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Protein

Axin-1

Gene

Axin1

Organism
Rattus norvegicus (Rat)
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 beta-catenin to inhibit the Wnt signaling pathway and ventralize embryos, but also dorsalizes embryos by activating a Wnt-independent JNK signaling pathway. Also facilitates the phosphorylation of APC by GSK3B. 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).By similarity

GO - Molecular functioni

  • armadillo repeat domain binding Source: BHF-UCL
  • beta-catenin binding Source: BHF-UCL
  • GTPase activator activity Source: GO_Central
  • identical protein binding Source: IntAct
  • protein domain specific binding Source: RGD
  • protein homodimerization activity Source: UniProtKB
  • protein kinase binding Source: BHF-UCL
  • receptor binding Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Apoptosis, Wnt signaling pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Axin-1
Alternative name(s):
Axis inhibition protein 1
Short name:
rAxin
Gene namesi
Name:Axin1
Synonyms:Axin
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620859. Axin1.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity
  • Cell membrane 1 Publication
  • Membrane By similarity

  • Note: On UV irradiation, translocates to the nucleus and colocalizes with DAAX (By similarity). MACF1 is required for its translocation to cell membrane (By similarity).By similarity

GO - Cellular componenti

  • beta-catenin destruction complex Source: BHF-UCL
  • cell cortex Source: GO_Central
  • cytoplasmic, membrane-bounded vesicle Source: GO_Central
  • cytoplasmic microtubule Source: GO_Central
  • cytoplasmic vesicle Source: BHF-UCL
  • nucleus Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB
  • postsynaptic density Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002208901 – 827Axin-1Add BLAST827

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei75Phosphoserine; by CK1By similarity1
Modified residuei77Phosphoserine; by CK1By similarity1
Modified residuei217Phosphoserine; by CK1By similarity1
Modified residuei468Phosphoserine; by CK1By similarity1
Modified residuei480Phosphothreonine; by GSK3-beta1 Publication1
Modified residuei485Phosphoserine; by GSK3-betaBy similarity1
Modified residuei492PhosphoserineBy similarity1
Modified residuei509PhosphoserineBy similarity1
Modified residuei578PhosphoserineBy similarity1
Cross-linki822Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki825Glycyl 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. Also phosphorylated by CDK2 which regulates interaction with CTNBB1 (By similarity).By similarity
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).By similarity
Ubiquitinated by RNF146 when poly-ADP-ribosylated, leading to its degradation and subsequent activation of the Wnt signaling pathway. Sumoylation at Lys-858 and Lys-861 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 (By similarity).By similarity

Keywords - PTMi

ADP-ribosylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiO70239.
PRIDEiO70239.

PTM databases

iPTMnetiO70239.
PhosphoSitePlusiO70239.

Expressioni

Tissue specificityi

Highly expressed in testis, thymus and lung. Less expression in cerebrum, cerebellum, heart, kidney, skeletal muscle, spleen and liver.1 Publication

Gene expression databases

BgeeiENSRNOG00000020414.

Interactioni

Subunit structurei

Homodimer (By similarity). 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 AXIN1-HIPK2-TP53 complex (By similarity). 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 ANKRD6, PIAS1, PIAS2, PIAS4, MAP3K1, MAP3K4, SUMO1, SMAD6, SMAD7 and RNF111. Interacts with DIXDC1; the interaction prevents interaction with MAP3K1. 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 (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. Interacts with MACF1. Found in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B. Interacts with TNKS. Interacts with DAB2; the interaction is mutually exclusive with the AXIN1:PPP1CA interaction (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-6857773,EBI-6857773
AMMECR1Q9Y4X03EBI-6857773,EBI-8583355From a different organism.
CAV1Q031355EBI-6857773,EBI-603614From a different organism.
CSNK1EP496747EBI-6857773,EBI-749343From a different organism.
DVL1O1464012EBI-6857773,EBI-723489From a different organism.
LRP6O7558112EBI-6857773,EBI-910915From a different organism.

GO - Molecular functioni

  • armadillo repeat domain binding Source: BHF-UCL
  • beta-catenin binding Source: BHF-UCL
  • identical protein binding Source: IntAct
  • protein domain specific binding Source: RGD
  • protein homodimerization activity Source: UniProtKB
  • protein kinase binding Source: BHF-UCL
  • receptor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi249455. 9 interactors.
IntActiO70239. 10 interactors.
MINTiMINT-1532436.
STRINGi10116.ENSRNOP00000027705.

Structurei

Secondary structure

1827
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi748 – 754Combined sources7
Beta strandi761 – 768Combined sources8
Helixi772 – 778Combined sources7
Beta strandi785 – 792Combined sources8
Beta strandi799 – 805Combined sources7
Beta strandi818 – 825Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WSPX-ray2.90A/B/C744-827[»]
2D5GX-ray3.20A/B/C/D/E/F743-827[»]
ProteinModelPortaliO70239.
SMRiO70239.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO70239.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini88 – 211RGSPROSITE-ProRule annotationAdd BLAST124
Domaini745 – 827DIXPROSITE-ProRule annotationAdd BLAST83

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni209 – 338Interaction with TP53By similarityAdd BLAST130
Regioni348 – 432Interaction with GSK3B1 PublicationAdd BLAST85
Regioni433 – 501Interaction with CTNNB1Add BLAST69

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi20 – 29Tankyrase-binding motif10

Domaini

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

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG3589. Eukaryota.
ENOG410YMJD. LUCA.
HOVERGENiHBG004324.
InParanoidiO70239.
KOiK02157.

