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Q14764

- MVP_HUMAN

UniProt

Q14764 - MVP_HUMAN

Protein

Major vault protein

Gene

MVP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Required for normal vault structure. Vaults are multi-subunit structures that may act as scaffolds for proteins involved in signal transduction. Vaults may also play a role in nucleo-cytoplasmic transport. Down-regulates INFG-mediated STAT1 signaling and subsequent activation of JAK. Down-regulates SRC activity and signaling through MAP kinases.3 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein kinase binding Source: UniProtKB
    3. protein phosphatase binding Source: UniProtKB

    GO - Biological processi

    1. cell proliferation Source: Ensembl
    2. ERBB signaling pathway Source: UniProtKB
    3. mRNA transport Source: UniProtKB-KW
    4. negative regulation of protein autophosphorylation Source: UniProtKB
    5. negative regulation of protein tyrosine kinase activity Source: UniProtKB
    6. negative regulation of signaling Source: UniProtKB
    7. protein activation cascade Source: Ensembl
    8. protein transport Source: UniProtKB-KW

    Keywords - Molecular functioni

    Ribonucleoprotein

    Keywords - Biological processi

    mRNA transport, Protein transport, Translocation, Transport

    Enzyme and pathway databases

    SignaLinkiQ14764.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Major vault protein
    Short name:
    MVP
    Alternative name(s):
    Lung resistance-related protein
    Gene namesi
    Name:MVP
    Synonyms:LRP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:7531. MVP.

    Subcellular locationi

    Cytoplasm. Nucleusnuclear pore complex
    Note: 5% found in the nuclear pore complex. Translocates from the nucleus to the cytoplasm upon EGF treatment.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoskeleton Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProtKB
    4. membrane Source: UniProtKB
    5. nuclear pore Source: UniProtKB-SubCell
    6. nucleus Source: UniProtKB
    7. perinuclear region of cytoplasm Source: UniProtKB
    8. ribonucleoprotein complex Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cytoplasm, Nuclear pore complex, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA31332.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 893892Major vault proteinPRO_0000158980Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications

    Post-translational modificationi

    Phosphorylated on Tyr residues after EGF stimulation.1 Publication
    Dephosphorylated by PTPN11.

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ14764.
    PaxDbiQ14764.
    PeptideAtlasiQ14764.
    PRIDEiQ14764.

    2D gel databases

    OGPiQ14764.
    REPRODUCTION-2DPAGEIPI00000105.

    PTM databases

    PhosphoSiteiQ14764.

    Expressioni

    Tissue specificityi

    Present in most normal tissues. Higher expression observed in epithelial cells with secretory and excretory functions, as well as in cells chronically exposed to xenobiotics, such as bronchial cells and cells lining the intestine. Overexpressed in many multidrug-resistant cancer cells.

    Inductioni

    Up-regulated by IFNG/IFN-gamma.1 Publication

    Gene expression databases

    ArrayExpressiQ14764.
    BgeeiQ14764.
    CleanExiHS_MVP.
    GenevestigatoriQ14764.

    Organism-specific databases

    HPAiCAB002752.
    CAB022717.
    HPA002321.

    Interactioni

    Subunit structurei

    The vault ribonucleoprotein particle is a huge (400 A x 670 A) cage structure of 12.9 MDa. It consists of a dimer of half-vaults, with each half-vault comprising 39 identical major vault protein (MVP) chains, PARP4 and one or more vault RNAs (vRNAs). Interacts with TEP1. Interacts with PTEN and activated MAPK1. The phosphorylated protein interacts with the SH2 domains of PTPN11 and SRC. Interacts with APEX1. May interact with ZNF540.6 Publications

    Protein-protein interaction databases

    BioGridi115286. 25 interactions.
    IntActiQ14764. 18 interactions.
    MINTiMINT-5004583.
    STRINGi9606.ENSP00000349977.

    Structurei

    Secondary structure

    1
    893
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi120 – 1256
    Beta strandi137 – 1393
    Beta strandi141 – 1477
    Helixi148 – 1503
    Beta strandi157 – 1637
    Beta strandi170 – 18112
    Beta strandi185 – 1873
    Beta strandi195 – 1984
    Beta strandi208 – 21710

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Y7XNMR-A113-221[»]
    ProteinModelPortaliQ14764.
    SMRiQ14764. Positions 1-815.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ14764.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati2 – 5655MVP 1Add
    BLAST
    Repeati57 – 11155MVP 2Add
    BLAST
    Repeati112 – 16453MVP 3Add
    BLAST
    Repeati165 – 21753MVP 4Add
    BLAST
    Repeati218 – 27255MVP 5Add
    BLAST
    Repeati273 – 32351MVP 6Add
    BLAST
    Repeati324 – 37956MVP 7Add
    BLAST
    Repeati380 – 45778MVP 8Add
    BLAST
    Repeati458 – 52063MVP 9Add
    BLAST

    Domaini

    MVP 3 mediates interaction with PTEN.
    MVP 4 mediates interaction with PARP4.

    Sequence similaritiesi

    Contains 9 MVP (vault) repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG70525.
    HOGENOMiHOG000255109.
    HOVERGENiHBG003499.
    InParanoidiQ14764.
    KOiK17266.
    OMAiQDPLADR.
    OrthoDBiEOG773XFB.
    PhylomeDBiQ14764.
    TreeFamiTF329353.

    Family and domain databases

    InterProiIPR021870. MVP_shoulder.
    IPR002499. Vault_N.
    [Graphical view]
    PfamiPF11978. MVP_shoulder. 1 hit.
    PF01505. Vault. 5 hits.
    [Graphical view]
    PROSITEiPS51224. MVP. 8 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q14764-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATEEFIIRI PPYHYIHVLD QNSNVSRVEV GPKTYIRQDN ERVLFAPMRM    50
    VTVPPRHYCT VANPVSRDAQ GLVLFDVTGQ VRLRHADLEI RLAQDPFPLY 100
    PGEVLEKDIT PLQVVLPNTA LHLKALLDFE DKDGDKVVAG DEWLFEGPGT 150
    YIPRKEVEVV EIIQATIIRQ NQALRLRARK ECWDRDGKER VTGEEWLVTT 200
    VGAYLPAVFE EVLDLVDAVI LTEKTALHLR ARRNFRDFRG VSRRTGEEWL 250
    VTVQDTEAHV PDVHEEVLGV VPITTLGPHN YCVILDPVGP DGKNQLGQKR 300
    VVKGEKSFFL QPGEQLEQGI QDVYVLSEQQ GLLLRALQPL EEGEDEEKVS 350
    HQAGDHWLIR GPLEYVPSAK VEVVEERQAI PLDENEGIYV QDVKTGKVRA 400
    VIGSTYMLTQ DEVLWEKELP PGVEELLNKG QDPLADRGEK DTAKSLQPLA 450
    PRNKTRVVSY RVPHNAAVQV YDYREKRARV VFGPELVSLG PEEQFTVLSL 500
    SAGRPKRPHA RRALCLLLGP DFFTDVITIE TADHARLQLQ LAYNWHFEVN 550
    DRKDPQETAK LFSVPDFVGD ACKAIASRVR GAVASVTFDD FHKNSARIIR 600
    TAVFGFETSE AKGPDGMALP RPRDQAVFPQ NGLVVSSVDV QSVEPVDQRT 650
    RDALQRSVQL AIEITTNSQE AAAKHEAQRL EQEARGRLER QKILDQSEAE 700
    KARKELLELE ALSMAVESTG TAKAEAESRA EAARIEGEGS VLQAKLKAQA 750
    LAIETEAELQ RVQKVRELEL VYARAQLELE VSKAQQLAEV EVKKFKQMTE 800
    AIGPSTIRDL AVAGPEMQVK LLQSLGLKST LITDGSTPIN LFNTAFGLLG 850
    MGPEGQPLGR RVASGPSPGE GISPQSAQAP QAPGDNHVVP VLR 893
    Length:893
    Mass (Da):99,327
    Last modified:January 23, 2007 - v4
    Checksum:i6FEE5545B0A3FE65
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti635 – 6351V → I.
    Corresponds to variant rs35916172 [ dbSNP | Ensembl ].
    VAR_050179
    Natural varianti651 – 6511R → Q.
    Corresponds to variant rs3764944 [ dbSNP | Ensembl ].
    VAR_050180

