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Protein

Major vault protein

Gene

MVP

Organism
Homo sapiens (Human)
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.3 Publications

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB
  • protein phosphatase binding Source: UniProtKB

GO - Biological processi

  • cell proliferation Source: Ensembl
  • ERBB signaling pathway Source: UniProtKB
  • mRNA transport Source: UniProtKB-KW
  • negative regulation of protein autophosphorylation Source: UniProtKB
  • negative regulation of protein tyrosine kinase activity Source: UniProtKB
  • negative regulation of signaling Source: UniProtKB
  • protein activation cascade Source: Ensembl
  • protein transport Source: UniProtKB-KW
Complete GO annotation...

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 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:7531. MVP.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytoskeleton Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • membrane Source: UniProtKB
  • nuclear pore Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • ribonucleoprotein complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nuclear pore complex, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31332.

Polymorphism and mutation databases

BioMutaiMVP.
DMDMi21542417.

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
Modified residuei445 – 4451Phosphoserine1 Publication

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

BgeeiQ14764.
CleanExiHS_MVP.
ExpressionAtlasiQ14764. baseline and differential.
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. 70 interactions.
IntActiQ14764. 19 interactions.
MINTiMINT-5004583.
STRINGi9606.ENSP00000349977.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MATEEFIIRI PPYHYIHVLD QNSNVSRVEV GPKTYIRQDN ERVLFAPMRM
60 70 80 90 100
VTVPPRHYCT VANPVSRDAQ GLVLFDVTGQ VRLRHADLEI RLAQDPFPLY
110 120 130 140 150
PGEVLEKDIT PLQVVLPNTA LHLKALLDFE DKDGDKVVAG DEWLFEGPGT
160 170 180 190 200
YIPRKEVEVV EIIQATIIRQ NQALRLRARK ECWDRDGKER VTGEEWLVTT
210 220 230 240 250
VGAYLPAVFE EVLDLVDAVI LTEKTALHLR ARRNFRDFRG VSRRTGEEWL
260 270 280 290 300
VTVQDTEAHV PDVHEEVLGV VPITTLGPHN YCVILDPVGP DGKNQLGQKR
310 320 330 340 350
VVKGEKSFFL QPGEQLEQGI QDVYVLSEQQ GLLLRALQPL EEGEDEEKVS
360 370 380 390 400
HQAGDHWLIR GPLEYVPSAK VEVVEERQAI PLDENEGIYV QDVKTGKVRA
410 420 430 440 450
VIGSTYMLTQ DEVLWEKELP PGVEELLNKG QDPLADRGEK DTAKSLQPLA
460 470 480 490 500
PRNKTRVVSY RVPHNAAVQV YDYREKRARV VFGPELVSLG PEEQFTVLSL
510 520 530 540 550
SAGRPKRPHA RRALCLLLGP DFFTDVITIE TADHARLQLQ LAYNWHFEVN
560 570 580 590 600
DRKDPQETAK LFSVPDFVGD ACKAIASRVR GAVASVTFDD FHKNSARIIR
610 620 630 640 650
TAVFGFETSE AKGPDGMALP RPRDQAVFPQ NGLVVSSVDV QSVEPVDQRT
660 670 680 690 700
RDALQRSVQL AIEITTNSQE AAAKHEAQRL EQEARGRLER QKILDQSEAE
710 720 730 740 750
KARKELLELE ALSMAVESTG TAKAEAESRA EAARIEGEGS VLQAKLKAQA
760 770 780 790 800
LAIETEAELQ RVQKVRELEL VYARAQLELE VSKAQQLAEV EVKKFKQMTE
810 820 830 840 850
AIGPSTIRDL AVAGPEMQVK LLQSLGLKST LITDGSTPIN LFNTAFGLLG
860 870 880 890
MGPEGQPLGR RVASGPSPGE GISPQSAQAP QAPGDNHVVP VLR
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:
EMBLi
GenBanki
DDBJi
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_001280133.1. NM_001293204.1.
NP_001280134.1. NM_001293205.1.
NP_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.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001280133.1. NM_001293204.1.
NP_001280134.1. NM_001293205.1.
NP_005106.2. NM_005115.4.
NP_059447.2. NM_017458.3.
UniGeneiHs.632177.

3D structure databases

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

Protein-protein interaction databases

BioGridi115286. 70 interactions.
IntActiQ14764. 19 interactions.
MINTiMINT-5004583.
STRINGi9606.ENSP00000349977.

PTM databases

PhosphoSiteiQ14764.

Polymorphism and mutation databases

BioMutaiMVP.
DMDMi21542417.

2D gel databases

OGPiQ14764.
REPRODUCTION-2DPAGEIPI00000105.

Proteomic databases

MaxQBiQ14764.
PaxDbiQ14764.
PeptideAtlasiQ14764.
PRIDEiQ14764.

Protocols and materials databases

DNASUi9961.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi9961.
GeneCardsiGC16P029831.
HGNCiHGNC:7531. MVP.
HPAiCAB002752.
CAB022717.
HPA002321.
MIMi605088. gene.
neXtProtiNX_Q14764.
PharmGKBiPA31332.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

SignaLinkiQ14764.

Miscellaneous databases

EvolutionaryTraceiQ14764.
GeneWikiiMajor_vault_protein.
GenomeRNAii9961.
NextBioi37586.
PROiQ14764.
SOURCEiSearch...

Gene expression databases

BgeeiQ14764.
CleanExiHS_MVP.
ExpressionAtlasiQ14764. baseline and differential.
GenevestigatoriQ14764.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  18. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. "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: May 27, 2015
This is version 139 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

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 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.