CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024139
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 homolog; Williams-Beuren syndrome chromosomal region 9 protein homolog 
Gene Name
 Baz1b 
Gene Synonyms/Alias
 Wbscr9; Wstf 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
410LKAKGRGKGILNGQKacetylation[1]
446MTLLDMAKGTQKMTRacetylation[2]
502ALSCVISKTARLLSNacetylation[2, 3]
502ALSCVISKTARLLSNubiquitination[4]
1068EVATRLQKGGLGYMEubiquitination[4]
1331DDLVLQTKRISRRQSacetylation[3, 5]
Reference
 [1] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [4] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [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
 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 (By similarity). 
Sequence Annotation
 DOMAIN 20 126 WAC.
 DOMAIN 605 669 DDT.
 DOMAIN 1352 1422 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.
 MOD_RES 266 266 Phosphothreonine (By similarity).
 MOD_RES 283 283 Phosphoserine.
 MOD_RES 330 330 Phosphoserine (By similarity).
 MOD_RES 345 345 Phosphoserine (By similarity).
 MOD_RES 361 361 Phosphoserine (By similarity).
 MOD_RES 374 374 Phosphoserine (By similarity).
 MOD_RES 706 706 Phosphoserine (By similarity).
 MOD_RES 709 709 Phosphoserine (By similarity).
 MOD_RES 717 717 Phosphoserine (By similarity).
 MOD_RES 1315 1315 Phosphoserine (By similarity).
 MOD_RES 1338 1338 Phosphoserine.
 MOD_RES 1464 1464 Phosphoserine.
 MOD_RES 1466 1466 Phosphoserine.
 MOD_RES 1468 1468 Phosphoserine.  
Keyword
 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; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1479 AA 
Protein Sequence
MAPLLGRKPF PLVKPLPGEE PLFTIPHTQE AFRTREEYEA RLERYSERIW TCKSTGSSQL 60
THKEAWEEEQ EVAELLKEEF PNWYEKLVLE MVHHNTASLE KLVDSAWLEI MTKYAVGEEC 120
DFEVGKEKML KVKIVKIHPL EKVDEEAVEK KSDGACDSPS SDKENSSQMA QDLQKKETVV 180
KEDEGRRESI NDRARRSPRK LPTSLKKGER KWAPPKFLPH KYDVKLQNED KIISNVPADS 240
LIRTERPPNK EILRYFIRHN ALRAGTGENA PWVVEDELVK KYSLPSKFSD FLLDPYKYMT 300
LNPSTKRRNT GSPDRKPSKK PKRDSSSLSS PLNPKLWCHV HLEKSLNGPP LKVKNSKNSK 360
SPEEHLEGVM KIMSPNNNKL HSFHIPKKGP AAKKPGKHSD KPLKAKGRGK GILNGQKSTG 420
NSKSPSKCVK TPKTKMKQMT LLDMAKGTQK MTRTPRSSGG VPRSSGKPHK HLPPAALHLI 480
AYYKENKDKE DKKSALSCVI SKTARLLSNE DRARLPEELR ALVQKRYELL EHKKRWASMS 540
EEQRKEYLKK KRQELKERLR EKAKERRERE MLERLEKQKR FEDQELGGRN LPAFRLVDTP 600
EGLPNTLFGD VALVVEFLSC YSGLLLPDAQ YPITAVSLME ALSADKGGFL YLNRVLVILL 660
QTLLQDEIAE DYGELGMKLS EIPLTLHSVS ELVRLCLRRC DVQEDSEGSE TDDNKDSTPF 720
EDNEVQDEFL EKLETSEFFE LTSEEKLRIL TALCHRILMT YSVQDHMETR QQVSAELWKE 780
RLAVLKEEND KKRAEKQKRK EMEARNKENG KEENVLGKVD RKKEIVKIEQ QVEVEADDMI 840
SAVKSRRLLS MQAKRKREIQ ERETKVRLER EAEEERMRKH KAAAEKAFQE GIAKAKLVLR 900
RTPIGTDRNH NRYWLFSNEV PGLFIEKGWV HNSIDYRFKH HRKDHSNLPD DDYCPRSKKA 960
NLGKNASVNA HHGPALEAVE TTVPKQGQNL WFLCDSQKEL DELLSCLHPQ GIRESQLKER 1020
LEKRYQEITH SIYLARKPNL GLKSCDGNQE LLNFLRSDLI EVATRLQKGG LGYMEGTSEF 1080
EARVISLEKL KDFGECVIAL QASVIKKFLQ GFMAPKQKKR KLQSEDSTKS EEVDEEKKMV 1140
EEAKVASALE KWKTAIREAQ TFSRMHVLLG MLDACIKWDM SAENARCKVC RKKGEDDKLI 1200
LCDECNKAFH LFCLRPALYE VPDGEWQCPA CQPPTARRNS RGRNYTEEST SEGSEGDESG 1260
EEEEEEEEEE EEEEDYEVAG LRLRPRKTIR GKQSVIPAAR PGRPPGKKSH PARRSRPKDD 1320
PEVDDLVLQT KRISRRQSLE LQKCEDILHK LVKYRFSWPF REPVTRDEAE DYYDVIEHPM 1380
DFQTIQNKCS CGNYRSVQEF LTDMKQVFAN AELYNCRGSH VLSCMEKTEQ CLLALLQKHL 1440
PGHPYVRRKR RKFPDRLADD EGDSDSESVG QSRGRRQKK 1479 
Gene Ontology
 GO:0005721; C:centromeric heterochromatin; IDA:MGI.
 GO:0000793; C:condensed chromosome; IDA:MGI.
 GO:0043596; C:nuclear replication fork; IEA:Compara.
 GO:0005634; C:nucleus; IDA:MGI.
 GO:0071778; C:WINAC complex; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003682; F:chromatin binding; ISS:UniProtKB.
 GO:0070577; F:histone acetyl-lysine binding; ISS:UniProtKB.
 GO:0035173; F:histone kinase activity; ISS:UniProtKB.
 GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:EC.
 GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
 GO:0071884; F:vitamin D receptor activator activity; IMP:BHF-UCL.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0043044; P:ATP-dependent chromatin remodeling; IEA:Compara.
 GO:0006333; P:chromatin assembly or disassembly; IDA:MGI.
 GO:0048096; P:chromatin-mediated maintenance of transcription; IMP:BHF-UCL.
 GO:0034725; P:DNA replication-dependent nucleosome disassembly; IEA:Compara.
 GO:0006302; P:double-strand break repair; IMP:BHF-UCL.
 GO:0003007; P:heart morphogenesis; IMP:BHF-UCL.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
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.