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Protein

Beta-catenin-interacting protein 1

Gene

CTNNBIP1

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

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

GO - Biological processi

  1. anterior/posterior pattern specification Source: GO_Central
  2. branching involved in ureteric bud morphogenesis Source: GO_Central
  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 initiation from RNA polymerase II promoter Source: Ensembl
  9. negative regulation of Wnt signaling pathway Source: GO_Central
  10. positive regulation of monocyte differentiation Source: BHF-UCL
  11. positive regulation of osteoblast differentiation Source: BHF-UCL
  12. regulation of vascular permeability involved in acute inflammatory response Source: BHF-UCL
  13. Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

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
Complete GO annotation...

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.
ExpressionAtlasiQ9NSA3. baseline and differential.
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. 20 interactions.
IntActiQ9NSA3. 8 interactions.
MINTiMINT-249497.
STRINGi9606.ENSP00000366466.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00510000048990.
HOGENOMiHOG000037432.
HOVERGENiHBG051037.
InParanoidiQ9NSA3.
KOiK04493.
OMAiSHEEMYI.
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

        10         20         30         40         50
MNREGAPGKS PEEMYIQQKV RVLLMLRKMG SNLTASEEEF LRTYAGVVNS
60 70 80
QLSQLPPHSI DQGAEDVVMA FSRSETEDRR Q
Length:81
Mass (Da):9,170
Last modified:October 1, 2000 - v1
Checksum:i3DA6CF90B50CE942
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi121313. 20 interactions.
IntActiQ9NSA3. 8 interactions.
MINTiMINT-249497.
STRINGi9606.ENSP00000366466.

PTM databases

PhosphoSiteiQ9NSA3.

Polymorphism databases

DMDMi29428025.

Proteomic databases

MaxQBiQ9NSA3.
PaxDbiQ9NSA3.
PeptideAtlasiQ9NSA3.
PRIDEiQ9NSA3.

Protocols and materials databases

DNASUi56998.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi56998.
GeneCardsiGC01M009908.
HGNCiHGNC:16913. CTNNBIP1.
HPAiCAB024893.
HPA042617.
MIMi607758. gene.
neXtProtiNX_Q9NSA3.
PharmGKBiPA27014.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG39852.
GeneTreeiENSGT00510000048990.
HOGENOMiHOG000037432.
HOVERGENiHBG051037.
InParanoidiQ9NSA3.
KOiK04493.
OMAiSHEEMYI.
OrthoDBiEOG71P2DG.
PhylomeDBiQ9NSA3.

Enzyme and pathway databases

ReactomeiREACT_200731. deactivation of the beta-catenin transactivating complex.

Miscellaneous databases

EvolutionaryTraceiQ9NSA3.
GeneWikiiCTNNBIP1.
GenomeRNAii56998.
NextBioi62715.
PROiQ9NSA3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NSA3.
CleanExiHS_CTNNBIP1.
ExpressionAtlasiQ9NSA3. baseline and differential.
GenevestigatoriQ9NSA3.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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: February 4, 2015
This is version 123 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

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 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.