BCL9_HUMAN
ID BCL9_HUMAN Reviewed; 1426 AA.
AC O00512; Q5T489;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 4.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=B-cell CLL/lymphoma 9 protein;
DE Short=B-cell lymphoma 9 protein;
DE Short=Bcl-9;
DE AltName: Full=Protein legless homolog;
GN Name=BCL9;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHROMOSOMAL TRANSLOCATION.
RC TISSUE=Fetal brain;
RX PubMed=9490669;
RA Willis T.G., Zalcberg I.R., Coignet L.J.A., Wlodarska I., Stul M.,
RA Jadayel D.M., Bastard C., Treleaven J.G., Catovsky D., Silva M.L.M.,
RA Dyer M.J.S.;
RT "Molecular cloning of translocation t(1;14)(q21;q32) defines a novel gene
RT (BCL9) at chromosome 1q21.";
RL Blood 91:1873-1881(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION.
RX PubMed=11955446; DOI=10.1016/s0092-8674(02)00679-7;
RA Kramps T., Peter O., Brunner E., Nellen D., Froesch B., Chatterjee S.,
RA Murone M., Zuellig S., Basler K.;
RT "Wnt/wingless signaling requires BCL9/legless-mediated recruitment of
RT pygopus to the nuclear beta-catenin-TCF complex.";
RL Cell 109:47-60(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-318, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-172, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-315, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-907 AND SER-917, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104; SER-157; THR-315;
RP SER-687; SER-689 AND SER-917, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-315, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 347-392 IN COMPLEX WITH CTNNB1
RP AND TCF7L2, INTERACTION WITH CTNNB1, AND MUTAGENESIS OF HIS-358; ARG-359;
RP LEU-366 AND ILE-369.
RX PubMed=17052462; DOI=10.1016/j.molcel.2006.09.001;
RA Sampietro J., Dahlberg C.L., Cho U.S., Hinds T.R., Kimelman D., Xu W.;
RT "Crystal structure of a beta-catenin/BCL9/Tcf4 complex.";
RL Mol. Cell 24:293-300(2006).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 174-205 IN COMPLEX WITH PYGO1 AND
RP HISTONE H3K4ME2.
RX PubMed=18498752; DOI=10.1016/j.molcel.2008.03.011;
RA Fiedler M., Sanchez-Barrena M.J., Nekrasov M., Mieszczanek J., Rybin V.,
RA Muller J., Evans P., Bienz M.;
RT "Decoding of methylated histone H3 tail by the Pygo-BCL9 Wnt signaling
RT complex.";
RL Mol. Cell 30:507-518(2008).
CC -!- FUNCTION: Involved in signal transduction through the Wnt pathway.
CC Promotes beta-catenin's transcriptional activity (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:11955446}.
CC -!- SUBUNIT: Binds to beta-catenin (CTNNB1), PYGO1 and PYGO2; the
CC interaction with PYGO1 increases PYGO1 affinity to histone H3
CC methylated at 'Lys 4'. {ECO:0000269|PubMed:17052462,
CC ECO:0000269|PubMed:18498752}.
CC -!- INTERACTION:
CC O00512; Q6P1J9: CDC73; NbExp=2; IntAct=EBI-533127, EBI-930143;
CC O00512; P35222: CTNNB1; NbExp=5; IntAct=EBI-533127, EBI-491549;
CC O00512; Q9Y3Y4: PYGO1; NbExp=8; IntAct=EBI-533127, EBI-3397474;
CC O00512; Q9BRQ0: PYGO2; NbExp=3; IntAct=EBI-533127, EBI-932471;
CC O00512; P18824: arm; Xeno; NbExp=3; IntAct=EBI-533127, EBI-216128;
CC O00512; Q9V9W8: pygo; Xeno; NbExp=3; IntAct=EBI-533127, EBI-152653;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected at low levels in thymus, prostate, testis,
CC ovary and small intestine, and at lower levels in spleen, colon and
CC blood.
CC -!- DISEASE: Note=A chromosomal aberration involving BCL9 is found in a
CC patient with precursor B-cell acute lymphoblastic leukemia (ALL).
CC Translocation t(1;14)(q21;q32). This translocation leaves the coding
CC region intact, but may have pathogenic effects due to alterations in
CC the expression level of BCL9. Several cases of translocations within
CC the 3'-UTR of BCL9 have been found in B-cell malignancies.
CC {ECO:0000269|PubMed:9490669}.
CC -!- SIMILARITY: Belongs to the BCL9 family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-27 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA73942.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/BCL9ID466.html";
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DR EMBL; Y13620; CAA73942.1; ALT_FRAME; mRNA.
DR EMBL; AL359207; CAI15198.1; -; Genomic_DNA.
DR EMBL; CH471223; EAW50932.1; -; Genomic_DNA.
DR CCDS; CCDS30833.1; -.
DR RefSeq; NP_004317.2; NM_004326.3.
DR RefSeq; XP_005273028.1; XM_005272971.4.
DR PDB; 2GL7; X-ray; 2.60 A; C/F=347-392.
DR PDB; 2VP7; X-ray; 1.65 A; B=174-205.
DR PDB; 2VPB; X-ray; 1.59 A; B=174-205.
DR PDB; 2VPD; X-ray; 2.77 A; B/D=174-205.
DR PDB; 2VPE; X-ray; 1.70 A; B/D=177-205.
DR PDB; 2VPG; X-ray; 1.60 A; B/D=177-205.
DR PDB; 3SL9; X-ray; 2.20 A; C/D/F/H=344-396.
DR PDBsum; 2GL7; -.
DR PDBsum; 2VP7; -.
DR PDBsum; 2VPB; -.
DR PDBsum; 2VPD; -.
DR PDBsum; 2VPE; -.
DR PDBsum; 2VPG; -.
DR PDBsum; 3SL9; -.
DR AlphaFoldDB; O00512; -.
DR SMR; O00512; -.
DR BioGRID; 107079; 70.
DR CORUM; O00512; -.
DR IntAct; O00512; 56.
DR MINT; O00512; -.
DR STRING; 9606.ENSP00000234739; -.
DR BindingDB; O00512; -.
DR ChEMBL; CHEMBL3712821; -.
DR GlyGen; O00512; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O00512; -.
DR PhosphoSitePlus; O00512; -.
DR BioMuta; BCL9; -.
DR EPD; O00512; -.
DR jPOST; O00512; -.
DR MassIVE; O00512; -.
DR MaxQB; O00512; -.
DR PaxDb; O00512; -.
DR PeptideAtlas; O00512; -.
DR PRIDE; O00512; -.
DR ProteomicsDB; 47950; -.
DR Antibodypedia; 20242; 166 antibodies from 24 providers.
DR DNASU; 607; -.
DR Ensembl; ENST00000234739.8; ENSP00000234739.3; ENSG00000116128.12.
DR GeneID; 607; -.
DR KEGG; hsa:607; -.
DR MANE-Select; ENST00000234739.8; ENSP00000234739.3; NM_004326.4; NP_004317.2.
DR UCSC; uc031uul.2; human.
DR CTD; 607; -.
DR DisGeNET; 607; -.
DR GeneCards; BCL9; -.
DR HGNC; HGNC:1008; BCL9.
DR HPA; ENSG00000116128; Low tissue specificity.
DR MIM; 602597; gene.
DR neXtProt; NX_O00512; -.
DR OpenTargets; ENSG00000116128; -.
DR PharmGKB; PA25318; -.
DR VEuPathDB; HostDB:ENSG00000116128; -.
DR eggNOG; ENOG502QREN; Eukaryota.
DR GeneTree; ENSGT00730000110915; -.
DR HOGENOM; CLU_004930_1_0_1; -.
DR InParanoid; O00512; -.
DR OMA; ECNSTEH; -.
DR OrthoDB; 156519at2759; -.
DR PhylomeDB; O00512; -.
DR TreeFam; TF331144; -.
DR PathwayCommons; O00512; -.
DR Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
DR SignaLink; O00512; -.
DR SIGNOR; O00512; -.
DR BioGRID-ORCS; 607; 59 hits in 1076 CRISPR screens.
DR ChiTaRS; BCL9; human.
DR EvolutionaryTrace; O00512; -.
DR GeneWiki; BCL9; -.
DR GenomeRNAi; 607; -.
DR Pharos; O00512; Tbio.
DR PRO; PR:O00512; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O00512; protein.
DR Bgee; ENSG00000116128; Expressed in cortical plate and 137 other tissues.
DR ExpressionAtlas; O00512; baseline and differential.
DR Genevisible; O00512; HS.
DR GO; GO:1990907; C:beta-catenin-TCF complex; IDA:FlyBase.
DR GO; GO:0005801; C:cis-Golgi network; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0016528; C:sarcoplasm; IEA:Ensembl.
DR GO; GO:0008013; F:beta-catenin binding; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:InterPro.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0045445; P:myoblast differentiation; IEA:Ensembl.
DR GO; GO:0014908; P:myotube differentiation involved in skeletal muscle regeneration; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR Gene3D; 3.30.40.10; -; 1.
DR IDEAL; IID00002; -.
DR InterPro; IPR015668; Bcl-9/Bcl-9l.
DR InterPro; IPR024670; BCL9_beta-catenin-bd_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15185; PTHR15185; 1.
DR Pfam; PF11502; BCL9; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromosomal rearrangement; Methylation; Nucleus;
KW Phosphoprotein; Proto-oncogene; Reference proteome; Wnt signaling pathway.
FT CHAIN 1..1426
FT /note="B-cell CLL/lymphoma 9 protein"
FT /id="PRO_0000064885"
FT REGION 1..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..205
FT /note="Interaction with PYGO1"
FT REGION 207..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..374
FT /note="Interaction with CTNNB1"
FT /evidence="ECO:0000269|PubMed:17052462"
FT REGION 597..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 910..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1032..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1152..1203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1253..1275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..274
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..341
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..892
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..947
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1052
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 172
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 315
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D219"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 801
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9D219"
FT MOD_RES 844
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D219"
FT MOD_RES 907
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 917
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 671
FT /note="P -> S (in dbSNP:rs3820129)"
FT /id="VAR_046545"
FT VARIANT 782
FT /note="R -> K (in dbSNP:rs34002844)"
FT /id="VAR_046546"
FT MUTAGEN 358
FT /note="H->A: Abolishes interaction with CTNNB1."
