ID CTBL1_HUMAN Reviewed; 563 AA. AC Q8WYA6; B4DE16; Q0VAL9; Q0VAM0; Q53HI8; Q5JWZ2; Q5JWZ3; Q5JWZ7; Q5JWZ8; AC Q8N454; Q8NCL2; Q8TBD6; Q96KD2; Q9H7A5; Q9NQF9; Q9NTX0; Q9Y3M7; DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 178. DE RecName: Full=Beta-catenin-like protein 1; DE AltName: Full=Nuclear-associated protein; DE Short=NAP; DE AltName: Full=Testis development protein NYD-SP19; GN Name=CTNNBL1; Synonyms=C20orf33; ORFNames=PP8304; 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] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR RP LOCATION, AND POSSIBLE FUNCTION. RX PubMed=12659813; DOI=10.1016/s0888-7543(02)00038-1; RA Jabbour L.S., Welter J.F., Kollar J., Hering T.M.; RT "Sequence, gene structure, and expression pattern of CTNNBL1, a minor-class RT intron-containing gene - evidence for a role in apoptosis."; RL Genomics 81:292-303(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Testis; RA Sha J.H., Li J.M., Zhou Z.M.; RT "A new testis development gene NYD-SP19 from human testes."; RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15498874; DOI=10.1073/pnas.0404089101; RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X., RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.; RT "Large-scale cDNA transfection screening for genes related to cancer RT development and progression."; RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4). RC TISSUE=Aortic smooth muscle, and Mammary gland; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Skin; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 327-563. RC TISSUE=Coronary artery; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP INTERACTION WITH AICDA, SUBCELLULAR LOCATION, POSSIBLE FUNCTION, AND RP MUTAGENESIS OF 16-LYS--LYS-33. RX PubMed=18722174; DOI=10.1016/j.molcel.2008.07.009; RA Conticello S.G., Ganesh K., Xue K., Lu M., Rada C., Neuberger M.S.; RT "Interaction between antibody-diversification enzyme AID and spliceosome- RT associated factor CTNNBL1."; RL Mol. Cell 31:474-484(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-91, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [11] RP IDENTIFICATION AS A COMPONENT OF THE PRP19-CDC5L COMPLEX, SUBCELLULAR RP LOCATION, AND INTERACTION WITH CWC15 AND CDC5L. RX PubMed=20176811; DOI=10.1128/mcb.01505-09; RA Grote M., Wolf E., Will C.L., Lemm I., Agafonov D.E., Schomburg A., RA Fischle W., Urlaub H., Luhrmann R.; RT "Molecular architecture of the human Prp19/CDC5L complex."; RL Mol. Cell. Biol. 30:2105-2119(2010). RN [12] 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 [13] RP INTERACTION WITH AICDA; CDC5L; PRPF31; KPNA1 AND KPNA2, AND SUBCELLULAR RP LOCATION. RX PubMed=21385873; DOI=10.1074/jbc.m110.208769; RA Ganesh K., Adam S., Taylor B., Simpson P., Rada C., Neuberger M.; RT "CTNNBL1 is a novel nuclear localization sequence-binding protein that RT recognizes RNA-splicing factors CDC5L and Prp31."; RL J. Biol. Chem. 286:17091-17102(2011). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-545, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-545, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [18] RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS), AND ARM REPEATS. RX PubMed=23897482; DOI=10.1107/s0907444913011360; RA Huang X., Wang G., Wu Y., Du Z.; RT "The structure of full-length human CTNNBL1 reveals a distinct member of RT the armadillo-repeat protein family."; RL Acta Crystallogr. D 69:1598-1608(2013). RN [19] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), NUCLEAR EXPORT SIGNAL, HEAT REPEATS, RP MUTAGENESIS OF 521-MET--PHE-563, AND COILED-COIL. RX PubMed=24269683; DOI=10.1016/j.febslet.2013.11.013; RA Ganesh K., van Maldegem F., Telerman S.B., Simpson P., Johnson C.M., RA Williams R.L., Neuberger M.S., Rada C.; RT "Structural and mutational analysis reveals that CTNNBL1 binds NLSs in a RT manner distinct from that of its closest armadillo-relative, karyopherin RT alpha."; RL FEBS Lett. 588:21-27(2014). RN [20] RP INVOLVEMENT IN IMD9, VARIANT IMD99 VAL-466, FUNCTION, INTERACTION WITH RP AICDA AND CDC5L, AND CHARACTERIZATION OF VARIANT IMD99 VAL-466. RX PubMed=32484799; DOI=10.1172/jci131297; RA Kuhny M., Forbes L.R., Cakan E., Vega-Loza A., Kostiuk V., Dinesh R.K., RA Glauzy S., Stray-Pedersen A., Pezzi A.E., Hanson I.C., Vargas-Hernandez A., RA Xu M.L., Coban-Akdemir Z.H., Jhangiani S.N., Muzny D.M., Gibbs R.A., RA Lupski J.R., Chinn I.K., Schatz D.G., Orange J.S., Meffre E.; RT "Disease-associated CTNNBL1 mutation impairs somatic hypermutation by RT decreasing nuclear AID."; RL J. Clin. Invest. 130:4411-4422(2020). CC -!- FUNCTION: Component of the PRP19-CDC5L complex that forms an integral CC part of the spliceosome and is required for activating pre-mRNA CC splicing. Participates in AID/AICDA-mediated somatic hypermutation CC (SHM) and class-switch recombination (CSR), 2 processes resulting in CC the production of high-affinity, mutated isotype-switched antibodies CC (PubMed:32484799). {ECO:0000269|PubMed:32484799}. CC -!- SUBUNIT: Component of the PRP19-CDC5L splicing complex composed of a CC core complex comprising a homotetramer of PRPF19, CDC5L, PLRG1 and CC BCAS2, and at least three less stably associated proteins CTNNBL1, CC CWC15 and HSPA8. Interacts directly with CWC15 and CDC5L in the complex CC (PubMed:32484799). Interacts with AICDA; the interaction is important CC for the antibody diversification activity of AICDA (PubMed:18722174, CC PubMed:21385873). Interacts with PRPF31 (via its NLS). Interacts (via CC its N-terminal NLS) with KPNA1 and KPNA2. {ECO:0000269|PubMed:18722174, CC ECO:0000269|PubMed:20176811, ECO:0000269|PubMed:21385873, CC ECO:0000269|PubMed:32484799}. CC -!- INTERACTION: CC Q8WYA6; Q00994: BEX3; NbExp=3; IntAct=EBI-748128, EBI-741753; CC Q8WYA6; Q7Z7H3: CATIP; NbExp=3; IntAct=EBI-748128, EBI-10258233; CC Q8WYA6; Q99459: CDC5L; NbExp=7; IntAct=EBI-748128, EBI-374880; CC Q8WYA6; Q96GN5: CDCA7L; NbExp=4; IntAct=EBI-748128, EBI-5278764; CC Q8WYA6; Q9NS37: CREBZF; NbExp=3; IntAct=EBI-748128, EBI-632965; CC Q8WYA6; Q9P013: CWC15; NbExp=6; IntAct=EBI-748128, EBI-2371709; CC Q8WYA6; O95751: LDOC1; NbExp=4; IntAct=EBI-748128, EBI-740738; CC Q8WYA6; Q9NPJ6: MED4; NbExp=3; IntAct=EBI-748128, EBI-394607; CC Q8WYA6; P50222: MEOX2; NbExp=3; IntAct=EBI-748128, EBI-748397; CC Q8WYA6; Q9UKN5: PRDM4; NbExp=3; IntAct=EBI-748128, EBI-2803427; CC Q8WYA6; Q13573: SNW1; NbExp=2; IntAct=EBI-748128, EBI-632715; CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q8WYA6-1; Sequence=Displayed; CC Name=2; Synonyms=NYD-SP19; CC IsoId=Q8WYA6-2; Sequence=VSP_004058, VSP_004059; CC Name=3; CC IsoId=Q8WYA6-3; Sequence=VSP_015182; CC Name=4; CC IsoId=Q8WYA6-4; Sequence=VSP_055261; CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in skeletal CC muscle, placenta, heart, spleen, testis and thyroid. CC {ECO:0000269|PubMed:12659813}. CC -!- DOMAIN: The surface residues of the concave side of the superhelical CC ARM repeat region contribute to, but are not essential for NLS binding. CC {ECO:0000269|PubMed:24269683}. CC -!- DISEASE: Immunodeficiency 99 with hypogammaglobulinemia and autoimmune CC cytopenias (IMD99) [MIM:619846]: An autosomal recessive immunologic CC disorder characterized by recurrent sinopulmonary infections appearing CC in early childhood, B- and T-cell lymphopenia, and progressive severe CC hypogammaglobulinemia with decreased memory B cells. Patients may CC develop autoimmune cytopenias, such as thrombocytopenia, or autoimmune CC features, such as vitiligo. {ECO:0000269|PubMed:32484799}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SEQUENCE CAUTION: CC Sequence=AAQ15267.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAB14992.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF239607; AAL69567.1; -; mRNA. DR EMBL; AF367471; AAK53407.1; -; mRNA. DR EMBL; AF370431; AAQ15267.1; ALT_FRAME; mRNA. DR EMBL; AK074663; BAC11121.1; -; mRNA. DR EMBL; AK293420; BAG56927.1; -; mRNA. DR EMBL; AK024761; BAB14992.1; ALT_INIT; mRNA. DR EMBL; AL118499; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL109964; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL023804; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC022802; AAH22802.1; -; mRNA. DR EMBL; BC121005; AAI21006.1; -; mRNA. DR EMBL; BC121006; AAI21007.1; -; mRNA. DR EMBL; AK222592; BAD96312.1; -; mRNA. DR CCDS; CCDS13298.1; -. [Q8WYA6-1] DR CCDS; CCDS63269.1; -. [Q8WYA6-4] DR RefSeq; NP_001268424.1; NM_001281495.1. [Q8WYA6-4] DR RefSeq; NP_110517.2; NM_030877.4. [Q8WYA6-1] DR RefSeq; XP_011527219.1; XM_011528917.2. DR PDB; 4CB8; X-ray; 2.90 A; A=77-563. DR PDB; 4CB9; X-ray; 3.00 A; A=1-563. DR PDB; 4CBA; X-ray; 3.10 A; A=77-563. DR PDB; 4HM9; X-ray; 3.10 A; A=1-563. DR PDB; 4HNM; X-ray; 2.90 A; A=75-563. DR PDB; 4MFU; X-ray; 2.74 A; A=77-563. DR PDB; 4MFV; X-ray; 2.92 A; A/B=33-563. DR PDB; 7ABI; EM; 8.00 A; S=1-563. DR PDBsum; 4CB8; -. DR