UniProtKB - P03230 (LMP1_EBVB9)

BLAST

>sp|P03230|LMP1_EBVB9 Latent membrane protein 1 OS=Epstein-Barr virus (strain B95-8) OX=10377 GN=LMP1 PE=1 SV=1
MEHDLERGPPGPRRPPRGPPLSSSLGLALLLLLLALLFWLYIVMSDWTGGALLVLYSFAL
MLIIIILIIFIFRRDLLCPLGALCILLLMITLLLIALWNLHGQALFLGIVLFIFGCLLVL
GIWIYLLEMLWRLGATIWQLLAFFLAFFLDLILLIIALYLQQNWWTLLVDLLWLLLFLAI
LIWMYYHGQRHSDEHHHDDSLPHPQQATDDSGHESDSNSNEGRHHLLVSGAGDGPPLCSQ
NLGAPGGGPDNGPQDPDNTDDNGPQDPDNTDDNGPHDPLPQDPDNTDDNGPQDPDNTDDN
GPHDPLPHSPSDSAGNDGGPPQLTEEVENKGGDQGPPLMTDGGGGHSHDSGHGGGDPHLP
TLLLGSSGSGGDDDDPHGPVQLSYYD

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History
Entry version 106 (23 May 2018)
Sequence version 1 (21 Jul 1986)
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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: -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

activation by virus of host NF-kappaB transcription factor activity Source: UniProtKB-KW
suppression by virus of host TRAF activity Source: UniProtKB-KW
suppression by virus of host TYK2 activity Source: UniProtKB-KW
suppression by virus of host type I interferon-mediated signaling pathway Source: UniProtKB-KW
transformation of host cell by virus Source: InterPro

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Biological process	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

Biological process

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: Protein p25
Gene namesⁱ	Name:LMP1 ORF Names:BNLF1
Organismⁱ	Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Taxonomic identifierⁱ	10377 [NCBI]
Taxonomic lineageⁱ	Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Gammaherpesvirinae › Lymphocryptovirus › Epstein-Barr virus (strain GD1)
Virus hostⁱ	Homo sapiens (Human) [TaxID: 9606]
Proteomesⁱ	UP000153037 Componentⁱ: Genome

Subcellular locationⁱ

Host cell membrane
1 Publication
Manual assertion based on experiment inⁱ
- Ref.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.
; Multi-pass membrane protein
1 Publication
Manual assertion based on experiment inⁱ
- Ref.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.

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	1 – 23	CytoplasmicAdd BLAST	23
Transmembraneⁱ	24 – 44	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	45 – 51	Extracellular	7
Transmembraneⁱ	52 – 72	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	73 – 75	Cytoplasmic	3
Transmembraneⁱ	76 – 96	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	97 – 106	Extracellular	10
Transmembraneⁱ	107 – 127	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	128 – 139	CytoplasmicAdd BLAST	12
Transmembraneⁱ	140 – 160	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	161 – 163	Extracellular	3
Transmembraneⁱ	164 – 184	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	185 – 386	CytoplasmicAdd BLAST	202

GO - Cellular componentⁱ

host cell membrane
Source: CACAO
Inferred from direct assayⁱ
- 23609879
host cell plasma membrane Source: UniProtKB-SubCell
integral component of membrane Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Host cell membrane, Host membrane, Membrane

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Mutagenesisⁱ	330	K → R: No effect on ubiquitination and proteasomal degradation. 1 Publication		1

Keywords - Diseaseⁱ

Oncogene

Chemistry databases

ChEMBLⁱ	CHEMBL1795089

ChEMBLⁱ

CHEMBL1795089

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000038310	1 – 386	Latent membrane protein 1Add BLAST		386
ChainⁱPRO_0000038311	242 – 386	Protein p25Add BLAST		145

Post-translational modificationⁱ

Ubiquitinated on the N-terminus.1 Publication

Keywords - PTMⁱ

Phosphoprotein, Ubl conjugation

PTM databases

SwissPalmⁱ	P03230

SwissPalmⁱ

P03230

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

With	Entry	#Exp.	IntAct	Notes
IKBKB	O14920	2	EBI-6973030,EBI-81266	From Homo sapiens.
IRF7	Q92985-1	5	EBI-6973030,EBI-8850881	From a different organism.
RABAC1	Q9UI14	9	EBI-6973030,EBI-712367	From Homo sapiens.
TNIK	Q9UKE5	7	EBI-6973030,EBI-1051794	From Homo sapiens.
TRADD	Q15628	4	EBI-6973030,EBI-359215	From Homo sapiens.
UBE2I	P63279	5	EBI-6973030,EBI-80168	From Homo sapiens.
ZMYND11	Q15326	3	EBI-6973030,EBI-2623509	From Homo sapiens.