FT /evidence="ECO:0000269|PubMed:17052462"
FT MUTAGEN 359
FT /note="R->A: Abolishes interaction with CTNNB1."
FT /evidence="ECO:0000269|PubMed:17052462"
FT MUTAGEN 366
FT /note="L->A: Abolishes interaction with CTNNB1; when
FT associated with A-369."
FT /evidence="ECO:0000269|PubMed:17052462"
FT MUTAGEN 369
FT /note="I->A: Abolishes interaction with CTNNB1; when
FT associated with A-366."
FT /evidence="ECO:0000269|PubMed:17052462"
FT CONFLICT 240
FT /note="A -> V (in Ref. 1; CAA73942)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="Q -> P (in Ref. 1; CAA73942)"
FT /evidence="ECO:0000305"
FT CONFLICT 609
FT /note="Q -> R (in Ref. 1; CAA73942)"
FT /evidence="ECO:0000305"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:2VPB"
FT HELIX 182..193
FT /evidence="ECO:0007829|PDB:2VPB"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:2VPD"
FT HELIX 353..373
FT /evidence="ECO:0007829|PDB:3SL9"
SQ SEQUENCE 1426 AA; 149290 MW; 51EF3D0DCA2103CB CRC64;
MHSSNPKVRS SPSGNTQSSP KSKQEVMVRP PTVMSPSGNP QLDSKFSNQG KQGGSASQSQ
PSPCDSKSGG HTPKALPGPG GSMGLKNGAG NGAKGKGKRE RSISADSFDQ RDPGTPNDDS
DIKECNSADH IKSQDSQHTP HSMTPSNATA PRSSTPSHGQ TTATEPTPAQ KTPAKVVYVF
STEMANKAAE AVLKGQVETI VSFHIQNISN NKTERSTAPL NTQISALRND PKPLPQQPPA
PANQDQNSSQ NTRLQPTPPI PAPAPKPAAP PRPLDRESPG VENKLIPSVG SPASSTPLPP
DGTGPNSTPN NRAVTPVSQG SNSSSADPKA PPPPPVSSGE PPTLGENPDG LSQEQLEHRE
RSLQTLRDIQ RMLFPDEKEF TGAQSGGPQQ NPGVLDGPQK KPEGPIQAMM AQSQSLGKGP
GPRTDVGAPF GPQGHRDVPF SPDEMVPPSM NSQSGTIGPD HLDHMTPEQI AWLKLQQEFY
EEKRRKQEQV VVQQCSLQDM MVHQHGPRGV VRGPPPPYQM TPSEGWAPGG TEPFSDGINM
PHSLPPRGMA PHPNMPGSQM RLPGFAGMIN SEMEGPNVPN PASRPGLSGV SWPDDVPKIP
DGRNFPPGQG IFSGPGRGER FPNPQGLSEE MFQQQLAEKQ LGLPPGMAME GIRPSMEMNR
MIPGSQRHME PGNNPIFPRI PVEGPLSPSR GDFPKGIPPQ MGPGRELEFG MVPSGMKGDV
NLNVNMGSNS QMIPQKMREA GAGPEEMLKL RPGGSDMLPA QQKMVPLPFG EHPQQEYGMG
PRPFLPMSQG PGSNSGLRNL REPIGPDQRT NSRLSHMPPL PLNPSSNPTS LNTAPPVQRG
LGRKPLDISV AGSQVHSPGI NPLKSPTMHQ VQSPMLGSPS GNLKSPQTPS QLAGMLAGPA
AAASIKSPPV LGSAAASPVH LKSPSLPAPS PGWTSSPKPP LQSPGIPPNH KAPLTMASPA
MLGNVESGGP PPPTASQPAS VNIPGSLPSS TPYTMPPEPT LSQNPLSIMM SRMSKFAMPS
STPLYHDAIK TVASSDDDSP PARSPNLPSM NNMPGMGINT QNPRISGPNP VVPMPTLSPM
GMTQPLSHSN QMPSPNAVGP NIPPHGVPMG PGLMSHNPIM GHGSQEPPMV PQGRMGFPQG
FPPVQSPPQQ VPFPHNGPSG GQGSFPGGMG FPGEGPLGRP SNLPQSSADA ALCKPGGPGG
PDSFTVLGNS MPSVFTDPDL QEVIRPGATG IPEFDLSRII PSEKPSQTLQ YFPRGEVPGR
KQPQGPGPGF SHMQGMMGEQ APRMGLALPG MGGPGPVGTP DIPLGTAPSM PGHNPMRPPA
FLQQGMMGPH HRMMSPAQST MPGQPTLMSN PAAAVGMIPG KDRGPAGLYT HPGPVGSPGM
MMSMQGMMGP QQNIMIPPQM RPRGMAADVG MGGFSQGPGN PGNMMF
