Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

E3 ubiquitin-protein ligase MIR1 (EC 2.3.2.27) (IE1B protein) (Modulator of immune recognition 1) (ORF K3) (RING-type E3 ubiquitin transferase MIR1)

 MIR1_HHV8P              Reviewed;         333 AA.
P90495; O40920; Q2HRC5;
27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
27-SEP-2017, entry version 119.
RecName: Full=E3 ubiquitin-protein ligase MIR1;
EC=2.3.2.27;
AltName: Full=IE1B protein;
AltName: Full=Modulator of immune recognition 1;
AltName: Full=ORF K3;
AltName: Full=RING-type E3 ubiquitin transferase MIR1 {ECO:0000305};
Name=K3;
Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's
sarcoma-associated herpesvirus).
Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae;
Gammaherpesvirinae; Rhadinovirus.
NCBI_TaxID=868565;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9032328;
Nicholas J., Ruvolo V., Zong J., Ciufo D., Guo H.-G., Reitz M.S.,
Hayward G.S.;
"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.";
J. Virol. 71:1963-1974(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11435597; DOI=10.1128/JVI.75.15.7161-7174.2001;
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.;
"Transcription pattern of human herpesvirus 8 open reading frame k3 in
primary effusion lymphoma and kaposi's sarcoma.";
J. Virol. 75:7161-7174(2001).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Neipel F., Albrecht J.-C., Ensser A., Huang Y.-Q., Li J.J.,
Friedman-Kien A.E., Fleckenstein B.;
"The genome of human herpesvirus 8 cloned from Kaposi's sarcoma.";
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=8962146; DOI=10.1073/pnas.93.25.14862;
Russo J.J., Bohenzky R.A., Chien M.-C., Chen J., Yan M., Maddalena D.,
Parry J.P., Peruzzi D., Edelman I.S., Chang Y., Moore P.S.;
"Nucleotide sequence of the Kaposi sarcoma-associated herpesvirus
(HHV8).";
Proc. Natl. Acad. Sci. U.S.A. 93:14862-14867(1996).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16760382; DOI=10.1099/vir.0.81919-0;
Rezaee S.A.R., Cunningham C., Davison A.J., Blackbourn D.J.;
"Kaposi's sarcoma-associated herpesvirus immune modulation: an
overview.";
J. Gen. Virol. 87:1781-1804(2006).
[6]
FUNCTION.
PubMed=10859362; DOI=10.1073/pnas.140129797;
Coscoy L., Ganem D.;
"Kaposi's sarcoma-associated herpesvirus encodes two proteins that
block cell surface display of MHC class I chains by enhancing their
endocytosis.";
Proc. Natl. Acad. Sci. U.S.A. 97:8051-8056(2000).
[7]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10799607; DOI=10.1128/JVI.74.11.5300-5309.2000;
Ishido S., Wang C., Lee B.-S., Cohen G.B., Jung J.U.;
"Downregulation of major histocompatibility complex class I molecules
by Kaposi's sarcoma-associated herpesvirus K3 and K5 proteins.";
J. Virol. 74:5300-5309(2000).
[8]
FUNCTION.
PubMed=11756476; DOI=10.1083/jcb.200111010;
Coscoy L., Sanchez D.J., Ganem D.;
"A novel class of herpesvirus-encoded membrane-bound E3 ubiquitin
ligases regulates endocytosis of proteins involved in immune
recognition.";
J. Cell Biol. 155:1265-1273(2001).
[9]
INTERACTION WITH HUMAN HLA-A, DOMAIN RINGV-TYPE ZINC-FINGER, AND
MUTAGENESIS OF TRP-41.
PubMed=12006494; DOI=10.1093/emboj/21.10.2418;
Hewitt E.W., Duncan L., Mufti D., Baker J., Stevenson P.G.,
Lehner P.J.;
"Ubiquitylation of MHC class I by the K3 viral protein signals
internalization and TSG101-dependent degradation.";
EMBO J. 21:2418-2429(2002).
[10]
FUNCTION.
PubMed=15864354; DOI=10.1172/JCI200524041;
Sanchez D.J., Gumperz J.E., Ganem D.;
"Regulation of CD1d expression and function by a herpesvirus
infection.";
J. Clin. Invest. 115:1369-1378(2005).
[11]
FUNCTION.
