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Q9BRT3

- MIEN1_HUMAN

UniProt

Q9BRT3 - MIEN1_HUMAN

Protein

Migration and invasion enhancer 1

Gene

MIEN1

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

    Increases cell migration by inducing filopodia formation at the leading edge of migrating cells. Plays a role in regulation of apoptosis, possibly through control of CASP3. May be involved in a redox-related process.2 Publications

    GO - Molecular functioni

    1. selenium binding Source: InterPro

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. cell redox homeostasis Source: InterPro
    3. negative regulation of apoptotic process Source: UniProtKB
    4. positive regulation of cell migration Source: UniProtKB
    5. positive regulation of filopodium assembly Source: UniProtKB

    Keywords - Biological processi

    Apoptosis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Migration and invasion enhancer 1
    Alternative name(s):
    HBV X-transactivated gene 4 protein
    HBV XAg-transactivated protein 4
    Protein C35
    Gene namesi
    Name:MIEN1
    Synonyms:C17orf37, RDX12, XTP4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:28230. MIEN1.

    Subcellular locationi

    Cytoplasmcytosol. Cell membrane; Lipid-anchor; Cytoplasmic side
    Note: Concentrates at the leading edge of migrating cells. Localizes outside membrane raft regions.

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt
    3. intrinsic component of the cytoplasmic side of the plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi112 – 1154Missing: No effect on subcellular location. Low protein abundance, suggesting that stability is affected. 1 Publication
    Mutagenesisi112 – 1121C → S: Abolishes prenylation. Predominantly cysolic with little plasma membrane-associated expression. Reduces cell migration by affecting filopodia formation. 1 Publication

    Organism-specific databases

    PharmGKBiPA134947080.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 112111Migration and invasion enhancer 1PRO_0000265099Add
    BLAST
    Propeptidei113 – 1153Removed in mature formCuratedPRO_0000396008

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Disulfide bondi30 ↔ 33Redox-active1 Publication
    Lipidationi112 – 1121S-geranylgeranyl cysteine3 Publications

    Post-translational modificationi

    Isoprenylation facilitates association with the plasma membrane and enhances the migratory phenotype of cells by inducing increased filopodia formation.3 Publications

    Keywords - PTMi

    Acetylation, Disulfide bond, Lipoprotein, Prenylation

    Proteomic databases

    MaxQBiQ9BRT3.
    PaxDbiQ9BRT3.
    PRIDEiQ9BRT3.

    PTM databases

    PhosphoSiteiQ9BRT3.

    Expressioni

    Tissue specificityi

    Among normal tissues, present only in Leydig cells. Strongly up-regulated in breast cancers and in brain cancer distant metastasis (at protein level). Up-regulated in prostate cancer cells and in the higher grades of prostate adenocarcinoma (at protein level).2 Publications

    Gene expression databases

    ArrayExpressiQ9BRT3.
    BgeeiQ9BRT3.
    CleanExiHS_C17orf37.
    GenevestigatoriQ9BRT3.

    Organism-specific databases

    HPAiHPA056650.
    HPA061344.

    Interactioni

    Subunit structurei

    Interacts with GPX1.By similarity

    Protein-protein interaction databases

    STRINGi9606.ENSP00000377778.

    Structurei

    Secondary structure

    1
    115
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi26 – 294
    Turni31 – 344
    Helixi36 – 4611
    Turni47 – 493
    Beta strandi51 – 533
    Beta strandi56 – 594
    Beta strandi61 – 633
    Beta strandi65 – 684
    Helixi77 – 804
    Turni86 – 905
    Helixi91 – 966
    Turni97 – 993

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2LJKNMR-A1-115[»]
    ProteinModelPortaliQ9BRT3.
    SMRiQ9BRT3. Positions 1-115.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the SelWTH family.Curated

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiNOG85235.
    HOGENOMiHOG000275576.
    HOVERGENiHBG059755.
    InParanoidiQ9BRT3.
    KOiK07401.
    OMAiMYTSSAS.
    OrthoDBiEOG7SR4Q5.
    PhylomeDBiQ9BRT3.
    TreeFamiTF326627.

