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Protein

Axin-1

Gene

Axin1

Organism
Mus musculus (Mouse)
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 (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.By similarity3 Publications

GO - Molecular functioni

  • armadillo repeat domain binding Source: GO_Central
  • beta-catenin binding Source: MGI
  • enzyme binding Source: MGI
  • GTPase activator activity Source: GO_Central
  • identical protein binding Source: MGI
  • I-SMAD binding Source: BHF-UCL
  • p53 binding Source: MGI
  • protein complex scaffold Source: BHF-UCL
  • protein C-terminus binding Source: MGI
  • protein domain specific binding Source: MGI
  • protein homodimerization activity Source: UniProtKB
  • protein kinase binding Source: ParkinsonsUK-UCL
  • protein self-association Source: MGI
  • R-SMAD binding Source: MGI
  • signal transducer activity Source: MGI
  • SMAD binding Source: MGI
  • ubiquitin protein ligase binding Source: BHF-UCL

GO - Biological processi

  • activation of JUN kinase activity Source: GO_Central
  • activation of protein kinase activity Source: MGI
  • apoptotic process Source: UniProtKB-KW
  • axial mesoderm development Source: MGI
  • axial mesoderm formation Source: MGI
  • beta-catenin destruction complex disassembly Source: Reactome
  • canonical Wnt signaling pathway Source: MGI
  • canonical Wnt signaling pathway involved in neural plate anterior/posterior pattern formation Source: GO_Central
  • cell death Source: GO_Central
  • cellular protein complex assembly Source: MGI
  • cellular response to organic cyclic compound Source: GO_Central
  • cytoplasmic microtubule organization Source: MGI
  • determination of left/right symmetry Source: GO_Central
  • dorsal/ventral axis specification Source: MGI
  • dorsal/ventral pattern formation Source: MGI
  • embryonic eye morphogenesis Source: GO_Central
  • forebrain anterior/posterior pattern specification Source: GO_Central
  • genetic imprinting Source: MGI
  • head development Source: MGI
  • in utero embryonic development Source: MGI
  • muscle cell development Source: GO_Central
  • negative regulation of canonical Wnt signaling pathway Source: MGI
  • negative regulation of fat cell differentiation Source: MGI
  • negative regulation of protein metabolic process Source: MGI
  • negative regulation of transcription elongation from RNA polymerase II promoter Source: MGI
  • negative regulation of Wnt signaling pathway Source: MGI
  • nucleocytoplasmic transport Source: MGI
  • olfactory placode formation Source: GO_Central
  • optic placode formation Source: GO_Central
  • positive regulation of JNK cascade Source: UniProtKB
  • positive regulation of JUN kinase activity Source: MGI
  • positive regulation of peptidyl-serine phosphorylation Source: ParkinsonsUK-UCL
  • positive regulation of peptidyl-threonine phosphorylation Source: ParkinsonsUK-UCL
  • positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: MGI
  • positive regulation of protein catabolic process Source: MGI
  • positive regulation of protein kinase activity Source: CACAO
  • positive regulation of protein phosphorylation Source: MGI
  • positive regulation of protein ubiquitination Source: MGI
  • positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: MGI
  • positive regulation of transcription, DNA-templated Source: BHF-UCL
  • positive regulation of transforming growth factor beta receptor signaling pathway Source: MGI
  • positive regulation of ubiquitin-protein transferase activity Source: BHF-UCL
  • post-anal tail morphogenesis Source: MGI
  • protein catabolic process Source: MGI
  • protein homooligomerization Source: MGI
  • protein polyubiquitination Source: MGI
  • regulation of catenin import into nucleus Source: MGI
  • regulation of protein phosphorylation Source: MGI
  • sensory perception of sound Source: MGI
  • Wnt-activated signaling pathway involved in forebrain neuron fate commitment Source: GO_Central
  • Wnt signaling pathway Source: MGI
  • Wnt signaling pathway involved in somitogenesis Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Apoptosis, Wnt signaling pathway

Enzyme and pathway databases

ReactomeiR-MMU-4641262. Disassembly of the destruction complex and recruitment of AXIN to the membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Axin-1
Alternative name(s):
Axis inhibition protein 1
Protein Fused
Gene namesi
Name:Axin1
Synonyms:Axin, Fu
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1096327. Axin1.

Subcellular locationi

GO - Cellular componenti

  • beta-catenin destruction complex Source: ParkinsonsUK-UCL
  • cell cortex Source: MGI
  • cell periphery Source: MGI
  • cytoplasm Source: BHF-UCL
  • cytoplasmic, membrane-bounded vesicle Source: MGI
  • cytosol Source: Reactome
  • lateral plasma membrane Source: MGI
  • nucleus Source: MGI
  • perinuclear region of cytoplasm Source: MGI
  • plasma membrane Source: UniProtKB
  • postsynaptic density Source: GO_Central
  • protein complex Source: MGI
  • Wnt signalosome Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi480T → A: Greatly reduced GSK3B-mediated phosphorylation; when associated with A-485 and A-492. 1 Publication1
Mutagenesisi485S → A: Greatly reduced GSK3B-mediated phosphorylation and large effect on the inhibitory activity in Wnt-signaling; when associated with A-480 and A-492. 1 Publication1
Mutagenesisi492S → A: Greatly reduced GSK3B-mediated phosphorylation; when associated with A-480 and A-485. 1 Publication1
Mutagenesisi492S → I: Little effect on inhibitory activity on Wnt-signaling. 1 Publication1
Mutagenesisi495S → A: No effect on phosphorylation. Little effect on inhibitory activity on Wnt-signaling. 1 Publication1
Mutagenesisi858 – 863Missing : Abolishes binding of PIAS1 and PIAS2. Dramatically reduces sumoylation and abolishes AXIN1-mediated JNK activation. No effect on homodimerization nor on Wnt-signaling. 1 Publication6
Mutagenesisi858K → A: Decreased sumoylation followed by increased ubiquitination; when associated with A-861. 1 Publication1
Mutagenesisi861K → A: Decreased sumoylation followed by increased ubiquitination; when associated with A-858. 1 Publication1

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002208891 – 863Axin-1Add BLAST863

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei75PhosphoserineCombined sources1
Modified residuei77Phosphoserine; by CK1By similarity1
Modified residuei217PhosphoserineCombined sources1
Modified residuei468Phosphoserine; by CK1By similarity1
Modified residuei480Phosphothreonine; by GSK3-beta1 Publication1
Modified residuei485Phosphoserine; by GSK3-beta1 Publication1
Modified residuei492Phosphoserine1 Publication1
Modified residuei509PhosphoserineBy similarity1
Cross-linki858Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)2 Publications
Cross-linki861Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)2 Publications

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 (By similarity). Also phosphorylated by CDK2 which regulates interaction with CTNBB1.By similarity2 Publications
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. 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.By similarity2 Publications

Keywords - PTMi

ADP-ribosylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiO35625.
PRIDEiO35625.

PTM databases

iPTMnetiO35625.
PhosphoSitePlusiO35625.

Expressioni

Tissue specificityi

Expressed in embryonic stem cells.

Developmental stagei

Widely expressed at E10.5 to E16.5 day.

Gene expression databases

BgeeiENSMUSG00000024182.
CleanExiMM_AXIN1.

Interactioni

Subunit structurei

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.By similarity10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CTNNB1P352224EBI-2365912,EBI-491549From a different organism.
Dab2P980784EBI-2365912,EBI-1391846
Dvl3Q610622EBI-2365912,EBI-1538450
GSK3BP498415EBI-2365912,EBI-373586From a different organism.
LRP6O755812EBI-2365912,EBI-910915From a different organism.
Ppp1caP621372EBI-2365912,EBI-357187
Rnf111Q99ML94EBI-2365912,EBI-646015
Smad3Q8BUN52EBI-2365912,EBI-2337983
Smad6O351822EBI-2365912,EBI-4321242
Smad7O352532EBI-2365912,EBI-5274835
TGIF1Q155832EBI-2365912,EBI-714215From a different organism.
TNKSO952714EBI-2365912,EBI-1105254From a different organism.
Wwtr1Q9EPK54EBI-2365912,EBI-1211920
YAP1P469373EBI-2365912,EBI-1044059From a different organism.

GO - Molecular functioni

  • armadillo repeat domain binding Source: GO_Central
  • beta-catenin binding Source: MGI
  • enzyme binding Source: MGI
  • identical protein binding Source: MGI
  • I-SMAD binding Source: BHF-UCL
  • p53 binding Source: MGI
  • protein complex scaffold Source: BHF-UCL
  • protein C-terminus binding Source: MGI
  • protein domain specific binding Source: MGI
  • protein homodimerization activity Source: UniProtKB
  • protein kinase binding Source: ParkinsonsUK-UCL
  • protein self-association Source: MGI
  • R-SMAD binding Source: MGI
  • SMAD binding Source: MGI
  • ubiquitin protein ligase binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi198287. 35 interactors.
DIPiDIP-42637N.
IntActiO35625. 27 interactors.
MINTiMINT-1543084.
STRINGi10090.ENSMUSP00000073974.

Structurei

Secondary structure

1863
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi64 – 66Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UTMX-ray2.00C1-80[»]
ProteinModelPortaliO35625.
SMRiO35625.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini88 – 211RGSPROSITE-ProRule annotationAdd BLAST124
Domaini781 – 863DIXPROSITE-ProRule annotationAdd BLAST83

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni209 – 338Interaction with TP531 PublicationAdd BLAST130
Regioni348 – 432Interaction with GSK3BBy similarityAdd BLAST85
Regioni433 – 501Interaction with beta-cateninBy similarityAdd BLAST69
Regioni505 – 758Interaction with RNF111By similarityAdd BLAST254
Regioni572 – 790Interaction with PPP2CABy similarityAdd BLAST219
Regioni678 – 753Interaction with HIPK21 PublicationAdd BLAST76

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.
InParanoidiO35625.
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]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: O35625-1) [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
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 PLPPSRLTQK LLLETAAPRA PSSRRYNEGR ELRYGSWREP
310 320 330 340 350
VNPYYVNSGY ALAPATSAND SEQQSLSSDA DTLSLTDSSV DGIPPYRIRK
360 370 380 390 400
QHRREMQESI 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 HGKHVPKLGL KLDTAGLHHH RHVHHHVHHN SARPKEQMEA
560 570 580 590 600
EVARRVQSSF SWGPETHGHA KPRSYSENAG TTLSAGDLAF GGKTSAPSKR
610 620 630 640 650
NTKKAESGKN ANAEVPSTTE DAEKNQKIMQ WIIEGEKEIS RHRKAGHGSS
660 670 680 690 700
GLRKQQAHES SRPLSIERPG AVHPWVSAQL RNSVQPSHLF IQDPTMPPNP
710 720 730 740 750
APNPLTQLEE ARRRLEEEEK RANKLPSKQR YVQAVMQRGR TCVRPACAPV
760 770 780 790 800
LSVVPAVSDL ELSETETKSQ RKAGGGSAPP CDSIVVAYYF CGEPIPYRTL
810 820 830 840 850
VRGRAVTLGQ FKELLTKKGS YRYYFKKVSD EFDCGVVFEE VREDEAVLPV
860
FEEKIIGKVE KVD
Length:863
Mass (Da):96,276
Last modified:October 3, 2012 - v3
Checksum:i2216D66E92387B81
GO
Isoform 2 (identifier: O35625-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     731-766: Missing.

Show »
Length:827
Mass (Da):92,418
Checksum:i0D99A235EEDC597E
GO

Sequence cautioni

The sequence AAC53285 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti589A → P in AAC53285 (PubMed:9230313).Curated1
Sequence conflicti787A → G in AAC53285 (PubMed:9230313).Curated1
Sequence conflicti846A → P in AAC53285 (PubMed:9230313).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_000452731 – 766Missing in isoform 2. 1 PublicationAdd BLAST36

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF009011 mRNA. Translation: AAC53285.1. Different initiation.
AC126438 Genomic DNA. No translation available.
AC140047 Genomic DNA. No translation available.
RefSeqiNP_033863.2. NM_009733.2.
UniGeneiMm.23684.

Genome annotation databases

GeneIDi12005.
KEGGimmu:12005.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF009011 mRNA. Translation: AAC53285.1. Different initiation.
AC126438 Genomic DNA. No translation available.
AC140047 Genomic DNA. No translation available.
RefSeqiNP_033863.2. NM_009733.2.
UniGeneiMm.23684.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UTMX-ray2.00C1-80[»]
ProteinModelPortaliO35625.
SMRiO35625.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198287. 35 interactors.
DIPiDIP-42637N.
IntActiO35625. 27 interactors.
MINTiMINT-1543084.
STRINGi10090.ENSMUSP00000073974.

PTM databases

iPTMnetiO35625.
PhosphoSitePlusiO35625.

Proteomic databases

PaxDbiO35625.
PRIDEiO35625.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi12005.
KEGGimmu:12005.

Organism-specific databases

CTDi8312.
MGIiMGI:1096327. Axin1.

Phylogenomic databases

eggNOGiKOG3589. Eukaryota.
ENOG410YMJD. LUCA.
HOVERGENiHBG004324.
InParanoidiO35625.
KOiK02157.

Enzyme and pathway databases

ReactomeiR-MMU-4641262. Disassembly of the destruction complex and recruitment of AXIN to the membrane.

Miscellaneous databases

ChiTaRSiAxin1. mouse.
PROiO35625.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000024182.
CleanExiMM_AXIN1.

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_MOUSE
AccessioniPrimary (citable) accession number: O35625
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: October 3, 2012
Last modified: November 30, 2016
This is version 166 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.