DRAVPR_ID	Sequence	Sequence_Length	Name	Source	Uniprot_ID	Gene	PDB_ID	Target_Organism	Activity	Predicted_structure_ID	Comment	Modification	Pubmed_ID	Author	Title
DRAVPR0001	MDKQNSQMNASHPETNLPVGYPPQYPPTAFQGPPGYSGYPGPQVSYPPPPAGHSGPGPAGFPVPNQPVYNQPVYNQPVGAAGVPWMPAPQPPLNCPPGLEYLSQIDQILIHQQIELLEVLTGFETNNKYEIKNSFGQRVYFAAEDTDCCTRNCCGPSRPFTLRIIDNMGQEVITLERPLRCSSCCCPCCLQEIEIQAPPGVPIGYVIQTWHPCLPKFTIQNEKREDVLKISGPCVVCSCCGDVDFEIKSLDEQCVVGKISKHWTGILREAFTDADNFGIQFPLDLDVKMKAVMIGACFLIDFMFFESTGSQEQKSGVW	318	"Phospholipid scramblase 1(PL scramblase 1,PLSCR1)"	Homo sapiens (Human)	O15162	PLSCR1	1Y2A	"HBV,HIV-1,HTLV1,IAV,EBV,HCMV,HCV,VSV"	"[Ref.35650588]Hepatitis B virus(HBV):PLSCR1 plays an antiviral role by promoting the ubiquitination and proteasomal degradation of the HBV X protein (HBx), resulting in reduced HBx levels.##Human immunodeficiency virus type-1(HIV-1):PLSCR1 exhibits antiviral activity by inhibiting Tat functions by reducing its nuclear localization and perturbing the virus entry process by modulating CD4-SLPI interaction.##Human T-lymphotropic virus type 1 (HTLV-1):PLSCR1-Tax interaction reduced the cytoplasmic redistribution of Tax and its homodimerization, thus inhibiting Tax-mediated transactivation of HTLV-1 long terminal repeat.##Influenza A virus (IAV):PLSCR1 inhibits the nuclear import of NP/vRNP thus limiting viral replication.##Epstein-Barr virus (EBV): PLSCR1 represses BZLF1-dependent lytic gene expression.##Human cytomegalovirus (HCMV):PLSCR1 inhibits CREB functions and CREB-IE2, CBP-IE2 complexes, resulting in the repression of HCMV replication.##[Ref.15308695]Vesicular stomatitis virus (VSV):PLSCR1 inhibits accumulation of primary VSV transcripts, similar to the effects of IFN against VSV.##[Ref.21806988]Hepatitis C virus (HCV):PLSCR1 contributes to HCV entry and infection through HCVpp and HCVcc assays."	AF-O15162-F1	PLSCR1 may play a role in the antiviral response of interferon (IFN) by amplifying and enhancing the IFN response through increased expression of select subset of potent antiviral genes.	"¢ÙPhosphorylation of Tyr at position 69,74,161¢ÚThe Cys at position 184,185,186,188 and 189 indicates S-palmitoyl cysteine."	15308695##21806988##35650588	"Dong B, Zhou Q, Zhao J, Zhou A, Harty RN, Bose S, Banerjee A, Slee R, Guenther J, Williams BR, Wiedmer T, Sims PJ, Silverman RH.?##Gong Q, Cheng M, Chen H, Liu X, Si Y, Yang Y, Yuan Y, Jin C, Yang W, He F, Wang J.##Dal Col J, Lamberti MJ, Nigro A, Casolaro V, Fratta E, Steffan A, Montico B. "	Phospholipid scramblase 1 potentiates the antiviral activity of interferon.?##Phospholipid scramblase 1 mediates hepatitis C virus entry into host cells.##Phospholipid scramblase 1: a protein with multiple functions via multiple molecular interactors.
