Q9NSA3 (CNBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-catenin-interacting protein 1

Alternative name(s):
Inhibitor of beta-catenin and Tcf-4

Gene names

Name:	CTNNBIP1
Synonyms:	ICAT

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	81 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Wnt signaling pathway
Cellular component	Cytoplasm Nucleus
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Wnt receptor 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: Compara negative regulation of Wnt receptor 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: Compara negative regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara negative regulation of transcription initiation from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara 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_component	beta-catenin destruction complex Inferred from direct assay PubMed 16188939. Source: BHF-UCL cytosol Inferred from direct assay PubMed 18287330. Source: BHF-UCL nucleus Inferred from direct assay PubMed 18287330PubMed 19569129. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CTNNB1	P35222	6	EBI-747082,EBI-491549
Ctnnb1	Q02248	7	EBI-747082,EBI-397872	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 81

81

Beta-catenin-interacting protein 1

PRO_0000152882

Secondary structure

1

.

.

.

.

.

.

.

81

Helix Strand Turn

Details...

Helix

11 – 28

18

Helix

35 – 43

9

Helix

45 – 52

8

Sequences

	Sequence		Length	Mass (Da)
	Q9NSA3 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 3DA6CF90B50CE942	FASTA	81	9,170
	10 20 30 40 50 60 MNREGAPGKS PEEMYIQQKV RVLLMLRKMG SNLTASEEEF LRTYAGVVNS QLSQLPPHSI 70 80 DQGAEDVVMA FSRSETEDRR Q

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.

IPI

IPI00025001.

RefSeq

NP_001012329.1. NM_001012329.1.
NP_064633.1. NM_020248.2.

UniGene

Hs.463759.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q9NSA3.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9NSA3. 6 interactions.

MINT

MINT-249497.

STRING

9606.ENSP00000366466.

PTM databases

PhosphoSite

Q9NSA3.

Polymorphism databases

DMDM

29428025.

Proteomic databases

PaxDb

Q9NSA3.

PeptideAtlas

Q9NSA3.

PRIDE

Q9NSA3.

Protocols and materials databases

DNASU

56998.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000377256; ENSP00000366466; ENSG00000178585.
ENST00000377258; ENSP00000366468; ENSG00000178585.
ENST00000377263; ENSP00000366474; ENSG00000178585.
ENST00000400904; ENSP00000383696; ENSG00000178585.
ENST00000537447; ENSP00000444681; ENSG00000178585.

GeneID

56998.

KEGG

hsa:56998.

UCSC

uc001aqk.1. human.

Organism-specific databases

CTD

56998.

GeneCards

GC01M009908.

HGNC

HGNC:16913. CTNNBIP1.

HPA

CAB024893.

MIM

607758. gene.

neXtProt

NX_Q9NSA3.

PharmGKB

PA27014.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG39852.

HOGENOM

HOG000037432.

HOVERGEN

HBG051037.

InParanoid

Q9NSA3.

KO

K04493.

OMA

HPIDQGA.

OrthoDB

EOG4GB77S.

Gene expression databases

ArrayExpress

Q9NSA3.

Bgee

Q9NSA3.

CleanEx

HS_CTNNBIP1.

Genevestigator

Q9NSA3.

GermOnline

ENSG00000178585. Homo sapiens.

Family and domain databases

Gene3D

1.10.10.490. 1 hit.

InterPro

IPR009428. ICAT.
[Graphical view]

Pfam

PF06384. ICAT. 1 hit.
[Graphical view]

SUPFAM

SSF81730. ICAT. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q9NSA3.

GenomeRNAi

56998.

NextBio

62715.

SOURCE

Search...

Entry information

Entry name

CNBP1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.