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Q9D219

- BCL9_MOUSE

UniProt

Q9D219 - BCL9_MOUSE

Protein

B-cell CLL/lymphoma 9 protein

Gene

Bcl9

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 3 (27 Sep 2005)
      Previous versions | rss
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    Functioni

    Promotes beta-catenin's transcriptional activity. Involved in signal transduction through the Wnt pathway By similarity.By similarity

    GO - Molecular functioni

    1. beta-catenin binding Source: MGI

    GO - Biological processi

    1. canonical Wnt signaling pathway Source: MGI
    2. myotube differentiation involved in skeletal muscle regeneration Source: MGI
    3. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    4. skeletal muscle cell differentiation Source: MGI
    5. somatic stem cell maintenance Source: MGI

    Keywords - Biological processi

    Wnt signaling pathway

    Enzyme and pathway databases

    ReactomeiREACT_216539. formation of the beta-catenin:TCF transactivating complex.
    REACT_219771. deactivation of the beta-catenin transactivating complex.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    B-cell CLL/lymphoma 9 protein
    Short name:
    B-cell lymphoma 9 protein
    Short name:
    Bcl-9
    Gene namesi
    Name:Bcl9
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:1924828. Bcl9.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. cis-Golgi network Source: MGI
    2. cytoplasm Source: MGI
    3. Golgi apparatus Source: MGI
    4. nucleus Source: MGI

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14251425B-cell CLL/lymphoma 9 proteinPRO_0000064886Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei104 – 1041Phosphoserine1 Publication
    Modified residuei172 – 1721PhosphothreonineBy similarity
    Modified residuei315 – 3151PhosphothreonineBy similarity
    Modified residuei318 – 3181PhosphoserineBy similarity
    Modified residuei352 – 3521Phosphoserine1 Publication
    Modified residuei686 – 6861Phosphoserine1 Publication
    Modified residuei843 – 8431N6-acetyllysine1 Publication
    Modified residuei906 – 9061PhosphoserineBy similarity
    Modified residuei916 – 9161PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiQ9D219.
    PRIDEiQ9D219.

    PTM databases

    PhosphoSiteiQ9D219.

    Expressioni

    Gene expression databases

    BgeeiQ9D219.
    CleanExiMM_BCL9.
    GenevestigatoriQ9D219.

    Interactioni

    Subunit structurei

    Binds to beta-catenin (CTNNB1), PYGO1 and PYGO2; the interaction with PYGO1 increases PYGO1 affinity to histone H3 methylated at 'Lys 4'.By similarity

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000046152.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9D219.
    SMRiQ9D219. Positions 174-205, 348-374.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni177 – 20529Interacts with PYGO1By similarityAdd
    BLAST
    Regioni358 – 37417Interacts with CTNNB1By similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi231 – 13771147Pro-richAdd
    BLAST
    Compositional biasi1379 – 142446Met-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the BCL9 family.Curated

    Phylogenomic databases

    eggNOGiNOG74241.
    GeneTreeiENSGT00730000110915.
    HOGENOMiHOG000060118.
    HOVERGENiHBG031116.
    InParanoidiB2RQC0.
    OMAiMGSNPQM.
    OrthoDBiEOG7327N1.
    PhylomeDBiQ9D219.
    TreeFamiTF331144.

    Family and domain databases

    InterProiIPR015668. Bcl-9.
    IPR024670. BCL9_beta-catenin-bd_dom.
    [Graphical view]
    PANTHERiPTHR15185. PTHR15185. 1 hit.
    PfamiPF11502. BCL9. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9D219-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHPSNPKVRS SPSGNTQSSP KSKQEVMVRP PTVMSPSGNP QLDSKFSNQG     50
    KPGGSASQSQ PSPCDSKSGG HTPKALPGPG GSMGLKNGAG NGAKGKGKRE 100
    RSISADSFDQ RDPGTPNDDS DIKECNSADH IKSQESQHTP HSMTPSTATA 150
    PRSSTPSHGQ TPAPEPISAQ KTPAKVVYVF STEMANKAAE AVLKGQVETI 200
    VSFHIQNISN SKSERSTAPL NTQIPTLRND PKPLPQQPPA PANQDQNSSQ 250
    NARLQPTPPI QAPAPKPTAA PRPLDRESPG VENKLIPPVG SPGSSTPLPP 300
    DGTGPNSTPN NRAVTPVSQG SNSSSADPKA PPPPPVSGGE PPTLGENPDG 350
    LSQEQLEHRE RSLQTLRDIQ RMLFPDEKEF TAGQTGGPQQ NTGVLDGPQK 400
    KPDGPIQAMM SQSQSLGKGP GPRTDVGAPF GPQGHRDVPF SPDEMVPPNM 450
    SSQSGPIGPD HLDHMTPEQI AWLKLQQEFY EEKRRKQEQV VVQQCSLQDM 500
    MVHQHGPRGV VRGPPPPYQM APGEGWAPGA EPFPDGINIS HSLPPRGMAP 550
    HPNMPGSQMR LPGFAGMINS EMEGPNVPNP ASRPGLSGVS WPDDVPKIPD 600
    GRNFPPGQGV FSGPGRGERF PNPQGLSEEM FQQQLAEKQL ALPPGMSMEG 650
    IRPGMEMNRM IPGSQRHMEP GSNPIFPRIP VEGPLSPSRG DFPKGMPPQI 700
    GPGRELEFGM VPGGMKGEVN LNVNMGSSSQ MIPQKMREAG AGPEEMMKLR 750
    PGSSEMLPAQ QKMVPLPFGE HPQQEYGVGP RPFLPMSQGP GSNSGLRNLR 800
    EPIGPDQRTN SRLSHMPPLP LNPSSNPTSL STAPPVQRGL GRKPLDISVA 850
    GSQVHSPGIN PLKSPTMHQV QSPMLGSPSG NLKSPQTPSQ LAGMLAGPAA 900
    AASIKSPPVL GSAAASPVHL KSPSLPAPSP GWTSSPKPPL QSPGIPPNHK 950
    APLTMASPAM LGSVESGGPP PPTASQPASV NIPGSLPSST PYPMPPEPTL 1000
    SQNPLSIMMS RMSKFAMPSS TPLYHDAIKT VASSDDDSPP ARSPNLPSMN 1050
    SMPGMGINTQ NPRISGPNPV VPMPTLSPMG MTQPLSHSNQ MPSPNAMGPS 1100
    IPPHGVPMGP GLMSHNPIMG HGSQEPPMVP QGRMGFPQGF PPVQSPPQQV 1150
    PFPHNGPTGG QGNFPGGIGF PGEGPLGRPS NLPQSSADPA LCKPGGPGAP 1200
    DSFTVLGNSM PSVFTDPDLQ EVIRPGATGI PEFDLSRIIP SEKPSQTLQY 1250
    FPRGEVPGRK QPQGPGPGFS HMQGMMSDQA PRMGLALPGM GGPGPVGTPD 1300
    IPLGTSPSMP GHNPMRPPAF LQQGMMGPHH RMMSPAQSTV PGPATLMTNP 1350
    AAAVGMIPGK DRGPAGLYTH PGPVGSPGMM MSMQGMMGPQ QNIMIPPQMR 1400
    PRGMAADVGM GGFSQGPGNP GNMMF 1425
    Length:1,425
    Mass (Da):148,971
    Last modified:September 27, 2005 - v3
    Checksum:i77347CF56FC4A815
    GO

    Sequence cautioni

    The sequence AAH19641.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1134 – 11341M → V in BAB32190. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY296061 mRNA. Translation: AAQ62699.1.
    BC019641 mRNA. Translation: AAH19641.1. Different initiation.
    BC137850 mRNA. Translation: AAI37851.1.
    AK020724 mRNA. Translation: BAB32190.1.
    AK084676 mRNA. Translation: BAC39248.1.
    CCDSiCCDS17654.1.
    RefSeqiNP_084209.3. NM_029933.4.
    XP_006502351.1. XM_006502288.1.
    XP_006502352.1. XM_006502289.1.
    XP_006502353.1. XM_006502290.1.
    UniGeneiMm.226175.
    Mm.482931.

