[1]
|
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2840285 [NCBI, ExPASy, EBI, Israel, Japan]
Laux G.,
Perricaudet M.,
Farrell P.J.;
"A spliced Epstein-Barr virus gene expressed in immortalized lymphocytes is created by circularization of the linear viral genome.";
EMBO J. 7:769-774(1988).
|
[2]
|
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LMP2A AND LMP2B).
PubMed=2536113 [NCBI, ExPASy, EBI, Israel, Japan]
Sample J.,
Liebowitz D.,
Kieff E.;
"Two related Epstein-Barr virus membrane proteins are encoded by separate genes.";
J. Virol. 63:933-937(1989).
|
[3]
|
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM LMP2A).
DOI=10.1038/310207a0; PubMed=6087149 [NCBI, ExPASy, EBI, Israel, Japan]
Baer R.,
Bankier A.T.,
Biggin M.D.,
Deininger P.L.,
Farrell P.J.,
Gibson T.J.,
Hatfull G.,
Hudson G.S.,
Satchwell S.C.,
Seguin C.,
Tuffnell P.S.,
Barrell B.G.;
"DNA sequence and expression of the B95-8 Epstein-Barr virus genome.";
Nature 310:207-211(1984).
|
[4]
|
PHOSPHORYLATION.
PubMed=1710288 [NCBI, ExPASy, EBI, Israel, Japan]
Longnecker R.,
Druker B.,
Roberts T.M.,
Kieff E.;
"An Epstein-Barr virus protein associated with cell growth transformation interacts with a tyrosine kinase.";
J. Virol. 65:3681-3692(1991).
|
[5]
|
FUNCTION.
PubMed=8290598 [NCBI, ExPASy, EBI, Israel, Japan]
Miller C.L.,
Lee J.H.,
Kieff E.,
Longnecker R.;
"An integral membrane protein (LMP2) blocks reactivation of Epstein-Barr virus from latency following surface immunoglobulin crosslinking.";
Proc. Natl. Acad. Sci. U.S.A. 91:772-776(1994).
|
[6]
|
INTERACTION WITH HUMAN SYK AND LYN.
DOI=10.1016/S1074-7613(95)80040-9; PubMed=7895172 [NCBI, ExPASy, EBI, Israel, Japan]
Miller C.L.,
Burkhardt A.L.,
Lee J.H.,
Stealey B.,
Longnecker R.,
Bolen J.B.,
Kieff E.;
"Integral membrane protein 2 of Epstein-Barr virus regulates reactivation from latency through dominant negative effects on protein-tyrosine kinases.";
Immunity 2:155-166(1995).
|
[7]
|
MUTAGENESIS OF TYR-74; TYR-85 AND TYR-112.
PubMed=9733815 [NCBI, ExPASy, EBI, Israel, Japan]
Fruehling S.,
Swart R.,
Dolwick K.M.,
Kremmer E.,
Longnecker R.;
"Tyrosine 112 of latent membrane protein 2A is essential for protein tyrosine kinase loading and regulation of Epstein-Barr virus latency.";
J. Virol. 72:7796-7806(1998).
|
[8]
|
FUNCTION.
DOI=10.1016/S1074-7613(00)80623-8; PubMed=9768760 [NCBI, ExPASy, EBI, Israel, Japan]
Caldwell R.G.,
Wilson J.B.,
Anderson S.J.,
Longnecker R.;
"Epstein-Barr virus LMP2A drives B cell development and survival in the absence of normal B cell receptor signals.";
Immunity 9:405-411(1998).
|
[9]
|
INTERACTION WITH HUMAN ITCH AND NEDD4L.
DOI=10.1128/MCB.20.22.8526-8535.2000; PubMed=11046148 [NCBI, ExPASy, EBI, Israel, Japan]
Winberg G.,
Matskova L.,
Chen F.,
Plant P.,
Rotin D.,
Gish G.,
Ingham R.,
Ernberg I.,
Pawson T.;
"Latent membrane protein 2A of Epstein-Barr virus binds WW domain E3 protein-ubiquitin ligases that ubiquitinate B-cell tyrosine kinases.";
Mol. Cell. Biol. 20:8526-8535(2000).
|
[10]
|
SUBCELLULAR LOCATION.
DOI=10.1016/S1074-7613(01)00089-9; PubMed=11163230 [NCBI, ExPASy, EBI, Israel, Japan]
Dykstra M.L.,
Longnecker R.,
Pierce S.K.;
"Epstein-Barr virus coopts lipid rafts to block the signaling and antigen transport functions of the BCR.";
Immunity 14:57-67(2001).
|
[11]
|
SUBCELLULAR LOCATION.
PubMed=11961256 [NCBI, ExPASy, EBI, Israel, Japan]
Lynch D.T.,
Zimmerman J.S.,
Rowe D.T.;
"Epstein-Barr virus latent membrane protein 2B (LMP2B) co-localizes with LMP2A in perinuclear regions in transiently transfected cells.";
J. Gen. Virol. 83:1025-1035(2002).
|
[12]
|
UBIQUITINATION.
DOI=10.1006/viro.2002.1562; PubMed=12202215 [NCBI, ExPASy, EBI, Israel, Japan]
Ikeda M.,
Ikeda A.,
Longnecker R.;
"Lysine-independent ubiquitination of Epstein-Barr virus LMP2A.";
Virology 300:153-159(2002).
|
|
- FUNCTION: 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.
- FUNCTION: Isoform LMP2B may be a negative regulator of isoform LMP2A.
- SUBUNIT: Isoform LMP2A cytoplasmic N-terminal domain interacts with human SRC family protein tyrosine kinases SYK and LYN. Binds human ITCH, WWP2 and NEDD4L.
- SUBCELLULAR LOCATION: Isoform LMP2A: Cell membrane; Multi-pass membrane protein. Note=Isoform LMP2A is localized in plasma membrane lipid rafts.
- SUBCELLULAR LOCATION: Isoform LMP2B: Intracytoplasmic membrane; Multi-pass membrane protein. Cytoplasm, perinuclear region. Note=Isoform LMP2B localizes to perinuclear regions.
- ALTERNATIVE PRODUCTS:
2 named isoforms [FASTA] produced by alternative splicing.
|
| Name | LMP2B |
| Synonyms | TP2 |
| Isoform ID | P13285-2 |
| Features which should be applied to build the isoform sequence: VSP_016139. |
|
|
- PTM: Isoform LMP2A is phosphorylated on cytoplasmic N-terminal tyrosines residues, possibly by human LYN.
- PTM: Can be ubiquitinated at by human ITCH and WWP2 on the N-terminus in a lysine-independent manner.
- MISCELLANEOUS: In healthy individuals, EBV typically establishes a persistent latent infection in which the virus can be detected in resting, nonproliferating peripheral B-lymphocytes. These latently infected cells express only 2 virally encoded genes, LMP2A and EBNA1.
|
ExPASy Home page
SIB Switzerland
