BRD2_BOVIN
ID BRD2_BOVIN Reviewed; 803 AA.
AC Q32S26;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Bromodomain-containing protein 2;
GN Name=BRD2;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16573526; DOI=10.1111/j.1365-2052.2005.01395.x;
RA Childers C.P., Newkirk H.L., Honeycutt D.A., Ramlachan N., Muzney D.M.,
RA Sodergren E., Gibbs R.A., Weinstock G.M., Womack J.E., Skow L.C.;
RT "Comparative analysis of the bovine MHC class IIb sequence identifies
RT inversion breakpoints and three unexpected genes.";
RL Anim. Genet. 37:121-129(2006).
CC -!- FUNCTION: Binds hyperacetylated chromatin and plays a role in the
CC regulation of transcription, probably by chromatin remodeling.
CC Regulates transcription of the CCND1 gene. Plays a role in nucleosome
CC assembly (By similarity). May play a role in spermatogenesis or
CC folliculogenesis (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with E2F1 and with histone H4 acetylated
CC at 'Lys-13' (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Detected on chromatin
CC and nucleosomes. {ECO:0000250}.
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DR EMBL; AY957499; AAY34703.1; -; Genomic_DNA.
DR RefSeq; NP_001039331.1; NM_001045866.1.
DR RefSeq; XP_005223266.1; XM_005223209.3.
DR RefSeq; XP_005223267.1; XM_005223210.3.
DR RefSeq; XP_005223268.1; XM_005223211.3.
DR RefSeq; XP_015315205.1; XM_015459719.1.
DR RefSeq; XP_015315206.1; XM_015459720.1.
DR AlphaFoldDB; Q32S26; -.
DR SMR; Q32S26; -.
DR STRING; 9913.ENSBTAP00000014704; -.
DR PaxDb; Q32S26; -.
DR PRIDE; Q32S26; -.
DR Ensembl; ENSBTAT00000014704; ENSBTAP00000014704; ENSBTAG00000011074.
DR GeneID; 505358; -.
DR KEGG; bta:505358; -.
DR CTD; 6046; -.
DR VEuPathDB; HostDB:ENSBTAG00000011074; -.
DR VGNC; VGNC:26557; BRD2.
DR eggNOG; KOG1474; Eukaryota.
DR GeneTree; ENSGT00940000153385; -.
DR HOGENOM; CLU_001499_0_4_1; -.
DR InParanoid; Q32S26; -.
DR OMA; MNIPHYP; -.
DR OrthoDB; 619848at2759; -.
DR TreeFam; TF317345; -.
DR Reactome; R-BTA-8951936; RUNX3 regulates p14-ARF.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000011074; Expressed in intramuscular adipose tissue and 105 other tissues.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0070577; F:lysine-acetylated histone binding; ISS:UniProtKB.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:Ensembl.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR GO; GO:0006334; P:nucleosome assembly; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd05497; Bromo_Brdt_I_like; 1.
DR CDD; cd05498; Bromo_Brdt_II_like; 1.
DR Gene3D; 1.20.1270.220; -; 1.
DR Gene3D; 1.20.920.10; -; 2.
DR InterPro; IPR043508; Bromo_Brdt_I.
DR InterPro; IPR043509; Bromo_Brdt_II.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR027353; NET_dom.
DR InterPro; IPR038336; NET_sf.
DR Pfam; PF17035; BET; 1.
DR Pfam; PF00439; Bromodomain; 2.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 2.
DR SUPFAM; SSF47370; SSF47370; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 2.
DR PROSITE; PS50014; BROMODOMAIN_2; 2.
DR PROSITE; PS51525; NET; 1.
PE 3: Inferred from homology;
KW Acetylation; Bromodomain; Chromatin regulator; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT CHAIN 1..803
FT /note="Bromodomain-containing protein 2"
FT /id="PRO_0000239862"
FT DOMAIN 91..163
FT /note="Bromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 364..436
FT /note="Bromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 634..716
FT /note="NET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00857"
FT REGION 53..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 556..560
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 312..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..512
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..564
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..652
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..803
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P25440"
FT MOD_RES 6
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P25440"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25440"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25440"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25440"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25440"
SQ SEQUENCE 803 AA; 88122 MW; DE0F35E3A3A55D2A CRC64;
MLQNVTPHNK LPGEGNAGLL GLGPEAAAPG KRIRKPSLLY EGFESPTMAS VPALQLTPAN
PPPPEVSNPK KPGRVTNQLQ YLHKVVMKAL WKHQFAWPFR QPVDAVKLGL PDYHKIIKQP
MDMGTIKRRL ENNYYWAASE CMQDFNTMFT NCYIYNKPTD DIVLMAQTLE KIFLQKVASM
PQEEQELVVT IPKNSHKKGA KLAALQGSIT SAHQVPAVSS VSHTALYTPP PEIPTTVLNI
PHPSVISSPL LKSLHSAGPP LLAVSAAPPA QPLAKKKGVK RKADTTTPTP TAILAPGSPA
SPPGGLEPKA ARLPPVRRES GRPIKPPRKD LPDSQQQHQS SKKGKLSEQL KHCNGILKEL
LSKKHAAYAW PFYKPVDASA LGLHDYHDII KHPMDLSTVK RKMENRDYRD AQEFAADVRL
MFSNCYKYNP PDHDVVAMAR KLQDVFEFRY AKMPDEPLEP GPLPVSTALP PGLAKSSSES
SSEESSSESS SEEEEEEDED EEEEEEESES SDSEEERAHR LAELQEQLRA VHEQLAALSQ
GPISKPKRKR EKKEKKKKRK AEKHRGRAGA DEDDKGPRAP RPSQPKKSKK AGGGGSSGAA
TLGPPGFGPS GGGATKLPKK ATKTAPPALP AGYDSEEEEE SRPMSYDEKR QLSLDINKLP
GEKLGRVVHI IQAREPSLRD SNPEEIEIDF ETLKPSTLRE LERYVLSCLR KKPRKPYTIK
KPVGKTKEEL ALEKKRELEK RLQDVSGQLN STKKPPKKAS EKTETSSAQQ VAVSRLSASS
SSSDSSSSSS SSSSSDTSDS DSG
