ID A0A384BH61_URSMA Unreviewed; 1719 AA.
AC A0A384BH61;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 03-AUG-2022, sequence version 2.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Bromodomain adjacent to zinc finger domain protein 2A isoform X3 {ECO:0000313|RefSeq:XP_008681886.2};
GN Name=BAZ2A {ECO:0000313|RefSeq:XP_008681886.2};
OS Ursus maritimus (Polar bear) (Thalarctos maritimus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=29073 {ECO:0000313|Proteomes:UP000261680, ECO:0000313|RefSeq:XP_008681886.2};
RN [1] {ECO:0000313|RefSeq:XP_008681886.2}
RP IDENTIFICATION.
RC TISSUE=Whole blood {ECO:0000313|RefSeq:XP_008681886.2};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the WAL family. {ECO:0000256|ARBA:ARBA00007444}.
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DR RefSeq; XP_008681886.2; XM_008683664.2.
DR OrthoDB; 2912910at2759; -.
DR Proteomes; UP000261680; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd05503; Bromo_BAZ2A_B_like; 1.
DR CDD; cd01397; HAT_MBD; 1.
DR CDD; cd15629; PHD_BAZ2A; 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; IPR017956; AT_hook_DNA-bd_motif.
DR InterPro; IPR037374; BAZ2A/B_Bromo.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR018501; DDT_dom.
DR InterPro; IPR016177; DNA-bd_dom_sf.
DR InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR InterPro; IPR028940; PHD_BAZ2A.
DR InterPro; IPR028942; WHIM1_dom.
DR InterPro; IPR028941; WHIM2_dom.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45915:SF5; BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 2A; 1.
DR PANTHER; PTHR45915; TRANSCRIPTION INTERMEDIARY FACTOR; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF02791; DDT; 1.
DR Pfam; PF01429; MBD; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF15612; WHIM1; 1.
DR Pfam; PF15613; WSD; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00384; AT_hook; 4.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00571; DDT; 1.
DR SMART; SM00391; MBD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF54171; DNA-binding domain; 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; PS50982; MBD; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000261680};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 307..378
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT DOMAIN 657..722
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1491..1541
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1624..1694
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 133..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..1077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1092..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1570..1596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..997
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1041
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1161..1175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1719 AA; 191311 MW; ADF2FC1494EBBBAC CRC64;
MCGYNGSVPS VESLHQEVSV LVPDPTVSCL DDPSHLPDQL EDTPILSEVS LEPFNPLAPE
PVSGGLYGID DTELMGTEDK LPLEDSPVIS ALDCPSLNNA TAFSLLADDS QTSASIFASP
TSPSVLGESV LQDNSFDLNN GSDAEQEEME TQASDFPPPL TQPASDQSST IQLHPATSPA
VLPTVSPAVS LAVSPAASLE ISPEVSPVAS PAVSPEISPV ISPAAFPAVS PTSSAALPPV
SSEVSLTGSP VTSPKVSPAA SPVAVLPTAS PADKDVSTFP ETTTDLEEIT GEGVTTSGSG
DVLRRRIATP EEVRLPLQHG WRREVRIKKG SHRWQGETWY YGPCGKRMKQ FPEVIKYLSR
NVVHNVRREH FSFSPRMPVG DFFEERDTPE GLQWVQLSAE EIPSRIQAIT GKRGRPRNTE
KAKTKEVPKV KRGRGRPPKV KIAELLNKTD NRLLKKLEAQ ETLNEEDKAK MSKIKKKMKQ
KVQRGECQPT IQGQARNKRK QEAKSLKQKE AKKKSKAEKE KVKTKQEKLK EKVKREKKEK
VKMKEKEEVA KGKSACKADK ALAVQRRLEE RQRQQMILEE MKKPTEDMCL TDHQVVRGEE
QVLGSWVLEG PVVKTFPLKE PPRYPDCCLQ VCLTALPLLS LQPLPDFSRI PGLILPSGAF
SDCLTIVEFL HSFGKVLGFD PAKDVPSLGV LQEGLLCQGD SLGEVQDLLV RLLKAALYDP
GLPSYCQSLK ILGEKVSEIP LTRDNVSEIL RCFLMAYGVE PALCDSLRTQ PFQAQPPQQK
AAVLAFLVHE LNGSTLIINE IDKTLESMSS YRKNKWIVEG RLRRLKTALA KRTGRPEIEM
QGPEEGLGRR RSSRIMEETS GMEEEEEEET IATVHGRRGR RDGEVDATAS SIPELERQIE
KLSKRQLFFR KKLLHSSQML RAVSLGQDRY RRRYWVLPYL AGIFVEGTEE SLVPEDMIKQ
ETDSLKVAAR PAPSPAPSSL KKELAGSSTS ASTPTRARGR PRKTKPGSLQ PRHLKSPSRD
QGSEQPDAQL QPEIQPHPQL QAQPQLQPPP QLQLHPQPQN GFLEPEGSPL SLGQSQHDLS
QSAFLSWLSQ TQSHGSLLSS SVLTPDSSPG KLDPTPSQPL EEPEPDEAES VPDAQAPWFN
FSAQMPCNAA PTPPPAVSED QPALSPQQPA SSKPMNRPGA ANPCSPIQLS STPLPGMASK
RRTGDSGGTP QSLTGLGQPK RRGRPPSKFF KQMEQRYLTQ LTAQPVPPEM GSGWWCIQDP
ETLDATLKAL HPRGIREKAL HKHLNKHRDF LQEVCLRPST DPIFEPSQLP AFQEGMISWS
PKEKTYETDL AVLQWVEELE QRVILSDLQI RGWTCPSPDS TREDLAYCEH LPDSQEDMTW
RGRVREGLAP QRKATNPLDL AVMRLAALEQ NVERRYLREP LWPAHEVVLE KALLSTPPGA
PQCATTEISY EITPRIRAWR QTLERCRSAA QVCLCLGQLE RSIAWEKSVN KVTCLVCRKG
DNDEFLLLCD GCDRGCHIYC HRPKMEAVPE GDWFCAVCLA QQVEGGFTQK PGFPKRGQKR
KSSYELNFPE SDSRRRRVLS RGRESPAVPR YSDEGLSPSK RRRFSMRNHH SDLTFCEIIL
MEMESHDAAW PFLEPVNPRL VSGYRRIIKN PMDFSTMRER LLRGGYTSSE EFAADALLVF
DNCQTFNEDD SEVGKAGHIM RRFFESRWEE FYQGKQANL
//