Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O15169

- AXIN1_HUMAN

UniProt

O15169 - AXIN1_HUMAN

Protein

Axin-1

Gene

AXIN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 2 (10 May 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    1. armadillo repeat domain binding Source: BHF-UCL
    2. beta-catenin binding Source: BHF-UCL
    3. enzyme binding Source: UniProtKB
    4. GTPase activator activity Source: RefGenome
    5. identical protein binding Source: BHF-UCL
    6. I-SMAD binding Source: BHF-UCL
    7. protein binding Source: UniProtKB
    8. protein complex scaffold Source: BHF-UCL
    9. protein homodimerization activity Source: UniProtKB
    10. protein kinase binding Source: BHF-UCL
    11. signal transducer activity Source: BHF-UCL
    12. SMAD binding Source: BHF-UCL
    13. ubiquitin protein ligase binding Source: UniProtKB

    GO - Biological processi

    1. activation of JUN kinase activity Source: RefGenome
    2. activation of protein kinase activity Source: BHF-UCL
    3. apoptotic process Source: UniProtKB-KW
    4. axial mesoderm formation Source: RefGenome
    5. canonical Wnt signaling pathway Source: UniProtKB
    6. canonical Wnt signaling pathway involved in neural plate anterior/posterior pattern formation Source: RefGenome
    7. cell death Source: RefGenome
    8. cellular protein complex assembly Source: BHF-UCL
    9. cellular response to organic cyclic compound Source: RefGenome
    10. cytoplasmic microtubule organization Source: RefGenome
    11. determination of left/right symmetry Source: RefGenome
    12. dorsal/ventral axis specification Source: RefGenome
    13. embryonic eye morphogenesis Source: RefGenome
    14. embryonic skeletal joint morphogenesis Source: RefGenome
    15. forebrain anterior/posterior pattern specification Source: RefGenome
    16. genetic imprinting Source: Ensembl
    17. in utero embryonic development Source: Ensembl
    18. muscle cell development Source: RefGenome
    19. negative regulation of canonical Wnt signaling pathway Source: RefGenome
    20. negative regulation of fat cell differentiation Source: RefGenome
    21. negative regulation of protein metabolic process Source: Ensembl
    22. negative regulation of transcription elongation from RNA polymerase II promoter Source: Ensembl
    23. negative regulation of Wnt signaling pathway Source: BHF-UCL
    24. nucleocytoplasmic transport Source: Ensembl
    25. olfactory placode formation Source: RefGenome
    26. optic placode formation Source: RefGenome
    27. positive regulation of GTPase activity Source: GOC
    28. positive regulation of JNK cascade Source: UniProtKB
    29. positive regulation of peptidyl-serine phosphorylation Source: BHF-UCL
    30. positive regulation of peptidyl-threonine phosphorylation Source: BHF-UCL
    31. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: Ensembl
    32. positive regulation of protein catabolic process Source: BHF-UCL
    33. positive regulation of protein phosphorylation Source: BHF-UCL
    34. positive regulation of protein ubiquitination Source: BHF-UCL
    35. positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: BHF-UCL
    36. positive regulation of transcription, DNA-templated Source: BHF-UCL
    37. positive regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
    38. positive regulation of ubiquitin-protein transferase activity Source: BHF-UCL
    39. post-anal tail morphogenesis Source: Ensembl
    40. protein catabolic process Source: Ensembl
    41. protein homooligomerization Source: Ensembl
    42. protein polyubiquitination Source: Ensembl
    43. regulation of catenin import into nucleus Source: RefGenome
    44. sensory perception of sound Source: Ensembl
    45. termination of G-protein coupled receptor signaling pathway Source: InterPro
    46. Wnt-activated signaling pathway involved in forebrain neuron fate commitment Source: RefGenome
    47. Wnt signaling pathway involved in somitogenesis Source: RefGenome

    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_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    REACT_200766. degradation of AXIN.
    REACT_200777. TCF dependent signaling in response to WNT.
    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: 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

    1. beta-catenin destruction complex Source: UniProtKB
    2. cell cortex Source: RefGenome
    3. cell periphery Source: BHF-UCL
    4. cytoplasm Source: UniProtKB
    5. cytoplasmic membrane-bounded vesicle Source: RefGenome
    6. cytoplasmic microtubule Source: RefGenome
    7. cytoplasmic vesicle Source: BHF-UCL
    8. cytosol Source: Reactome
    9. Golgi apparatus Source: Ensembl
    10. lateral plasma membrane Source: MGI
    11. nucleus Source: UniProtKB
    12. perinuclear region of cytoplasm Source: BHF-UCL
    13. postsynaptic density Source: RefGenome

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Hepatocellular carcinoma (HCC) [MIM:114550]: A primary malignant neoplasm of epithelial liver cells. The major risk factors for HCC are chronic hepatitis B virus (HBV) infection, chronic hepatitis C virus (HCV) infection, prolonged dietary aflatoxin exposure, alcoholic cirrhosis, and cirrhosis due to other causes.1 Publication
    Note: The gene represented in this entry is involved in disease pathogenesis.
    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) [MIM:607864]: A condition characterized by the occurrence of duplications of different organs in the caudal region.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry. Caudal duplication anomaly is associated with hypermethylation of the AXIN1 promoter.