DRAVPR0002	MSCHNCSDPQVLCSSGQLFLQPLWDHLRSWEALLQSPFFPVIFSITTYVGFCLPFVVLDILCSWVPALRRYKIHPDFSPSAQQLLPCLGQTLYQHVMFVFPVTLLHWARSPALLPHEAPELLLLLHHILFCLLLFDMEFFVWHLLHHKVPWLYRTFHKVHHQNSSSFALATQYMSVWELFSLGFFDMMNVTLLGCHPLTTLTFHVVNIWLSVEDHSGYNFPWSTHRLVPFGWYGGVVHHDLHHSHFNCNFAPYFTHWDKILGTLRTASVPAR	272	Cholesterol 25-hydroxylase(h25OH)	Homo sapiens (Human)	O95992	CH25H 	None	"SARS-CoV-2,VSV"	"[Ref.33239446]SARS-CoV-2:The product of Cholesterol 25-hydroxylase, 25-hydroxycholesterol, activates the ER-localized enzyme ACAT to induce internalization of accessible cholesterol on the plasma membrane and restricts SARS-CoV-2 S protein-mediated fusion which inhibits virus replication.(inhibition of VSV-SARS-CoV-2 infection in MA104 cells(EC50=1.49 ?M))."	AF-O95992-F1	"25HC has been shown to have broad antiviral activity by inhibiting the host cell entry of human immunodeficiency virus (HIV), vesicular stomatitis virus (VSV), Zika virus (ZIKV), Ebola virus (EBOV), Nipah virus (NiV), Russian spring-summer encephalitis virus (RSSEV), porcine viruses (PEDV, PEGV, porcine intestine coronavirus), reovirus, and norovirus. For ZIKV, treatment with 25HC protected mice and rhesus monkeys from ZIKV infection."	"Glycosylation of Asn at position 5,163,189."	33239446##32944968	"Zang R, Case JB, Yutuc E, Ma X, Shen S, Gomez Castro MF, Liu Z, Zeng Q, Zhao H, Son J, Rothlauf PW, Kreutzberger AJB, Hou G, Zhang H, Bose S, Wang X, Vahey MD, Mani K, Griffiths WJ, Kirchhausen T, Fremont DH, Guo H, Diwan A, Wang Y, Diamond MS, Whelan SPJ, Ding S. ##Wang S, Li W, Hui H, Tiwari SK, Zhang Q, Croker BA, Rawlings S, Smith D, Carlin AF, Rana TM. "	Cholesterol 25-hydroxylase suppresses SARS-CoV-2 replication by blocking membrane fusion.?##Cholesterol 25-Hydroxylase inhibits SARS-CoV-2 and other coronaviruses by depleting membrane cholesterol.
DRAVPR0003	MMDLRNTPAKSLDKFIEDYLLPDTCFRMQINHAIDIICGFLKERCFRGSSYPVCVSKVVKGGSSGKGTTLRGRSDADLVVFLSPLTTFQDQLNRRGEFIQEIRRQLEACQRERAFSVKFEVQAPRWGNPRALSFVLSSLQLGEGVEFDVLPAFDALGQLTGGYKPNPQIYVKLIEECTDLQKEGEFSTCFTELQRDFLKQRPTKLKSLIRLVKHWYQNCKKKLGKLPPQYALELLTVYAWERGSMKTHFNTAQGFRTVLELVINYQQLCIYWTKYYDFKNPIIEKYLRRQLTKPRPVILDPADPTGNLGGGDPKGWRQLAQEAEAWLNYPCFKNWDGSPVSSWILLAESNSADDETDDPRRYQKYGYIGTHEYPHFSHRPSTLQAASTPQAEEDWTCTIL	400	2'-5'-oligoadenylate synthase 1(OAS1)	Homo sapiens (Human)	P00973	OAS1	4IG8	SARS-CoV-2	"[Ref.34581622]SARS-CoV-2:OAS1 recognizes short stretches of double-stranded RNA (dsRNA) and activates RNase L, which leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication."	AF-P00973-F1	"When prenylated at C-terminal, acts as a double-stranded RNA (dsRNA) sensor specifically targeted to membranous replicative organelles in SARS coronavirus-2/SARS-CoV-2 infected cells where it binds to dsRNA structures in the SARS-CoV-2 5'-UTR and initiates a potent block to SARS-CoV-2 replication.?"	The Cys at position 397 indicates S-geranylgeranyl cysteine.	34581622	"Wickenhagen A, Sugrue E, Lytras S, Kuchi S, Noerenberg M, Turnbull ML, Loney C, Herder V, Allan J, Jarmson I, Cameron-Ruiz N, Varjak M, Pinto RM, Lee JY, Iselin L, Palmalux N, Stewart DG, Swingler S, Greenwood EJD, Crozier TWM, Gu Q, Davies EL, Clohisey S, Wang B, Trindade Maranh?o Costa F, Freire Santana M, de Lima Ferreira LC, Murphy L, Fawkes A, Meynert A, Grimes G; ISARIC4C Investigators, Da Silva Filho JL, Marti M, Hughes J, Stanton RJ, Wang ECY, Ho A, Davis I, Jarrett RF, Castello A, Robertson DL, Semple MG, Openshaw PJM, Palmarini M, Lehner PJ, Baillie JK, Rihn SJ, Wilson SJ."	A prenylated dsRNA sensor protects against severe COVID-19.?