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X79882 mRNA. Translation: CAA56256.2.
    BC015623 mRNA. Translation: AAH15623.1.
    AJ238512
    , AJ238514, AJ238516, AJ238518 Genomic DNA. Translation: CAB55354.1.
    AJ238519
    , AJ238514, AJ238516, AJ238518 Genomic DNA. Translation: CAB55355.1.
    AJ291365 Genomic DNA. Translation: CAC35313.1.
    AJ291366 mRNA. Translation: CAC35314.1.
    AJ291367 mRNA. Translation: CAC35316.1.
    CCDSiCCDS10656.1.
    PIRiS57723.
    RefSeqiNP_005106.2. NM_005115.4.
    NP_059447.2. NM_017458.3.
    UniGeneiHs.632177.

    Genome annotation databases

    EnsembliENST00000357402; ENSP00000349977; ENSG00000013364.
    ENST00000395353; ENSP00000378760; ENSG00000013364.
    GeneIDi9961.
    KEGGihsa:9961.
    UCSCiuc002dui.3. human.

    Polymorphism databases

    DMDMi21542417.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X79882 mRNA. Translation: CAA56256.2 .
    BC015623 mRNA. Translation: AAH15623.1 .
    AJ238512
    , AJ238514 , AJ238516 , AJ238518 Genomic DNA. Translation: CAB55354.1 .
    AJ238519
    , AJ238514 , AJ238516 , AJ238518 Genomic DNA. Translation: CAB55355.1 .
    AJ291365 Genomic DNA. Translation: CAC35313.1 .
    AJ291366 mRNA. Translation: CAC35314.1 .
    AJ291367 mRNA. Translation: CAC35316.1 .
    CCDSi CCDS10656.1.
    PIRi S57723.
    RefSeqi NP_005106.2. NM_005115.4.
    NP_059447.2. NM_017458.3.
    UniGenei Hs.632177.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Y7X NMR - A 113-221 [» ]
    ProteinModelPortali Q14764.
    SMRi Q14764. Positions 1-815.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115286. 25 interactions.
    IntActi Q14764. 18 interactions.
    MINTi MINT-5004583.
    STRINGi 9606.ENSP00000349977.

    PTM databases

    PhosphoSitei Q14764.

    Polymorphism databases

    DMDMi 21542417.

    2D gel databases

    OGPi Q14764.
    REPRODUCTION-2DPAGE IPI00000105.

    Proteomic databases

    MaxQBi Q14764.
    PaxDbi Q14764.
    PeptideAtlasi Q14764.
    PRIDEi Q14764.

    Protocols and materials databases

    DNASUi 9961.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000357402 ; ENSP00000349977 ; ENSG00000013364 .
    ENST00000395353 ; ENSP00000378760 ; ENSG00000013364 .
    GeneIDi 9961.
    KEGGi hsa:9961.
    UCSCi uc002dui.3. human.

    Organism-specific databases

    CTDi 9961.
    GeneCardsi GC16P029831.
    HGNCi HGNC:7531. MVP.
    HPAi CAB002752.
    CAB022717.
    HPA002321.
    MIMi 605088. gene.
    neXtProti NX_Q14764.
    PharmGKBi PA31332.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG70525.
    HOGENOMi HOG000255109.
    HOVERGENi HBG003499.
    InParanoidi Q14764.
    KOi K17266.
    OMAi QDPLADR.
    OrthoDBi EOG773XFB.
    PhylomeDBi Q14764.
    TreeFami TF329353.