    Keywords - Diseasei

    Disease mutation, Tumor suppressor

    Organism-specific databases

    MIMi114550. phenotype.
    607864. phenotype.
    PharmGKBiPA25195.

    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 CK12 Publications
    Modified residuei77 – 771Phosphoserine; by CK12 Publications
    Modified residuei217 – 2171Phosphoserine; by CK12 Publications
    Modified residuei469 – 4691Phosphoserine; by CK12 Publications
    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

    ArrayExpressiO15169.
    BgeeiO15169.
    CleanExiHS_AXIN1.
    GenevestigatoriO15169.

    Organism-specific databases

    HPAiCAB012987.

    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
    CTNNB1P3522226EBI-710484,EBI-491549
    Ctnnb1Q022485EBI-710484,EBI-397872From a different organism.
    DAB2IPQ5VWQ8-22EBI-710484,EBI-9543020
    FBXW11Q9UKB14EBI-710484,EBI-355189
    GSK3AP498402EBI-710484,EBI-1044067
    GSK3BP4984132EBI-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

    Protein-protein interaction databases

    BioGridi113909. 56 interactions.
    DIPiDIP-34630N.
    IntActiO15169. 63 interactions.
    MINTiMINT-100969.
    STRINGi9606.ENSP00000262320.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOVERGENiHBG004324.
    InParanoidiO15169.
    KOiK02157.
    OMAiIMQWIIE.
    OrthoDBiEOG79PJQ0.
    PhylomeDBiO15169.
    TreeFamiTF315454.

    Family and domain databases

    Gene3Di1.10.196.10. 2 hits.
    InterProiIPR014936. Axin_b-cat-bd.
    IPR001158. DIX.
    IPR024066. Regulat_G_prot_signal_dom1.
    IPR016137. Regulat_G_prot_signal_superfam.
    IPR000342. RGS_dom.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    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. Align

    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

    MNIQEQGFPL DLGASFTEDA PRPPVPGEEG ELVSTDPRPA SYSFCSGKGV    50
    GIKGETSTAT PRRSDLDLGY EPEGSASPTP PYLKWAESLH SLLDDQDGIS 100
    LFRTFLKQEG CADLLDFWFA CTGFRKLEPC DSNEEKRLKL ARAIYRKYIL 150
    DNNGIVSRQT KPATKSFIKG CIMKQLIDPA MFDQAQTEIQ ATMEENTYPS 200
    FLKSDIYLEY TRTGSESPKV CSDQSSGSGT GKGISGYLPT LNEDEEWKCD 250
    QDMDEDDGRD AAPPGRLPQK LLLETAAPRV SSSRRYSEGR EFRYGSWREP 300
    VNPYYVNAGY ALAPATSAND SEQQSLSSDA DTLSLTDSSV DGIPPYRIRK 350
    QHRREMQESV QVNGRVPLPH IPRTYRVPKE VRVEPQKFAE ELIHRLEAVQ 400
    RTREAEEKLE ERLKRVRMEE EGEDGDPSSG PPGPCHKLPP APAWHHFPPR 450
    CVDMGCAGLR DAHEENPESI LDEHVQRVLR TPGRQSPGPG HRSPDSGHVA 500
    KMPVALGGAA SGHGKHVPKS GAKLDAAGLH HHRHVHHHVH HSTARPKEQV 550
    EAEATRRAQS SFAWGLEPHS HGARSRGYSE SVGAAPNASD GLAHSGKVGV 600
    ACKRNAKKAE SGKSASTEVP GASEDAEKNQ KIMQWIIEGE KEISRHRRTG 650
    HGSSGTRKPQ PHENSRPLSL EHPWAGPQLR TSVQPSHLFI QDPTMPPHPA 700
    PNPLTQLEEA RRRLEEEEKR ASRAPSKQRY VQEVMRRGRA CVRPACAPVL 750
    HVVPAVSDME LSETETRSQR KVGGGSAQPC DSIVVAYYFC GEPIPYRTLV 800
    RGRAVTLGQF KELLTKKGSY RYYFKKVSDE FDCGVVFEEV REDEAVLPVF 850
    EEKIIGKVEK VD 862
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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]
    XP_005255666.1. XM_005255609.2. [O15169-1]
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS10405.1. [O15169-1 ]
    CCDS10406.1. [O15169-2 ]
    RefSeqi NP_003493.1. NM_003502.3. [O15169-1 ]
    NP_851393.1. NM_181050.2. [O15169-2 ]
    XP_005255666.1. XM_005255609.2. [O15169-1 ]
    UniGenei Hs.592082.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DK8 X-ray 1.57 A 74-220 [» ]
    1EMU X-ray 1.90 A 80-211 [» ]
    1O9U X-ray 2.40 B 383-400 [» ]
    3ZDI X-ray 2.64 B 383-400 [» ]
    4B7T X-ray 2.77 B 383-400 [» ]
    4NM0 X-ray 2.50 B 383-402 [» ]
    4NM3 X-ray 2.10 B 383-402 [» ]
    4NM5 X-ray 2.30 B 383-402 [» ]
    4NM7 X-ray 2.30 B 383-402 [» ]
    4NU1 X-ray 2.50 B 383-402 [» ]
    ProteinModelPortali O15169.
    SMRi O15169. Positions 74-220, 779-862.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113909. 56 interactions.
    DIPi DIP-34630N.
    IntActi O15169. 63 interactions.
    MINTi MINT-100969.
    STRINGi 9606.ENSP00000262320.

