HCVH:POLG

Species (Taxon ID)	Hepatitis C virus genotype 1a (isolate H) (HCV). (11108)
Gene Name(s)	No Information Provided.
Protein Name(s)	Genome polyprotein Core protein p21 Capsid protein C p21 Core protein p19 Envelope glycoprotein E1 gp32 gp35 Envelope glycoprotein E2 NS1 gp68 gp70 Viroporin p7 Protease NS2-3 p23 Serine protease NS3 Hepacivirin NS3P p70 Non-structural protein 4A NS4A p8 Non-structural protein 4B NS4B p27 Non-structural protein 5A NS5A p56 RNA-directed RNA polymerase NS5B p68
External Links
UniProt	P27958
EMBL	M67463 AF009606 AF011751 AF011752 AF011753
PIR	A36814
PDB	1A1R 1A1V 1CWX 1HEI 1JR6 1N1L 1ONB 1R7C 1R7D 1R7E 1R7F 1R7G 1RGQ 2A4R 2F9V 2HD0 2JXF 2KDR 2N1P 2O8M 2OBO 2OBQ 2OC0 2OC1 2OC7 2OC8 2OIN 2P59 2QV1 2XI2 2XI3 2XNI 4CL1 4JZN 4JZO 4MWF 4N0Y 4Q0X 4XVJ 4Z0X 5EOC 5ERW 5FGB 5FGC 5JZI 6BQJ 6BQK 6BZU 6BZV 6BZW 6BZY
PDBsum	1A1R 1A1V 1CWX 1HEI 1JR6 1N1L 1ONB 1R7C 1R7D 1R7E 1R7F 1R7G 1RGQ 2A4R 2F9V 2HD0 2JXF 2KDR 2N1P 2O8M 2OBO 2OBQ 2OC0 2OC1 2OC7 2OC8 2OIN 2P59 2QV1 2XI2 2XI3 2XNI 4CL1 4JZN 4JZO 4MWF 4N0Y 4Q0X 4XVJ 4Z0X 5EOC 5ERW 5FGB 5FGC 5JZI 6BQJ 6BQK 6BZU 6BZV 6BZW 6BZY
DisProt	DP00588
ProteinModelPortal	P27958
SMR	P27958
ELM	P27958
IntAct	P27958
BindingDB	P27958
ChEMBL	CHEMBL3638344
DrugBank	DB08644
iPTMnet	P27958
SwissPalm	P27958
PRIDE	P27958
euHCVdb	AF009606 AF011751 AF011752 AF011753 M67463
OrthoDB	VOG0900004E
BRENDA	3.4.21.98 3.6.4.13
Reactome	R-HSA-8854214
EvolutionaryTrace	P27958
Proteomes	UP000000518 UP000115192
GO	GO:0039714 GO:0033116 GO:0005576 GO:0030430 GO:0044164 GO:0044165 GO:0044167 GO:0044177 GO:0044186 GO:0033644 GO:0044191 GO:0042025 GO:0044220 GO:0020002 GO:0033647 GO:0016021 GO:0044385 GO:0019031 GO:0019013 GO:0055036 GO:0005524 GO:0008026 GO:0016887 GO:0060590 GO:0004197 GO:0017151 GO:0019899 GO:0031072 GO:0042802 GO:0005216 GO:1990254 GO:0019900 GO:0042288 GO:0002039 GO:0008233 GO:0019903 GO:0017137 GO:0003723 GO:0003968 GO:0005124 GO:0004252 GO:0008236 GO:0017124 GO:0097677 GO:0005198 GO:0035663 GO:0008134 GO:0031369 GO:0008270 GO:0075512 GO:0039654 GO:0039520 GO:0071593 GO:0039645 GO:0044833 GO:0019056 GO:0033663 GO:1990214 GO:0002674 GO:0032780 GO:0030889 GO:0060548 GO:0050689 GO:1900102 GO:0060702 GO:1900118 GO:0032715 GO:0070104 GO:0033673 GO:0031953 GO:0050709 GO:0090201 GO:1900369 GO:0034136 GO:0034144 GO:0034156 GO:0034164 GO:0000122 GO:0010804 GO:0042532 GO:0039707 GO:1990219 GO:1990216 GO:0010694 GO:0030307 GO:0008284 GO:0032467 GO:0010628 GO:1903721 GO:0045862 GO:0051047 GO:0045727 GO:1903265 GO:0048524 GO:0051259 GO:1900101 GO:0019050 GO:0046774 GO:0039560 GO:0039545 GO:0039644 GO:0039580 GO:0039613 GO:0039563 GO:0039547 GO:0039653 GO:0039502 GO:0019087 GO:0044053 GO:0046762 GO:0019082 GO:0039694 GO:0019062
CDD	cd00079
Gene3D	2.20.25.210 2.20.25.220
InterPro	IPR011492 IPR002521 IPR002522 IPR002519 IPR002531 IPR002518 IPR000745 IPR001490 IPR002868 IPR013193 IPR038568 IPR024350 IPR014001 IPR001650 IPR013192 IPR038170 IPR027417 IPR009003 IPR004109 IPR007094 IPR002166
Pfam	PF07652 PF01543 PF01542 PF01539 PF01560 PF01538 PF01006 PF01001 PF01506 PF08300 PF08301 PF12941 PF02907 PF00998
ProDom	PD001388
SMART	SM00487 SM00490
SUPFAM	SSF50494 SSF52540
PROSITE	PS51693 PS51192 PS51822 PS50507

