ID   BAZ1B_DANRE             Reviewed;        1536 AA.
AC   A2BIL7;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   02-SEP-2026, entry version 113.
DE   RecName: Full=Tyrosine-protein kinase BAZ1B;
DE            EC=2.7.10.2;
DE   AltName: Full=Bromodomain adjacent to zinc finger domain protein 1B;
DE   AltName: Full=Williams syndrome transcription factor homolog;
GN   Name=baz1b; Synonyms=wstf; ORFNames=ch211-203b8.1;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1349, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18307296; DOI=10.1021/pr700667w;
RA   Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA   Slijper M., Heck A.J.R.;
RT   "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT   analysis down to a single embryo.";
RL   J. Proteome Res. 7:1555-1564(2008).
CC   -!- FUNCTION: Atypical tyrosine-protein kinase that plays a central role in
CC       chromatin remodeling and acts as a transcription regulator. Involved in
CC       DNA damage response by phosphorylating 'Tyr-142' of histone H2AX
CC       (H2AXY142ph). H2AXY142ph plays a central role in DNA repair and acts as
CC       a mark that distinguishes between apoptotic and repair responses to
CC       genotoxic stress. Essential component of the WICH complex, a chromatin
CC       remodeling complex that mobilizes nucleosomes and reconfigures
CC       irregular chromatin to a regular nucleosomal array structure. The WICH
CC       complex regulates the transcription of various genes, has a role in RNA
CC       polymerase I and RNA polymerase III transcription, mediates the histone
CC       H2AX phosphorylation at 'Tyr-142', and is involved in the maintenance
CC       of chromatin structures during DNA replication processes.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:20101, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:61978, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Interacts with smarca5/snf2h; the interaction is direct and
CC       forms the WICH complex. Component of the B-WICH complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00063,
CC       ECO:0000255|PROSITE-ProRule:PRU00475}. Note=Accumulates in
CC       pericentromeric heterochromatin during replication. Targeted to
CC       replication foci throughout S phase (By similarity). Localizes to sites
CC       of DNA damage (By similarity). {ECO:0000250|UniProtKB:Q9UIG0}.
CC   -!- DOMAIN: The bromo domain mediates the specific interaction with
CC       acetylated histones. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the WAL family. BAZ1B subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAM13000.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; BX950182; CAM13000.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; A2BIL7; -.
DR   SMR; A2BIL7; -.
DR   FunCoup; A2BIL7; 1119.
DR   STRING; 7955.ENSDARP00000132502; -.
DR   iPTMnet; A2BIL7; -.
DR   PaxDb; 7955-ENSDARP00000132502; -.
DR   PeptideAtlas; A2BIL7; -.
DR   AGR; ZFIN:ZDB-GENE-010328-16; -.
DR   ZFIN; ZDB-GENE-010328-16; baz1b.
DR   eggNOG; KOG1245; Eukaryota.
DR   InParanoid; A2BIL7; -.
DR   PhylomeDB; A2BIL7; -.
DR   Reactome; R-DRE-5250924; B-WICH complex positively regulates rRNA expression.
DR   Reactome; R-DRE-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR   PRO; PR:A2BIL7; -.
DR   Proteomes; UP000000437; Unplaced.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0090535; C:WICH complex; IBA:GO_Central.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0140801; F:histone H2AXY142 kinase activity; ISS: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:0006338; P:chromatin remodeling; IBA:GO_Central.
DR   GO; GO:0006974; P:DNA damage response; ISS:UniProtKB.
DR   GO; GO:0043687; P:post-translational protein modification; ISS:UniProtKB.
DR   CDD; cd05505; Bromo_WSTF_like; 1.
DR   CDD; cd15628; PHD_BAZ1B; 1.
DR   FunFam; 3.30.40.10:FF:000131; tyrosine-protein kinase BAZ1B isoform X1; 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; 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; 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   ATP-binding; Bromodomain; Coiled coil; DNA damage; Kinase; Metal-binding;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation; Transferase;
KW   Tyrosine-protein kinase; Zinc; Zinc-finger.
FT   CHAIN           1..1536
FT                   /note="Tyrosine-protein kinase BAZ1B"
FT                   /id="PRO_0000378188"
FT   DOMAIN          25..130
FT                   /note="WAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00475"
FT   DOMAIN          603..667
FT                   /note="DDT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00063"
FT   DOMAIN          1366..1470
FT                   /note="Bromo"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT   ZN_FING         1202..1252
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   REGION          144..207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          304..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          557..579
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          785..839
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          940..973
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1256..1371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1477..1536
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          515..583
FT                   /evidence="ECO:0000255"
FT   COILED          768..803
FT                   /evidence="ECO:0000255"
FT   COILED          850..890
FT                   /evidence="ECO:0000255"
FT   COILED          1261..1293
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        151..196
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..343
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..355
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        392..401
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        443..452
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        785..832
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        941..955
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        962..972
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1266..1287
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1297..1316
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1325..1350
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1491..1502
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1506..1524
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1525..1536
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1349
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18307296"
SQ   SEQUENCE   1536 AA;  176213 MW;  2493AB082E67F6B2 CRC64;
     MAPLLGRKPY PLVKPLSEPP GPGEEVYTIE HTKEAFRNKE EYEARLRRYG ERIWTCKSTG
     SSQLTHKEAW EEEQEVTELL QEEYPVWFEK PVLEIVHHNT VPLDKLVDQV WVEILTKYAV
     GEKCDLMVGN DKTLSVEVVK IHPLENPPEE NAEKKMEGAC DSPSSDKENA SQENLKKEPQ
     SKEEESRRES LSDRARRSPR KLPTTMKEEK KKWVMPKFLP HKYDVKLVNE DKVISDVPAD
     NLFRTERPPN KEIMRYFIRH YALRLGSGES APWVVEDELV KKFSLPSKFS DFLLDPHKFL
     AENPSTKRKS LSSPEGKPRK RLKNVETGTG GEGAKGDKKK NKDSQNIPLS PTIWSHMQVK
     KVNGSPLKMK NSGTSKKSDE ENVLGTPKSS KKQGDKKSSD PKRRRKSGLN KTPNSQRLSK
     KEDKSLGGAK KPRMKQMTLL DLAKSPAAAG SPKKQRRSST TGSAKLGKPF PPMALHLLRF
     YKENKGKEDK KTTLSSLLSK AAKALSPEDR SRLPEELKEL VQKRWELLEQ KRRWALMSEE
     EKQSVLKQKR QEVKQKLREK AKERREKEMQ VRREMSRRYE DQELEGKNLP AFRLFDMPEG
     LPNTIFGDVA MVVEFLHCYS GLLMPDDQYP ITSIALLEAL AGEKAGFLYL NRVLVVLLQT
     LLQDELAEGY SELDMPLSEI PLTMHSVSEL VRLCLRPSDA HEEESARGSD DWQSGADFDD
     MVSSEFLEKL ETAEVFELDP QEKVSLLLAL CHRILMTYSV EDHVEAVHQK SAEMWKERVA
     TLKEANDRKR AEKQKRKEQM ETKTDGDVLI KAEKKKESTV KKETPKVLPK EEPEPEDMIS
     TVKSRRLMSI QAKKEKEEQE RLNKVRMEKE AEEERIRRQK AATEKAFQDA VTKAKLVLRR
     TPLGTDRNHN RYWLFSDVVP GLYIEKGWVH ESIDYSFTLP PEEEPVLTEE EEEEEEVKKE
     EETEDGEKED EGSIISASND ISQQGAPSHE SSIETTVPKQ GQNLWFVCDT PKDFDELLES
     LHPQGVRESE LKIRLQINYQ EILHSIHLTK KGNPGLKTCD GHQELLKFLR SDIIEVASRL
     QKGGLGYLED TSEFEEFEER VKTLEKLPEF GECVIALQES VIKKFLQGFM APKQKKKKKT
     GGEESTTAEE VDDQKKLAEE ARVATAVEKW KTAVREAQTF SRMHVLLGML DACIKWDMSA
     ENARCKVCRR KGEDDKLILC DECNKAFHLF CLRPALYRIP AGEWLCPACQ PTIARRSSRG
     RNYKEDSEEE EDSEEEDEEE SEEEDSEEEH RNTGHSLRSR KKVKTSSKSK MQKKPAKPAS
     RSASKTDTNP SKTSPKSSAK PKSRAAPSSP VDIDELVRQS SKPPSRKKDV ELQKCEEILQ
     KIMKFRHSWP FREPVSAEEA EDYQDVITSP MDLTTMQGKF KSSEYHSASD FIEDMKLIFS
     NAEEYNQPSS NVLTCMSRTE EAFVELLQKS LPGVSYLRRR TRKRAATPSD NSDDDDDDEE
     EDERSKKQKN GKQGKKASSK RKVEHSRTEK YQTKQK
//