CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015446
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 BCL-6 corepressor 
Protein Synonyms/Alias
 BCoR 
Gene Name
 BCOR 
Gene Synonyms/Alias
 KIAA1575 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
40VNDGDASKARLELREubiquitination[1]
100LCGLGSEKGREAATSubiquitination[1]
175LDRPASDKQSPLNINubiquitination[1]
392AARLSNGKYPKAPEGacetylation[2]
528NGKSMSLKNKALDWAubiquitination[1]
530KSMSLKNKALDWAIPubiquitination[1]
774ILETSSTKLHPDVPTubiquitination[3]
783HPDVPTDKNLKPNPNubiquitination[1]
786VPTDKNLKPNPNWNQubiquitination[1]
872FHETYTFKQPVFTVSubiquitination[1, 4, 5]
889SVLAGTNKENLGLPVubiquitination[3]
1029RFSELEMKEREGGHPubiquitination[3]
1104DKDLPVEKYFVERQPubiquitination[4, 5]
1460ARRLIVNKNAGETLLubiquitination[1, 3, 4, 5, 6, 7, 8]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [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] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [7] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [8] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572] 
Functional Description
 Transcriptional corepressor. May specifically inhibit gene expression when recruited to promoter regions by sequence specific DNA-binding proteins such as BCL6 and MLLT3. This repression may be mediated at least in part by histone deacetylase activities which can associate with this corepressor. Involved in the repression of TFAP2A; impairs binding of BCL6 and KDM2B to TFAP2A promoter regions. Via repression of TFAP2A acts as a negative regulator of osteo-dentiogenic capacity in adult stem cells; the function implies inhibition of methylation on histone H3 'Lys-4' (H3K4me3) and 'Lys-36' (H3K36me2). 
Sequence Annotation
 REPEAT 1462 1495 ANK 1.
 REPEAT 1496 1525 ANK 2.
 REPEAT 1529 1558 ANK 3.
 REGION 498 514 Interaction with BCL6.
 MOD_RES 336 336 Phosphoserine.
 MOD_RES 340 340 Phosphoserine.
 MOD_RES 365 365 Phosphoserine.
 MOD_RES 367 367 Phosphoserine.
 MOD_RES 392 392 N6-acetyllysine.
 MOD_RES 423 423 Phosphoserine.
 MOD_RES 1139 1139 Phosphoserine.
 MOD_RES 1142 1142 Phosphoserine (By similarity).
 MOD_RES 1410 1410 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; ANK repeat; Chromatin regulator; Complete proteome; Disease mutation; Microphthalmia; Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1755 AA 
Protein Sequence
MLSATPLYGN VHSWMNSERV RMCGASEDRK ILVNDGDASK ARLELREENP LNHNVVDAST 60
AHRIDGLAAL SMDRTGLIRE GLRVPGNIVY SSLCGLGSEK GREAATSTLG GLGFSSERNP 120
EMQFKPNTPE TVEASAVSGK PPNGFSAIYK TPPGIQKSAV ATAEALGLDR PASDKQSPLN 180
INGASYLRLP WVNPYMEGAT PAIYPFLDSP NKYSLNMYKA LLPQQSYSLA QPLYSPVCTN 240
GERFLYLPPP HYVGPHIPSS LASPMRLSTP SASPAIPPLV HCADKSLPWK MGVSPGNPVD 300
SHAYPHIQNS KQPRVPSAKA VTSGLPGDTA LLLPPSPRPS PRVHLPTQPA ADTYSEFHKH 360
