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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).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
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. cis-Golgi network Source: MGI
  2. cytoplasm Source: MGI
  3. Golgi apparatus 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 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

MaxQBiQ9D219.
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.
InParanoidiQ9D219.
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

        10         20         30         40         50
MHPSNPKVRS SPSGNTQSSP KSKQEVMVRP PTVMSPSGNP QLDSKFSNQG
60 70 80 90 100
KPGGSASQSQ PSPCDSKSGG HTPKALPGPG GSMGLKNGAG NGAKGKGKRE
110 120 130 140 150
RSISADSFDQ RDPGTPNDDS DIKECNSADH IKSQESQHTP HSMTPSTATA
160 170 180 190 200
PRSSTPSHGQ TPAPEPISAQ KTPAKVVYVF STEMANKAAE AVLKGQVETI
210 220 230 240 250
VSFHIQNISN SKSERSTAPL NTQIPTLRND PKPLPQQPPA PANQDQNSSQ
260 270 280 290 300
NARLQPTPPI QAPAPKPTAA PRPLDRESPG VENKLIPPVG SPGSSTPLPP
310 320 330 340 350
DGTGPNSTPN NRAVTPVSQG SNSSSADPKA PPPPPVSGGE PPTLGENPDG
360 370 380 390 400
LSQEQLEHRE RSLQTLRDIQ RMLFPDEKEF TAGQTGGPQQ NTGVLDGPQK
410 420 430 440 450
KPDGPIQAMM SQSQSLGKGP GPRTDVGAPF GPQGHRDVPF SPDEMVPPNM
460 470 480 490 500
SSQSGPIGPD HLDHMTPEQI AWLKLQQEFY EEKRRKQEQV VVQQCSLQDM
510 520 530 540 550
MVHQHGPRGV VRGPPPPYQM APGEGWAPGA EPFPDGINIS HSLPPRGMAP
560 570 580 590 600
HPNMPGSQMR LPGFAGMINS EMEGPNVPNP ASRPGLSGVS WPDDVPKIPD
610 620 630 640 650
GRNFPPGQGV FSGPGRGERF PNPQGLSEEM FQQQLAEKQL ALPPGMSMEG
660 670 680 690 700
IRPGMEMNRM IPGSQRHMEP GSNPIFPRIP VEGPLSPSRG DFPKGMPPQI
710 720 730 740 750
GPGRELEFGM VPGGMKGEVN LNVNMGSSSQ MIPQKMREAG AGPEEMMKLR
760 770 780 790 800
PGSSEMLPAQ QKMVPLPFGE HPQQEYGVGP RPFLPMSQGP GSNSGLRNLR
810 820 830 840 850
EPIGPDQRTN SRLSHMPPLP LNPSSNPTSL STAPPVQRGL GRKPLDISVA
860 870 880 890 900
GSQVHSPGIN PLKSPTMHQV QSPMLGSPSG NLKSPQTPSQ LAGMLAGPAA
910 920 930 940 950
AASIKSPPVL GSAAASPVHL KSPSLPAPSP GWTSSPKPPL QSPGIPPNHK
960 970 980 990 1000
APLTMASPAM LGSVESGGPP PPTASQPASV NIPGSLPSST PYPMPPEPTL
1010 1020 1030 1040 1050
SQNPLSIMMS RMSKFAMPSS TPLYHDAIKT VASSDDDSPP ARSPNLPSMN
1060 1070 1080 1090 1100
SMPGMGINTQ NPRISGPNPV VPMPTLSPMG MTQPLSHSNQ MPSPNAMGPS
1110 1120 1130 1140 1150
IPPHGVPMGP GLMSHNPIMG HGSQEPPMVP QGRMGFPQGF PPVQSPPQQV
1160 1170 1180 1190 1200
PFPHNGPTGG QGNFPGGIGF PGEGPLGRPS NLPQSSADPA LCKPGGPGAP
1210 1220 1230 1240 1250
DSFTVLGNSM PSVFTDPDLQ EVIRPGATGI PEFDLSRIIP SEKPSQTLQY
1260 1270 1280 1290 1300
FPRGEVPGRK QPQGPGPGFS HMQGMMSDQA PRMGLALPGM GGPGPVGTPD
1310 1320 1330 1340 1350
IPLGTSPSMP GHNPMRPPAF LQQGMMGPHH RMMSPAQSTV PGPATLMTNP
1360 1370 1380 1390 1400
AAAVGMIPGK DRGPAGLYTH PGPVGSPGMM MSMQGMMGPQ QNIMIPPQMR
1410 1420
PRGMAADVGM GGFSQGPGNP GNMMF
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

MaxQBi Q9D219.
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 Q9D219.
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: October 29, 2014
This is version 93 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