BRMS1_MOUSE
ID BRMS1_MOUSE Reviewed; 246 AA.
AC Q99N20;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Breast cancer metastasis-suppressor 1 homolog;
GN Name=Brms1;
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 [MRNA].
RC STRAIN=BALB/cJ;
RA Samant R.S., Debies M.T., Welch D.R.;
RT "Brms1: murine homolog of human breast metastasis suppressor gene-1
RT (BRMS1).";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=11774238; DOI=10.1002/ijc.1569;
RA Samant R.S., Debies M.T., Shevde L.A., Verderame M.F., Welch D.R.;
RT "Identification and characterization of the murine ortholog (brms1) of
RT breast-cancer metastasis suppressor 1 (BRMS1).";
RL Int. J. Cancer 97:15-20(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary 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).
CC -!- FUNCTION: Transcriptional repressor. Down-regulates transcription
CC activation by NF-kappa-B by promoting the deacetylation of RELA at
CC 'Lys-310'. Promotes HDAC1 binding to promoter regions. Down-regulates
CC expression of anti-apoptotic genes that are controlled by NF-kappa-B.
CC Promotes apoptosis in cells that have inadequate adherence to a
CC substrate, a process called anoikis, and may thereby inhibit metastasis
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homohexamer (Potential). Interacts with SNX6, HDAC1 and RELA.
CC Interacts with ARID4A. Identified in mSin3A corepressor complexes
CC together with SIN3A, SIN3B, RBBP4, RBBP7, SAP30, SUDS3, ARID4A, HDAC1
CC and HDAC2. Interacts with SPOP; this recruits the protein to a
CC ubiquitin ligase complex containing SPOP and CUL3 (By similarity).
CC {ECO:0000250, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Predominantly nuclear. {ECO:0000250}.
CC -!- DOMAIN: Contains an N-terminal anti-parallel coiled coil formed by two
CC BRMS1 chains; this region can form homohexamers. {ECO:0000250}.
CC -!- PTM: Ubiquitinated by a cullin-RING-based BCR (BTB-CUL3-RBX1) E3
CC ubiquitin-protein ligase complex containing SPOP, leading to
CC proteasomal degradation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the BRMS1 family. {ECO:0000305}.
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DR EMBL; AF233580; AAK15007.1; -; mRNA.
DR EMBL; AF368292; AAK51553.1; -; Genomic_DNA.
DR EMBL; BC016108; AAH16108.1; -; mRNA.
DR CCDS; CCDS50355.1; -.
DR RefSeq; NP_598916.1; NM_134155.1.
DR AlphaFoldDB; Q99N20; -.
DR SMR; Q99N20; -.
DR BioGRID; 223258; 2.
DR ComplexPortal; CPX-3441; SIN3A histone deacetylase complex, ES cell-specific variant.
DR ComplexPortal; CPX-3443; SIN3A histone deacetylase complex.
DR ComplexPortal; CPX-3444; SIN3B histone deacetylase complex.
DR IntAct; Q99N20; 2.
DR MINT; Q99N20; -.
DR STRING; 10090.ENSMUSP00000112266; -.
DR iPTMnet; Q99N20; -.
DR PhosphoSitePlus; Q99N20; -.
DR EPD; Q99N20; -.
DR jPOST; Q99N20; -.
DR MaxQB; Q99N20; -.
DR PaxDb; Q99N20; -.
DR PRIDE; Q99N20; -.
DR ProteomicsDB; 273766; -.
DR Antibodypedia; 4414; 303 antibodies from 32 providers.
DR DNASU; 107392; -.
DR Ensembl; ENSMUST00000116567; ENSMUSP00000112266; ENSMUSG00000080268.
DR GeneID; 107392; -.
DR KEGG; mmu:107392; -.
DR UCSC; uc008gbz.1; mouse.
DR CTD; 25855; -.
DR MGI; MGI:2388804; Brms1.
DR VEuPathDB; HostDB:ENSMUSG00000080268; -.
DR eggNOG; KOG4466; Eukaryota.
DR GeneTree; ENSGT00940000161779; -.
DR HOGENOM; CLU_050862_1_0_1; -.
DR InParanoid; Q99N20; -.
DR OMA; SEKHMAV; -.
DR OrthoDB; 1456563at2759; -.
DR PhylomeDB; Q99N20; -.
DR TreeFam; TF323740; -.
DR Reactome; R-MMU-3214815; HDACs deacetylate histones.
DR BioGRID-ORCS; 107392; 8 hits in 71 CRISPR screens.
DR ChiTaRS; Brms1; mouse.
DR PRO; PR:Q99N20; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q99N20; protein.
DR Bgee; ENSMUSG00000080268; Expressed in spermatid and 176 other tissues.
DR ExpressionAtlas; Q99N20; baseline and differential.
DR Genevisible; Q99N20; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016580; C:Sin3 complex; IC:ComplexPortal.
DR GO; GO:0070822; C:Sin3-type complex; IBA:GO_Central.
DR GO; GO:0042826; F:histone deacetylase binding; IBA:GO_Central.
DR GO; GO:0051059; F:NF-kappaB binding; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0030336; P:negative regulation of cell migration; IC:ComplexPortal.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:1902455; P:negative regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:2000210; P:positive regulation of anoikis; ISS:UniProtKB.
DR GO; GO:0090312; P:positive regulation of protein deacetylation; ISS:UniProtKB.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI.
DR InterPro; IPR013907; Sds3.
DR PANTHER; PTHR21964; PTHR21964; 1.
DR Pfam; PF08598; Sds3; 1.
DR SMART; SM01401; Sds3; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Coiled coil; Cytoplasm; Isopeptide bond; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Tumor suppressor; Ubl conjugation.
FT CHAIN 1..246
FT /note="Breast cancer metastasis-suppressor 1 homolog"
FT /id="PRO_0000064989"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 51..98
FT /evidence="ECO:0000250"
FT COMPBIAS 15..49
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 184
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9HCU9"
FT CROSSLNK 242
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5PSV4"
SQ SEQUENCE 246 AA; 28210 MW; 3825F0B5CB84E575 CRC64;
MPIQPSGKET EEMEAEGDSA AEMNGEADES EEERSGSQTE SEEESSEMDD EDYERRRSEC
VSEMLDLEKQ FSELKEKLFR ERLSQLRLRL EEVGAERAPE YTEPLGGLQQ SLKIRIQVAG
IYKGFCLDVI RNKYECELQG AKQHLESEKM LLYDTLLGEL QERIQRLEED RQSLDISSEW
WDDKLHSRSS SKAGDAMPPS KRKKAPLVSG PYIVYMLQEI DILEDWTAIK KARAAVSPQK
RKADGP
