CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022999
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tyrosine-protein kinase BAZ1B 
Protein Synonyms/Alias
 Bromodomain adjacent to zinc finger domain protein 1B; Williams syndrome transcription factor; Williams-Beuren syndrome chromosomal region 10 protein; Williams-Beuren syndrome chromosomal region 9 protein; hWALp2 
Gene Name
 BAZ1B 
Gene Synonyms/Alias
 WBSC10; WBSCR10; WBSCR9; WSTF 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
14RKPFPLVKPLPGEEPubiquitination[1]
128DFEVGKEKMLKVKIVubiquitination[2]
281VEDELVKKYSLPSKFubiquitination[2]
287KKYSLPSKFSDFLLDubiquitination[2]
297DFLLDPYKYMTLNPSubiquitination[1, 3, 4]
306MTLNPSTKRKNTGSPubiquitination[1]
322RKPSKKSKTDNSSLSubiquitination[1, 2]
335LSSPLNPKLWCHVHLubiquitination[1]
426GNSKSPKKGLKTPKTacetylation[5]
445MTLLDMAKGTQKMTRubiquitination[2]
483LHLIAYYKENKDREDubiquitination[1]
501ALSCVISKTARLLSSubiquitination[1, 2, 6]
532RYELLEHKKRWASMSubiquitination[2]
588EDQELTGKNLPAFRLubiquitination[2, 3, 4, 6, 7]
778QMSAELWKERLAVLKubiquitination[2, 3, 4]
817KVENGLGKTDRKKEIacetylation[6, 8]
854LLAIQAKKEREIQERubiquitination[2]
885KHKAAAEKAFQEGIAubiquitination[2]
893AFQEGIAKAKLVMRRacetylation[8]
893AFQEGIAKAKLVMRRubiquitination[2, 6]
1043RKPNLGLKSCDGNQEubiquitination[6]
1068EVATRLQKGGLGYVEubiquitination[2, 3, 4, 6, 7]
1089ARVISLEKLKDFGECubiquitination[1]
1151KVASALEKWKTAIREubiquitination[2]
1335DELVLQTKRSSRRQSacetylation[6, 8, 9]
1335DELVLQTKRSSRRQSubiquitination[2, 6, 7, 10]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [2] 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]
 [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] 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]
 [6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 
Functional Description
 Atypical tyrosine-protein kinase that plays a central role in chromatin remodeling and acts as a transcription regulator. Involved in DNA damage response by phosphorylating 'Tyr-142' of histone H2AX (H2AXY142ph). H2AXY142ph plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Essential component of the WICH complex, a chromatin remodeling complex that mobilizes nucleosomes and reconfigures irregular chromatin to a regular nucleosomal array structure. The WICH complex regulates the transcription of various genes, has a role in RNA polymerase I and RNA polymerase III transcription, mediates the histone H2AX phosphorylation at 'Tyr-142', and is involved in the maintenance of chromatin structures during DNA replication processes. In the complex, it mediates the recruitment of the WICH complex to replication foci during DNA replication. Also involved in vitamin D-coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR), which is required for the ligand-bound VDR- mediated transrepression of the CYP27B1 gene. In the WINAC complex, plays an essential role by targeting the complex to acetylated histones, an essential step for VDR-promoter association. 
Sequence Annotation
 DOMAIN 20 126 WAC.
 DOMAIN 604 668 DDT.
 DOMAIN 1356 1426 Bromo.
 ZN_FING 1184 1234 PHD-type.
 REGION 1 345 Mediates the tyrosine-protein kinase
 MOTIF 207 213 C motif.
 MOD_RES 161 161 Phosphoserine (By similarity).
 MOD_RES 266 266 Phosphothreonine.
 MOD_RES 283 283 Phosphoserine (By similarity).
 MOD_RES 330 330 Phosphoserine.
 MOD_RES 345 345 Phosphoserine.
 MOD_RES 347 347 Phosphoserine.
 MOD_RES 349 349 Phosphoserine.
 MOD_RES 361 361 Phosphoserine.
 MOD_RES 374 374 Phosphoserine.
 MOD_RES 699 699 Phosphoserine.
 MOD_RES 705 705 Phosphoserine.
 MOD_RES 708 708 Phosphoserine.
 MOD_RES 716 716 Phosphoserine.
 MOD_RES 947 947 Phosphoserine.
 MOD_RES 1315 1315 Phosphoserine.
 MOD_RES 1342 1342 Phosphoserine.
 MOD_RES 1468 1468 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; ATP-binding; Bromodomain; Coiled coil; Complete proteome; DNA damage; Kinase; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription; Transcription regulation; Transferase; Tyrosine-protein kinase; Williams-Beuren syndrome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1483 AA 
Protein Sequence
MAPLLGRKPF PLVKPLPGEE PLFTIPHTQE AFRTREEYEA RLERYSERIW TCKSTGSSQL 60
THKEAWEEEQ EVAELLKEEF PAWYEKLVLE MVHHNTASLE KLVDTAWLEI MTKYAVGEEC 120
DFEVGKEKML KVKIVKIHPL EKVDEEATEK KSDGACDSPS SDKENSSQIA QDHQKKETVV 180
KEDEGRRESI NDRARRSPRK LPTSLKKGER KWAPPKFLPH KYDVKLQNED KIISNVPADS 240
LIRTERPPNK EIVRYFIRHN ALRAGTGENA PWVVEDELVK KYSLPSKFSD FLLDPYKYMT 300
LNPSTKRKNT GSPDRKPSKK SKTDNSSLSS PLNPKLWCHV HLKKSLSGSP LKVKNSKNSK 360
SPEEHLEEMM KMMSPNKLHT NFHIPKKGPP AKKPGKHSDK PLKAKGRSKG ILNGQKSTGN 420
SKSPKKGLKT PKTKMKQMTL LDMAKGTQKM TRAPRNSGGT PRTSSKPHKH LPPAALHLIA 480
YYKENKDRED KRSALSCVIS KTARLLSSED RARLPEELRS LVQKRYELLE HKKRWASMSE 540
EQRKEYLKKK REELKKKLKE KAKERREKEM LERLEKQKRY EDQELTGKNL PAFRLVDTPE 600
GLPNTLFGDV AMVVEFLSCY SGLLLPDAQY PITAVSLMEA LSADKGGFLY LNRVLVILLQ 660
TLLQDEIAED YGELGMKLSE IPLTLHSVSE LVRLCLRRSD VQEESEGSDT DDNKDSAAFE 720
DNEVQDEFLE KLETSEFFEL TSEEKLQILT ALCHRILMTY SVQDHMETRQ QMSAELWKER 780
LAVLKEENDK KRAEKQKRKE MEAKNKENGK VENGLGKTDR KKEIVKFEPQ VDTEAEDMIS 840
AVKSRRLLAI QAKKEREIQE REMKVKLERQ AEEERIRKHK AAAEKAFQEG IAKAKLVMRR 900
TPIGTDRNHN RYWLFSDEVP GLFIEKGWVH DSIDYRFNHH CKDHTVSGDE DYCPRSKKAN 960
LGKNASMNTQ HGTATEVAVE TTTPKQGQNL WFLCDSQKEL DELLNCLHPQ GIRESQLKER 1020
LEKRYQDIIH SIHLARKPNL GLKSCDGNQE LLNFLRSDLI EVATRLQKGG LGYVEETSEF 1080
EARVISLEKL KDFGECVIAL QASVIKKFLQ GFMAPKQKRR KLQSEDSAKT EEVDEEKKMV 1140
EEAKVASALE KWKTAIREAQ TFSRMHVLLG MLDACIKWDM SAENARCKVC RKKGEDDKLI 1200
LCDECNKAFH LFCLRPALYE VPDGEWQCPA CQPATARRNS RGRNYTEESA SEDSEDDESD 1260
EEEEEEEEEE EEEDYEVAGL RLRPRKTIRG KHSVIPPAAR SGRRPGKKPH STRRSQPKAP 1320
PVDDAEVDEL VLQTKRSSRR QSLELQKCEE ILHKIVKYRF SWPFREPVTR DEAEDYYDVI 1380
THPMDFQTVQ NKCSCGSYRS VQEFLTDMKQ VFTNAEVYNC RGSHVLSCMV KTEQCLVALL 1440
HKHLPGHPYV RRKRKKFPDR LAEDEGDSEP EAVGQSRGRR QKK 1483 
Gene Ontology
 GO:0005721; C:centromeric heterochromatin; IEA:Compara.
 GO:0000793; C:condensed chromosome; IEA:Compara.
 GO:0071778; C:WINAC complex; IDA:BHF-UCL.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003682; F:chromatin binding; IDA:UniProtKB.
 GO:0070577; F:histone acetyl-lysine binding; IDA:UniProtKB.
 GO:0035173; F:histone kinase activity; IDA:UniProtKB.
 GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:EC.
 GO:0032947; F:protein complex scaffold; IDA:BHF-UCL.
 GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
 GO:0071884; F:vitamin D receptor activator activity; IMP:BHF-UCL.
 GO:0008270; F:zinc ion binding; NAS:UniProtKB.
 GO:0043044; P:ATP-dependent chromatin remodeling; IDA:BHF-UCL.
 GO:0048096; P:chromatin-mediated maintenance of transcription; ISS:BHF-UCL.
 GO:0034725; P:DNA replication-dependent nucleosome disassembly; IMP:BHF-UCL.
 GO:0006302; P:double-strand break repair; ISS:BHF-UCL.
 GO:0003007; P:heart morphogenesis; ISS:BHF-UCL.
 GO:0006351; P:transcription, DNA-dependent; NAS:BHF-UCL. 
Interpro
 IPR001487; Bromodomain.
 IPR018359; Bromodomain_CS.
 IPR018500; DDT_dom_subgr.
 IPR018501; DDT_dom_superfamily.
 IPR013136; WSTF_Acf1_Cbp146.
 IPR019786; Zinc_finger_PHD-type_CS.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF00439; Bromodomain
 PF00628; PHD
 PF10537; WAC_Acf1_DNA_bd 
SMART
 SM00297; BROMO
 SM00571; DDT
 SM00249; PHD
 SM00184; RING 
PROSITE
 PS00633; BROMODOMAIN_1
 PS50014; BROMODOMAIN_2
 PS50827; DDT
 PS51136; WAC
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS
 PR00503; BROMODOMAIN.