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Protein

E3 ubiquitin-protein ligase MIR1

Gene

K3

Organism
Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

E3 ubiquitin-protein ligase which promotes ubiquitination and subsequent degradation of host MHC-I and CD1D molecules, presumably to prevent lysis of infected cells by cytotoxic T-lymphocytes. 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. Induces ubiquitination not only on lysines, but also on cysteine residues.5 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi12Zinc1
Metal bindingi24Zinc1
Metal bindingi26Zinc1
Metal bindingi34Zinc1
Metal bindingi37Zinc1
Metal bindingi50Zinc1
Metal bindingi53Zinc1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1 – 60RING-CH-typePROSITE-ProRule annotationAdd BLAST60

GO - Molecular functioni

GO - Biological processi

  • endocytosis involved in viral entry into host cell Source: CACAO
  • modulation by virus of host protein ubiquitination Source: CACAO
  • protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: CACAO
  • suppression by virus of host adaptive immune response Source: CACAO
  • suppression by virus of host interferon receptor activity Source: UniProtKB-KW
  • suppression by virus of host type I interferon-mediated signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon receptors by virus, Inhibition of host interferon signaling pathway by virus, Ubl conjugation pathway, Viral immunoevasion

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi6.3.2.19. 2803.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase MIR1 (EC:6.3.2.-)
Alternative name(s):
IE1B protein
Modulator of immune recognition 1
ORF K3
Gene namesi
Name:K3
OrganismiHuman herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
Taxonomic identifieri868565 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeGammaherpesvirinaeRhadinovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000000942 Componenti: Genome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 82CytoplasmicSequence analysisAdd BLAST82
Transmembranei83 – 103HelicalSequence analysisAdd BLAST21
Topological domaini104 – 121ExtracellularSequence analysisAdd BLAST18
Transmembranei122 – 142HelicalSequence analysisAdd BLAST21
Topological domaini143 – 333CytoplasmicSequence analysisAdd BLAST191

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host endoplasmic reticulum, Host membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi41W → A: Loss of ubiquitination activity and degradation of class I molecules. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002213891 – 333E3 ubiquitin-protein ligase MIR1Add BLAST333

Expressioni

Keywords - Developmental stagei

Early protein

Interactioni

Subunit structurei

Binds human MHC-I and CD1D.Curated

Binary interactionsi

WithEntry#Exp.IntActNotes
P889412EBI-6149947,EBI-7922689From a different organism.
P889512EBI-6149947,EBI-7923148From a different organism.

Protein-protein interaction databases

BioGridi1776989. 14 interactors.
IntActiP90495. 16 interactors.
MINTiMINT-2824800.

Structurei

Secondary structure

1333
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni10 – 13Combined sources4
Helixi29 – 31Combined sources3
Helixi35 – 45Combined sources11
Turni51 – 53Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VYXNMR-A1-60[»]
ProteinModelPortaliP90495.
SMRiP90495.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP90495.

Family & Domainsi

Sequence similaritiesi

Contains 1 RING-CH-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1 – 60RING-CH-typePROSITE-ProRule annotationAdd BLAST60

Keywords - Domaini

Transmembrane, Transmembrane helix, Zinc-finger

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR033275. MARCH-like.
IPR011016. Znf_RING-CH.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR23012. PTHR23012. 1 hit.
PfamiPF12906. RINGv. 1 hit.
[Graphical view]
SMARTiSM00744. RINGv. 1 hit.
[Graphical view]
PROSITEiPS51292. ZF_RING_CH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P90495-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDEDVPVCW ICNEELGNER FRACGCTGEL ENVHRSCLST WLTISRNTAC
60 70 80 90 100
QICGVVYNTR VVWRPLREMT LLPRLTYQEG LELIVFIFIM TLGAAGLAAA
110 120 130 140 150
TWVWLYIVGG HDPEIDHVAA AAYYVFFVFY QLFVVFGLGA FFHMMRHVGR
160 170 180 190 200
AYAAVNTRVE VFPYRPRPTS PECAVEEIEL QEILPRGDNQ DEEGPAGAAP
210 220 230 240 250
GDQNGPAGAA PGDQDGPADG APVHRDSEES VDEAAGYKEA GEPTHNDGRD
260 270 280 290 300
DNVEPTAVGC DCNNLGAERY RATYCGGYVG AQSGDGAYSV SCHNKAGPSS
310 320 330
LVDILPQGLP GGGYGSMGVI RKRSAVSSAL MFH
Length:333
Mass (Da):36,005
Last modified:May 1, 1997 - v1
Checksum:iC9CCE79B87D3F553
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti195 – 204Missing in AAB62674 (Ref. 3) Curated10
Sequence conflicti195 – 204Missing in ABD28858 (PubMed:16760382).Curated10
Sequence conflicti281A → V in AAB62674 (Ref. 3) Curated1
Sequence conflicti310P → L in ABD28858 (PubMed:16760382).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U75698 Genomic DNA. Translation: AAC57091.1.
AF307516 mRNA. Translation: AAK83788.1.
AF307517 mRNA. Translation: AAK83789.1.
AF307518 mRNA. Translation: AAK83790.1.
AF307519 mRNA. Translation: AAK83791.1.
U71365 Genomic DNA. Translation: AAC34939.1.
U83350 Genomic DNA. Translation: AAC56950.1.
U93872 Genomic DNA. Translation: AAB62674.1.
AF148805 Genomic DNA. Translation: ABD28858.1.
RefSeqiYP_001129360.1. NC_009333.1.

Genome annotation databases

GeneIDi4961486.
KEGGivg:4961486.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U75698 Genomic DNA. Translation: AAC57091.1.
AF307516 mRNA. Translation: AAK83788.1.
AF307517 mRNA. Translation: AAK83789.1.
AF307518 mRNA. Translation: AAK83790.1.
AF307519 mRNA. Translation: AAK83791.1.
U71365 Genomic DNA. Translation: AAC34939.1.
U83350 Genomic DNA. Translation: AAC56950.1.
U93872 Genomic DNA. Translation: AAB62674.1.
AF148805 Genomic DNA. Translation: ABD28858.1.
RefSeqiYP_001129360.1. NC_009333.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VYXNMR-A1-60[»]
ProteinModelPortaliP90495.
SMRiP90495.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1776989. 14 interactors.
IntActiP90495. 16 interactors.
MINTiMINT-2824800.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi4961486.
KEGGivg:4961486.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi6.3.2.19. 2803.

Miscellaneous databases

EvolutionaryTraceiP90495.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR033275. MARCH-like.
IPR011016. Znf_RING-CH.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR23012. PTHR23012. 1 hit.
PfamiPF12906. RINGv. 1 hit.
[Graphical view]
SMARTiSM00744. RINGv. 1 hit.
[Graphical view]
PROSITEiPS51292. ZF_RING_CH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMIR1_HHV8P
AccessioniPrimary (citable) accession number: P90495
Secondary accession number(s): O40920, Q2HRC5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: May 1, 1997
Last modified: November 30, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

Specific for HLA-A, HLA-B, HLA-C and HLA-E alleles.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.