Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9HCU9 (BRMS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Breast cancer metastasis-suppressor 1
Gene names
Name:BRMS1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length246 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.7 Ref.8 Ref.9

Subunit structure

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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11

Subcellular location

Nucleus. Cytoplasm. Note: Predominantly nuclear. Ref.8 Ref.9 Ref.10

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. Ref.6

Domain

Contains an N-terminal anti-parallel coiled coil formed by two BRMS1 chains; this region can form homohexamers. Ref.11

Post-translational modification

Ubiquitinated by a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex containing SPOP, leading to proteasomal degradation. Ref.10

Sequence similarities

Belongs to the BRMS1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 246246Breast cancer metastasis-suppressor 1
PRO_0000064988

Regions

Coiled coil51 – 9848 Ref.11

Secondary structure

... 246
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9HCU9 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 89FB59FB96ECD4DB

FASTA24628,461
        10         20         30         40         50         60 
MPVQPPSKDT EEMEAEGDSA AEMNGEEEES EEERSGSQTE SEEESSEMDD EDYERRRSEC 

        70         80         90        100        110        120 
VSEMLDLEKQ FSELKEKLFR ERLSQLRLRL EEVGAERAPE YTEPLGGLQR SLKIRIQVAG 

       130        140        150        160        170        180 
IYKGFCLDVI RNKYECELQG AKQHLESEKL LLYDTLQGEL QERIQRLEED RQSLDLSSEW 

       190        200        210        220        230        240 
WDDKLHARGS SRSWDSLPPS KRKKAPLVSG PYIVYMLQEI DILEDWTAIK KARAAVSPQK 


RKSDGP 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS8135.1.
RefSeqNP_056214.1. NM_015399.3.
UniGeneHs.100426.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2XUSX-ray1.91A/B51-98[»]
4AUVX-ray2.00A/B/C/D/E/F/G/H51-84[»]
ProteinModelPortalQ9HCU9.
SMRQ9HCU9. Positions 54-94.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117379. 27 interactions.
DIPDIP-24250N.
IntActQ9HCU9. 21 interactions.
MINTMINT-1389009.
STRING9606.ENSP00000396052.

PTM databases

PhosphoSiteQ9HCU9.

Polymorphism databases

DMDM18202959.

Proteomic databases

MaxQBQ9HCU9.
PaxDbQ9HCU9.
PRIDEQ9HCU9.

Protocols and materials databases

DNASU25855.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359957; ENSP00000353042; ENSG00000174744.
GeneID25855.
KEGGhsa:25855.
UCSCuc001ohp.1. human.

Organism-specific databases

CTD25855.
GeneCardsGC11M066104.
HGNCHGNC:17262. BRMS1.
HPACAB010824.
HPA019637.
MIM606259. gene.
neXtProtNX_Q9HCU9.
PharmGKBPA164741342.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG260250.
HOGENOMHOG000007483.
HOVERGENHBG050734.
InParanoidQ9HCU9.
PhylomeDBQ9HCU9.

Gene expression databases

ArrayExpressQ9HCU9.
BgeeQ9HCU9.
CleanExHS_BRMS1.
GenevestigatorQ9HCU9.

Family and domain databases

InterProIPR013907. Sds3.
[Graphical view]
PfamPF08598. Sds3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9HCU9.
GeneWikiBRMS1.
GenomeRNAi25855.
NextBio47213.
PROQ9HCU9.
SOURCESearch...

Entry information

Entry nameBRMS1_HUMAN
AccessionPrimary (citable) accession number: Q9HCU9
Secondary accession number(s): Q6IAI2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM