ID A0A384BI04_URSMA Unreviewed; 1965 AA.
AC A0A384BI04;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 03-AUG-2022, sequence version 2.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Bromodomain adjacent to zinc finger domain protein 2A isoform X1 {ECO:0000313|RefSeq:XP_008681879.2, ECO:0000313|RefSeq:XP_040493074.1};
GN Name=BAZ2A {ECO:0000313|RefSeq:XP_008681879.2,
GN ECO:0000313|RefSeq:XP_040493074.1, ECO:0000313|RefSeq:XP_040493075.1,
GN ECO:0000313|RefSeq:XP_040493076.1, ECO:0000313|RefSeq:XP_040493077.1,
GN ECO:0000313|RefSeq:XP_040493078.1};
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_008681879.2};
RN [1] {ECO:0000313|RefSeq:XP_008681879.2, ECO:0000313|RefSeq:XP_040493074.1}
RP IDENTIFICATION.
RC TISSUE=Whole blood {ECO:0000313|RefSeq:XP_008681879.2,
RC ECO:0000313|RefSeq:XP_040493074.1};
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_008681879.2; XM_008683657.2.
DR RefSeq; XP_040493074.1; XM_040637140.1.
DR RefSeq; XP_040493075.1; XM_040637141.1.
DR RefSeq; XP_040493076.1; XM_040637142.1.
DR RefSeq; XP_040493077.1; XM_040637143.1.
DR RefSeq; XP_040493078.1; XM_040637144.1.
DR STRING; 29073.ENSUMAP00000024314; -.
DR KEGG; umr:103656292; -.
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 553..624
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT DOMAIN 903..968
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1737..1787
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1870..1940
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1211..1323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1338..1473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1816..1842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..685
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..781
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1227..1243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1267..1287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1338..1360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1407..1421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1429..1443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1965 AA; 217312 MW; F202A84C397BA2F2 CRC64;
MEANDHFNFT GLPPAPAASG LKPSPSSGEG LYTNGSPMNF PQQGKSLNGD VNVNGLSTVS
HTTTSGILNS APHSSSTSHL HHPSVAYDCL WNYSQYPSAN PGNNLKDPPL LSQFSGGQYP
LNGILGGSRQ PSSPSHNTNL RAGSQEFWAN GTQSPMGLNF DSQELYDSFP DQNFEVMPNG
PPSFFTSPQT SPMLGSSIQT FAPSQEVGSG IHPDEVAEKE LTSVVAENGT GLVGSLELEE
EQPELKMCGY NGSVPSVESL HQEVSVLVPD PTVSCLDDPS HLPDQLEDTP ILSEVSLEPF
NPLAPEPVSG GLYGIDDTEL MGTEDKLPLE DSPVISALDC PSLNNATAFS LLADDSQTSA
SIFASPTSPS VLGESVLQDN SFDLNNGSDA EQEEMETQAS DFPPPLTQPA SDQSSTIQLH
PATSPAVLPT VSPAVSLAVS PAASLEISPE VSPVASPAVS PEISPVISPA AFPAVSPTSS
AALPPVSSEV SLTGSPVTSP KVSPAASPVA VLPTASPADK DVSTFPETTT DLEEITGEGV
TTSGSGDVLR RRIATPEEVR LPLQHGWRRE VRIKKGSHRW QGETWYYGPC GKRMKQFPEV
IKYLSRNVVH NVRREHFSFS PRMPVGDFFE ERDTPEGLQW VQLSAEEIPS RIQAITGKRG
RPRNTEKAKT KEVPKVKRGR GRPPKVKIAE LLNKTDNRLL KKLEAQETLN EEDKAKMSKI
KKKMKQKVQR GECQPTIQGQ ARNKRKQEAK SLKQKEAKKK SKAEKEKVKT KQEKLKEKVK
REKKEKVKMK EKEEVAKGKS ACKADKALAV QRRLEERQRQ QMILEEMKKP TEDMCLTDHQ
VVRGEEQVLG SWVLEGPVVK TFPLKEPPRY PDCCLQVCLT ALPLLSLQPL PDFSRIPGLI
LPSGAFSDCL TIVEFLHSFG KVLGFDPAKD VPSLGVLQEG LLCQGDSLGE VQDLLVRLLK
AALYDPGLPS YCQSLKILGE KVSEIPLTRD NVSEILRCFL MAYGVEPALC DSLRTQPFQA
QPPQQKAAVL AFLVHELNGS TLIINEIDKT LESMSSYRKN KWIVEGRLRR LKTALAKRTG
RPEIEMQGPE EGLGRRRSSR IMEETSGMEE EEEEETIATV HGRRGRRDGE VDATASSIPE
LERQIEKLSK RQLFFRKKLL HSSQMLRAVS LGQDRYRRRY WVLPYLAGIF VEGTEESLVP
EDMIKQETDS LKVAARPAPS PAPSSLKKEL AGSSTSASTP TRARGRPRKT KPGSLQPRHL
KSPSRDQGSE QPDAQLQPEI QPHPQLQAQP QLQPPPQLQL HPQPQNGFLE PEGSPLSLGQ
SQHDLSQSAF LSWLSQTQSH GSLLSSSVLT PDSSPGKLDP TPSQPLEEPE PDEAESVPDA
QAPWFNFSAQ MPCNAAPTPP PAVSEDQPAL SPQQPASSKP MNRPGAANPC SPIQLSSTPL
PGMASKRRTG DSGGTPQSLT GLGQPKRRGR PPSKFFKQME QRYLTQLTAQ PVPPEMGSGW
WCIQDPETLD ATLKALHPRG IREKALHKHL NKHRDFLQEV CLRPSTDPIF EPSQLPAFQE
GMISWSPKEK TYETDLAVLQ WVEELEQRVI LSDLQIRGWT CPSPDSTRED LAYCEHLPDS
QEDMTWRGRV REGLAPQRKA TNPLDLAVMR LAALEQNVER RYLREPLWPA HEVVLEKALL
STPPGAPQCA TTEISYEITP RIRAWRQTLE RCRSAAQVCL CLGQLERSIA WEKSVNKVTC
LVCRKGDNDE FLLLCDGCDR GCHIYCHRPK MEAVPEGDWF CAVCLAQQVE GGFTQKPGFP
KRGQKRKSSY ELNFPESDSR RRRVLSRGRE SPAVPRYSDE GLSPSKRRRF SMRNHHSDLT
FCEIILMEME SHDAAWPFLE PVNPRLVSGY RRIIKNPMDF STMRERLLRG GYTSSEEFAA
DALLVFDNCQ TFNEDDSEVG KAGHIMRRFF ESRWEEFYQG KQANL
//
