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P90495

- MIR1_HHV8P

UniProt

P90495 - MIR1_HHV8P

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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: 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi12 – 121Zinc
Metal bindingi24 – 241Zinc
Metal bindingi26 – 261Zinc
Metal bindingi34 – 341Zinc
Metal bindingi37 – 371Zinc
Metal bindingi50 – 501Zinc
Metal bindingi53 – 531Zinc

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1 – 6060RING-CH-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. endocytosis involved in viral entry into host cell Source: CACAO
  2. modulation by virus of host protein ubiquitination Source: CACAO
  3. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: CACAO
  4. suppression by virus of host adaptive immune response Source: CACAO
  5. suppression by virus of host interferon receptor activity Source: UniProtKB-KW
  6. 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

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]
ProteomesiUP000000942: Genome

Subcellular locationi

Host cell membrane 1 Publication; Multi-pass membrane protein 1 Publication. Host endoplasmic reticulum 1 Publication
Note: Probably exerts its effects at the plasma membrane during viral infection.

GO - Cellular componenti

  1. host cell endoplasmic reticulum Source: UniProtKB-KW
  2. host cell plasma membrane Source: UniProtKB-KW
  3. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi41 – 411W → A: Loss of ubiquitination activity and degradation of class I molecules. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 333333E3 ubiquitin-protein ligase MIR1PRO_0000221389Add
BLAST

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

IntActiP90495. 16 interactions.
MINTiMINT-2824800.

Structurei

Secondary structure

1
333
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni10 – 134
Helixi29 – 313
Helixi35 – 4511
Turni51 – 533

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VYXNMR-A1-60[»]
ProteinModelPortaliP90495.
SMRiP90495. Positions 1-60.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP90495.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 8282CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini104 – 12118ExtracellularSequence AnalysisAdd
BLAST
Topological domaini143 – 333191CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei83 – 10321HelicalSequence AnalysisAdd
BLAST
Transmembranei122 – 14221HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1 – 6060RING-CH-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Transmembrane, Transmembrane helix, Zinc-finger

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR011016. Znf_RING-CH.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti195 – 20410Missing in AAB62674. 1 PublicationCurated
Sequence conflicti195 – 20410Missing in ABD28858. (PubMed:16760382)Curated
Sequence conflicti281 – 2811A → V in AAB62674. 1 PublicationCurated
Sequence conflicti310 – 3101P → L in ABD28858. (PubMed:16760382)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
RefSeqi YP_001129360.1. NC_009333.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1VYX NMR - A 1-60 [» ]
ProteinModelPortali P90495.
SMRi P90495. Positions 1-60.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P90495. 16 interactions.
MINTi MINT-2824800.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 4961486.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

EvolutionaryTracei P90495.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR011016. Znf_RING-CH.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view ]
Pfami PF12906. RINGv. 1 hit.
[Graphical view ]
SMARTi SM00744. RINGv. 1 hit.
[Graphical view ]
PROSITEi PS51292. ZF_RING_CH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A single 13-kilobase divergent locus in the Kaposi sarcoma-associated herpesvirus (human herpesvirus 8) genome contains nine open reading frames that are homologous to or related to cellular proteins."
    Nicholas J., Ruvolo V., Zong J., Ciufo D., Guo H.-G., Reitz M.S., Hayward G.S.
    J. Virol. 71:1963-1974(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Transcription pattern of human herpesvirus 8 open reading frame k3 in primary effusion lymphoma and kaposi's sarcoma."
    Rimessi P., Bonaccorsi A., Sturzl M., Fabris M., Brocca-Cofano E., Caputo A., Melucci-Vigo G., Falchi M., Cafaro A., Cassai E., Ensoli B., Monini P.
    J. Virol. 75:7161-7174(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The genome of human herpesvirus 8 cloned from Kaposi's sarcoma."
    Neipel F., Albrecht J.-C., Ensser A., Huang Y.-Q., Li J.J., Friedman-Kien A.E., Fleckenstein B.
    Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Kaposi's sarcoma-associated herpesvirus immune modulation: an overview."
    Rezaee S.A.R., Cunningham C., Davison A.J., Blackbourn D.J.
    J. Gen. Virol. 87:1781-1804(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "Kaposi's sarcoma-associated herpesvirus encodes two proteins that block cell surface display of MHC class I chains by enhancing their endocytosis."
    Coscoy L., Ganem D.
    Proc. Natl. Acad. Sci. U.S.A. 97:8051-8056(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Downregulation of major histocompatibility complex class I molecules by Kaposi's sarcoma-associated herpesvirus K3 and K5 proteins."
    Ishido S., Wang C., Lee B.-S., Cohen G.B., Jung J.U.
    J. Virol. 74:5300-5309(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. "A novel class of herpesvirus-encoded membrane-bound E3 ubiquitin ligases regulates endocytosis of proteins involved in immune recognition."
    Coscoy L., Sanchez D.J., Ganem D.
    J. Cell Biol. 155:1265-1273(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Ubiquitylation of MHC class I by the K3 viral protein signals internalization and TSG101-dependent degradation."
    Hewitt E.W., Duncan L., Mufti D., Baker J., Stevenson P.G., Lehner P.J.
    EMBO J. 21:2418-2429(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN HLA-A, DOMAIN RINGV-TYPE ZINC-FINGER, MUTAGENESIS OF TRP-41.
  10. "Regulation of CD1d expression and function by a herpesvirus infection."
    Sanchez D.J., Gumperz J.E., Ganem D.
    J. Clin. Invest. 115:1369-1378(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Ubiquitination on nonlysine residues by a viral E3 ubiquitin ligase."
    Cadwell K., Coscoy L.
    Science 309:127-130(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Solution structure of the Kaposi's sarcoma-associated herpesvirus K3 N-terminal domain reveals a Novel E2-binding C4HC3-type RING domain."
    Dodd R.B., Allen M.D., Brown S.E., Sanderson C.M., Duncan L.M., Lehner P.J., Bycroft M., Read R.J.
    J. Biol. Chem. 279:53840-53847(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-60.

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: October 29, 2014
This is version 102 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

External Data

Dasty 3