PDBsum; 4CB9; -. DR PDBsum; 4CBA; -. DR PDBsum; 4HM9; -. DR PDBsum; 4HNM; -. DR PDBsum; 4MFU; -. DR PDBsum; 4MFV; -. DR PDBsum; 7ABI; -. DR AlphaFoldDB; Q8WYA6; -. DR EMDB; EMD-11697; -. DR SMR; Q8WYA6; -. DR BioGRID; 121123; 229. DR ComplexPortal; CPX-5824; PRP19-CDC5L complex. DR CORUM; Q8WYA6; -. DR IntAct; Q8WYA6; 51. DR MINT; Q8WYA6; -. DR STRING; 9606.ENSP00000355050; -. DR GlyGen; Q8WYA6; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q8WYA6; -. DR PhosphoSitePlus; Q8WYA6; -. DR SwissPalm; Q8WYA6; -. DR BioMuta; CTNNBL1; -. DR DMDM; 29840792; -. DR EPD; Q8WYA6; -. DR jPOST; Q8WYA6; -. DR MassIVE; Q8WYA6; -. DR MaxQB; Q8WYA6; -. DR PaxDb; 9606-ENSP00000355050; -. DR PeptideAtlas; Q8WYA6; -. DR ProteomicsDB; 75151; -. [Q8WYA6-1] DR ProteomicsDB; 75152; -. [Q8WYA6-2] DR ProteomicsDB; 75153; -. [Q8WYA6-3] DR Pumba; Q8WYA6; -. DR Antibodypedia; 750; 367 antibodies from 35 providers. DR CPTC; Q8WYA6; 1 antibody. DR DNASU; 56259; -. DR Ensembl; ENST00000361383.11; ENSP00000355050.6; ENSG00000132792.20. [Q8WYA6-1] DR Ensembl; ENST00000373469.1; ENSP00000362568.1; ENSG00000132792.20. [Q8WYA6-3] DR Ensembl; ENST00000373473.5; ENSP00000362572.1; ENSG00000132792.20. [Q8WYA6-2] DR Ensembl; ENST00000628103.2; ENSP00000487198.1; ENSG00000132792.20. [Q8WYA6-4] DR GeneID; 56259; -. DR KEGG; hsa:56259; -. DR MANE-Select; ENST00000361383.11; ENSP00000355050.6; NM_030877.5; NP_110517.2. DR UCSC; uc002xhh.4; human. [Q8WYA6-1] DR AGR; HGNC:15879; -. DR CTD; 56259; -. DR DisGeNET; 56259; -. DR GeneCards; CTNNBL1; -. DR HGNC; HGNC:15879; CTNNBL1. DR HPA; ENSG00000132792; Low tissue specificity. DR MalaCards; CTNNBL1; -. DR MIM; 611537; gene. DR MIM; 619846; phenotype. DR neXtProt; NX_Q8WYA6; -. DR OpenTargets; ENSG00000132792; -. DR PharmGKB; PA27015; -. DR VEuPathDB; HostDB:ENSG00000132792; -. DR eggNOG; KOG2734; Eukaryota. DR GeneTree; ENSGT00390000006931; -. DR HOGENOM; CLU_017098_2_1_1; -. DR InParanoid; Q8WYA6; -. DR OMA; TDWREQE; -. DR OrthoDB; 7396at2759; -. DR PhylomeDB; Q8WYA6; -. DR TreeFam; TF314294; -. DR PathwayCommons; Q8WYA6; -. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR SignaLink; Q8WYA6; -. DR SIGNOR; Q8WYA6; -. DR BioGRID-ORCS; 56259; 719 hits in 1167 CRISPR screens. DR ChiTaRS; CTNNBL1; human. DR GeneWiki; CTNNBL1; -. DR GenomeRNAi; 56259; -. DR Pharos; Q8WYA6; Tbio. DR PRO; PR:Q8WYA6; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; Q8WYA6; Protein. DR Bgee; ENSG00000132792; Expressed in left testis and 200 other cell types or tissues. DR ExpressionAtlas; Q8WYA6; baseline and differential. DR GO; GO:0005813; C:centrosome; IDA:HPA. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0000974; C:Prp19 complex; IDA:UniProtKB. DR GO; GO:0005681; C:spliceosomal complex; IDA:UniProtKB. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; NAS:ComplexPortal. DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB. DR GO; GO:0016445; P:somatic diversification of immunoglobulins; IMP:UniProtKB. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR039678; CTNNBL1. DR InterPro; IPR013180; CTNNBL1_N. DR PANTHER; PTHR14978:SF4; BETA-CATENIN-LIKE PROTEIN 1; 1. DR PANTHER; PTHR14978; BETA-CATENIN-LIKE PROTEIN 1 NUCLEAR ASSOCIATED PROTEIN; 1. DR Pfam; PF08216; CTNNBL; 1. DR SMART; SM01156; DUF1716; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR Genevisible; Q8WYA6; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Adaptive immunity; Alternative splicing; KW Coiled coil; Cytoplasm; Disease variant; Immunity; mRNA processing; KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW Spliceosome. FT CHAIN 1..563 FT /note="Beta-catenin-like protein 1" FT /id="PRO_0000079490" FT REPEAT 79..129 FT /note="HEAT 1" FT REPEAT 134..176 FT /note="HEAT 2" FT REPEAT 178..228 FT /note="ARM 1" FT REPEAT 229..273 FT /note="ARM 2" FT REPEAT 274..323 FT /note="ARM 3" FT REPEAT 325..363 FT /note="ARM 4" FT REPEAT 364..417 FT /note="ARM 5" FT REGION 1..49 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 476..540 FT /evidence="ECO:0000269|PubMed:24269683" FT MOTIF 16..33 FT /note="Nuclear localization signal" FT MOTIF 130..140 FT /note="Nuclear export signal (NES)" FT /evidence="ECO:0000305" FT COMPBIAS 14..49 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT MOD_RES 91 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 389 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 545 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT VAR_SEQ 1..252 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_015182" FT VAR_SEQ 1..187 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_004058" FT VAR_SEQ 1..27 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055261" FT VAR_SEQ 188 FT /note="L -> M (in isoform 2)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_004059" FT VARIANT 466 FT /note="M -> V (in IMD99; when expressed in a B lymphocyte FT cell line, leads to decreased frequencies of somatic FT hypermutations, a process involved in the production of FT isotype-switched high-affinity antibodies, the defect that FT can be rescued by the wild-type protein; decrease FT interaction with AICDA, hence impairs AICDA nuclear FT localization; may decrease protein stability; no effect on FT interaction with CDC5L; dbSNP:rs201986512)" FT /evidence="ECO:0000269|PubMed:32484799" FT /id="VAR_087117" FT VARIANT 507 FT /note="N -> D (in dbSNP:rs4811236)" FT /id="VAR_059638" FT MUTAGEN 16..33 FT /note="Missing: Nuclear and cytoplasmic localization." FT /evidence="ECO:0000269|PubMed:18722174" FT MUTAGEN 521..563 FT /note="Missing: No change in NLS binding nor folding." FT /evidence="ECO:0000269|PubMed:24269683" FT CONFLICT 222 FT /note="V -> A (in Ref. 6; AAI21006)" FT /evidence="ECO:0000305" FT CONFLICT 329 FT /note="R -> L (in Ref. 4; BAB14992)" FT /evidence="ECO:0000305" FT CONFLICT 340 FT /note="N -> Y (in Ref. 4; BAC11121)" FT /evidence="ECO:0000305" FT CONFLICT 439 FT /note="D -> N (in Ref. 4; BAB14992 and 7; BAD96312)" FT /evidence="ECO:0000305" FT CONFLICT 445 FT /note="H -> Q (in Ref. 4; BAB14992)" FT /evidence="ECO:0000305" FT TURN 54..56 FT /evidence="ECO:0007829|PDB:4HM9" FT HELIX 57..63 FT /evidence="ECO:0007829|PDB:4HM9" FT HELIX 81..102 FT /evidence="ECO:0007829|PDB:4MFU" FT STRAND 105..107 FT /evidence="ECO:0007829|PDB:4MFV" FT HELIX 111..125 FT /evidence="ECO:0007829|PDB:4MFU" FT TURN 126..129 FT /evidence="ECO:0007829|PDB:4MFU" FT HELIX 131..134 FT /evidence="ECO:0007829|PDB:4CB8" FT HELIX 135..139 FT /evidence="ECO:0007829|PDB:4MFU" FT HELIX 142..149 FT /evidence="ECO:0007829|PDB:4MFU" FT HELIX 155..170 FT /evidence="ECO:0007829|PDB:4MFU" FT HELIX 171..173 FT /evidence="ECO:0007829|PDB:4MFU" FT STRAND 174..176 FT /evidence="ECO:0007829|PDB:4MFV" FT HELIX 179..190 FT /evidence="ECO:0007829|PDB:4MFU" FT HELIX 193..203 FT /evidence="ECO:0007829|PDB:4MFU" FT HELIX 209..228 FT /evidence="ECO:0007829|PDB:4MFU" FT HELIX 232..239 FT /evidence="ECO:0007829|PDB:4MFU" FT HELIX 241..250 FT /evidence="ECO:0007829|PDB:4MFU" FT HELIX 257..270 FT /evidence="ECO:0007829|PDB:4MFU" FT HELIX 274..282 FT /evidence="ECO:0007829|PDB:4MFU" FT HELIX 285..294 FT /evidence="ECO:0007829|PDB:4MFU" FT STRAND 297..299 FT /evidence="ECO:0007829|PDB:4MFU" FT HELIX 304..322 FT /evidence="ECO:0007829|PDB:4MFU" FT HELIX 325..332 FT /evidence="ECO:0007829|PDB:4MFU" FT HELIX 335..344 FT /evidence="ECO:0007829|PDB:4MFU" FT HELIX 350..361 FT /evidence="ECO:0007829|PDB:4MFU" FT HELIX 364..366 FT /evidence="ECO:0007829|PDB:4MFU" FT HELIX 367..375 FT /evidence="ECO:0007829|PDB:4MFU" FT HELIX 378..387 FT /evidence="ECO:0007829|PDB:4MFU" FT HELIX 393..396 FT /evidence="ECO:0007829|PDB:4CB8" FT HELIX 401..417 FT /evidence="ECO:0007829|PDB:4MFU" FT HELIX 420..429 FT /evidence="ECO:0007829|PDB:4MFU" FT HELIX 432..469 FT /evidence="ECO:0007829|PDB:4MFU" FT HELIX 475..487 FT /evidence="ECO:0007829|PDB:4MFU" FT HELIX 490..504 FT /evidence="ECO:0007829|PDB:4MFU" FT HELIX 509..520 FT /evidence="ECO:0007829|PDB:4MFU" FT TURN 521..523 FT /evidence="ECO:0007829|PDB:4MFU" FT HELIX 526..539 FT /evidence="ECO:0007829|PDB:4MFU" FT STRAND 542..544 FT /evidence="ECO:0007829|PDB:4HNM" FT HELIX 546..559 FT /evidence="ECO:0007829|PDB:4MFU" FT TURN 560..562 FT /evidence="ECO:0007829|PDB:4MFU" SQ SEQUENCE 563 AA; 65173 MW; 791BAFCEC5916B5A CRC64; MDVGELLSYQ PNRGTKRPRD DEEEEQKMRR KQTGTRERGR YREEEMTVVE EADDDKKRLL QIIDRDGEEE EEEEEPLDES SVKKMILTFE KRSYKNQELR IKFPDNPEKF MESELDLNDI IQEMHVVATM PDLYHLLVEL NAVQSLLGLL GHDNTDVSIA VVDLLQELTD IDTLHESEEG AEVLIDALVD GQVVALLVQN LERLDESVKE EADGVHNTLA IVENMAEFRP EMCTEGAQQG LLQWLLKRLK AKMPFDANKL YCSEVLAILL QDNDENRELL GELDGIDVLL QQLSVFKRHN PSTAEEQEMM ENLFDSLCSC LMLSSNRERF LKGEGLQLMN LMLREKKISR SSALKVLDHA MIGPEGTDNC HKFVDILGLR TIFPLFMKSP RKIKKVGTTE KEHEEHVCSI LASLLRNLRG QQRTRLLNKF TENDSEKVDR LMELHFKYLG AMQVADKKIE GEKHDMVRRG EIIDNDTEEE FYLRRLDAGL FVLQHICYIM AEICNANVPQ IRQRVHQILN MRGSSIKIVR HIIKEYAENI GDGRSPEFRE NEQKRILGLL ENF //