CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016214
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 B-cell CLL/lymphoma 9-like protein 
Protein Synonyms/Alias
 B-cell lymphoma 9-like protein; BCL9-like protein; Protein BCL9-2 
Gene Name
 BCL9L 
Gene Synonyms/Alias
 DLNB11 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
36HCPPAPAKPMHPENKacetylation[1, 2, 3]
108VPPFSSLKGKVKRDRacetylation[2]
110PFSSLKGKVKRDRSVacetylation[2]
137PSLDSEAKEVAPRSKacetylation[2, 4, 5]
Reference
 [1] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [3] Proteome-wide prediction of acetylation substrates.
 Basu A, Rose KL, Zhang J, Beavis RC, Ueberheide B, Garcia BA, Chait B, Zhao Y, Hunt DF, Segal E, Allis CD, Hake SB.
 Proc Natl Acad Sci U S A. 2009 Aug 18;106(33):13785-90. [PMID: 19666589]
 [4] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [5] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 
Functional Description
 Transcriptional regulator that acts as an activator. Promotes beta-catenin transcriptional activity. Plays a role in tumorigenesis. Enhances the neoplastic transforming activity of CTNNB1 (By similarity). 
Sequence Annotation
 REGION 304 533 Necessary for interaction with CTNNB1 (By
 MOD_RES 21 21 Phosphoserine.
 MOD_RES 25 25 Phosphoserine.
 MOD_RES 36 36 N6-acetyllysine.
 MOD_RES 88 88 Phosphoserine.
 MOD_RES 108 108 N6-acetyllysine.
 MOD_RES 116 116 Phosphoserine.
 MOD_RES 118 118 Phosphoserine.
 MOD_RES 137 137 N6-acetyllysine.
 MOD_RES 750 750 Phosphoserine.
 MOD_RES 813 813 Phosphoserine.
 MOD_RES 915 915 Phosphoserine.
 MOD_RES 975 975 Phosphoserine.
 MOD_RES 987 987 Phosphoserine (By similarity).
 MOD_RES 997 997 Phosphoserine (By similarity).
 MOD_RES 1004 1004 Phosphoserine.
 MOD_RES 1010 1010 Phosphoserine.
 MOD_RES 1017 1017 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Activator; Alternative splicing; Complete proteome; Nucleus; Phosphoprotein; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1499 AA 
Protein Sequence
MRILANKTRL PHPRRREAPG SPPLSPRGHC PPAPAKPMHP ENKLTNHGKT GNGGAQSQHQ 60
NVNQGPTCNV GSKGVGAGNH GAKANQISPS NSSLKNPQAG VPPFSSLKGK VKRDRSVSVD 120
SGEQREAGTP SLDSEAKEVA PRSKRRCVLE RKQPYSGDEW CSGPDSEEDD KPIGATHNCN 180
VADPAMAAPQ LGPGQTTQLP LSESSVPGAP HGPPPGLRPD APGGGGGGGG VPGKPPSQFV 240
YVFTTHLANT AAEAVLQGRA DSILAYHQQN VPRAKLDQAP KVPPTPEPLP LSTPSAGTPQ 300
SQPPPLPPPP PPAPGSAPPA LPPEGPPEDS SQDLAPNSVG AASTGGGTGG THPNTPTATT 360
ANNPLPPGGD PSSAPGPALL GEAAAPGNGQ RSLVGSEGLS KEQLEHRERS LQTLRDIERL 420
LLRSGETEPF LKGPPGGAGE GGPPAQAPPP PQQPPTAPPS GLKKYEEPLQ SMISQTQSLG 480
GPPLEHEVPG HPPGGDMGQQ MNMMIQRLGQ DSLTPEQVAW RKLQEEYYEE KRRKEEQIGL 540
HGSRPLQDMM GMGGMMVRGP PPPYHSKPGD QWPPGMGAQL RGPMDVQDPM QLRGGPPFPG 600
PRFPGNQIQR VPGFGGMQSM PMEVPMNAMQ RPVRPGMGWT EDLPPMGGPS NFAQNTMPYP 660
GGQGEAERFM TPRVREELLR HQLLEKRSMG MQRPLGMAGS GMGQSMEMER MMQAHRQMDP 720
AMFPGQMAGG EGLAGTPMGM EFGGGRGLLS PPMGQSGLRE VDPPMGPGNL NMNMNVNMNM 780
NMNLNVQMTP QQQMLMSQKM RGPGDLMGPQ GLSPEEMARV RAQNSSGVMG GPQKMLMPSQ 840
FPNQGQQGFS GGQGPYQAMS QDMGNTQDMF SPDQSSMPMS NVGTTRLSHM PLPPASNPPG 900
TVHSAPNRGL GRRPSDLTIS INQMGSPGMG HLKSPTLSQV HSPLVTSPSA NLKSPQTPSQ 960
MVPLPSANPP GPLKSPQVLG SSLSVRSPTG SPSRLKSPSM AVPSPGWVAS PKTAMPSPGV 1020
SQNKQPPLNM NSSTTLSNME QGTLPPSGPR SSSSAPPANP PSGLMNPSLP FTSSPDPTPS 1080
QNPLSLMMTQ MSKYAMPSST PLYHNAIKTI ATSDDELLPD RPLLPPPPPP QGSGPGISNS 1140
QPSQMHLNSA AAQSPMGMNL PGQQPLSHEP PPAMLPSPTP LGSNIPLHPN AQGTGGPPQN 1200
SMMMAPGGPD SLNAPCGPVP SSSQMMPFPP RLQQPHGAMA PTGGGGGGPG LQQHYPSGMA 1260
LPPEDLPNQP PGPMPPQQHL MGKAMAGRMG DAYPPGVLPG VASVLNDPEL SEVIRPTPTG 1320
IPEFDLSRII PSEKPSSTLQ YFPKSENQPP KAQPPNLHLM NLQNMMAEQT PSRPPNLPGQ 1380
QGVQRGLNMS MCHPGQMSLL GRTGVPPQQG MVPHGLHQGV MSPPQGLMTQ QNFMLMKQRG 1440
VGGEVYSQPP HMLSPQGSLM GPPPQQNLMV SHPLRQRSVS LDSQMGYLPA PGGMANLPF 1499 
Gene Ontology
 GO:0005634; C:nucleus; IC:BHF-UCL.
 GO:0008013; F:beta-catenin binding; IDA:MGI.
 GO:0003713; F:transcription coactivator activity; NAS:BHF-UCL.
 GO:0060070; P:canonical Wnt receptor signaling pathway; IEA:Compara.
 GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IMP:BHF-UCL.
 GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:BHF-UCL.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
 GO:0035914; P:skeletal muscle cell differentiation; IEA:Compara.
 GO:0035019; P:somatic stem cell maintenance; IEA:Compara.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR015668; Bcl-9.
 IPR024670; BCL9_beta-catenin-bd_dom. 
Pfam
 PF11502; BCL9 
SMART
  
PROSITE
  
PRINTS