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:1903301	positive regulation of hexokinase activity	PMID:24390321^[1]	ECO:0000314			P		Figure 7 shows statistically significant increases in hexokinase activity due to NS5A. Hepatitis C NS5A was used on Human Hexokinase	complete CACAO 13339
	GO:0019054	modulation by virus of host process	PMID:24390321^[1]	ECO:0000314			P		Figures 6 and 7 show that Hepatitis C Virus NS5A affect Human Glycolysis.	complete CACAO 13342
enables	GO:0035663	Toll-like receptor 2 binding	PMID:15521019^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0032467	positive regulation of cytokinesis	PMID:15521019^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0019900	kinase binding	PMID:17616579^[3]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0044053	translocation of peptides or proteins into host cell cytoplasm	PMID:25193851^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0000182)	Seeded From UniProt	complete
involved_in	GO:0039502	suppression by virus of host type I interferon-mediated signaling pathway	PMID:15825084^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0050709	negative regulation of protein secretion	PMID:16203724^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P04114)	Seeded From UniProt	complete
involved_in	GO:0000122	negative regulation of transcription by RNA polymerase II	PMID:16203724^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P55157)	Seeded From UniProt	complete
involved_in	GO:0001172	transcription, RNA-templated	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0003968	P		Seeded From UniProt	complete
involved_in	GO:0001172	transcription, RNA-templated	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0003968	P		Seeded From UniProt	complete
involved_in	GO:0001172	transcription, RNA-templated	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0003968	P		Seeded From UniProt	complete
involved_in	GO:0034220	ion transmembrane transport	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0005216	P		Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004109	P		Seeded From UniProt	complete
enables	GO:0008026	ATP-dependent helicase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR011492	F		Seeded From UniProt	complete
enables	GO:0008236	serine-type peptidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004109	F		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR013192	F		Seeded From UniProt	complete
involved_in	GO:0016032	viral process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000745	P		Seeded From UniProt	complete
enables	GO:0017111	nucleoside-triphosphatase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001490 InterPro:IPR002868	F		Seeded From UniProt	complete
part_of	GO:0019012	virion	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000745	C		Seeded From UniProt	complete
part_of	GO:0019028	viral capsid	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002522	C		Seeded From UniProt	complete
part_of	GO:0019031	viral envelope	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002519	C		Seeded From UniProt	complete
involved_in	GO:0019087	transformation of host cell by virus	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004109	P		Seeded From UniProt	complete
involved_in	GO:0039694	viral RNA genome replication	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002166 InterPro:IPR007094	P		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002166	F		Seeded From UniProt	complete
enables	GO:0003968	RNA-directed 5'-3' RNA polymerase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001490 InterPro:IPR002166 InterPro:IPR002868 InterPro:IPR007094	F		Seeded From UniProt	complete
enables	GO:0004197	cysteine-type endopeptidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001490 InterPro:IPR002518 InterPro:IPR002868	F		Seeded From UniProt	complete
enables	GO:0004252	serine-type endopeptidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001490 InterPro:IPR002868	F		Seeded From UniProt	complete
enables	GO:0005198	structural molecule activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002521 InterPro:IPR002522	F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR011492	F		Seeded From UniProt	complete
enables	GO:0003968	RNA-directed 5'-3' RNA polymerase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.7.7.48	F		Seeded From UniProt	complete
enables	GO:0017111	nucleoside-triphosphatase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.6.1.15	F		Seeded From UniProt	complete
involved_in	GO:0008284	positive regulation of cell population proliferation	PMID:12730672^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:O15350-2)	Seeded From UniProt	complete
involved_in	GO:0008284	positive regulation of cell population proliferation	PMID:12730672^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:O15350-1)	Seeded From UniProt	complete
involved_in	GO:0008284	positive regulation of cell population proliferation	PMID:12730672^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P04637)	Seeded From UniProt	complete
part_of	GO:0042025	host cell nucleus	PMID:12730672^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0044220	host cell perinuclear region of cytoplasm	PMID:12730672^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0030430	host cell cytoplasm	PMID:12730672^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0002039	p53 binding	PMID:12730672^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P04637	F		Seeded From UniProt	complete
involved_in	GO:0019056	modulation by virus of host transcription	PMID:12730672^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:O15350-2)	Seeded From UniProt	complete
involved_in	GO:0019056	modulation by virus of host transcription	PMID:12730672^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:O15350-1)	Seeded From UniProt	complete
involved_in	GO:0044833	modulation by virus of host protein transport	PMID:12730672^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P04637)	Seeded From UniProt	complete
involved_in	GO:0019056	modulation by virus of host transcription	PMID:12730672^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P04637)	Seeded From UniProt	complete
involved_in	GO:0046762	viral budding from ER membrane	PMID:17257269^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0044220	host cell perinuclear region of cytoplasm	PMID:14985081^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0030430	host cell cytoplasm	PMID:14985081^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1900118	negative regulation of execution phase of apoptosis	PMID:14985081^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1903721	positive regulation of I-kappaB phosphorylation	PMID:11374864^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1903265	positive regulation of tumor necrosis factor-mediated signaling pathway	PMID:11374864^[10]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P39429)	Seeded From UniProt	complete
involved_in	GO:1903265	positive regulation of tumor necrosis factor-mediated signaling pathway	PMID:11374864^[10]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P01375)	Seeded From UniProt	complete
enables	GO:0060590	ATPase regulator activity	PMID:10074132^[11]	ECO:0000314	direct assay evidence used in manual assertion		F	has_regulation_target:(UniProtKB:O00571)	Seeded From UniProt	complete
involved_in	GO:0002674	negative regulation of acute inflammatory response	PMID:20162731^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0033663	negative regulation by symbiont of host defense-related protein level	PMID:20162731^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0070104	negative regulation of interleukin-6-mediated signaling pathway	PMID:20162731^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1990216	positive regulation by symbiont of host transcription	PMID:20162731^[12]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P02675)	Seeded From UniProt	complete
involved_in	GO:0010628	positive regulation of gene expression	PMID:20162731^[12]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P02675)	Seeded From UniProt	complete
involved_in	GO:0010628	positive regulation of gene expression	PMID:10074132^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:O00571)	Seeded From UniProt	complete
part_of	GO:0044186	host cell lipid droplet	PMID:25122793^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0044165	host cell endoplasmic reticulum	PMID:25122793^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0030430	host cell cytoplasm	PMID:15846844^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0042288	MHC class I protein binding	PMID:15846844^[14]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q95HD8	F		Seeded From UniProt	complete
enables	GO:0019903	protein phosphatase binding	PMID:15846844^[14]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P24666	F		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:15846844^[14]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9Y680	F		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:15846844^[14]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q6P1N9	F		Seeded From UniProt	complete
enables	GO:1990254	keratin filament binding	PMID:15846844^[14]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P08727	F		Seeded From UniProt	complete
enables	GO:1990254	keratin filament binding	PMID:15846844^[14]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P05783	F		Seeded From UniProt	complete
enables	GO:1990254	keratin filament binding	PMID:15846844^[14]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P05787	F		Seeded From UniProt	complete
enables	GO:0017151	DEAD/H-box RNA helicase binding	PMID:15846844^[14]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P17844	F		Seeded From UniProt	complete
enables	GO:0031072	heat shock protein binding	PMID:15846844^[14]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P10809	F		Seeded From UniProt	complete
part_of	GO:0033647	host intracellular organelle	PMID:15846844^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0017151	DEAD/H-box RNA helicase binding	PMID:20862261^[15]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O00571	F		Seeded From UniProt	complete
involved_in	GO:1900369	negative regulation of RNA interference	PMID:18325616^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0060702	negative regulation of endoribonuclease activity	PMID:18325616^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:20881089^[17]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P27958:PRO_0000037566	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:10721731^[18]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P27958:PRO_0000037566	F		Seeded From UniProt	complete