PubMed=15994556; DOI=10.1126/science.1110340;
Cadwell K., Coscoy L.;
"Ubiquitination on nonlysine residues by a viral E3 ubiquitin
ligase.";
Science 309:127-130(2005).
[12]
STRUCTURE BY NMR OF 1-60.
PubMed=15465811; DOI=10.1074/jbc.M409662200;
Dodd R.B., Allen M.D., Brown S.E., Sanderson C.M., Duncan L.M.,
Lehner P.J., Bycroft M., Read R.J.;
"Solution structure of the Kaposi's sarcoma-associated herpesvirus K3
N-terminal domain reveals a Novel E2-binding C4HC3-type RING domain.";
J. Biol. Chem. 279:53840-53847(2004).
-!- FUNCTION: 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. {ECO:0000269|PubMed:10799607,
ECO:0000269|PubMed:10859362, ECO:0000269|PubMed:11756476,
ECO:0000269|PubMed:15864354, ECO:0000269|PubMed:15994556}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Binds human MHC-I and CD1D. {ECO:0000305}.
-!- INTERACTION:
P88941:- (xeno); NbExp=2; IntAct=EBI-6149947, EBI-7922689;
P88951:RIR2 (xeno); NbExp=2; IntAct=EBI-6149947, EBI-7923148;
-!- SUBCELLULAR LOCATION: Host cell membrane
{ECO:0000269|PubMed:10799607}; Multi-pass membrane protein
{ECO:0000269|PubMed:10799607}. Host endoplasmic reticulum
{ECO:0000269|PubMed:10799607}. Note=Probably exerts its effects at
the plasma membrane during viral infection.
-!- MISCELLANEOUS: Specific for HLA-A, HLA-B, HLA-C and HLA-E alleles.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U75698; AAC57091.1; -; Genomic_DNA.
EMBL; AF307516; AAK83788.1; -; mRNA.
EMBL; AF307517; AAK83789.1; -; mRNA.
EMBL; AF307518; AAK83790.1; -; mRNA.
EMBL; AF307519; AAK83791.1; -; mRNA.
EMBL; U71365; AAC34939.1; -; Genomic_DNA.
EMBL; U83350; AAC56950.1; -; Genomic_DNA.
EMBL; U93872; AAB62674.1; -; Genomic_DNA.
EMBL; AF148805; ABD28858.1; -; Genomic_DNA.
RefSeq; YP_001129360.1; NC_009333.1.
PDB; 1VYX; NMR; -; A=1-60.
PDBsum; 1VYX; -.
ProteinModelPortal; P90495; -.
SMR; P90495; -.
BioGrid; 1776989; 14.
IntAct; P90495; 16.
MINT; MINT-2824800; -.
GeneID; 4961486; -.
KEGG; vg:4961486; -.
KO; K21665; -.
OrthoDB; VOG0900011O; -.
BRENDA; 6.3.2.19; 2803.
UniPathway; UPA00143; -.
EvolutionaryTrace; P90495; -.
Proteomes; UP000000942; Genome.
GO; GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IMP:CACAO.
GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IMP:CACAO.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IDA:CACAO.
GO; GO:0039504; P:suppression by virus of host adaptive immune response; IMP:CACAO.
GO; GO:0039511; P:suppression by virus of host interferon receptor activity; IEA:UniProtKB-KW.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR033275; MARCH-like.
InterPro; IPR011016; Znf_RING-CH.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
PANTHER; PTHR23012; PTHR23012; 1.
Pfam; PF12906; RINGv; 1.
SMART; SM00744; RINGv; 1.
PROSITE; PS51292; ZF_RING_CH; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Early protein; Host cell membrane;
Host endoplasmic reticulum; Host membrane; 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; Membrane;
Metal-binding; Reference proteome; Transferase; Transmembrane;
Transmembrane helix; Ubl conjugation pathway; Viral immunoevasion;
Zinc; Zinc-finger.
CHAIN 1 333 E3 ubiquitin-protein ligase MIR1.
/FTId=PRO_0000221389.
TOPO_DOM 1 82 Cytoplasmic. {ECO:0000255}.
TRANSMEM 83 103 Helical. {ECO:0000255}.
TOPO_DOM 104 121 Extracellular. {ECO:0000255}.
TRANSMEM 122 142 Helical. {ECO:0000255}.
TOPO_DOM 143 333 Cytoplasmic. {ECO:0000255}.
ZN_FING 1 60 RING-CH-type. {ECO:0000255|PROSITE-
ProRule:PRU00623}.
METAL 12 12 Zinc.
METAL 24 24 Zinc.
METAL 26 26 Zinc.
METAL 34 34 Zinc.
METAL 37 37 Zinc.
METAL 50 50 Zinc.
METAL 53 53 Zinc.
MUTAGEN 41 41 W->A: Loss of ubiquitination activity and
degradation of class I molecules.
{ECO:0000269|PubMed:12006494}.
CONFLICT 195 204 Missing (in Ref. 3; AAB62674 and 5;
ABD28858). {ECO:0000305}.
CONFLICT 281 281 A -> V (in Ref. 3; AAB62674).
{ECO:0000305}.
CONFLICT 310 310 P -> L (in Ref. 5; ABD28858).
{ECO:0000305}.
TURN 10 13 {ECO:0000244|PDB:1VYX}.
HELIX 29 31 {ECO:0000244|PDB:1VYX}.
HELIX 35 45 {ECO:0000244|PDB:1VYX}.
TURN 51 53 {ECO:0000244|PDB:1VYX}.
SEQUENCE 333 AA; 36005 MW; C9CCE79B87D3F553 CRC64;
MEDEDVPVCW ICNEELGNER FRACGCTGEL ENVHRSCLST WLTISRNTAC QICGVVYNTR
VVWRPLREMT LLPRLTYQEG LELIVFIFIM TLGAAGLAAA TWVWLYIVGG HDPEIDHVAA
AAYYVFFVFY QLFVVFGLGA FFHMMRHVGR AYAAVNTRVE VFPYRPRPTS PECAVEEIEL
QEILPRGDNQ DEEGPAGAAP GDQNGPAGAA PGDQDGPADG APVHRDSEES VDEAAGYKEA
GEPTHNDGRD DNVEPTAVGC DCNNLGAERY RATYCGGYVG AQSGDGAYSV SCHNKAGPSS
LVDILPQGLP GGGYGSMGVI RKRSAVSSAL MFH


Related products :

Catalog number Product name Quantity
EIAAB45296 Ac2-121,E3 ubiquitin-protein ligase UHRF1,Liver regeneration-related protein LRRG126,Rat,Rattus norvegicus,Ubiquitin-like PHD and RING finger domain-containing protein 1,Ubiquitin-like-containing PHD
EIAAB35429 E3 ubiquitin-protein ligase RNF149,Goliath-related E3 ubiquitin-protein ligase 4,Greul4,Mouse,Mus musculus,RING finger protein 149,Rnf149
EIAAB35404 E3 ubiquitin-protein ligase RNF133,Goliath-related E3 ubiquitin-protein ligase 2,Greul2,Mouse,Mus musculus,RING finger protein 133,Rnf133
EIAAB35402 E3 ubiquitin-protein ligase RNF128,Gene related to anergy in lymphocytes protein,Goliath-related E3 ubiquitin-protein ligase 1,Grail,Greul1,MNCb-3816,Mouse,Mus musculus,RING finger protein 128,Rnf128
EIAAB35409 E3 ubiquitin-protein ligase RNF135,Homo sapiens,Human,L13,REUL,RIG-I E3 ubiquitin ligase,RING finger protein 135,Riplet,RNF135
EIAAB35496 E3 ubiquitin-protein ligase RNF216,Homo sapiens,Human,RING finger protein 216,RNF216,Triad domain-containing protein 3,TRIAD3,UBCE7IP1,Ubiquitin-conjugating enzyme 7-interacting protein 1,ZIN,Zinc fin
EIAAB35497 E3 ubiquitin-protein ligase RNF216,Mouse,Mus musculus,RING finger protein 216,Rnf216,Triad domain-containing protein 3,Triad3,Ubce7ip1,UbcM4-interacting protein 83,Ubiquitin-conjugating enzyme 7-inter
EIAAB45297 E3 ubiquitin-protein ligase UHRF1,Mouse,Mus musculus,Np95,Nuclear protein 95,Nuclear zinc finger protein Np95,Ubiquitin-like PHD and RING finger domain-containing protein 1,Ubiquitin-like-containing P
EIAAB45116 E3 ubiquitin-protein ligase UBR3,Homo sapiens,Human,KIAA2024,N-recognin-3,Ubiquitin-protein ligase E3-alpha-3,Ubiquitin-protein ligase E3-alpha-III,UBR3,Zinc finger protein 650,ZNF650
EIAAB45117 E3 ubiquitin-protein ligase UBR3,Kiaa2024,Mouse,Mus musculus,N-recognin-3,Ubiquitin-protein ligase E3-alpha-3,Ubiquitin-protein ligase E3-alpha-III,Ubr3,Zfp650,Zinc finger protein 650,Znf650
EIAAB45298 E3 ubiquitin-protein ligase UHRF2,Mouse,Mus musculus,NIRF,Nirf,Np95-like ring finger protein,Nuclear protein 97,Nuclear zinc finger protein Np97,Ubiquitin-like PHD and RING finger domain-containing pr
EIAAB33372 Kiaa0161,Mouse,Mus musculus,Probable E3 ubiquitin-protein ligase RNF144A,RING finger protein 144A,Rnf144,Rnf144a,Ubce7ip4,UbcM4-interacting protein 4,Ubiquitin-conjugating enzyme 7-interacting protein
EIAAB33371 Homo sapiens,Human,KIAA0161,Probable E3 ubiquitin-protein ligase RNF144A,RING finger protein 144A,RNF144,RNF144A,UBCE7IP4,UbcM4-interacting protein 4,Ubiquitin-conjugating enzyme 7-interacting protein
25-863 RNF217 is an E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. 0.05 mg
29-847 KIAA1333 is a probable E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted subs 0.05 mg
25-866 HECTD2 is a probable E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substr 0.05 mg
25-847 MARCH7 is an E3 ubiquitin-protein ligase which may specifically enhance the E2 activity of HIP2. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioeste 0.05 mg
EIAAB45115 C6orf133,E3 ubiquitin-protein ligase UBR2,Homo sapiens,Human,KIAA0349,N-recognin-2,Ubiquitin-protein ligase E3-alpha-2,Ubiquitin-protein ligase E3-alpha-II,UBR2
EIAAB44818 Homo sapiens,Human,NICE5,PRO3094,Protein NICE-5,UBE2Q,UBE2Q1,Ubiquitin carrier protein Q1,Ubiquitin-conjugating enzyme E2 Q1,Ubiquitin-protein ligase Q1
EIAAB44908 Cell proliferation-inducing gene 50 protein,Homo sapiens,HSPC150,Human,PIG50,UBE2T,Ubiquitin carrier protein T,Ubiquitin-conjugating enzyme E2 T,Ubiquitin-protein ligase T
EIAAB25831 C1orf166,E3 ubiquitin-protein ligase MUL1,GIDE,Growth inhibition and death E3 ligase,Homo sapiens,Human,MAPL,Mitochondrial ubiquitin ligase activator of NFKB 1,Mitochondrial-anchored protein ligase,MU
25-830 FBXO21 contains 1 F-box domain. It is a substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex.This gene encodes a member of the F-box protein family whi 0.05 mg
25-845 HACE1 contains 6 ANK repeats and 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain. HACE1 is an E3 ubiquitin-protein ligase that may function in cellular proteins degradation. 0.05 mg
18-003-44311 Ubiquitin-conjugating enzyme E2-25 kDa - EC 6.3.2.19; Ubiquitin-protein ligase; Ubiquitin carrier protein; E2(25K); Huntingtin-interacting protein 2; HIP-2 Polyclonal 0.1 mg Protein A
10-663-45300 ubiquitin-conjugating enzyme (UBC9) Human - EC 6.3.2.19; SUMO-1-protein ligase; Ubiquitin-conjugating enzyme E2 I; Ubiquitin-protein ligase I; Ubiquitin carrier protein I; Ubiquitin carrier protein 9; 1 mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur