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Database: UniProt
Entry: F1N6I8_BOVIN
LinkDB: F1N6I8_BOVIN
Original site: F1N6I8_BOVIN 
ID   F1N6I8_BOVIN            Unreviewed;      1898 AA.
AC   F1N6I8;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 3.
DT   27-MAR-2024, entry version 90.
DE   SubName: Full=Bromodomain adjacent to zinc finger domain 2A {ECO:0000313|Ensembl:ENSBTAP00000038030.5};
GN   Name=BAZ2A {ECO:0000313|Ensembl:ENSBTAP00000038030.5,
GN   ECO:0000313|VGNC:VGNC:26430};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000038030.5, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000038030.5, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000038030.5,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000038030.5}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000038030.5};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the WAL family. {ECO:0000256|ARBA:ARBA00007444}.
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DR   RefSeq; NP_001180159.2; NM_001193230.2.
DR   SMR; F1N6I8; -.
DR   STRING; 9913.ENSBTAP00000038030; -.
DR   PaxDb; 9913-ENSBTAP00000038030; -.
DR   Ensembl; ENSBTAT00000038215.5; ENSBTAP00000038030.5; ENSBTAG00000017840.6.
DR   GeneID; 509799; -.
DR   KEGG; bta:509799; -.
DR   CTD; 11176; -.
DR   VEuPathDB; HostDB:ENSBTAG00000017840; -.
DR   VGNC; VGNC:26430; BAZ2A.
DR   eggNOG; KOG1245; Eukaryota.
DR   GeneTree; ENSGT00940000159490; -.
DR   HOGENOM; CLU_000899_1_0_1; -.
DR   InParanoid; F1N6I8; -.
DR   OMA; GMIMWER; -.
DR   TreeFam; TF329083; -.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000017840; Expressed in thymus and 106 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0033553; C:rDNA heterochromatin; IBA:GO_Central.
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:UP000009136};
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          538..609
FT                   /note="MBD"
FT                   /evidence="ECO:0000259|PROSITE:PS50982"
FT   DOMAIN          840..905
FT                   /note="DDT"
FT                   /evidence="ECO:0000259|PROSITE:PS50827"
FT   DOMAIN          1670..1720
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          1803..1873
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          366..448
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          642..668
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          709..770
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1016..1065
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1149..1256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1277..1406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1755..1782
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        366..440
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        645..668
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        728..770
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1016..1042
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1149..1178
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1181..1195
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1204..1237
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1312..1326
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1340..1368
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1898 AA;  210125 MW;  6FA60EEF9DD94F80 CRC64;
     MKMEANDHFN FTGLPPAPAA SGLKPSPSSG EGLYTNGSPM NFPQQGKSLN GDVNVNGLST
     VSHTTTSGIL NSAPHSSSTS HLHHPNVAYD CLWNYSQYPS ANPGSNLKDP PLLSQFSGGQ
     YPLNGILGGS RQPSSPSHNT NLRAGSQEFW ANGTQSPMGL NFDSQELYDS FPDQNFEVMP
     NGPPSFFTSP QTSPMLGSSI QTFAPSQEVG SGIHPDEAAE KELTSVVTEN GAGLVGSLEL
     EEEQPELKMC GYNGSVPSVE SLHQEVSVLV PDPTVSCLDD PSHLPDQLED TPILSEVSLE
     PFNTLAPEPV SGGLYGIDDT ELMGAEDKLP LEDSPVISAL DCPSLNNATA FSLLADDSQT
     SASIFASPTS PPVLGESVLQ DNSFDLNNGS DAEQEEMETQ ASDFPPLTQP APDQSSTIQL
     HPATSPAVSP TASSAVSLPV SPAASPEISP AISPAAFPEV SPASSAALPP VSSEVSLTAS
     PVTSPKASPA ASPAAVFPTV SPADKDISSV PETIADLEDT TVEGVPPSGS GDVLRRRIAT
     PEEVRLPLQH GWRREVRIKK GSHRWQGETW YYGPCGKRMK QFPEVIKYLS RNVVHNVRRE
     HFSFSPRMPV GDFFEERDTP EGLQWVQLSA EEIPSRIQAI TGKRGRPRNT EKAKTKEVPK
     VKRGRGRPPK VKITELLNKT DTRLLKKLEA QETLNEEDKA KMCKIKKKIK QKVQRGECQT
     TNQGQAKNKR KQETKSLKQK EAKKKSKAEK EKVKTKQEKL KEKVKREKKE KVKMKEKEEV
     AKTKPTGKAD KVLATQRRLE ERQRQQMILE EMKKPTEDMC LTDHQPLPDF SRIPGLILPS
     GAFSDCLTIV EFLHSFGKVL GFDPAKDVPS LGVLQEGLLC QGDSLGEVQD LLVRLLRAAL
     CDPGLPSYCQ SLKILGEKVS EIPLTRDNVS EILRCFLMAY GVEPALCDSL RTQPFQAQPP
     QQKAAVLAFL VHELNGSTLI INEIDKTLES MSSYRKNKWI VEGRLRRLKT ALAKRTGRPE
     VELQGPEEGL GRRRSSRIME ETSGMEEEEE EETAAAVHGR RGRRDGEVDI TASSIPELER
     QIEKLSKRQL FFRKKLLHSS QMLRAVSLGQ DRYRRRYWVL PYLTGIFVEG TEGSLVPEDV
     IKQETDSLKV ATHSTTSPTS FSLKRELAGS STSASSPARA RGRPRKTKPG SMQPRHLKSH
     SKGQGSEEPQ TQLQPETQSH PQLQAHAQPQ LQSHPHTHNG FLEPEGSPLS LGQSQHDLSQ
     SAFLSWLSQT QNHGSLLSSS VLTPDSSPGK LDPAPSHAPE EPEPDETEAS PDSQAPWFNF
     SAQMPCNAAP TPPPAVSEDQ PTLSPQLPAS SKPVSRASAA NAYSPGPFSS TPLLGMAHKR
     QAGDPGETPQ SPTGQGQPKR RGRPPSKFFK QMEQRYLTQL TAQPVPPEMR SGWWWIRDPE
     TLDATLKALH PRGIREKALH KHLNKHRDFL QEVCLRPSTD PIFEPSQLPA FEEGIVSWTP
     KEKTYETDLA VLQWVEELEQ RVILSDLQIR GWTCPSPDST REDLAYCEHL ADSQEDITWR
     GRGKEGLAPQ RKTTNPLDLA VMRLAALEQN VERRYLREPL WPAHEVVLEK ALLSTPSSAP
     QCTPTEISYE ITPRVRAWRQ TLERCRSAAQ VCLCLGQLER SIAWEKSVNK VTCLVCRKGD
     NDEFLLLCDG CDRGCHIYCL RPKMEAVPEG DWFCAVCLAQ QVEGELTQKS GFPKRGQKRK
     SGYVLTFPEG DNRRRRLLPR GRESPAVPRY SEEGLSPSKR RRVSMRNHHS DLTFCEIILM
     EMESHDAAWP FLEPVNPRLV SGYRRIIKNP MDFSTMRERL LRGGYTSSEE FAADALLVFD
     NCQTFNEDDS EVGKAGHIMR RFFESRWEEF YQGKQANL
//
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