BAP60_DROME
ID BAP60_DROME Reviewed; 515 AA.
AC Q9VYG2; O76490;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Brahma-associated protein of 60 kDa;
DE AltName: Full=BRM-associated protein 60 {ECO:0000303|PubMed:9735357};
GN Name=Bap60; ORFNames=CG4303;
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;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC28455.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 57-75, IDENTIFICATION IN
RP THE BRAHMA COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=9735357; DOI=10.1242/dev.125.20.3955;
RA Papoulas O., Beek S.J., Moseley S.L., McCallum C.M., Sarte M., Shearn A.,
RA Tamkun J.W.;
RT "The Drosophila trithorax group proteins BRM, ASH1 and ASH2 are subunits of
RT distinct protein complexes.";
RL Development 125:3955-3966(1998).
RN [2] {ECO:0000312|EMBL:AAF48235.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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 [3] {ECO:0000312|EMBL:AAF48235.1}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
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 [4] {ECO:0000312|EMBL:AAL39528.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL39528.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
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 [5] {ECO:0000305}
RP INTERACTION WITH MOR.
RX PubMed=10809665;
RA Kal A.J., Mahmoudi T., Zak N.B., Verrijzer C.P.;
RT "The Drosophila brahma complex is an essential coactivator for the
RT trithorax group protein zeste.";
RL Genes Dev. 14:1058-1071(2000).
RN [6] {ECO:0000305}
RP IDENTIFICATION IN THE BRAHMA COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15060132; DOI=10.1128/mcb.24.8.3077-3088.2004;
RA Mohrmann L., Langenberg K., Krijgsveld J., Kal A.J., Heck A.J.,
RA Verrijzer C.P.;
RT "Differential targeting of two distinct SWI/SNF-related Drosophila
RT chromatin-remodeling complexes.";
RL Mol. Cell. Biol. 24:3077-3088(2004).
RN [7] {ECO:0000305}
RP FUNCTION, INTERACTION WITH SISA AND SC, DEVELOPMENTAL STAGE, DNA-BINDING,
RP AND MUTAGENESIS OF LYS-158; LYS-166 AND ARG-185.
RX PubMed=16083904; DOI=10.1016/j.jmb.2005.07.009;
RA Moller A., Avila F.W., Erickson J.W., Jackle H.;
RT "Drosophila BAP60 is an essential component of the Brahma complex, required
RT for gene activation and repression.";
RL J. Mol. Biol. 352:329-337(2005).
RN [8] {ECO:0000305}
RP INTERACTION WITH P53.
RX PubMed=20308539; DOI=10.1073/pnas.1002447107;
RA Lunardi A., Di Minin G., Provero P., Dal Ferro M., Carotti M., Del Sal G.,
RA Collavin L.;
RT "A genome-scale protein interaction profile of Drosophila p53 uncovers
RT additional nodes of the human p53 network.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:6322-6327(2010).
RN [9]
RP FUNCTION, INTERACTION WITH ERM, AND DISRUPTION PHENOTYPE.
RX PubMed=24618901; DOI=10.7554/elife.01906;
RA Koe C.T., Li S., Rossi F., Wong J.J., Wang Y., Zhang Z., Chen K., Aw S.S.,
RA Richardson H.E., Robson P., Sung W.K., Yu F., Gonzalez C., Wang H.;
RT "The Brm-HDAC3-Erm repressor complex suppresses dedifferentiation in
RT Drosophila type II neuroblast lineages.";
RL Elife 3:E01906-E01906(2014).
RN [10]
RP INTERACTION WITH AKIRIN.
RX PubMed=25180232; DOI=10.15252/embj.201488456;
RA Bonnay F., Nguyen X.H., Cohen-Berros E., Troxler L., Batsche E.,
RA Camonis J., Takeuchi O., Reichhart J.M., Matt N.;
RT "Akirin specifies NF-kappaB selectivity of Drosophila innate immune
RT response via chromatin remodeling.";
RL EMBO J. 33:2349-2362(2014).
CC -!- FUNCTION: Involved in the recruitment and site-specific anchoring of
CC the Brahma complex at specific promoter sites (PubMed:16083904,
CC PubMed:24618901). The Brahma complex is a multiprotein complex which is
CC the equivalent of the yeast SWI/SNF complex and acts by remodeling the
CC chromatin by catalyzing an ATP-dependent alteration in the structure of
CC nucleosomal DNA (PubMed:16083904, PubMed:24618901). This complex can
CC both serve as a transcriptional coactivator or corepressor, depending
CC on the context (PubMed:16083904). Participates in X-chromosomal dosage
CC compensation (PubMed:16083904). Participates in neurogenesis
CC (PubMed:16083904, PubMed:24618901). {ECO:0000269|PubMed:16083904,
CC ECO:0000269|PubMed:24618901}.
CC -!- SUBUNIT: There are 2 distinct Brahma complexes in the fruit fly, the
CC Brahma-associated proteins (BAP) and Polybromo-containing BAP (PBAP)
CC complexes, which are composed of common subunits Brm, Mor, Snr1/Bap45,
CC Bap111/Dalo, Bap55, Bap60 and Act42A/Bap47, and additional signature
CC subunits osa in the BAP complex and Polybromo and Bap170 in the PBAP
CC complex (PubMed:15060132). Interacts with sisA and sc
CC (PubMed:16083904). Interacts with mor (PubMed:10809665). Interacts with
CC p53 (PubMed:20308539). Interacts with erm (via N-terminal)
CC (PubMed:24618901). Interacts with akirin; interaction is immune
CC stimulation-dependent; activates selected Rel target gene promoters
CC (PubMed:25180232). {ECO:0000269|PubMed:10809665,
CC ECO:0000269|PubMed:15060132, ECO:0000269|PubMed:16083904,
CC ECO:0000269|PubMed:20308539, ECO:0000269|PubMed:24618901,
CC ECO:0000269|PubMed:25180232, ECO:0000269|PubMed:9735357}.
CC -!- INTERACTION:
CC Q9VYG2; Q9VS59: akirin; NbExp=4; IntAct=EBI-75169, EBI-96644;
CC Q9VYG2; O96757: stumps; NbExp=3; IntAct=EBI-75169, EBI-74922;
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Maternal expression is uniform at the blastoderm stage. Zygotic
CC expression becomes predominant at the extended band stage. After germ
CC band retraction, expression is restricted to the ventral nerve chord
CC and the brain. {ECO:0000269|PubMed:16083904}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in ectopic
CC expression of type II neuroblast lineages in larval brains.
CC {ECO:0000269|PubMed:24618901}.
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DR EMBL; AF071503; AAC28455.1; -; mRNA.
DR EMBL; AE014298; AAF48235.1; -; Genomic_DNA.
DR EMBL; AY069383; AAL39528.1; -; mRNA.
DR RefSeq; NP_511143.2; NM_078588.4.
DR AlphaFoldDB; Q9VYG2; -.
DR SMR; Q9VYG2; -.
DR BioGRID; 58653; 141.
DR IntAct; Q9VYG2; 17.
DR MINT; Q9VYG2; -.
DR STRING; 7227.FBpp0073572; -.
DR PaxDb; Q9VYG2; -.
DR PRIDE; Q9VYG2; -.
DR EnsemblMetazoa; FBtr0073741; FBpp0073572; FBgn0025463.
DR GeneID; 32268; -.
DR KEGG; dme:Dmel_CG4303; -.
DR UCSC; CG4303-RA; d. melanogaster.
DR CTD; 32268; -.
DR FlyBase; FBgn0025463; Bap60.
DR VEuPathDB; VectorBase:FBgn0025463; -.
DR eggNOG; KOG2570; Eukaryota.
DR GeneTree; ENSGT00940000156629; -.
DR HOGENOM; CLU_023529_0_2_1; -.
DR InParanoid; Q9VYG2; -.
DR OMA; PYFWNSD; -.
DR OrthoDB; 1027566at2759; -.
DR PhylomeDB; Q9VYG2; -.
DR Reactome; R-DME-3214858; RMTs methylate histone arginines.