part_of	GO:0042025	host cell nucleus	PMID:14985081^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1900118	negative regulation of execution phase of apoptosis	PMID:14985081^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1990214	negative regulation by symbiont of host protein levels	PMID:15825084^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P42224)	Seeded From UniProt	complete
involved_in	GO:0039502	suppression by virus of host type I interferon-mediated signaling pathway	PMID:15825084^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0044164	host cell cytosol	PMID:23667408^[19]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1900102	negative regulation of endoplasmic reticulum unfolded protein response	PMID:23667408^[19]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0044165	host cell endoplasmic reticulum	PMID:23667408^[19]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1990214	negative regulation by symbiont of host protein levels	PMID:15825084^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P42224)	Seeded From UniProt	complete
involved_in	GO:0039502	suppression by virus of host type I interferon-mediated signaling pathway	PMID:15825084^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0044165	host cell endoplasmic reticulum	PMID:8091646^[20]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0030889	negative regulation of B cell proliferation	PMID:10400713^[21]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P60033)	Seeded From UniProt	complete
involved_in	GO:0071593	lymphocyte aggregation	PMID:10400713^[21]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0033673	negative regulation of kinase activity	PMID:12610133^[22]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q9Z2B5)	Seeded From UniProt	complete
involved_in	GO:0031953	negative regulation of protein autophosphorylation	PMID:12610133^[22]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q9Z2B5)	Seeded From UniProt	complete
involved_in	GO:1900101	regulation of endoplasmic reticulum unfolded protein response	PMID:23667408^[19]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030307	positive regulation of cell growth	PMID:10390359^[23]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P19525)	Seeded From UniProt	complete
involved_in	GO:1990219	positive regulation by symbiont of host protein levels	PMID:10390359^[23]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0039580	suppression by virus of host PKR activity	PMID:10390359^[23]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P19525)	Seeded From UniProt	complete
involved_in	GO:0039613	suppression by virus of host protein phosphorylation	PMID:10390359^[23]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P19525)	Seeded From UniProt	complete
involved_in	GO:0045727	positive regulation of translation	PMID:12610133^[22]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q9Z2B5)	Seeded From UniProt	complete
part_of	GO:0044186	host cell lipid droplet	PMID:25122793^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0044177	host cell Golgi apparatus	PMID:25122793^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0044165	host cell endoplasmic reticulum	PMID:25122793^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1990214	negative regulation by symbiont of host protein levels	PMID:15825084^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P42224)	Seeded From UniProt	complete
involved_in	GO:0039502	suppression by virus of host type I interferon-mediated signaling pathway	PMID:15825084^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
colocalizes_with	GO:0044220	host cell perinuclear region of cytoplasm	PMID:12604806^[24]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005124	scavenger receptor binding	PMID:12356718^[25]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q8WTV0	F		Seeded From UniProt	complete
involved_in	GO:0090201	negative regulation of release of cytochrome c from mitochondria	PMID:12595532^[26]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q9UHD4)	Seeded From UniProt	complete
involved_in	GO:0060548	negative regulation of cell death	PMID:12595532^[26]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q9UHD4)	Seeded From UniProt	complete
part_of	GO:0030430	host cell cytoplasm	PMID:12595532^[26]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0042025	host cell nucleus	PMID:12595532^[26]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0044220	host cell perinuclear region of cytoplasm	PMID:12595532^[26]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0044165	host cell endoplasmic reticulum	PMID:25122793^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:12692242^[27]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P27958:PRO_0000037572	F		Seeded From UniProt	complete
part_of	GO:0033644	host cell membrane	PMID:7769685^[28]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0044164	host cell cytosol	PMID:7769685^[28]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0030430	host cell cytoplasm	PMID:9514871^[29]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0042025	host cell nucleus	PMID:9514871^[29]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	PMID:25193851^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:8861917^[30]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004252	serine-type endopeptidase activity	PMID:8861917^[30]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008233	peptidase activity	PMID:7769699^[31]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008233	peptidase activity	PMID:15303969^[32]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:1990214	negative regulation by symbiont of host protein levels	PMID:15825084^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P42224)	Seeded From UniProt	complete
involved_in	GO:0039502	suppression by virus of host type I interferon-mediated signaling pathway	PMID:15825084^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008236	serine-type peptidase activity	PMID:10570951^[33]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0030430	host cell cytoplasm	PMID:14524621^[34]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0042025	host cell nucleus	PMID:14524621^[34]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
colocalizes_with	GO:0044165	host cell endoplasmic reticulum	PMID:21559518^[35]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0051047	positive regulation of secretion	PMID:16033967^[36]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
colocalizes_with	GO:0044220	host cell perinuclear region of cytoplasm	PMID:16033967^[36]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
colocalizes_with	GO:0030430	host cell cytoplasm	PMID:16033967^[36]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0010694	positive regulation of alkaline phosphatase activity	PMID:16033967^[36]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:12692242^[27]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P27958:PRO_0000037573	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:11119590^[37]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P27958:PRO_0000037573	F		Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0008236	P		Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0008233	P		Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0008233	P		Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004252	P		Seeded From UniProt	complete
involved_in	GO:0048524	positive regulation of viral process	PMID:7769685^[28]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045862	positive regulation of proteolysis	PMID:7769685^[28]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P27958:PRO_0000037573)	Seeded From UniProt	complete
involved_in	GO:1990214	negative regulation by symbiont of host protein levels	PMID:15825084^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P42224)	Seeded From UniProt	complete
involved_in	GO:0039502	suppression by virus of host type I interferon-mediated signaling pathway	PMID:15825084^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
colocalizes_with	GO:0044165	host cell endoplasmic reticulum	PMID:21559518^[35]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0039502	suppression by virus of host type I interferon-mediated signaling pathway	PMID:15825084^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
colocalizes_with	GO:0044165	host cell endoplasmic reticulum	PMID:21559518^[35]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:12692242^[27]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P27958:PRO_0000037575	F		Seeded From UniProt	complete
part_of	GO:0039714	cytoplasmic viral factory	PMID:26874015^[38]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0039560	suppression by virus of host IRF9 activity	PMID:17275127^[39]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q00978)	Seeded From UniProt	complete
involved_in	GO:0046774	suppression by virus of host intracellular interferon activity	PMID:17275127^[39]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P01563)	Seeded From UniProt	complete
involved_in	GO:0039613	suppression by virus of host protein phosphorylation	PMID:17275127^[39]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0044220	host cell perinuclear region of cytoplasm	PMID:17275127^[39]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0097677	STAT family protein binding	PMID:17275127^[39]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P42224	F		Seeded From UniProt	complete
involved_in	GO:0042532	negative regulation of tyrosine phosphorylation of STAT protein	PMID:17275127^[39]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P42224)	Seeded From UniProt	complete
part_of	GO:0039714	cytoplasmic viral factory	PMID:26152585^[40]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0030430	host cell cytoplasm	PMID:11821416^[41]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0039547	suppression by virus of host TRAF activity	PMID:11821416^[41]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P39429)	Seeded From UniProt	complete
involved_in	GO:0039644	suppression by virus of host NF-kappaB transcription factor activity	PMID:11821416^[41]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P39429)	Seeded From UniProt	complete
part_of	GO:0042025	host cell nucleus	PMID:11821416^[41]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0039644	suppression by virus of host NF-kappaB transcription factor activity	PMID:11821416^[41]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010804	negative regulation of tumor necrosis factor-mediated signaling pathway	PMID:11821416^[41]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1990219	positive regulation by symbiont of host protein levels	PMID:10390359^[23]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
