BRM1L_MOUSE
ID BRM1L_MOUSE Reviewed; 323 AA.
AC Q3U1T3; Q8JZX8;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Breast cancer metastasis-suppressor 1-like protein;
GN Name=Brms1l;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD;
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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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: Involved in the histone deacetylase (HDAC1)-dependent
CC transcriptional repression activity. When overexpressed in lung cancer
CC cell line that lacks p53/TP53 expression, inhibits cell growth (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the Sin3/HDAC1 corepressor complex at least
CC composed of BRMS1, BRMS1L and ING2/ING1L. Interacts with HDAC and SIN3A
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3U1T3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3U1T3-2; Sequence=VSP_028347, VSP_028348;
CC -!- SIMILARITY: Belongs to the BRMS1 family. {ECO:0000305}.
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DR EMBL; AK154678; BAE32759.1; -; mRNA.
DR EMBL; AK155742; BAE33410.1; -; mRNA.
DR EMBL; BC034885; AAH34885.1; -; mRNA.
DR CCDS; CCDS36453.1; -. [Q3U1T3-1]
DR RefSeq; NP_001032845.1; NM_001037756.2. [Q3U1T3-1]
DR AlphaFoldDB; Q3U1T3; -.
DR SMR; Q3U1T3; -.
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 STRING; 10090.ENSMUSP00000082500; -.
DR iPTMnet; Q3U1T3; -.
DR PhosphoSitePlus; Q3U1T3; -.
DR EPD; Q3U1T3; -.
DR MaxQB; Q3U1T3; -.
DR PaxDb; Q3U1T3; -.
DR PeptideAtlas; Q3U1T3; -.
DR PRIDE; Q3U1T3; -.
DR ProteomicsDB; 273843; -. [Q3U1T3-1]
DR ProteomicsDB; 273844; -. [Q3U1T3-2]
DR Antibodypedia; 23255; 117 antibodies from 20 providers.
DR DNASU; 52592; -.
DR Ensembl; ENSMUST00000059250; ENSMUSP00000082500; ENSMUSG00000012076. [Q3U1T3-1]
DR Ensembl; ENSMUST00000219419; ENSMUSP00000151316; ENSMUSG00000012076. [Q3U1T3-2]
DR GeneID; 52592; -.
DR KEGG; mmu:52592; -.
DR UCSC; uc007noz.1; mouse. [Q3U1T3-2]
DR UCSC; uc007npa.1; mouse. [Q3U1T3-1]
DR CTD; 84312; -.
DR MGI; MGI:1196337; Brms1l.
DR VEuPathDB; HostDB:ENSMUSG00000012076; -.
DR eggNOG; KOG4466; Eukaryota.
DR GeneTree; ENSGT00940000158921; -.
DR HOGENOM; CLU_050862_2_0_1; -.
DR InParanoid; Q3U1T3; -.
DR OMA; ICIDRKD; -.
DR OrthoDB; 1456563at2759; -.
DR PhylomeDB; Q3U1T3; -.
DR TreeFam; TF323740; -.
DR BioGRID-ORCS; 52592; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Brms1l; mouse.
DR PRO; PR:Q3U1T3; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q3U1T3; protein.
DR Bgee; ENSMUSG00000012076; Expressed in morula and 228 other tissues.
DR Genevisible; Q3U1T3; MM.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
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:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0030336; P:negative regulation of cell migration; IC:ComplexPortal.
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:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
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 Alternative splicing; Coiled coil; Growth regulation; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..323
FT /note="Breast cancer metastasis-suppressor 1-like protein"
FT /id="PRO_0000305310"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 52..84
FT /evidence="ECO:0000255"
FT COILED 149..180
FT /evidence="ECO:0000255"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..50
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PSV4"
FT CROSSLNK 240
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5PSV4"
FT CROSSLNK 246
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5PSV4"
FT VAR_SEQ 149..178
FT /note="EKLLLYDTVQSELEEKIRRLEEDRHSIDIT -> CGTTSFSHGKRGRIRSAP
FT TRRSRSLSQVHI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028347"
FT VAR_SEQ 179..323
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028348"
SQ SEQUENCE 323 AA; 37657 MW; BD608ACFD4276E2B CRC64;
MPVHSRGDKK ETNHHDEMEV DYAENEGSSS EDEDTESSSV SEDGDSSEMD DEDCERRRME
CLDEMSNLEK QFTDLKDQLY KERLSQVDAK LQEVIAGKAP EYLEPLATLQ ENMQIRTKVA
GIYRELCLES VKNKYECEIQ ASRQHCESEK LLLYDTVQSE LEEKIRRLEE DRHSIDITSE
LWNDELQSRK KRKDPFSPDK KKPVVVSGPY IVYMLQDLDI LEDWTTIRKA MATLGPHRVK
TEPPVKLEKH LHSARSEEGR LYYDGEWYIR GQTICIDRKD ECPTSAVITT INHDEVWFKR
PDGSKSKLYI SQLQKGKYSI KHS
