CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022998
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Bromodomain adjacent to zinc finger domain protein 2A 
Protein Synonyms/Alias
 Transcription termination factor I-interacting protein 5; TTF-I-interacting protein 5; Tip5; hWALp3 
Gene Name
 BAZ2A 
Gene Synonyms/Alias
 KIAA0314; TIP5 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
568RREVRIKKGSHRWQGubiquitination[1]
680RGRPPKVKITELLNKacetylation[2]
1676AWEKSVNKVTCLVCRubiquitination[3, 4]
1746PKRGQKRKSGYSLNFacetylation[5]
1901WEEFYQGKQANL***ubiquitination[1, 6]
Reference
 [1] 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]
 [2] Reversible acetylation of the chromatin remodelling complex NoRC is required for non-coding RNA-dependent silencing.
 Zhou Y, Schmitz KM, Mayer C, Yuan X, Akhtar A, Grummt I.
 Nat Cell Biol. 2009 Aug;11(8):1010-6. [PMID: 19578370]
 [3] 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]
 [4] 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]
 [5] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [6] 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
Functional Description
 Essential component of the NoRC (nucleolar remodeling complex) complex, a complex that mediates silencing of a fraction of rDNA by recruiting histone-modifying enzymes and DNA methyltransferases, leading to heterochromatin formation and transcriptional silencing. In the complex, it plays a central role by being recruited to rDNA and by targeting chromatin modifying enzymes such as HDAC1, leading to repress RNA polymerase I transcription. Recruited to rDNA via its interaction with TTF1 and its ability to recognize and bind histone H4 acetylated on 'Lys- 16' (H4K16ac), leading to deacetylation of H4K5ac, H4K8ac, H4K12ac but not H4K16ac. Specifically binds pRNAs, 150-250 nucleotide RNAs that are complementary in sequence to the rDNA promoter; pRNA- binding is required for heterochromatin formation and rDNA silencing (By similarity). 
Sequence Annotation
 DOMAIN 546 617 MBD.
 DOMAIN 848 913 DDT.
 DOMAIN 1810 1880 Bromo.
 DNA_BIND 649 661 A.T hook 1.
 DNA_BIND 670 682 A.T hook 2.
 DNA_BIND 1186 1198 A.T hook 3.
 DNA_BIND 1404 1416 A.T hook 4.
 ZN_FING 1676 1726 PHD-type.
 MOD_RES 134 134 Phosphoserine.
 MOD_RES 509 509 Phosphoserine.
 MOD_RES 680 680 N6-acetyllysine; by KAT8.
 MOD_RES 1051 1051 Phosphoserine (By similarity).
 MOD_RES 1397 1397 Phosphoserine.
 MOD_RES 1559 1559 Phosphoserine.
 MOD_RES 1747 1747 Phosphoserine.
 MOD_RES 1770 1770 Phosphoserine.
 MOD_RES 1783 1783 Phosphoserine.
 MOD_RES 1785 1785 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Bromodomain; Chromatin regulator; Coiled coil; Complete proteome; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Repressor; RNA-binding; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1905 AA 
Protein Sequence
MEMEANDHFN FTGLPPAPAA SGLKPSPSSG EGLYTNGSPM NFPQQGKSLN GDVNVNGLST 60
VSHTTTSGIL NSAPHSSSTS HLHHPSVAYD CLWNYSQYPS ANPGSNLKDP PLLSQFSGGQ 120
YPLNGILGGS RQPSSPSHNT NLRAGSQEFW ANGTQSPMGL NFDSQELYDS FPDQNFEVMP 180
NGPPSFFTSP QTSPMLGSSI QTFAPSQEVG SGIHPDEAAE KEMTSVVAEN GTGLVGSLEL 240
EEEQPELKMC GYNGSVPSVE SLHQEVSVLV PDPTVSCLDD PSHLPDQLED TPILSEDSLE 300
PFNSLAPEPV SGGLYGIDDT ELMGAEDKLP LEDSPVISAL DCPSLNNATA FSLLADDSQT 360
STSIFASPTS PPVLGESVLQ DNSFDLNNGS DAEQEEMETQ SSDFPPSLTQ PAPDQSSTIQ 420
LHPATSPAVS PTTSPAVSLV VSPAASPEIS PEVCPAASTV VSPAVFSVVS PASSAVLPAV 480
SLEVPLTASV TSPKASPVTS PAAAFPTASP ANKDVSSFLE TTADVEEITG EGLTASGSGD 540
VMRRRIATPE EVRLPLQHGW RREVRIKKGS HRWQGETWYY GPCGKRMKQF PEVIKYLSRN 600
VVHSVRREHF SFSPRMPVGD FFEERDTPEG LQWVQLSAEE IPSRIQAITG KRGRPRNTEK 660
AKTKEVPKVK RGRGRPPKVK ITELLNKTDN RPLKKLEAQE TLNEEDKAKI AKSKKKMRQK 720
VQRGECQTTI QGQARNKRKQ ETKSLKQKEA KKKSKAEKEK GKTKQEKLKE KVKREKKEKV 780
KMKEKEEVTK AKPACKADKT LATQRRLEER QRQQMILEEM KKPTEDMCLT DHQPLPDFSR 840
VPGLTLPSGA FSDCLTIVEF LHSFGKVLGF DPAKDVPSLG VLQEGLLCQG DSLGEVQDLL 900
VRLLKAALHD PGFPSYCQSL KILGEKVSEI PLTRDNVSEI LRCFLMAYGV EPALCDRLRT 960
QPFQAQPPQQ KAAVLAFLVH ELNGSTLIIN EIDKTLESMS SYRKNKWIVE GRLRRLKTVL 1020
AKRTGRSEVE MEGPEECLGR RRSSRIMEET SGMEEEEEEE SIAAVPGRRG RRDGEVDATA 1080
SSIPELERQI EKLSKRQLFF RKKLLHSSQM LRAVSLGQDR YRRRYWVLPY LAGIFVEGTE 1140
GNLVPEEVIK KETDSLKVAA HASLNPALFS MKMELAGSNT TASSPARARG RPRKTKPGSM 1200
QPRHLKSPVR GQDSEQPQAQ LQPEAQLHAP AQPQPQLQLQ LQSHKGFLEQ EGSPLSLGQS 1260
QHDLSQSAFL SWLSQTQSHS SLLSSSVLTP DSSPGKLDPA PSQPPEEPEP DEAESSPDPQ 1320
ALWFNISAQM PCNAAPTPPP AVSEDQPTPS PQQLASSKPM NRPSAANPCS PVQFSSTPLA 1380
GLAPKRRAGD PGEMPQSPTG LGQPKRRGRP PSKFFKQMEQ RYLTQLTAQP VPPEMCSGWW 1440
WIRDPEMLDA MLKALHPRGI REKALHKHLN KHRDFLQEVC LRPSADPIFE PRQLPAFQEG 1500
IMSWSPKEKT YETDLAVLQW VEELEQRVIM SDLQIRGWTC PSPDSTREDL AYCEHLSDSQ 1560
EDITWRGRGR EGLAPQRKTT NPLDLAVMRL AALEQNVERR YLREPLWPTH EVVLEKALLS 1620
TPNGAPEGTT TEISYEITPR IRVWRQTLER CRSAAQVCLC LGQLERSIAW EKSVNKVTCL 1680
VCRKGDNDEF LLLCDGCDRG CHIYCHRPKM EAVPEGDWFC TVCLAQQVEG EFTQKPGFPK 1740
RGQKRKSGYS LNFSEGDGRR RRVLLRGRES PAAGPRYSEE GLSPSKRRRL SMRNHHSDLT 1800
FCEIILMEME SHDAAWPFLE PVNPRLVSGY RRIIKNPMDF STMRERLLRG GYTSSEEFAA 1860
DALLVFDNCQ TFNEDDSEVG KAGHIMRRFF ESRWEEFYQG KQANL 1905 
Gene Ontology
 GO:0005677; C:chromatin silencing complex; ISS:UniProtKB.
 GO:0005730; C:nucleolus; ISS:UniProtKB.
 GO:0033553; C:rDNA heterochromatin; ISS:UniProtKB.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0070577; F:histone acetyl-lysine binding; ISS:UniProtKB.
 GO:0016922; F:ligand-dependent nuclear receptor binding; NAS:BHF-UCL.
 GO:0003723; F:RNA binding; ISS:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006338; P:chromatin remodeling; NAS:UniProtKB.
 GO:0000183; P:chromatin silencing at rDNA; ISS:UniProtKB.
 GO:0006306; P:DNA methylation; ISS:UniProtKB.
 GO:0070869; P:heterochromatin assembly involved in chromatin silencing; IEA:Compara.
 GO:0016575; P:histone deacetylation; ISS:UniProtKB.
 GO:0051567; P:histone H3-K9 methylation; IEA:Compara.
 GO:0070933; P:histone H4 deacetylation; IEA:Compara.
 GO:0034770; P:histone H4-K20 methylation; IEA:Compara.
 GO:0006351; P:transcription, DNA-dependent; NAS:UniProtKB. 
Interpro
 IPR017956; AT_hook_DNA-bd_motif.
 IPR001487; Bromodomain.
 IPR018359; Bromodomain_CS.
 IPR004022; DDT_dom.
 IPR018500; DDT_dom_subgr.
 IPR018501; DDT_dom_superfamily.
 IPR016177; DNA-bd_integrase-typ.
 IPR001739; Methyl_CpG_DNA-bd.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF00439; Bromodomain
 PF02791; DDT
 PF01429; MBD
 PF00628; PHD 
SMART
 SM00384; AT_hook
 SM00297; BROMO
 SM00571; DDT
 SM00391; MBD
 SM00249; PHD 
PROSITE
 PS00633; BROMODOMAIN_1
 PS50014; BROMODOMAIN_2
 PS50827; DDT
 PS50982; MBD
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS
 PR00503; BROMODOMAIN.