NOT\|involved_in	GO:0039502	suppression by virus of host type I interferon-mediated signaling pathway	PMID:15825084^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0019900	kinase binding	PMID:15607035^[42]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P42356	F		Seeded From UniProt	complete
enables	GO:0017137	Rab GTPase binding	PMID:17686842^[43]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q96BZ9	F		Seeded From UniProt	complete
involved_in	GO:0019050	suppression by virus of host apoptotic process	PMID:16530520^[44]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0033644	host cell membrane	PMID:16530520^[44]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0044186	host cell lipid droplet	PMID:22491470^[45]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
colocalizes_with	GO:0044165	host cell endoplasmic reticulum	PMID:22491470^[45]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
colocalizes_with	GO:0044165	host cell endoplasmic reticulum	PMID:21559518^[35]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0034164	negative regulation of toll-like receptor 9 signaling pathway	PMID:17567694^[46]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034156	negative regulation of toll-like receptor 7 signaling pathway	PMID:17567694^[46]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034144	negative regulation of toll-like receptor 4 signaling pathway	PMID:17567694^[46]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034136	negative regulation of toll-like receptor 2 signaling pathway	PMID:17567694^[46]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032715	negative regulation of interleukin-6 production	PMID:17567694^[46]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0044220	host cell perinuclear region of cytoplasm	PMID:10702287^[47]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0039653	suppression by virus of host transcription	PMID:10702287^[47]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008134	transcription factor binding	PMID:10702287^[47]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q6ZRS2	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:12692242^[27]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P27958:PRO_0000037576	F		Seeded From UniProt	complete
part_of	GO:0030430	host cell cytoplasm	PMID:9514871^[29]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0042025	host cell nucleus	PMID:9514871^[29]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
NOT\|involved_in	GO:0039502	suppression by virus of host type I interferon-mediated signaling pathway	PMID:15825084^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
colocalizes_with	GO:0044165	host cell endoplasmic reticulum	PMID:21559518^[35]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0017151	DEAD/H-box RNA helicase binding	PMID:21559518^[35]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9H6S0	F		Seeded From UniProt	complete
part_of	GO:0044220	host cell perinuclear region of cytoplasm	PMID:11922617^[48]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0032780	negative regulation of ATPase activity	PMID:11922617^[48]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q14240)	Seeded From UniProt	complete
enables	GO:0031369	translation initiation factor binding	PMID:11922617^[48]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q14240	F		Seeded From UniProt	complete
enables	GO:0003968	RNA-directed 5'-3' RNA polymerase activity	PMID:11922617^[48]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0001172	transcription, RNA-templated	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0003968	P		Seeded From UniProt	complete
part_of	GO:0033116	endoplasmic reticulum-Golgi intermediate compartment membrane	Reactome:R-HSA-8854290	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0008233	peptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	F		Seeded From UniProt	complete
involved_in	GO:0039563	suppression by virus of host STAT1 activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1105	P		Seeded From UniProt	complete
enables	GO:0003968	RNA-directed 5'-3' RNA polymerase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0696	F		Seeded From UniProt	complete
involved_in	GO:0039545	suppression by virus of host MAVS activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1097	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
part_of	GO:0020002	host cell plasma membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1032 UniProtKB-SubCell:SL-0375	C		Seeded From UniProt	complete
part_of	GO:0044186	host cell lipid droplet	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1041 UniProtKB-SubCell:SL-0401	C		Seeded From UniProt	complete
part_of	GO:0016021	integral component of membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0812	C		Seeded From UniProt	complete
involved_in	GO:0039654	fusion of virus membrane with host endosome membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1170	P		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
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
involved_in	GO:0008152	metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0511	P		Seeded From UniProt	complete
part_of	GO:0019028	viral capsid	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0167	C		Seeded From UniProt	complete
part_of	GO:0019031	viral envelope	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0261	C		Seeded From UniProt	complete
involved_in	GO:0051259	protein complex oligomerization	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1182	P		Seeded From UniProt	complete
involved_in	GO:0039707	pore formation by virus in membrane of host cell	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1182	P		Seeded From UniProt	complete
involved_in	GO:0039645	modulation by virus of host G1/S transition checkpoint	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1078	P		Seeded From UniProt	complete
enables	GO:0016779	nucleotidyltransferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0548	F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F		Seeded From UniProt	complete
part_of	GO:0044385	integral to membrane of host cell	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1182	C		Seeded From UniProt	complete
involved_in	GO:0046718	viral entry into host cell	GO_REF:0000037 GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1160 UniProtKB-KW:KW-1162	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:0008234	cysteine-type peptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0788	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
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt	complete
involved_in	GO:0039663	membrane fusion involved in viral entry into host cell	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1168	P		Seeded From UniProt	complete
involved_in	GO:0075512	clathrin-dependent endocytosis of virus by host cell	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1165	P		Seeded From UniProt	complete
involved_in	GO:0039520	induction by virus of host autophagy	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1072	P		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
enables	GO:0017124	SH3 domain binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0729	F		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
part_of	GO:0033650	host cell mitochondrion	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1045 UniProtKB-SubCell:SL-0407	C		Seeded From UniProt	complete
part_of	GO:0044165	host cell endoplasmic reticulum	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1038	C		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0964 UniProtKB-SubCell:SL-0243	C		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0694	F		Seeded From UniProt	complete
enables	GO:0005216	ion channel activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1182	F		Seeded From UniProt	complete
involved_in	GO:0019062	virion attachment to host cell	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1161	P		Seeded From UniProt	complete
enables	GO:0004386	helicase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0347	F		Seeded From UniProt	complete
involved_in	GO:0075509	endocytosis involved in viral entry into host cell	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1164	P		Seeded From UniProt	complete
involved_in	GO:0039502	suppression by virus of host type I interferon-mediated signaling pathway	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1114	P		Seeded From UniProt	complete
part_of	GO:0019013	viral nucleocapsid	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0543	C		Seeded From UniProt	complete
enables	GO:0003824	catalytic activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0511	F		Seeded From UniProt	complete
involved_in	GO:0006811	ion transport	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0406	P		Seeded From UniProt	complete
involved_in	GO:0030683	evasion or tolerance by virus of host immune response	GO_REF:0000037 GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0899 UniProtKB-KW:KW-0922	P		Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F		Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	P		Seeded From UniProt	complete
part_of	GO:0019012	virion	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0946 UniProtKB-SubCell:SL-0274	C		Seeded From UniProt	complete
enables	GO:0008236	serine-type peptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0720	F		Seeded From UniProt	complete
part_of	GO:0033644	host cell membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1043	C		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:0039547	suppression by virus of host TRAF activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1110	P		Seeded From UniProt	complete
part_of	GO:0044220	host cell perinuclear region of cytoplasm	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0382	C		Seeded From UniProt	complete
part_of	GO:0055036	virion membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0275	C		Seeded From UniProt	complete
part_of	GO:0044167	host cell endoplasmic reticulum membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0390	C		Seeded From UniProt	complete
part_of	GO:0044191	host cell mitochondrial membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0410	C		Seeded From UniProt	complete
involved_in	GO:0050689	negative regulation of defense response to virus by host	PMID:24263861^[49]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0019082	viral protein processing	PMID:24263861^[49]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
edit table