Family and domain databases

CDDicd11582. Axin_TNKS_binding. 1 hit.
Gene3Di1.10.196.10. 2 hits.
InterProiIPR029797. AXIN1.
IPR014936. Axin_b-cat-bd.
IPR032101. Axin_TNKS-bd.
IPR001158. DIX.
IPR016137. RGS.
IPR024066. RGS_subdom1.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERiPTHR10845:SF11. PTHR10845:SF11. 1 hit.
PfamiPF16646. AXIN1_TNKS_BD. 1 hit.
PF08833. 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]

Sequencei

Sequence statusi: Complete.

O70239-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNVQEQGFPL DLGASFTEDA PRPPVPGEEG ELVSTDSRPV NHSFCSGKGT
60 70 80 90 100
SIKSETSTAT PRRSDLDLGY EPEGSASPTP PYLRWAESLH SLLDDQDGIS
110 120 130 140 150
LFRTFLKQEG CADLLDFWFA CSGFRKLEPC DSNEEKRLKL ARAIYRKYIL
160 170 180 190 200
DSNGIVSRQT KPATKSFIKD CVMKQQIDPA MFDQAQTEIQ STMEENTYPS
210 220 230 240 250
FLKSDIYLEY TRTGSESPKV CSDQSSGSGT GKGMSGYLPT LNEDEEWKCD
260 270 280 290 300
QDADEDDGRD SVPPSRLTQK LLLETAAPRA PSSRRYNEGR ELRYGSWREP
310 320 330 340 350
VNPYYVNSGY ALAPATSAND SEQQSLSSDA DTLSLTDSSV DGIPPYRIRK
360 370 380 390 400
QHRREMQESV QVNGRVPLPH IPRTYRMPKE IRVEPQKFAE ELIHRLEAVQ
410 420 430 440 450
RTREAEEKLE ERLKRVRMEE EGEDGEMPSG PMASHKLPSV PAWHHFPPRY
460 470 480 490 500
VDMGCSGLRD AHEENPESIL DEHVQRVMRT PGCQSPGPGH RSPDSGHVAK
510 520 530 540 550
TAVLGGTASG HGKHAPKLGL KLDSAGLHHH RHVHHHVHHN SARPKEQMEA
560 570 580 590 600
EAARRVQSSF SWGPETHGHA KPRSYSESTG TNPSAGDLAF GGKASAPSKR
610 620 630 640 650
NTKKAESGKN ASAEVPSTTE DAEKNQKIMQ WIIEGEKEIS RHRKAGHGSS
660 670 680 690 700
GMRKQQAHES SRPLSIERPG AVHPWVSAQL RNSVQPSHLF IQDPTMPPNP
710 720 730 740 750
APNPLTQLEE ARRRLEEEEK RANKLPSKQR TKSQRKAGGG SAPPCDSIVV
760 770 780 790 800
AYYFCGEPIP YRTLVRGRAV TLGQFKELLT KKGSYRYYFK KVSDEFDCGV
810 820
VFEEVREDEA ILPVFEEKII GKVEKVD
Length:827
Mass (Da):92,285
Last modified:May 10, 2002 - v3
Checksum:iBB1EE9CCECF6D487
GO

Sequence cautioni

The sequence AAC40066 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF017756 mRNA. Translation: AAC40066.1. Different initiation.
PIRiT08422.
RefSeqiNP_077381.1. NM_024405.1.
UniGeneiRn.31781.

Genome annotation databases

GeneIDi79257.
KEGGirno:79257.
UCSCiRGD:620859. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF017756 mRNA. Translation: AAC40066.1. Different initiation.
PIRiT08422.
RefSeqiNP_077381.1. NM_024405.1.
UniGeneiRn.31781.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WSPX-ray2.90A/B/C744-827[»]
2D5GX-ray3.20A/B/C/D/E/F743-827[»]
ProteinModelPortaliO70239.
SMRiO70239.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249455. 9 interactors.
IntActiO70239. 10 interactors.
MINTiMINT-1532436.
STRINGi10116.ENSRNOP00000027705.

PTM databases

iPTMnetiO70239.
PhosphoSitePlusiO70239.

Proteomic databases

PaxDbiO70239.
PRIDEiO70239.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi79257.
KEGGirno:79257.
UCSCiRGD:620859. rat.

Organism-specific databases

CTDi8312.
RGDi620859. Axin1.

Phylogenomic databases

eggNOGiKOG3589. Eukaryota.
ENOG410YMJD. LUCA.
HOVERGENiHBG004324.
InParanoidiO70239.
KOiK02157.

Miscellaneous databases

EvolutionaryTraceiO70239.
PROiO70239.

Gene expression databases

BgeeiENSRNOG00000020414.

Family and domain databases

CDDicd11582. Axin_TNKS_binding. 1 hit.
Gene3Di1.10.196.10. 2 hits.
InterProiIPR029797. AXIN1.
IPR014936. Axin_b-cat-bd.
IPR032101. Axin_TNKS-bd.
IPR001158. DIX.
IPR016137. RGS.
IPR024066. RGS_subdom1.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERiPTHR10845:SF11. PTHR10845:SF11. 1 hit.
PfamiPF16646. AXIN1_TNKS_BD. 1 hit.
PF08833. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiAXIN1_RAT
AccessioniPrimary (citable) accession number: O70239
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 10, 2002
Last modified: November 2, 2016
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.