HCVCO:POLG

Species (Taxon ID)	Hepatitis C virus genotype 1b (isolate Con1) (HCV). (333284)
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 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	Q9WMX2
EMBL	AJ238799
PIR	A61196 PQ0246 PS0329
PDB	1ZH1 2JY0 2KWT 2KWZ 3FQL 3FQM 3FQQ 3KN2 3KQH 3KQK 3KQL 3KQN 3KQU 3Q0Z 3QGD 3QGE 3QGF 3QGG 4NLD 4U01 5E4F 5PZK 5PZL 5PZM 5PZN 5PZO 5PZP 5TRH 5TRI 5TRJ 5TRK 5TWN
PDBsum	1ZH1 2JY0 2KWT 2KWZ 3FQL 3FQM 3FQQ 3KN2 3KQH 3KQK 3KQL 3KQN 3KQU 3Q0Z 3QGD 3QGE 3QGF 3QGG 4NLD 4U01 5E4F 5PZK 5PZL 5PZM 5PZN 5PZO 5PZP 5TRH 5TRI 5TRJ 5TRK 5TWN
DisProt	DP00615
ProteinModelPortal	Q9WMX2
SMR	Q9WMX2
IntAct	Q9WMX2
MINT	Q9WMX2
BindingDB	Q9WMX2
ChEMBL	CHEMBL5536
DrugBank	DB07238
iPTMnet	Q9WMX2
PRIDE	Q9WMX2
euHCVdb	AJ238799
OrthoDB	VOG090000UE
EvolutionaryTrace	Q9WMX2
Proteomes	UP000007414
GO	GO:0005576 GO:0030430 GO:0044165 GO:0044167 GO:0044186 GO:0044191 GO:0033650 GO:0042025 GO:0044220 GO:0020002 GO:0016021 GO:0044385 GO:0032991 GO:0019031 GO:0019013 GO:0055036 GO:0003779 GO:0005524 GO:0008026 GO:0004197 GO:0005216 GO:0042803 GO:0003723 GO:0003968 GO:0004252 GO:0017124 GO:0005198 GO:0008270 GO:0075520 GO:0075512 GO:0039654 GO:0039520 GO:0075519 GO:0039645 GO:0039707 GO:1990219 GO:0039690 GO:0051259 GO:0006355 GO:0039545 GO:0039563 GO:0039547 GO:0039502 GO:0006351 GO:0019087 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
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
part_of	GO:0032991	protein-containing complex	PMID:15902263^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:19244328^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:19244328^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:19244328^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0039694	viral RNA genome replication	PMID:15339921^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:15339921^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0039690	positive stranded viral RNA replication	PMID:18032500^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:15902263^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:15902263^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:1990219	positive regulation by symbiont of host protein levels	PMID:21914078^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P08670)\|has_regulation_target:(UniProtKB:P21333)	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
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
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: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
part_of	GO:0030430	host cell cytoplasm	PMID:21914078^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0044220	host cell perinuclear region of cytoplasm	PMID:21914078^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0044165	host cell endoplasmic reticulum	PMID:25262680^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0033650	host cell mitochondrion	PMID:25262680^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0030430	host cell cytoplasm	PMID:21914078^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0044220	host cell perinuclear region of cytoplasm	PMID:21914078^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0030430	host cell cytoplasm	PMID:18562541^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0044220	host cell perinuclear region of cytoplasm	PMID:18562541^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0044165	host cell endoplasmic reticulum	PMID:25262680^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0033650	host cell mitochondrion	PMID:25262680^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0030430	host cell cytoplasm	PMID:21914078^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0044220	host cell perinuclear region of cytoplasm	PMID:21914078^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0075519	microtubule-dependent intracellular transport of viral material	PMID:18562541^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0075520	actin-dependent intracellular transport of virus	PMID:18562541^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003779	actin binding	PMID:18562541^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P60709	F		Seeded From UniProt	complete
part_of	GO:0044220	host cell perinuclear region of cytoplasm	PMID:18562541^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0030430	host cell cytoplasm	PMID:18562541^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003968	RNA-directed 5'-3' RNA polymerase activity	PMID:25262680^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0044165	host cell endoplasmic reticulum	PMID:25262680^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0033650	host cell mitochondrion	PMID:25262680^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0044220	host cell perinuclear region of cytoplasm	PMID:25262680^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:15989969^[8]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0044167	host cell endoplasmic reticulum membrane	PMID:15989969^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		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
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
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
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
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
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: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
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: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
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
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
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
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
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
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: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
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
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: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
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
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
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: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
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: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
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
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: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
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: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: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
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
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
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
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: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
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: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: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
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
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: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: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
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
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
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: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
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
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
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
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Notes

References

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

↑ ^1.0 ^1.1 ^1.2 Tellinghuisen, TL et al. (2005) Structure of the zinc-binding domain of an essential component of the hepatitis C virus replicase. Nature 435 374-9 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 Love, RA et al. (2009) Crystal structure of a novel dimeric form of NS5A domain I protein from hepatitis C virus. J. Virol. 83 4395-403 PubMed GONUTS page
↑ ^3.0 ^3.1 Tellinghuisen, TL et al. (2004) The NS5A protein of hepatitis C virus is a zinc metalloprotein. J. Biol. Chem. 279 48576-87 PubMed GONUTS page
↑ Tellinghuisen, TL et al. (2008) Identification of residues required for RNA replication in domains II and III of the hepatitis C virus NS5A protein. J. Virol. 82 1073-83 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 ^5.6 Ghosh, S et al. (2011) Association of filamin A and vimentin with hepatitis C virus proteins in infected human hepatocytes. J. Viral Hepat. 18 e568-77 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 ^6.3 ^6.4 ^6.5 ^6.6 ^6.7 Kim, JH et al. (2014) Interaction of stomatin with hepatitis C virus RNA polymerase stabilizes the viral RNA replicase complexes on detergent-resistant membranes. J. Microbiol. Biotechnol. 24 1744-54 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 ^7.4 ^7.5 ^7.6 Lai, CK et al. (2008) Association of hepatitis C virus replication complexes with microtubules and actin filaments is dependent on the interaction of NS3 and NS5A. J. Virol. 82 8838-48 PubMed GONUTS page
↑ ^8.0 ^8.1 Watashi, K et al. (2005) Cyclophilin B is a functional regulator of hepatitis C virus RNA polymerase. Mol. Cell 19 111-22 PubMed GONUTS page

[PMID:15902263-1] 1.0 ^1.1 ^1.2 Tellinghuisen, TL et al. (2005) Structure of the zinc-binding domain of an essential component of the hepatitis C virus replicase. Nature 435 374-9 PubMed GONUTS page

[PMID:19244328-2] 2.0 ^2.1 ^2.2 Love, RA et al. (2009) Crystal structure of a novel dimeric form of NS5A domain I protein from hepatitis C virus. J. Virol. 83 4395-403 PubMed GONUTS page

[PMID:15339921-3] 3.0 ^3.1 Tellinghuisen, TL et al. (2004) The NS5A protein of hepatitis C virus is a zinc metalloprotein. J. Biol. Chem. 279 48576-87 PubMed GONUTS page

[PMID:18032500-4] Tellinghuisen, TL et al. (2008) Identification of residues required for RNA replication in domains II and III of the hepatitis C virus NS5A protein. J. Virol. 82 1073-83 PubMed GONUTS page

[PMID:21914078-5] 5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 ^5.6 Ghosh, S et al. (2011) Association of filamin A and vimentin with hepatitis C virus proteins in infected human hepatocytes. J. Viral Hepat. 18 e568-77 PubMed GONUTS page

[PMID:25262680-6] 6.0 ^6.1 ^6.2 ^6.3 ^6.4 ^6.5 ^6.6 ^6.7 Kim, JH et al. (2014) Interaction of stomatin with hepatitis C virus RNA polymerase stabilizes the viral RNA replicase complexes on detergent-resistant membranes. J. Microbiol. Biotechnol. 24 1744-54 PubMed GONUTS page

[PMID:18562541-7] 7.0 ^7.1 ^7.2 ^7.3 ^7.4 ^7.5 ^7.6 Lai, CK et al. (2008) Association of hepatitis C virus replication complexes with microtubules and actin filaments is dependent on the interaction of NS3 and NS5A. J. Virol. 82 8838-48 PubMed GONUTS page

[PMID:15989969-8] 8.0 ^8.1 Watashi, K et al. (2005) Cyclophilin B is a functional regulator of hepatitis C virus RNA polymerase. Mol. Cell 19 111-22 PubMed GONUTS page

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HCVCO:POLG

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