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

Shutoff protein (100 kDa protein) (p100K) (100K-chaperone protein) (L4-100K) (Shutoff protein 100K)

 SHUT_ADECR              Reviewed;         689 AA.
P68967; Q65957;
01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
01-FEB-2005, sequence version 1.
07-JUN-2017, entry version 41.
RecName: Full=Shutoff protein {ECO:0000255|HAMAP-Rule:MF_04060};
AltName: Full=100 kDa protein {ECO:0000255|HAMAP-Rule:MF_04060};
Short=p100K {ECO:0000255|HAMAP-Rule:MF_04060};
AltName: Full=100K-chaperone protein {ECO:0000255|HAMAP-Rule:MF_04060};
AltName: Full=L4-100K {ECO:0000255|HAMAP-Rule:MF_04060};
AltName: Full=Shutoff protein 100K {ECO:0000255|HAMAP-Rule:MF_04060};
Name=L4 {ECO:0000255|HAMAP-Rule:MF_04060};
Canine adenovirus serotype 1 (strain RI261) (CAdV-1) (Canine
adenovirus 1 (strain RI261)).
Viruses; dsDNA viruses, no RNA stage; Adenoviridae; Mastadenovirus;
Canine mastadenovirus A.
NCBI_TaxID=69151;
NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=9129661;
Morrison M.D., Onions D.E., Nicolson L.;
"Complete DNA sequence of canine adenovirus type 1.";
J. Gen. Virol. 78:873-878(1997).
-!- FUNCTION: Protein that inhibits host translation while promoting
late viral translation by ribosome shunting. Blocks host cap-
dependent translation by binding to eIF4G, displacing MKNK1 from
cap initiation complexes and preventing EIF4E phosphorylation.
Binds to the tripartite leader sequence of viral late mRNAs and
recruits host eIF4G, PABPC1/poly-A binding protein and 40S
ribosomes subunits on viral mRNAs, allowing ribosome shunting and
efficient translation of late viral mRNAs even though conventional
translation via ribosome scanning from the cap has been shut off
in the host cell. During assembly, acts as a chaperone protein
that helps hexon proteins assembly into trimers.
{ECO:0000255|HAMAP-Rule:MF_04060}.
-!- SUBUNIT: Monomer. Interacts with hexon protein; this interaction
allows chaperoning and trimerization of hexon proteins. Interacts
(via N-terminus) with host initiation factor EIF4G (via C-
terminus). Interacts (via RRM domain) with viral mRNAs that
contain the tripartite leader; this interaction allows ribosome
shunting and expression of viral late mRNAs. {ECO:0000255|HAMAP-
Rule:MF_04060}.
-!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-
Rule:MF_04060}.
-!- INDUCTION: Expressed in the late phase of the viral replicative
cycle. {ECO:0000255|HAMAP-Rule:MF_04060}.
-!- PTM: Might be cleaved by the viral protease. {ECO:0000255|HAMAP-
Rule:MF_04060}.
-!- PTM: Phosphorylated. Tyrosine phosphorylation enhances
preferential binding to tripartite leader mRNAs and allows
ribosome shunting. {ECO:0000255|HAMAP-Rule:MF_04060}.
-!- PTM: Methylated. Asymmetric dimethylation by host PRMT1 of the
Arg/Gly-rich region may regulate shutoff protein binding to hexon
and promote the capsid assembly in the nucleus.
{ECO:0000255|HAMAP-Rule:MF_04060}.
-!- MISCELLANEOUS: All late proteins expressed from the major late
promoter are produced by alternative splicing and alternative
polyadenylation of the same gene giving rise to non-overlapping
ORFs. A leader sequence is present in the N-terminus of all these
mRNAs and is recognized by the viral shutoff protein to provide
expression although conventional translation via ribosome scanning
from the cap has been shut off in the host cell.
{ECO:0000255|HAMAP-Rule:MF_04060}.
-!- SIMILARITY: Belongs to the adenoviridae shutoff protein family.
{ECO:0000255|HAMAP-Rule:MF_04060}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Y07760; CAA69039.1; -; Genomic_DNA.
RefSeq; AP_000062.1; AC_000003.1.
RefSeq; NP_044201.1; NC_001734.1.
GeneID; 1488934; -.
KEGG; vg:1488934; -.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0019060; P:intracellular transport of viral protein in host cell; IEA:InterPro.
GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
GO; GO:0039704; P:viral translational shunt; ISS:UniProtKB.
HAMAP; MF_04060; ADV_SHUT; 1.
InterPro; IPR003381; Adeno_100.
Pfam; PF02438; Adeno_100; 1.
3: Inferred from homology;
Chaperone; Eukaryotic host gene expression shutoff by virus;
Eukaryotic host translation shutoff by virus; Host cytoplasm;
Host gene expression shutoff by virus; Host-virus interaction;
Inhibition of eukaryotic host translation factors by virus;
Late protein; Methylation; Phosphoprotein; RNA-binding;
Translational shunt; Transport.
CHAIN 1 689 Shutoff protein.
/FTId=PRO_0000221861.
DOMAIN 292 410 RRM. {ECO:0000255|HAMAP-Rule:MF_04060}.
REGION 226 289 Binding to host EIF4G.
{ECO:0000255|HAMAP-Rule:MF_04060}.
MOD_RES 309 309 Phosphotyrosine; by host.
{ECO:0000255|HAMAP-Rule:MF_04060}.
MOD_RES 627 627 Phosphotyrosine; by host.
{ECO:0000255|HAMAP-Rule:MF_04060}.
SEQUENCE 689 AA; 77373 MW; 6062D58E0ACE7763 CRC64;
MSEEPVSGTT VEIEEDTHTP PNSPVLETFS LSPEPEAEAC PNTDRYLSAN LLCKHLQRQS
AIVLDSIKDQ LQVPTSVSEL SCAYERSLLC PNIPPKQQSN GTCEANPKLN FYPTFLVPET
LATYHIFFVN QKIPVSCKAN RAKADKALTL QEGDCLPDYE TMDTVSRVFE GLGGEVVAEN
ALQNNDSVLV ELKEDNPRLA VLKRNLSVSH FAYPAVHLPP KIITTVMNNL LVKRANPSAD
VSELDPDGGQ EVVSDTELSR WLNTSDPETL EKQRKLVMGS VLVTVVLECM QRLFTSKDMV
KKIGETLHYT FRHGYVSLAC KISNVELTNV VTYMGILHEN RLGQTTLHHT IQGETRRDYI
RDSIFLILIH TWQTAMGIWQ QCLEEENLKE LAKLVQKIKK PLYTETSQRL MGKQLANVVF
PPKLLETFNK GLPDIVNQSM MQNFRSFILE RSGILPSMTC ALPTDFIPIH FKECPPTMWP
YTYLLRLANF FMYHNDLCYD MEGEGLLEHY CRCNLCTPHR CLATNPAMLN ETQLIGTFDI
RGPGGENGAE SSSGLKLTAG MWTSAFLRKF ESSDYHAHKI HFYENQSKPP SVEPTPCVIT
QSSILAQLHD IKKAREEFLL KKGQGQYLDP HTGEPLNAAG PSVESGHEFQ GDGRHREPKR
GRHFRQRGGP RKPPRAHAGG EPDVRGTTS


