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 LAP (EC 2.3.2.27) (Leukemia associated protein) (LAP) (RING-type E3 ubiquitin transferase LAP)

 LAP_LSDV                Reviewed;         162 AA.
Q91T40;
10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
10-MAY-2017, entry version 79.
RecName: Full=E3 ubiquitin-protein ligase LAP;
EC=2.3.2.27;
AltName: Full=Leukemia associated protein;
Short=LAP;
AltName: Full=RING-type E3 ubiquitin transferase LAP {ECO:0000305};
Name=LW010;
Lumpy skin disease virus (LSDV).
Viruses; dsDNA viruses, no RNA stage; Poxviridae; Chordopoxvirinae;
Capripoxvirus.
NCBI_TaxID=59509;
NCBI_TaxID=9913; Bos taurus (Bovine).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Neethling;
Stipinovich C., Vreede F.T., Kara P.D., Wallace D.B., Nel L.H.,
Viljoen G.J.;
"Molecular characterization of important regions of the Lumpy skin
disease virus genome.";
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12827464; DOI=10.1007/s00705-003-0102-0;
Kara P.D., Afonso C.L., Wallace D.B., Kutish G.F., Abolnik C., Lu Z.,
Vreede F.T., Taljaard L.C.F., Zsak A., Viljoen G.J., Rock D.L.;
"Comparative sequence analysis of the South African vaccine strain and
two virulent field isolates of Lumpy skin disease virus.";
Arch. Virol. 148:1335-1356(2003).
-!- FUNCTION: E3 ubiquitin-protein ligase which promotes
ubiquitination and subsequent degradation of host MHC-I and CD4
molecules, presumably to prevent lysis of infected cells by
cytotoxic T-lymphocytes and NK cell. Binds target molecules
through transmembrane interaction. 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 (By similarity). {ECO:0000250}.
-!- 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.
-!- SUBCELLULAR LOCATION: Host membrane {ECO:0000305}; Multi-pass
membrane protein {ECO:0000305}. Host Golgi apparatus, host trans-
Golgi network membrane. Host early endosome membrane
{ECO:0000250}.
-!- DOMAIN: The RING-CH-type zinc finger domain is required for E3
ligase activity. {ECO:0000255|PROSITE-ProRule:PRU00623}.
-!- SIMILARITY: Belongs to the poxviridae LAP protein family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF336128; AAK43550.1; -; Genomic_DNA.
EMBL; AF409138; AAN02734.1; -; Genomic_DNA.
ProteinModelPortal; Q91T40; -.
GO; GO:0044174; C:host cell endosome; IEA:UniProtKB-KW.
GO; GO:0044177; C:host cell Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0033644; C:host cell 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:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-KW.
GO; GO:0039504; P:suppression by virus of host adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0046776; P:suppression by virus of host antigen processing and presentation of peptide antigen via MHC class I; 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.
3: Inferred from homology;
Host endosome; Host Golgi apparatus; Host membrane;
Host-virus interaction;
Inhibition of host adaptive immune response by virus;
Inhibition of host MHC class I molecule presentation by virus;
Membrane; Metal-binding;
Modulation of host ubiquitin pathway by viral E3 ligase;
Modulation of host ubiquitin pathway by virus; Transferase;
Transmembrane; Transmembrane helix; Ubl conjugation pathway;
Viral immunoevasion; Zinc; Zinc-finger.
CHAIN 1 162 E3 ubiquitin-protein ligase LAP.
/FTId=PRO_0000396003.
TOPO_DOM 1 78 Cytoplasmic. {ECO:0000255}.
TRANSMEM 79 99 Helical. {ECO:0000255}.
TOPO_DOM 100 121 Lumenal. {ECO:0000255}.
TRANSMEM 122 142 Helical. {ECO:0000255}.
TOPO_DOM 143 162 Cytoplasmic. {ECO:0000255}.
ZN_FING 3 61 RING-CH-type. {ECO:0000255|PROSITE-
ProRule:PRU00623}.
COMPBIAS 89 94 Poly-Leu.
SEQUENCE 162 AA; 18782 MW; 5F914A4080F729EE CRC64;
MEGSDNTNTH CWICKDEYNV STNFCNCKNE FKIVHKNCLE EWINFSHNTK CKICNGKYNI
KKNKKSCLRW KCSFMYCNVP AICVSLICLL LLPLTILLVK FNLKSMLENI ENRDLIALIS
AMAYSLPCVV GFITVVHILI ALYDYYLAAK SDNTTYQVYE YI


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
EIAAB35404 E3 ubiquitin-protein ligase RNF133,Goliath-related E3 ubiquitin-protein ligase 2,Greul2,Mouse,Mus musculus,RING finger protein 133,Rnf133
EIAAB35429 E3 ubiquitin-protein ligase RNF149,Goliath-related E3 ubiquitin-protein ligase 4,Greul4,Mouse,Mus musculus,RING finger protein 149,Rnf149
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
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
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
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
25-847 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
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
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
25-845 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; 0.05 mg
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