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O00512

- BCL9_HUMAN

UniProt

O00512 - BCL9_HUMAN

Protein

B-cell CLL/lymphoma 9 protein

Gene

BCL9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 4 (23 Sep 2008)
      Previous versions | rss
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    Functioni

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

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

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

    Keywords - Biological processi

    Wnt signaling pathway

    Enzyme and pathway databases

    ReactomeiREACT_200731. deactivation of the beta-catenin transactivating complex.
    REACT_200753. formation of the beta-catenin:TCF transactivating complex.
    SignaLinkiO00512.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:BCL9
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:1008. BCL9.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. cis-Golgi network Source: MGI
    2. Golgi apparatus Source: Ensembl
    3. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    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.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi358 – 3581H → A: Abolishes interaction with CTNNB1. 1 Publication
    Mutagenesisi359 – 3591R → A: Abolishes interaction with CTNNB1. 1 Publication
    Mutagenesisi366 – 3661L → A: Abolishes interaction with CTNNB1; when associated with A-369. 1 Publication
    Mutagenesisi369 – 3691I → A: Abolishes interaction with CTNNB1; when associated with A-366. 1 Publication

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    PharmGKBiPA25318.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14261426B-cell CLL/lymphoma 9 proteinPRO_0000064885Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei104 – 1041PhosphoserineBy similarity
    Modified residuei172 – 1721Phosphothreonine1 Publication
    Modified residuei315 – 3151Phosphothreonine1 Publication
    Modified residuei318 – 3181Phosphoserine1 Publication
    Modified residuei352 – 3521PhosphoserineBy similarity
    Modified residuei687 – 6871PhosphoserineBy similarity
    Modified residuei844 – 8441N6-acetyllysineBy similarity
    Modified residuei907 – 9071Phosphoserine1 Publication
    Modified residuei917 – 9171Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO00512.
    PaxDbiO00512.
    PRIDEiO00512.

    PTM databases

    PhosphoSiteiO00512.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    BgeeiO00512.
    CleanExiHS_BCL9.
    GenevestigatoriO00512.

    Organism-specific databases

    HPAiHPA020274.

    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'.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    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

    Protein-protein interaction databases

    BioGridi107079. 5 interactions.
    IntActiO00512. 8 interactions.
    MINTiMINT-4773273.
    STRINGi9606.ENSP00000234739.

    Structurei

    Secondary structure

    1
    1426
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi178 – 1803
    Helixi182 – 19312
    Beta strandi196 – 1994
    Helixi353 – 37321

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliO00512.
    SMRiO00512. Positions 174-205, 348-374.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO00512.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni177 – 20529Interacts with PYGO1Add
    BLAST
    Regioni358 – 37417Interacts with CTNNB1Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi231 – 13781148Pro-richAdd
    BLAST
    Compositional biasi331 – 3355Poly-Pro
    Compositional biasi514 – 5174Poly-Pro
    Compositional biasi900 – 9034Poly-Ala
    Compositional biasi970 – 9734Poly-Pro

    Sequence similaritiesi

    Belongs to the BCL9 family.Curated

    Phylogenomic databases

    eggNOGiNOG74241.
    HOGENOMiHOG000060118.
    HOVERGENiHBG031116.
    InParanoidiO00512.
    OMAiPGGSDML.
    OrthoDBiEOG7327N1.
    PhylomeDBiO00512.
    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.

    O00512-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHSSNPKVRS SPSGNTQSSP KSKQEVMVRP PTVMSPSGNP QLDSKFSNQG     50
    KQGGSASQSQ PSPCDSKSGG HTPKALPGPG GSMGLKNGAG NGAKGKGKRE 100
    RSISADSFDQ RDPGTPNDDS DIKECNSADH IKSQDSQHTP HSMTPSNATA 150
    PRSSTPSHGQ TTATEPTPAQ KTPAKVVYVF STEMANKAAE AVLKGQVETI 200
    VSFHIQNISN NKTERSTAPL NTQISALRND PKPLPQQPPA PANQDQNSSQ 250
    NTRLQPTPPI PAPAPKPAAP PRPLDRESPG VENKLIPSVG SPASSTPLPP 300
    DGTGPNSTPN NRAVTPVSQG SNSSSADPKA PPPPPVSSGE PPTLGENPDG 350
    LSQEQLEHRE RSLQTLRDIQ RMLFPDEKEF TGAQSGGPQQ NPGVLDGPQK 400
    KPEGPIQAMM AQSQSLGKGP GPRTDVGAPF GPQGHRDVPF SPDEMVPPSM 450
    NSQSGTIGPD HLDHMTPEQI AWLKLQQEFY EEKRRKQEQV VVQQCSLQDM 500
    MVHQHGPRGV VRGPPPPYQM TPSEGWAPGG TEPFSDGINM PHSLPPRGMA 550
    PHPNMPGSQM RLPGFAGMIN SEMEGPNVPN PASRPGLSGV SWPDDVPKIP 600
    DGRNFPPGQG IFSGPGRGER FPNPQGLSEE MFQQQLAEKQ LGLPPGMAME 650
    GIRPSMEMNR MIPGSQRHME PGNNPIFPRI PVEGPLSPSR GDFPKGIPPQ 700
    MGPGRELEFG MVPSGMKGDV NLNVNMGSNS QMIPQKMREA GAGPEEMLKL 750
    RPGGSDMLPA QQKMVPLPFG EHPQQEYGMG PRPFLPMSQG PGSNSGLRNL 800
    REPIGPDQRT NSRLSHMPPL PLNPSSNPTS LNTAPPVQRG LGRKPLDISV 850
    AGSQVHSPGI NPLKSPTMHQ VQSPMLGSPS GNLKSPQTPS QLAGMLAGPA 900
    AAASIKSPPV LGSAAASPVH LKSPSLPAPS PGWTSSPKPP LQSPGIPPNH 950
    KAPLTMASPA MLGNVESGGP PPPTASQPAS VNIPGSLPSS TPYTMPPEPT 1000
    LSQNPLSIMM SRMSKFAMPS STPLYHDAIK TVASSDDDSP PARSPNLPSM 1050
    NNMPGMGINT QNPRISGPNP VVPMPTLSPM GMTQPLSHSN QMPSPNAVGP 1100
    NIPPHGVPMG PGLMSHNPIM GHGSQEPPMV PQGRMGFPQG FPPVQSPPQQ 1150
    VPFPHNGPSG GQGSFPGGMG FPGEGPLGRP SNLPQSSADA ALCKPGGPGG 1200
    PDSFTVLGNS MPSVFTDPDL QEVIRPGATG IPEFDLSRII PSEKPSQTLQ 1250
    YFPRGEVPGR KQPQGPGPGF SHMQGMMGEQ APRMGLALPG MGGPGPVGTP 1300
    DIPLGTAPSM PGHNPMRPPA FLQQGMMGPH HRMMSPAQST MPGQPTLMSN 1350
    PAAAVGMIPG KDRGPAGLYT HPGPVGSPGM MMSMQGMMGP QQNIMIPPQM 1400
    RPRGMAADVG MGGFSQGPGN PGNMMF 1426
    Length:1,426
    Mass (Da):149,290
    Last modified:September 23, 2008 - v4
    Checksum:i51EF3D0DCA2103CB
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti240 – 2401A → V in CAA73942. (PubMed:9490669)Curated
    Sequence conflicti487 – 4871Q → P in CAA73942. (PubMed:9490669)Curated
    Sequence conflicti609 – 6091Q → R in CAA73942. (PubMed:9490669)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti671 – 6711P → S.
    Corresponds to variant rs3820129 [ dbSNP | Ensembl ].
    VAR_046545
    Natural varianti782 – 7821R → K.
    Corresponds to variant rs34002844 [ dbSNP | Ensembl ].
    VAR_046546

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y13620 mRNA. Translation: CAA73942.1. Frameshift.
    AL359207 Genomic DNA. Translation: CAI15198.1.
    CH471223 Genomic DNA. Translation: EAW50932.1.
    CCDSiCCDS30833.1.
    RefSeqiNP_004317.2. NM_004326.3.
    XP_005273028.1. XM_005272971.2.
    XP_006711546.1. XM_006711483.1.
    UniGeneiHs.415209.

    Genome annotation databases

    EnsembliENST00000234739; ENSP00000234739; ENSG00000116128.
    GeneIDi607.
    KEGGihsa:607.
    UCSCiuc001epq.3. human.

    Keywords - Coding sequence diversityi

    Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y13620 mRNA. Translation: CAA73942.1 . Frameshift.
    AL359207 Genomic DNA. Translation: CAI15198.1 .
    CH471223 Genomic DNA. Translation: EAW50932.1 .
    CCDSi CCDS30833.1.
    RefSeqi NP_004317.2. NM_004326.3.
    XP_005273028.1. XM_005272971.2.
    XP_006711546.1. XM_006711483.1.
    UniGenei Hs.415209.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2GL7 X-ray 2.60 C/F 347-392 [» ]
    2VP7 X-ray 1.65 B 174-205 [» ]
    2VPB X-ray 1.59 B 174-205 [» ]
    2VPD X-ray 2.77 B/D 174-205 [» ]
    2VPE X-ray 1.70 B/D 177-205 [» ]
    2VPG X-ray 1.60 B/D 177-205 [» ]
    3SL9 X-ray 2.20 C/D/F/H 344-396 [» ]
    ProteinModelPortali O00512.
    SMRi O00512. Positions 174-205, 348-374.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107079. 5 interactions.
    IntActi O00512. 8 interactions.
    MINTi MINT-4773273.
    STRINGi 9606.ENSP00000234739.

    PTM databases

    PhosphoSitei O00512.

    Proteomic databases

    MaxQBi O00512.
    PaxDbi O00512.
    PRIDEi O00512.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000234739 ; ENSP00000234739 ; ENSG00000116128 .
    GeneIDi 607.
    KEGGi hsa:607.
    UCSCi uc001epq.3. human.

    Organism-specific databases

    CTDi 607.
    GeneCardsi GC01P147013.
    H-InvDB HIX0028826.
    HGNCi HGNC:1008. BCL9.
    HPAi HPA020274.
    MIMi 602597. gene.
    neXtProti NX_O00512.
    PharmGKBi PA25318.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG74241.
    HOGENOMi HOG000060118.
    HOVERGENi HBG031116.
    InParanoidi O00512.
    OMAi PGGSDML.
    OrthoDBi EOG7327N1.
    PhylomeDBi O00512.
    TreeFami TF331144.

    Enzyme and pathway databases

    Reactomei REACT_200731. deactivation of the beta-catenin transactivating complex.
    REACT_200753. formation of the beta-catenin:TCF transactivating complex.
    SignaLinki O00512.

    Miscellaneous databases

    EvolutionaryTracei O00512.
    GeneWikii BCL9.
    GenomeRNAii 607.
    NextBioi 2469.
    PROi O00512.
    SOURCEi Search...

    Gene expression databases

    Bgeei O00512.
    CleanExi HS_BCL9.
    Genevestigatori O00512.

    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. "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.
      , 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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-318, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    6. 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.

    Entry informationi

    Entry nameiBCL9_HUMAN
    AccessioniPrimary (citable) accession number: O00512
    Secondary accession number(s): Q5T489
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2002
    Last sequence update: September 23, 2008
    Last modified: October 1, 2014
    This is version 129 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Caution

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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3