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Breast cancer metastasis-suppressor 1

 BRMS1_HUMAN             Reviewed;         246 AA.
Q9HCU9; Q6IAI2;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
18-JUL-2018, entry version 139.
RecName: Full=Breast cancer metastasis-suppressor 1;
Name=BRMS1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
PubMed=10850410;
Seraj M.J., Samant R.S., Verderame M.F., Welch D.R.;
"Functional evidence for a novel human breast carcinoma metastasis
suppressor, BRMS1, encoded at chromosome 11q13.";
Cancer Res. 60:2764-2769(2000).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Welch D.R., Samant R.S., Debies M.T., Seraj M.J., Verderame M.F.;
"Genomic structure and chromosomal localization of the breast
metastasis suppressor gene, BRMS1.";
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
TISSUE SPECIFICITY, AND POSSIBLE INVOLVEMENT IN INVASION/MIGRATION OF
TROPHOBLAST CELLS.
PubMed=12414911; DOI=10.1210/jc.2002-021093;
Janneau J.-L., Maldonado-Estrada J., Tachdjian G., Miran I., Motte N.,
Saulnier P., Sabourin J.-C., Cote J.-F., Simon B., Frydman R.,
Chaouat G., Bellet D.;
"Transcriptional expression of genes involved in cell invasion and
migration by normal and tumoral trophoblast cells.";
J. Clin. Endocrinol. Metab. 87:5336-5339(2002).
[7]
FUNCTION, INTERACTION WITH ARID4A, AND IDENTIFICATION IN A COMPLEX
WITH SIN3A; SIN3B; HDAC1; HDAC2; SAP30; SUDS3; RBBP4 AND RBBP7.
PubMed=14581478; DOI=10.1074/jbc.M307969200;
Meehan W.J., Samant R.S., Hopper J.E., Carrozza M.J., Shevde L.A.,
Workman J.L., Eckert K.A., Verderame M.F., Welch D.R.;
"Breast cancer metastasis suppressor 1 (BRMS1) forms complexes with
retinoblastoma-binding protein 1 (RBP1) and the mSin3 histone
deacetylase complex and represses transcription.";
J. Biol. Chem. 279:1562-1569(2004).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HDAC1 AND RELA.
PubMed=17000776; DOI=10.1128/MCB.00940-06;
Liu Y., Smith P.W., Jones D.R.;
"Breast cancer metastasis suppressor 1 functions as a corepressor by
enhancing histone deacetylase 1-mediated deacetylation of RelA/p65 and
promoting apoptosis.";
Mol. Cell. Biol. 26:8683-8696(2006).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SNX6.
PubMed=20830743; DOI=10.1002/jcb.22874;
Rivera J., Megias D., Bravo J.;
"Sorting nexin 6 interacts with breast cancer metastasis suppressor-1
and promotes transcriptional repression.";
J. Cell. Biochem. 111:1464-1472(2010).
[10]
UBIQUITINATION, SUBCELLULAR LOCATION, INTERACTION WITH SPOP, AND
IDENTIFICATION IN A COMPLEX WITH CUL3 AND SPOP.
PubMed=22085717; DOI=10.1016/j.bbrc.2011.10.154;
Kim B., Nam H.J., Pyo K.E., Jang M.J., Kim I.S., Kim D., Boo K.,
Lee S.H., Yoon J.B., Baek S.H., Kim J.H.;
"Breast cancer metastasis suppressor 1 (BRMS1) is destabilized by the
Cul3-SPOP E3 ubiquitin ligase complex.";
Biochem. Biophys. Res. Commun. 415:720-726(2011).
[11]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-184, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[12]
X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 51-98, COILED-COIL DOMAIN,
AND SUBUNIT.
