CNBP1_HUMAN
ID CNBP1_HUMAN Reviewed; 81 AA.
AC Q9NSA3; Q5T4V2;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Beta-catenin-interacting protein 1;
DE AltName: Full=Inhibitor of beta-catenin and Tcf-4;
GN Name=CTNNBIP1; Synonyms=ICAT;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10898789;
RA Tago K., Nakamura T., Nishita M., Hyodo J., Nagai S., Murata Y., Adachi S.,
RA Ohwada S., Morishita Y., Shibuya H., Akiyama T.;
RT "Inhibition of Wnt signaling by ICAT, a novel beta-catenin-interacting
RT protein.";
RL Genes Dev. 14:1741-1749(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH CTNNB1, AND FUNCTION.
RX PubMed=12408824; DOI=10.1016/s1097-2765(02)00637-8;
RA Graham T.A., Clements W.K., Kimelman D., Xu W.;
RT "The crystal structure of the beta-catenin/ICAT complex reveals the
RT inhibitory mechanism of ICAT.";
RL Mol. Cell 10:563-571(2002).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH CTNNB1.
RX PubMed=12408825; DOI=10.1016/s1097-2765(02)00631-7;
RA Daniels D.L., Weis W.I.;
RT "ICAT inhibits beta-catenin binding to Tcf/Lef-family transcription factors
RT and the general coactivator p300 using independent structural modules.";
RL Mol. Cell 10:573-584(2002).
CC -!- FUNCTION: Prevents the interaction between CTNNB1 and TCF family
CC members, and acts as negative regulator of the Wnt signaling pathway.
CC {ECO:0000269|PubMed:12408824}.
CC -!- SUBUNIT: Binds CTNNB1. {ECO:0000269|PubMed:12408824,
CC ECO:0000269|PubMed:12408825}.
CC -!- INTERACTION:
CC Q9NSA3; P35222: CTNNB1; NbExp=14; IntAct=EBI-747082, EBI-491549;
CC Q9NSA3; Q9BRT9: GINS4; NbExp=3; IntAct=EBI-747082, EBI-747500;
CC Q9NSA3; Q0VD86: INCA1; NbExp=3; IntAct=EBI-747082, EBI-6509505;
CC Q9NSA3; P14923: JUP; NbExp=4; IntAct=EBI-747082, EBI-702484;
CC Q9NSA3; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-747082, EBI-11749135;
CC Q9NSA3; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-747082, EBI-10172290;
CC Q9NSA3; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-747082, EBI-3958099;
CC Q9NSA3; Q4VC12: MSS51; NbExp=3; IntAct=EBI-747082, EBI-11599933;
CC Q9NSA3; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-747082, EBI-22310682;
CC Q9NSA3; Q7Z4N8: P4HA3; NbExp=3; IntAct=EBI-747082, EBI-10181968;
CC Q9NSA3; Q04864: REL; NbExp=3; IntAct=EBI-747082, EBI-307352;
CC Q9NSA3; Q86W54-2: SPATA24; NbExp=3; IntAct=EBI-747082, EBI-12041693;
CC Q9NSA3; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-747082, EBI-739895;
CC Q9NSA3; Q02248: Ctnnb1; Xeno; NbExp=7; IntAct=EBI-747082, EBI-397872;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CTNNBIP1 family. {ECO:0000305}.
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DR EMBL; AB021262; BAB03458.1; -; mRNA.
DR EMBL; AL357140; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471130; EAW71631.1; -; Genomic_DNA.
DR EMBL; BC014300; AAH14300.1; -; mRNA.
DR EMBL; BC146892; AAI46893.1; -; mRNA.
DR EMBL; BC146896; AAI46897.1; -; mRNA.
DR CCDS; CCDS106.1; -.
DR RefSeq; NP_001012329.1; NM_001012329.1.
DR RefSeq; NP_064633.1; NM_020248.2.
DR RefSeq; XP_016857342.1; XM_017001853.1.
DR RefSeq; XP_016857343.1; XM_017001854.1.
DR RefSeq; XP_016857344.1; XM_017001855.1.
DR PDB; 1LUJ; X-ray; 2.50 A; B=1-75.
DR PDB; 1M1E; X-ray; 2.10 A; B=1-81.
DR PDB; 1T08; X-ray; 2.10 A; B=8-53.
DR PDBsum; 1LUJ; -.
DR PDBsum; 1M1E; -.
DR PDBsum; 1T08; -.
DR AlphaFoldDB; Q9NSA3; -.
DR SMR; Q9NSA3; -.
DR BioGRID; 121313; 42.
DR CORUM; Q9NSA3; -.
DR IntAct; Q9NSA3; 25.
DR MINT; Q9NSA3; -.
DR STRING; 9606.ENSP00000366474; -.
DR BindingDB; Q9NSA3; -.
DR ChEMBL; CHEMBL4523468; -.
DR iPTMnet; Q9NSA3; -.
DR MetOSite; Q9NSA3; -.
DR PhosphoSitePlus; Q9NSA3; -.
