenin phosphorylation cascade.
REACT_263873. degradation of AXIN.
REACT_263893. truncations of AMER1 destabilize the destruction complex.
REACT_263992. APC truncation mutants have impaired AXIN binding.
REACT_264030. AXIN missense mutants destabilize the destruction complex.
REACT_264034. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_264092. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_264127. T41 mutants of beta-catenin aren't phosphorylated.
REACT_264295. S45 mutants of beta-catenin aren't phosphorylated.
REACT_264581. S33 mutants of beta-catenin aren't phosphorylated.
REACT_264596. TCF dependent signaling in response to WNT.
REACT_264636. S37 mutants of beta-catenin aren't phosphorylated.
SignaLinkiO15169.

Names & Taxonomyi

Protein namesi
Recommended name:
Axin-1
Alternative name(s):
Axis inhibition protein 1
Short name:
hAxin
Gene namesi
Name:AXIN1
Synonyms:AXIN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:903. AXIN1.

Subcellular locationi

  • 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.By similarity

GO - Cellular componenti

  • beta-catenin destruction complex Source: UniProtKB
  • cell cortex Source: GO_Central
  • cell periphery Source: BHF-UCL
  • cytoplasm Source: UniProtKB
  • cytoplasmic membrane-bounded vesicle Source: GO_Central
  • cytoplasmic microtubule Source: GO_Central
  • cytoplasmic vesicle Source: BHF-UCL
  • cytosol Source: Reactome
  • Golgi apparatus Source: Ensembl
  • lateral plasma membrane Source: MGI
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: BHF-UCL
  • plasma membrane Source: GO_Central
  • postsynaptic density Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Hepatocellular carcinoma (HCC)1 Publication

The gene represented in this entry is involved in disease pathogenesis.

Disease descriptionA 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.

See also OMIM:114550
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti106 – 1061L → R in HCC. 1 Publication
VAR_015589
Natural varianti345 – 3451P → L in HCC. 1 Publication
VAR_015590
Natural varianti425 – 4251G → S in HCC. 1 Publication
Corresponds to variant rs116350678 [ dbSNP | Ensembl ].
VAR_015591
Natural varianti650 – 6501G → S in HCC and in hepatoblastoma. 1 Publication
Corresponds to variant rs117208012 [ dbSNP | Ensembl ].
VAR_015592
Caudal duplication anomaly (CADUA)1 Publication

The disease is caused by mutations affecting the gene represented in this entry. Caudal duplication anomaly is associated with hypermethylation of the AXIN1 promoter.

Disease descriptionA condition characterized by the occurrence of duplications of different organs in the caudal region.

See also OMIM:607864

Keywords - Diseasei

Disease mutation, Tumor suppressor

Organism-specific databases

MIMi114550. phenotype.
607864. phenotype.
PharmGKBiPA25195.

Polymorphism and mutation databases

BioMutaiAXIN1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 862862Axin-1PRO_0000220888Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei75 – 751Phosphoserine; by CK11 Publication
Modified residuei77 – 771Phosphoserine; by CK11 Publication
Modified residuei217 – 2171Phosphoserine; by CK11 Publication
Modified residuei469 – 4691Phosphoserine; by CK11 Publication
Modified residuei481 – 4811Phosphothreonine; by GSK3-beta1 Publication
Modified residuei486 – 4861Phosphoserine; by GSK3-betaBy similarity
Modified residuei493 – 4931PhosphoserineBy similarity
Cross-linki857 – 857Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki860 – 860Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

Post-translational modificationi

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 AXIN1.2 Publications
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.1 Publication
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.2 Publications

Keywords - PTMi

ADP-ribosylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO15169.
PaxDbiO15169.
PRIDEiO15169.

PTM databases

PhosphoSiteiO15169.

Expressioni

Tissue specificityi

Ubiquitously expressed.

Gene expression databases

BgeeiO15169.
CleanExiHS_AXIN1.
ExpressionAtlasiO15169. baseline and differential.
GenevisibleiO15169. HS.

Organism-specific databases

HPAiCAB012987.
HPA042412.

Interactioni

Subunit structurei

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.By similarity13 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ANP32AP396872EBI-710484,EBI-359234
apcP700392EBI-710484,EBI-8069633From a different organism.
CRMP1Q141942EBI-710484,EBI-473101
CSNK1EP496744EBI-710484,EBI-749343
CTNNB1P3522241EBI-710484,EBI-491549
Ctnnb1Q022485EBI-710484,EBI-397872From a different organism.
DAB2IPQ5VWQ8-22EBI-710484,EBI-9543020
FBXW11Q9UKB14EBI-710484,EBI-355189
GSK3AP498402EBI-710484,EBI-1044067
GSK3BP4984142EBI-710484,EBI-373586
MYCP0110610EBI-710484,EBI-447544
PPM1AP358132EBI-710484,EBI-989143
PPP1CAP621364EBI-710484,EBI-357253
RNF111Q6ZNA42EBI-710484,EBI-2129175
Rnf111Q99ML95EBI-710484,EBI-646015From a different organism.
SMAD7O151058EBI-710484,EBI-3861591
TNKS2Q9H2K22EBI-710484,EBI-4398527
TP53P046374EBI-710484,EBI-366083
TRIM29Q141342EBI-710484,EBI-702370
TUBG1P232584EBI-710484,EBI-302589
YAP1P4693711EBI-710484,EBI-1044059

Protein-protein interaction databases

BioGridi113909. 57 interactions.
DIPiDIP-34630N.
IntActiO15169. 66 interactions.
MINTiMINT-100969.
STRINGi9606.ENSP00000262320.

Structurei

Secondary structure

1
862
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi81 – 877Combined sources
Helixi89 – 924Combined sources
Helixi96 – 10712Combined sources
Turni108 – 1103Combined sources
Helixi112 – 12615Combined sources
Helixi131 – 1333Combined sources
Helixi134 – 14815Combined sources
Helixi155 – 1595Combined sources
Helixi162 – 17413Combined sources
Turni179 – 1824Combined sources
Helixi183 – 19513Combined sources
Helixi197 – 2015Combined sources
Helixi205 – 2084Combined sources
Turni209 – 2124Combined sources
Helixi385 – 40016Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DK8X-ray1.57A74-220[»]
1EMUX-ray1.90A80-211[»]
1O9UX-ray2.40B383-400[»]
3ZDIX-ray2.64B383-400[»]
4B7TX-ray2.77B383-400[»]
4NM0X-ray2.50B383-402[»]
4NM3X-ray2.10B383-402[»]
4NM5X-ray2.30B383-402[»]
4NM7X-ray2.30B383-402[»]
4NU1X-ray2.50B383-402[»]
ProteinModelPortaliO15169.
SMRiO15169. Positions 74-220, 779-862.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO15169.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini88 – 211124RGSPROSITE-ProRule annotationAdd
BLAST
Domaini780 – 86283DIXPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni209 – 338130Interaction with TP53By similarityAdd
BLAST
Regioni348 – 43386Interaction with GSK3BBy similarityAdd
BLAST
Regioni434 – 50269Interaction with CTNNB1By similarityAdd
BLAST
Regioni507 – 757251Interaction with RNF111Add
BLAST
Regioni575 – 789215Interaction with PPP2CAAdd
BLAST
Regioni677 – 75276Interaction with HIPK2By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi20 – 2910Tankyrase-binding motif

Domaini

The tankyrase-binding motif (also named TBD) is required for interaction with tankyrase TNKS and TNKS2.1 Publication

Sequence similaritiesi

Contains 1 DIX domain.PROSITE-ProRule annotation
Contains 1 RGS domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG238205.
GeneTreeiENSGT00390000010011.
HOVERGENiHBG004324.
InParanoidiO15169.
KOiK02157.
OMAiIMQWIIE.
OrthoDBiEOG79PJQ0.
PhylomeDBiO15169.
TreeFamiTF315454.

