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Q9NSA3 (CNBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-catenin-interacting protein 1
Alternative name(s):
Inhibitor of beta-catenin and Tcf-4
Gene names
Name:CTNNBIP1
Synonyms:ICAT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length81 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Prevents the interaction between CTNNB1 and TCF family members, and acts as negative regulator of the Wnt signaling pathway. Ref.6

Subunit structure

Binds CTNNB1.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Sequence similarities

Belongs to the CTNNBIP1 family.

Ontologies

Keywords
   Biological processWnt signaling pathway
   Cellular componentCytoplasm
Nucleus
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

anterior/posterior pattern specification

Inferred from Biological aspect of Ancestor. Source: RefGenome

branching involved in ureteric bud morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of DNA binding

Inferred from electronic annotation. Source: Ensembl

negative regulation of Wnt signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of mesenchymal cell proliferation

Inferred from mutant phenotype PubMed 18977368. Source: BHF-UCL

negative regulation of protein binding

Inferred from direct assay Ref.7PubMed 18287330. Source: BHF-UCL

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from mutant phenotype PubMed 18977368. Source: BHF-UCL

negative regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription initiation from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of monocyte differentiation

Inferred from mutant phenotype PubMed 19569129. Source: BHF-UCL

positive regulation of osteoblast differentiation

Inferred from mutant phenotype PubMed 18977368. Source: BHF-UCL

regulation of vascular permeability involved in acute inflammatory response

Inferred from mutant phenotype PubMed 18287330. Source: BHF-UCL

   Cellular_componentbeta-catenin destruction complex

Inferred from direct assay PubMed 16188939. Source: BHF-UCL

cytoplasm

Inferred from direct assay PubMed 19569129. Source: BHF-UCL

cytosol

Inferred from direct assay PubMed 18287330. Source: BHF-UCL

nucleus

Inferred from direct assay PubMed 18287330PubMed 19569129. Source: BHF-UCL

   Molecular_functionarmadillo repeat domain binding

Inferred from physical interaction Ref.7. Source: BHF-UCL

beta-catenin binding

Inferred from physical interaction Ref.7PubMed 18287330. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CTNNB1P352229EBI-747082,EBI-491549
Ctnnb1Q022487EBI-747082,EBI-397872From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 8181Beta-catenin-interacting protein 1
PRO_0000152882

Secondary structure

....... 81
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9NSA3 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 3DA6CF90B50CE942

FASTA819,170
        10         20         30         40         50         60 
MNREGAPGKS PEEMYIQQKV RVLLMLRKMG SNLTASEEEF LRTYAGVVNS QLSQLPPHSI 

        70         80 
DQGAEDVVMA FSRSETEDRR Q 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001012329.1. NM_001012329.1.
NP_064633.1. NM_020248.2.
UniGeneHs.463759.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LUJX-ray2.50B1-75[»]
1M1EX-ray2.10B1-81[»]
1T08X-ray2.10B8-53[»]
ProteinModelPortalQ9NSA3.
SMRQ9NSA3. Positions 8-53.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121313. 16 interactions.
IntActQ9NSA3. 7 interactions.
MINTMINT-249497.
STRING9606.ENSP00000366466.

PTM databases

PhosphoSiteQ9NSA3.

Polymorphism databases

DMDM29428025.

Proteomic databases

PaxDbQ9NSA3.
PeptideAtlasQ9NSA3.
PRIDEQ9NSA3.

Protocols and materials databases

DNASU56998.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000377256; ENSP00000366466; ENSG00000178585.
ENST00000377258; ENSP00000366468; ENSG00000178585.
ENST00000377263; ENSP00000366474; ENSG00000178585.
ENST00000400904; ENSP00000383696; ENSG00000178585.
ENST00000537447; ENSP00000444681; ENSG00000178585.
GeneID56998.
KEGGhsa:56998.
UCSCuc001aqk.1. human.

Organism-specific databases

CTD56998.
GeneCardsGC01M009908.
HGNCHGNC:16913. CTNNBIP1.
HPACAB024893.
HPA042617.
MIM607758. gene.
neXtProtNX_Q9NSA3.
PharmGKBPA27014.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG39852.
HOGENOMHOG000037432.
HOVERGENHBG051037.
InParanoidQ9NSA3.
KOK04493.
OMAMNREGAS.
OrthoDBEOG71P2DG.
PhylomeDBQ9NSA3.

Gene expression databases

BgeeQ9NSA3.
CleanExHS_CTNNBIP1.
GenevestigatorQ9NSA3.

Family and domain databases

Gene3D1.10.10.490. 1 hit.
InterProIPR009428. ICAT.
[Graphical view]
PfamPF06384. ICAT. 1 hit.
[Graphical view]
SUPFAMSSF81730. SSF81730. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9NSA3.
GeneWikiCTNNBIP1.
GenomeRNAi56998.
NextBio62715.
PROQ9NSA3.
SOURCESearch...

Entry information

Entry nameCNBP1_HUMAN
AccessionPrimary (citable) accession number: Q9NSA3
Secondary accession number(s): Q5T4V2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM