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Protein

Breast cancer metastasis-suppressor 1

Gene

BRMS1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

GO - Molecular functioni

  1. histone deacetylase binding Source: GO_Central
  2. NF-kappaB binding Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. chromatin organization Source: Reactome
  3. histone deacetylation Source: GO_Central
  4. negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
  5. negative regulation of transcription, DNA-templated Source: UniProtKB
  6. negative regulation of transcription from RNA polymerase II promoter Source: GO_Central
  7. positive regulation of anoikis Source: UniProtKB
  8. positive regulation of protein deacetylation Source: UniProtKB
  9. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Apoptosis, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_263923. HDACs deacetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Breast cancer metastasis-suppressor 1
Gene namesi
Name:BRMS1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:17262. BRMS1.

Subcellular locationi

  1. Nucleus
  2. Cytoplasm

  3. Note: Predominantly nuclear.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleoplasm Source: Reactome
  3. nucleus Source: UniProtKB
  4. Sin3-type complex Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA164741342.

Polymorphism and mutation databases

BioMutaiBRMS1.
DMDMi18202959.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 246246Breast cancer metastasis-suppressor 1PRO_0000064988Add
BLAST

Post-translational modificationi

Ubiquitinated by a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex containing SPOP, leading to proteasomal degradation.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiQ9HCU9.
PaxDbiQ9HCU9.
PRIDEiQ9HCU9.

PTM databases

PhosphoSiteiQ9HCU9.

Expressioni

Tissue specificityi

Expression levels are higher in term placentas than in early placentas. Low levels of expression observed in normal pregnancies and in molar pregnancies.1 Publication

Gene expression databases

BgeeiQ9HCU9.
CleanExiHS_BRMS1.
ExpressionAtlasiQ9HCU9. baseline and differential.
GenevestigatoriQ9HCU9.

Organism-specific databases

HPAiCAB010824.
HPA019637.

Interactioni

Subunit structurei

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.Curated5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CEP70Q8NHQ13EBI-714781,EBI-739624
DNAJB6O751902EBI-714781,EBI-1053164
HDAC1Q135474EBI-714781,EBI-301834
HDAC2Q927694EBI-714781,EBI-301821
HDAC4P565242EBI-714781,EBI-308629
HDAC5Q9UQL62EBI-714781,EBI-715576
HDAC6Q9UBN72EBI-714781,EBI-301697
NMIQ132872EBI-714781,EBI-372942
NMIQ8WTW24EBI-714781,EBI-10174268
SMARCE1Q969G33EBI-714781,EBI-455078
SUDS3Q9H7L92EBI-714781,EBI-540496

Protein-protein interaction databases

BioGridi117379. 41 interactions.
DIPiDIP-24250N.
IntActiQ9HCU9. 33 interactions.
MINTiMINT-1389009.
STRINGi9606.ENSP00000396052.

Structurei

Secondary structure

1
246
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi55 – 9339Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XUSX-ray1.91A/B51-98[»]
4AUVX-ray2.00A/B/C/D/E/F/G/H51-84[»]
SMRiQ9HCU9. Positions 54-94.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HCU9.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili51 – 98481 PublicationAdd
BLAST

Domaini

Contains an N-terminal anti-parallel coiled coil formed by two BRMS1 chains; this region can form homohexamers.

Sequence similaritiesi

Belongs to the BRMS1 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG260250.
GeneTreeiENSGT00530000063177.
HOGENOMiHOG000007483.
HOVERGENiHBG050734.
InParanoidiQ9HCU9.
PhylomeDBiQ9HCU9.

Family and domain databases

InterProiIPR013907. Sds3.
[Graphical view]
PfamiPF08598. Sds3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9HCU9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVQPPSKDT EEMEAEGDSA AEMNGEEEES EEERSGSQTE SEEESSEMDD
60 70 80 90 100
EDYERRRSEC VSEMLDLEKQ FSELKEKLFR ERLSQLRLRL EEVGAERAPE
110 120 130 140 150
YTEPLGGLQR SLKIRIQVAG IYKGFCLDVI RNKYECELQG AKQHLESEKL
160 170 180 190 200
LLYDTLQGEL QERIQRLEED RQSLDLSSEW WDDKLHARGS SRSWDSLPPS
210 220 230 240
KRKKAPLVSG PYIVYMLQEI DILEDWTAIK KARAAVSPQK RKSDGP
Length:246
Mass (Da):28,461
Last modified:March 1, 2001 - v1
Checksum:i89FB59FB96ECD4DB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF159141 mRNA. Translation: AAG00075.1.
AF281036 Genomic DNA. Translation: AAK69131.1.
CR457173 mRNA. Translation: CAG33454.1.
AK313773 mRNA. Translation: BAG36511.1.
BC009834 mRNA. Translation: AAH09834.1.
CCDSiCCDS8135.1.
RefSeqiNP_056214.1. NM_015399.3.
UniGeneiHs.100426.

Genome annotation databases

EnsembliENST00000359957; ENSP00000353042; ENSG00000174744.
GeneIDi25855.
KEGGihsa:25855.
UCSCiuc001ohp.1. human.

Polymorphism and mutation databases

BioMutaiBRMS1.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF159141 mRNA. Translation: AAG00075.1.
AF281036 Genomic DNA. Translation: AAK69131.1.
CR457173 mRNA. Translation: CAG33454.1.
AK313773 mRNA. Translation: BAG36511.1.
BC009834 mRNA. Translation: AAH09834.1.
CCDSiCCDS8135.1.
RefSeqiNP_056214.1. NM_015399.3.
UniGeneiHs.100426.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XUSX-ray1.91A/B51-98[»]
4AUVX-ray2.00A/B/C/D/E/F/G/H51-84[»]
SMRiQ9HCU9. Positions 54-94.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117379. 41 interactions.
DIPiDIP-24250N.
IntActiQ9HCU9. 33 interactions.
MINTiMINT-1389009.
STRINGi9606.ENSP00000396052.

PTM databases

PhosphoSiteiQ9HCU9.

Polymorphism and mutation databases

BioMutaiBRMS1.
DMDMi18202959.

Proteomic databases

MaxQBiQ9HCU9.
PaxDbiQ9HCU9.
PRIDEiQ9HCU9.

Protocols and materials databases

DNASUi25855.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000359957; ENSP00000353042; ENSG00000174744.
GeneIDi25855.
KEGGihsa:25855.
UCSCiuc001ohp.1. human.

Organism-specific databases

CTDi25855.
GeneCardsiGC11M066104.
HGNCiHGNC:17262. BRMS1.
HPAiCAB010824.
HPA019637.
MIMi606259. gene.
neXtProtiNX_Q9HCU9.
PharmGKBiPA164741342.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG260250.
GeneTreeiENSGT00530000063177.
HOGENOMiHOG000007483.
HOVERGENiHBG050734.
InParanoidiQ9HCU9.
PhylomeDBiQ9HCU9.

Enzyme and pathway databases

ReactomeiREACT_263923. HDACs deacetylate histones.

Miscellaneous databases

EvolutionaryTraceiQ9HCU9.
GeneWikiiBRMS1.
GenomeRNAii25855.
NextBioi47213.
PROiQ9HCU9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9HCU9.
CleanExiHS_BRMS1.
ExpressionAtlasiQ9HCU9. baseline and differential.
GenevestigatoriQ9HCU9.

Family and domain databases

InterProiIPR013907. Sds3.
[Graphical view]
PfamiPF08598. Sds3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Functional evidence for a novel human breast carcinoma metastasis suppressor, BRMS1, encoded at chromosome 11q13."
    Seraj M.J., Samant R.S., Verderame M.F., Welch D.R.
    Cancer Res. 60:2764-2769(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  2. "Genomic structure and chromosomal localization of the breast metastasis suppressor gene, BRMS1."
    Welch D.R., Samant R.S., Debies M.T., Seraj M.J., Verderame M.F.
    Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta.
  6. "Transcriptional expression of genes involved in cell invasion and migration by normal and tumoral trophoblast cells."
    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.
    J. Clin. Endocrinol. Metab. 87:5336-5339(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, POSSIBLE INVOLVEMENT IN INVASION/MIGRATION OF TROPHOBLAST CELLS.
  7. "Breast cancer metastasis suppressor 1 (BRMS1) forms complexes with retinoblastoma-binding protein 1 (RBP1) and the mSin3 histone deacetylase complex and represses transcription."
    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.
    J. Biol. Chem. 279:1562-1569(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ARID4A, IDENTIFICATION IN A COMPLEX WITH SIN3A; SIN3B; HDAC1; HDAC2; SAP30; SUDS3; RBBP4 AND RBBP7.
  8. "Breast cancer metastasis suppressor 1 functions as a corepressor by enhancing histone deacetylase 1-mediated deacetylation of RelA/p65 and promoting apoptosis."
    Liu Y., Smith P.W., Jones D.R.
    Mol. Cell. Biol. 26:8683-8696(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HDAC1 AND RELA.
  9. "Sorting nexin 6 interacts with breast cancer metastasis suppressor-1 and promotes transcriptional repression."
    Rivera J., Megias D., Bravo J.
    J. Cell. Biochem. 111:1464-1472(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SNX6.
  10. "Breast cancer metastasis suppressor 1 (BRMS1) is destabilized by the Cul3-SPOP E3 ubiquitin ligase complex."
    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.
    Biochem. Biophys. Res. Commun. 415:720-726(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, SUBCELLULAR LOCATION, INTERACTION WITH SPOP, IDENTIFICATION IN A COMPLEX WITH CUL3 AND SPOP.
  11. "The structure of BRMS1 nuclear export signal and SNX6 interacting region reveals a hexamer formed by antiparallel coiled coils."
    Spinola-Amilibia M., Rivera J., Ortiz-Lombardia M., Romero A., Neira J.L., Bravo J.
    J. Mol. Biol. 411:1114-1127(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 51-98, COILED-COIL DOMAIN, SUBUNIT.

Entry informationi

Entry nameiBRMS1_HUMAN
AccessioniPrimary (citable) accession number: Q9HCU9
Secondary accession number(s): Q6IAI2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: March 1, 2001
Last modified: April 29, 2015
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.