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Q14764 (MVP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Major vault protein

Short name=MVP
Alternative name(s):
Lung resistance-related protein
Gene names
Name:MVP
Synonyms:LRP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length893 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.11 Ref.12

Subunit structure

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. Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.18

Subcellular location

Cytoplasm. Nucleusnuclear pore complex. Note: 5% found in the nuclear pore complex. Translocates from the nucleus to the cytoplasm upon EGF treatment. Ref.9 Ref.11

Tissue specificity

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.

Induction

Up-regulated by IFNG/IFN-gamma. Ref.12

Domain

MVP 3 mediates interaction with PTEN.

MVP 4 mediates interaction with PARP4.

Post-translational modification

Phosphorylated on Tyr residues after EGF stimulation. Ref.9 Ref.11

Dephosphorylated by PTPN11. Ref.9 Ref.11

Sequence similarities

Contains 9 MVP (vault) repeats.

Ontologies

Keywords
   Biological processmRNA transport
Protein transport
Translocation
Transport
   Cellular componentCytoplasm
Nuclear pore complex
Nucleus
   Coding sequence diversityPolymorphism
   DomainRepeat
   Molecular functionRibonucleoprotein
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processERBB signaling pathway

Inferred from direct assay Ref.9. Source: UniProtKB

cell proliferation

Inferred from electronic annotation. Source: Ensembl

mRNA transport

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of protein autophosphorylation

Inferred from direct assay Ref.11. Source: UniProtKB

negative regulation of protein tyrosine kinase activity

Inferred from direct assay Ref.11. Source: UniProtKB

negative regulation of signaling

Inferred from direct assay Ref.11. Source: UniProtKB

protein activation cascade

Inferred from electronic annotation. Source: Ensembl

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay Ref.11. Source: UniProtKB

cytoskeleton

Inferred from direct assay Ref.11. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 21362503. Source: UniProtKB

nuclear pore

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.9Ref.11. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay Ref.11. Source: UniProtKB

ribonucleoprotein complex

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionprotein binding

Inferred from physical interaction Ref.9Ref.10Ref.13. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.11. Source: UniProtKB

protein phosphatase binding

Inferred from direct assay Ref.9. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 893892Major vault protein
PRO_0000158980

Regions

Repeat2 – 5655MVP 1
Repeat57 – 11155MVP 2
Repeat112 – 16453MVP 3
Repeat165 – 21753MVP 4
Repeat218 – 27255MVP 5
Repeat273 – 32351MVP 6
Repeat324 – 37956MVP 7
Repeat380 – 45778MVP 8
Repeat458 – 52063MVP 9

Amino acid modifications

Modified residue21N-acetylalanine Ref.6 Ref.16 Ref.17

Natural variations

Natural variant6351V → I.
Corresponds to variant rs35916172 [ dbSNP | Ensembl ].
VAR_050179
Natural variant6511R → Q.
Corresponds to variant rs3764944 [ dbSNP | Ensembl ].
VAR_050180

Secondary structure

.................. 893
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q14764 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 6FEE5545B0A3FE65

FASTA89399,327
        10         20         30         40         50         60 
MATEEFIIRI PPYHYIHVLD QNSNVSRVEV GPKTYIRQDN ERVLFAPMRM VTVPPRHYCT 

        70         80         90        100        110        120 
VANPVSRDAQ GLVLFDVTGQ VRLRHADLEI RLAQDPFPLY PGEVLEKDIT PLQVVLPNTA 

       130        140        150        160        170        180 
LHLKALLDFE DKDGDKVVAG DEWLFEGPGT YIPRKEVEVV EIIQATIIRQ NQALRLRARK 

       190        200        210        220        230        240 
ECWDRDGKER VTGEEWLVTT VGAYLPAVFE EVLDLVDAVI LTEKTALHLR ARRNFRDFRG 

       250        260        270        280        290        300 
VSRRTGEEWL VTVQDTEAHV PDVHEEVLGV VPITTLGPHN YCVILDPVGP DGKNQLGQKR 

       310        320        330        340        350        360 
VVKGEKSFFL QPGEQLEQGI QDVYVLSEQQ GLLLRALQPL EEGEDEEKVS HQAGDHWLIR 

       370        380        390        400        410        420 
GPLEYVPSAK VEVVEERQAI PLDENEGIYV QDVKTGKVRA VIGSTYMLTQ DEVLWEKELP 

       430        440        450        460        470        480 
PGVEELLNKG QDPLADRGEK DTAKSLQPLA PRNKTRVVSY RVPHNAAVQV YDYREKRARV 

       490        500        510        520        530        540 
VFGPELVSLG PEEQFTVLSL SAGRPKRPHA RRALCLLLGP DFFTDVITIE TADHARLQLQ 

       550        560        570        580        590        600 
LAYNWHFEVN DRKDPQETAK LFSVPDFVGD ACKAIASRVR GAVASVTFDD FHKNSARIIR 

