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HHV11:ICP0

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Species (Taxon ID) Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus1). (10299)
Gene Name(s) ICP0 (synonyms: IE110)
Protein Name(s) E3 ubiquitin-protein ligase ICP0

Alpha-0 protein Immediate-early protein IE110 Trans-acting transcriptional protein ICP0 VMW110

External Links
UniProt P08393
EMBL X14112
X14112
X04614
PIR A29152
RefSeq NP_044601.1
NP_044660.1
ProteinModelPortal P08393
DIP DIP-42446N
IntAct P08393
MINT MINT-1345075
GeneID 2703389
2703390
Proteomes UP000009294
GO GO:0030430
GO:0042025
GO:0019033
GO:0003677
GO:0016874
GO:0004842
GO:0008270
GO:0075342
GO:0039648
GO:0045732
GO:0000209
GO:0019046
GO:0034340
GO:0039593
GO:0039548
GO:0006351
Gene3D 3.30.40.10
InterPro IPR018957
IPR001841
IPR013083
IPR017907
Pfam PF00097
SMART SM00184
PROSITE PS00518
PS50089

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0039548

suppression by virus of host IRF3 activity

PMID:2861674[1]

ECO:0000314

P

Figure 1 shows ICP0 inhibits the sustained activation of IRF3 during the later stages of an HSV-1 infection.

complete
CACAO 5176

GO:0019046

release from viral latency

PMID:19264778[2]

ECO:0000315

P

Table 1 shows plaque formation (indicating cell lysis) before and after induction on ICP0 production. Table 10 also shows a summary of the data.

complete
CACAO 5194

GO:0019033

viral tegument

PMID:23408623[3]

ECO:0000314

C

Figure 6C

complete
CACAO 7002

part_of

GO:0019033

viral tegument

PMID:23408623[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004842

ubiquitin-protein transferase activity

PMID:15247261[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0000209

protein polyubiquitination

PMID:15247261[4]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0034340

response to type I interferon

PMID:16873258[5]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0075342

disruption by symbiont of host cell PML body

PMID:20106921[6]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0042025

host cell nucleus

PMID:15247261[4]

ECO:0000303

author statement without traceable support used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0039548

suppression by virus of host IRF3 activity

PMID:14747533[7]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR018957

F

Seeded From UniProt

complete

involved_in

GO:0045732

positive regulation of protein catabolic process

PMID:15247261[4]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0019046

release from viral latency

PMID:15247261[4]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0039648

modulation by virus of host protein ubiquitination

GO_REF:0000037
GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1128
UniProtKB-KW:KW-1130

P

Seeded From UniProt

complete

involved_in

GO:0039503

suppression by virus of host innate immune response

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1090

P

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

involved_in

GO:0016032

viral process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0945

P

Seeded From UniProt

complete

involved_in

GO:0030683

evasion or tolerance by virus of host immune response

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0899

P

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0238

F

Seeded From UniProt

complete

part_of

GO:0030430

host cell cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1035
UniProtKB-SubCell:SL-0381

C

Seeded From UniProt

complete

involved_in

GO:0039548

suppression by virus of host IRF3 activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1092

P

Seeded From UniProt

complete

part_of

GO:0042025

host cell nucleus

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1048
UniProtKB-SubCell:SL-0414

C

Seeded From UniProt

complete

involved_in

GO:0039593

suppression by virus of host exit from mitosis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1098

P

Seeded From UniProt

complete

involved_in

GO:0019042

viral latency

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1251

P

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

involved_in

GO:0060153

modulation by virus of host cell cycle

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1121

P

Seeded From UniProt

complete

involved_in

GO:0019046

release from viral latency

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1272

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Holley, MC (1985) Adaptation of a ciliary basal apparatus to cell shape changes in a contractile epithelium. Tissue Cell 17 321-34 PubMed GONUTS page
  2. Everett, RD et al. (2009) Analysis of the functions of herpes simplex virus type 1 regulatory protein ICP0 that are critical for lytic infection and derepression of quiescent viral genomes. J. Virol. 83 4963-77 PubMed GONUTS page
  3. 3.0 3.1 Henaff, D et al. (2013) Analysis of the early steps of herpes simplex virus 1 capsid tegumentation. J. Virol. 87 4895-906 PubMed GONUTS page
  4. 4.0 4.1 4.2 4.3 4.4 Canning, M et al. (2004) A RING finger ubiquitin ligase is protected from autocatalyzed ubiquitination and degradation by binding to ubiquitin-specific protease USP7. J. Biol. Chem. 279 38160-8 PubMed GONUTS page
  5. Negorev, DG et al. (2006) Differential role of Sp100 isoforms in interferon-mediated repression of herpes simplex virus type 1 immediate-early protein expression. J. Virol. 80 8019-29 PubMed GONUTS page
  6. Everett, RD et al. (2010) Comparison of the biological and biochemical activities of several members of the alphaherpesvirus ICP0 family of proteins. J. Virol. 84 3476-87 PubMed GONUTS page
  7. Lin, R et al. (2004) The herpes simplex virus ICP0 RING finger domain inhibits IRF3- and IRF7-mediated activation of interferon-stimulated genes. J. Virol. 78 1675-84 PubMed GONUTS page