    Enzyme and pathway databases

    SignaLinki Q14764.

    Miscellaneous databases

    EvolutionaryTracei Q14764.
    GeneWikii Major_vault_protein.
    GenomeRNAii 9961.
    NextBioi 37586.
    PROi Q14764.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14764.
    Bgeei Q14764.
    CleanExi HS_MVP.
    Genevestigatori Q14764.

    Family and domain databases

    InterProi IPR021870. MVP_shoulder.
    IPR002499. Vault_N.
    [Graphical view ]
    Pfami PF11978. MVP_shoulder. 1 hit.
    PF01505. Vault. 5 hits.
    [Graphical view ]
    PROSITEi PS51224. MVP. 8 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Scheffer G.L.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO C-TERMINUS.
    3. "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: Eye.
    4. "Cloning and initial analysis of the human multidrug resistance-related MVP/LRP gene promoter."
      Lange C., Walther W., Schwabe H., Stein U.
      Biochem. Biophys. Res. Commun. 278:125-133(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-169.
    5. "A small upstream open reading frame causes inhibition of human major vault protein expression from a ubiquitous mRNA splice variant."
      Holzmann K., Ambrosch I., Elbling L., Micksche M., Berger W.
      FEBS Lett. 494:99-104(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-65.
      Tissue: Lung cancer.
    6. Quadroni M., Potts A., Barblan J., Bienvenut W.V.
      Submitted (JAN-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-9; 68-82 AND 462-474, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Melanoma.
    7. Cited for: ASSOCIATION WITH TEP1.
    8. Cited for: INTERACTION WITH PTEN.
    9. "The major vault protein is a novel substrate for the tyrosine phosphatase SHP-2 and scaffold protein in epidermal growth factor signaling."
      Kolli S., Zito C.I., Mossink M.H., Wiemer E.A.C., Bennett A.M.
      J. Biol. Chem. 279:29374-29385(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYROSINE RESIDUES, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH PTPN11, SUBCELLULAR LOCATION, FUNCTION.
    10. "A novel human zinc finger protein ZNF540 interacts with MVP and inhibits transcriptional activities of the ERK signal pathway."
      Xiang Z., Yuan W., Luo N., Wang Y., Tan K., Deng Y., Zhou X., Zhu C., Li Y., Liu M., Wu X., Li Y.
      Biochem. Biophys. Res. Commun. 347:288-296(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZNF540.
    11. "Crosstalk between Src and major vault protein in epidermal growth factor-dependent cell signalling."
      Kim E., Lee S., Mian M.F., Yun S.U., Song M., Yi K.-S., Ryu S.H., Suh P.-G.
      FEBS J. 273:793-804(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SRC, TYROSINE PHOSPHORYLATION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    12. "The major vault protein is responsive to and interferes with interferon-gamma-mediated STAT1 signals."
      Steiner E., Holzmann K., Pirker C., Elbling L., Micksche M., Sutterluety H., Berger W.
      J. Cell Sci. 119:459-469(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, FUNCTION.
    13. "Regulatory role of human AP-endonuclease (APE1/Ref-1) in YB-1-mediated activation of the multidrug resistance gene MDR1."
      Chattopadhyay R., Das S., Maiti A.K., Boldogh I., Xie J., Hazra T.K., Kohno K., Mitra S., Bhakat K.K.
      Mol. Cell. Biol. 28:7066-7080(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APEX1.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Solution structure of a two-repeat fragment of major vault protein."
      Kozlov G., Vavelyuk O., Minailiuc O., Banville D., Gehring K., Ekiel I.
      J. Mol. Biol. 356:444-452(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 113-221, INTERACTION WITH PARP4.

    Entry informationi

    Entry nameiMVP_HUMAN
    AccessioniPrimary (citable) accession number: Q14764
    Secondary accession number(s): Q96BG4
    , Q9BPW6, Q9BQT1, Q9UBD1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 133 of the entry and version 4 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3