ID BAZ1B_HUMAN Reviewed; 1483 AA. AC Q9UIG0; B9EGK3; D3DXE9; O95039; O95247; O95277; Q6P1K4; Q86UJ6; DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 30-AUG-2002, sequence version 2. DT 24-JAN-2024, entry version 215. DE RecName: Full=Tyrosine-protein kinase BAZ1B; DE EC=2.7.10.2 {ECO:0000269|PubMed:19092802}; DE AltName: Full=Bromodomain adjacent to zinc finger domain protein 1B; DE AltName: Full=Williams syndrome transcription factor; DE AltName: Full=Williams-Beuren syndrome chromosomal region 10 protein; DE AltName: Full=Williams-Beuren syndrome chromosomal region 9 protein; DE AltName: Full=hWALp2; GN Name=BAZ1B; Synonyms=WBSC10, WBSCR10, WBSCR9, WSTF; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=9858827; DOI=10.1159/000015110; RA Peoples R.J., Cisco M.J., Kaplan P., Francke U.; RT "Identification of the WBSCR9 gene, encoding a novel transcriptional RT regulator, in the Williams-Beuren syndrome deletion at 7q11.23."; RL Cytogenet. Cell Genet. 82:238-246(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INVOLVEMENT IN WBS. RX PubMed=9828126; DOI=10.1006/geno.1998.5578; RA Lu X., Meng X., Morris C.A., Keating M.T.; RT "A novel human gene, WSTF, is deleted in Williams Syndrome."; RL Genomics 54:241-249(1998). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Testis; RX PubMed=10662543; DOI=10.1006/geno.1999.6071; RA Jones M.H., Hamana N., Nezu J., Shimane M.; RT "A novel family of bromodomain genes."; RL Genomics 63:40-45(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP FUNCTION, IDENTIFICATION IN THE WICH-5 ISWI CHROMATIN REMODELING COMPLEX, RP INTERACTION WITH SMARCA5, AND SUBCELLULAR LOCATION. RX PubMed=11980720; DOI=10.1093/emboj/21.9.2231; RA Bozhenok L., Wade P.A., Varga-Weisz P.; RT "WSTF-ISWI chromatin remodeling complex targets heterochromatic replication RT foci."; RL EMBO J. 21:2231-2241(2002). RN [8] RP FUNCTION, INTERACTION WITH PCNA AND SMARCA5, AND SUBCELLULAR LOCATION. RX PubMed=15543136; DOI=10.1038/ncb1196; RA Poot R.A., Bozhenok L., van den Berg D.L.C., Steffensen S., Ferreira F., RA Grimaldi M., Gilbert N., Ferreira J., Varga-Weisz P.D.; RT "The Williams syndrome transcription factor interacts with PCNA to target RT chromatin remodelling by ISWI to replication foci."; RL Nat. Cell Biol. 6:1236-1244(2004). RN [9] RP RETRACTED PAPER. RX PubMed=16252006; DOI=10.1038/sj.emboj.7600853; RA Fujiki R., Kim M.-S., Sasaki Y., Yoshimura K., Kitagawa H., Kato S.; RT "Ligand-induced transrepression by VDR through association of WSTF with RT acetylated histones."; RL EMBO J. 24:3881-3894(2005). RN [10] RP RETRACTION NOTICE OF PUBMED:16252006. RX PubMed=25452584; DOI=10.15252/embj.201470110; RA Fujiki R., Kim M.-S., Sasaki Y., Yoshimura K., Kitagawa H., Kato S.; RT "Retraction: 'Ligand-induced transrepression by VDR through association of RT WSTF with acetylated histones'."; RL EMBO J. 33:2881-2881(2014). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1342 AND SER-1468, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [12] RP FUNCTION, IDENTIFICATION IN THE B-WICH COMPLEX, AND INTERACTION WITH RP SMARCA5; DDX21; DEK; MYBBP1A; SF3B1; ERCC6 AND MYO1C. RX PubMed=16603771; DOI=10.1074/jbc.m600233200; RA Cavellan E., Asp P., Percipalle P., Oestlund Farrants A.-K.; RT "The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear RT proteins in transcription."; RL J. Biol. Chem. 281:16264-16271(2006). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH CDT1. RX PubMed=18162579; DOI=10.1091/mbc.e07-09-0859; RA Sugimoto N., Kitabayashi I., Osano S., Tatsumi Y., Yugawa T., RA Narisawa-Saito M., Matsukage A., Kiyono T., Fujita M.; RT "Identification of novel human Cdt1-binding proteins by a proteomics RT approach: proteolytic regulation by APC/CCdh1."; RL Mol. Biol. Cell 19:1007-1021(2008). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1468, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330; SER-374; SER-699; RP SER-705; SER-708; SER-716; SER-947; SER-1315 AND SER-1468, ACETYLATION AT RP LYS-1335, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [17] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF CYS-338. RX PubMed=19092802; DOI=10.1038/nature07668; RA Xiao A., Li H., Shechter D., Ahn S.H., Fabrizio L.A., Erdjument-Bromage H., RA Ishibe-Murakami S., Wang B., Tempst P., Hofmann K., Patel D.J., RA Elledge S.J., Allis C.D.; RT "WSTF regulates the H2A.X DNA damage response via a novel tyrosine kinase RT activity."; RL Nature 457:57-62(2009). RN [18] RP FUNCTION. RX PubMed=19234442; DOI=10.1038/nature07849; RA Cook P.J., Ju B.G., Telese F., Wang X., Glass C.K., Rosenfeld M.G.; RT "Tyrosine dephosphorylation of H2AX modulates apoptosis and survival RT decisions."; RL Nature 458:591-596(2009). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-705, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-266; SER-345; SER-347; RP SER-349; SER-361; SER-1342 AND SER-1468, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347; SER-349; SER-705; RP SER-1342 AND SER-1468, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349; SER-361; SER-947 AND RP SER-1468, ACETYLATION AT LYS-1335, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-716; SER-947 AND SER-1468, RP ACETYLATION AT LYS-1335, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [24] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-826 AND LYS-1089, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [25] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-826, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [26] RP SUBCELLULAR LOCATION. RX PubMed=25593309; DOI=10.1101/gad.252189.114; RA Gong F., Chiu L.Y., Cox B., Aymard F., Clouaire T., Leung J.W., RA Cammarata M., Perez M., Agarwal P., Brodbelt J.S., Legube G., Miller K.M.; RT "Screen identifies bromodomain protein ZMYND8 in chromatin recognition of RT transcription-associated DNA damage that promotes homologous RT recombination."; RL Genes Dev. 29:197-211(2015). RN [27] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-826 AND LYS-1089, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [28] RP FUNCTION, IDENTIFICATION IN THE WICH-1 ISWI CHROMATIN REMODELING COMPLEX, RP IDENTIFICATION IN THE WICH-5 CHROMATIN REMODELING COMPLEX, AND INTERACTION RP WITH SMARCA1 AND SMARCA5. RX PubMed=28801535; DOI=10.15252/embr.201744011; RA Oppikofer M., Bai T., Gan Y., Haley B., Liu P., Sandoval W., Ciferri C., RA Cochran A.G.; RT "Expansion of the ISWI chromatin remodeler family with new active RT complexes."; RL EMBO Rep. 18:1697-1706(2017). RN [29] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-826; LYS-853; LYS-1043; LYS-1089 RP AND LYS-1107, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [30] RP STRUCTURE BY NMR OF 1185-1235. RX PubMed=11124022; DOI=10.1006/jmbi.2000.4308; RA Pascual J., Martinez-Yamout M., Dyson H.J., Wright P.E.; RT "Structure of the PHD zinc finger from human Williams-Beuren syndrome RT transcription factor."; RL J. Mol. Biol. 304:723-729(2000). CC -!- FUNCTION: Atypical tyrosine-protein kinase that plays a central role in CC chromatin remodeling and acts as a transcription regulator CC (PubMed:19092802). Involved in DNA damage response by phosphorylating CC 'Tyr-142' of histone H2AX (H2AXY142ph) (PubMed:19092802, CC PubMed:19234442). H2AXY142ph plays a central role in DNA repair and CC acts as a mark that distinguishes between apoptotic and repair CC responses to genotoxic stress (PubMed:19092802, PubMed:19234442). CC Regulatory subunit of the ATP-dependent WICH-1 and WICH-5 ISWI CC chromatin remodeling complexes, which form ordered nucleosome arrays on CC chromatin and facilitate access to DNA during DNA-templated processes CC such as DNA replication, transcription, and repair (PubMed:11980720, CC PubMed:28801535). Both complexes regulate the spacing of nucleosomes CC along the chromatin and have the ability to slide mononucleosomes to CC the center of a DNA template (PubMed:28801535). The WICH-1 ISWI CC chromatin remodeling complex has a lower ATP hydrolysis rate than the CC WICH-5 ISWI chromatin remodeling complex (PubMed:28801535). The WICH-5 CC ISWI chromatin-remodeling complex regulates the transcription of CC various genes, has a role in RNA polymerase I transcription (By CC similarity). Within the B-WICH complex has a role in RNA polymerase III CC transcription (PubMed:16603771). Mediates the recruitment of the WICH-5 CC ISWI chromatin remodeling complex to replication foci during DNA CC replication (PubMed:15543136). {ECO:0000250|UniProtKB:Q9Z277, CC ECO:0000269|PubMed:11980720, ECO:0000269|PubMed:15543136, CC ECO:0000269|PubMed:16603771, ECO:0000269|PubMed:19092802, CC ECO:0000269|PubMed:19234442, ECO:0000269|PubMed:28801535}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl- CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; CC Evidence={ECO:0000269|PubMed:19092802}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:19092802}; CC -!- SUBUNIT: Component of the WICH-1 ISWI chromatin remodeling complex, at CC least composed of SMARCA1 and BAZ1B/WSTF, which regulates the spacing CC of histone octamers on the DNA template to facilitate access to DNA CC (PubMed:28801535). Within the WICH-1 ISWI chromatin remodeling complex CC interacts with SMARCA1; the interaction is direct (PubMed:28801535). CC Component of the WICH-5 ISWI chromatin remodeling complex (also called CC the WICH complex), at least composed of SMARCA5/SNF2H and BAZ1B/WSTF, CC which regulates the spacing of histone octamers on the DNA template to CC facilitate access to DNA (PubMed:11980720, PubMed:28801535). Within the CC WICH-5 ISWI chromatin remodeling complex interacts with SMARCA5/SNF2H; CC the interaction is direct (PubMed:11980720, PubMed:15543136, CC PubMed:28801535). Component of the B-WICH chromatin remodeling complex, CC at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, CC ERCC6, MYBBP1A and DDX21 (PubMed:16603771). Within the B-WICH chromatin CC remodeling complex, interacts with SMARCA5/SNF2H, DDX21, DEK, MYBBP1A, CC SF3B1, ERCC6 and MYO1C (PubMed:16603771). Interacts with PCNA; the CC interaction is direct and is required for BAZ1B/WSTF binding to CC replication foci during S phase (PubMed:15543136). Interacts with CDT1 CC (PubMed:18162579). {ECO:0000250|UniProtKB:Q9Z277, CC ECO:0000269|PubMed:11980720, ECO:0000269|PubMed:15543136, CC ECO:0000269|PubMed:16603771, ECO:0000269|PubMed:18162579, CC ECO:0000269|PubMed:28801535}. CC -!