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Q9NSA3

- CNBP1_HUMAN

UniProt

Q9NSA3 - CNBP1_HUMAN

Protein

Beta-catenin-interacting protein 1

Gene

CTNNBIP1

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

    Prevents the interaction between CTNNB1 and TCF family members, and acts as negative regulator of the Wnt signaling pathway.1 Publication

    GO - Molecular functioni

    1. armadillo repeat domain binding Source: BHF-UCL
    2. beta-catenin binding Source: BHF-UCL
    3. protein binding Source: IntAct

    GO - Biological processi

    1. anterior/posterior pattern specification Source: RefGenome
    2. branching involved in ureteric bud morphogenesis Source: RefGenome
    3. negative regulation of DNA binding Source: Ensembl
    4. negative regulation of mesenchymal cell proliferation Source: BHF-UCL
    5. negative regulation of protein binding Source: BHF-UCL
    6. negative regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    7. negative regulation of smooth muscle cell proliferation Source: Ensembl
    8. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    9. negative regulation of transcription initiation from RNA polymerase II promoter Source: Ensembl
    10. negative regulation of Wnt signaling pathway Source: RefGenome
    11. positive regulation of monocyte differentiation Source: BHF-UCL
    12. positive regulation of osteoblast differentiation Source: BHF-UCL
    13. regulation of vascular permeability involved in acute inflammatory response Source: BHF-UCL
    14. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Biological processi

    Wnt signaling pathway

    Enzyme and pathway databases

    ReactomeiREACT_200731. deactivation of the beta-catenin transactivating complex.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-catenin-interacting protein 1
    Alternative name(s):
    Inhibitor of beta-catenin and Tcf-4
    Gene namesi
    Name:CTNNBIP1
    Synonyms:ICAT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:16913. CTNNBIP1.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. beta-catenin destruction complex Source: BHF-UCL
    2. cytoplasm Source: BHF-UCL
    3. cytosol Source: BHF-UCL
    4. nucleus Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27014.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 8181Beta-catenin-interacting protein 1PRO_0000152882Add
    BLAST

    Proteomic databases

    MaxQBiQ9NSA3.
    PaxDbiQ9NSA3.
    PeptideAtlasiQ9NSA3.
    PRIDEiQ9NSA3.

    PTM databases

    PhosphoSiteiQ9NSA3.

    Expressioni

    Gene expression databases

    BgeeiQ9NSA3.
    CleanExiHS_CTNNBIP1.
    GenevestigatoriQ9NSA3.

    Organism-specific databases

    HPAiCAB024893.
    HPA042617.

    Interactioni

    Subunit structurei

    Binds CTNNB1.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CTNNB1P352229EBI-747082,EBI-491549
    Ctnnb1Q022487EBI-747082,EBI-397872From a different organism.

    Protein-protein interaction databases

    BioGridi121313. 16 interactions.
    IntActiQ9NSA3. 7 interactions.
    MINTiMINT-249497.
    STRINGi9606.ENSP00000366466.

    Structurei

    Secondary structure

    1
    81
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi11 – 2818
    Helixi35 – 439
    Helixi45 – 528

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1LUJX-ray2.50B1-75[»]
    1M1EX-ray2.10B1-81[»]
    1T08X-ray2.10B8-53[»]
    ProteinModelPortaliQ9NSA3.
    SMRiQ9NSA3. Positions 8-53.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NSA3.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the CTNNBIP1 family.Curated

    Phylogenomic databases

    eggNOGiNOG39852.
    HOGENOMiHOG000037432.
    HOVERGENiHBG051037.
    InParanoidiQ9NSA3.
    KOiK04493.
    OMAiMNREGAS.
    OrthoDBiEOG71P2DG.
    PhylomeDBiQ9NSA3.

    Family and domain databases

    Gene3Di1.10.10.490. 1 hit.
    InterProiIPR009428. ICAT.
    [Graphical view]
    PfamiPF06384. ICAT. 1 hit.
    [Graphical view]
    SUPFAMiSSF81730. SSF81730. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9NSA3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNREGAPGKS PEEMYIQQKV RVLLMLRKMG SNLTASEEEF LRTYAGVVNS   50
    QLSQLPPHSI DQGAEDVVMA FSRSETEDRR Q 81
    Length:81
    Mass (Da):9,170
    Last modified:October 1, 2000 - v1
    Checksum:i3DA6CF90B50CE942
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB021262 mRNA. Translation: BAB03458.1.
    AL357140 Genomic DNA. Translation: CAI16886.1.
    CH471130 Genomic DNA. Translation: EAW71631.1.
    BC014300 mRNA. Translation: AAH14300.1.
    BC146892 mRNA. Translation: AAI46893.1.
    BC146896 mRNA. Translation: AAI46897.1.
    CCDSiCCDS106.1.
    RefSeqiNP_001012329.1. NM_001012329.1.
    NP_064633.1. NM_020248.2.
    XP_006710842.1. XM_006710779.1.
    UniGeneiHs.463759.

