Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10377-00302
Entry Name
UniProt Accession
Theoretical PI
4.85
Molecular Weight
53011.46
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Latent membrane protein 2
Protein Synonyms/Alias
Terminal protein;
Gene Name
LMP2
Gene Synonyms/Alias
Created Date
01-JAN-1990
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
124
Canonical
RGSMNPVCLPVIVAP
[1]
S-Palmitoylation
245
Canonical
RWRRLTVCGGIMFLA
[1]
S-Palmitoylation
339
Canonical
TLVVLLICSSCSSCP
[1]
S-Palmitoylation
342
Canonical
VLLICSSCSSCPLSK
[1]
S-Palmitoylation
345
Canonical
ICSSCSSCPLSKILL
[1]
S-Palmitoylation
426
Canonical
TYGPVFMCLGGLLTM
[1]
S-Palmitoylation
472
Canonical
ALFGVIRCCRYCCYY
[1]
S-Palmitoylation
473
Canonical
LFGVIRCCRYCCYYC
[1]
S-Palmitoylation
476
Canonical
VIRCCRYCCYYCLTL
[1]
S-Palmitoylation
477
Canonical
IRCCRYCCYYCLTLE
[1]
S-Palmitoylation
480
Canonical
CRYCCYYCLTLESEE
[1]
S-Palmitoylation
Organism
Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
NCBI Taxa ID
10377
Reference
[1] Katzman RB, Longnecker R. LMP2A does not require palmitoylation to localize tobuoyant complexes or for function. J Virol. 2004 Oct;78(20):10878-87. PubMedPMID: 15452208; PubMed Central PMCID: PMC521828.[PMID:15452208]
Functional Description
Isoform LMP2A maintains EBV latent infection of B- lymphocyte, by preventing lytic reactivation of the virus in response to surface immunoglobulin (sIg) cross-linking. Acts like a dominant negative inhibitor of the sIg-associated protein tyrosine kinases, LYN and SYK. Also blocks translocation of the B- cell antigen receptor (BCR) into lipid rafts, preventing the subsequent signaling and accelerated internalization of the BCR upon BCR cross-linking. Serves as a molecular scaffold to recruit SYK, LYN and E3 protein-ubiquitin ligases, such as ITCH and NEDD4L, leading to ubiquitination and potential degradation of both tyrosines kinases. Possesses a constitutive signaling activity in non-transformed cells, inducing bypass of normal B lymphocyte developmental checkpoints allowing immunoglobulin- negative cells to colonize peripheral lymphoid organs.
Sequence Annotation
Topological domain: 1 123 Cytoplasmic.
Transmembrane: 124 144 Helical.
Topological domain: 145 147 Extracellular.
Transmembrane: 148 168 Helical.
Topological domain: 169 177 Cytoplasmic.
Transmembrane: 178 198 Helical.
Topological domain: 199 211 Extracellular.
Transmembrane: 212 232 Helical.
Topological domain: 233 241 Cytoplasmic.
Transmembrane: 242 262 Helical.
Topological domain: 263 267 Extracellular.
Transmembrane: 268 288 Helical.
Topological domain: 289 296 Cytoplasmic.
Transmembrane: 297 317 Helical.
Topological domain: 318 318 Extracellular.
Transmembrane: 319 339 Helical.
Topological domain: 340 354 Cytoplasmic.
Transmembrane: 355 375 Helical.
Topological domain: 376 388 Extracellular.
Transmembrane: 389 409 Helical.
Topological domain: 410 422 Cytoplasmic.
Transmembrane: 423 443 Helical.
Topological domain: 444 449 Extracellular.
Transmembrane: 450 470 Helical.
Topological domain: 471 497 Cytoplasmic.
Motif: 97 101 PPPPY WW-binding.
Modified residue: 112 112 Phosphotyrosine; by host.
Protein Length
497 AA.
Protein Sequence
(Canonical)
MGSLEMVPMG AGPPSPGGDP DGYDGGNNSQ YPSASGSSGN TPTPPNDEER ESNEEPPPPY  60
EDPYWGNGDR HSDYQPLGTQ DQSLYLGLQH DGNDGLPPPP YSPRDDSSQH IYEEAGRGSM  120
NPVCLPVIVA PYLFWLAAIA ASCFTASVST VVTATGLALS LLLLAAVASS YAAAQRKLLT  180
PVTVLTAVVT FFAICLTWRI EDPPFNSLLF ALLAAAGGLQ GIYVLVMLVL LILAYRRRWR  240
RLTVCGGIMF LACVLVLIVD AVLQLSPLLG AVTVVSMTLL LLAFVLWLSS PGGLGTLGAA  300
LLTLAAALAL LASLILGTLN LTTMFLLMLL WTLVVLLICS SCSSCPLSKI LLARLFLYAL  360
ALLLLASALI AGGSILQTNF KSLSSTEFIP NLFCMLLLIV AGILFILAIL TEWGSGNRTY  420
GPVFMCLGGL LTMVAGAVWL TVMSNTLLSA WILTAGFLIF LIGFALFGVI RCCRYCCYYC  480
LTLESEERPP TPYRNTV                                                 497
FASTA
(Canonical)
>LipidDB-10377-00302|P13285
MGSLEMVPMGAGPPSPGGDPDGYDGGNNSQYPSASGSSGNTPTPPNDEERESNEEPPPPY
EDPYWGNGDRHSDYQPLGTQDQSLYLGLQHDGNDGLPPPPYSPRDDSSQHIYEEAGRGSM
NPVCLPVIVAPYLFWLAAIAASCFTASVSTVVTATGLALSLLLLAAVASSYAAAQRKLLT
PVTVLTAVVTFFAICLTWRIEDPPFNSLLFALLAAAGGLQGIYVLVMLVLLILAYRRRWR
RLTVCGGIMFLACVLVLIVDAVLQLSPLLGAVTVVSMTLLLLAFVLWLSSPGGLGTLGAA
LLTLAAALALLASLILGTLNLTTMFLLMLLWTLVVLLICSSCSSCPLSKILLARLFLYAL
ALLLLASALIAGGSILQTNFKSLSSTEFIPNLFCMLLLIVAGILFILAILTEWGSGNRTY
GPVFMCLGGLLTMVAGAVWLTVMSNTLLSAWILTAGFLIFLIGFALFGVIRCCRYCCYYC
LTLESEERPPTPYRNTV
Gene Ontology
GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-KW
GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-KW
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0039649; P:modulation by virus of host ubiquitin-protein ligase activity; IEA:UniProtKB-KW
GO:0019042; P:viral latency; IEA:InterPro
Interpro
InterPro; IPR010881; Herpes_LMP2
Pfam
Pfam; PF07415; Herpes_LMP2;
SMART
PROSITE
PRINTS