ID A0A2Y9S885_PHYMC Unreviewed; 1483 AA.
AC A0A2Y9S885;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Tyrosine-protein kinase BAZ1B {ECO:0000313|RefSeq:XP_023974881.1, ECO:0000313|RefSeq:XP_028354071.1};
GN Name=BAZ1B {ECO:0000313|RefSeq:XP_023974881.1,
GN ECO:0000313|RefSeq:XP_028354071.1, ECO:0000313|RefSeq:XP_028354072.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_023974881.1};
RN [1] {ECO:0000313|RefSeq:XP_023974881.1, ECO:0000313|RefSeq:XP_028354071.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_023974881.1,
RC ECO:0000313|RefSeq:XP_028354071.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00475}.
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DR RefSeq; XP_023974881.1; XM_024119113.3.
DR RefSeq; XP_028354071.1; XM_028498270.2.
DR RefSeq; XP_028354072.1; XM_028498271.2.
DR STRING; 9755.ENSPCTP00005010307; -.
DR Ensembl; ENSPCTT00005011418; ENSPCTP00005010307; ENSPCTG00005007357.
DR KEGG; pcad:102976261; -.
DR OrthoDB; 5490909at2759; -.
DR Proteomes; UP000248484; Chromosome 14.
DR GO; GO:0110016; C:B-WICH complex; IEA:Ensembl.
DR GO; GO:0043596; C:nuclear replication fork; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0090535; C:WICH complex; IEA:Ensembl.
DR GO; GO:0140801; F:histone H2AXY142 kinase activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:DNA damage response; IEA:Ensembl.
DR GO; GO:1905213; P:negative regulation of mitotic chromosome condensation; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IEA:Ensembl.
DR GO; GO:0043687; P:post-translational protein modification; IEA:Ensembl.
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_023974881.1,
KW ECO:0000313|RefSeq:XP_028354071.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00475}; Reference proteome {ECO:0000313|Proteomes:UP000248484};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000313|RefSeq:XP_023974881.1,
KW ECO:0000313|RefSeq:XP_028354071.1}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 20..126
FT /note="WAC"
FT /evidence="ECO:0000259|PROSITE:PS51136"
FT DOMAIN 604..668
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1184..1234
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1187..1232
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1356..1426
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 144..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 380..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..821
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 537..583
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 144..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ SEQUENCE 1483 AA; 170985 MW; A23296FD58A2BD73 CRC64;
MAPLLGRKPF PLVKPLPGEE PLFTIAHTQE AFRTREEYEA RLERYSERIW TCKSTGSSQL
THKEAWEEEQ EVAELLKEEF PAWYEKLVLE MVHHNTASLE KLVDTAWLEI MTKYAVGEEC
DFEVGKEKML KVRIVKIHPL EKVDEEATEK KSDGACDSPS SDKENSSQIA QDHQKKEAIV
KEDEGRRESI NDRARRSPRK LPTSLKKGER KWAPPKFLPH KYDVKLQNED KIISNVPADS
LIRTERPPNK EILRYFIRHN ALRAGTGENA PWVVEDELVK KYSLPSKFSD FLLDPYKYMT
LNPSTKRKNT GSPDRKPSKK SKTDNSSLSS PLNPKLWCHV HLKKSLNGSP LKVKNSKNSK
SPEEHLEEVM KMMSPNKLHA NFHIPKKGPP GKKSGKHSDK PLKAKGRSKG ILNGQKSTGN
SKSPKKGLKT PKTKMKQMTL LDMAKGTQKV TRAPRNSGGT PRSSSKPHKH LPPAALHLIA
YYKENKDRED KKSALSCVIS KTARLLSSED RARLPEELRS IVQKRFELLE HKKRWASMSE
EQRKEYLKKK REELKEKLKE KAKERREKEM LEKLEKQKRY EDQELTGKNL PTFKLVDTPE
GLPNTLFGDV AMVVEFLSCY SGLLLPDAQY PITAVSLMEA LSAEKGGFLY LNRVLVILLQ
TLLQDEIAED YGELGMKLSE IPLTLHSVSE LVRLCLRKSD IQEESEGSDT DDNKDSAPFE
DNEVQDEFLE KLETSEFFEL TSEEKLQILT ALCHRILMTY SVQDHMETRQ QMSAELWKER
LAVLKEENDK KRAEKQKRKE MEARNKENGK EENGLGKADR KKEVVKFEPQ VDMEAEDMIS
AVKSRRLLAI QAKKEREIQE REMKVKLERE AEEERIRKHK AAAEKAFQEG IAKAKLVMRR
TPIGTDRNHN RYWLFSDEVP GLFIEKGWVH DSIDYRFNHH RKDHADSPDE DYCPRSKKAN
LGKNVNMNTQ HGPATEIAVE TTIPKQGQNL WFLCDSQKEL DELLNCLHPQ GIRESQLKER
LEKRYQDIIH SIHLARKPNL GLKSCDGNQE LLNFLRSDLI EVATRLQKGG LGYVEETSEF
EARVISLEKL KDFGECVIAL QASVIKKFLQ GFMAPKQKRR KLQSEDSAKT EEVDEEKKMA
EEAKVASALE KWKTAIREAQ TFSRMHVLLG MLDACIKWDM SAENARCKVC RKKGEDDKLI
LCDECNKAFH LFCLRPALYE VPDGEWQCPA CQPATARRNS RGRNYTEESA SEDSEDDESN
EEEEEEEEEE GEEDYEVAGL RLRPRKTVRG KQGVIPPAAR PGRRPGKKPH PTRRSRPKAS
PVDEAEVDEL VLQTKRSSRR QSLELQKCEE ILHKIVKYRF SWPFREPVTR DEAEDYYDVI
THPMDFQTMQ NKCSCGSYRS VQEFLTDMKQ VFTNAELYNC RGSHVLNCMV KTEQCLMALL
HKHLPGHPYV RRKRKKFPDR LAEDEGDSEP EPVGQSRGRR QKK
//
