CTBL1_HUMAN
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 03-AUG-2022, entry version 169.
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).
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 Ig class switching
CC recombination (CSR). May induce apoptosis.
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
CC complex. Interacts with AICDA; the interaction is important for the
CC antibody diversification activity of AICDA. Interacts with PRPF31 (via
CC its NLS). Interacts (via its N-terminal NLS) with KPNA1 and KPNA2.
CC {ECO:0000269|PubMed:18722174, ECO:0000269|PubMed:20176811,
CC ECO:0000269|PubMed:21385873}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAQ15267.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB14992.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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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 SMR; Q8WYA6; -.
DR BioGRID; 121123; 194.
DR ComplexPortal; CPX-5824; PRP19-CDC5L complex.
DR CORUM; Q8WYA6; -.
DR IntAct; Q8WYA6; 50.
DR MINT; Q8WYA6; -.
DR STRING; 9606.ENSP00000355050; -.
DR GlyGen; Q8WYA6; 1 site, 1 O-linked glycan (1 site).
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; Q8WYA6; -.
DR PeptideAtlas; Q8WYA6; -.
DR PRIDE; Q8WYA6; -.
DR ProteomicsDB; 75151; -. [Q8WYA6-1]
DR ProteomicsDB; 75152; -. [Q8WYA6-2]
DR ProteomicsDB; 75153; -. [Q8WYA6-3]
DR Antibodypedia; 750; 329 antibodies from 35 providers.
DR CPTC; Q8WYA6; 1 antibody.
DR DNASU; 56259; -.
DR Ensembl; ENST00000361383.11; ENSP00000355050.6; ENSG00000132792.19. [Q8WYA6-1]
DR Ensembl; ENST00000373469.1; ENSP00000362568.1; ENSG00000132792.19. [Q8WYA6-3]
DR Ensembl; ENST00000373473.5; ENSP00000362572.1; ENSG00000132792.19. [Q8WYA6-2]
DR Ensembl; ENST00000405275.6; ENSP00000384355.2; ENSG00000132792.19. [Q8WYA6-4]
DR Ensembl; ENST00000628103.2; ENSP00000487198.1; ENSG00000132792.19. [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 CTD; 56259; -.
DR DisGeNET; 56259; -.
DR GeneCards; CTNNBL1; -.
DR HGNC; HGNC:15879; CTNNBL1.
DR HPA; ENSG00000132792; Low tissue specificity.
DR MIM; 611537; gene.
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; 724270at2759; -.
DR PhylomeDB; Q8WYA6; -.
DR TreeFam; TF314294; -.
DR PathwayCommons; Q8WYA6; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; Q8WYA6; -.
DR BioGRID-ORCS; 56259; 687 hits in 1090 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 198 other tissues.
DR ExpressionAtlas; Q8WYA6; baseline and differential.
DR Genevisible; Q8WYA6; HS.
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:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC: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; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039678; CTNNBL1.
DR InterPro; IPR013180; CTNNBL1_N.
DR PANTHER; PTHR14978; PTHR14978; 1.
DR Pfam; PF08216; CTNNBL; 1.
DR SMART; SM01156; DUF1716; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; Coiled coil;
KW Cytoplasm; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; 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 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
