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Brahma-associated protein of 60 kDa (BRM-associated protein 60)

 BAP60_DROME             Reviewed;         515 AA.
Q9VYG2; O76490;
03-APR-2013, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
18-JUL-2018, entry version 139.
RecName: Full=Brahma-associated protein of 60 kDa;
AltName: Full=BRM-associated protein 60 {ECO:0000303|PubMed:9735357};
Name=Bap60; ORFNames=CG4303;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1] {ECO:0000305, ECO:0000312|EMBL:AAC28455.1}
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 57-75, IDENTIFICATION
IN THE BRAHMA COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=9735357;
Papoulas O., Beek S.J., Moseley S.L., McCallum C.M., Sarte M.,
Shearn A., Tamkun J.W.;
"The Drosophila trithorax group proteins BRM, ASH1 and ASH2 are
subunits of distinct protein complexes.";
Development 125:3955-3966(1998).
[2] {ECO:0000312|EMBL:AAF48235.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3] {ECO:0000312|EMBL:AAF48235.1}
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4] {ECO:0000312|EMBL:AAL39528.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley {ECO:0000312|EMBL:AAL39528.1};
TISSUE=Embryo {ECO:0000269|PubMed:12537569};
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5] {ECO:0000305}
INTERACTION WITH MOR.
PubMed=10809665;
Kal A.J., Mahmoudi T., Zak N.B., Verrijzer C.P.;
"The Drosophila brahma complex is an essential coactivator for the
trithorax group protein zeste.";
Genes Dev. 14:1058-1071(2000).
[6] {ECO:0000305}
IDENTIFICATION IN THE BRAHMA COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=15060132; DOI=10.1128/MCB.24.8.3077-3088.2004;
Mohrmann L., Langenberg K., Krijgsveld J., Kal A.J., Heck A.J.,
Verrijzer C.P.;
"Differential targeting of two distinct SWI/SNF-related Drosophila
chromatin-remodeling complexes.";
Mol. Cell. Biol. 24:3077-3088(2004).
[7] {ECO:0000305}
FUNCTION, INTERACTION WITH SISA AND SC, DEVELOPMENTAL STAGE,
DNA-BINDING, AND MUTAGENESIS OF LYS-158; LYS-166 AND ARG-185.
PubMed=16083904; DOI=10.1016/j.jmb.2005.07.009;
Moller A., Avila F.W., Erickson J.W., Jackle H.;
"Drosophila BAP60 is an essential component of the Brahma complex,
required for gene activation and repression.";
J. Mol. Biol. 352:329-337(2005).
[8] {ECO:0000305}
INTERACTION WITH P53.
PubMed=20308539; DOI=10.1073/pnas.1002447107;
Lunardi A., Di Minin G., Provero P., Dal Ferro M., Carotti M.,
Del Sal G., Collavin L.;
"A genome-scale protein interaction profile of Drosophila p53 uncovers
additional nodes of the human p53 network.";
Proc. Natl. Acad. Sci. U.S.A. 107:6322-6327(2010).
[9]
FUNCTION, INTERACTION WITH ERM, AND DISRUPTION PHENOTYPE.
PubMed=24618901; DOI=10.7554/eLife.01906.001;
Koe C.T., Li S., Rossi F., Wong J.J., Wang Y., Zhang Z., Chen K.,
Aw S.S., Richardson H.E., Robson P., Sung W.K., Yu F., Gonzalez C.,
Wang H.;
"The Brm-HDAC3-Erm repressor complex suppresses dedifferentiation in
Drosophila type II neuroblast lineages.";
Elife 3:E01906-E01906(2014).
-!- FUNCTION: Involved in the recruitment and site-specific anchoring
of the Brahma complex at specific promoter sites (PubMed:16083904,
PubMed:24618901). The Brahma complex is a multiprotein complex
which is the equivalent of the yeast SWI/SNF complex and acts by
remodeling the chromatin by catalyzing an ATP-dependent alteration
in the structure of nucleosomal DNA (PubMed:16083904,
PubMed:24618901). This complex can both serve as a transcriptional
coactivator or corepressor, depending on the context
(PubMed:16083904). Participates in X-chromosomal dosage
compensation (PubMed:16083904). Participates in neurogenesis
(PubMed:16083904, PubMed:24618901). {ECO:0000269|PubMed:16083904,
ECO:0000269|PubMed:24618901}.
-!- SUBUNIT: There are 2 distinct Brahma complexes in the fruit fly,
the Brahma-associated proteins (BAP) and Polybromo-containing BAP
(PBAP) complexes, which are composed of common subunits Brm, Mor,
Snr1/Bap45, Bap111/Dalo, Bap55, Bap60 and Act42A/Bap47, and
additional signature subunits osa in the BAP complex and Polybromo
and Bap170 in the PBAP complex (PubMed:15060132). Interacts with
sisA and sc (PubMed:16083904). Interacts with mor
(PubMed:10809665). Interacts with p53 (PubMed:20308539). Interacts
with erm (via N-terminal) (PubMed:24618901).
{ECO:0000269|PubMed:10809665, ECO:0000269|PubMed:15060132,
ECO:0000269|PubMed:16083904, ECO:0000269|PubMed:20308539,
ECO:0000269|PubMed:24618901, ECO:0000269|PubMed:9735357}.
-!- INTERACTION:
Q9VS59:akirin; NbExp=5; IntAct=EBI-75169, EBI-96644;
O96757:stumps; NbExp=3; IntAct=EBI-75169, EBI-74922;
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
Maternal expression is uniform at the blastoderm stage. Zygotic
expression becomes predominant at the extended band stage. After
germ band retraction, expression is restricted to the ventral
nerve chord and the brain. {ECO:0000269|PubMed:16083904}.
-!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in ectopic
expression of type II neuroblast lineages in larval brains.
{ECO:0000269|PubMed:24618901}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF071503; AAC28455.1; -; mRNA.
EMBL; AE014298; AAF48235.1; -; Genomic_DNA.
EMBL; AY069383; AAL39528.1; -; mRNA.
RefSeq; NP_511143.2; NM_078588.4.
UniGene; Dm.2154; -.
ProteinModelPortal; Q9VYG2; -.
SMR; Q9VYG2; -.
BioGrid; 58653; 134.
IntAct; Q9VYG2; 92.
MINT; Q9VYG2; -.
STRING; 7227.FBpp0073572; -.
PaxDb; Q9VYG2; -.
PRIDE; Q9VYG2; -.
EnsemblMetazoa; FBtr0073741; FBpp0073572; FBgn0025463.
GeneID; 32268; -.
KEGG; dme:Dmel_CG4303; -.
UCSC; CG4303-RA; d. melanogaster.
CTD; 32268; -.
FlyBase; FBgn0025463; Bap60.
eggNOG; KOG2570; Eukaryota.
eggNOG; COG5531; LUCA.
GeneTree; ENSGT00390000017809; -.
InParanoid; Q9VYG2; -.
KO; K11650; -.
OMA; FRLPWVE; -.
OrthoDB; EOG091G06WW; -.
PhylomeDB; Q9VYG2; -.
Reactome; R-DME-3214858; RMTs methylate histone arginines.
Reactome; R-DME-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
ChiTaRS; Bap60; fly.
GenomeRNAi; 32268; -.
PRO; PR:Q9VYG2; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0025463; -.
Genevisible; Q9VYG2; DM.
GO; GO:0035060; C:brahma complex; IDA:FlyBase.
GO; GO:0071565; C:nBAF complex; IEA:InterPro.
GO; GO:0071564; C:npBAF complex; IEA:InterPro.
GO; GO:0005719; C:nuclear euchromatin; IDA:FlyBase.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0016586; C:RSC-type complex; IDA:FlyBase.
GO; GO:0016514; C:SWI/SNF complex; IEA:InterPro.
GO; GO:0003677; F:DNA binding; IDA:FlyBase.
GO; GO:0017022; F:myosin binding; IPI:FlyBase.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; IPI:FlyBase.
GO; GO:0008134; F:transcription factor binding; ISS:FlyBase.
GO; GO:0007406; P:negative regulation of neuroblast proliferation; IMP:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IGI:FlyBase.
GO; GO:0031453; P:positive regulation of heterochromatin assembly; IMP:FlyBase.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:GOC.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:FlyBase.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:FlyBase.
GO; GO:0006366; P:transcription by RNA polymerase II; IEA:GOC.
Gene3D; 1.10.245.10; -; 1.
InterPro; IPR038041; SMARCD1.
InterPro; IPR019835; SWIB_domain.
InterPro; IPR036885; SWIB_MDM2_dom_sf.
InterPro; IPR003121; SWIB_MDM2_domain.
PANTHER; PTHR13844:SF1; PTHR13844:SF1; 1.
Pfam; PF02201; SWIB; 1.
SMART; SM00151; SWIB; 1.
SUPFAM; SSF47592; SSF47592; 1.
1: Evidence at protein level;
Complete proteome; Developmental protein; Direct protein sequencing;
DNA-binding; Phosphoprotein; Reference proteome; Transcription;
Transcription regulation.
CHAIN 1 515 Brahma-associated protein of 60 kDa.
/FTId=PRO_0000421980.
DOMAIN 294 366 SWIB. {ECO:0000255}.
REGION 116 204 DNA-binding.
{ECO:0000269|PubMed:16083904}.
MUTAGEN 158 158 K->A: Loss of DNA-binding. Does not
affect function in vivo; when associated
with A-166 and A-185.
{ECO:0000269|PubMed:16083904}.
MUTAGEN 166 166 K->A: Loss of DNA-binding. Does not
affect function in vivo; when associated
with A-158 and A-185.
{ECO:0000269|PubMed:16083904}.
MUTAGEN 185 185 R->A: Loss of DNA-binding. Does not
affect function in vivo; when associated
with A-158 and A-166.
{ECO:0000269|PubMed:16083904}.
CONFLICT 435 435 K -> N (in Ref. 1; AAC28455).
{ECO:0000305}.
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


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