Related products :

Catalog number Product name Quantity
HYA-100K-1 Select-HA™100K 1 mg
Z5040002-100K M-MLV Reverse Transcriptase 100,000 units
HYA-100KEF-1 Select-HA™100K Low Endotoxin 1 mg
EIAAB30443 Androgen-induced proliferation inhibitor,Androgen-induced prostate proliferative shutoff-associated protein AS3,Aprin,As3,Pds5b,Rat,Rattus norvegicus,Sister chromatid cohesion protein PDS5 homolog B
EIAAB30441 Androgen-induced proliferation inhibitor,Androgen-induced prostate proliferative shutoff-associated protein AS3,Aprin,As3,Kiaa0979,Mouse,Mus musculus,Pds5b,Sister chromatid cohesion protein PDS5 homol
EIAAB30444 Androgen-induced proliferation inhibitor,Androgen-induced prostate proliferative shutoff-associated protein AS3,APRIN,AS3,Homo sapiens,Human,KIAA0979,PDS5B,Sister chromatid cohesion protein PDS5 homol
orb81737 HIV-2 gp36 His tag protein HIV-2 gp36 His tag recombinant- is 64 kDa protein and contains the sequence of HIV-2 envelope immunodominant regions gp36 having 6X His tag chaperone protein on the N-termin 100
orb81519 E.coli Chaperone Protein SKP protein Proteins 5
EIAAB41553 Leucine-rich repeat-containing protein 35,Lrrc35,Rat,Rattus norvegicus,Tbcel,Tubulin-specific chaperone cofactor E-like protein
EIAAB41552 Leucine-rich repeat-containing protein 35,Lrrc35,Mouse,Mus musculus,Tbcel,Tubulin-specific chaperone cofactor E-like protein
EIAAB41554 EL,Homo sapiens,Human,Leucine-rich repeat-containing protein 35,LRRC35,TBCEL,Tubulin-specific chaperone cofactor E-like protein
EIAAB11300 ABBP-2,APOBEC1-binding protein 2,DnaJ homolog subfamily B member 11,DnaJ protein homolog 9,DNAJB11,EDJ,ER-associated DNAJ,ER-associated dnaJ protein 3,ER-associated Hsp40 co-chaperone,ERdj3,ERJ3,ERj3p
EIAAB32887 C21LRP,C21-LRP,Chromosome 21 leucine-rich protein,Down syndrome critical region protein 2,DSCR2,Homo sapiens,Human,PAC1,PAC-1,Proteasome assembly chaperone 1,PSMG1
PAH-G1-2 Protein Arrays containing 234 Human Protein for simultaneous detection of Protein function, including Protein-protein interaction, Protein modification, antibody specificity, auto-antibody and small m 1 glass slide with 2 sub-arrays
29-850 The protein contains a RING finger, a motif present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions.The protein encoded by this 0.1 mg
29-844 RNF40 contains a RING finger, a motif known to be involved in protein-protein and protein-DNA interactions. This protein was reported to interact with the tumor suppressor protein RB1. Studies of the 0.1 mg
EIAAB32890 HCCA3,Hepatocellular carcinoma-susceptibility protein 3,Homo sapiens,Human,PAC2,PAC-2,Proteasome assembly chaperone 2,PSMG2,TNFSF5IP1,Tumor necrosis factor superfamily member 5-induced protein 1
EIAAB44668 Dap12,DNAX-activation protein 12,Karap,KAR-associated protein,Killer-activating receptor-associated protein,Mouse,Mus musculus,TYRO protein tyrosine kinase-binding protein,Tyrobp
EIAAB10617 DCN1-like protein 1,DCUN1 domain-containing protein 1,Dcun1d1,Dcun1l1,Defective in cullin neddylation protein 1-like protein 1,Mouse,Mus musculus,Rp42,Tes3,Testis-specific protein 3
EIAAB44667 DAP12,DNAX-activation protein 12,Homo sapiens,Human,KARAP,KAR-associated protein,Killer-activating receptor-associated protein,TYRO protein tyrosine kinase-binding protein,TYROBP
30-202 Calmegin is a testis-specific endoplasmic reticulum chaperone protein. CLGN may play a role in spermatogeneisis and infertility.Calmegin is a testis-specific endoplasmic reticulum chaperone protein. C 0.1 mg
18-003-43520 HSPB1-associated protein 1 - 27 KdA heat shock protein-associated protein 1; Protein associated with small stress protein 1 Polyclonal 0.05 mg Aff Pur
AS12 1848 Antibody: ZCP2 | Zinc Chaperone Protein, Immunogen: recombinant ZCP2 protein, ID 536252, Host: rabbit, polyclonal, Confirmed reactivity: Chlamydomonas reinhardtii 200
EIAAB25665 AML1T1,CBFA2T1,CDR,Cyclin-D-related protein,Eight twenty one protein,ETO,Homo sapiens,Human,MTG8,Protein CBFA2T1,Protein ETO,Protein MTG8,RUNX1T1,Zinc finger MYND domain-containing protein 2,ZMYND2
orb81519 E.coli Chaperone Protein SKP protein SKP Recombinant E.coli produced in E.coli is a single, non-glycosylated polypeptide chain containing 162 amino acids (21-161 a.a.) and having a molecular mass of 1 5


 

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