Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - O70239 (AXIN1_RAT)

Entry version 164 (08 May 2019)
Sequence version 3 (10 May 2002)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

Axin-1

Gene

Axin1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 beta-catenin to inhibit the Wnt signaling pathway and ventralize embryos, but also dorsalizes embryos by activating a Wnt-independent JNK signaling pathway (By similarity). Also facilitates the phosphorylation of APC by GSK3B (By similarity). Facilitates the phosphorylation of TP53 by HIPK2 upon ultraviolet irradiation (By similarity). Enhances TGF-beta signaling by recruiting the RNF111 E3 ubiquitin ligase and promoting the degradation of inhibitory SMAD7 (By similarity).By similarity

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDevelopmental protein
Biological processApoptosis, Wnt signaling pathway

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Axin-1
Alternative name(s):
Axis inhibition protein 1
Short name:
rAxin
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Axin1
Synonyms:Axin
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Rat genome database

More...RGDi		620859 Axin1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002208901 – 827Axin-1Add BLAST827

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei75Phosphoserine; by CK1By similarity1
Modified residuei77Phosphoserine; by CK1By similarity1
Modified residuei217Phosphoserine; by CK1By similarity1
Modified residuei468Phosphoserine; by CK1By similarity1
Modified residuei480Phosphothreonine; by GSK3-betaBy similarity1
Modified residuei485Phosphoserine; by GSK3-betaBy similarity1
Modified residuei492PhosphoserineBy similarity1
Modified residuei509PhosphoserineBy similarity1
Modified residuei578PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		O70239

PRoteomics IDEntifications database

More...PRIDEi		O70239

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		O70239

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		O70239

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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 (By similarity). 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 (By similarity). Also binds ANKRD6, PIAS1, PIAS2, PIAS4, MAP3K1, MAP3K4, SUMO1, SMAD6, SMAD7 and RNF111 (By similarity). Interacts with DIXDC1; the interaction prevents interaction with MAP3K1 (By similarity). Interacts with MDFI; the interaction decreases AXIN1-mediated JUN N-terminal kinase (JNK) activation (By similarity). Interacts with MDFIC; the interaction inhibits beta-cateninin-mediated signaling and AXIN1-mediated JUN N-terminal kinase (JNK) activation (By similarity). Interacts with LRP5 (via its phosphorylated PPPSP motifs); the interaction is stimulated by WNT1 and GSK3B and activates beta-catenin signaling (By similarity). Interacts (via the C-terminal) with PPP1CA; the interaction dephosphorylates AXIN1 and regulates interaction with GSK3B (By similarity). 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 (By similarity). Interacts with CTNNB1 (via the armadillo repeats 2-7) (By similarity). Interacts with GSK3B; the interaction hyperphosphorylates CTNNB1 leading to its ubiquitination and destruction (PubMed:9482734, PubMed:16815997). Interacts with MACF1 (PubMed:16815997). Found in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B (PubMed:16815997). Interacts with TNKS (By similarity). Interacts with DAB2; the interaction is mutually exclusive with the AXIN1:PPP1CA interaction (By similarity). Interacts with WDR26 (By similarity). Interacts with GID8 (By similarity).By similarity2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		249455, 9 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		O70239

Database of interacting proteins

More...DIPi		DIP-29400N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		O70239

Protein interaction database and analysis system

More...IntActi		O70239, 10 interactors

Molecular INTeraction database

More...MINTi		O70239

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000027705

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1827
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WSPX-ray2.90A/B/C744-827[»]
2D5GX-ray3.20A/B/C/D/E/F743-827[»]

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		O70239

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		O70239

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini88 – 211RGSPROSITE-ProRule annotationAdd BLAST124
Domaini745 – 827DIXPROSITE-ProRule annotationAdd BLAST83

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni209 – 338Interaction with TP53By similarityAdd BLAST130
Regioni348 – 432Interaction with GSK3B1 PublicationAdd BLAST85
Regioni433 – 501Interaction with CTNNB1Add BLAST69

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi20 – 29Tankyrase-binding motif10

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3589 Eukaryota
ENOG410YMJD LUCA

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		O70239

KEGG Orthology (KO)

More...KOi		K02157

Family and domain databases

Conserved Domains Database

More...CDDi		cd11582 Axin_TNKS_binding, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.196.10, 2 hits
3.10.20.380, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR029797 AXIN1
IPR014936 Axin_b-cat-bd
IPR032101 Axin_TNKS-bd
IPR001158 DIX
IPR038207 DIX_dom_sf
IPR016137 RGS
IPR036305 RGS_sf
IPR024066 RGS_subdom1/3
IPR029071 Ubiquitin-like_domsf

The PANTHER Classification System

More...PANTHERi		PTHR46102:SF3 PTHR46102:SF3, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF16646 AXIN1_TNKS_BD, 1 hit
PF08833 Axin_b-cat_bind, 1 hit
PF00778 DIX, 1 hit
PF00615 RGS, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01301 RGSPROTEIN

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00021 DAX, 1 hit
SM00315 RGS, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48097 SSF48097, 1 hit
SSF54236 SSF54236, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50841 DIX, 1 hit
PS50132 RGS, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iBB1EE9CCECF6D487
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

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

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AF017756 mRNA Translation: AAC40066.1 Different initiation.

Protein sequence database of the Protein Information Resource

More...PIRi		T08422

NCBI Reference Sequences

More...RefSeqi		NP_077381.1, NM_024405.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		79257

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:79257

UCSC genome browser

More...UCSCi		RGD:620859 rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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

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[»]
SMRiO70239
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249455, 9 interactors
CORUMiO70239
DIPiDIP-29400N
ELMiO70239
IntActiO70239, 10 interactors
MINTiO70239
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

Comparative Toxicogenomics Database

More...CTDi		8312
RGDi620859 Axin1

Phylogenomic databases

eggNOGiKOG3589 Eukaryota
ENOG410YMJD LUCA
InParanoidiO70239
KOiK02157

Miscellaneous databases

EvolutionaryTraceiO70239

Protein Ontology

More...PROi		PR:O70239

Family and domain databases

CDDicd11582 Axin_TNKS_binding, 1 hit
Gene3Di1.10.196.10, 2 hits
3.10.20.380, 1 hit
InterProiView protein in InterPro
IPR029797 AXIN1
IPR014936 Axin_b-cat-bd
IPR032101 Axin_TNKS-bd
IPR001158 DIX
IPR038207 DIX_dom_sf
IPR016137 RGS
IPR036305 RGS_sf
IPR024066 RGS_subdom1/3
IPR029071 Ubiquitin-like_domsf
PANTHERiPTHR46102:SF3 PTHR46102:SF3, 1 hit
PfamiView protein in Pfam
PF16646 AXIN1_TNKS_BD, 1 hit
PF08833 Axin_b-cat_bind, 1 hit
PF00778 DIX, 1 hit
PF00615 RGS, 1 hit
PRINTSiPR01301 RGSPROTEIN
SMARTiView protein in SMART
SM00021 DAX, 1 hit
SM00315 RGS, 1 hit
SUPFAMiSSF48097 SSF48097, 1 hit
SSF54236 SSF54236, 1 hit
PROSITEiView protein in PROSITE
PS50841 DIX, 1 hit
PS50132 RGS, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAXIN1_RAT
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O70239
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 10, 2002
Last modified: May 8, 2019
This is version 164 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again