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Protein

Latent membrane protein 1

Gene

LMP1

Organism
Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a CD40 functional homolog to prevent apoptosis of infected B-lymphocytes and drive their proliferation. Functions as a constitutively active tumor necrosis factor receptor that induces the activation of several signaling pathways, including those of the NF-kappa-B family. LMP1 signaling leads to up-regulation of antiapoptotic proteins and provide growth signals in latently infected cells. Interacts with host UBE2I and subsequently affects the sumoylation state of several cellular proteins. For example, induces the sumoylation of host IRF7 thereby limiting its transcriptional activity and modulating the activation of innate immune responses.3 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Activation of host NF-kappa-B by virus, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host RLR pathway by virus, Inhibition of host TRAFs by virus, Inhibition of host TYK2 by virus, Viral immunoevasion

Names & Taxonomyi

Protein namesi
Recommended name:
Latent membrane protein 1
Short name:
LMP-1
Alternative name(s):
Protein p63
Cleaved into the following chain:
Gene namesi
Name:LMP1
ORF Names:BNLF1
OrganismiEpstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Taxonomic identifieri10377 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeGammaherpesvirinaeLymphocryptovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000007640 Componenti: Genome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 2322CytoplasmicAdd
BLAST
Transmembranei24 – 4421HelicalSequence analysisAdd
BLAST
Topological domaini45 – 517Extracellular
Transmembranei52 – 7221HelicalSequence analysisAdd
BLAST
Topological domaini73 – 753Cytoplasmic
Transmembranei76 – 9621HelicalSequence analysisAdd
BLAST
Topological domaini97 – 10610Extracellular
Transmembranei107 – 12721HelicalSequence analysisAdd
BLAST
Topological domaini128 – 13912CytoplasmicAdd
BLAST
Transmembranei140 – 16021HelicalSequence analysisAdd
BLAST
Topological domaini161 – 1633Extracellular
Transmembranei164 – 18421HelicalSequence analysisAdd
BLAST
Topological domaini185 – 386202CytoplasmicAdd
BLAST

GO - Cellular componenti

  • host cell membrane Source: CACAO
  • host cell plasma membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi330 – 3301K → R: No effect on ubiquitination and proteasomal degradation. 1 Publication

Keywords - Diseasei

Oncogene

Chemistry

ChEMBLiCHEMBL1795089.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCurated
Chaini2 – 386385Latent membrane protein 1PRO_0000038310Add
BLAST
Chaini242 – 386145Protein p25PRO_0000038311Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylglutamate; by hostCurated

Post-translational modificationi

Ubiquitinated on the N-terminus.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

PTM databases

iPTMnetiP03230.
SwissPalmiP03230.

Interactioni

Subunit structurei

Interacts (via PXQXT motif) with host tumor necrosis factor receptor-associated factor (TRAF) proteins TRAF1, TRAF2, TRAF3 and TRAF5. Interacts with human protein ZMYND11; leading to negatively regulate NF-kappa-B activation. Interacts with host UBE2I; this interaction induces the sumoylation of various cellular proteins. Interacts with host IRF7.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RABAC1Q9UI149EBI-6973030,EBI-712367From a different organism.
UBE2IP632795EBI-6973030,EBI-80168From a different organism.
ZMYND11Q153263EBI-6973030,EBI-2623509From a different organism.

Protein-protein interaction databases

BioGridi971792. 6 interactions.
DIPiDIP-29603N.
DIP-43767N.
IntActiP03230. 6 interactions.
MINTiMINT-1509916.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CZYX-ray2.00D/E204-210[»]
ProteinModelPortaliP03230.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03230.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni194 – 23239CTAR1Add
BLAST
Regioni351 – 38636CTAR2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi204 – 2085Interaction with host TRAF proteins

Domaini

Two regions, C-terminal-activating region 1 (CTAR1) and CTAR2, have been identified within the cytoplasmic carboxy terminal domain that activates NF-kappa-B.1 Publication

Sequence similaritiesi

Belongs to the herpesviridae LMP-1 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

KOiK19459.

Family and domain databases

InterProiIPR007961. Herpes_LMP1.
[Graphical view]
PfamiPF05297. Herpes_LMP1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P03230-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEHDLERGPP GPRRPPRGPP LSSSLGLALL LLLLALLFWL YIVMSDWTGG
60 70 80 90 100
ALLVLYSFAL MLIIIILIIF IFRRDLLCPL GALCILLLMI TLLLIALWNL
110 120 130 140 150
HGQALFLGIV LFIFGCLLVL GIWIYLLEML WRLGATIWQL LAFFLAFFLD
160 170 180 190 200
LILLIIALYL QQNWWTLLVD LLWLLLFLAI LIWMYYHGQR HSDEHHHDDS
210 220 230 240 250
LPHPQQATDD SGHESDSNSN EGRHHLLVSG AGDGPPLCSQ NLGAPGGGPD
260 270 280 290 300
NGPQDPDNTD DNGPQDPDNT DDNGPHDPLP QDPDNTDDNG PQDPDNTDDN
310 320 330 340 350
GPHDPLPHSP SDSAGNDGGP PQLTEEVENK GGDQGPPLMT DGGGGHSHDS
360 370 380
GHGGGDPHLP TLLLGSSGSG GDDDDPHGPV QLSYYD
Length:386
Mass (Da):41,982
Last modified:July 21, 1986 - v1
Checksum:i1E19446E857DB8A3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01995 Genomic DNA. Translation: CAA26023.1.
K02165 Genomic DNA. Translation: AAA45888.1.
V01555 Genomic DNA. No translation available.
AJ507799 Genomic DNA. Translation: CAD53472.1.
PIRiD43045. QQBE50.
RefSeqiYP_401722.1. NC_007605.1.

Genome annotation databases

GeneIDi3783750.
KEGGivg:3783750.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01995 Genomic DNA. Translation: CAA26023.1.
K02165 Genomic DNA. Translation: AAA45888.1.
V01555 Genomic DNA. No translation available.
AJ507799 Genomic DNA. Translation: CAD53472.1.
PIRiD43045. QQBE50.
RefSeqiYP_401722.1. NC_007605.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CZYX-ray2.00D/E204-210[»]
ProteinModelPortaliP03230.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi971792. 6 interactions.
DIPiDIP-29603N.
DIP-43767N.
IntActiP03230. 6 interactions.
MINTiMINT-1509916.

Chemistry

ChEMBLiCHEMBL1795089.

PTM databases

iPTMnetiP03230.
SwissPalmiP03230.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3783750.
KEGGivg:3783750.

Phylogenomic databases

KOiK19459.

Miscellaneous databases

EvolutionaryTraceiP03230.

Family and domain databases

InterProiIPR007961. Herpes_LMP1.
[Graphical view]
PfamiPF05297. Herpes_LMP1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of an mRNA transcribed in latent growth-transforming virus infection indicates that it may encode a membrane protein."
    Fennewald S., van Santen V., Kieff E.
    J. Virol. 51:411-419(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Two related but differentially expressed potential membrane proteins encoded by the EcoRI Dhet region of Epstein-Barr virus B95-8."
    Hudson G.S., Farrell P.J., Barrell B.G.
    J. Virol. 53:528-535(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Posttranslational processing of an Epstein-Barr virus-encoded membrane protein expressed in cells transformed by Epstein-Barr virus."
    Baichwal V.R., Sudgen B.
    J. Virol. 61:866-875(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  5. "Transformation of Balb 3T3 cells by the BNLF-1 gene of Epstein-Barr virus."
    Baichwal V.R., Sudgen B.
    Oncogene 2:461-467(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: TRANSFORMING PROPERTIES.
  6. "Processing of the Epstein-Barr virus-encoded latent membrane protein p63/LMP."
    Moorthy R., Thorley-Lawson D.A.
    J. Virol. 64:829-837(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING.
  7. "The Epstein-Barr virus latent membrane protein-1 (LMP1) mediates activation of NF-kappa B and cell surface phenotype via two effector regions in its carboxy-terminal cytoplasmic domain."
    Huen D.S., Henderson S.A., Croom-Carter D., Rowe M.
    Oncogene 10:549-560(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN CTAR1 AND CTAR2.
  8. "Degradation of the epstein-barr virus latent membrane protein 1 (LMP1) by the ubiquitin-proteasome pathway. Targeting via ubiquitination of the N-terminal residue."
    Aviel S., Winberg G., Massucci M., Ciechanover A.
    J. Biol. Chem. 275:23491-23499(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-330, UBIQUITINATION.
  9. "BS69, a specific adaptor in the latent membrane protein 1-mediated c-Jun N-terminal kinase pathway."
    Wan J., Zhang W., Wu L., Bai T., Zhang M., Lo K.W., Chui Y.L., Cui Y., Tao Q., Yamamoto M., Akira S., Wu Z.
    Mol. Cell. Biol. 26:448-456(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HOST PROTEIN ZMYND11.
  10. "IRF7 activation by Epstein-Barr virus latent membrane protein 1 requires localization at activation sites and TRAF6, but not TRAF2 or TRAF3."
    Song Y.J., Izumi K.M., Shinners N.P., Gewurz B.E., Kieff E.
    Proc. Natl. Acad. Sci. U.S.A. 105:18448-18453(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HOST IRF7.
  11. "BS69 negatively regulates the canonical NF-kappaB activation induced by Epstein-Barr virus-derived LMP1."
    Ikeda O., Sekine Y., Mizushima A., Oritani K., Yasui T., Fujimuro M., Muromoto R., Nanbo A., Matsuda T.
    FEBS Lett. 583:1567-1574(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HOST PROTEIN ZMYND11.
  12. "BS69 cooperates with TRAF3 in the regulation of Epstein-Barr virus-derived LMP1/CTAR1-induced NF-kappaB activation."
    Ikeda O., Miyasaka Y., Yoshida R., Mizushima A., Oritani K., Sekine Y., Kuroda M., Yasui T., Fujimuro M., Muromoto R., Nanbo A., Matsuda T.
    FEBS Lett. 584:865-872(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HOST PROTEIN ZMYND11.
  13. "Epstein-Barr virus latent membrane protein 1 (LMP1) C-terminal-activating region 3 contributes to LMP1-mediated cellular migration via its interaction with Ubc9."
    Bentz G.L., Whitehurst C.B., Pagano J.S.
    J. Virol. 85:10144-10153(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HOST UBE2I.
  14. "Epstein-Barr virus latent membrane protein 1 regulates the function of interferon regulatory factor 7 by inducing its sumoylation."
    Bentz G.L., Shackelford J., Pagano J.S.
    J. Virol. 86:12251-12261(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "NF-kappaB and IRF7 pathway activation by Epstein-Barr virus Latent Membrane Protein 1."
    Ersing I., Bernhardt K., Gewurz B.E.
    Viruses 5:1587-1606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  16. "Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation."
    Richardson J.S., Richardson D.C.
    Proc. Natl. Acad. Sci. U.S.A. 99:2754-2759(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 204-210.

Entry informationi

Entry nameiLMP1_EBVB9
AccessioniPrimary (citable) accession number: P03230
Secondary accession number(s): Q777A4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 11, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.