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Q9HCU9

- BRMS1_HUMAN

UniProt

Q9HCU9 - BRMS1_HUMAN

Protein

Breast cancer metastasis-suppressor 1

Gene

BRMS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    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. NF-kappaB binding Source: UniProtKB
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
    3. negative regulation of transcription, DNA-templated Source: UniProtKB
    4. positive regulation of anoikis Source: UniProtKB
    5. positive regulation of protein deacetylation Source: UniProtKB
    6. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Apoptosis, Transcription, Transcription regulation

    Names & Taxonomyi

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

    Organism-specific databases

    HGNCiHGNC:17262. BRMS1.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Predominantly nuclear.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA164741342.

    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

    ArrayExpressiQ9HCU9.
    BgeeiQ9HCU9.
    CleanExiHS_BRMS1.
    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 CUL3.5 PublicationsCurated

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    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
    SMARCE1Q969G32EBI-714781,EBI-455078
    SUDS3Q9H7L92EBI-714781,EBI-540496

    Protein-protein interaction databases

    BioGridi117379. 27 interactions.
    DIPiDIP-24250N.
    IntActiQ9HCU9. 21 interactions.
    MINTiMINT-1389009.
    STRINGi9606.ENSP00000396052.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2XUSX-ray1.91A/B51-98[»]
    4AUVX-ray2.00A/B/C/D/E/F/G/H51-84[»]
    ProteinModelPortaliQ9HCU9.
    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.
    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

    MPVQPPSKDT EEMEAEGDSA AEMNGEEEES EEERSGSQTE SEEESSEMDD    50
    EDYERRRSEC VSEMLDLEKQ FSELKEKLFR ERLSQLRLRL EEVGAERAPE 100
    YTEPLGGLQR SLKIRIQVAG IYKGFCLDVI RNKYECELQG AKQHLESEKL 150
    LLYDTLQGEL QERIQRLEED RQSLDLSSEW WDDKLHARGS SRSWDSLPPS 200
    KRKKAPLVSG PYIVYMLQEI DILEDWTAIK KARAAVSPQK RKSDGP 246
    Length:246
    Mass (Da):28,461
    Last modified:March 1, 2001 - v1
    Checksum:i89FB59FB96ECD4DB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 databases

    DMDMi18202959.

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS8135.1.
    RefSeqi NP_056214.1. NM_015399.3.
    UniGenei Hs.100426.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2XUS X-ray 1.91 A/B 51-98 [» ]
    4AUV X-ray 2.00 A/B/C/D/E/F/G/H 51-84 [» ]
    ProteinModelPortali Q9HCU9.
    SMRi Q9HCU9. Positions 54-94.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117379. 27 interactions.
    DIPi DIP-24250N.
    IntActi Q9HCU9. 21 interactions.
    MINTi MINT-1389009.
    STRINGi 9606.ENSP00000396052.

    PTM databases

    PhosphoSitei Q9HCU9.

    Polymorphism databases

    DMDMi 18202959.

    Proteomic databases

    MaxQBi Q9HCU9.
    PaxDbi Q9HCU9.
    PRIDEi Q9HCU9.

    Protocols and materials databases

    DNASUi 25855.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000359957 ; ENSP00000353042 ; ENSG00000174744 .
    GeneIDi 25855.
    KEGGi hsa:25855.
    UCSCi uc001ohp.1. human.

    Organism-specific databases

    CTDi 25855.
    GeneCardsi GC11M066104.
    HGNCi HGNC:17262. BRMS1.
    HPAi CAB010824.
    HPA019637.
    MIMi 606259. gene.
    neXtProti NX_Q9HCU9.
    PharmGKBi PA164741342.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG260250.
    HOGENOMi HOG000007483.
    HOVERGENi HBG050734.
    InParanoidi Q9HCU9.
    PhylomeDBi Q9HCU9.

    Miscellaneous databases

    EvolutionaryTracei Q9HCU9.
    GeneWikii BRMS1.
    GenomeRNAii 25855.
    NextBioi 47213.
    PROi Q9HCU9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9HCU9.
    Bgeei Q9HCU9.
    CleanExi HS_BRMS1.
    Genevestigatori Q9HCU9.

    Family and domain databases

    InterProi IPR013907. Sds3.
    [Graphical view ]
    Pfami PF08598. Sds3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 105 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