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

Tegument protein VP22

 VP22_HHV11              Reviewed;         301 AA.
P10233; B9VQH7; Q09I85;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
25-OCT-2017, entry version 77.
RecName: Full=Tegument protein VP22;
ORFNames=UL49;
Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus
1).
Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae;
Alphaherpesvirinae; Simplexvirus.
NCBI_TaxID=10299;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=2839594; DOI=10.1099/0022-1317-69-7-1531;
McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C.,
McNab D., Perry L.J., Scott J.E., Taylor P.;
"The complete DNA sequence of the long unique region in the genome of
herpes simplex virus type 1.";
J. Gen. Virol. 69:1531-1574(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Nonneuroinvasive mutant HF10;
PubMed=17218138; DOI=10.1016/j.micinf.2006.10.019;
Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.;
"Determination and analysis of the DNA sequence of highly attenuated
herpes simplex virus type 1 mutant HF10, a potential oncolytic
virus.";
Microbes Infect. 9:142-149(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=17 syn+;
Cunningham C., Davison A.J.;
"Herpes simplex virus type 1 bacterial artificial chromosome.";
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
[4]
IDENTIFICATION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
PubMed=1312128; DOI=10.1099/0022-1317-73-3-723;
Elliott G.D., Meredith D.M.;
"The herpes simplex virus type 1 tegument protein VP22 is encoded by
gene UL49.";
J. Gen. Virol. 73:723-726(1992).
[5]
SUBCELLULAR LOCATION.
STRAIN=Isolate 1802;
PubMed=8659129; DOI=10.1006/viro.1996.0286;
Leslie J., Rixon F.J., McLauchlan J.;
"Overexpression of the herpes simplex virus type 1 tegument protein
VP22 increases its incorporation into virus particles.";
Virology 220:60-68(1996).
[6]
FUNCTION.
PubMed=9658087;
Elliott G., O'Hare P.;
"Herpes simplex virus type 1 tegument protein VP22 induces the
stabilization and hyperacetylation of microtubules.";
J. Virol. 72:6448-6455(1998).
[7]
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=11967313; DOI=10.1128/JVI.76.10.4961-4970.2002;
Martin A., O'Hare P., McLauchlan J., Elliott G.;
"Herpes simplex virus tegument protein VP22 contains overlapping
domains for cytoplasmic localization, microtubule interaction, and
chromatin binding.";
J. Virol. 76:4961-4970(2002).
[8]
FUNCTION, AND INTERACTION WITH HOST SET.
PubMed=12917472; DOI=10.1099/vir.0.19326-0;
van Leeuwen H., Okuwaki M., Hong R., Chakravarti D., Nagata K.,
O'Hare P.;
"Herpes simplex virus type 1 tegument protein VP22 interacts with TAF-
I proteins and inhibits nucleosome assembly but not regulation of
histone acetylation by INHAT.";
J. Gen. Virol. 84:2501-2510(2003).
[9]
SUBCELLULAR LOCATION.
STRAIN=F;
PubMed=15795259; DOI=10.1128/JVI.79.8.4730-4743.2005;
Yedowitz J.C., Kotsakis A., Schlegel E.F., Blaho J.A.;
"Nuclear localizations of the herpes simplex virus type 1 tegument
proteins VP13/14, vhs, and VP16 precede VP22-dependent microtubule
reorganization and VP22 nuclear import.";
J. Virol. 79:4730-4743(2005).
[10]
INTERACTION WITH GD AND GE.
STRAIN=F;
PubMed=17035313; DOI=10.1128/JVI.01842-06;
Farnsworth A., Wisner T.W., Johnson D.C.;
"Cytoplasmic residues of herpes simplex virus glycoprotein gE required
for secondary envelopment and binding of tegument proteins VP22 and
UL11 to gE and gD.";
J. Virol. 81:319-331(2007).
[11]
INTERACTION WITH GE.
STRAIN=17 syn+;
PubMed=16997344; DOI=10.1016/j.virol.2006.08.024;
O'Regan K.J., Bucks M.A., Murphy M.A., Wills J.W., Courtney R.J.;
"A conserved region of the herpes simplex virus type 1 tegument
protein VP22 facilitates interaction with the cytoplasmic tail of
glycoprotein E (gE).";
Virology 358:192-200(2007).
[12]
SUBCELLULAR LOCATION.
STRAIN=F;
PubMed=18353954; DOI=10.1128/JVI.02681-07;
Sugimoto K., Uema M., Sagara H., Tanaka M., Sata T., Hashimoto Y.,
Kawaguchi Y.;
"Simultaneous tracking of capsid, tegument, and envelope protein
localization in living cells infected with triply fluorescent herpes
simplex virus 1.";
J. Virol. 82:5198-5211(2008).
[13]
SUBCELLULAR LOCATION.
STRAIN=F;
PubMed=18596102; DOI=10.1128/JVI.00904-08;
Loret S., Guay G., Lippe R.;
"Comprehensive characterization of extracellular herpes simplex virus
type 1 virions.";
J. Virol. 82:8605-8618(2008).
[14]
SUBCELLULAR LOCATION, INTERACTION WITH GE AND VP16, AND LACK OF
INTERACTION WITH GD.
PubMed=19279114; DOI=10.1128/JVI.00069-09;
Stylianou J., Maringer K., Cook R., Bernard E., Elliott G.;
"Virion incorporation of the herpes simplex virus type 1 tegument
protein VP22 occurs via glycoprotein E-specific recruitment to the
late secretory pathway.";
J. Virol. 83:5204-5218(2009).
[15]
FUNCTION, AND INTERACTION WITH GE AND GM.
PubMed=22993164; DOI=10.1128/JVI.01913-12;
Maringer K., Stylianou J., Elliott G.;
"A network of protein interactions around the herpes simplex virus
tegument protein VP22.";
J. Virol. 86:12971-12982(2012).
[16]
FUNCTION.
PubMed=22951838; DOI=10.1128/JVI.01975-12;
Mbong E.F., Woodley L., Dunkerley E., Schrimpf J.E., Morrison L.A.,
Duffy C.;
"Deletion of the herpes simplex virus 1 UL49 gene results in mRNA and
protein translation defects that are complemented by secondary
mutations in UL41.";
J. Virol. 86:12351-12361(2012).
[17]
FUNCTION, AND INTERACTION WITH UL16.
PubMed=24131716; DOI=10.1128/JVI.02555-13;
Starkey J.L., Han J., Chadha P., Marsh J.A., Wills J.W.;
"Elucidation of the block to herpes simplex virus egress in the
absence of tegument protein UL16 reveals a novel interaction with
VP22.";
J. Virol. 88:110-119(2014).
-!- FUNCTION: Tegument protein that plays different roles during the
time course of infection. Participates in both the accumulation of
viral mRNAs and viral protein translation at late time of
infection. Modulates the RNase activity of the virion host shutoff
protein UL41 probably to ensure necessary levels of key cellular
mRNAs and proteins. Plays a role in microtubule reorganization
that occurs after viral infection by stabilizing microtubule
network. Finally, may prevent nucleosomal deposition onto the
viral genome by interacting with and inhibiting host SET.
{ECO:0000269|PubMed:12917472, ECO:0000269|PubMed:15795259,
ECO:0000269|PubMed:22951838, ECO:0000269|PubMed:22993164,
ECO:0000269|PubMed:24131716, ECO:0000269|PubMed:9658087}.
-!- SUBUNIT: Interacts with gE (via C-terminus); this interaction is
necessary for the recruitment of VP22 to the Golgi and its
packaging into virions. Interacts with gM (via C-terminus).
Interacts with VP16; this interaction allows the formation of a
tripartite complex composed of VP16, VP22 and UL41/VHS. According
PubMed:17035313 interacts with gD (via C-terminus). According
PubMed:19279114 does not interact with gD. Interacts with host
SET; this interaction may interfere with SET-mediated nucleosomal
deposition onto the viral genome. Interacts with the capsid-
binding protein UL16. {ECO:0000269|PubMed:12917472,
ECO:0000269|PubMed:16997344, ECO:0000269|PubMed:17035313,
ECO:0000269|PubMed:19279114, ECO:0000269|PubMed:22993164,
ECO:0000269|PubMed:24131716}.
-!- INTERACTION:
P06492:UL48; NbExp=2; IntAct=EBI-7490002, EBI-7489933;
-!- SUBCELLULAR LOCATION: Virion tegument
{ECO:0000269|PubMed:18596102, ECO:0000269|PubMed:8659129}. Host
cytoplasm {ECO:0000269|PubMed:11967313,
ECO:0000269|PubMed:1312128, ECO:0000269|PubMed:18353954,
ECO:0000269|PubMed:19279114}. Host nucleus
{ECO:0000269|PubMed:11967313, ECO:0000269|PubMed:15795259,
ECO:0000269|PubMed:18353954}. Host Golgi apparatus
{ECO:0000269|PubMed:19279114}. Note=One of the most abundant
tegument protein (about 2000 copies per virion). Localizes in the
cytoplasm at 8 hours postinfection and in the nucleus at 16 hours
postinfection. During virion morphogenesis, this protein probably
accumulates at the trans-Golgi where secondary envelopment occurs.
-!- PTM: Highly phosphorylated in the host cell. Packaging is
selective for underphosphorylated forms.
{ECO:0000305|PubMed:1312128}.
-!- SIMILARITY: Belongs to the alphaherpesvirinae VP22 tegument
protein family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X14112; CAA32299.1; -; Genomic_DNA.
EMBL; DQ889502; ABI63510.1; -; Genomic_DNA.
EMBL; FJ593289; ACM62272.1; -; Genomic_DNA.
PIR; D30089; WMBEF9.
RefSeq; YP_009137124.1; NC_001806.2.
PDB; 4XAL; X-ray; 1.87 A; A=174-281.
PDBsum; 4XAL; -.
SMR; P10233; -.
BioGrid; 971444; 8.
DIP; DIP-57160N; -.
IntAct; P10233; 3.
MINT; MINT-6732747; -.
PRIDE; P10233; -.
GeneID; 2703417; -.
KEGG; vg:2703417; -.
OrthoDB; VOG090000JT; -.
Proteomes; UP000009294; Genome.
Proteomes; UP000180652; Genome.
GO; GO:0044177; C:host cell Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0019033; C:viral tegument; IEA:UniProtKB-SubCell.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR006908; Herpes_UL49.
Pfam; PF04823; Herpes_UL49_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Host cytoplasm; Host Golgi apparatus;
Host nucleus; Host-virus interaction; Phosphoprotein;
Reference proteome; Virion; Virion tegument.
CHAIN 1 301 Tegument protein VP22.
/FTId=PRO_0000116093.
REGION 174 267 Interaction with gE.
MOTIF 163 166 Nuclear localization signal.
{ECO:0000250|UniProtKB:P30022}.
MOTIF 232 244 Nuclear export signal.
{ECO:0000250|UniProtKB:P30022}.
COMPBIAS 102 105 Poly-Pro.
VARIANT 20 20 E -> G (in strain: 17 syn+).
VARIANT 135 135 P -> Q (in strain: Nonneuroinvasive
mutant HF10).
VARIANT 141 141 R -> C (in strain: Nonneuroinvasive
mutant HF10).
VARIANT 220 220 L -> I (in strain: 17 syn+).
STRAND 182 184 {ECO:0000244|PDB:4XAL}.
HELIX 191 224 {ECO:0000244|PDB:4XAL}.
HELIX 229 238 {ECO:0000244|PDB:4XAL}.
STRAND 241 244 {ECO:0000244|PDB:4XAL}.
HELIX 248 250 {ECO:0000244|PDB:4XAL}.
HELIX 251 257 {ECO:0000244|PDB:4XAL}.
SEQUENCE 301 AA; 32254 MW; 6E9539C2AEE13E29 CRC64;
MTSRRSVKSG PREVPRDEYE DLYYTPSSGM ASPDSPPDTS RRGALQTRSR QRGEVRFVQY
DESDYALYGG SSSEDDEHPE VPRTRRPVSG AVLSGPGPAR APPPPAGSGG AGRTPTTAPR
APRTQRVATK APAAPAAETT RGRKSAQPES AALPDAPAST APTRSKTPAQ GLARKLHFST
APPNPDAPWT PRVAGFNKRV FCAAVGRLAA MHARMAAVQL WDMSRPRTDE DLNELLGITT
IRVTVCEGKN LLQRANELVN PDVVQDVDAA TATRGRSAAS RPTERPRAPA RSASRPRRPV
E


Related products :

Catalog number Product name Quantity
'BIN190 VZV HHV-3 Tegument protein VP22 antigen 1 mg
BIN190 VZV _ HHV_3 Tegument protein VP22 1 mg
BIN190 VZV _ HHV_3 Tegument protein VP22 1 mg
BIN190 VZV _ HHV_3 Tegument protein VP22 1 mg
'BIN190 VZV _ HHV-3 Tegument protein VP22 antigen 1 mg
Y104031 Cytomegalovirus (CMV) pp65 Tegument Protein (UL83) 200ug
Y102230 Cytomegalovirus (CMV) pp65 Tegument Protein (UL83) 200ug
C-VC-T681 anti-CMV antibodies Tegument protein (p68 nuclear) [clone C-VC-1)
C-VC-T681 Tegument protein (p68 nuclear) [clone C-VC-1) anti-CMV antibodies
Y053061 Anti-CMV Tegument protein (p68 nuclear) [clone C-vc-1] Antibody 100 μg
Y104031 Cytomegalovirus (CMV) pp65 Tegument Protein (UL83) Antibody 200ug
Y102230 Cytomegalovirus (CMV) pp65 Tegument Protein (UL83) Antibody 200ug
CSB-RP183074Ba Recombinant Human cytomegalovirus Tegument protein UL99 500ug
GWB-F1528D Cytomegalovirus (CMV) pp65 Tegument Protein (UL83), Antibody
Y053061 Anti_CMV Tegument protein (p68 nuclear) [clone C_vc_1] 100 μg
Y053061 Anti-CMV Tegument protein p68 nuclear [clone C-vc-1] antibody 250ug
10-663-45068 Cytomegalo Virus phosphoprotein-65 (pp65_UL83) - PP65; Tegument protein UL83 N_A 0.5 mg
10-663-45068 Cytomegalo Virus phosphoprotein-65 (pp65_UL83) - PP65; Tegument protein UL83 N_A 1 mg
10-663-45068 Cytomegalo Virus phosphoprotein-65 (pp65_UL83) - PP65; Tegument protein UL83 N_A 0.1 mg
CSB-RP183074Ba Recombinant Human cytomegalovirus Tegument protein UL99 Source: E.coli 1mg
10-663-45069 Cytomegalo Virus phosphoprotein 150 (pp150) - pp150; 150 kDa matrix phosphoprotein; Basic phosphoprotein; BPP; Tegument protein UL32 N_A 0.5 mg
10-663-45069 Cytomegalo Virus phosphoprotein 150 (pp150) - pp150; 150 kDa matrix phosphoprotein; Basic phosphoprotein; BPP; Tegument protein UL32 N_A 1 mg
10-663-45069 Cytomegalo Virus phosphoprotein 150 (pp150) - pp150; 150 kDa matrix phosphoprotein; Basic phosphoprotein; BPP; Tegument protein UL32 N_A 0.1 mg
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


 

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