BRD2_CANLF
ID BRD2_CANLF Reviewed; 803 AA.
AC Q5TJG6;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Bromodomain-containing protein 2;
GN Name=BRD2;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Doberman pinscher;
RX PubMed=15607421; DOI=10.1016/j.ygeno.2004.09.009;
RA Debenham S.L., Hart E.A., Ashurst J.L., Howe K.L., Quail M.A.,
RA Ollier W.E.R., Binns M.M.;
RT "Genomic sequence of the class II region of the canine MHC: comparison with
RT the MHC of other mammalian species.";
RL Genomics 85:48-59(2005).
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; AJ630365; CAI11405.1; -; Genomic_DNA.
DR RefSeq; NP_001041552.1; NM_001048087.1.
DR RefSeq; XP_005627105.1; XM_005627048.2.
DR RefSeq; XP_005627106.1; XM_005627049.2.
DR AlphaFoldDB; Q5TJG6; -.
DR SMR; Q5TJG6; -.
DR STRING; 9612.ENSCAFP00000001265; -.
DR PaxDb; Q5TJG6; -.
DR Ensembl; ENSCAFT00030026700; ENSCAFP00030023306; ENSCAFG00030014374.
DR Ensembl; ENSCAFT00040037292; ENSCAFP00040032495; ENSCAFG00040020153.
DR Ensembl; ENSCAFT00845033101; ENSCAFP00845025912; ENSCAFG00845018726.
DR GeneID; 474868; -.
DR KEGG; cfa:474868; -.
DR CTD; 6046; -.
DR VEuPathDB; HostDB:ENSCAFG00845018726; -.
DR eggNOG; KOG1474; Eukaryota.
DR GeneTree; ENSGT00940000153385; -.
DR HOGENOM; CLU_001499_0_4_1; -.
DR InParanoid; Q5TJG6; -.
DR OMA; MNIPHYP; -.
DR OrthoDB; 619848at2759; -.
DR TreeFam; TF317345; -.
DR Proteomes; UP000002254; Chromosome 12.
DR Bgee; ENSCAFG00000000871; Expressed in granulocyte and 46 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_0000211179"
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 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..653
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..653
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 305
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; 88272 MW; B6BE990A1887F457 CRC64;
MLQNVTPHSK LPGEGNAGLL GLGPEAAAPG KRIRKPSLLY EGFESPTMAS VPALQLTPAN
PPPPEVSNPK KPGRVTNQLQ YLHKVVMKAL WKHQFAWPFR QPVDAVKLGL PDYHKIIKQP
MDMGTIKRRL ENNYYWAASE CMQDFNTMFT NCYIYNKPTD DIVLMAQTLE KIFLQKVASM
PQEEQELVVT IPKNSHKKGA KLAALQGSIT SAHQVPAVSS VSHTALYTPP PEIPTTVLNI
PHPSVISSPL LKSLHSAGPQ LLAVSAAPPA QPLAKKKGVK RKADTTTPTP TAILAPGSPA
SPPGSLEAKA ARLPPMRRES GRPIKPPRKD LPDSQQQHQS SKKGKLSEQL KHCNGILKEL
LSKKHAAYAW PFYKPVDASA LGLHDYHDII KHPMDLSTVK RKMENRDYRD AQEFAADVRL
MFSNCYKYNP PDHDVVAMAR KLQDVFEFRY AKMPDEPLEP GPLPVSTALP PGLAKSSSES
SSEESSSESS SEEDEEEDEE EEEEEEESES SDSEEERAHR LAELQEQLRA VHEQLAALSQ
GPISKPKRKR EKKEKKKKRK AEKHRGRAGV DEDDKGSRAP RPSQPKKSKK ASGSGGGSAA
TLGPPGFGPS GGSGTKLPKK ATKTAPPALP TGYDSEEEEE SRPMSYDEKR QLSLDINKLP
GEKLGRVVHI IQAREPSLRD SNPEEIEIDF ETLKPSTLRE LERYVLSCLR KKPRKPYTIK
KPVGKTKEEL ALEKKRELEK RLQDVSGQLN STKKPPKKAS EKTESSSTQQ VAVSRLSASS
SSSDSSSSSS SSSSSDTSDS DSG