- INTERACTION: CC Q9UIG0; O60264: SMARCA5; NbExp=7; IntAct=EBI-927482, EBI-352588; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00063, CC ECO:0000255|PROSITE-ProRule:PRU00475, ECO:0000269|PubMed:11980720, CC ECO:0000269|PubMed:15543136, ECO:0000269|PubMed:16603771, CC ECO:0000269|PubMed:25593309}. Note=Accumulates in pericentromeric CC heterochromatin during replication (PubMed:15543136). Co-localizes with CC PCNA at replication foci during S phase (PubMed:15543136). Co-localizes CC with SMARCA5/SNF2H at replication foci during late-S phase CC (PubMed:15543136). Also localizes to replication foci independently of CC SMARCA5/SNF2H and PCNA (PubMed:15543136). Localizes to sites of DNA CC damage (PubMed:25593309). {ECO:0000269|PubMed:15543136, CC ECO:0000269|PubMed:25593309}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9UIG0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UIG0-2; Sequence=VSP_000552; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with high levels of CC expression in heart, brain, placenta, skeletal muscle and ovary. CC -!- DEVELOPMENTAL STAGE: Expressed at equal levels in 19-23 weeks old fetal CC tissues. CC -!- DISEASE: Note=BAZ1B is located in the Williams-Beuren syndrome (WBS) CC critical region. WBS results from a hemizygous deletion of several CC genes on chromosome 7q11.23, thought to arise as a consequence of CC unequal crossing over between highly homologous low-copy repeat CC sequences flanking the deleted region. Haploinsufficiency of BAZ1B may CC be the cause of certain cardiovascular and musculo-skeletal CC abnormalities observed in the disease. CC -!- SIMILARITY: Belongs to the WAL family. BAZ1B subfamily. {ECO:0000305}. CC -!- CAUTION: Was shown to interact with VDR and with acetylated histones CC via its Bromo domain, but this work has later been retracted. CC {ECO:0000305|PubMed:16252006, ECO:0000305|PubMed:25452584}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC97879.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAD04720.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=AAH65029.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=BAA89210.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF084479; AAD08675.1; -; mRNA. DR EMBL; AF072810; AAC97879.1; ALT_FRAME; mRNA. DR EMBL; AB032253; BAA89210.1; ALT_FRAME; mRNA. DR EMBL; AC005074; AAD04720.1; ALT_SEQ; Genomic_DNA. DR EMBL; AC005089; AAP22332.1; -; Genomic_DNA. DR EMBL; CH471200; EAW69680.1; -; Genomic_DNA. DR EMBL; CH471200; EAW69681.1; -; Genomic_DNA. DR EMBL; BC065029; AAH65029.1; ALT_SEQ; mRNA. DR EMBL; BC136520; AAI36521.1; -; mRNA. DR CCDS; CCDS5549.1; -. [Q9UIG0-1] DR RefSeq; NP_115784.1; NM_032408.3. [Q9UIG0-1] DR RefSeq; XP_016868262.1; XM_017012773.1. DR PDB; 1F62; NMR; -; A=1185-1235. DR PDB; 5NNF; X-ray; 1.15 A; B=217-226. DR PDBsum; 1F62; -. DR PDBsum; 5NNF; -. DR AlphaFoldDB; Q9UIG0; -. DR SMR; Q9UIG0; -. DR BioGRID; 114497; 190. DR ComplexPortal; CPX-1099; B-WICH chromatin remodelling complex. DR ComplexPortal; CPX-757; WICH chromatin remodelling complex. DR CORUM; Q9UIG0; -. DR DIP; DIP-35642N; -. DR ELM; Q9UIG0; -. DR IntAct; Q9UIG0; 52. DR MINT; Q9UIG0; -. DR STRING; 9606.ENSP00000342434; -. DR BindingDB; Q9UIG0; -. DR ChEMBL; CHEMBL3588730; -. DR CarbonylDB; Q9UIG0; -. DR GlyGen; Q9UIG0; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9UIG0; -. DR PhosphoSitePlus; Q9UIG0; -. DR SwissPalm; Q9UIG0; -. DR BioMuta; BAZ1B; -. DR DMDM; 22653670; -. DR EPD; Q9UIG0; -. DR jPOST; Q9UIG0; -. DR MassIVE; Q9UIG0; -. DR MaxQB; Q9UIG0; -. DR PaxDb; 9606-ENSP00000342434; -. DR PeptideAtlas; Q9UIG0; -. DR ProteomicsDB; 84514; -. [Q9UIG0-1] DR ProteomicsDB; 84515; -. [Q9UIG0-2] DR Pumba; Q9UIG0; -. DR ABCD; Q9UIG0; 1 sequenced antibody. DR Antibodypedia; 14309; 327 antibodies from 32 providers. DR DNASU; 9031; -. DR Ensembl; ENST00000339594.9; ENSP00000342434.4; ENSG00000009954.11. [Q9UIG0-1] DR Ensembl; ENST00000404251.1; ENSP00000385442.1; ENSG00000009954.11. [Q9UIG0-1] DR GeneID; 9031; -. DR KEGG; hsa:9031; -. DR MANE-Select; ENST00000339594.9; ENSP00000342434.4; NM_032408.4; NP_115784.1. DR UCSC; uc003tyc.4; human. [Q9UIG0-1] DR AGR; HGNC:961; -. DR CTD; 9031; -. DR DisGeNET; 9031; -. DR GeneCards; BAZ1B; -. DR HGNC; HGNC:961; BAZ1B. DR HPA; ENSG00000009954; Low tissue specificity. DR MalaCards; BAZ1B; -. DR MIM; 605681; gene. DR neXtProt; NX_Q9UIG0; -. DR OpenTargets; ENSG00000009954; -. DR Orphanet; 904; Williams syndrome. DR PharmGKB; PA25271; -. DR VEuPathDB; HostDB:ENSG00000009954; -. DR eggNOG; KOG1245; Eukaryota. DR GeneTree; ENSGT00940000156831; -. DR HOGENOM; CLU_004410_0_0_1; -. DR InParanoid; Q9UIG0; -. DR OMA; RFNHRKD; -. DR OrthoDB; 5490909at2759; -. DR PhylomeDB; Q9UIG0; -. DR TreeFam; TF106397; -. DR PathwayCommons; Q9UIG0; -. DR Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression. DR Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks. DR SignaLink; Q9UIG0; -. DR SIGNOR; Q9UIG0; -. DR BioGRID-ORCS; 9031; 153 hits in 1183 CRISPR screens. DR ChiTaRS; BAZ1B; human. DR EvolutionaryTrace; Q9UIG0; -. DR GeneWiki; BAZ1B; -. DR GenomeRNAi; 9031; -. DR Pharos; Q9UIG0; Tbio. DR PRO; PR:Q9UIG0; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q9UIG0; Protein. DR Bgee; ENSG00000009954; Expressed in oocyte and 210 other cell types or tissues. DR GO; GO:0110016; C:B-WICH complex; IDA:ComplexPortal. DR GO; GO:0000793; C:condensed chromosome; IEA:Ensembl. DR GO; GO:0005730; C:nucleolus; NAS:ComplexPortal. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005721; C:pericentric heterochromatin; ISO:ComplexPortal. DR GO; GO:0090535; C:WICH complex; IDA:ComplexPortal. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0042393; F:histone binding; IBA:GO_Central. DR GO; GO:0140801; F:histone H2AXY142 kinase activity; IDA:UniProtKB. DR GO; GO:0035173; F:histone kinase activity; IBA:GO_Central. DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB. DR GO; GO:0006338; P:chromatin remodeling; IMP:BHF-UCL. DR GO; GO:0006974; P:DNA damage response; IDA:UniProtKB. DR GO; GO:1905213; P:negative regulation of mitotic chromosome condensation; IDA:ComplexPortal. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0035066; P:positive regulation of histone acetylation; NAS:ComplexPortal. DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; NAS:ComplexPortal. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; NAS:ComplexPortal. DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IDA:ComplexPortal. DR GO; GO:0043687; P:post-translational protein modification; IDA:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; NAS:BHF-UCL. DR CDD; cd05505; Bromo_WSTF_like; 1. DR CDD; cd15628; PHD_BAZ1B; 1. DR Gene3D; 1.20.920.10; Bromodomain-like; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR047174; BAZ1B. DR InterPro; IPR037375; BAZ1B_Bromo. DR InterPro; IPR047256; BAZ1B_PHD. DR InterPro; IPR001487; Bromodomain. DR InterPro; IPR036427; Bromodomain-like_sf. DR InterPro; IPR018359; Bromodomain_CS. DR InterPro; IPR018501; DDT_dom. DR InterPro; IPR028942; WHIM1_dom. DR InterPro; IPR028941; WHIM2_dom. DR InterPro; IPR013136; WSTF_Acf1_Cbp146. DR InterPro; IPR019786; Zinc_finger_PHD-type_CS. DR InterPro; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR001965; Znf_PHD. DR InterPro; IPR019787; Znf_PHD-finger. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR46802; TYROSINE-PROTEIN KINASE BAZ1B; 1. DR PANTHER; PTHR46802:SF1; TYROSINE-PROTEIN KINASE BAZ1B; 1. DR Pfam; PF00439; Bromodomain; 1. DR Pfam; PF00628; PHD; 1. DR Pfam; PF10537; WAC_Acf1_DNA_bd; 1. DR Pfam; PF15612; WHIM1; 1. DR Pfam; PF15613; WSD; 1. DR PRINTS; PR00503; BROMODOMAIN. DR SMART; SM00297; BROMO; 1. DR SMART; SM00571; DDT; 1. DR SMART; SM00249; PHD; 1. DR SUPFAM; SSF47370; Bromodomain; 1. DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1. DR PROSITE; PS00633; BROMODOMAIN_1; 1. DR PROSITE; PS50014; BROMODOMAIN_2; 1. DR PROSITE; PS50827; DDT; 1. DR PROSITE; PS51136; WAC; 1. DR PROSITE; PS01359; ZF_PHD_1; 1. DR PROSITE; PS50016; ZF_PHD_2; 1. DR Genevisible; Q9UIG0; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Bromodomain; KW Coiled coil; DNA damage; Isopeptide bond; Kinase; Metal-binding; KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; KW Transcription; Transcription regulation; Transferase; KW Tyrosine-protein kinase; Ubl conjugation; Williams-Beuren syndrome; Zinc; KW Zinc-finger. FT CHAIN 1..1483 FT /note="Tyrosine-protein kinase BAZ1B" FT /id="PRO_0000211170" FT DOMAIN 20..126 FT /note="WAC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00475" FT DOMAIN 604..668 FT /note="DDT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00063" FT DOMAIN 1356..1426 FT /note="Bromo" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT ZN_FING 1184..1234 FT /note="PHD-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146" FT REGION 145..212 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 302..333 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 379..432 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 446..470 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 788..817 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1237..1326 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1455..1483 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 533..586 FT /evidence="ECO:0000255" FT COILED 768..814 FT /evidence="ECO:0000255" FT COILED 850..893 FT /evidence="ECO:0000255" FT COILED 1245..1283 FT /evidence="ECO:0000255" FT MOTIF 207..213 FT /note="C motif" FT COMPBIAS 168..212 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 411..426 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 450..464 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1250..1275 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 152 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Z277" FT MOD_RES 158 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Z277" FT MOD_RES 161 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Z277" FT MOD_RES 266 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 330 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 345 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 347 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 349 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 361 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 374 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 699 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 705 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692" FT MOD_RES 708 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 716 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:24275569" FT MOD_RES 947 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 1315 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1335 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9Z277" FT MOD_RES 1342 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT MOD_RES 1468 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT CROSSLNK 826 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 826 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25114211, FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 853 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1043 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1089 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733" FT CROSSLNK 1107 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 660..663 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10662543" FT /id="VSP_000552" FT MUTAGEN 338 FT /note="C->A: Loss of tyrosine-protein kinase activity." FT /evidence="ECO:0000269|PubMed:19092802" FT CONFLICT 14 FT /note="K -> N (in Ref. 3; BAA89210)" FT /evidence="ECO:0000305" FT CONFLICT 22 FT /note="L -> F (in Ref. 3; BAA89210)" FT /evidence="ECO:0000305" FT CONFLICT 136 FT /note="K -> E (in Ref. 1; AAD08675)" FT /evidence="ECO:0000305" FT CONFLICT 823 FT /note="E -> R (in Ref. 3; BAA89210)" FT /evidence="ECO:0000305" FT CONFLICT 1191 FT /note="R -> P (in Ref. 3; BAA89210)" FT /evidence="ECO:0000305" FT CONFLICT 1354 FT /note="K -> M (in Ref. 2; AAC97879)" FT /evidence="ECO:0000305" FT CONFLICT 1438 FT /note="A -> V (in Ref. 3; BAA89210)" FT /evidence="ECO:0000305" FT TURN 1188..1190 FT /evidence="ECO:0007829|PDB:1F62" FT TURN 1203..1205 FT /evidence="ECO:0007829|PDB:1F62" FT HELIX 1211..1214 FT /evidence="ECO:0007829|PDB:1F62" FT TURN 1229..1231 FT /evidence="ECO:0007829|PDB:1F62" SQ SEQUENCE 1483 AA; 170903 MW; 0CC146FEBB954261 CRC64; MAPLLGRKPF PLVKPLPGEE PLFTIPHTQE AFRTREEYEA RLERYSERIW TCKSTGSSQL THKEAWEEEQ EVAELLKEEF PAWYEKLVLE MVHHNTASLE KLVDTAWLEI MTKYAVGEEC DFEVGKEKML KVKIVKIHPL EKVDEEATEK KSDGACDSPS SDKENSSQIA QDHQKKETVV KEDEGRRESI NDRARRSPRK LPTSLKKGER KWAPPKFLPH KYDVKLQNED KIISNVPADS LIRTERPPNK EIVRYFIRHN ALRAGTGENA PWVVEDELVK KYSLPSKFSD FLLDPYKYMT LNPSTKRKNT GSPDRKPSKK SKTDNSSLSS PLNPKLWCHV HLKKSLSGSP LKVKNSKNSK SPEEHLEEMM KMMSPNKLHT NFHIPKKGPP AKKPGKHSDK PLKAKGRSKG ILNGQKSTGN SKSPKKGLKT PKTKMKQMTL LDMAKGTQKM TRAPRNSGGT PRTSSKPHKH LPPAALHLIA YYKENKDRED KRSALSCVIS KTARLLSSED RARLPEELRS LVQKRYELLE HKKRWASMSE EQRKEYLKKK REELKKKLKE KAKERREKEM LERLEKQKRY EDQELTGKNL PAFRLVDTPE GLPNTLFGDV AMVVEFLSCY SGLLLPDAQY PITAVSLMEA LSADKGGFLY LNRVLVILLQ TLLQDEIAED YGELGMKLSE IPLTLHSVSE LVRLCLRRSD VQEESEGSDT DDNKDSAAFE DNEVQDEFLE KLETSEFFEL TSEEKLQILT ALCHRILMTY SVQDHMETRQ QMSAELWKER LAVLKEENDK KRAEKQKRKE MEAKNKENGK VENGLGKTDR KKEIVKFEPQ VDTEAEDMIS AVKSRRLLAI QAKKEREIQE REMKVKLERQ AEEERIRKHK AAAEKAFQEG IAKAKLVMRR TPIGTDRNHN RYWLFSDEVP GLFIEKGWVH DSIDYRFNHH CKDHTVSGDE DYCPRSKKAN LGKNASMNTQ HGTATEVAVE TTTPKQGQNL WFLCDSQKEL DELLNCLHPQ GIRESQLKER LEKRYQDIIH SIHLARKPNL GLKSCDGNQE LLNFLRSDLI EVATRLQKGG LGYVEETSEF EARVISLEKL KDFGECVIAL QASVIKKFLQ GFMAPKQKRR KLQSEDSAKT EEVDEEKKMV EEAKVASALE KWKTAIREAQ TFSRMHVLLG MLDACIKWDM SAENARCKVC RKKGEDDKLI LCDECNKAFH LFCLRPALYE VPDGEWQCPA CQPATARRNS RGRNYTEESA SEDSEDDESD EEEEEEEEEE EEEDYEVAGL RLRPRKTIRG KHSVIPPAAR SGRRPGKKPH STRRSQPKAP PVDDAEVDEL VLQTKRSSRR QSLELQKCEE ILHKIVKYRF SWPFREPVTR DEAEDYYDVI THPMDFQTVQ NKCSCGSYRS VQEFLTDMKQ VFTNAEVYNC RGSHVLSCMV KTEQCLVALL HKHLPGHPYV RRKRKKFPDR LAEDEGDSEP EAVGQSRGRR QKK //