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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
 
 
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