BCL9L_MOUSE
ID BCL9L_MOUSE Reviewed; 1494 AA.
AC Q67FY2; Q641L9; Q6GQY0; Q6I7B5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
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=BCL9-related beta-catenin-binding protein;
DE AltName: Full=Protein BCL9-2;
GN Name=Bcl9l; Synonyms=B9l;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CTNNB1,
RP DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=15574752; DOI=10.1158/0008-5472.can-04-2254;
RA Adachi S., Jigami T., Yasui T., Nakano T., Ohwada S., Omori Y., Sugano S.,
RA Ohkawara B., Shibuya H., Nakamura T., Akiyama T.;
RT "Role of a BCL9-related beta-catenin-binding protein, B9L, in tumorigenesis
RT induced by aberrant activation of Wnt signaling.";
RL Cancer Res. 64:8496-8501(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND INTERACTION WITH
RP CTNNB1.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1091-1494 (ISOFORM 1/2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-994; SER-1001 AND SER-1007,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-912; SER-923; SER-939;
RP SER-944; SER-984; SER-988; SER-994; SER-1001 AND SER-1007, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-36; LYS-108; LYS-110 AND LYS-137,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-677, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
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.
CC {ECO:0000269|PubMed:15371335}.
CC -!- SUBUNIT: Found in a complex with CDC73; CTNNB1 and PYGO1 (By
CC similarity). Interacts with CTNNB1. {ECO:0000250,
CC ECO:0000269|PubMed:15371335, ECO:0000269|PubMed:15574752,
CC ECO:0000269|PubMed:17052462}.
CC -!- INTERACTION:
CC Q67FY2; P35222: CTNNB1; Xeno; NbExp=2; IntAct=EBI-5234367, EBI-491549;
CC Q67FY2; Q9NZC7: WWOX; Xeno; NbExp=3; IntAct=EBI-5234367, EBI-4320739;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15574752}.
CC Note=localized also in punctate nuclear bodies as well in the
CC cytoplasm. Colocalizes with CTNNB1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q67FY2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q67FY2-2; Sequence=VSP_030209;
CC -!- TISSUE SPECIFICITY: Expressed in kidney, liver, lung, testis, brain,
CC spleen, heart and skeletal muscle. Highly expressed in numerous
CC colorectal tumors compared to corresponding non-cancerous tissues.
CC {ECO:0000269|PubMed:15574752}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo.
CC {ECO:0000269|PubMed:15574752}.
CC -!- DOMAIN: Tne C-terminal domain is important for its transactivation
CC activity.
CC -!- SIMILARITY: Belongs to the BCL9 family. {ECO:0000305}.
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DR EMBL; AB128033; BAD24964.1; -; mRNA.
DR EMBL; AY296058; AAQ62696.1; -; mRNA.
DR EMBL; BC072555; AAH72555.1; -; mRNA.
DR EMBL; BC082304; AAH82304.1; -; mRNA.
DR CCDS; CCDS40601.1; -. [Q67FY2-1]
DR CCDS; CCDS90549.1; -. [Q67FY2-2]
DR RefSeq; NP_084532.2; NM_030256.2. [Q67FY2-1]
DR RefSeq; XP_006510764.1; XM_006510701.3. [Q67FY2-1]
DR RefSeq; XP_006510765.1; XM_006510702.3. [Q67FY2-1]
DR RefSeq; XP_006510766.1; XM_006510703.3. [Q67FY2-1]
DR RefSeq; XP_006510767.1; XM_006510704.3. [Q67FY2-1]
DR RefSeq; XP_006510768.1; XM_006510705.3.
DR RefSeq; XP_017169189.1; XM_017313700.1. [Q67FY2-1]
DR AlphaFoldDB; Q67FY2; -.
DR SMR; Q67FY2; -.
DR BioGRID; 219776; 2.
DR IntAct; Q67FY2; 6.
DR STRING; 10090.ENSMUSP00000074516; -.
DR iPTMnet; Q67FY2; -.
DR PhosphoSitePlus; Q67FY2; -.
DR EPD; Q67FY2; -.
DR jPOST; Q67FY2; -.
DR MaxQB; Q67FY2; -.
DR PaxDb; Q67FY2; -.
DR PeptideAtlas; Q67FY2; -.
DR PRIDE; Q67FY2; -.
DR ProteomicsDB; 273549; -. [Q67FY2-1]
DR ProteomicsDB; 273550; -. [Q67FY2-2]
DR Antibodypedia; 32548; 138 antibodies from 25 providers.
DR DNASU; 80288; -.
DR Ensembl; ENSMUST00000074989; ENSMUSP00000074516; ENSMUSG00000063382. [Q67FY2-1]
DR Ensembl; ENSMUST00000218183; ENSMUSP00000151837; ENSMUSG00000063382. [Q67FY2-1]
DR Ensembl; ENSMUST00000220303; ENSMUSP00000151342; ENSMUSG00000063382. [Q67FY2-2]
DR GeneID; 80288; -.
DR KEGG; mmu:80288; -.
DR UCSC; uc009pdu.1; mouse. [Q67FY2-1]
DR CTD; 283149; -.
DR MGI; MGI:1933114; Bcl9l.
DR VEuPathDB; HostDB:ENSMUSG00000063382; -.
DR eggNOG; ENOG502QR2B; Eukaryota.
DR GeneTree; ENSGT00730000110915; -.
DR HOGENOM; CLU_004973_0_0_1; -.
DR InParanoid; Q67FY2; -.
DR OMA; EMFGPDQ; -.
DR OrthoDB; 156519at2759; -.
DR PhylomeDB; Q67FY2; -.
DR TreeFam; TF331144; -.
DR Reactome; R-MMU-201722; Formation of the beta-catenin:TCF transactivating complex.
DR BioGRID-ORCS; 80288; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Bcl9l; mouse.
DR PRO; PR:Q67FY2; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q67FY2; protein.
DR Bgee; ENSMUSG00000063382; Expressed in neurocranium bone and 189 other tissues.
DR ExpressionAtlas; Q67FY2; baseline and differential.
DR Genevisible; Q67FY2; MM.
DR GO; GO:1990907; C:beta-catenin-TCF complex; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0008013; F:beta-catenin binding; IPI:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:InterPro.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IGI:MGI.
DR GO; GO:0045445; P:myoblast differentiation; IGI:MGI.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0022604; P:regulation of cell morphogenesis; ISO:MGI.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IGI:MGI.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IGI:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IGI:MGI.
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 Acetylation; Activator; Alternative splicing; Isopeptide bond; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..1494
FT /note="B-cell CLL/lymphoma 9-like protein"
FT /id="PRO_0000314080"
FT REGION 1..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..530
FT /note="Necessary for interaction with CTNNB1"
FT REGION 905..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1113..1206
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..103
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 191..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..323
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..458
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..958
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..995
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1068
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1132
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1133..1147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1180
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1181..1203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UU0"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UU0"
FT MOD_RES 36
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UU0"
FT MOD_RES 108
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 110
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UU0"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UU0"
FT MOD_RES 137
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UU0"
FT MOD_RES 511
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86UU0"
FT MOD_RES 677
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 747
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UU0"
FT MOD_RES 810
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UU0"
FT MOD_RES 912
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 923
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 935
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UU0"
FT MOD_RES 939
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 944
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 972
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UU0"
FT MOD_RES 984
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 988
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 994
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1001
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1007
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1014
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UU0"
FT CROSSLNK 1339
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86UU0"
FT VAR_SEQ 1..37
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15371335,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_030209"
FT CONFLICT 569..570
FT /note="WP -> CA (in Ref. 1; BAD24964)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1494 AA; 156680 MW; 31A9904C5923581C CRC64;
MRILANKTRL PHPRRREAPG SPPLSPRGHC PPAPAKPMHP ENKLTNHGKT GNGGAQSQHQ
NVNQGPTCNL GSKGVGAGSH GAKANQISPS NSSLKNPQAG VSPFSSLKGK VKRERSVSVD
SGEQREAGTP SLDSEAKEVA PRSKRRCVLE RKQPYSGDEW CSGPDSEEDD KPIAAAHNCN
VADPAMVTPQ LGPGQTAQLP LSESSAPGPQ HGPQPGLRPD VPGGGGGGVP GKPPSQFVYV
FTTHLANTAA EAVLQGRAES ILAYHQQNVP RAKLDQAPKV PPTPEPLPLN TPSAGTPQSQ
PPPLPPPPPA PGSAPPALPP EGPPEDTSQD LAPNSVGAAS TGGGTGGTHP NTPTAATANN
PLPPGGDPGS APGSALLGEA TPTGNGQRNL VGSEGLSKEQ LEHRERSLQT LRDIERLLLR
SGETEPFLKG PPGGAGEGGP PAQAPSAAQP PPSAPPGGLK KYEEPLQSMI SQTQSLGGPP
LEHEVPGHPQ GGDMGQQMNM MMQRLGQDSL TPEQVAWRKL QEEYYEEKRR KEEQIGLHGG
RPLQDMVGMG GMMGRGPPPP YHSKPGDQWP PGMGAQLRGP MDVQDPMQLR PGPPFPGPRF
PGNQMQRVPG FGGMQSMPME VPMNAMQRPV RPGMAWNEDL PPIGGPSNFA QNAVPYPGGQ
GEAERFMTPR VREELLRHQL LEKRSMGMQR PLGMAGSGMG QSMEMERMIQ AHRQMDPAMF
PGQMTGGDGL AGTPMGIEFG GGRGLLSPPM GQSGLREVDP PMGPGNLNMN MNVNMNMNMN
LNVQMTPQQQ MLMSQKMRGP GDMMGPQGLS PEEMARVRAQ NSSGMMGGPQ KMLMPSQFPN
QGQQGFSGGQ GPYQAMPQDM GNTPDMFSPD QSSVPMGTVG TARLSHMPLP PASNPPGSVH
LASNRGLGRR PSDLTISINQ MGSPGMGHLK SPTLSQVHSP LVTSPSANLK SPQTPSQMVP
LPSANPPGPL KSPQVLSSSL GVRSPTGSPS RLKSPSMAVP SPGWVASPKT AMPSPGVSQN
KQPPLSINSS STLGNVEQGA LPPSAPRNSS SAPPANPSSG LMNPSLPFTS SPDPTPSQNP
LSLMMSQMSK YAMPSSTPLY HNAIKTIATS DDELLPDRPL LPPPPPPQGS GPGISNNQPN
QMHMNPAAAQ SPMGMNLPGQ QPLSHEPPPT MLPSPTPLGS NIPLHPNAQG TGGSSQNSMM
MAPGGPDSLN APCGPVPSSS QMMSFPPRLQ QPHGAMAPTG AGGPGLQQHY PSGMALPPED
LPTQPPGPIP PQQHLMGKGM TGRMGDAYPP GVLPGVASVL NDPELSEVIR PTPTGIPEFD
LSRIIPSEKP SSTLQYFPKS ENQPPKAQPP NLHLMNLQNM MAEQTPSRPP NLPGQQGVQR
GLSMSMCHPG QMSLLGRTGV PPQQGMVPHG LHQGVMSPPQ GLMTQQNFML MKQRGVGGEV
YTQPPHMLSP QGSLMGPPPQ QNLMVSHPLR QRSVSLDSQM GYLPTPGSMA NLPF