Notes

References

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

↑ ^1.0 ^1.1 Ramière, C et al. (2014) Activity of hexokinase is increased by its interaction with hepatitis C virus protein NS5A. J. Virol. 88 3246-54 PubMed GONUTS page
↑ ^2.0 ^2.1 Dolganiuc, A et al. (2004) Hepatitis C core and nonstructural 3 proteins trigger toll-like receptor 2-mediated pathways and inflammatory activation. Gastroenterology 127 1513-24 PubMed GONUTS page
↑ Randall, G et al. (2007) Cellular cofactors affecting hepatitis C virus infection and replication. Proc. Natl. Acad. Sci. U.S.A. 104 12884-9 PubMed GONUTS page
↑ ^4.0 ^4.1 Picard-Jean, F et al. (2014) The intracellular inhibition of HCV replication represents a novel mechanism of action by the innate immune Lactoferrin protein. Antiviral Res. 111 13-22 PubMed GONUTS page
↑ ^5.00 ^5.01 ^5.02 ^5.03 ^5.04 ^5.05 ^5.06 ^5.07 ^5.08 ^5.09 ^5.10 ^5.11 ^5.12 ^5.13 Lin, W et al. (2005) Hepatitis C virus expression suppresses interferon signaling by degrading STAT1. Gastroenterology 128 1034-41 PubMed GONUTS page
↑ ^6.0 ^6.1 Domitrovich, AM et al. (2005) Hepatitis C virus nonstructural proteins inhibit apolipoprotein B100 secretion. J. Biol. Chem. 280 39802-8 PubMed GONUTS page
↑ ^7.00 ^7.01 ^7.02 ^7.03 ^7.04 ^7.05 ^7.06 ^7.07 ^7.08 ^7.09 ^7.10 Alisi, A et al. (2003) Physical and functional interaction between HCV core protein and the different p73 isoforms. Oncogene 22 2573-80 PubMed GONUTS page
↑ Hourioux, C et al. (2007) Core protein domains involved in hepatitis C virus-like particle assembly and budding at the endoplasmic reticulum membrane. Cell. Microbiol. 9 1014-27 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 ^9.3 ^9.4 Cao, Y et al. (2004) Hepatitis C virus core protein interacts with p53-binding protein, 53BP2/Bbp/ASPP2, and inhibits p53-mediated apoptosis. Biochem. Biophys. Res. Commun. 315 788-95 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 Chung, YM et al. (2001) Hepatitis C virus core protein potentiates TNF-alpha-induced NF-kappaB activation through TRAF2-IKKbeta-dependent pathway. Biochem. Biophys. Res. Commun. 284 15-9 PubMed GONUTS page
↑ ^11.0 ^11.1 You, LR et al. (1999) Hepatitis C virus core protein interacts with cellular putative RNA helicase. J. Virol. 73 2841-53 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 ^12.3 ^12.4 Ait-Goughoulte, M et al. (2010) Hepatitis C virus core protein interacts with fibrinogen-beta and attenuates cytokine stimulated acute-phase response. Hepatology 51 1505-13 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 ^13.3 ^13.4 ^13.5 Lee, JY et al. (2014) Apolipoprotein E likely contributes to a maturation step of infectious hepatitis C virus particles and interacts with viral envelope glycoproteins. J. Virol. 88 12422-37 PubMed GONUTS page
↑ ^14.00 ^14.01 ^14.02 ^14.03 ^14.04 ^14.05 ^14.06 ^14.07 ^14.08 ^14.09 ^14.10 Kang, SM et al. (2005) Proteomic profiling of cellular proteins interacting with the hepatitis C virus core protein. Proteomics 5 2227-37 PubMed GONUTS page
↑ Sun, C et al. (2010) Hepatitis C virus core-derived peptides inhibit genotype 1b viral genome replication via interaction with DDX3X. PLoS ONE 5 PubMed GONUTS page
↑ ^16.0 ^16.1 Chen, W et al. (2008) HCV core protein interacts with Dicer to antagonize RNA silencing. Virus Res. 133 250-8 PubMed GONUTS page
↑ Mousseau, G et al. (2011) Dimerization-driven interaction of hepatitis C virus core protein with NS3 helicase. J. Gen. Virol. 92 101-11 PubMed GONUTS page
↑ Flajolet, M et al. (2000) A genomic approach of the hepatitis C virus generates a protein interaction map. Gene 242 369-79 PubMed GONUTS page
↑ ^19.0 ^19.1 ^19.2 ^19.3 Egan, PA et al. (2013) Hepatitis C Virus Envelope Protein E1 Binds PERK and Represses the Unfolded Protein Response. Open Virol J 7 37-40 PubMed GONUTS page
↑ Selby, MJ et al. (1994) Complex processing and protein:protein interactions in the E2:NS2 region of HCV. Virology 204 114-22 PubMed GONUTS page
↑ ^21.0 ^21.1 Flint, M et al. (1999) Characterization of hepatitis C virus E2 glycoprotein interaction with a putative cellular receptor, CD81. J. Virol. 73 6235-44 PubMed GONUTS page
↑ ^22.0 ^22.1 ^22.2 Pavio, N et al. (2003) Protein synthesis and endoplasmic reticulum stress can be modulated by the hepatitis C virus envelope protein E2 through the eukaryotic initiation factor 2alpha kinase PERK. J. Virol. 77 3578-85 PubMed GONUTS page
↑ ^23.0 ^23.1 ^23.2 ^23.3 ^23.4 Taylor, DR et al. (1999) Inhibition of the interferon-inducible protein kinase PKR by HCV E2 protein. Science 285 107-10 PubMed GONUTS page
↑ Kien, F et al. (2003) Analysis of the subcellular localization of hepatitis C virus E2 glycoprotein in live cells using EGFP fusion proteins. J. Gen. Virol. 84 561-6 PubMed GONUTS page
↑ Scarselli, E et al. (2002) The human scavenger receptor class B type I is a novel candidate receptor for the hepatitis C virus. EMBO J. 21 5017-25 PubMed GONUTS page