    Family and domain databases

    Gene3Di3.40.30.10. 1 hit.
    InterProiIPR011893. Selenoprotein_Rdx-typ.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF10262. Rdx. 1 hit.
    [Graphical view]
    SUPFAMiSSF52833. SSF52833. 1 hit.
    TIGRFAMsiTIGR02174. CXXU_selWTH. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9BRT3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGEPGQTSV APPPEEVEPG SGVRIVVEYC EPCGFEATYL ELASAVKEQY    50
    PGIEIESRLG GTGAFEIEIN GQLVFSKLEN GGFPYEKDLI EAIRRASNGE 100
    TLEKITNSRP PCVIL 115
    Length:115
    Mass (Da):12,403
    Last modified:June 1, 2001 - v1
    Checksum:i5D8B911C0F23DDC1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY508814 mRNA. Translation: AAR92035.1.
    AF490253 mRNA. Translation: AAO85461.1.
    AC079199 Genomic DNA. No translation available.
    BC006006 mRNA. Translation: AAH06006.1.
    CCDSiCCDS11344.1.
    RefSeqiNP_115715.3. NM_032339.3.
    UniGeneiHs.333526.

    Genome annotation databases

    EnsembliENST00000394231; ENSP00000377778; ENSG00000141741.
    GeneIDi84299.
    KEGGihsa:84299.
    UCSCiuc002hsq.3. human.

    Polymorphism databases

    DMDMi74732925.

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY508814 mRNA. Translation: AAR92035.1 .
    AF490253 mRNA. Translation: AAO85461.1 .
    AC079199 Genomic DNA. No translation available.
    BC006006 mRNA. Translation: AAH06006.1 .
    CCDSi CCDS11344.1.
    RefSeqi NP_115715.3. NM_032339.3.
    UniGenei Hs.333526.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2LJK NMR - A 1-115 [» ]
    ProteinModelPortali Q9BRT3.
    SMRi Q9BRT3. Positions 1-115.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000377778.

    PTM databases

    PhosphoSitei Q9BRT3.

    Polymorphism databases

    DMDMi 74732925.

    Proteomic databases

    MaxQBi Q9BRT3.
    PaxDbi Q9BRT3.
    PRIDEi Q9BRT3.

    Protocols and materials databases

    DNASUi 84299.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000394231 ; ENSP00000377778 ; ENSG00000141741 .
    GeneIDi 84299.
    KEGGi hsa:84299.
    UCSCi uc002hsq.3. human.

    Organism-specific databases

    CTDi 84299.
    GeneCardsi GC17M037886.
    H-InvDB HIX0013783.
    HGNCi HGNC:28230. MIEN1.
    HPAi HPA056650.
    HPA061344.
    MIMi 611802. gene.
    neXtProti NX_Q9BRT3.
    PharmGKBi PA134947080.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG85235.
    HOGENOMi HOG000275576.
    HOVERGENi HBG059755.
    InParanoidi Q9BRT3.
    KOi K07401.
    OMAi MYTSSAS.
    OrthoDBi EOG7SR4Q5.
    PhylomeDBi Q9BRT3.
    TreeFami TF326627.

    Miscellaneous databases

    ChiTaRSi MIEN1. human.
    GenomeRNAii 84299.
    NextBioi 73960.
    PROi Q9BRT3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BRT3.
    Bgeei Q9BRT3.
    CleanExi HS_C17orf37.
    Genevestigatori Q9BRT3.

    Family and domain databases

    Gene3Di 3.40.30.10. 1 hit.
    InterProi IPR011893. Selenoprotein_Rdx-typ.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF10262. Rdx. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52833. SSF52833. 1 hit.
    TIGRFAMsi TIGR02174. CXXU_selWTH. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, ISOPRENYLATION.
    2. "Cloning and identification of human gene 4 transactivated by hepatitis B virus X antigen."
      Liu Y., Cheng J., Lu Y., Wang G., Zhang L., Chen J., Li L.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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: Brain.
    5. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    6. "Novel gene C17orf37 in 17q12 amplicon promotes migration and invasion of prostate cancer cells."
      Dasgupta S., Wasson L.M., Rauniyar N., Prokai L., Borejdo J., Vishwanatha J.K.
      Oncogene 28:2860-2872(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, ISOPRENYLATION AT CYS-112.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Prenylated c17orf37 induces filopodia formation to promote cell migration and metastasis."
      Dasgupta S., Cushman I., Kpetemey M., Casey P.J., Vishwanatha J.K.
      J. Biol. Chem. 286:25935-25946(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, ISOPRENYLATION AT CYS-112, MUTAGENESIS OF CYS-112 AND 112-CYS--LEU-115.
    9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Solution structure of the oncogenic MIEN1 protein reveals a thioredoxin-like fold with a redox-active motif."
      Hsu C.H., Shen T.L., Chang C.F., Chang Y.Y., Huang L.Y.
      PLoS ONE 7:E52292-E52292(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR, DISULFIDE BOND.

    Entry informationi

    Entry nameiMIEN1_HUMAN
    AccessioniPrimary (citable) accession number: Q9BRT3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 12, 2006
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 96 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 17
      Human chromosome 17: 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