ID A0A2Y9JEB5_ENHLU Unreviewed; 1454 AA.
AC A0A2Y9JEB5;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Tyrosine-protein kinase BAZ1B isoform X3 {ECO:0000313|RefSeq:XP_022356129.1, ECO:0000313|RefSeq:XP_022356130.1};
GN Name=LOC111145522 {ECO:0000313|RefSeq:XP_022356129.1,
GN ECO:0000313|RefSeq:XP_022356130.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022356130.1};
RN [1] {ECO:0000313|RefSeq:XP_022356129.1, ECO:0000313|RefSeq:XP_022356130.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022356129.1,
RC ECO:0000313|RefSeq:XP_022356130.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00475}.
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DR RefSeq; XP_022356129.1; XM_022500421.1.
DR RefSeq; XP_022356130.1; XM_022500422.1.
DR Proteomes; UP000248482; 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_022356129.1,
KW ECO:0000313|RefSeq:XP_022356130.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00475}; Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000313|RefSeq:XP_022356129.1,
KW ECO:0000313|RefSeq:XP_022356130.1}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 1..100
FT /note="WAC"
FT /evidence="ECO:0000259|PROSITE:PS51136"
FT DOMAIN 578..642
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1157..1207
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1160..1205
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1327..1397
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 119..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1210..1297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1426..1454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 511..557
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 142..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1223..1246
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1454 AA; 167225 MW; 165B0A6776956BE2 CRC64;
MLFPASTANR EYEARLERYS ERIWTCKSTG SSQLTHKEAW EEEQEVAELL KEEFPAWYEK
LVLEMVHHNT ASLEKLVDTA WLEIMTKYAV GEECDFEVGK EKMLKVRIVK IHPLEKVDEE
AAEKKSDGAC DSPSSDKENS GQIPQDHQKK EAIVKEDEGR RESINDRARR SPRKLPTSLK
KGERKWAPPK FLPHKYDVKL QNEDKIISNV PADSLIRTER PPNKEILRYF IRHNALRAGT
GENAPWVVED ELVKKYSLPS KFSDFLLDPY KYMTLNPSTK RKNTGSPDRK PSKKSKTDNS
SLSSPLNPKL WCHVHLKKSL NGSPLKVKNS KNSRSPEEHL EEVMKMMSPA KLHSNFHIPK
KGPPARKSGK HNDKPLKAKG RSKGILNGQK STGNSKSPKK GLKTPKTKMK QMTLLDMAKG
TQKMTRAPRN SGGTARSSSK PHKHLPPAAL HLIAYYKENK DREDKKSALS CVISKTARLL
SSEDRARLPE ELRSLVQKRF ELLEHKKRWA SMSEEQRKEY LKKKREELKE KLKEKAKERR
EKEMLEKLEK QKRYEDQELS GKSLPAFRLV DTPEGLPNTL FGDVAMVVEF LSCYSGLLLP
DAQYPITAVS LMEALSAEKG GFLYLNRVLV ILLQTLLQDE IAEDYGELGM KLSEIPLTLH
SVSELVRLCL RRSDVQEESE GSDADDNKDS APFEDNEVQD EFLEKLETSE FFELTSEEKL
QILTALCHRI LMTYSVQDHM ETRQQMSAEL WKERLAVLKE ENDKKRAEKQ KRKEMEARNK
ENGKEENGLG KPDRKKEVVK FEPHVDLGAE DMISAVKSRR LLAIQAKKER EIQEREMKVK
LEREAEEERI RRHKAAAEKA FQEGIAKAKL VMRRTPIGTD RNHNRYWLFS DEVPGLFIEK
GWVHDSIDYR FSHRKDRADP ADEDYCPRSK KANLGKNANV NAQPGPATEV AVETTIPKQG
QNLWFLCDSQ KELDELLNCL HPQGIRESQL KERLEKRYQD IIHSIHLARK PNLGLKSCDG
NQELLNFLRS DLIEVATRLQ KGGLGYVEET SEFEARVISL EKLKDFGECV IALQASVIKK
FLQGFMAPRQ KRRKLQSEDS AKMEEVDEEK KLAEEAEVAS ALEKWKTAIR EAQTFSRMHV
LLGMLDACIK WDMSAENARC KVCRKKGEDD KLVLCDECNK AFHLFCLRPA LYEVPDGEWQ
CPACQPATAR RNSRGRNYTE ESASEDSEDD ESDDEEEEEE EEEADYEVAG LRLRPRKTAR
AKQGVLPAAA RPGRRPGKKP HPARKSRPKA PPVDDAEVEE LVLQTKRSSR RQSLELQKCE
EILHKIVKYR FSWPFREPVT RDEAEDYYDV ITHPMDFQTM QNKCSCGSYR SVQEFLSDMK
QVFANAELYN CRGSHVLTCT VKTEQCLVAL LHKHLPGHPY VRRKRKKFPD RLAEDEGDSE
SETIGQSRGR RQKK
//
