Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Major vault protein

Gene

Mvp

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

  • cell proliferation Source: UniProtKB
  • ERBB signaling pathway Source: MGI
  • negative regulation of protein autophosphorylation Source: MGI
  • negative regulation of protein tyrosine kinase activity Source: MGI
  • negative regulation of signaling Source: MGI
  • protein activation cascade Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Names & Taxonomyi

Protein namesi
Recommended name:
Major vault protein
Short name:
MVP
Gene namesi
Name:Mvp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1925638. Mvp.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 861860Major vault proteinPRO_0000158981Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei421 – 4211PhosphoserineBy similarity
Cross-linki444 – 444Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

Post-translational modificationi

Phosphorylated on Tyr residues after EGF stimulation.By similarity
Dephosphorylated by PTPN11.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9EQK5.
MaxQBiQ9EQK5.
PaxDbiQ9EQK5.
PeptideAtlasiQ9EQK5.
PRIDEiQ9EQK5.

2D gel databases

REPRODUCTION-2DPAGEQ9EQK5.

PTM databases

iPTMnetiQ9EQK5.
PhosphoSiteiQ9EQK5.

Expressioni

Gene expression databases

BgeeiQ9EQK5.
CleanExiMM_MVP.

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 PTEN and activated MAPK1. The phosphorylated protein interacts with the SH2 domains of PTPN11 and SRC. Interacts with APEX1 (By similarity). May interact with ZNF540 (By similarity). Interacts with TEP1.By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ9EQK5. 5 interactions.
MINTiMINT-4102629.
STRINGi10090.ENSMUSP00000127250.

Structurei

Secondary structure

1
861
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 104Combined sources
Beta strandi14 – 207Combined sources
Turni21 – 233Combined sources
Beta strandi26 – 3611Combined sources
Beta strandi41 – 433Combined sources
Beta strandi51 – 533Combined sources
Beta strandi57 – 637Combined sources
Beta strandi77 – 793Combined sources
Beta strandi88 – 914Combined sources
Beta strandi93 – 975Combined sources
Beta strandi104 – 1118Combined sources
Beta strandi113 – 1153Combined sources
Beta strandi119 – 1279Combined sources
Beta strandi132 – 1343Combined sources
Beta strandi142 – 15110Combined sources
Beta strandi157 – 1648Combined sources
Beta strandi166 – 1683Combined sources
Beta strandi172 – 18312Combined sources
Beta strandi185 – 1873Combined sources
Beta strandi195 – 1984Combined sources
Beta strandi202 – 2043Combined sources
Beta strandi210 – 2178Combined sources
Beta strandi225 – 2339Combined sources
Beta strandi238 – 2403Combined sources
Beta strandi248 – 2514Combined sources
Turni253 – 2553Combined sources
Beta strandi257 – 2593Combined sources
Beta strandi265 – 2728Combined sources
Beta strandi274 – 2763Combined sources
Beta strandi280 – 2867Combined sources
Beta strandi290 – 2923Combined sources
Beta strandi299 – 30810Combined sources
Beta strandi315 – 3228Combined sources
Beta strandi324 – 3263Combined sources
Beta strandi331 – 3366Combined sources
Beta strandi356 – 3594Combined sources
Beta strandi361 – 3655Combined sources
Beta strandi369 – 3779Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GF5X-ray2.50A/B1-383[»]
3GNFX-ray2.10B1-383[»]
3GNGX-ray3.00A1-383[»]
ProteinModelPortaliQ9EQK5.
SMRiQ9EQK5. Positions 1-815.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9EQK5.

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.By similarity
MVP 4 mediates interaction with PARP4.By similarity

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IF6T. Eukaryota.
ENOG410ZCU8. LUCA.
HOVERGENiHBG003499.
InParanoidiQ9EQK5.

Family and domain databases

InterProiIPR021870. MVP_shoulder.
IPR002499. Vault_N.
[Graphical view]
PfamiPF11978. MVP_shoulder. 1 hit.
PF01505. Vault. 4 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.

Q9EQK5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATEEAIIRI PPYHYIHVLD QNSNVSRVEV GPKTYIRQDN ERVLFAPVRM
60 70 80 90 100
VTVPPRHYCI VANPVSRDAQ SSVLFDVTGQ VRLRHADQEI RLAQDPFPLY
110 120 130 140 150
PGELLEKDIT PLQVVLPNTA LHLKALLDFE DKNGDKVMAG DEWLFEGPGT
160 170 180 190 200
YIPQKEVEVV EIIQATVIKQ NQALRLRARK ECFDRDGKER VTGEEWLVRS
210 220 230 240 250
VGAYLPAVFE EVLDLVDAVI LTEKTALHLR ARQNFKDLRG VAHRTGEEWL
260 270 280 290 300
VTVQDTEAHV PDVYEEVLGV VPITTLGPRH YCVILDPMGP DGKNQLGQKR
310 320 330 340 350
VVKGEKSFFL QPGERLERGI QDVYVLSEQQ GLLLKALQPL EEGEGEEKVA
360 370 380 390 400
HQAGDRWLIR GPLEYVPSAK VEVVEERQAI PLDQNEGIYV QDVKTGKVRA
410 420 430 440 450
VIGSTYMLTQ DEVLWEKELP SGVEELLNLG HDPLADRGQK GTAKVLQPSA
460 470 480 490 500
ARNKTRVVSY RVPHNAAVQV YDYRAKRARV VFGPELVSLD PEEQFTVLSL
510 520 530 540 550
SAGRPKRPHA RRALCLLLGP DFFTDVITIE TADHARLQLQ LAYNWHFELK
560 570 580 590 600
NRNDPEETAK LFSVPDFVGD ACKAIASRVR GAVASVTFDD FHKNSARIIR
610 620 630 640 650
MAVFGFEMSE DAGPDGALLP RARDRAVFPQ NGLVVSSVDV QSVEPVDQRT
660 670 680 690 700
RDALQRSVQL AIEITTNSQE AAAKHEAQRL EQEARGRLER QKILDQSEAE
710 720 730 740 750
KARKELLELE AMSMAVESTG NAKAEAESRA EAARIEGEGS VLQAKLKAQA
760 770 780 790 800
LAIETEAELE RVKKVREMEL IYSRAQLELE VSKAQQLADV EAKKFKEMTE
810 820 830 840 850
ALGPGTIRDL AVAGPEMQVK LLQSLGLKST LITDGSSPIN LFNTAFGLLG
860
LGSDGQPPVQ K
Length:861
Mass (Da):95,924
Last modified:July 27, 2011 - v4
Checksum:iB722F4FA747CA378
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti348 – 3481K → R in AAG43520 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF210456 mRNA. Translation: AAG43520.1.
AY046318 Genomic DNA. Translation: AAL02325.1.
CH466531 Genomic DNA. Translation: EDL17488.1.
CH466531 Genomic DNA. Translation: EDL17489.1.
BC006709 mRNA. Translation: AAH06709.1.
RefSeqiXP_011240254.1. XM_011241952.1.
UniGeneiMm.228797.

Genome annotation databases

GeneIDi78388.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF210456 mRNA. Translation: AAG43520.1.
AY046318 Genomic DNA. Translation: AAL02325.1.
CH466531 Genomic DNA. Translation: EDL17488.1.
CH466531 Genomic DNA. Translation: EDL17489.1.
BC006709 mRNA. Translation: AAH06709.1.
RefSeqiXP_011240254.1. XM_011241952.1.
UniGeneiMm.228797.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GF5X-ray2.50A/B1-383[»]
3GNFX-ray2.10B1-383[»]
3GNGX-ray3.00A1-383[»]
ProteinModelPortaliQ9EQK5.
SMRiQ9EQK5. Positions 1-815.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9EQK5. 5 interactions.
MINTiMINT-4102629.
STRINGi10090.ENSMUSP00000127250.

PTM databases

iPTMnetiQ9EQK5.
PhosphoSiteiQ9EQK5.

2D gel databases

REPRODUCTION-2DPAGEQ9EQK5.

Proteomic databases

EPDiQ9EQK5.
MaxQBiQ9EQK5.
PaxDbiQ9EQK5.
PeptideAtlasiQ9EQK5.
PRIDEiQ9EQK5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi78388.

Organism-specific databases

CTDi9961.
MGIiMGI:1925638. Mvp.

Phylogenomic databases

eggNOGiENOG410IF6T. Eukaryota.
ENOG410ZCU8. LUCA.
HOVERGENiHBG003499.
InParanoidiQ9EQK5.

Miscellaneous databases

ChiTaRSiMvp. mouse.
EvolutionaryTraceiQ9EQK5.
PROiQ9EQK5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9EQK5.
CleanExiMM_MVP.

Family and domain databases

InterProiIPR021870. MVP_shoulder.
IPR002499. Vault_N.
[Graphical view]
PfamiPF11978. MVP_shoulder. 1 hit.
PF01505. Vault. 4 hits.
[Graphical view]
PROSITEiPS51224. MVP. 8 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of the major vault protein and vault RNA from Mus musculus."
    Wiemer E.A.C., Mossink M.H., van Zon A., Schoester M., de Boevere M., Scheper R.J., Sonneveld P.
    Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  5. "The telomerase/vault-associated protein TEP1 is required for vault RNA stability and its association with the vault particle."
    Kickhoefer V.A., Liu Y., Kong L.B., Snow B.E., Stewart P.L., Harrington L., Rome L.H.
    J. Cell Biol. 152:157-164(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH TEP1.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  7. "The mechanism of vault opening from the high resolution structure of the N-terminal repeats of MVP."
    Querol-Audi J., Casanas A., Uson I., Luque D., Caston J.R., Fita I., Verdaguer N.
    EMBO J. 28:3450-3457(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-383, SUBUNIT.

Entry informationi

Entry nameiMVP_MOUSE
AccessioniPrimary (citable) accession number: Q9EQK5
Secondary accession number(s): Q922X6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 101 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.