BAZ1B_DANRE
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 03-AUG-2022, entry version 95.
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=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 -!- 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). {ECO:0000250}.
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 STRING; 7955.ENSDARP00000104660; -.
DR iPTMnet; A2BIL7; -.
DR PaxDb; A2BIL7; -.
DR PeptideAtlas; A2BIL7; -.
DR PRIDE; A2BIL7; -.
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; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0090535; C:WICH complex; IBA:GO_Central.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:1990164; P:histone H2A phosphorylation; IBA:GO_Central.
DR GO; GO:0043687; P:post-translational protein modification; ISS:UniProtKB.
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; 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; 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 1383..1453
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 144..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..969
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1267..1287
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1296..1315
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1319..1344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1522..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