    Genome annotation databases

    EnsembliENST00000377256; ENSP00000366466; ENSG00000178585.
    ENST00000377258; ENSP00000366468; ENSG00000178585.
    ENST00000377263; ENSP00000366474; ENSG00000178585.
    ENST00000400904; ENSP00000383696; ENSG00000178585.
    GeneIDi56998.
    KEGGihsa:56998.
    UCSCiuc001aqk.1. human.

    Polymorphism databases

    DMDMi29428025.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB021262 mRNA. Translation: BAB03458.1 .
    AL357140 Genomic DNA. Translation: CAI16886.1 .
    CH471130 Genomic DNA. Translation: EAW71631.1 .
    BC014300 mRNA. Translation: AAH14300.1 .
    BC146892 mRNA. Translation: AAI46893.1 .
    BC146896 mRNA. Translation: AAI46897.1 .
    CCDSi CCDS106.1.
    RefSeqi NP_001012329.1. NM_001012329.1.
    NP_064633.1. NM_020248.2.
    XP_006710842.1. XM_006710779.1.
    UniGenei Hs.463759.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1LUJ X-ray 2.50 B 1-75 [» ]
    1M1E X-ray 2.10 B 1-81 [» ]
    1T08 X-ray 2.10 B 8-53 [» ]
    ProteinModelPortali Q9NSA3.
    SMRi Q9NSA3. Positions 8-53.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121313. 16 interactions.
    IntActi Q9NSA3. 7 interactions.
    MINTi MINT-249497.
    STRINGi 9606.ENSP00000366466.

    PTM databases

    PhosphoSitei Q9NSA3.

    Polymorphism databases

    DMDMi 29428025.

    Proteomic databases

    MaxQBi Q9NSA3.
    PaxDbi Q9NSA3.
    PeptideAtlasi Q9NSA3.
    PRIDEi Q9NSA3.

    Protocols and materials databases

    DNASUi 56998.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000377256 ; ENSP00000366466 ; ENSG00000178585 .
    ENST00000377258 ; ENSP00000366468 ; ENSG00000178585 .
    ENST00000377263 ; ENSP00000366474 ; ENSG00000178585 .
    ENST00000400904 ; ENSP00000383696 ; ENSG00000178585 .
    GeneIDi 56998.
    KEGGi hsa:56998.
    UCSCi uc001aqk.1. human.

    Organism-specific databases

    CTDi 56998.
    GeneCardsi GC01M009908.
    HGNCi HGNC:16913. CTNNBIP1.
    HPAi CAB024893.
    HPA042617.
    MIMi 607758. gene.
    neXtProti NX_Q9NSA3.
    PharmGKBi PA27014.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG39852.
    HOGENOMi HOG000037432.
    HOVERGENi HBG051037.
    InParanoidi Q9NSA3.
    KOi K04493.
    OMAi MNREGAS.
    OrthoDBi EOG71P2DG.
    PhylomeDBi Q9NSA3.

    Enzyme and pathway databases

    Reactomei REACT_200731. deactivation of the beta-catenin transactivating complex.

    Miscellaneous databases

    EvolutionaryTracei Q9NSA3.
    GeneWikii CTNNBIP1.
    GenomeRNAii 56998.
    NextBioi 62715.
    PROi Q9NSA3.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9NSA3.
    CleanExi HS_CTNNBIP1.
    Genevestigatori Q9NSA3.

    Family and domain databases

    Gene3Di 1.10.10.490. 1 hit.
    InterProi IPR009428. ICAT.
    [Graphical view ]
    Pfami PF06384. ICAT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF81730. SSF81730. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Inhibition of Wnt signaling by ICAT, a novel beta-catenin-interacting protein."
      Tago K., Nakamura T., Nishita M., Hyodo J., Nagai S., Murata Y., Adachi S., Ohwada S., Morishita Y., Shibuya H., Akiyama T.
      Genes Dev. 14:1741-1749(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. 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].
      Tissue: Brain and Lung.
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. "The crystal structure of the beta-catenin/ICAT complex reveals the inhibitory mechanism of ICAT."
      Graham T.A., Clements W.K., Kimelman D., Xu W.
      Mol. Cell 10:563-571(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH CTNNB1, FUNCTION.
    7. "ICAT inhibits beta-catenin binding to Tcf/Lef-family transcription factors and the general coactivator p300 using independent structural modules."
      Daniels D.L., Weis W.I.
      Mol. Cell 10:573-584(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH CTNNB1.

    Entry informationi

    Entry nameiCNBP1_HUMAN
    AccessioniPrimary (citable) accession number: Q9NSA3
    Secondary accession number(s): Q5T4V2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 28, 2003
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 119 of the entry and version 1 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 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3