BRD2_RAT
ID BRD2_RAT Reviewed; 798 AA.
AC Q6MGA9;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Bromodomain-containing protein 2;
DE AltName: Full=Protein RING3;
GN Name=Brd2; Synonyms=Ring3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15060004; DOI=10.1101/gr.1987704;
RA Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H.,
RA Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
RT "The genomic sequence and comparative analysis of the rat major
RT histocompatibility complex.";
RL Genome Res. 14:631-639(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297 AND SER-631, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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}.
CC -!- DOMAIN: One bromodomain is sufficient for a partial interaction with
CC histone H4 acetylated at 'Lys-13'. {ECO:0000250}.
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DR EMBL; BX883042; CAE83937.1; -; Genomic_DNA.
DR RefSeq; NP_997660.1; NM_212495.1.
DR RefSeq; XP_017443518.1; XM_017588029.1.
DR RefSeq; XP_017457067.1; XM_017601578.1.
DR RefSeq; XP_017457068.1; XM_017601579.1.
DR RefSeq; XP_017457351.1; XM_017601862.1.
DR AlphaFoldDB; Q6MGA9; -.
DR SMR; Q6MGA9; -.
DR STRING; 10116.ENSRNOP00000000535; -.
DR iPTMnet; Q6MGA9; -.
DR PhosphoSitePlus; Q6MGA9; -.
DR PaxDb; Q6MGA9; -.
DR PRIDE; Q6MGA9; -.
DR Ensembl; ENSRNOT00000000535; ENSRNOP00000000535; ENSRNOG00000000461.
DR GeneID; 294276; -.
DR KEGG; rno:294276; -.
DR UCSC; RGD:1303324; rat.
DR CTD; 6046; -.
DR RGD; 1303324; Brd2.
DR eggNOG; KOG1474; Eukaryota.
DR GeneTree; ENSGT00940000153385; -.
DR HOGENOM; CLU_001499_0_4_1; -.
DR InParanoid; Q6MGA9; -.
DR OMA; MNIPHYP; -.
DR OrthoDB; 619848at2759; -.
DR PhylomeDB; Q6MGA9; -.
DR TreeFam; TF317345; -.
DR Reactome; R-RNO-8951936; RUNX3 regulates p14-ARF.
DR PRO; PR:Q6MGA9; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000461; Expressed in testis and 19 other tissues.
DR ExpressionAtlas; Q6MGA9; baseline and differential.
DR Genevisible; Q6MGA9; RN.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0001843; P:neural tube closure; ISO:RGD.
DR GO; GO:0006334; P:nucleosome assembly; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; Bromodomain; Chromatin regulator; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT CHAIN 1..798
FT /note="Bromodomain-containing protein 2"
FT /id="PRO_0000274006"
FT DOMAIN 90..162
FT /note="Bromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 363..435
FT /note="Bromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 630..712
FT /note="NET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00857"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 553..557
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 311..335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..509
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..524
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..561
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..578
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..648
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..798
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 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25440"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25440"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25440"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 798 AA; 88051 MW; A6A530A04AB12EC9 CRC64;
MLQNVTPHKL PGEGNAGLLG LGPEAAAPGK RIRKPSLLYE GFESPTMASV PALQLAPANP
PPPEVSNPKK PGRVTNQLQY LHKVVMKALW KHQFAWPFRQ PVDAVKLGLP DYHKIIKQPM
DMGTIKRRLE NNYYWAASEC MQDFNTMFTN CYIYNKPTDD IVLMAQTLEK IFLQKVASMP
QEEQELVVTI PKNSHKKGAK LAALQGSITS AHQVPAVSSV SHTALYTPPP EIPTTVLNIP
HPSVISSPLL KSLHSAGPPL LAVSAAPPAQ PLAKKKGVKR KADTTTPTPT AILAPGSPAS
PPGSLEPKAA RLPPMRRESG RPIKPPRKDL PDSQQQHQSS KKGKLSEQLK HCNGILKELL
SKKHAAYAWP FYKPVDASAL GLHDYHDIIK HPMDLSTVKR KMENRDYRDA QEFAADVRLM
FSNCYKYNPP DHDVVAMARK LQDVFEFRYA KMPDEPLEPG PLPVSTALPP GLAKSSSESS
SEESSSESSS EEEEEEDEED EEEESESSDS EEERAHRLAE LQEQLRAVHE QLAALSQGPI
SKPKRKREKK EKKKKRKAEK HRGRIGIDED DKGPRAPRPL QPKKSKKAGG GGSNATTLSH
PGFGTSAGSS NKLPKKAQKT APPVLPTGYD SEEEEESRPM SYDEKRQLSL DINKLPGEKL
GRVVHIIQAR EPSLRDSNPE EIEIDFETLK PSTLRELERY VLSCLRKKPR KPYTIRKPVG
KTKEELALEK KRELEKRLQD VSGQLNSTKK PPKKASEKTE SSAQQVAVSR LSASSSSSDS
SSSSSSSSSS DTSDSDSG
