BCL9_MOUSE
ID BCL9_MOUSE Reviewed; 1425 AA.
AC Q9D219; B2RQC0; Q67FX9; Q8BUJ8; Q8VE74;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=B-cell CLL/lymphoma 9 protein;
DE Short=B-cell lymphoma 9 protein;
DE Short=Bcl-9;
GN Name=Bcl9;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=C57BL/6J;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain, and Mammary gland;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 484-1425.
RC STRAIN=C57BL/6J; TISSUE=Heart, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND SER-686, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Spleen, and 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-843, AND IDENTIFICATION BY MASS
RP 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-800, 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: Promotes beta-catenin's transcriptional activity. Involved in
CC signal transduction through the Wnt pathway (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:15371335}.
CC -!- SUBUNIT: Binds to beta-catenin (CTNNB1), PYGO1 and PYGO2; the
CC interaction with PYGO1 increases PYGO1 affinity to histone H3
CC methylated at 'Lys 4'. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15371335}.
CC -!- SIMILARITY: Belongs to the BCL9 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH19641.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY296061; AAQ62699.1; -; mRNA.
DR EMBL; BC019641; AAH19641.1; ALT_INIT; mRNA.
DR EMBL; BC137850; AAI37851.1; -; mRNA.
DR EMBL; AK020724; BAB32190.1; -; mRNA.
DR EMBL; AK084676; BAC39248.1; -; mRNA.
DR CCDS; CCDS17654.1; -.
DR RefSeq; NP_084209.3; NM_029933.4.
DR RefSeq; XP_006502351.1; XM_006502288.3.
DR RefSeq; XP_006502352.1; XM_006502289.3.
DR RefSeq; XP_006502353.1; XM_006502290.2.
DR AlphaFoldDB; Q9D219; -.
DR SMR; Q9D219; -.
DR BioGRID; 218773; 3.
DR IntAct; Q9D219; 2.
DR STRING; 10090.ENSMUSP00000046152; -.
DR iPTMnet; Q9D219; -.
DR PhosphoSitePlus; Q9D219; -.
DR EPD; Q9D219; -.
DR jPOST; Q9D219; -.
DR MaxQB; Q9D219; -.
DR PaxDb; Q9D219; -.
DR PeptideAtlas; Q9D219; -.
DR PRIDE; Q9D219; -.
DR ProteomicsDB; 273551; -.
DR Antibodypedia; 20242; 166 antibodies from 24 providers.
DR DNASU; 77578; -.
DR Ensembl; ENSMUST00000046521; ENSMUSP00000046152; ENSMUSG00000038256.
DR Ensembl; ENSMUST00000166341; ENSMUSP00000131692; ENSMUSG00000038256.
DR GeneID; 77578; -.
DR KEGG; mmu:77578; -.
DR UCSC; uc008qot.2; mouse.
DR CTD; 607; -.
DR MGI; MGI:1924828; Bcl9.
DR VEuPathDB; HostDB:ENSMUSG00000038256; -.
DR eggNOG; ENOG502QREN; Eukaryota.
DR GeneTree; ENSGT00730000110915; -.
DR HOGENOM; CLU_004930_1_0_1; -.
DR InParanoid; Q9D219; -.
DR OMA; ECNSTEH; -.
DR OrthoDB; 156519at2759; -.
DR PhylomeDB; Q9D219; -.
DR TreeFam; TF331144; -.
DR Reactome; R-MMU-201722; Formation of the beta-catenin:TCF transactivating complex.
DR BioGRID-ORCS; 77578; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Bcl9; mouse.
DR PRO; PR:Q9D219; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9D219; protein.
DR Bgee; ENSMUSG00000038256; Expressed in undifferentiated genital tubercle and 222 other tissues.
DR Genevisible; Q9D219; MM.
DR GO; GO:1990907; C:beta-catenin-TCF complex; ISO:MGI.
DR GO; GO:0005801; C:cis-Golgi network; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0016528; C:sarcoplasm; 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:0014908; P:myotube differentiation involved in skeletal muscle regeneration; IGI:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI: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; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Wnt signaling pathway.
FT CHAIN 1..1425
FT /note="B-cell CLL/lymphoma 9 protein"
FT /id="PRO_0000064886"
FT REGION 1..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..205
FT /note="Interaction with PYGO1"
FT /evidence="ECO:0000250"
FT REGION 207..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..374
FT /note="Interaction with CTNNB1"
FT /evidence="ECO:0000250"
FT REGION 577..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1031..1051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1153..1199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1252..1275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..272
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..341
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..835
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..891
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..946
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1051
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00512"
FT MOD_RES 172
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00512"
FT MOD_RES 315
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00512"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00512"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 686
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00512"
FT MOD_RES 800
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 843
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 906
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00512"
FT MOD_RES 916
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00512"
FT CONFLICT 1134
FT /note="M -> V (in Ref. 3; BAB32190)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1425 AA; 148971 MW; 77347CF56FC4A815 CRC64;
MHPSNPKVRS SPSGNTQSSP KSKQEVMVRP PTVMSPSGNP QLDSKFSNQG KPGGSASQSQ
PSPCDSKSGG HTPKALPGPG GSMGLKNGAG NGAKGKGKRE RSISADSFDQ RDPGTPNDDS
DIKECNSADH IKSQESQHTP HSMTPSTATA PRSSTPSHGQ TPAPEPISAQ KTPAKVVYVF
STEMANKAAE AVLKGQVETI VSFHIQNISN SKSERSTAPL NTQIPTLRND PKPLPQQPPA
PANQDQNSSQ NARLQPTPPI QAPAPKPTAA PRPLDRESPG VENKLIPPVG SPGSSTPLPP
DGTGPNSTPN NRAVTPVSQG SNSSSADPKA PPPPPVSGGE PPTLGENPDG LSQEQLEHRE
RSLQTLRDIQ RMLFPDEKEF TAGQTGGPQQ NTGVLDGPQK KPDGPIQAMM SQSQSLGKGP
GPRTDVGAPF GPQGHRDVPF SPDEMVPPNM SSQSGPIGPD HLDHMTPEQI AWLKLQQEFY
EEKRRKQEQV VVQQCSLQDM MVHQHGPRGV VRGPPPPYQM APGEGWAPGA EPFPDGINIS
HSLPPRGMAP HPNMPGSQMR LPGFAGMINS EMEGPNVPNP ASRPGLSGVS WPDDVPKIPD
GRNFPPGQGV FSGPGRGERF PNPQGLSEEM FQQQLAEKQL ALPPGMSMEG IRPGMEMNRM
IPGSQRHMEP GSNPIFPRIP VEGPLSPSRG DFPKGMPPQI GPGRELEFGM VPGGMKGEVN
LNVNMGSSSQ MIPQKMREAG AGPEEMMKLR PGSSEMLPAQ QKMVPLPFGE HPQQEYGVGP
RPFLPMSQGP GSNSGLRNLR EPIGPDQRTN SRLSHMPPLP LNPSSNPTSL STAPPVQRGL
GRKPLDISVA GSQVHSPGIN PLKSPTMHQV QSPMLGSPSG NLKSPQTPSQ LAGMLAGPAA
AASIKSPPVL GSAAASPVHL KSPSLPAPSP GWTSSPKPPL QSPGIPPNHK APLTMASPAM
LGSVESGGPP PPTASQPASV NIPGSLPSST PYPMPPEPTL SQNPLSIMMS RMSKFAMPSS
TPLYHDAIKT VASSDDDSPP ARSPNLPSMN SMPGMGINTQ NPRISGPNPV VPMPTLSPMG
MTQPLSHSNQ MPSPNAMGPS IPPHGVPMGP GLMSHNPIMG HGSQEPPMVP QGRMGFPQGF
PPVQSPPQQV PFPHNGPTGG QGNFPGGIGF PGEGPLGRPS NLPQSSADPA LCKPGGPGAP
DSFTVLGNSM PSVFTDPDLQ EVIRPGATGI PEFDLSRIIP SEKPSQTLQY FPRGEVPGRK
QPQGPGPGFS HMQGMMSDQA PRMGLALPGM GGPGPVGTPD IPLGTSPSMP GHNPMRPPAF
LQQGMMGPHH RMMSPAQSTV PGPATLMTNP AAAVGMIPGK DRGPAGLYTH PGPVGSPGMM
MSMQGMMGPQ QNIMIPPQMR PRGMAADVGM GGFSQGPGNP GNMMF
