BCL9L_HUMAN
ID BCL9L_HUMAN Reviewed; 1499 AA.
AC Q86UU0; A1A4C1; Q67FY1; Q6ZWJ0; Q6ZWK2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=B-cell CLL/lymphoma 9-like protein;
DE Short=B-cell lymphoma 9-like protein;
DE Short=BCL9-like protein;
DE AltName: Full=Protein BCL9-2;
GN Name=BCL9L; Synonyms=DLNB11;
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 2).
RX PubMed=15371335; DOI=10.1101/gad.317604;
RA Brembeck F.H., Schwarz-Romond T., Bakkers J., Wilhelm S., Hammerschmidt M.,
RA Birchmeier W.;
RT "Essential role of BCL9-2 in the switch between beta-catenin's adhesive and
RT transcriptional functions.";
RL Genes Dev. 18:2225-2230(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Kubo T., Arai Y., Ohira M., Gamou T., Maeno G., Sakiyama T., Toyoda A.,
RA Hattori M., Sakaki Y., Nakagawara A., Ohki M.;
RT "Identification of a 500-kb region of common allelic loss in chromosome
RT 11q23 in non-MYCN amplified type of neuroblastoma.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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] OF 707-1499 (ISOFORM 4).
RC TISSUE=Prostate;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 865-1499 (ISOFORMS 1/2), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 466-1499 (ISOFORM 3).
RC TISSUE=Brain;
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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=12964048;
RA Katoh M., Katoh M.;
RT "Identification and characterization of human BCL9L gene and mouse Bcl9l
RT gene in silico.";
RL Int. J. Mol. Med. 12:643-649(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-915, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP INTERACTION WITH CTNNB1.
RX PubMed=17052462; DOI=10.1016/j.molcel.2006.09.001;
RA Sampietro J., Dahlberg C.L., Cho U.S., Hinds T.R., Kimelman D., Xu W.;
RT "Crystal structure of a beta-catenin/BCL9/Tcf4 complex.";
RL Mol. Cell 24:293-300(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17129358; DOI=10.1111/j.1349-7006.2006.00363.x;
RA Sakamoto I., Ohwada S., Toya H., Togo N., Kashiwabara K., Oyama T.,
RA Nakajima T., Ito H., Adachi S., Jigami T., Akiyama T.;
RT "Up-regulation of a BCL9-related beta-catenin-binding protein, B9L, in
RT different stages of sporadic colorectal adenoma.";
RL Cancer Sci. 98:83-87(2007).
RN [11]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17309600; DOI=10.1111/j.1349-7006.2007.00430.x;
RA Toya H., Oyama T., Ohwada S., Togo N., Sakamoto I., Horiguchi J.,
RA Koibuchi Y., Adachi S., Jigami T., Nakajima T., Akiyama T.;
RT "Immunohistochemical expression of the beta-catenin-interacting protein B9L
RT is associated with histological high nuclear grade and immunohistochemical
RT ErbB2/HER-2 expression in breast cancers.";
RL Cancer Sci. 98:484-490(2007).
RN [12]
RP IDENTIFICATION IN A COMPLEX WITH CDC73; CTNNB1 AND PYGO1, AND INTERACTION
RP WITH CTNNB1.
RX PubMed=17113272; DOI=10.1016/j.mod.2006.09.006;
RA Hoffmans R., Basler K.;
RT "BCL9-2 binds Arm/beta-catenin in a Tyr142-independent manner and requires
RT Pygopus for its function in Wg/Wnt signaling.";
RL Mech. Dev. 124:59-67(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-813, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118; SER-1004; SER-1010 AND
RP SER-1017, AND IDENTIFICATION BY 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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-36; LYS-108 AND LYS-137, AND
RP IDENTIFICATION BY MASS 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-750; SER-813;
RP SER-1004 AND SER-1010, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-25; SER-88; SER-116;
RP SER-118 AND SER-975, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-25; SER-88; SER-424;
RP THR-514; SER-750; SER-813; SER-915; SER-938; SER-947; SER-997; SER-1004 AND
RP SER-1017, AND IDENTIFICATION BY 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-1017, AND
RP IDENTIFICATION BY 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 [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1344, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Transcriptional regulator that acts as an activator. Promotes
CC beta-catenin transcriptional activity. Plays a role in tumorigenesis.
CC Enhances the neoplastic transforming activity of CTNNB1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Found in a complex with CDC73; CTNNB1 and PYGO1. Interacts
CC with CTNNB1. {ECO:0000269|PubMed:17052462,
CC ECO:0000269|PubMed:17113272}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17129358,
CC ECO:0000269|PubMed:17309600}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q86UU0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86UU0-2; Sequence=VSP_030205;
CC Name=3;
CC IsoId=Q86UU0-3; Sequence=VSP_030207, VSP_030208;
CC Name=4;
CC IsoId=Q86UU0-4; Sequence=VSP_030206;
CC -!- TISSUE SPECIFICITY: Expressed in breast, ductal and invasive ductal
CC carcinomas of the breast, sporadic colorectal adenomas and carcinomas
CC (at protein level). Expressed in fetal brain. Expressed in lung,
CC amygdala, eye, prostate, pancreatic and prostate cancers, head and neck
CC tumors and embryonal tumor. {ECO:0000269|PubMed:12964048,
CC ECO:0000269|PubMed:17129358, ECO:0000269|PubMed:17309600}.
CC -!- DOMAIN: Tne C-terminal domain is important for its transactivation
CC activity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the BCL9 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH33257.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC85500.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC85512.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY296059; AAQ62697.1; -; mRNA.
DR EMBL; AB094091; BAC76045.1; -; mRNA.
DR EMBL; CH471065; EAW67418.1; -; Genomic_DNA.
DR EMBL; BC033257; AAH33257.1; ALT_INIT; mRNA.
DR EMBL; AK122650; BAC85500.1; ALT_INIT; mRNA.
DR EMBL; AK122882; BAC85512.1; ALT_INIT; mRNA.
DR CCDS; CCDS8403.1; -. [Q86UU0-1]
DR RefSeq; NP_872363.1; NM_182557.2. [Q86UU0-1]
DR RefSeq; XP_005271568.1; XM_005271511.2.
DR RefSeq; XP_006718878.1; XM_006718815.2. [Q86UU0-1]
DR PDB; 2XB1; X-ray; 1.90 A; A/C=237-271.
DR PDB; 4UP0; X-ray; 1.28 A; A=240-268.
DR PDB; 4UP5; X-ray; 1.65 A; A=240-268.
DR PDBsum; 2XB1; -.
DR PDBsum; 4UP0; -.
DR PDBsum; 4UP5; -.
DR AlphaFoldDB; Q86UU0; -.
DR SMR; Q86UU0; -.
DR BioGRID; 129475; 39.
DR IntAct; Q86UU0; 17.
DR MINT; Q86UU0; -.
DR STRING; 9606.ENSP00000335320; -.
DR GlyGen; Q86UU0; 7 sites, 2 O-linked glycans (7 sites).
DR iPTMnet; Q86UU0; -.
DR PhosphoSitePlus; Q86UU0; -.
DR BioMuta; BCL9L; -.
DR DMDM; 74750433; -.
DR EPD; Q86UU0; -.
DR jPOST; Q86UU0; -.
DR MassIVE; Q86UU0; -.
DR MaxQB; Q86UU0; -.
DR PaxDb; Q86UU0; -.
DR PeptideAtlas; Q86UU0; -.
DR PRIDE; Q86UU0; -.
DR ProteomicsDB; 69890; -. [Q86UU0-1]
DR ProteomicsDB; 69891; -. [Q86UU0-2]
DR ProteomicsDB; 69892; -. [Q86UU0-3]
DR ProteomicsDB; 69893; -. [Q86UU0-4]
DR Antibodypedia; 32548; 138 antibodies from 25 providers.
DR DNASU; 283149; -.
DR Ensembl; ENST00000334801.7; ENSP00000335320.3; ENSG00000186174.13. [Q86UU0-1]
DR Ensembl; ENST00000683865.1; ENSP00000507778.1; ENSG00000186174.13. [Q86UU0-1]
DR GeneID; 283149; -.
DR KEGG; hsa:283149; -.
DR MANE-Select; ENST00000683865.1; ENSP00000507778.1; NM_001378213.1; NP_001365142.1.
DR UCSC; uc001pug.5; human. [Q86UU0-1]
DR CTD; 283149; -.
DR DisGeNET; 283149; -.
DR GeneCards; BCL9L; -.
DR HGNC; HGNC:23688; BCL9L.
DR HPA; ENSG00000186174; Low tissue specificity.
DR MIM; 609004; gene.
DR neXtProt; NX_Q86UU0; -.
DR OpenTargets; ENSG00000186174; -.
DR PharmGKB; PA134974002; -.
DR VEuPathDB; HostDB:ENSG00000186174; -.
DR eggNOG; ENOG502QR2B; Eukaryota.
DR GeneTree; ENSGT00730000110915; -.
DR HOGENOM; CLU_004973_0_0_1; -.
DR InParanoid; Q86UU0; -.
DR OMA; EMFGPDQ; -.
DR OrthoDB; 156519at2759; -.
DR PhylomeDB; Q86UU0; -.
DR TreeFam; TF331144; -.
DR PathwayCommons; Q86UU0; -.
DR Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
DR SignaLink; Q86UU0; -.
DR BioGRID-ORCS; 283149; 31 hits in 1084 CRISPR screens.
DR ChiTaRS; BCL9L; human.
DR GenomeRNAi; 283149; -.
DR Pharos; Q86UU0; Tbio.
DR PRO; PR:Q86UU0; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q86UU0; protein.
DR Bgee; ENSG00000186174; Expressed in granulocyte and 169 other tissues.
DR ExpressionAtlas; Q86UU0; baseline and differential.
DR Genevisible; Q86UU0; HS.
DR GO; GO:1990907; C:beta-catenin-TCF complex; IDA:FlyBase.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; IDA:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; NAS:BHF-UCL.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0045445; P:myoblast differentiation; IEA:Ensembl.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IMP:BHF-UCL.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR015668; Bcl-9/Bcl-9l.
DR InterPro; IPR024670; BCL9_beta-catenin-bd_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15185; PTHR15185; 1.
DR Pfam; PF11502; BCL9; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing;
KW Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..1499
FT /note="B-cell CLL/lymphoma 9-like protein"
FT /id="PRO_0000314079"
FT REGION 1..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..533
FT /note="Necessary for interaction with CTNNB1"
FT /evidence="ECO:0000250"
FT REGION 888..1084
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1116..1201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..38
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..326
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..458
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..961
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..998
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1049
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1064
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1135
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1165..1183
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1184..1199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 36
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 108
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 110
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q67FY2"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 137
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 514
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 680
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q67FY2"
FT MOD_RES 750
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 813
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 915
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 926
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q67FY2"
FT MOD_RES 938
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 942
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q67FY2"
FT MOD_RES 947
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 975
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 987
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q67FY2"
FT MOD_RES 991
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q67FY2"
FT MOD_RES 997
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1004
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1010
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 1017
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT CROSSLNK 1344
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 9..13
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15371335"
FT /id="VSP_030205"
FT VAR_SEQ 1238..1283
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030206"
FT VAR_SEQ 1333..1394
FT /note="EKPSSTLQYFPKSENQPPKAQPPNLHLMNLQNMMAEQTPSRPPNLPGQQGVQ
FT RGLNMSMCHP -> WFLRTRPFSFCLYLLRILSLLMWLTPLPPLPAGGWPGGQVPAGAV
FT NRALRFCAGLCVCCISVF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030207"
FT VAR_SEQ 1395..1499
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030208"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:4UP0"
FT HELIX 245..256
FT /evidence="ECO:0007829|PDB:4UP0"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:4UP0"
FT HELIX 263..266
FT /evidence="ECO:0007829|PDB:4UP0"
SQ SEQUENCE 1499 AA; 157129 MW; 8415C2EDB7AA9C0C CRC64;
MRILANKTRL PHPRRREAPG SPPLSPRGHC PPAPAKPMHP ENKLTNHGKT GNGGAQSQHQ
NVNQGPTCNV GSKGVGAGNH GAKANQISPS NSSLKNPQAG VPPFSSLKGK VKRDRSVSVD
SGEQREAGTP SLDSEAKEVA PRSKRRCVLE RKQPYSGDEW CSGPDSEEDD KPIGATHNCN
VADPAMAAPQ LGPGQTTQLP LSESSVPGAP HGPPPGLRPD APGGGGGGGG VPGKPPSQFV
YVFTTHLANT AAEAVLQGRA DSILAYHQQN VPRAKLDQAP KVPPTPEPLP LSTPSAGTPQ
SQPPPLPPPP PPAPGSAPPA LPPEGPPEDS SQDLAPNSVG AASTGGGTGG THPNTPTATT
ANNPLPPGGD PSSAPGPALL GEAAAPGNGQ RSLVGSEGLS KEQLEHRERS LQTLRDIERL
LLRSGETEPF LKGPPGGAGE GGPPAQAPPP PQQPPTAPPS GLKKYEEPLQ SMISQTQSLG
GPPLEHEVPG HPPGGDMGQQ MNMMIQRLGQ DSLTPEQVAW RKLQEEYYEE KRRKEEQIGL
HGSRPLQDMM GMGGMMVRGP PPPYHSKPGD QWPPGMGAQL RGPMDVQDPM QLRGGPPFPG
PRFPGNQIQR VPGFGGMQSM PMEVPMNAMQ RPVRPGMGWT EDLPPMGGPS NFAQNTMPYP
GGQGEAERFM TPRVREELLR HQLLEKRSMG MQRPLGMAGS GMGQSMEMER MMQAHRQMDP
AMFPGQMAGG EGLAGTPMGM EFGGGRGLLS PPMGQSGLRE VDPPMGPGNL NMNMNVNMNM
NMNLNVQMTP QQQMLMSQKM RGPGDLMGPQ GLSPEEMARV RAQNSSGVMG GPQKMLMPSQ
FPNQGQQGFS GGQGPYQAMS QDMGNTQDMF SPDQSSMPMS NVGTTRLSHM PLPPASNPPG
TVHSAPNRGL GRRPSDLTIS INQMGSPGMG HLKSPTLSQV HSPLVTSPSA NLKSPQTPSQ
MVPLPSANPP GPLKSPQVLG SSLSVRSPTG SPSRLKSPSM AVPSPGWVAS PKTAMPSPGV
SQNKQPPLNM NSSTTLSNME QGTLPPSGPR SSSSAPPANP PSGLMNPSLP FTSSPDPTPS
QNPLSLMMTQ MSKYAMPSST PLYHNAIKTI ATSDDELLPD RPLLPPPPPP QGSGPGISNS
QPSQMHLNSA AAQSPMGMNL PGQQPLSHEP PPAMLPSPTP LGSNIPLHPN AQGTGGPPQN
SMMMAPGGPD SLNAPCGPVP SSSQMMPFPP RLQQPHGAMA PTGGGGGGPG LQQHYPSGMA
LPPEDLPNQP PGPMPPQQHL MGKAMAGRMG DAYPPGVLPG VASVLNDPEL SEVIRPTPTG
IPEFDLSRII PSEKPSSTLQ YFPKSENQPP KAQPPNLHLM NLQNMMAEQT PSRPPNLPGQ
QGVQRGLNMS MCHPGQMSLL GRTGVPPQQG MVPHGLHQGV MSPPQGLMTQ QNFMLMKQRG
VGGEVYSQPP HMLSPQGSLM GPPPQQNLMV SHPLRQRSVS LDSQMGYLPA PGGMANLPF