DR Reactome; R-DME-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-DME-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-DME-9707564; Cytoprotection by HMOX1.
DR SignaLink; Q9VYG2; -.
DR BioGRID-ORCS; 32268; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Bap60; fly.
DR GenomeRNAi; 32268; -.
DR PRO; PR:Q9VYG2; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0025463; Expressed in secondary oocyte and 55 other tissues.
DR Genevisible; Q9VYG2; DM.
DR GO; GO:0035060; C:brahma complex; IDA:FlyBase.
DR GO; GO:0000791; C:euchromatin; IDA:FlyBase.
DR GO; GO:0071565; C:nBAF complex; IEA:InterPro.
DR GO; GO:0071564; C:npBAF complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0016514; C:SWI/SNF complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:FlyBase.
DR GO; GO:0017022; F:myosin binding; IPI:FlyBase.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:FlyBase.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0008134; F:transcription factor binding; ISS:FlyBase.
DR GO; GO:0007406; P:negative regulation of neuroblast proliferation; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:FlyBase.
DR GO; GO:0031453; P:positive regulation of heterochromatin assembly; IMP:FlyBase.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR Gene3D; 1.10.245.10; -; 1.
DR InterPro; IPR038041; SMARCD1.
DR InterPro; IPR019835; SWIB_domain.
DR InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR InterPro; IPR003121; SWIB_MDM2_domain.
DR PANTHER; PTHR13844:SF1; PTHR13844:SF1; 1.
DR Pfam; PF02201; SWIB; 1.
DR SMART; SM00151; SWIB; 1.
DR SUPFAM; SSF47592; SSF47592; 1.
DR PROSITE; PS51925; SWIB_MDM2; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Direct protein sequencing; DNA-binding;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..515
FT /note="Brahma-associated protein of 60 kDa"
FT /id="PRO_0000421980"
FT DOMAIN 291..368
FT /note="SWIB/MDM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01273"
FT REGION 1..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..204
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:16083904"
FT COMPBIAS 13..44
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 158
FT /note="K->A: Loss of DNA-binding. Does not affect function
FT in vivo; when associated with A-166 and A-185."
FT /evidence="ECO:0000269|PubMed:16083904"
FT MUTAGEN 166
FT /note="K->A: Loss of DNA-binding. Does not affect function
FT in vivo; when associated with A-158 and A-185."
FT /evidence="ECO:0000269|PubMed:16083904"
FT MUTAGEN 185
FT /note="R->A: Loss of DNA-binding. Does not affect function
FT in vivo; when associated with A-158 and A-166."
FT /evidence="ECO:0000269|PubMed:16083904"
FT CONFLICT 435
FT /note="K -> N (in Ref. 1; AAC28455)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 515 AA; 58170 MW; C7823B09A2DBDF2C CRC64;
MSQRFAPGQA PVQSRYQPPP PAPGMRPYPP PGASFPPRGF PLHPNTTQPV PGTANVAGVP
GVPGVPGVPG PSLLQRAAQQ PGFQSSLRGT GAGGGGVGSG GGSKRSNESR SLGGGGSKSD
FATAKKKKKL AEKILPQKVR DLVPESQAYM DLLTFERKLD ATIMRKRLDI QEALKRPMKQ
KRKLRIFISN TFYPSKEPTN DGEEGAVASW ELRVEGRLLE DGKGDPNTKI KRKFSSFFKS
LVIELDKELY GPDNHLVEWH RTHTTQETDG FQVKRPGDRN VRCTILLLLD YQPLQFKLDP
RLARLLGVHT QTRPVIISAL WQYIKTHKLQ DAHEREYINC DKYLEQIFSC QRMKFAEIPQ
RLNPLLHPPD PIVINHFIES GAENKQTACY DIDVEVDDTL KNQMNSFLMS TASQQEIQGL
DTKIHETVDT INQMKTNREF FLSFAKDPQM FIHRWIISET RDLKLMTDVA GNPEEERRAE
FYYQPWTHEA VSRYFFTKVN QKRAELEQAL GIRNG
