ID G5BG74_HETGA Unreviewed; 1480 AA.
AC G5BG74;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE SubName: Full=Tyrosine-protein kinase BAZ1B {ECO:0000313|EMBL:EHB08285.1};
GN ORFNames=GW7_08892 {ECO:0000313|EMBL:EHB08285.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB08285.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB08285.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00475}.
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DR EMBL; JH170081; EHB08285.1; -; Genomic_DNA.
DR RefSeq; XP_004840127.1; XM_004840070.1.
DR STRING; 10181.G5BG74; -.
DR GeneID; 101708143; -.
DR KEGG; hgl:101708143; -.
DR CTD; 9031; -.
DR eggNOG; KOG1245; Eukaryota.
DR InParanoid; G5BG74; -.
DR OrthoDB; 5490909at2759; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
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|EMBL:EHB08285.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00475}; Reference proteome {ECO:0000313|Proteomes:UP000006813};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000313|EMBL:EHB08285.1};
KW 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 1182..1232
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1185..1230
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1353..1423
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 145..210
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 381..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1118..1138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1235..1274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1288..1323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1450..1480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 537..579
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 168..210
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 1248..1272
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1480 AA; 170866 MW; BA05579DE93881CA CRC64;
MAPLLGRKPF PLVKPLPGEE PLFTIPHTQE AFRTREEYEA RLERYSERIW TCKSTGSSQL
THKEAWEEEQ EVAELLKEEF PTWYEKLVLE MVHHNTASLE KLVDTAWLEI MTKYAVGEEC
DFEVGKEKML KVKIVKIHPL EKVDEEATEK KSDGACDSPS SDKENSSQMA QDHQKKEAVV
KEDEGRREII NDRARRSPRK LPTSLKKGER KWAPPKFLPH KYDVKLQNED KIISNVPADS
LIRTERPPNK EILRYFIRHN ALRAGAGENA PWVVEDELVK KYSLPSKFSD FLLDPYKYMT
LNPSTKRKNT GSPDRKPSKK SKTDNSSLSS PLNPKLWCHV HLKKSLNGSP LKMKNSKNSK
SPEEHLEEVM KMMSPNKLHA NFHIPKRGPA AKKPGKHSDK PLKAKGRSKG ILNGQKSTGS
SKSPKKGLKT PKTKMKQMTL LDMAKGTQKM ARAPRNSGGT PRSSSKPHKH LPPAALHLIA
YYKENKDRED KKSALSCVIS KTARLLSSED RARLPEELRT IVQKRYELLE HRKRWASMSE
EQRKEYLKKK RQELKEKLKE KAKERRQKEM LEKLEKQKRY EDQELAGKNL PTFRLVDTPE
GLPNTLFGDV ALVVEFLSCY SGLLLPDAQY PITAVSLMEA LSADKGGFLY LNRVLVILLQ
TLLQDEIAED YGELGMKLSE IPLTLHSVSE LVRLCLRRSD AQEESESSDT DDKDSAPFED
NEVQDEFLEK LETSEFFELT SEEKLQILTA LCHRILMTYS VQDHMETRQQ MSAELWKERL
AVLKEENDKK RAEKQKRKEM EARSKENGKE ENGLGKTDRK KEIVKFEPQV DMEAEDMISA
VKSRRLLALQ AKREREIQER EMKVKLEREA EEERIRKHKA AAEKAFQEGI ARAKLVMRRT
PIGTDRNHNR YWLFSDEVPG LFIEKGWAHD SIDYRFNHHR KDHADSSGED YCPRSKKANL
GKNASMNTHR SALEIAVETT IPKQGQNLWF LCDSQKELDD LLNCLHPQGI RESQLKERLE
KRYQDIIHSI HLARKPNLGL KCCDGNQELL NFLRSDLIEV ATRLQKGGLG YVEETSEFEA
RVISLEKLKD FGECVIALQA SVIKKFLQGF MAPKQKRRKV QSEDSAKTEE VDEEKKMAEE
EKVASALEKW KTAIREAQTF SRMHVLLGML DACIKWDMSA ENARCKVCRK KGEDDKLILC
DECNKAFHLF CLRPALYEVP DGEWQCPACQ PATARRNSRG RNYTEESASE DSEDDESDSE
EEEEEEEEEE DYEVAGLRLR PRKIIRGKQI VIPPASRPGR RPGKKPHPPQ RSQQKASPVD
DVEVDELVLQ TKRSSRRQSL ELQKCEEILH KIVKYRFSWP FREPVTRDEA EDYYDVITQP
MDFQTMQNKC SCGNYRSVQE FLTDMKQVFT NAELYNCRGS HVLNCTVKTE QCLVALLHKH
LPGHPYVRRK RKKFPDRLAD DEVDSDPEPV GQSRGRRQKK
//