BAZ1B_XENLA
ID BAZ1B_XENLA Reviewed; 1441 AA.
AC A8DZJ1; A0JMY1; Q6GQ06;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 74.
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;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16448863; DOI=10.1016/j.modgep.2005.10.001;
RA Cus R., Maurus D., Kuehl M.;
RT "Cloning and developmental expression of WSTF during Xenopus laevis
RT embryogenesis.";
RL Gene Expr. Patterns 6:340-346(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-774.
RC TISSUE=Embryo, and Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- TISSUE SPECIFICITY: Highly expressed in the neural tube.
CC {ECO:0000269|PubMed:16448863}.
CC -!- DEVELOPMENTAL STAGE: Detected maternally in mature unfertilized oocytes
CC and ubiquitously expressed until embryonic stage 16. In stage 17/18,
CC expression becomes restricted to the closing neural tube.
CC {ECO:0000269|PubMed:16448863}.
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=AAH72944.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AM084226; CAJ29032.1; -; mRNA.
DR EMBL; BC072944; AAH72944.1; ALT_SEQ; mRNA.
DR EMBL; BC126047; AAI26048.1; -; mRNA.
DR RefSeq; NP_001136259.1; NM_001142787.1.
DR AlphaFoldDB; A8DZJ1; -.
DR SMR; A8DZJ1; -.
DR BioGRID; 101759; 1.
DR IntAct; A8DZJ1; 1.
DR PRIDE; A8DZJ1; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IEA:InterPro.
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 2: Evidence at transcript level;
KW ATP-binding; Bromodomain; Coiled coil; DNA damage; Kinase; Metal-binding;
KW Nucleotide-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Transferase; Tyrosine-protein kinase; Zinc;
KW Zinc-finger.
FT CHAIN 1..1441
FT /note="Tyrosine-protein kinase BAZ1B"
FT /id="PRO_0000378189"
FT DOMAIN 26..132
FT /note="WAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00475"
FT DOMAIN 578..642
FT /note="DDT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00063"
FT DOMAIN 1321..1391
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT ZN_FING 1151..1201
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 147..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1204..1308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1408..1441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 513..558
FT /evidence="ECO:0000255"
FT COILED 813..861
FT /evidence="ECO:0000255"
FT COILED 1080..1113
FT /evidence="ECO:0000255"
FT COILED 1213..1253
FT /evidence="ECO:0000255"
FT COMPBIAS 147..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..692
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1216..1244
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1253..1276
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1279..1300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1420..1441
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 275
FT /note="A -> P (in Ref. 2; AAI26048)"
FT /evidence="ECO:0000305"
FT CONFLICT 763
FT /note="G -> E (in Ref. 1; CAJ29032)"
FT /evidence="ECO:0000305"
FT CONFLICT 771
FT /note="A -> E (in Ref. 1; CAJ29032)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1441 AA; 166153 MW; 9124174FDBBC09ED CRC64;
MAPLLGRRPF PLVKPLSEAA TGEGEEEVYM IEHSKEAFRS REEYESRLER YAERIWTCKS
TGSSQLTHKE AWDEEQEVAE LLKEEFPVWY EKQVLEMVHH NTISLDKLVD QSWMEIMTKY
ADGEECDFEV GPEKYLRAKI VKVHPLEKEE QASEKKSEGS CDSPSSDKEN SNKVAQDIQL
KEESNRLESL SSLRESDRAR RSPRKLPTSL KKEEKKWVPP KFLPHKYDVK LLNEDKVISF
VPVDSLYRSE RPPNKEILRY FIRHNALRIG TGENAPWVVE DELVKKYTLP SKFSDFLLDP
HKYMTLNPSS ATKRKSLGSP DQKPAKKSKK SPLSPSSWSL ANLKKTAVNS SSSEEEMQLM
IGANLNKKGS IGKKSDKKKP KNGKSQVLNG QKISAKTRSP KKGLKSPKLK QMTLLDMAKS
TPKVSRAQKG GSNTPRSSSK PNKYLPPAAL HLISYYRDNK NREDRKSALS ALISKVARML
SAEDRKRLPD DLQELVQKRY ELLEHRKQWA VMTEEQREEY MRKKREALKA RIKEKTRERK
QKEREERLEK QKRYEDQDLT GKSLPTFKLV DTPEGLPNAL FGDVAMVIEF LSGYSDLLLP
DGQYPVTAVS LMEALAAEKG GFMYLNRGLV VLLQTLLQDE IAEDYGELGM KLSEIPLTLH
SASELVRLCL RKSDSPAGEN ESIEKGDEDS EGSAVYQDDE VEDEYLEKLE TSEFFELTTE
EKLHILAALC HRILMTYSVQ DHVDAKQQRS GELWKERLAI LKGENDKKRA AKQKRKEQGT
VKPKEEVQAA KIVKKQEKIN TQQDNDAEDM ISAVKSRRLQ AMQAKKEKEE HEKLTKERIE
RETEEERSRK QKASAEKAFH EGIAKAKLVL RRSPLGTDRN HNRYWLFSDE VPGLYIEKGW
VHDSINYRFS PESKQDSEQD AEESEDANSS IGCPDDSTQR EEKHAETTVP KQGQNLWFLC
DTQKELDELL DSLHPQGFRE SQLKERLQNR YQDIMHSIHL ARKQNLGLKT CDGQQELLNF
LRSDIIEVAT RLQKGGLGYL DDTTEFEAKV RTFENLKDFG ECIVFLQAAV IKKFLQGFMA
PKQKKRKHQS EEAAAKAEEQ DEEKKMAEEA KVASAVEKWK VAIRDAQTFS RMHVLLGMLD
ACIKWDMSSE NARCKVCRKK GEDDKLILCD ECNKAFHLFC LRPVLFNIPD GEWLCPACQP
ATARRSSRGR NYAEDSTQDE DEEEEEEESE EEEEEESDEE EEEQEMMGQR LRSRKAAKGK
PGRPTRRGRP PKNNTHSRVS RQRYVEDTEA DVEEMVRQSK PTSRRQNQEF QKCEEILAKL
IKYRFSWPFR EPFNADEIED YTKVVTTPMD FQTMQSKCSC GSYQTVQEFL NDLKLVFGNT
ELYYEAGSSQ LSCLEKTEQC ARDLLGKHLP AHTYQRRHRK HQSPEPEPET ANPGRGRKQK
K