YARISTSPSV ALSKPYMTVS SEFPAARLSN GKYPKAPEGG EGAQPVPGHA RKTAVQDRKD 420
GSSPPLLEKQ TVTKDVTDKP LDLSSKVVDV DASKADHMKK MAPTVLVHSR AGSGLVLSGS 480
EIPKETLSPP GNGCAIYRSE IISTAPSSWV VPGPSPNEEN NGKSMSLKNK ALDWAIPQQR 540
SSSCPRMGGT DAVITNVSGS VSSAGRPASA SPAPNANADG TKTSRSSVET TPSVIQHVGQ 600
PPATPAKHSS STSSKGAKAS NPEPSFKANE NGLPPSSIFL SPNEAFRSPP IPYPRSYLPY 660
PAPEGIAVSP LSLHGKGPVY PHPVLLPNGS LFPGHLAPKP GLPYGLPTGR PEFVTYQDAL 720
GLGMVHPMLI PHTPIEITKE EKPERRSRSH ERARYEDPTL RNRFSEILET SSTKLHPDVP 780
TDKNLKPNPN WNQGKTVVKS DKLVYVDLLR EEPDAKTDTN VSKPSFAAES VGQSAEPPKP 840
SVEPALQQHR DFIALREELG RISDFHETYT FKQPVFTVSK DSVLAGTNKE NLGLPVSTPF 900
LEPPLGSDGP AVTFGKTQED PKPFCVGSAP PSVDVTPTYT KDGADEAESN DGKVLKPKPS 960
KLAKRIANSA GYVGDRFKCV TTELYADSSQ LSREQRALQM EGLQEDSILC LPAAYCERAM 1020
MRFSELEMKE REGGHPATKD SEMCKFSPAD WERLKGNQDK KPKSVTLEEA IAEQNESERC 1080
EYSVGNKHRD PFEAPEDKDL PVEKYFVERQ PVSEPPADQV ASDMPHSPTL RVDRKRKVSG 1140
DSSHTETTAE EVPEDPLLKA KRRRVSKDDW PEREMTNSSS NHLEDPHYSE LTNLKVCIEL 1200
TGLHPKKQRH LLHLRERWEQ QVSAADGKPG RQSRKEVTQA TQPEAIPQGT NITEEKPGRK 1260
RAEAKGNRSW SEESLKPSDN EQGLPVFSGS PPMKSLSSTS AGGKKQAQPS CAPASRPPAK 1320
QQKIKENQKT DVLCADEEED CQAASLLQKY TDNSEKPSGK RLCKTKHLIP QESRRGLPLT 1380
GEYYVENADG KVTVRRFRKR PEPSSDYDLS PAKQEPKPFD RLQQLLPASQ STQLPCSSSP 1440
QETTQSRPMP PEARRLIVNK NAGETLLQRA ARLGYEEVVL YCLENKICDV NHRDNAGYCA 1500
LHEACARGWL NIVRHLLEYG ADVNCSAQDG TRPLHDAVEN DHLEIVRLLL SYGADPTLAT 1560
YSGRTIMKMT HSELMEKFLT DYLNDLQGRN DDDASGTWDF YGSSVCEPDD ESGYDVLANP 1620
PGPEDQDDDD DAYSDVFEFE FSETPLLPCY NIQVSVAQGP RNWLLLSDVL KKLKMSSRIF 1680
RCNFPNVEIV TIAEAEFYRQ VSASLLFSCS KDLEAFNPES KELLDLVEFT NEIQTLLGSS 1740
VEWLHPSDLA SDNYW 1755 
Gene Ontology
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0031072; F:heat shock protein binding; IDA:UniProtKB.
 GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
 GO:0044212; F:transcription regulatory region DNA binding; IMP:UniProtKB.
 GO:0007507; P:heart development; IMP:UniProtKB.
 GO:0035518; P:histone H2A monoubiquitination; IDA:UniProtKB.
 GO:0030502; P:negative regulation of bone mineralization; IMP:UniProtKB.
 GO:0000415; P:negative regulation of histone H3-K36 methylation; IMP:UniProtKB.
 GO:0051572; P:negative regulation of histone H3-K4 methylation; IMP:UniProtKB.
 GO:0070171; P:negative regulation of tooth mineralization; IMP:UniProtKB.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
 GO:0042476; P:odontogenesis; IMP:UniProtKB.
 GO:0060021; P:palate development; IMP:UniProtKB.
 GO:0065001; P:specification of axis polarity; IMP:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR002110; Ankyrin_rpt.
 IPR020683; Ankyrin_rpt-contain_dom. 
Pfam
 PF12796; Ank_2 
SMART
 SM00248; ANK 
PROSITE
 PS50297; ANK_REP_REGION
 PS50088; ANK_REPEAT 
PRINTS