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UniProtKB - Q14764 (MVP_HUMAN)

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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 IFNG-mediated STAT1 signaling and subsequent activation of JAK. Down-regulates SRC activity and signaling through MAP kinases.3 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein kinase binding Source: UniProtKB
  • protein phosphatase binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  • 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
  • neutrophil degranulation Source: Reactome
  • protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywordsi

Molecular functionRibonucleoprotein
Biological processmRNA transport, Protein transport, Translocation, Transport

Enzyme and pathway databases

ReactomeiR-HSA-6798695. Neutrophil degranulation.
SignaLinkiQ14764.

Protein family/group databases

TCDBi1.I.1.1.3. the nuclear pore complex (npc) family.

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:7531. MVP.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytoskeleton Source: UniProtKB
  • cytosol Source: HPA
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • ficolin-1-rich granule lumen Source: Reactome
  • intracellular ribonucleoprotein complex Source: UniProtKB-KW
  • membrane Source: UniProtKB
  • nuclear pore Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • secretory granule lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nuclear pore complex, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi9961.
OpenTargetsiENSG00000013364.
PharmGKBiPA31332.

Polymorphism and mutation databases

BioMutaiMVP.
DMDMi21542417.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00001589802 – 893Major vault proteinAdd BLAST892

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Cross-linki444Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei445PhosphoserineCombined sources1
Cross-linki704Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ14764.
PaxDbiQ14764.
PeptideAtlasiQ14764.
PRIDEiQ14764.

2D gel databases

OGPiQ14764.
REPRODUCTION-2DPAGEiIPI00000105.

PTM databases

iPTMnetiQ14764.
PhosphoSitePlusiQ14764.
SwissPalmiQ14764.

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

BgeeiENSG00000013364.
CleanExiHS_MVP.
ExpressionAtlasiQ14764. baseline and differential.
GenevisibleiQ14764. HS.

Organism-specific databases

HPAiCAB002752.
CAB022717.
HPA002321.
HPA064740.

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

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-2816254,EBI-2816254

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein kinase binding Source: UniProtKB
  • protein phosphatase binding Source: UniProtKB
Complete GO annotation...

Protein-protein interaction databases

BioGridi115286. 93 interactors.
IntActiQ14764. 39 interactors.
MINTiMINT-5004583.
STRINGi9606.ENSP00000349977.

Structurei

Secondary structure

1893
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi120 – 125Combined sources6
Beta strandi137 – 139Combined sources3
Beta strandi141 – 147Combined sources7
Helixi148 – 150Combined sources3
Beta strandi157 – 163Combined sources7
Beta strandi170 – 181Combined sources12
Beta strandi185 – 187Combined sources3
Beta strandi195 – 198Combined sources4
Beta strandi208 – 217Combined sources10

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ14764.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati2 – 56MVP 1Add BLAST55
Repeati57 – 111MVP 2Add BLAST55
Repeati112 – 164MVP 3Add BLAST53
Repeati165 – 217MVP 4Add BLAST53
Repeati218 – 272MVP 5Add BLAST55
Repeati273 – 323MVP 6Add BLAST51
Repeati324 – 379MVP 7Add BLAST56
Repeati380 – 457MVP 8Add BLAST78
Repeati458 – 520MVP 9Add BLAST63

Domaini

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IF6T. Eukaryota.
ENOG410ZCU8. LUCA.
GeneTreeiENSGT00390000008969.
HOGENOMiHOG000255109.
HOVERGENiHBG003499.
InParanoidiQ14764.
KOiK17266.
OMAiVFPQNGL.
OrthoDBiEOG091G032A.
PhylomeDBiQ14764.
TreeFamiTF329353.

Family and domain databases

CDDicd08825. MVP_shoulder. 1 hit.
InterProiView protein in InterPro
IPR021870. MVP_shoulder.
IPR002499. Vault_N.
PfamiView protein in Pfam
PF11978. MVP_shoulder. 1 hit.
PF01505. Vault. 4 hits.
PROSITEiView protein in PROSITE
PS51224. MVP. 8 hits.

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_050179635V → I. Corresponds to variant dbSNP:rs35916172Ensembl.1
Natural variantiVAR_050180651R → Q. Corresponds to variant dbSNP:rs3764944Ensembl.1

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.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiMVP_HUMAN
AccessioniPrimary (citable) accession number: Q14764
Secondary accession number(s): Q96BG4
, Q9BPW6, Q9BQT1, Q9UBD1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: August 30, 2017
This is version 160 of the entry and version 4 of the sequence. See 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