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							<x>952.866060</x>
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						<gene id="873CD178-2084-4606-82CA-054112B5382E">
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							<x>1052.404299</x>
							<y>869.398621</y>
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Is a short-lived protein, degradated
via ubiquitin-proteasome pathway
[Nakagava K-2000].
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							<x>547.720703</x>
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								<sn>NS4B</sn><nm>Nonstructural protein NS4B </nm><sy>P27</sy><os id="DEDC969D-8050-4930-8D53-D1BF209326BF"><Latin>Hepatitis C virus</Latin><English>human hepatitis C virus</English></os><dbref><name>SWISS-PROT</name><ac>P26660</ac><id>POLG_HCVJ6;</id></dbref><fn>active</fn><mm>monomer</mm><ref id="C0D12E2B-EAA0-4127-AD09-C95868CE2493"><authors>Elazar M., Cheong K.H., Liu P., Greenberg H.B., Rice C.M., Glenn J.S.</authors><journal id="journal211"><nm>J.Virology</nm></journal><title>Amphipathic helix-dependent localization of NS5A mediates hepatitis C virus RNA replication.</title><year>2003</year><pages><first>6055</first><last>6061</last></pages></ref><ref id="827B846A-3CB9-4215-B68E-569D86B8FAA0"><authors>Hugle T., Fehrmann F., Bieck E., Kohara M., Krausslich H.G., Rice C.M., Blum H.E., Moradpour D.</authors><journal id="journal317"><nm>Virology</nm></journal><title>The hepatitis C virus nonstructural protein 4B is an integral endoplasmic reticulum membrane protein.</title><year>2001</year><pages><first>70</first><last>81</last></pages></ref></object>
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									<ref id="143B2006-9DA0-4801-8A96-732B947C1114">
										<title>Characterization of cell lines carrying self-replicating hepatitis C virus RNAs.</title>
										<authors>Pietschmann T., Lohmann V., Rutter G., Kurpanek K., Bartenschlager R.</authors>
										<journal id="journal211">
											<nm>J.Virology</nm>
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										<pages>
											<first>1252</first>
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										<dt>18.10.2004;Khlebodarova T.M.;created</dt>
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					<object id="proteinID18987"><sn>c-fos</sn><nm>c-fos</nm><os id="organismID953"><Latin>Homo sapiens</Latin><English>human</English></os><gn id="geneID10777"><sn>c-fos</sn><nm>c-fos protooncogene</nm><os id="organismID953"><Latin>Homo sapiens</Latin><English>human</English></os></gn><fn>inactive</fn><md>no data</md><mm>monomer</mm><cell id="cellID2494"><sn>JEG-3</sn><de>choriocarcinoma cells</de><os id="organismID953"><Latin>Homo sapiens</Latin><English>human</English></os></cell><ref id="literID921"><authors>Albanese C, Johnson J, Watanabe G., Eklund N., Vu D., Arnold A., Pestell R.G.</authors><journal id="journal167"><nm>J.Biol.Chem.</nm></journal><title>Transforming p21ras mutants and c-Ets-2 activate the cyclin D1 promoter through distinguishable regions.</title><year>1995</year><pages><first>23589</first><last>23597</last></pages></ref><ref id="literID21086"><authors>Grosch S., Kaina B.</authors><journal id="journal32"><nm>Biochem.Biophys.Res.Commun.</nm></journal><title>Transcriptional activation of apurinic/apyrimidinic endonuclease (Ape, Ref-1) by oxidative stress requires CREB</title><year>1999</year><pages><first>859</first><last>863</last></pages></ref><total_comment_item><cc>
C-Fos represses the cyclin D1 promoter in Cos and JEG-3 cells [Albanese C. et al., 1995]
</cc></total_comment_item><dt>13.5.2000.;Stepanenko I.L.;created</dt><dt>27.01.2002;Turn;updated</dt></object>
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				<protein id="FB5B92B6-66C1-4AA9-ACF7-D80806EBE344">
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					<x>620.052259</x>
					<y>1300.300112</y>
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				<protein id="C4AEC6D4-1E01-4DC7-8648-4541C019801F">
					<object id="proteinID17091"><sn>Akt</sn><nm>protein kinase B</nm><sy>RAC-alpha serine/threonine-protein kinase </sy><sy>RAC</sy><sy>EC 2.7.1.37 </sy><sy>RAC-PK-alpha</sy><sy>C-AKT</sy><sy>PKB</sy><sy>AKT1</sy><os id="organismID953"><Latin>Homo sapiens</Latin><English>human</English></os><dbref><name>SWISS-PROT</name><ac>P31749</ac><id>KRAC_HUMAN</id></dbref><fn>active</fn><md>phosphorylated</md><mm>monomer</mm><inducer id="repressor126"/><cell id="cellID1575"><sn>293</sn><de>293 kidney epithelial cells</de><os id="organismID953"><Latin>Homo sapiens</Latin><English>human</English></os></cell><cell id="cellID2236"><sn>HeLa</sn><de>human tumor cell line, epithelial fibroblasts, cervical carcinoma cell line</de><os id="organismID953"><Latin>Homo sapiens</Latin><English>human</English></os></cell><cell id="cellID2734"><sn>MCF-7</sn><de>MCF-7 breast cancer cells</de><os id="organismID953"><Latin>Homo sapiens</Latin><English>human</English></os></cell><cell id="cellID2522"><sn>Jurkat</sn><de>CD4+ T lymphoblastoid cell line</de><os id="organismID953"><Latin>Homo sapiens</Latin><English>human</English></os></cell><ref id="literID33357"><authors>Kim A.H., Khursigara G., Sun X., Franke T.F., ChaoM.V.</authors><journal id="journal234"><nm>Mol.Cell.Biol.</nm></journal><title>Akt Phosphorylates and Negatively Regulates Apoptosis Signal-Regulating Kinase 1.</title><year>2001</year><pages><first>893</first><last>901</last></pages></ref><total_comment_item><cc>
serine/threonine kinases
</cc></total_comment_item><dt>28-Feb-02.;Alena N.;created</dt><dt>05-Dec-02.;Alena N.;updated</dt><dt>07.10.2004;Khlebodarova T.M.;edited</dt><dt>02.02.2005;Stepanenko I.L.;edited</dt></object>
					<x>2053.406739</x>
					<y>672.331392</y>
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				<protein id="F8908E38-EA5A-49D8-A05C-6C145B2B88A4">
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Activation of the kinase requires hierarchical phosphorylation at multiple sites, culminating in
the phosphorylation of the threonine in position 229 (Thr229), in the catalytic domain by PDK1.
The phosphorylation of Thr229 appears to depend on phosphorylation of Thr389, and
this reaction is facilitated by converting four (Ser/Thr)-Pro phosphorylation sites in the
autoinhibitory domain to acidic residues.
</cc></total_comment_item><dt>06.11.2002;Alena N.;created</dt><dt>07.10.2004;Khlebodarova T.M.;edited</dt></object>
					<x>1992.273937</x>
					<y>704.225922</y>
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					<object id="proteinID31070"><sn>IFN-gamma</sn><nm>interferon-gamma</nm><sy>IMMUNE INTERFERON</sy><os id="organismID953"><Latin>Homo sapiens</Latin><English>human</English></os><dbref><name>SWISS-PROT</name><ac>P01579</ac><id>ING_HUMAN</id></dbref><gn id="geneID16310"><sn>IFN-gamma</sn><nm>interferon-gamma</nm><os id="organismID953"><Latin>Homo sapiens</Latin><English>human</English></os></gn><fn>active</fn><md>no data</md><mm>multimer</mm><inducer id="repressor30"><name>corticosteroids</name></inducer><inducer id="repressor138"><name>prostaglandins</name></inducer><inducer id="repressor134"><name>PMA/ionomycin</name></inducer><cell id="cellID1771"><sn>B-cell</sn><de>B-lymphocytes</de><os id="organismID953"><Latin>Homo sapiens</Latin><English>human</English></os></cell><cell id="cellID2522"><sn>Jurkat</sn><de>CD4+ T lymphoblastoid cell line</de><os id="organismID953"><Latin>Homo sapiens</Latin><English>human</English></os></cell><cell id="cellID3111"><sn>T-cell</sn><de>T-lymphocytes</de><os id="organismID953"><Latin>Homo sapiens</Latin><English>human</English></os></cell><ref id="literID612"><authors>Ajjan R.A., Kamaruddin N.A., Crisp M., Watson P.F., Ludgate M., Weetman A.P..</authors><journal id="journal75"><nm>Clin.Endocrinol.(Oxf.)</nm></journal><title>Regulation and tissue distribution of the human sodium iodide symporter gene.</title><year>1998</year><pages><first>517</first><last>523</last></pages></ref><ref id="literID32100"><authors>Kasai K., Banba N., Motohashi S., Hattori Y., Manaka K., Shimoda S.I..</authors><journal id="journal124"><nm>FEBS Lett.</nm></journal><title>Expression of monocyte chemoattractant protein-1 mRNA and protein in cultured human thyrocytes.</title><year>1996</year><pages><first>137</first><last>140</last></pages></ref><total_comment_item><cc>
cytokine
Length: 166 AA [unprocessed precursor]
Molecular weight: 19348 Da [-//-]
Tetramer with molecular weight
of monomer-17 kDa.
IFN-gamma by itself is a weak stimulant of MCP-1 in thyrocytes, but has a synergistic stimulatory activity with either IL-1 or TNF-alpha (Kasai K. et al., 1996).
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The expression of RB gene is increased graduallly during the G1 transition and peaks at the G1/S boundary, reduce in S and low in G2.
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							<ref id="143B2006-9DA0-4801-8A96-732B947C1114">
								<title>Characterization of cell lines carrying self-replicating hepatitis C virus RNAs.</title>
								<authors>Pietschmann T., Lohmann V., Rutter G., Kurpanek K., Bartenschlager R.</authors>
								<journal id="journal211">
									<nm>J.Virology</nm>
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								<year>2001</year>
								<pages>
									<first>1252</first>
									<last>1264</last>
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								<dt>18.10.2004;Khlebodarova T.M.;created</dt>
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							<value>16 h</value>
						</half-life>
						<local_comment_item>
							<CC>half-life of basal phosphorylated form of NS5A was 16 h, and hilf-life of hyperphophorylated form of NS5A was 7 h.</CC>
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					<object id="proteinID30327"><sn>HSP90</sn><nm>90-kDa heat shock protein</nm><os id="organismID953"><Latin>Homo sapiens</Latin><English>human</English></os><dbref><name>SWISS-PROT</name><ac>P08238</ac><id>HS9B_HUMAN</id></dbref><gn id="geneID15887"><sn>HSP90beta</sn><nm>90-kDa heat shock protein</nm><os id="organismID953"><Latin>Homo sapiens</Latin><English>human</English></os></gn><fn>active</fn><md>phosphorylated</md><mm>monomer</mm><ref id="3191E6E4-6E7D-4376-A002-9EEF4DF459E3"><authors>Waxman L., Whitney M., Pollok B.A., Kuo L.C., Darke P.L.</authors><journal id="journal287"><nm>Proc.Natl.Acad.Sci.USA</nm></journal><title>Host cell factor requirement for hepatitis C virus enzyme maturation.</title><year>2001</year><pages><first>13931</first><last>13935</last></pages></ref><dt>08.6.2000.;Stepanenko I.L.;created</dt><dt>26.10.2004;Khlebodarova T.M.;edited</dt></object>
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The cyclin-dependent kinase inhibitor p21waf1/Cip1 is a downstream effector of the p53-dependent cell growth arrest.
</cc></total_comment_item><dt>25.05.2001;Grigoriev S.A.;updated</dt><dt>29.06.2002;Turn;updated</dt><dt>26.12.2000;Grigoriev S.A.;created</dt><dt>06.10.2004;Khlebodarova T.M.;edited</dt><dt>26.10.2004;Khlebodarova T.M.;edited</dt></object>
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					<object id="B3CDE92F-E6FE-41A2-B4AD-ED92409ED0FE">
						<local_comment_item>
							<CC>accumulation of lipid droplets</CC>
						</local_comment_item>
						<sn>lipid accumulation</sn><nm>lipid accumulation</nm><dt>28.10.2004;Khlebodarova T.M.;created</dt><dt>28.10.2004;Khlebodarova T.M.;edited</dt></object>
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				<protein id="3702D14C-CBE2-42BF-B9C2-3E1CB3BC0D7E">
					<object id="proteinID16333"><sn>APOA2</sn><nm>apolipoprotein AII</nm><sy>APOAII</sy><os id="organismID953"><Latin>Homo sapiens</Latin><English>human</English></os><dbref><name>SWISS-PROT</name><ac>P02652</ac><id>APA2_HUMAN</id></dbref><gn id="geneID9782"><sn>apolipoprotein AII</sn><nm>APOA2</nm><os id="organismID953"><Latin>Homo sapiens</Latin><English>human</English></os></gn><fn>active</fn><md>no data</md><mm>homodimer</mm><cell id="cellID4415"><sn>intestine</sn><de>intestine</de><os id="organismID953"><Latin>Homo sapiens</Latin><English>human</English></os></cell><cell id="cellID4555"><sn>liver</sn><de>liver</de><os id="organismID953"><Latin>Homo sapiens</Latin><English>human</English></os></cell><ref id="literID5674"><authors>Breslow J.L.</authors><journal id="journal271"><nm>Physiol.Rev.</nm></journal><title>Apolipoprotein genetic variation and human disease.</title><year>1988</year><pages><first>85</first><last>132</last></pages></ref><total_comment_item><cc>
In vitro apo A-II has been shown to
displace apo A-I from HDL particles
as well as to both activate hepatic lipase and inhibit LCAT [Breslow J.L., 1988]
</cc></total_comment_item><dt>30-Nov-02.;Proscura A.L.;created</dt><dt>07-Dec-02.;Proscura A.L.;updated</dt><dt>28.10.2004;Khlebodarova T.M.;edited</dt></object>
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					<x>2294.657227</x>
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				<reaction id="1C30B4FF-F2B9-401D-932C-FF7C6BC9BDE2">
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					<y>816.544556</y>
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				<reaction id="A3A87068-79A3-4949-A099-50C384F1091D">
					<object id="reaction68D6783D-BB0C-42FA-AEDD-71029F624942">
						<type>no data</type>
						<nm>reaction</nm><ef>direct</ef><evidence>experimental</evidence><input><input_item><protein id="EDCB8239-1E76-4F85-996F-6816B089E88E"><name>core protein</name><os id="DEDC969D-8050-4930-8D53-D1BF209326BF"><Latin>Hepatitis C virus</Latin><English>human hepatitis C virus</English></os></protein></input_item></input><output><output_item><protein id="EDCB8239-1E76-4F85-996F-6816B089E88E"><name>core protein</name><os id="DEDC969D-8050-4930-8D53-D1BF209326BF"><Latin>Hepatitis C virus</Latin><English>human hepatitis C virus</English></os></protein></output_item></output><ref id="51808A5B-7B69-498F-8E7D-D48F9C18C0E1"><authors>Suzuki R., Matsuura Y., Suzuki T, Ando A., Chiba J., Harada S., Saito I., Miyamura T.</authors><journal id="journal181"><nm>J.Gen.Virol.</nm></journal><title>Nuclear localization of the truncated hepatitis C virus core protein with its hydrophobic C terminus deleted.</title><year>1995</year><pages><first>53</first><last>61</last></pages></ref><ref id="A4365C9A-841-4600-9E7F-0966574CCC8E"><authors>Chang S.C., Yen J.H., Kang H.Y., Jang M.H., Chang M.F.</authors><journal id="journal32"><nm>Biochem.Biophys.Res.Commun.</nm></journal><title>Nuclear localization signals in the core protein of hepatitis C virus.</title><year>1994</year><pages><first>1284</first><last>1290</last></pages></ref><dt>20.10.2004;Khlebodarova T.M.;edited</dt></object>
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				<protein id="D34C273D-CC9B-4B4F-9D80-196B4860C8B8">
					<object id="5489ACDA-413D-4802-9CED-21674DF94FC8"><sn>E2</sn><nm>Envelope glycoprotein E2 </nm><sy>NS1</sy><sy>GP68</sy><sy>GP70</sy><os id="DEDC969D-8050-4930-8D53-D1BF209326BF"><Latin>Hepatitis C virus</Latin><English>human hepatitis C virus</English></os><fn>active</fn><mm>monomer</mm><ref id="342BADB9-D3CB-4C66-9154-24D65BCBE006"><authors>Lin C., Lindenbach B.D., Pragai B.M., McCourt D.W., Rice C.M.</authors><journal id="journal211"><nm>J.Virology</nm></journal><title>Processing in the hepatitis C virus E2-NS2 region: identification of p7 and two distinct E2-specific products with different C termini.</title><year>1994</year><pages><first>5063</first><last>5073</last></pages></ref><ref id="5D545524-5E98-4E06-9C1B-249EC5051EBF"><authors>Penin F., Combet C., Germanidis G., Frainais P.O., Deleage G., Pawlotsky J.M.</authors><journal id="journal211"><nm>J.Virology</nm></journal><title>Conservation of the conformation and positive charges of hepatitis C virus E2 envelope glycoprotein hypervariable region 1 points to a role in cell attachment.</title><year>2001</year><pages><first>5703</first><last>5710</last></pages></ref><ref id="AD0737A7-D706-49AF-8483-9CF451537CE6"><authors>Deleersnyder V., Pillez A., Wychowski C., Blight K., Xu J., Hahn Y.S., Rice C.M., Dubuisson J.</authors><journal id="journal211"><nm>J.Virology</nm></journal><title>Formation of native hepatitis C virus glycoprotein complexes.</title><year>1997</year><pages><first>697</first><last>704</last></pages></ref><ref id="753A1558-4591-4793-B5C4-8D6EC4855693"><authors>Keck Z.Y., Op De Beeck A., Hadlock K.G., Xia J., Li T.K., Dubuisson J., Foung S.K.</authors><journal id="journal211"><nm>J.Virology</nm></journal><title>Hepatitis C virus E2 has three immunogenic domains containing conformational epitopes with distinct properties and biological functions.</title><year>2004</year><pages><first>9224</first><last>9232</last></pages></ref><dt>14.10.2004;Khlebodarova T.M.;edited</dt><dt>22.10.2004;Khlebodarova T.M.;edited</dt><dt>09.11.2004;Khlebodarova T.M.;edited</dt><dt>05.10.2004;Khlebodarova T.M.;edited</dt></object>
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