↑ ^26.0 ^26.1 ^26.2 ^26.3 ^26.4 Erdtmann, L et al. (2003) The hepatitis C virus NS2 protein is an inhibitor of CIDE-B-induced apoptosis. J. Biol. Chem. 278 18256-64 PubMed GONUTS page
↑ ^27.0 ^27.1 ^27.2 ^27.3 Dimitrova, M et al. (2003) Protein-protein interactions between hepatitis C virus nonstructural proteins. J. Virol. 77 5401-14 PubMed GONUTS page
↑ ^28.0 ^28.1 ^28.2 ^28.3 Satoh, S et al. (1995) The N-terminal region of hepatitis C virus nonstructural protein 3 (NS3) is essential for stable complex formation with NS4A. J. Virol. 69 4255-60 PubMed GONUTS page
↑ ^29.0 ^29.1 ^29.2 ^29.3 Ishido, S et al. (1998) Complex formation of NS5B with NS3 and NS4A proteins of hepatitis C virus. Biochem. Biophys. Res. Commun. 244 35-40 PubMed GONUTS page
↑ ^30.0 ^30.1 Kim, JL et al. (1996) Crystal structure of the hepatitis C virus NS3 protease domain complexed with a synthetic NS4A cofactor peptide. Cell 87 343-55 PubMed GONUTS page
↑ Lin, C et al. (1995) A central region in the hepatitis C virus NS4A protein allows formation of an active NS3-NS4A serine proteinase complex in vivo and in vitro. J. Virol. 69 4373-80 PubMed GONUTS page
↑ Khu, YL et al. (2004) Hepatitis C virus non-structural protein NS3 interacts with LMP7, a component of the immunoproteasome, and affects its proteasome activity. Biochem. J. 384 401-9 PubMed GONUTS page
↑ Drouet, C et al. (1999) Hepatitis C virus NS3 serine protease interacts with the serpin C1 inhibitor. FEBS Lett. 458 415-8 PubMed GONUTS page
↑ ^34.0 ^34.1 Iwai, A et al. (2003) Hepatitis C virus nonstructural protein NS3 binds to Sm-D1, a small nuclear ribonucleoprotein associated with autoimmune disease. Microbiol. Immunol. 47 601-11 PubMed GONUTS page
↑ ^35.0 ^35.1 ^35.2 ^35.3 ^35.4 ^35.5 Morohashi, K et al. (2011) Cyclosporin A associated helicase-like protein facilitates the association of hepatitis C virus RNA polymerase with its cellular cyclophilin B. PLoS ONE 6 e18285 PubMed GONUTS page
↑ ^36.0 ^36.1 ^36.2 ^36.3 Hidajat, R et al. (2005) Hepatitis C virus NS3 protein interacts with ELKS-{delta} and ELKS-{alpha}, members of a novel protein family involved in intracellular transport and secretory pathways. J. Gen. Virol. 86 2197-208 PubMed GONUTS page
↑ Khu, YL et al. (2001) Mutations that affect dimer formation and helicase activity of the hepatitis C virus helicase. J. Virol. 75 205-14 PubMed GONUTS page
↑ Eyre, NS et al. (2016) Phosphorylation of NS5A Serine-235 is essential to hepatitis C virus RNA replication and normal replication compartment formation. Virology 491 27-44 PubMed GONUTS page
↑ ^39.0 ^39.1 ^39.2 ^39.3 ^39.4 ^39.5 Lan, KH et al. (2007) HCV NS5A inhibits interferon-alpha signaling through suppression of STAT1 phosphorylation in hepatocyte-derived cell lines. J. Hepatol. 46 759-67 PubMed GONUTS page
↑ Romero-Brey, I et al. (2015) NS5A Domain 1 and Polyprotein Cleavage Kinetics Are Critical for Induction of Double-Membrane Vesicles Associated with Hepatitis C Virus Replication. MBio 6 e00759 PubMed GONUTS page
↑ ^41.0 ^41.1 ^41.2 ^41.3 ^41.4 ^41.5 Park, KJ et al. (2002) Nonstructural 5A protein of hepatitis C virus modulates tumor necrosis factor alpha-stimulated nuclear factor kappa B activation. J. Biol. Chem. 277 13122-8 PubMed GONUTS page
↑ Ahn, J et al. (2004) Systematic identification of hepatocellular proteins interacting with NS5A of the hepatitis C virus. J. Biochem. Mol. Biol. 37 741-8 PubMed GONUTS page
↑ Sklan, EH et al. (2007) A Rab-GAP TBC domain protein binds hepatitis C virus NS5A and mediates viral replication. J. Virol. 81 11096-105 PubMed GONUTS page
↑ ^44.0 ^44.1 Nanda, SK et al. (2006) The SH3 binding motif of HCV [corrected] NS5A protein interacts with Bin1 and is important for apoptosis and infectivity. Gastroenterology 130 794-809 PubMed GONUTS page
↑ ^45.0 ^45.1 Nevo-Yassaf, I et al. (2012) Role for TBC1D20 and Rab1 in hepatitis C virus replication via interaction with lipid droplet-bound nonstructural protein 5A. J. Virol. 86 6491-502 PubMed GONUTS page
↑ ^46.0 ^46.1 ^46.2 ^46.3 ^46.4 Abe, T et al. (2007) Hepatitis C virus nonstructural protein 5A modulates the toll-like receptor-MyD88-dependent signaling pathway in macrophage cell lines. J. Virol. 81 8953-66 PubMed GONUTS page
↑ ^47.0 ^47.1 ^47.2 Ghosh, AK et al. (2000) Hepatitis C virus NS5A protein modulates transcription through a novel cellular transcription factor SRCAP. J. Biol. Chem. 275 7184-8 PubMed GONUTS page
↑ ^48.0 ^48.1 ^48.2 ^48.3 Kyono, K et al. (2002) Human eukaryotic initiation factor 4AII associates with hepatitis C virus NS5B protein in vitro. Biochem. Biophys. Res. Commun. 292 659-66 PubMed GONUTS page
↑ ^49.0 ^49.1 Sakata, K et al. (2013) HCV NS3 protease enhances liver fibrosis via binding to and activating TGF-β type I receptor. Sci Rep 3 3243 PubMed GONUTS page

[PMID:24390321-1] 1.0 ^1.1 Ramière, C et al. (2014) Activity of hexokinase is increased by its interaction with hepatitis C virus protein NS5A. J. Virol. 88 3246-54 PubMed GONUTS page

[PMID:15521019-2] 2.0 ^2.1 Dolganiuc, A et al. (2004) Hepatitis C core and nonstructural 3 proteins trigger toll-like receptor 2-mediated pathways and inflammatory activation. Gastroenterology 127 1513-24 PubMed GONUTS page

[PMID:17616579-3] Randall, G et al. (2007) Cellular cofactors affecting hepatitis C virus infection and replication. Proc. Natl. Acad. Sci. U.S.A. 104 12884-9 PubMed GONUTS page

[PMID:25193851-4] 4.0 ^4.1 Picard-Jean, F et al. (2014) The intracellular inhibition of HCV replication represents a novel mechanism of action by the innate immune Lactoferrin protein. Antiviral Res. 111 13-22 PubMed GONUTS page

[PMID:15825084-5] 5.00 ^5.01 ^5.02 ^5.03 ^5.04 ^5.05 ^5.06 ^5.07 ^5.08 ^5.09 ^5.10 ^5.11 ^5.12 ^5.13 Lin, W et al. (2005) Hepatitis C virus expression suppresses interferon signaling by degrading STAT1. Gastroenterology 128 1034-41 PubMed GONUTS page

[PMID:16203724-6] 6.0 ^6.1 Domitrovich, AM et al. (2005) Hepatitis C virus nonstructural proteins inhibit apolipoprotein B100 secretion. J. Biol. Chem. 280 39802-8 PubMed GONUTS page

[PMID:12730672-7] 7.00 ^7.01 ^7.02 ^7.03 ^7.04 ^7.05 ^7.06 ^7.07 ^7.08 ^7.09 ^7.10 Alisi, A et al. (2003) Physical and functional interaction between HCV core protein and the different p73 isoforms. Oncogene 22 2573-80 PubMed GONUTS page

[PMID:17257269-8] Hourioux, C et al. (2007) Core protein domains involved in hepatitis C virus-like particle assembly and budding at the endoplasmic reticulum membrane. Cell. Microbiol. 9 1014-27 PubMed GONUTS page

[PMID:14985081-9] 9.0 ^9.1 ^9.2 ^9.3 ^9.4 Cao, Y et al. (2004) Hepatitis C virus core protein interacts with p53-binding protein, 53BP2/Bbp/ASPP2, and inhibits p53-mediated apoptosis. Biochem. Biophys. Res. Commun. 315 788-95 PubMed GONUTS page

[PMID:11374864-10] 10.0 ^10.1 ^10.2 Chung, YM et al. (2001) Hepatitis C virus core protein potentiates TNF-alpha-induced NF-kappaB activation through TRAF2-IKKbeta-dependent pathway. Biochem. Biophys. Res. Commun. 284 15-9 PubMed GONUTS page

[PMID:10074132-11] 11.0 ^11.1 You, LR et al. (1999) Hepatitis C virus core protein interacts with cellular putative RNA helicase. J. Virol. 73 2841-53 PubMed GONUTS page

[PMID:20162731-12] 12.0 ^12.1 ^12.2 ^12.3 ^12.4 Ait-Goughoulte, M et al. (2010) Hepatitis C virus core protein interacts with fibrinogen-beta and attenuates cytokine stimulated acute-phase response. Hepatology 51 1505-13 PubMed GONUTS page

[PMID:25122793-13] 13.0 ^13.1 ^13.2 ^13.3 ^13.4 ^13.5 Lee, JY et al. (2014) Apolipoprotein E likely contributes to a maturation step of infectious hepatitis C virus particles and interacts with viral envelope glycoproteins. J. Virol. 88 12422-37 PubMed GONUTS page

[PMID:15846844-14] 14.00 ^14.01 ^14.02 ^14.03 ^14.04 ^14.05 ^14.06 ^14.07 ^14.08 ^14.09 ^14.10 Kang, SM et al. (2005) Proteomic profiling of cellular proteins interacting with the hepatitis C virus core protein. Proteomics 5 2227-37 PubMed GONUTS page

[PMID:20862261-15] Sun, C et al. (2010) Hepatitis C virus core-derived peptides inhibit genotype 1b viral genome replication via interaction with DDX3X. PLoS ONE 5 PubMed GONUTS page

[PMID:18325616-16] 16.0 ^16.1 Chen, W et al. (2008) HCV core protein interacts with Dicer to antagonize RNA silencing. Virus Res. 133 250-8 PubMed GONUTS page

[PMID:20881089-17] Mousseau, G et al. (2011) Dimerization-driven interaction of hepatitis C virus core protein with NS3 helicase. J. Gen. Virol. 92 101-11 PubMed GONUTS page

[PMID:10721731-18] Flajolet, M et al. (2000) A genomic approach of the hepatitis C virus generates a protein interaction map. Gene 242 369-79 PubMed GONUTS page

[PMID:23667408-19] 19.0 ^19.1 ^19.2 ^19.3 Egan, PA et al. (2013) Hepatitis C Virus Envelope Protein E1 Binds PERK and Represses the Unfolded Protein Response. Open Virol J 7 37-40 PubMed GONUTS page

[PMID:8091646-20] Selby, MJ et al. (1994) Complex processing and protein:protein interactions in the E2:NS2 region of HCV. Virology 204 114-22 PubMed GONUTS page

[PMID:10400713-21] 21.0 ^21.1 Flint, M et al. (1999) Characterization of hepatitis C virus E2 glycoprotein interaction with a putative cellular receptor, CD81. J. Virol. 73 6235-44 PubMed GONUTS page

[PMID:12610133-22] 22.0 ^22.1 ^22.2 Pavio, N et al. (2003) Protein synthesis and endoplasmic reticulum stress can be modulated by the hepatitis C virus envelope protein E2 through the eukaryotic initiation factor 2alpha kinase PERK. J. Virol. 77 3578-85 PubMed GONUTS page

[PMID:10390359-23] 23.0 ^23.1 ^23.2 ^23.3 ^23.4 Taylor, DR et al. (1999) Inhibition of the interferon-inducible protein kinase PKR by HCV E2 protein. Science 285 107-10 PubMed GONUTS page

[PMID:12604806-24] Kien, F et al. (2003) Analysis of the subcellular localization of hepatitis C virus E2 glycoprotein in live cells using EGFP fusion proteins. J. Gen. Virol. 84 561-6 PubMed GONUTS page

[PMID:12356718-25] Scarselli, E et al. (2002) The human scavenger receptor class B type I is a novel candidate receptor for the hepatitis C virus. EMBO J. 21 5017-25 PubMed GONUTS page

[PMID:12595532-26] 26.0 ^26.1 ^26.2 ^26.3 ^26.4 Erdtmann, L et al. (2003) The hepatitis C virus NS2 protein is an inhibitor of CIDE-B-induced apoptosis. J. Biol. Chem. 278 18256-64 PubMed GONUTS page

[PMID:12692242-27] 27.0 ^27.1 ^27.2 ^27.3 Dimitrova, M et al. (2003) Protein-protein interactions between hepatitis C virus nonstructural proteins. J. Virol. 77 5401-14 PubMed GONUTS page

[PMID:7769685-28] 28.0 ^28.1 ^28.2 ^28.3 Satoh, S et al. (1995) The N-terminal region of hepatitis C virus nonstructural protein 3 (NS3) is essential for stable complex formation with NS4A. J. Virol. 69 4255-60 PubMed GONUTS page

[PMID:9514871-29] 29.0 ^29.1 ^29.2 ^29.3 Ishido, S et al. (1998) Complex formation of NS5B with NS3 and NS4A proteins of hepatitis C virus. Biochem. Biophys. Res. Commun. 244 35-40 PubMed GONUTS page

[PMID:8861917-30] 30.0 ^30.1 Kim, JL et al. (1996) Crystal structure of the hepatitis C virus NS3 protease domain complexed with a synthetic NS4A cofactor peptide. Cell 87 343-55 PubMed GONUTS page

[PMID:7769699-31] Lin, C et al. (1995) A central region in the hepatitis C virus NS4A protein allows formation of an active NS3-NS4A serine proteinase complex in vivo and in vitro. J. Virol. 69 4373-80 PubMed GONUTS page

[PMID:15303969-32] Khu, YL et al. (2004) Hepatitis C virus non-structural protein NS3 interacts with LMP7, a component of the immunoproteasome, and affects its proteasome activity. Biochem. J. 384 401-9 PubMed GONUTS page

[PMID:10570951-33] Drouet, C et al. (1999) Hepatitis C virus NS3 serine protease interacts with the serpin C1 inhibitor. FEBS Lett. 458 415-8 PubMed GONUTS page

[PMID:14524621-34] 34.0 ^34.1 Iwai, A et al. (2003) Hepatitis C virus nonstructural protein NS3 binds to Sm-D1, a small nuclear ribonucleoprotein associated with autoimmune disease. Microbiol. Immunol. 47 601-11 PubMed GONUTS page

[PMID:21559518-35] 35.0 ^35.1 ^35.2 ^35.3 ^35.4 ^35.5 Morohashi, K et al. (2011) Cyclosporin A associated helicase-like protein facilitates the association of hepatitis C virus RNA polymerase with its cellular cyclophilin B. PLoS ONE 6 e18285 PubMed GONUTS page

[PMID:16033967-36] 36.0 ^36.1 ^36.2 ^36.3 Hidajat, R et al. (2005) Hepatitis C virus NS3 protein interacts with ELKS-{delta} and ELKS-{alpha}, members of a novel protein family involved in intracellular transport and secretory pathways. J. Gen. Virol. 86 2197-208 PubMed GONUTS page

[PMID:11119590-37] Khu, YL et al. (2001) Mutations that affect dimer formation and helicase activity of the hepatitis C virus helicase. J. Virol. 75 205-14 PubMed GONUTS page

[PMID:26874015-38] Eyre, NS et al. (2016) Phosphorylation of NS5A Serine-235 is essential to hepatitis C virus RNA replication and normal replication compartment formation. Virology 491 27-44 PubMed GONUTS page

[PMID:17275127-39] 39.0 ^39.1 ^39.2 ^39.3 ^39.4 ^39.5 Lan, KH et al. (2007) HCV NS5A inhibits interferon-alpha signaling through suppression of STAT1 phosphorylation in hepatocyte-derived cell lines. J. Hepatol. 46 759-67 PubMed GONUTS page

[PMID:26152585-40] Romero-Brey, I et al. (2015) NS5A Domain 1 and Polyprotein Cleavage Kinetics Are Critical for Induction of Double-Membrane Vesicles Associated with Hepatitis C Virus Replication. MBio 6 e00759 PubMed GONUTS page

[PMID:11821416-41] 41.0 ^41.1 ^41.2 ^41.3 ^41.4 ^41.5 Park, KJ et al. (2002) Nonstructural 5A protein of hepatitis C virus modulates tumor necrosis factor alpha-stimulated nuclear factor kappa B activation. J. Biol. Chem. 277 13122-8 PubMed GONUTS page

[PMID:15607035-42] Ahn, J et al. (2004) Systematic identification of hepatocellular proteins interacting with NS5A of the hepatitis C virus. J. Biochem. Mol. Biol. 37 741-8 PubMed GONUTS page

[PMID:17686842-43] Sklan, EH et al. (2007) A Rab-GAP TBC domain protein binds hepatitis C virus NS5A and mediates viral replication. J. Virol. 81 11096-105 PubMed GONUTS page

[PMID:16530520-44] 44.0 ^44.1 Nanda, SK et al. (2006) The SH3 binding motif of HCV [corrected] NS5A protein interacts with Bin1 and is important for apoptosis and infectivity. Gastroenterology 130 794-809 PubMed GONUTS page

[PMID:22491470-45] 45.0 ^45.1 Nevo-Yassaf, I et al. (2012) Role for TBC1D20 and Rab1 in hepatitis C virus replication via interaction with lipid droplet-bound nonstructural protein 5A. J. Virol. 86 6491-502 PubMed GONUTS page

[PMID:17567694-46] 46.0 ^46.1 ^46.2 ^46.3 ^46.4 Abe, T et al. (2007) Hepatitis C virus nonstructural protein 5A modulates the toll-like receptor-MyD88-dependent signaling pathway in macrophage cell lines. J. Virol. 81 8953-66 PubMed GONUTS page

[PMID:10702287-47] 47.0 ^47.1 ^47.2 Ghosh, AK et al. (2000) Hepatitis C virus NS5A protein modulates transcription through a novel cellular transcription factor SRCAP. J. Biol. Chem. 275 7184-8 PubMed GONUTS page

[PMID:11922617-48] 48.0 ^48.1 ^48.2 ^48.3 Kyono, K et al. (2002) Human eukaryotic initiation factor 4AII associates with hepatitis C virus NS5B protein in vitro. Biochem. Biophys. Res. Commun. 292 659-66 PubMed GONUTS page

[PMID:24263861-49] 49.0 ^49.1 Sakata, K et al. (2013) HCV NS3 protease enhances liver fibrosis via binding to and activating TGF-β type I receptor. Sci Rep 3 3243 PubMed GONUTS page

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HCVH:POLG

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