       610        620        630        640        650        660 
TAVFGFETSE AKGPDGMALP RPRDQAVFPQ NGLVVSSVDV QSVEPVDQRT RDALQRSVQL 

       670        680        690        700        710        720 
AIEITTNSQE AAAKHEAQRL EQEARGRLER QKILDQSEAE KARKELLELE ALSMAVESTG 

       730        740        750        760        770        780 
TAKAEAESRA EAARIEGEGS VLQAKLKAQA LAIETEAELQ RVQKVRELEL VYARAQLELE 

       790        800        810        820        830        840 
VSKAQQLAEV EVKKFKQMTE AIGPSTIRDL AVAGPEMQVK LLQSLGLKST LITDGSTPIN 

       850        860        870        880        890 
LFNTAFGLLG MGPEGQPLGR RVASGPSPGE GISPQSAQAP QAPGDNHVVP VLR 

« Hide

References

« Hide 'large scale' references
[1]"The drug resistance-related protein LRP is the human major vault protein."
Scheffer G.L., Wijngaard P.L.J., Flens M.J., Izquierdo M.A., Slovak M.L., Pinedo H.M., Meijer C.J.L.M., Clevers H.C., Scheper R.J.
Nat. Med. 1:578-582(1995) [PubMed] [Europe PMC] [Abstract]
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]"Vaults and telomerase share a common subunit, TEP1."
Kickhoefer V.A., Stephen A.G., Harrington L., Robinson M.O., Rome L.H.
J. Biol. Chem. 274:32712-32717(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION WITH TEP1.
[8]"PTEN associates with the vault particles in HeLa cells."
Yu Z., Fotouhi-Ardakani N., Wu L., Maoui M., Wang S., Banville D., Shen S.-H.
J. Biol. Chem. 277:40247-40252(2002) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X79882 mRNA. Translation: CAA56256.2.
BC015623 mRNA. Translation: AAH15623.1.
AJ238512 expand/collapse EMBL AC list , AJ238514, AJ238516, AJ238518 Genomic DNA. Translation: CAB55354.1.
AJ238519 expand/collapse EMBL AC list , AJ238514, AJ238516, AJ238518 Genomic DNA. Translation: CAB55355.1.
AJ291365 Genomic DNA. Translation: CAC35313.1.
AJ291366 mRNA. Translation: CAC35314.1.
AJ291367 mRNA. Translation: CAC35316.1.
CCDSCCDS10656.1.
PIRS57723.
RefSeqNP_005106.2. NM_005115.4.
NP_059447.2. NM_017458.3.
UniGeneHs.632177.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y7XNMR-A113-221[»]
ProteinModelPortalQ14764.
SMRQ14764. Positions 1-815.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115286. 25 interactions.
IntActQ14764. 18 interactions.
MINTMINT-5004583.
STRING9606.ENSP00000349977.

PTM databases

PhosphoSiteQ14764.

Polymorphism databases

DMDM21542417.

2D gel databases

OGPQ14764.
REPRODUCTION-2DPAGEIPI00000105.

Proteomic databases

MaxQBQ14764.
PaxDbQ14764.
PeptideAtlasQ14764.
PRIDEQ14764.

Protocols and materials databases

DNASU9961.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000357402; ENSP00000349977; ENSG00000013364.
ENST00000395353; ENSP00000378760; ENSG00000013364.
GeneID9961.
KEGGhsa:9961.
UCSCuc002dui.3. human.

Organism-specific databases

CTD9961.
GeneCardsGC16P029831.
HGNCHGNC:7531. MVP.
HPACAB002752.
CAB022717.
HPA002321.
MIM605088. gene.
neXtProtNX_Q14764.
PharmGKBPA31332.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG70525.
HOGENOMHOG000255109.
HOVERGENHBG003499.
InParanoidQ14764.
KOK17266.
OMAQDPLADR.
OrthoDBEOG773XFB.
PhylomeDBQ14764.
TreeFamTF329353.

Enzyme and pathway databases

SignaLinkQ14764.

Gene expression databases

ArrayExpressQ14764.
BgeeQ14764.
CleanExHS_MVP.
GenevestigatorQ14764.

Family and domain databases

InterProIPR021870. MVP_shoulder.
IPR002499. Vault_N.
[Graphical view]
PfamPF11978. MVP_shoulder. 1 hit.
PF01505. Vault. 5 hits.
[Graphical view]
PROSITEPS51224. MVP. 8 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ14764.
GeneWikiMajor_vault_protein.
GenomeRNAi9961.
NextBio37586.
PROQ14764.
SOURCESearch...

Entry information

Entry nameMVP_HUMAN
AccessionPrimary (citable) accession number: Q14764
Secondary accession number(s): Q96BG4 expand/collapse secondary AC list , Q9BPW6, Q9BQT1, Q9UBD1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 132 of the entry and version 4 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM