BRD9_MOUSE
ID BRD9_MOUSE Reviewed; 596 AA.
AC Q3UQU0; Q0P669; Q5FWH1; Q811F7;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Bromodomain-containing protein 9;
GN Name=Brd9;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N, and NMRI; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP IDENTIFICATION IN THE GBAF COMPLEX, AND INTERACTION WITH BRD4.
RX PubMed=29374058; DOI=10.1074/jbc.ra117.001065;
RA Alpsoy A., Dykhuizen E.C.;
RT "Glioma tumor suppressor candidate region gene 1 (GLTSCR1) and its paralog
RT GLTSCR1-like form SWI/SNF chromatin remodeling subcomplexes.";
RL J. Biol. Chem. 293:3892-3903(2018).
CC -!- FUNCTION: Plays a role in chromatin remodeling and regulation of
CC transcription. Acts as a chromatin reader that recognizes and binds
CC acylated histones: binds histones that are acetylated and/or
CC butyrylated. Component of SWI/SNF chromatin remodeling subcomplex GBAF
CC that carries out key enzymatic activities, changing chromatin structure
CC by altering DNA-histone contacts within a nucleosome in an ATP-
CC dependent manner. Orchestrates also the RAD51-RAD54 complex formation
CC and thereby plays a role in homologous recombination (HR).
CC {ECO:0000250|UniProtKB:Q9H8M2}.
CC -!- SUBUNIT: Binds acetylated histones H3 and H4. Binds butyrylated histone
CC H4 (By similarity). Component of the multiprotein chromatin-remodeling
CC subcomplex SWI/SNF called GBAF, which includes at least BICRA or BICRAL
CC (mutually exclusive), BRD9, SS18, the core BAF subunits, SMARCA2/BRM,
CC SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, SMARCC1/BAF155, and SMARCD1/BAF60A
CC (PubMed:29374058). Interacts (via N-terminal bromodomain) with
CC acteylated RAD54. Interacts (via C-terminus) with RAD51 (By
CC similarity). {ECO:0000250|UniProtKB:Q9H8M2,
CC ECO:0000269|PubMed:29374058}.
CC -!- DOMAIN: The Bromo domain mediates interaction with histones that have
CC acetylated lysine residues at specific positions. Also recognizes and
CC binds histones that are butyrylated. {ECO:0000250|UniProtKB:Q9H8M2}.
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DR EMBL; AK142152; BAE24949.1; -; mRNA.
DR EMBL; BC031484; AAH31484.1; -; mRNA.
DR EMBL; BC046438; AAH46438.1; -; mRNA.
DR CCDS; CCDS88482.1; -.
DR RefSeq; NP_001019679.2; NM_001024508.3.
DR RefSeq; NP_001294970.1; NM_001308041.1.
DR AlphaFoldDB; Q3UQU0; -.
DR SMR; Q3UQU0; -.
DR BioGRID; 222796; 5.
DR ComplexPortal; CPX-4202; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA2 variant.
DR ComplexPortal; CPX-4204; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA2 variant.
DR ComplexPortal; CPX-4221; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA4 variant.
DR ComplexPortal; CPX-4222; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA4 variant.
DR ComplexPortal; CPX-4227; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA2 variant.
DR ComplexPortal; CPX-4228; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA2 variant.
DR ComplexPortal; CPX-4229; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA4 variant.
DR ComplexPortal; CPX-4230; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA4 variant.
DR IntAct; Q3UQU0; 1.
DR STRING; 10090.ENSMUSP00000096982; -.
DR BindingDB; Q3UQU0; -.
DR ChEMBL; CHEMBL3822347; -.
DR iPTMnet; Q3UQU0; -.
DR PhosphoSitePlus; Q3UQU0; -.
DR EPD; Q3UQU0; -.
DR jPOST; Q3UQU0; -.
DR MaxQB; Q3UQU0; -.
DR PaxDb; Q3UQU0; -.
DR PeptideAtlas; Q3UQU0; -.
DR PRIDE; Q3UQU0; -.
DR ProteomicsDB; 273762; -.
DR Antibodypedia; 8843; 163 antibodies from 26 providers.
DR Ensembl; ENSMUST00000222399; ENSMUSP00000152390; ENSMUSG00000057649.
DR GeneID; 105246; -.
DR KEGG; mmu:105246; -.
DR UCSC; uc007rej.1; mouse.
DR CTD; 65980; -.
DR MGI; MGI:2145317; Brd9.
DR VEuPathDB; HostDB:ENSMUSG00000057649; -.
DR eggNOG; KOG1828; Eukaryota.
DR GeneTree; ENSGT00950000183170; -.
DR InParanoid; Q3UQU0; -.
DR OrthoDB; 439339at2759; -.
DR PhylomeDB; Q3UQU0; -.
DR TreeFam; TF106439; -.
DR BioGRID-ORCS; 105246; 19 hits in 76 CRISPR screens.
DR ChiTaRS; Brd9; mouse.
DR PRO; PR:Q3UQU0; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q3UQU0; protein.
DR Bgee; ENSMUSG00000057649; Expressed in floor plate of midbrain and 238 other tissues.
DR ExpressionAtlas; Q3UQU0; baseline and differential.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0140288; C:GBAF complex; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016514; C:SWI/SNF complex; IDA:UniProtKB.
DR GO; GO:0070577; F:lysine-acetylated histone binding; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
DR GO; GO:0045596; P:negative regulation of cell differentiation; IC:ComplexPortal.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IC:ComplexPortal.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.20.920.10; -; 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR021900; DUF3512.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF12024; DUF3512; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Bromodomain; Chromatin regulator; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..596
FT /note="Bromodomain-containing protein 9"
FT /id="PRO_0000239220"
FT DOMAIN 153..223
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 38..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..216
FT /note="Histone H4K5ac H4K8ac and histone H4K5bu H4K8bu
FT binding"
FT /evidence="ECO:0000250|UniProtKB:Q9H8M2"
FT REGION 536..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 169
FT /note="Histone H4K5ac H4K8ac and histone H4K5bu H4K8bu
FT binding"
FT /evidence="ECO:0000250|UniProtKB:Q9H8M2"
FT SITE 222
FT /note="Histone H4K5ac H4K8ac and histone H4K5bu H4K8bu
FT binding"
FT /evidence="ECO:0000250|UniProtKB:Q9H8M2"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 372
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9H8M2"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8M2"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8M2"
FT CROSSLNK 372
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9H8M2"
FT CONFLICT 239
FT /note="K -> KQ (in Ref. 2; AAH31484)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 596 AA; 66840 MW; CC7DEEBEBF47F5DE CRC64;
MGKKHKKHKA EWRSSYEDYT DTPLEKPLKL VLKVGGSEVT ELSGSGHDSS YYDDRSDHER
ERHREKKKKK KKKSEKEKHL DEEERRKRKE EKKRKREKEH CDSEGEADAF DPGKKVEVEP
PPDRPVRACR TQPAENESTP IQRLLEHFLR QLQRKDPHGF FAFPVTDAIA PGYSMIIKHP
MDFGTMKDKI VANEYKSVTE FKADFKLMCD NAMTYNRPDT VYYKLAKKIL HAGFKMMSKA
ALLGSEDPAA EEPVPEVVPV QVETTKKSKK PSREVISCMF EPEGNACSLT DSTAEEHVLA
LVEHAADEAR DRINRFLPGG KMGYLKKLGD GSLLYSVVNA PEPDADEEET HPVDLSSLSS
KLLPGFTTLG FKDERRNKVT FLSSASTALS MQNNSVFGDL KSDEMELLYS AYGDETGVQC
ALSLQEFVKD AGSYSKKMVD DLLDQITGGD HSRMIFQLKQ RRSIPMRPAD EMKVGDPLGE
SGGPVLDFMS MKQYPDVSLD VSMLSSLGKV KKELDHEDSH LNLDETARLL QDLHEAQAER
GGSRPSSNLS SLSTASEREH PPPGSPSRLS VGEQPDVAHD PYEFLQSPEP AAPAKN
