ID A0A2U3YJQ2_LEPWE Unreviewed; 1443 AA.
AC A0A2U3YJQ2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Tyrosine-protein kinase BAZ1B {ECO:0000313|RefSeq:XP_006743941.1};
GN Name=BAZ1B {ECO:0000313|RefSeq:XP_006743941.1};
OS Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC Leptonychotes.
OX NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_006743941.1};
RN [1] {ECO:0000313|RefSeq:XP_006743941.1}
RP IDENTIFICATION.
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_006743941.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00475}.
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DR RefSeq; XP_006743941.1; XM_006743878.2.
DR STRING; 9713.A0A2U3YJQ2; -.
DR GeneID; 102743950; -.
DR KEGG; lww:102743950; -.
DR CTD; 9031; -.
DR OrthoDB; 5490909at2759; -.
DR Proteomes; UP000245341; Unplaced.
DR GO; GO:0090535; C:WICH complex; IEA:InterPro.
DR GO; GO:0140801; F:histone H2AXY142 kinase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05505; Bromo_WSTF_like; 1.
DR CDD; cd15628; PHD_BAZ1B; 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; 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 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; 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.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000313|RefSeq:XP_006743941.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00475}; Reference proteome {ECO:0000313|Proteomes:UP000245341};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000313|RefSeq:XP_006743941.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 1..87
FT /note="WAC"
FT /evidence="ECO:0000259|PROSITE:PS51136"
FT DOMAIN 565..629
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1144..1194
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1147..1192
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1316..1386
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 105..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 905..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1197..1286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1415..1443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 498..544
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 105..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1210..1235
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1443 AA; 165895 MW; 3A7FC464AD5C90A7 CRC64;
MAPLLGRKPF PLVKPLPGEE PLFTIAHTQE AFRTRDLKEE FPAWYEKLVL EMVHHNTASL
EKLVDTAWLE IMTKYAVGEE CDFEVGKEKM LKVRIVKIHP LEKVDEEATE KKSDGACDSP
SSDKENSSQI AQDHQKKEAI VKEDEGRRES ISDRARRSPR KLPTSLKKGE RKWAPPKFLP
HKYDVKLQNE DKIISNVPAD SLIRTERPPN KEILRYFIRH NALRAGTGEN APWVVEDELV
KKYSLPSKFS DFLLDPYKYM TLNPSTKRKN TGSPDRKPSK KSKTDNSSLS SPLNPKLWCH
VHLKKSLNGS PLKVKNSKNS KSPEEHLEEV MKMMSPNKLH ANFHIPKKGP PAKKSGKHSD
KPLKAKGRSK GILNGQKSTG NSKSPKKGLK TPKTKMKQMT LLDMAKGTQK MTRAPRNSGG
TARSSSKPHK HLPPAALHLI AYYKENKDRE DKKSALSCVI SKTARLLSSE DRARLPEELR
SIVQKRFELL EHKKRWASMS EEQRKEYLKK KREELKEKLK EKAKERREKE MLEKLEKQKR
YEDQELTGKS LPAFRLVDTP EGLPNTLFGD VAMVVEFLSC YSGLLLPDAQ YPITAVSLME
ALSAEKGGFL YLNRVLVILL QTLLQDEIAE DYGELGMKLS EIPLTLHSVS ELVRLCLRRS
DVQEESEGSD ADDNKDSAPF EDNEVQDEFL EKLETSEFFE LTSEEKLQIL TALCHRILMT
YSVQDHMETR QQMSAELWKE RLAVLKEEND KKRAEKQKRK EMEARNKENG KEENGLGKPD
RKKEVVKFEP QVDLGAEDMI SAVKSRRLLA IQAKKEREIQ EREMKVKLER EAEEERIRKH
KAAAEKAFQE GIAKAKLVMR RTPIGTDRNH NRYWLFSDEV PGLFIEKGWV HDSIDYRFNH
RKDRADSPDE DYCPRSKKAN LGKNASMNTQ PGPATEVAVE TTIPKQGQNL WFLCDSQKEL
DELLNCLHPQ GIRESQLKER LEKRYQDIIH SIHLARKPNL GLKSCDGNQE LLNFLRSDLI
EVATRLQKGG LGYVEETSEF EARVISLEKL KDFGECVIAL QASVIKKFLQ GFMAPKQKRR
KLQSEDSAKT EEVDEEKKLA EEAKVASALE KWKTAIREAQ TFSRMHVLLG MLDACIKWDM
SAENARCKVC RKKGEDDKLI LCDECNKAFH LFCLRPALYE VPDGEWQCPA CQPATARRNS
RGRNYTEESA SEDSEDDESD EEEEEEEEEE EEEDYEVAGL RLRPRKTVRG KQGVIPAAAR
PGRRPGKKPH PTRKSRPKAP PVDDAEVEEL VLQTKRSSRR QSLELQKCEE ILHKIVKYRF
SWPFREPVTR DEAEDYYDII THPMDFQTMQ NKCSCGSYRS VQEFLTDMKQ VFTNAELYNC
RGSHVLNCTV KTEQCLVALL HKHLPGHPYV RRKRKKFPDR LAEDEGDSES EPVGQSRGRR
QKK
//
