BAZ1B_HUMAN
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 03-AUG-2022, entry version 207.
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 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 [27]
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 [28]
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 [29]
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 Note=Accumulates in pericentromeric heterochromatin during replication.
CC Co-localizes with PCNA at replication foci during S phase
CC (PubMed:15543136). Co-localizes with SMARCA5/SNF2H at replication foci
CC during late-S phase (PubMed:15543136). Also localizes to replication
CC foci independently of SMARCA5/SNF2H and PCNA (PubMed:15543136).
CC {ECO:0000269|PubMed:15543136}.
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};
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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; 148.
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; 40.
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; Q9UIG0; -.
DR PeptideAtlas; Q9UIG0; -.
DR PRIDE; Q9UIG0; -.
DR ProteomicsDB; 84514; -. [Q9UIG0-1]
DR ProteomicsDB; 84515; -. [Q9UIG0-2]
DR ABCD; Q9UIG0; 1 sequenced antibody.
DR Antibodypedia; 14309; 286 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 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; 858930at2759; -.
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; 137 hits in 1099 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 208 other tissues.
DR Genevisible; Q9UIG0; HS.
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; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005721; C:pericentric heterochromatin; IEA:Ensembl.
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: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:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IMP:BHF-UCL.
DR GO; GO:1990164; P:histone H2A phosphorylation; IDA:ComplexPortal.
DR GO; GO:1905213; P:negative regulation of mitotic chromosome condensation; IDA:ComplexPortal.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IC:ComplexPortal.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IC: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:2001020; P:regulation of response to DNA damage stimulus; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; NAS:BHF-UCL.
DR CDD; cd05505; Bromo_WSTF_like; 1.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR037375; BAZ1B_Bromo.
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 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; SSF47370; 1.
DR SUPFAM; SSF57903; SSF57903; 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.
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
