BRM1L_HUMAN
ID BRM1L_HUMAN Reviewed; 323 AA.
AC Q5PSV4; A6NFW5; A6NH45; B2RD65; Q9BRI4;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Breast cancer metastasis-suppressor 1-like protein;
DE AltName: Full=BRMS1-homolog protein p40;
DE AltName: Full=BRMS1-like protein p40;
GN Name=BRMS1L;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, IDENTIFICATION IN THE
RP SIN3/HDAC1 COMPLEX, AND INTERACTION WITH HDAC AND SIN3A.
RX PubMed=15451426; DOI=10.1016/j.bbrc.2004.08.227;
RA Nikolaev A.Y., Papanikolaou N.A., Li M., Qin J., Gu W.;
RT "Identification of a novel BRMS1-homologue protein p40 as a component of
RT the mSin3A/p33(ING1b)/HDAC1 deacetylase complex.";
RL Biochem. Biophys. Res. Commun. 323:1216-1222(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Ovary;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [6]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-246, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-240, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-240, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-240 AND LYS-246, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
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.
CC {ECO:0000269|PubMed:15451426}.
CC -!- SUBUNIT: Component of the Sin3/HDAC1 corepressor complex at least
CC composed of BRMS1, BRMS1L and ING2/ING1L. Interacts with HDAC and
CC SIN3A. {ECO:0000269|PubMed:15451426}.
CC -!- INTERACTION:
CC Q5PSV4; P35609: ACTN2; NbExp=7; IntAct=EBI-5666615, EBI-77797;
CC Q5PSV4; Q9Y2J4: AMOTL2; NbExp=3; IntAct=EBI-5666615, EBI-746752;
CC Q5PSV4; Q9Y2J4-4: AMOTL2; NbExp=3; IntAct=EBI-5666615, EBI-10187270;
CC Q5PSV4; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-5666615, EBI-739624;
CC Q5PSV4; Q05D60: DEUP1; NbExp=3; IntAct=EBI-5666615, EBI-748597;
CC Q5PSV4; O00471: EXOC5; NbExp=3; IntAct=EBI-5666615, EBI-949824;
CC Q5PSV4; P22607: FGFR3; NbExp=3; IntAct=EBI-5666615, EBI-348399;
CC Q5PSV4; Q14957: GRIN2C; NbExp=3; IntAct=EBI-5666615, EBI-8285963;
CC Q5PSV4; P01112: HRAS; NbExp=3; IntAct=EBI-5666615, EBI-350145;
CC Q5PSV4; Q96EZ8: MCRS1; NbExp=5; IntAct=EBI-5666615, EBI-348259;
CC Q5PSV4; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-5666615, EBI-10172526;
CC Q5PSV4; P40424: PBX1; NbExp=3; IntAct=EBI-5666615, EBI-301611;
CC Q5PSV4; P40425: PBX2; NbExp=3; IntAct=EBI-5666615, EBI-348489;
CC Q5PSV4; Q8IYF3-3: TEX11; NbExp=3; IntAct=EBI-5666615, EBI-11523345;
CC Q5PSV4; P40222: TXLNA; NbExp=3; IntAct=EBI-5666615, EBI-359793;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5PSV4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5PSV4-2; Sequence=VSP_055547;
CC -!- SIMILARITY: Belongs to the BRMS1 family. {ECO:0000305}.
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DR EMBL; AY827074; AAV83797.1; -; mRNA.
DR EMBL; AK315424; BAG37812.1; -; mRNA.
DR EMBL; AL162311; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006250; AAH06250.2; -; mRNA.
DR CCDS; CCDS32066.1; -. [Q5PSV4-1]
DR RefSeq; NP_115728.2; NM_032352.3. [Q5PSV4-1]
DR RefSeq; XP_006720338.1; XM_006720275.2. [Q5PSV4-2]
DR RefSeq; XP_016877193.1; XM_017021704.1. [Q5PSV4-2]
DR RefSeq; XP_016877194.1; XM_017021705.1. [Q5PSV4-2]
DR AlphaFoldDB; Q5PSV4; -.
DR SMR; Q5PSV4; -.
DR BioGRID; 124038; 126.
DR ComplexPortal; CPX-3321; SIN3A histone deacetylase complex.
DR ComplexPortal; CPX-3322; SIN3B histone deacetylase complex.
DR ComplexPortal; CPX-3323; SIN3A histone deacetylase complex, ES cell-specific variant.
DR CORUM; Q5PSV4; -.
DR IntAct; Q5PSV4; 62.
DR MINT; Q5PSV4; -.
DR STRING; 9606.ENSP00000216807; -.
DR GlyGen; Q5PSV4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5PSV4; -.
DR PhosphoSitePlus; Q5PSV4; -.
DR BioMuta; BRMS1L; -.
DR DMDM; 158706476; -.
DR EPD; Q5PSV4; -.
DR jPOST; Q5PSV4; -.
DR MassIVE; Q5PSV4; -.
DR MaxQB; Q5PSV4; -.
DR PaxDb; Q5PSV4; -.
DR PeptideAtlas; Q5PSV4; -.
DR PRIDE; Q5PSV4; -.
DR ProteomicsDB; 3426; -.
DR ProteomicsDB; 63603; -. [Q5PSV4-1]
DR Antibodypedia; 23255; 117 antibodies from 20 providers.
DR DNASU; 84312; -.
DR Ensembl; ENST00000216807.12; ENSP00000216807.6; ENSG00000100916.14. [Q5PSV4-1]
DR GeneID; 84312; -.
DR KEGG; hsa:84312; -.
DR MANE-Select; ENST00000216807.12; ENSP00000216807.6; NM_032352.4; NP_115728.2.
DR UCSC; uc001wtl.4; human. [Q5PSV4-1]
DR CTD; 84312; -.
DR DisGeNET; 84312; -.
DR GeneCards; BRMS1L; -.
DR HGNC; HGNC:20512; BRMS1L.
DR HPA; ENSG00000100916; Low tissue specificity.
DR MIM; 618514; gene.
DR neXtProt; NX_Q5PSV4; -.
DR OpenTargets; ENSG00000100916; -.
DR PharmGKB; PA134968356; -.
DR VEuPathDB; HostDB:ENSG00000100916; -.
DR eggNOG; KOG4466; Eukaryota.
DR GeneTree; ENSGT00940000158921; -.
DR HOGENOM; CLU_050862_2_0_1; -.
DR InParanoid; Q5PSV4; -.
DR OMA; ICIDRKD; -.
DR OrthoDB; 1456563at2759; -.
DR PhylomeDB; Q5PSV4; -.
DR TreeFam; TF323740; -.
DR PathwayCommons; Q5PSV4; -.
DR SignaLink; Q5PSV4; -.
DR BioGRID-ORCS; 84312; 17 hits in 1080 CRISPR screens.
DR ChiTaRS; BRMS1L; human.
DR GenomeRNAi; 84312; -.
DR Pharos; Q5PSV4; Tbio.
DR PRO; PR:Q5PSV4; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q5PSV4; protein.
DR Bgee; ENSG00000100916; Expressed in left ventricle myocardium and 184 other tissues.
DR ExpressionAtlas; Q5PSV4; baseline and differential.
DR Genevisible; Q5PSV4; HS.
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 1: Evidence at protein 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_0000305309"
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:0007744|PubMed:23186163"
FT CROSSLNK 240
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 246
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..48
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055547"
FT CONFLICT 206
FT /note="V -> G (in Ref. 1; AAV83797)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 323 AA; 37629 MW; 35908ACFD439A117 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 GQTICIDKKD ECPTSAVITT INHDEVWFKR
PDGSKSKLYI SQLQKGKYSI KHS