Protein-protein interaction databases

BioGridⁱ	971792, 10 interactors
Database of interacting proteins More...DIPⁱ	DIP-29603N DIP-43767N
ELMⁱ	P03230
IntActⁱ	P03230, 14 interactors
Molecular INTeraction database More...MINTⁱ	P03230

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	P03230
SMRⁱ	P03230
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P03230

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	194 – 232	CTAR1Add BLAST		39
Regionⁱ	351 – 386	CTAR2Add BLAST		36

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	204 – 208	Interaction with host TRAF proteins		5

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

KEGG Orthology (KO) More...KOⁱ	K19459
Database of Orthologous Groups More...OrthoDBⁱ	VOG0900011F

Family and domain databases

InterProⁱ	View protein in InterPro IPR007961 Herpes_LMP1
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF05297 Herpes_LMP1, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

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

P03230-1 [UniParc]FASTA Add 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

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
PIRⁱ	D43045 QQBE50
NCBI Reference Sequences More...RefSeqⁱ	YP_401722.1, NC_007605.1

Genome annotation databases

GeneIDⁱ	3783750
KEGGⁱ	vg:3783750

Protein	Similar proteins		Species	Score	Length	Source
P03230	LMP-1		EBVG		386	UniRef100_P03230
Latent membrane protein 1 (Fragment)		EBVG		123
Latent membrane protein 1 (Fragment)		EBVG		123
Latent membrane protein 1 (Fragment)		EBVG		123
Latent membrane protein 1 (Fragment)		EBVG		123
+23

Protein	Similar proteins		Species	Score	Length	Source
P03230	Latent membrane protein 1	)	EBVR		386	UniRef90_P03230
LMP-1		EBVG		386
Latent membrane protein LMP-1		Epstein-Barr virus type 1		382
Latent membrane protein 1 (Fragment)		EBVG		123
Latent membrane protein 1 (Fragment)		EBVG		123
+126

Protein	Similar proteins		Species	Score	Length	Source
P03230	Latent membrane protein 1	)	EBVR		386	UniRef50_P03230
Latent membrane protein 1		EBVC		404
Latent membrane protein 1		EBVA8		371
Latent membrane protein 1		EBVG		366
Latent membrane protein LMP-1		Epstein-Barr virus type 1		382
+758

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
PIRⁱ	D43045 QQBE50
RefSeqⁱ	YP_401722.1, NC_007605.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1CZY	X-ray	2.00	D/E	204-210	[»]
ProteinModelPortalⁱ	P03230
SMRⁱ	P03230
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	971792, 10 interactors
DIPⁱ	DIP-29603N DIP-43767N
ELMⁱ	P03230
IntActⁱ	P03230, 14 interactors
MINTⁱ	P03230

Chemistry databases

ChEMBLⁱ	CHEMBL1795089

ChEMBLⁱ

CHEMBL1795089

PTM databases

SwissPalmⁱ	P03230

SwissPalmⁱ

P03230

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

GeneIDⁱ	3783750
KEGGⁱ	vg:3783750

Phylogenomic databases

KOⁱ	K19459
OrthoDBⁱ	VOG0900011F

Miscellaneous databases

EvolutionaryTraceⁱ	P03230
Protein Ontology More...PROⁱ	PR:P03230

Family and domain databases

InterProⁱ	View protein in InterPro IPR007961 Herpes_LMP1
Pfamⁱ	View protein in Pfam PF05297 Herpes_LMP1, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	LMP1_EBVB9
Accessionⁱ	P03230Primary (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 23, 2018
	This is version 106 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Viral Protein Annotation Program

UniProtKB

UniParc

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UniProtKB - P03230 (LMP1_EBVB9)

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Latent membrane protein 1

LMP1

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

GO - Cellular componenti

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Keywords - Diseasei

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Keywords - PTMi

PTM databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Motif

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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Functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