    Genome annotation databases

    EnsembliENSMUST00000046521; ENSMUSP00000046152; ENSMUSG00000038256.
    ENSMUST00000166341; ENSMUSP00000131692; ENSMUSG00000038256.
    GeneIDi77578.
    KEGGimmu:77578.
    UCSCiuc008qos.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY296061 mRNA. Translation: AAQ62699.1 .
    BC019641 mRNA. Translation: AAH19641.1 . Different initiation.
    BC137850 mRNA. Translation: AAI37851.1 .
    AK020724 mRNA. Translation: BAB32190.1 .
    AK084676 mRNA. Translation: BAC39248.1 .
    CCDSi CCDS17654.1.
    RefSeqi NP_084209.3. NM_029933.4.
    XP_006502351.1. XM_006502288.1.
    XP_006502352.1. XM_006502289.1.
    XP_006502353.1. XM_006502290.1.
    UniGenei Mm.226175.
    Mm.482931.

    3D structure databases

    ProteinModelPortali Q9D219.
    SMRi Q9D219. Positions 174-205, 348-374.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000046152.

    PTM databases

    PhosphoSitei Q9D219.

    Proteomic databases

    PaxDbi Q9D219.
    PRIDEi Q9D219.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000046521 ; ENSMUSP00000046152 ; ENSMUSG00000038256 .
    ENSMUST00000166341 ; ENSMUSP00000131692 ; ENSMUSG00000038256 .
    GeneIDi 77578.
    KEGGi mmu:77578.
    UCSCi uc008qos.1. mouse.

    Organism-specific databases

    CTDi 607.
    MGIi MGI:1924828. Bcl9.

    Phylogenomic databases

    eggNOGi NOG74241.
    GeneTreei ENSGT00730000110915.
    HOGENOMi HOG000060118.
    HOVERGENi HBG031116.
    InParanoidi B2RQC0.
    OMAi MGSNPQM.
    OrthoDBi EOG7327N1.
    PhylomeDBi Q9D219.
    TreeFami TF331144.

    Enzyme and pathway databases

    Reactomei REACT_216539. formation of the beta-catenin:TCF transactivating complex.
    REACT_219771. deactivation of the beta-catenin transactivating complex.

    Miscellaneous databases

    NextBioi 347136.
    PROi Q9D219.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9D219.
    CleanExi MM_BCL9.
    Genevestigatori Q9D219.

    Family and domain databases

    InterProi IPR015668. Bcl-9.
    IPR024670. BCL9_beta-catenin-bd_dom.
    [Graphical view ]
    PANTHERi PTHR15185. PTHR15185. 1 hit.
    Pfami PF11502. BCL9. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Essential role of BCL9-2 in the switch between beta-catenin's adhesive and transcriptional functions."
      Brembeck F.H., Schwarz-Romond T., Bakkers J., Wilhelm S., Hammerschmidt M., Birchmeier W.
      Genes Dev. 18:2225-2230(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
      Strain: C57BL/6.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain and Mammary gland.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 484-1425.
      Strain: C57BL/6J.
      Tissue: Heart and Spinal cord.
    4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    5. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND SER-686, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-843, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiBCL9_MOUSE
    AccessioniPrimary (citable) accession number: Q9D219
    Secondary accession number(s): B2RQC0
    , Q67FX9, Q8BUJ8, Q8VE74
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2002
    Last sequence update: September 27, 2005
    Last modified: October 1, 2014
    This is version 92 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3