DR BioMuta; CTNNBIP1; -.
DR DMDM; 29428025; -.
DR EPD; Q9NSA3; -.
DR jPOST; Q9NSA3; -.
DR MassIVE; Q9NSA3; -.
DR MaxQB; Q9NSA3; -.
DR PaxDb; Q9NSA3; -.
DR PeptideAtlas; Q9NSA3; -.
DR PRIDE; Q9NSA3; -.
DR ProteomicsDB; 82522; -.
DR TopDownProteomics; Q9NSA3; -.
DR Antibodypedia; 27763; 179 antibodies from 24 providers.
DR DNASU; 56998; -.
DR Ensembl; ENST00000377256.1; ENSP00000366466.1; ENSG00000178585.15.
DR Ensembl; ENST00000377258.5; ENSP00000366468.1; ENSG00000178585.15.
DR Ensembl; ENST00000377263.6; ENSP00000366474.1; ENSG00000178585.15.
DR Ensembl; ENST00000400904.7; ENSP00000383696.3; ENSG00000178585.15.
DR GeneID; 56998; -.
DR KEGG; hsa:56998; -.
DR MANE-Select; ENST00000377263.6; ENSP00000366474.1; NM_020248.3; NP_064633.1.
DR UCSC; uc001aqk.2; human.
DR CTD; 56998; -.
DR DisGeNET; 56998; -.
DR GeneCards; CTNNBIP1; -.
DR HGNC; HGNC:16913; CTNNBIP1.
DR HPA; ENSG00000178585; Tissue enhanced (esophagus, skin).
DR MIM; 607758; gene.
DR neXtProt; NX_Q9NSA3; -.
DR OpenTargets; ENSG00000178585; -.
DR PharmGKB; PA27014; -.
DR VEuPathDB; HostDB:ENSG00000178585; -.
DR eggNOG; ENOG502S3XR; Eukaryota.
DR GeneTree; ENSGT00940000161133; -.
DR HOGENOM; CLU_145119_1_0_1; -.
DR InParanoid; Q9NSA3; -.
DR OMA; SHEEMYI; -.
DR OrthoDB; 1457177at2759; -.
DR PhylomeDB; Q9NSA3; -.
DR PathwayCommons; Q9NSA3; -.
DR Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
DR SignaLink; Q9NSA3; -.
DR SIGNOR; Q9NSA3; -.
DR BioGRID-ORCS; 56998; 23 hits in 1076 CRISPR screens.
DR ChiTaRS; CTNNBIP1; human.
DR EvolutionaryTrace; Q9NSA3; -.
DR GeneWiki; CTNNBIP1; -.
DR GenomeRNAi; 56998; -.
DR Pharos; Q9NSA3; Tbio.
DR PRO; PR:Q9NSA3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9NSA3; protein.
DR Bgee; ENSG00000178585; Expressed in skin of leg and 197 other tissues.
DR ExpressionAtlas; Q9NSA3; baseline and differential.
DR Genevisible; Q9NSA3; HS.
DR GO; GO:0030877; C:beta-catenin destruction complex; IDA:BHF-UCL.
DR GO; GO:1990711; C:beta-catenin-ICAT complex; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0070016; F:armadillo repeat domain binding; IPI:BHF-UCL.
DR GO; GO:0008013; F:beta-catenin binding; IPI:BHF-UCL.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0043392; P:negative regulation of DNA binding; IEA:Ensembl.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IMP:BHF-UCL.
DR GO; GO:0072201; P:negative regulation of mesenchymal cell proliferation; IMP:BHF-UCL.
DR GO; GO:0032091; P:negative regulation of protein binding; IDA:BHF-UCL.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0060633; P:negative regulation of transcription initiation from RNA polymerase II promoter; IEA:Ensembl.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0045657; P:positive regulation of monocyte differentiation; IMP:BHF-UCL.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:BHF-UCL.
DR GO; GO:0002528; P:regulation of vascular permeability involved in acute inflammatory response; IMP:BHF-UCL.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.490; -; 1.
DR IDEAL; IID00102; -.
DR InterPro; IPR042999; CTNNBIP1.
DR InterPro; IPR009428; ICAT_dom.
DR InterPro; IPR036911; ICAT_sf.
DR PANTHER; PTHR47142; PTHR47142; 1.
DR Pfam; PF06384; ICAT; 1.
DR SUPFAM; SSF81730; SSF81730; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Wnt signaling pathway.
FT CHAIN 1..81
FT /note="Beta-catenin-interacting protein 1"
FT /id="PRO_0000152882"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JJN6"
FT HELIX 11..28
FT /evidence="ECO:0007829|PDB:1M1E"
FT HELIX 35..43
FT /evidence="ECO:0007829|PDB:1M1E"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:1M1E"
SQ SEQUENCE 81 AA; 9170 MW; 3DA6CF90B50CE942 CRC64;
MNREGAPGKS PEEMYIQQKV RVLLMLRKMG SNLTASEEEF LRTYAGVVNS QLSQLPPHSI
DQGAEDVVMA FSRSETEDRR Q
