CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012387
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Major vault protein 
Protein Synonyms/Alias
 MVP; Lung resistance-related protein 
Gene Name
 MVP 
Gene Synonyms/Alias
 LRP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
107YPGEVLEKDITPLQVubiquitination[1]
370LEYVPSAKVEVVEERubiquitination[1, 2, 3]
440PLADRGEKDTAKSLQubiquitination[3, 4]
444RGEKDTAKSLQPLAPubiquitination[1, 2, 3, 4, 5, 6, 7]
593VTFDDFHKNSARIIRubiquitination[1]
674NSQEAAAKHEAQRLEubiquitination[2]
745EGSVLQAKLKAQALAacetylation[8]
745EGSVLQAKLKAQALAubiquitination[1, 3]
747SVLQAKLKAQALAIEubiquitination[1, 2, 3]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [5] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [6] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [7] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [8] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 
Functional Description
 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. 
Sequence Annotation
 REPEAT 2 56 MVP 1.
 REPEAT 57 111 MVP 2.
 REPEAT 112 164 MVP 3.
 REPEAT 165 217 MVP 4.
 REPEAT 218 272 MVP 5.
 REPEAT 273 323 MVP 6.
 REPEAT 324 379 MVP 7.
 REPEAT 380 457 MVP 8.
 REPEAT 458 520 MVP 9.
 MOD_RES 2 2 N-acetylalanine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein; Polymorphism; Protein transport; Reference proteome; Repeat; Ribonucleoprotein; Translocation; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 893 AA 
Protein Sequence
MATEEFIIRI PPYHYIHVLD QNSNVSRVEV GPKTYIRQDN ERVLFAPMRM VTVPPRHYCT 60
VANPVSRDAQ GLVLFDVTGQ VRLRHADLEI RLAQDPFPLY PGEVLEKDIT PLQVVLPNTA 120
LHLKALLDFE DKDGDKVVAG DEWLFEGPGT YIPRKEVEVV EIIQATIIRQ NQALRLRARK 180
ECWDRDGKER VTGEEWLVTT VGAYLPAVFE EVLDLVDAVI LTEKTALHLR ARRNFRDFRG 240
VSRRTGEEWL VTVQDTEAHV PDVHEEVLGV VPITTLGPHN YCVILDPVGP DGKNQLGQKR 300
VVKGEKSFFL QPGEQLEQGI QDVYVLSEQQ GLLLRALQPL EEGEDEEKVS HQAGDHWLIR 360
GPLEYVPSAK VEVVEERQAI PLDENEGIYV QDVKTGKVRA VIGSTYMLTQ DEVLWEKELP 420
PGVEELLNKG QDPLADRGEK DTAKSLQPLA PRNKTRVVSY RVPHNAAVQV YDYREKRARV 480
VFGPELVSLG PEEQFTVLSL SAGRPKRPHA RRALCLLLGP DFFTDVITIE TADHARLQLQ 540
LAYNWHFEVN DRKDPQETAK LFSVPDFVGD ACKAIASRVR GAVASVTFDD FHKNSARIIR 600
TAVFGFETSE AKGPDGMALP RPRDQAVFPQ NGLVVSSVDV QSVEPVDQRT RDALQRSVQL 660
AIEITTNSQE AAAKHEAQRL EQEARGRLER QKILDQSEAE KARKELLELE ALSMAVESTG 720
TAKAEAESRA EAARIEGEGS VLQAKLKAQA LAIETEAELQ RVQKVRELEL VYARAQLELE 780
VSKAQQLAEV EVKKFKQMTE AIGPSTIRDL AVAGPEMQVK LLQSLGLKST LITDGSTPIN 840
LFNTAFGLLG MGPEGQPLGR RVASGPSPGE GISPQSAQAP QAPGDNHVVP VLR 893 
Gene Ontology
 GO:0005856; C:cytoskeleton; IDA:UniProtKB.
 GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
 GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
 GO:0030529; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
 GO:0019903; F:protein phosphatase binding; IDA:UniProtKB.
 GO:0038127; P:ERBB signaling pathway; IDA:UniProtKB.
 GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
 GO:0031953; P:negative regulation of protein autophosphorylation; IDA:UniProtKB.
 GO:0061099; P:negative regulation of protein tyrosine kinase activity; IDA:UniProtKB.
 GO:0023057; P:negative regulation of signaling; IDA:UniProtKB.
 GO:0015031; P:protein transport; IEA:UniProtKB-KW. 
Interpro
 IPR021870; MVP_shoulder.
 IPR002499; Vault_N. 
Pfam
 PF11978; MVP_shoulder
 PF01505; Vault 
SMART
  
PROSITE
 PS51224; MVP 
PRINTS