Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-868565-00499
Entry Name
UniProt Accession
Theoretical PI
5.37
Molecular Weight
27938.79
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
E3 ubiquitin-protein ligase MIR2
Protein Synonyms/Alias
6.3.2.-; IE1A protein; Modulator of immune recognition 2; ORF K5;
Gene Name
K5
Gene Synonyms/Alias
Created Date
27-SEP-2005
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
146
Canonical
VFAFGGICRVSGTVR
[1]
S-Palmitoylation
Organism
Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi' sarcoma-associated herpesvirus)
NCBI Taxa ID
868565
Reference
[1] Anania VG, Coscoy L. Palmitoylation of MIR2 is required for its function. JVirol. 2011 Mar;85(5):2288-95. doi: 10.1128/JVI.01961-10. Epub 2010 Dec 15.[PMID:21159884]
Functional Description
E3 ubiquitin-protein ligase which promotes ubiquitination and subsequent degradation of host MHC-I, CD86, ICAM1 and CD1D molecules, presumably to prevent lysis of infected cells by cytotoxic T-lymphocytes and NK cell. Binds target molecules through transmembrane interaction. E3 ubiquitin-protein ligases accept ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfer it to target protein. The result of this ubiquitination is the enhancement of the endocytosis of the target chain and the delivery to the lysosome, where it is proteolytically destroyed. Specific for HLA-A and HLA-B2 alleles.
Sequence Annotation
Topological domain: 1 83 Cytoplasmic.
Transmembrane: 84 104 Helical.
Topological domain: 105 124 Extracellular.
Transmembrane: 125 145 Helical.
Topological domain: 146 256 Cytoplasmic.
Protein Length
256 AA.
Protein Sequence
(Canonical)
MASKDVEEGV EGPICWICRE EVGNEGIHPC ACTGELDVVH PQCLSTWLTV SRNTACQMCR  60
VIYRTRTQWR SRLNLWPEME RQEIFELFLL MSVVVAGLVG VALCTWTLLV ILTAPAGTFS  120
PGAVLGFLCF FGFYQIFIVF AFGGICRVSG TVRALYAANN TRVTVLPYRR PRRPTANEDN  180
IELTVLVGPA GGTDEEPTDE SSEGDVASGD KERDGSSGDE PDGGPNDRAG LRGTARTDLC  240
APTKKPVRKN HPKNNG                                                  256
FASTA
(Canonical)
>LipidDB-868565-00499|P90489
MASKDVEEGVEGPICWICREEVGNEGIHPCACTGELDVVHPQCLSTWLTVSRNTACQMCR
VIYRTRTQWRSRLNLWPEMERQEIFELFLLMSVVVAGLVGVALCTWTLLVILTAPAGTFS
PGAVLGFLCFFGFYQIFIVFAFGGICRVSGTVRALYAANNTRVTVLPYRRPRRPTANEDN
IELTVLVGPAGGTDEEPTDESSEGDVASGDKERDGSSGDEPDGGPNDRAGLRGTARTDLC
APTKKPVRKNHPKNNG
Gene Ontology
GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-KW
GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-KW
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0016874; F:ligase activity; IEA:UniProtKB-KW
GO:0008270; F:zinc ion binding; IEA:InterPro
GO:0075509; P:endocytosis involved in viral entry into host cell; IMP:CACAO
GO:0039648; P:modulation by virus of host protein ubiquitination; IMP:CACAO
GO:0044078; P:positive regulation by symbiont of host receptor-mediated endocytosis; IMP:CACAO
GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IDA:CACAO
GO:0039504; P:suppression by virus of host adaptive immune response; IMP:CACAO
GO:0039511; P:suppression by virus of host interferon receptor activity; IEA:UniProtKB-KW
GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW
Interpro
InterPro; IPR011016; Znf_RING-CH
InterPro; IPR013083; Znf_RING/FYVE/PHD
Pfam
Pfam; PF12906; RINGv;
SMART
SMART; SM00744; RINGv;
PROSITE
PROSITE; PS51292; ZF_RING_CH;
PRINTS