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Q9D219

- BCL9_MOUSE

UniProt

Q9D219 - BCL9_MOUSE

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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

Functioni

Promotes beta-catenin's transcriptional activity. Involved in signal transduction through the Wnt pathway By similarity.1 Publication

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
Complete GO annotation...

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. Golgi apparatus Source: MGI
  2. cis-Golgi network Source: MGI
  3. cytoplasm Source: MGI
  4. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14251425B-cell CLL/lymphoma 9 protein
PRO_0000064886Add
BLAST

Amino acid modifications

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

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni177 – 20529Interacts with PYGO1 By similarity
Add
BLAST
Regioni358 – 37417Interacts with CTNNB1 By similarity
Add
BLAST

Compositional bias

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

Sequence similaritiesi

Belongs to the BCL9 family.

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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1134 – 11341M → V in BAB32190. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 91 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

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