BRDH_DROME
ID BRDH_DROME Reviewed; 1430 AA.
AC Q7JVP4;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Bromodomain-containing protein homolog {ECO:0000305};
DE AltName: Full=Protein Br140 {ECO:0000305};
GN Name=Br140 {ECO:0000312|FlyBase:FBgn0033155};
GN ORFNames=CG1845 {ECO:0000312|FlyBase:FBgn0033155};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAM50638.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM50638.1};
RC TISSUE=Head {ECO:0000312|EMBL:AAM50638.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE ENOK COMPLEX, INTERACTION WITH ELG1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=27198229; DOI=10.1101/gad.271429.115;
RA Huang F., Saraf A., Florens L., Kusch T., Swanson S.K., Szerszen L.T.,
RA Li G., Dutta A., Washburn M.P., Abmayr S.M., Workman J.L.;
RT "The Enok acetyltransferase complex interacts with Elg1 and negatively
RT regulates PCNA unloading to promote the G1/S transition.";
RL Genes Dev. 30:1198-1210(2016).
CC -!- FUNCTION: Scaffold subunit of the histone acetyltransferase (HAT) Enok
CC complex which has histone H3 acetyltransferase activity
CC (PubMed:27198229). As part of the Enok complex, associates with the
CC Elg1 RFC-like complex and down-regulates its PCNA-unloading function to
CC promote the G1/S transition (PubMed:27198229). May also play a role in
CC maintaining the protein levels and stability of enok (PubMed:27198229).
CC {ECO:0000269|PubMed:27198229}.
CC -!- SUBUNIT: Component of the Enok complex composed of at least Br140,
CC enok, Eaf6 and Ing5 (PubMed:27198229). As part of the Enok complex,
CC interacts with elg1 and the Elg1 RFC-like complex (PubMed:27198229).
CC {ECO:0000269|PubMed:27198229}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27198229}.
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DR EMBL; AE013599; AAF59276.1; -; Genomic_DNA.
DR EMBL; AE013599; AHN55953.1; -; Genomic_DNA.
DR EMBL; AY118778; AAM50638.1; -; mRNA.
DR RefSeq; NP_001286155.1; NM_001299226.1.
DR RefSeq; NP_610266.1; NM_136422.3.
DR SMR; Q7JVP4; -.
DR IntAct; Q7JVP4; 2.
DR STRING; 7227.FBpp0088092; -.
DR PRIDE; Q7JVP4; -.
DR EnsemblMetazoa; FBtr0089021; FBpp0088092; FBgn0033155.
DR EnsemblMetazoa; FBtr0345370; FBpp0311524; FBgn0033155.
DR GeneID; 35648; -.
DR KEGG; dme:Dmel_CG1845; -.
DR UCSC; CG1845-RA; d. melanogaster.
DR CTD; 35648; -.
DR FlyBase; FBgn0033155; Br140.
DR VEuPathDB; VectorBase:FBgn0033155; -.
DR eggNOG; KOG0955; Eukaryota.
DR GeneTree; ENSGT00940000169333; -.
DR HOGENOM; CLU_003589_1_0_1; -.
DR OMA; RDCDRSY; -.
DR OrthoDB; 566217at2759; -.
DR Reactome; R-DME-114608; Platelet degranulation.
DR Reactome; R-DME-6804758; Regulation of TP53 Activity through Acetylation.
DR BioGRID-ORCS; 35648; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 35648; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0033155; Expressed in cleaving embryo and 27 other tissues.
DR GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; IDA:FlyBase.
DR GO; GO:0010698; F:acetyltransferase activator activity; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:FlyBase.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd05839; BR140_related; 1.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR035502; BR140-rel_PWWD.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR019542; Enhancer_polycomb-like_N.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR013087; Znf_C2H2_type.
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 Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF10513; EPL1; 1.
DR Pfam; PF00855; PWWP; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS50812; PWWP; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Bromodomain; Metal-binding; Nucleus; Reference proteome; Repeat; Zinc;
KW Zinc-finger.
FT CHAIN 1..1430
FT /note="Bromodomain-containing protein homolog"
FT /id="PRO_0000455977"
FT DOMAIN 628..698
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 1305..1378
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT ZN_FING 23..49
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 283..333
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 337..370
FT /note="C2HC pre-PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 394..457
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 289
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 311
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 314
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 327
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
SQ SEQUENCE 1430 AA; 157119 MW; 716E23E1DB987DFD CRC64;
MGLDFDAVEY CKGVKTQQSQ PPFACPVRGC DRSYKTIMGL QYHLMKYDHD NPQPLTPVLT
PSRKKARSRS GGHHSTPRPH KDHPTPGGGG AEARNGCSSA SAGGGSASGV SARQYANPES
LVSYNEEEAT VTFNLDGKSV RLGIDDALPL VEDEEFAALV ARGCILNADA PPLEENAPWA
RVQVPVARVA EIPDYRVSDA PPRPLAYYRF IEKSLEELDG EVEYDVDEED SAWLEHMNEE
RQRLGLNAVG IDTMELLMDR LEKESHFQAA ANGTPTGVEV DDDAVCCICL DGECQNTNVI
LFCDMCNLAV HQDCYGVPYI PEGQWLCRRC LQSPSKPVNC VLCPNAGGAF KQTDHGQWAH
VVCALWIPEV RFANTVFLEP IDSIETIPPA RWRLTCYVCK EKGLGACIQC HRNSCYAAFH
VTCAQQAGLY MTMDTVKDGH NDSSMHVQKF AYCHAHTPAD AKLKMNVPDF EDTRHKMKEA
RKALAKKRST APVVLIPTIP PDRVQEIATM VTMQRKKEFL DRIIAYWTLK RHYRNGVPLL
RRLQSQGNNH GVIQRNGIEG SPDTGELYRQ LKYWQCLRQD LERARLLCEL VRKREKLKVA
FVRISEEVVM LQLNPLEAAL NKLLDALEAR DSMQIFREPV DTSEVPDYTD IVKQPMDLGT
MRAKLKECQY NSLEQLEADF DLMIQNCLAY NNKDTVFYRA GIRMRDQAAP LFVQVRKELQ
RDGLLARSQR YHVDHVEAEV EQELRLLLAA PASEGIVQKL LILADKSQVL KNPTYRTKKI
KQIRLEISRM RKSLQKARFA ARHSSHANQS QSDDEDTLGG SPSKKRTRKR FNSSGVDMEL
GHDDDDEEED SDEDSMGEDT VSKDLLNSTQ TPPCSPIKSL NNSSSPVGIN RRTAILLTRK
AQAALKRPSE PLTTPVKEEQ HNSQSSNTQS TSGSSSSVTT AATAASSGAG TLNHVLSSAP
PTASSFALTQ NNSSGGGALA SGTGIGGSSS AGTAAAASLT STALAMNSKL SANLPVKSPK
RPGRYRRVPE VRHSSSMSPK KSPNPAVTVS QALPMPETLP FERIPDSFRV YRANNQRDVS
DSDDAPSQSS SPCSSCSDFS MSGSCSDFDS DEASEGDADG DPDRDGGRSR SEERDSTSQE
GTTDAMDMQH ASLNNVQGNN GNMAISSSSG GSGGSSSEDD ELEERPLSAR QNKPMKVGTR
GTPTPTTMAR AVALSAGRGR GKRRSNLSES TSSTATPPPL RRAGKLRSAT PNASPLVNNI
KARRNTTAAG SAPLTNNNRS KHSEDSASSE RHNNHSHGQK PALEPLQLVW AKCRGYPWYP
ALILDPKTPK GFVYNGVPLP APPTDVLALR KNCLDEIVFL VLFFDVKRTW QWLPANKLDI
LGIDKQLDQQ KLVESRKPAE RKAVKKAYQD ALHYQSQVSD LEGQGPDPIM