PubMed=21777593; DOI=10.1016/j.jmb.2011.07.006;
Spinola-Amilibia M., Rivera J., Ortiz-Lombardia M., Romero A.,
Neira J.L., Bravo J.;
"The structure of BRMS1 nuclear export signal and SNX6 interacting
region reveals a hexamer formed by antiparallel coiled coils.";
J. Mol. Biol. 411:1114-1127(2011).
-!- FUNCTION: Transcriptional repressor. Down-regulates transcription
activation by NF-kappa-B by promoting the deacetylation of RELA at
'Lys-310'. Promotes HDAC1 binding to promoter regions. Down-
regulates expression of anti-apoptotic genes that are controlled
by NF-kappa-B. Promotes apoptosis in cells that have inadequate
adherence to a substrate, a process called anoikis, and may
thereby inhibit metastasis. May be a mediator of metastasis
suppression in breast carcinoma. {ECO:0000269|PubMed:14581478,
ECO:0000269|PubMed:17000776, ECO:0000269|PubMed:20830743}.
-!- SUBUNIT: Homohexamer (Potential). Interacts with SNX6, HDAC1 and
RELA. Interacts with ARID4A. Identified in mSin3A corepressor
complexes together with SIN3A, SIN3B, RBBP4, RBBP7, SAP30, SUDS3,
ARID4A, HDAC1 and HDAC2. Interacts with SPOP; this recruits the
protein to a ubiquitin ligase complex containing SPOP and CUL3.
{ECO:0000269|PubMed:14581478, ECO:0000269|PubMed:17000776,
ECO:0000269|PubMed:20830743, ECO:0000269|PubMed:21777593,
ECO:0000269|PubMed:22085717, ECO:0000305}.
-!- INTERACTION:
Q8NHQ1:CEP70; NbExp=3; IntAct=EBI-714781, EBI-739624;
O75190:DNAJB6; NbExp=2; IntAct=EBI-714781, EBI-1053164;
Q13547:HDAC1; NbExp=4; IntAct=EBI-714781, EBI-301834;
Q92769:HDAC2; NbExp=4; IntAct=EBI-714781, EBI-301821;
P56524:HDAC4; NbExp=2; IntAct=EBI-714781, EBI-308629;
Q9UQL6:HDAC5; NbExp=2; IntAct=EBI-714781, EBI-715576;
Q9UBN7:HDAC6; NbExp=2; IntAct=EBI-714781, EBI-301697;
Q13287:NMI; NbExp=6; IntAct=EBI-714781, EBI-372942;
Q969G3:SMARCE1; NbExp=3; IntAct=EBI-714781, EBI-455078;
Q9H7L9:SUDS3; NbExp=2; IntAct=EBI-714781, EBI-540496;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly
nuclear.
-!- TISSUE SPECIFICITY: Expression levels are higher in term placentas
than in early placentas. Low levels of expression observed in
normal pregnancies and in molar pregnancies.
{ECO:0000269|PubMed:12414911}.
-!- DOMAIN: Contains an N-terminal anti-parallel coiled coil formed by
two BRMS1 chains; this region can form homohexamers.
-!- PTM: Ubiquitinated by a cullin-RING-based BCR (BTB-CUL3-RBX1) E3
ubiquitin-protein ligase complex containing SPOP, leading to
proteasomal degradation. {ECO:0000269|PubMed:22085717}.
-!- SIMILARITY: Belongs to the BRMS1 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/BRMS1ID841ch11q13.html";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF159141; AAG00075.1; -; mRNA.
EMBL; AF281036; AAK69131.1; -; Genomic_DNA.
EMBL; CR457173; CAG33454.1; -; mRNA.
EMBL; AK313773; BAG36511.1; -; mRNA.
EMBL; BC009834; AAH09834.1; -; mRNA.
CCDS; CCDS8135.1; -.
RefSeq; NP_056214.1; NM_015399.3.
UniGene; Hs.100426; -.
PDB; 2XUS; X-ray; 1.91 A; A/B=51-98.
PDB; 4AUV; X-ray; 2.00 A; A/B/C/D/E/F/G/H=51-84.
PDBsum; 2XUS; -.
PDBsum; 4AUV; -.
ProteinModelPortal; Q9HCU9; -.
SMR; Q9HCU9; -.
BioGrid; 117379; 67.
CORUM; Q9HCU9; -.
DIP; DIP-24250N; -.
IntAct; Q9HCU9; 37.
MINT; Q9HCU9; -.
STRING; 9606.ENSP00000396052; -.
iPTMnet; Q9HCU9; -.
PhosphoSitePlus; Q9HCU9; -.
BioMuta; BRMS1; -.
DMDM; 18202959; -.
EPD; Q9HCU9; -.
MaxQB; Q9HCU9; -.
PaxDb; Q9HCU9; -.
PeptideAtlas; Q9HCU9; -.
PRIDE; Q9HCU9; -.
ProteomicsDB; 81803; -.
DNASU; 25855; -.
Ensembl; ENST00000359957; ENSP00000353042; ENSG00000174744.
GeneID; 25855; -.
KEGG; hsa:25855; -.
UCSC; uc001ohp.2; human.
CTD; 25855; -.
DisGeNET; 25855; -.
EuPathDB; HostDB:ENSG00000174744.13; -.
GeneCards; BRMS1; -.
HGNC; HGNC:17262; BRMS1.
HPA; CAB010824; -.
HPA; HPA019637; -.
MIM; 606259; gene.
neXtProt; NX_Q9HCU9; -.
OpenTargets; ENSG00000174744; -.
PharmGKB; PA164741342; -.
eggNOG; KOG4466; Eukaryota.
eggNOG; ENOG410Y9N9; LUCA.
GeneTree; ENSGT00910000144178; -.
HOGENOM; HOG000007483; -.
HOVERGEN; HBG050734; -.
InParanoid; Q9HCU9; -.
KO; K19196; -.
PhylomeDB; Q9HCU9; -.
Reactome; R-HSA-3214815; HDACs deacetylate histones.
EvolutionaryTrace; Q9HCU9; -.
GeneWiki; BRMS1; -.
GenomeRNAi; 25855; -.
PRO; PR:Q9HCU9; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000174744; -.
CleanEx; HS_BRMS1; -.
ExpressionAtlas; Q9HCU9; baseline and differential.
Genevisible; Q9HCU9; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0070822; C:Sin3-type complex; IBA:GO_Central.
GO; GO:0004407; F:histone deacetylase activity; TAS:Reactome.
GO; GO:0042826; F:histone deacetylase binding; IBA:GO_Central.
GO; GO:0051059; F:NF-kappaB binding; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:2000210; P:positive regulation of anoikis; IMP:UniProtKB.
GO; GO:0090312; P:positive regulation of protein deacetylation; IDA:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR013907; Sds3.
PANTHER; PTHR21964; PTHR21964; 1.
Pfam; PF08598; Sds3; 1.
SMART; SM01401; Sds3; 1.
1: Evidence at protein level;
3D-structure; Apoptosis; Coiled coil; Complete proteome; Cytoplasm;
Isopeptide bond; Nucleus; Reference proteome; Repressor;
Transcription; Transcription regulation; Tumor suppressor;
Ubl conjugation.
CHAIN 1 246 Breast cancer metastasis-suppressor 1.
/FTId=PRO_0000064988.
COILED 51 98 {ECO:0000269|PubMed:21777593}.
CROSSLNK 184 184 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 242 242 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q5PSV4}.
HELIX 55 93 {ECO:0000244|PDB:2XUS}.
SEQUENCE 246 AA; 28461 MW; 89FB59FB96ECD4DB CRC64;
MPVQPPSKDT EEMEAEGDSA AEMNGEEEES EEERSGSQTE SEEESSEMDD EDYERRRSEC
VSEMLDLEKQ FSELKEKLFR ERLSQLRLRL EEVGAERAPE YTEPLGGLQR SLKIRIQVAG
IYKGFCLDVI RNKYECELQG AKQHLESEKL LLYDTLQGEL QERIQRLEED RQSLDLSSEW
WDDKLHARGS SRSWDSLPPS KRKKAPLVSG PYIVYMLQEI DILEDWTAIK KARAAVSPQK
RKSDGP


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