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O00512 (BCL9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
B-cell CLL/lymphoma 9 protein

Short name=B-cell lymphoma 9 protein
Short name=Bcl-9
Alternative name(s):
Protein legless homolog
Gene names
Name:BCL9
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1426 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in signal transduction through the Wnt pathway. Promotes beta-catenin's transcriptional activity By similarity. Ref.4

Subunit structure

Binds to beta-catenin (CTNNB1), PYGO1 and PYGO2; the interaction with PYGO1 increases PYGO1 affinity to histone H3 methylated at 'Lys 4'. Ref.11

Subcellular location

Nucleus By similarity.

Tissue specificity

Detected at low levels in thymus, prostate, testis, ovary and small intestine, and at lower levels in spleen, colon and blood.

Involvement in disease

A chromosomal aberration involving BCL9 is found in a patient with precusor B-cell acute lymphoblastic leukemia (ALL). Translocation t(1;14)(q21;q32). This translocation leaves the coding region intact, but may have pathogenic effects due to alterations in the expression level of BCL9. Several cases of translocations within the 3'-UTR of BCL9 have been found in B-cell malignancies.

Sequence similarities

Belongs to the BCL9 family.

Caution

It is uncertain whether Met-1 or Met-27 is the initiator.

Sequence caution

The sequence CAA73942.1 differs from that shown. Reason: Frameshift at position 1391.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

armP188243EBI-533127,EBI-216128From a different organism.
CDC73Q6P1J92EBI-533127,EBI-930143
CTNNB1P352222EBI-533127,EBI-491549
pygoQ9V9W83EBI-533127,EBI-152653From a different organism.
PYGO1Q9Y3Y47EBI-533127,EBI-3397474
PYGO2Q9BRQ02EBI-533127,EBI-932471

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14261426B-cell CLL/lymphoma 9 protein
PRO_0000064885

Regions

Region177 – 20529Interacts with PYGO1
Region358 – 37417Interacts with CTNNB1
Compositional bias231 – 13781148Pro-rich
Compositional bias331 – 3355Poly-Pro
Compositional bias514 – 5174Poly-Pro
Compositional bias900 – 9034Poly-Ala
Compositional bias970 – 9734Poly-Pro

Amino acid modifications

Modified residue1041Phosphoserine By similarity
Modified residue1721Phosphothreonine Ref.6
Modified residue3151Phosphothreonine Ref.8
Modified residue3181Phosphoserine Ref.5
Modified residue3521Phosphoserine By similarity
Modified residue6871Phosphoserine By similarity
Modified residue8441N6-acetyllysine By similarity
Modified residue9071Phosphoserine Ref.10
Modified residue9171Phosphoserine Ref.10

Natural variations

Natural variant6711P → S.
Corresponds to variant rs3820129 [ dbSNP | Ensembl ].
VAR_046545
Natural variant7821R → K.
Corresponds to variant rs34002844 [ dbSNP | Ensembl ].
VAR_046546

Experimental info

Mutagenesis3581H → A: Abolishes interaction with CTNNB1. Ref.11
Mutagenesis3591R → A: Abolishes interaction with CTNNB1. Ref.11
Mutagenesis3661L → A: Abolishes interaction with CTNNB1; when associated with A-369. Ref.11
Mutagenesis3691I → A: Abolishes interaction with CTNNB1; when associated with A-366. Ref.11
Sequence conflict2401A → V in CAA73942. Ref.1
Sequence conflict4871Q → P in CAA73942. Ref.1
Sequence conflict6091Q → R in CAA73942. Ref.1

Secondary structure

......... 1426
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O00512 [UniParc].

Last modified September 23, 2008. Version 4.
Checksum: 51EF3D0DCA2103CB

FASTA1,426149,290
        10         20         30         40         50         60 
MHSSNPKVRS SPSGNTQSSP KSKQEVMVRP PTVMSPSGNP QLDSKFSNQG KQGGSASQSQ 

        70         80         90        100        110        120 
PSPCDSKSGG HTPKALPGPG GSMGLKNGAG NGAKGKGKRE RSISADSFDQ RDPGTPNDDS 

       130        140        150        160        170        180 
DIKECNSADH IKSQDSQHTP HSMTPSNATA PRSSTPSHGQ TTATEPTPAQ KTPAKVVYVF 

       190        200        210        220        230        240 
STEMANKAAE AVLKGQVETI VSFHIQNISN NKTERSTAPL NTQISALRND PKPLPQQPPA 

       250        260        270        280        290        300 
PANQDQNSSQ NTRLQPTPPI PAPAPKPAAP PRPLDRESPG VENKLIPSVG SPASSTPLPP 

       310        320        330        340        350        360 
DGTGPNSTPN NRAVTPVSQG SNSSSADPKA PPPPPVSSGE PPTLGENPDG LSQEQLEHRE 

       370        380        390        400        410        420 
RSLQTLRDIQ RMLFPDEKEF TGAQSGGPQQ NPGVLDGPQK KPEGPIQAMM AQSQSLGKGP 

       430        440        450        460        470        480 
GPRTDVGAPF GPQGHRDVPF SPDEMVPPSM NSQSGTIGPD HLDHMTPEQI AWLKLQQEFY 

       490        500        510        520        530        540 
EEKRRKQEQV VVQQCSLQDM MVHQHGPRGV VRGPPPPYQM TPSEGWAPGG TEPFSDGINM 

       550        560        570        580        590        600 
PHSLPPRGMA PHPNMPGSQM RLPGFAGMIN SEMEGPNVPN PASRPGLSGV SWPDDVPKIP 

       610        620        630        640        650        660 
DGRNFPPGQG IFSGPGRGER FPNPQGLSEE MFQQQLAEKQ LGLPPGMAME GIRPSMEMNR 

       670        680        690        700        710        720 
MIPGSQRHME PGNNPIFPRI PVEGPLSPSR GDFPKGIPPQ MGPGRELEFG MVPSGMKGDV 

       730        740        750        760        770        780 
NLNVNMGSNS QMIPQKMREA GAGPEEMLKL RPGGSDMLPA QQKMVPLPFG EHPQQEYGMG 

       790        800        810        820        830        840 
PRPFLPMSQG PGSNSGLRNL REPIGPDQRT NSRLSHMPPL PLNPSSNPTS LNTAPPVQRG 

       850        860        870        880        890        900 
LGRKPLDISV AGSQVHSPGI NPLKSPTMHQ VQSPMLGSPS GNLKSPQTPS QLAGMLAGPA 

       910        920        930        940        950        960 
AAASIKSPPV LGSAAASPVH LKSPSLPAPS PGWTSSPKPP LQSPGIPPNH KAPLTMASPA 

       970        980        990       1000       1010       1020 
MLGNVESGGP PPPTASQPAS VNIPGSLPSS TPYTMPPEPT LSQNPLSIMM SRMSKFAMPS 

      1030       1040       1050       1060       1070       1080 
STPLYHDAIK TVASSDDDSP PARSPNLPSM NNMPGMGINT QNPRISGPNP VVPMPTLSPM 

      1090       1100       1110       1120       1130       1140 
GMTQPLSHSN QMPSPNAVGP NIPPHGVPMG PGLMSHNPIM GHGSQEPPMV PQGRMGFPQG 

      1150       1160       1170       1180       1190       1200 
FPPVQSPPQQ VPFPHNGPSG GQGSFPGGMG FPGEGPLGRP SNLPQSSADA ALCKPGGPGG 

      1210       1220       1230       1240       1250       1260 
PDSFTVLGNS MPSVFTDPDL QEVIRPGATG IPEFDLSRII PSEKPSQTLQ YFPRGEVPGR 

      1270       1280       1290       1300       1310       1320 
KQPQGPGPGF SHMQGMMGEQ APRMGLALPG MGGPGPVGTP DIPLGTAPSM PGHNPMRPPA 

      1330       1340       1350       1360       1370       1380 
FLQQGMMGPH HRMMSPAQST MPGQPTLMSN PAAAVGMIPG KDRGPAGLYT HPGPVGSPGM 

      1390       1400       1410       1420 
MMSMQGMMGP QQNIMIPPQM RPRGMAADVG MGGFSQGPGN PGNMMF 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of translocation t(1;14)(q21;q32) defines a novel gene (BCL9) at chromosome 1q21."
Willis T.G., Zalcberg I.R., Coignet L.J.A., Wlodarska I., Stul M., Jadayel D.M., Bastard C., Treleaven J.G., Catovsky D., Silva M.L.M., Dyer M.J.S.
Blood 91:1873-1881(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fetal brain.
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Wnt/wingless signaling requires BCL9/legless-mediated recruitment of pygopus to the nuclear beta-catenin-TCF complex."
Kramps T., Peter O., Brunner E., Nellen D., Froesch B., Chatterjee S., Murone M., Zuellig S., Basler K.
Cell 109:47-60(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-318, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[6]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-172, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-907 AND SER-917, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Crystal structure of a beta-catenin/BCL9/Tcf4 complex."
Sampietro J., Dahlberg C.L., Cho U.S., Hinds T.R., Kimelman D., Xu W.
Mol. Cell 24:293-300(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 347-392 IN COMPLEX WITH CTNNB1 AND TCF7L2, INTERACTION WITH CTNNB1, MUTAGENESIS OF HIS-358; ARG-359; LEU-366 AND ILE-369.
[12]"Decoding of methylated histone H3 tail by the Pygo-BCL9 Wnt signaling complex."
Fiedler M., Sanchez-Barrena M.J., Nekrasov M., Mieszczanek J., Rybin V., Muller J., Evans P., Bienz M.
Mol. Cell 30:507-518(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 174-205 IN COMPLEX WITH PYGO1 AND HISTONE H3K4ME2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y13620 mRNA. Translation: CAA73942.1. Frameshift.
AL359207 Genomic DNA. Translation: CAI15198.1.
CH471223 Genomic DNA. Translation: EAW50932.1.
RefSeqNP_004317.2. NM_004326.3.
XP_005273028.1. XM_005272971.2.
UniGeneHs.415209.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GL7X-ray2.60C/F347-392[»]
2VP7X-ray1.65B174-205[»]
2VPBX-ray1.59B174-205[»]
2VPDX-ray2.77B/D174-205[»]
2VPEX-ray1.70B/D177-205[»]
2VPGX-ray1.60B/D177-205[»]
3SL9X-ray2.20C/D/F/H344-396[»]
ProteinModelPortalO00512.
SMRO00512. Positions 174-205, 348-374.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107079. 4 interactions.
IntActO00512. 8 interactions.
MINTMINT-4773273.
STRING9606.ENSP00000234739.

PTM databases

PhosphoSiteO00512.

Proteomic databases

PaxDbO00512.
PRIDEO00512.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000234739; ENSP00000234739; ENSG00000116128.
ENST00000585295; ENSP00000464022; ENSG00000266095.
GeneID607.
KEGGhsa:607.
UCSCuc001epq.3. human.

Organism-specific databases

CTD607.
GeneCardsGC01P147013.
H-InvDBHIX0028826.
HGNCHGNC:1008. BCL9.
HPAHPA020274.
MIM602597. gene.
neXtProtNX_O00512.
PharmGKBPA25318.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG74241.
HOGENOMHOG000060118.
HOVERGENHBG031116.
InParanoidO00512.
OMAPGGSDML.
OrthoDBEOG7327N1.
PhylomeDBO00512.
TreeFamTF331144.

Enzyme and pathway databases

SignaLinkO00512.

Gene expression databases

BgeeO00512.
CleanExHS_BCL9.
GenevestigatorO00512.

Family and domain databases

InterProIPR015668. Bcl-9.
IPR024670. BCL9_beta-catenin-bd_dom.
[Graphical view]
PANTHERPTHR15185. PTHR15185. 1 hit.
PfamPF11502. BCL9. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO00512.
GeneWikiBCL9.
GenomeRNAi607.
NextBio2469.
PROO00512.
SOURCESearch...

Entry information

Entry nameBCL9_HUMAN
AccessionPrimary (citable) accession number: O00512
Secondary accession number(s): Q5T489
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: September 23, 2008
Last modified: April 16, 2014
This is version 124 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM