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Protein

Beta-catenin-interacting protein 1

Gene

Ctnnbip1

Organism
Mus musculus (Mouse)
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.

GO - Molecular functioni

  • armadillo repeat domain binding Source: MGI
  • beta-catenin binding Source: MGI

GO - Biological processi

  • anterior/posterior pattern specification Source: MGI
  • branching involved in ureteric bud morphogenesis Source: MGI
  • negative regulation of DNA binding Source: BHF-UCL
  • negative regulation of mesenchymal cell proliferation Source: MGI
  • negative regulation of protein binding Source: MGI
  • negative regulation of protein complex assembly Source: BHF-UCL
  • negative regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  • negative regulation of smooth muscle cell proliferation Source: BHF-UCL
  • negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • negative regulation of transcription initiation from RNA polymerase II promoter Source: BHF-UCL
  • negative regulation of Wnt signaling pathway Source: MGI
  • positive regulation of monocyte differentiation Source: MGI
  • positive regulation of osteoblast differentiation Source: MGI
  • regulation of vascular permeability involved in acute inflammatory response Source: MGI
  • Wnt signaling pathway Source: MGI
Complete GO annotation...

Keywords - Biological processi

Wnt signaling pathway

Enzyme and pathway databases

ReactomeiR-MMU-3769402. 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:Catnbip1, Icat
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1915756. Ctnnbip1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi37 – 393EEE → AAA: Abolishes CTNNB1 binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8181Beta-catenin-interacting protein 1PRO_0000152883Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei59 – 591PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9JJN6.
PaxDbiQ9JJN6.
PRIDEiQ9JJN6.

PTM databases

iPTMnetiQ9JJN6.
PhosphoSiteiQ9JJN6.

Expressioni

Tissue specificityi

Highly expressed in heart, brain, liver and skeletal muscle. Detected at low levels in kidney, testis and lung.

Gene expression databases

BgeeiQ9JJN6.
CleanExiMM_CTNNBIP1.
GenevisibleiQ9JJN6. MM.

Interactioni

Subunit structurei

Binds CTNNB1.

GO - Molecular functioni

  • armadillo repeat domain binding Source: MGI
  • beta-catenin binding Source: MGI

Protein-protein interaction databases

BioGridi211930. 3 interactions.
MINTiMINT-139054.
STRINGi10090.ENSMUSP00000030839.

Structurei

3D structure databases

ProteinModelPortaliQ9JJN6.
SMRiQ9JJN6. Positions 8-53.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the CTNNBIP1 family.Curated

Phylogenomic databases

eggNOGiENOG410IYM5. Eukaryota.
ENOG4111UJF. LUCA.
GeneTreeiENSGT00510000048990.
HOGENOMiHOG000037432.
HOVERGENiHBG051037.
InParanoidiQ9JJN6.
KOiK04493.
OMAiSHEEMYI.
OrthoDBiEOG71P2DG.
PhylomeDBiQ9JJN6.

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.

Q9JJN6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNREGAPGKS PEEMYIQQKV RVLLMLRKMG SNLTASEEEF LRTYAGVVSS
60 70 80
QLSQLPQHSI DQGAEDVVMA FSRSETEDRR Q
Length:81
Mass (Da):9,174
Last modified:October 1, 2000 - v1
Checksum:i2C58D060B50CE942
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB021261 mRNA. Translation: BAB03457.1.
AK003595 mRNA. Translation: BAB22883.1.
AK009066 mRNA. Translation: BAB26052.1.
AK036181 mRNA. Translation: BAC29336.1.
AK048258 mRNA. Translation: BAC33287.1.
BC038253 mRNA. Translation: AAH38253.1.
CCDSiCCDS38975.1.
RefSeqiNP_001135402.1. NM_001141930.1.
NP_075954.1. NM_023465.4.
UniGeneiMm.299735.
Mm.474667.

Genome annotation databases

EnsembliENSMUST00000030839; ENSMUSP00000030839; ENSMUSG00000028988.
ENSMUST00000105692; ENSMUSP00000101317; ENSMUSG00000028988.
GeneIDi67087.
KEGGimmu:67087.
UCSCiuc008vwm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB021261 mRNA. Translation: BAB03457.1.
AK003595 mRNA. Translation: BAB22883.1.
AK009066 mRNA. Translation: BAB26052.1.
AK036181 mRNA. Translation: BAC29336.1.
AK048258 mRNA. Translation: BAC33287.1.
BC038253 mRNA. Translation: AAH38253.1.
CCDSiCCDS38975.1.
RefSeqiNP_001135402.1. NM_001141930.1.
NP_075954.1. NM_023465.4.
UniGeneiMm.299735.
Mm.474667.

3D structure databases

ProteinModelPortaliQ9JJN6.
SMRiQ9JJN6. Positions 8-53.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211930. 3 interactions.
MINTiMINT-139054.
STRINGi10090.ENSMUSP00000030839.

PTM databases

iPTMnetiQ9JJN6.
PhosphoSiteiQ9JJN6.

Proteomic databases

MaxQBiQ9JJN6.
PaxDbiQ9JJN6.
PRIDEiQ9JJN6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030839; ENSMUSP00000030839; ENSMUSG00000028988.
ENSMUST00000105692; ENSMUSP00000101317; ENSMUSG00000028988.
GeneIDi67087.
KEGGimmu:67087.
UCSCiuc008vwm.2. mouse.

Organism-specific databases

CTDi56998.
MGIiMGI:1915756. Ctnnbip1.

Phylogenomic databases

eggNOGiENOG410IYM5. Eukaryota.
ENOG4111UJF. LUCA.
GeneTreeiENSGT00510000048990.
HOGENOMiHOG000037432.
HOVERGENiHBG051037.
InParanoidiQ9JJN6.
KOiK04493.
OMAiSHEEMYI.
OrthoDBiEOG71P2DG.
PhylomeDBiQ9JJN6.

Enzyme and pathway databases

ReactomeiR-MMU-3769402. Deactivation of the beta-catenin transactivating complex.

Miscellaneous databases

ChiTaRSiCtnnbip1. mouse.
PROiQ9JJN6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JJN6.
CleanExiMM_CTNNBIP1.
GenevisibleiQ9JJN6. MM.

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], CHARACTERIZATION, MUTAGENESIS OF 37-GLU--GLU-39.
    Tissue: Embryo.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cerebellum, Embryo, Head and Tongue.
  3. "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].
    Strain: FVB/N.
    Tissue: Kidney.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiCNBP1_MOUSE
AccessioniPrimary (citable) accession number: Q9JJN6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: October 1, 2000
Last modified: June 8, 2016
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.