Family and domain databases

Gene3Di1.10.196.10. 2 hits.
InterProiIPR029797. AXIN1.
IPR014936. Axin_b-cat-bd.
IPR001158. DIX.
IPR016137. RGS.
IPR024066. RGS_subdom1.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERiPTHR10845:SF11. PTHR10845:SF11. 1 hit.
PfamiPF08833. Axin_b-cat_bind. 1 hit.
PF00778. DIX. 1 hit.
PF00615. RGS. 1 hit.
[Graphical view]
PRINTSiPR01301. RGSPROTEIN.
SMARTiSM00021. DAX. 1 hit.
SM00315. RGS. 1 hit.
[Graphical view]
SUPFAMiSSF48097. SSF48097. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50841. DIX. 1 hit.
PS50132. RGS. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O15169-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MNIQEQGFPL DLGASFTEDA PRPPVPGEEG ELVSTDPRPA SYSFCSGKGV
60 70 80 90 100
GIKGETSTAT PRRSDLDLGY EPEGSASPTP PYLKWAESLH SLLDDQDGIS
110 120 130 140 150
LFRTFLKQEG CADLLDFWFA CTGFRKLEPC DSNEEKRLKL ARAIYRKYIL
160 170 180 190 200
DNNGIVSRQT KPATKSFIKG CIMKQLIDPA MFDQAQTEIQ ATMEENTYPS
210 220 230 240 250
FLKSDIYLEY TRTGSESPKV CSDQSSGSGT GKGISGYLPT LNEDEEWKCD
260 270 280 290 300
QDMDEDDGRD AAPPGRLPQK LLLETAAPRV SSSRRYSEGR EFRYGSWREP
310 320 330 340 350
VNPYYVNAGY ALAPATSAND SEQQSLSSDA DTLSLTDSSV DGIPPYRIRK
360 370 380 390 400
QHRREMQESV QVNGRVPLPH IPRTYRVPKE VRVEPQKFAE ELIHRLEAVQ
410 420 430 440 450
RTREAEEKLE ERLKRVRMEE EGEDGDPSSG PPGPCHKLPP APAWHHFPPR
460 470 480 490 500
CVDMGCAGLR DAHEENPESI LDEHVQRVLR TPGRQSPGPG HRSPDSGHVA
510 520 530 540 550
KMPVALGGAA SGHGKHVPKS GAKLDAAGLH HHRHVHHHVH HSTARPKEQV
560 570 580 590 600
EAEATRRAQS SFAWGLEPHS HGARSRGYSE SVGAAPNASD GLAHSGKVGV
610 620 630 640 650
ACKRNAKKAE SGKSASTEVP GASEDAEKNQ KIMQWIIEGE KEISRHRRTG
660 670 680 690 700
HGSSGTRKPQ PHENSRPLSL EHPWAGPQLR TSVQPSHLFI QDPTMPPHPA
710 720 730 740 750
PNPLTQLEEA RRRLEEEEKR ASRAPSKQRY VQEVMRRGRA CVRPACAPVL
760 770 780 790 800
HVVPAVSDME LSETETRSQR KVGGGSAQPC DSIVVAYYFC GEPIPYRTLV
810 820 830 840 850
RGRAVTLGQF KELLTKKGSY RYYFKKVSDE FDCGVVFEEV REDEAVLPVF
860
EEKIIGKVEK VD
Length:862
Mass (Da):95,635
Last modified:May 10, 2002 - v2
Checksum:i10779173F5092F3F
GO
Isoform 2 (identifier: O15169-2) [UniParc]FASTAAdd to basket

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

Show »
Length:826
Mass (Da):91,653
Checksum:i4AA4187D70A5863D
GO

Sequence cautioni

The sequence AAC51624.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti360 – 3601V → A in AAC51624 (PubMed:9230313).Curated
Sequence conflicti451 – 4555CVDMG → LCWTWA in AAC51624 (PubMed:9230313).Curated
Sequence conflicti482 – 4821P → T in AAC51624 (PubMed:9230313).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti106 – 1061L → R in HCC. 1 Publication
VAR_015589
Natural varianti345 – 3451P → L in HCC. 1 Publication
VAR_015590
Natural varianti425 – 4251G → S in HCC. 1 Publication
Corresponds to variant rs116350678 [ dbSNP | Ensembl ].
VAR_015591
Natural varianti650 – 6501G → S in HCC and in hepatoblastoma. 1 Publication
Corresponds to variant rs117208012 [ dbSNP | Ensembl ].
VAR_015592
Natural varianti841 – 8411R → Q in hepatoblastoma. 1 Publication
Corresponds to variant rs34015754 [ dbSNP | Ensembl ].
VAR_015593

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei730 – 76536Missing in isoform 2. 1 PublicationVSP_019398Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS10405.1. [O15169-1]
CCDS10406.1. [O15169-2]
RefSeqiNP_003493.1. NM_003502.3. [O15169-1]
NP_851393.1. NM_181050.2. [O15169-2]
UniGeneiHs.592082.

Genome annotation databases

EnsembliENST00000262320; ENSP00000262320; ENSG00000103126. [O15169-1]
ENST00000354866; ENSP00000346935; ENSG00000103126. [O15169-2]
GeneIDi8312.
KEGGihsa:8312.
UCSCiuc002cgp.2. human. [O15169-1]
uc002cgq.2. human. [O15169-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS10405.1. [O15169-1]
CCDS10406.1. [O15169-2]
RefSeqiNP_003493.1. NM_003502.3. [O15169-1]
NP_851393.1. NM_181050.2. [O15169-2]
UniGeneiHs.592082.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DK8X-ray1.57A74-220[»]
1EMUX-ray1.90A80-211[»]
1O9UX-ray2.40B383-400[»]
3ZDIX-ray2.64B383-400[»]
4B7TX-ray2.77B383-400[»]
4NM0X-ray2.50B383-402[»]
4NM3X-ray2.10B383-402[»]
4NM5X-ray2.30B383-402[»]
4NM7X-ray2.30B383-402[»]
4NU1X-ray2.50B383-402[»]
ProteinModelPortaliO15169.
SMRiO15169. Positions 74-220, 779-862.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113909. 57 interactions.
DIPiDIP-34630N.
IntActiO15169. 66 interactions.
MINTiMINT-100969.
STRINGi9606.ENSP00000262320.

Chemistry

ChEMBLiCHEMBL3038464.

PTM databases

PhosphoSiteiO15169.

Polymorphism and mutation databases

BioMutaiAXIN1.

Proteomic databases

MaxQBiO15169.
PaxDbiO15169.
PRIDEiO15169.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262320; ENSP00000262320; ENSG00000103126. [O15169-1]
ENST00000354866; ENSP00000346935; ENSG00000103126. [O15169-2]
GeneIDi8312.
KEGGihsa:8312.
UCSCiuc002cgp.2. human. [O15169-1]
uc002cgq.2. human. [O15169-2]

Organism-specific databases

CTDi8312.
GeneCardsiGC16M000338.
HGNCiHGNC:903. AXIN1.
HPAiCAB012987.
HPA042412.
MIMi114550. phenotype.
603816. gene.
607864. phenotype.
neXtProtiNX_O15169.
PharmGKBiPA25195.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG238205.
GeneTreeiENSGT00390000010011.
HOVERGENiHBG004324.
InParanoidiO15169.
KOiK02157.
OMAiIMQWIIE.
OrthoDBiEOG79PJQ0.
PhylomeDBiO15169.
TreeFamiTF315454.

Enzyme and pathway databases

ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_11065. Beta-catenin phosphorylation cascade.
REACT_263873. degradation of AXIN.
REACT_263893. truncations of AMER1 destabilize the destruction complex.
REACT_263992. APC truncation mutants have impaired AXIN binding.
REACT_264030. AXIN missense mutants destabilize the destruction complex.
REACT_264034. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_264092. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_264127. T41 mutants of beta-catenin aren't phosphorylated.
REACT_264295. S45 mutants of beta-catenin aren't phosphorylated.
REACT_264581. S33 mutants of beta-catenin aren't phosphorylated.
REACT_264596. TCF dependent signaling in response to WNT.
REACT_264636. S37 mutants of beta-catenin aren't phosphorylated.
SignaLinkiO15169.

Miscellaneous databases

EvolutionaryTraceiO15169.
GeneWikiiAXIN1.
GenomeRNAii8312.
NextBioi31127.
PROiO15169.
SOURCEiSearch...

Gene expression databases

BgeeiO15169.
CleanExiHS_AXIN1.
ExpressionAtlasiO15169. baseline and differential.
GenevisibleiO15169. HS.

Family and domain databases

Gene3Di1.10.196.10. 2 hits.
InterProiIPR029797. AXIN1.
IPR014936. Axin_b-cat-bd.
IPR001158. DIX.
IPR016137. RGS.
IPR024066. RGS_subdom1.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERiPTHR10845:SF11. PTHR10845:SF11. 1 hit.
PfamiPF08833. Axin_b-cat_bind. 1 hit.
PF00778. DIX. 1 hit.
PF00615. RGS. 1 hit.
[Graphical view]
PRINTSiPR01301. RGSPROTEIN.
SMARTiSM00021. DAX. 1 hit.
SM00315. RGS. 1 hit.
[Graphical view]
SUPFAMiSSF48097. SSF48097. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50841. DIX. 1 hit.
PS50132. RGS. 1 hit.
[Graphical view]
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Publicationsi

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  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.
    , 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. 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. Cited for: INTERACTION WITH TNKS, UBIQUITINATION.
  21. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  22. "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.
  23. "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.
  24. "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.

Entry informationi

Entry nameiAXIN1_HUMAN
AccessioniPrimary (citable) accession number: O15169
Secondary accession number(s): Q4TT26
, Q4TT27, Q86YA7, Q8WVW6, Q96S28
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 10, 2002
Last modified: June 24, 2015
This is version 172 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.