    Chemistry

    ChEMBLi CHEMBL1255127.

    PTM databases

    PhosphoSitei O15169.

    Proteomic databases

    MaxQBi O15169.
    PaxDbi O15169.
    PRIDEi O15169.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262320 ; ENSP00000262320 ; ENSG00000103126 . [O15169-1 ]
    ENST00000354866 ; ENSP00000346935 ; ENSG00000103126 . [O15169-2 ]
    GeneIDi 8312.
    KEGGi hsa:8312.
    UCSCi uc002cgp.2. human. [O15169-1 ]
    uc002cgq.2. human. [O15169-2 ]

    Organism-specific databases

    CTDi 8312.
    GeneCardsi GC16M000338.
    HGNCi HGNC:903. AXIN1.
    HPAi CAB012987.
    MIMi 114550. phenotype.
    603816. gene.
    607864. phenotype.
    neXtProti NX_O15169.
    PharmGKBi PA25195.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG238205.
    HOVERGENi HBG004324.
    InParanoidi O15169.
    KOi K02157.
    OMAi IMQWIIE.
    OrthoDBi EOG79PJQ0.
    PhylomeDBi O15169.
    TreeFami TF315454.

    Enzyme and pathway databases

    Reactomei REACT_11063. Degradation of beta-catenin by the destruction complex.
    REACT_11065. Beta-catenin phosphorylation cascade.
    REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    REACT_200766. degradation of AXIN.
    REACT_200777. TCF dependent signaling in response to WNT.
    SignaLinki O15169.

    Miscellaneous databases

    EvolutionaryTracei O15169.
    GeneWikii AXIN1.
    GenomeRNAii 8312.
    NextBioi 31127.
    PROi O15169.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O15169.
    Bgeei O15169.
    CleanExi HS_AXIN1.
    Genevestigatori O15169.

    Family and domain databases

    Gene3Di 1.10.196.10. 2 hits.
    InterProi IPR014936. Axin_b-cat-bd.
    IPR001158. DIX.
    IPR024066. Regulat_G_prot_signal_dom1.
    IPR016137. Regulat_G_prot_signal_superfam.
    IPR000342. RGS_dom.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    Pfami PF08833. Axin_b-cat_bind. 1 hit.
    PF00778. DIX. 1 hit.
    PF00615. RGS. 1 hit.
    [Graphical view ]
    PRINTSi PR01301. RGSPROTEIN.
    SMARTi SM00021. DAX. 1 hit.
    SM00315. RGS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48097. SSF48097. 1 hit.
    SSF54236. SSF54236. 1 hit.
    PROSITEi PS50841. DIX. 1 hit.
    PS50132. RGS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "Structural basis of the axin-adenomatous polyposis coli interaction."
      Spink K.E., Polakis P., Weis W.I.
      EMBO J. 19:2270-2279(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 74-220 IN COMPLEX WITH APC.
    22. "Structural basis for recruitment of glycogen synthase kinase 3beta to the axin-APC scaffold complex."
      Dajani R., Fraser E., Roe S.M., Yeo M., Good V.M., Thompson V., Dale T.C., Pearl L.H.
      EMBO J. 22:494-501(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 383-400 IN COMPLEX WITH GSK3B.
    23. "Mutational spectrum of beta-catenin, AXIN1, and AXIN2 in hepatocellular carcinomas and hepatoblastomas."
      Taniguchi K., Roberts L.R., Aderca I.N., Dong X., Qian C., Murphy L.M., Nagorney D.M., Burgart L.J., Roche P.C., Smith D.I., Ross J.A., Liu W.
      Oncogene 21:4863-4871(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HCC ARG-106; LEU-345; SER-425 AND SER-650, VARIANT HEPATOBLASTOMA GLN-841.

    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: October 1, 2014
    This is version 164 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