DRAVPR0004	MEHGLRSIPAWTLDKFIEDYLLPDTTFGADVKSAVNVVCDFLKERCFQGAAHPVRVSKVVKGGSSGKGTTLKGKSDADLVVFLNNLTSFEDQLNRRGEFIKEIKKQLYEVQHERRFRVKFEVQSSWWPNARSLSFKLSAPHLHQEVEFDVLPAFDVLGHVNTSSKPDPRIYAILIEECTSLGKDGEFSTCFTELQRNFLKQRPTKLKSLIRLVKHWYQLCKEKLGKPLPPQYALELLTVFAWEQGNGCYEFNTAQGFRTVLELVINYQHLRIYWTKYYDFQHQEVSKYLHRQLRKARPVILDPADPTGNVAGGNPEGWRRLAEEADVWLWYPCFIKKDGSRVSSWDVPTVVPVPFEQVEENWTCILL	367	2'-5'-oligoadenylate synthase 1A	Mus musculus (Mouse)	P11928	Oas1a	None	SARS-CoV-2	"[Ref.34581622]SARS-CoV-2:OAS1 recognizes short stretches of double-stranded RNA (dsRNA) and activates RNase L, which leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication."	AF-P11928-F1	"Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNase L-dependent pathway or an alternative antiviral pathway independent of RNase L."	The Cys at position 364 indicates S-geranylgeranyl cysteine.	34581622	"Wickenhagen A, Sugrue E, Lytras S, Kuchi S, Noerenberg M, Turnbull ML, Loney C, Herder V, Allan J, Jarmson I, Cameron-Ruiz N, Varjak M, Pinto RM, Lee JY, Iselin L, Palmalux N, Stewart DG, Swingler S, Greenwood EJD, Crozier TWM, Gu Q, Davies EL, Clohisey S, Wang B, Trindade Maranh?o Costa F, Freire Santana M, de Lima Ferreira LC, Murphy L, Fawkes A, Meynert A, Grimes G; ISARIC4C Investigators, Da Silva Filho JL, Marti M, Hughes J, Stanton RJ, Wang ECY, Ho A, Davis I, Jarrett RF, Castello A, Robertson DL, Semple MG, Openshaw PJM, Palmarini M, Lehner PJ, Baillie JK, Rihn SJ, Wilson SJ."	A prenylated dsRNA sensor protects against severe COVID-19.?
DRAVPR0005	MHRRRSRSCREDQKPVMDDQRDLISNNEQLPMLGRRPGAPESKCSRGALYTGFSILVTLLLAGQATTAYFLYQQQGRLDKLTVTSQNLQLENLRMKLPKPPKPVSKMRMATPLLMQALPMGALPQGPMQNATKYGNMTEDHVMHLLQNADPLKVYPPLKGSFPENLRHLKNTMETIDWKVFESWMHHWLLFEMSRHSLEQKPTDAPPKVLTKCQEEVSHIPAVHPGSFRPKCDENGNYLPLQCYGSIGYCWCVFPNGTEVPNTRSRGHHNCSESLELEDPSSGLGVTKQDLGPVPM	296	HLA class II histocompatibility antigen gamma chain(CD74)	Homo sapiens (Human)	P04233	CD74 	1A6A##1ICF##1IIE##1L3H##1MUJ##3PDO##3PGC##3PGD##3QXA##3QXD##4AEN##4AH2##4X5W##5KSU##5KSV	"EBOV,SARS-CoV-2"	"[Ref.32855215]Ebola virus (EBOV):The p41 isoform of CD74 disrupts cathepsin-mediated Ebola glycoprotein processing, which prevents viral fusion and entry.##SARS-CoV-2: CD74 p41 can stymie the endosomal entry of coronaviruses including SARS-CoV-2."	AF-P04233-F1	"Has antiviral activity by stymieing the endosomal entry of Ebola virus and coronaviruses, including SARS-CoV-2"	"¢ÙGlycosylation of Asn at position 130,136,256.¢ÚThere are three disulfide bonds between Cys213 and Cys232, Cys243 and Cys250, Cys252 and Cys271.¢ÛGlycosylation of Thr at position 203.¢ÜGlycosylation of Ser at position 281."	32855215	"Bruchez A, Sha K, Johnson J, Chen L, Stefani C, McConnell H, Gaucherand L, Prins R, Matreyek KA, Hume AJ, M¨¹hlberger E, Schmidt EV, Olinger GG, Stuart LM, Lacy-Hulbert A."	MHC class II transactivator CIITA induces cell resistance to Ebola virus and SARS-like coronaviruses.
DRAVPR0006	MRCLAPRPAGSYLSEPQGSSQCATMELGPLEGGYLELLNSDADPLCLYHFYDQMDLAGEEEIELYSEPDTDTINCDQFSRLLCDMEGDEETREAYANIAELDQYVFQDSQLEGLSKDIFKHIGPDEVIGESMEMPAEVGQKSQKRPFPEELPADLKHWKPAEPPTVVTGSLLVRPVSDCSTLPCLPLPALFNQEPASGQMRLEKTDQIPMPFSSSSLSCLNLPEGPIQFVPTISTLPHGLWQISEAGTGVSSIFIYHGEVPQASQVPPPSGFTVHGLPTSPDRPGSTSPFAPSATDLPSMPEPALTSRANMTEHKTSPTQCPAAGEVSNKLPKWPEPVEQFYRSLQDTYGAEPAGPDGILVEVDLVQARLERSSSKSLERELATPDWAERQLAQGGLAEVLLAAKEHRRPRETRVIAVLGKAGQGKSYWAGAVSRAWACGRLPQYDFVFSVPCHCLNRPGDAYGLQDLLFSLGPQPLVAADEVFSHILKRPDRVLLILDGFEELEAQDGFLHSTCGPAPAEPCSLRGLLAGLFQKKLLRGCTLLLTARPRGRLVQSLSKADALFELSGFSMEQAQAYVMRYFESSGMTEHQDRALTLLRDRPLLLSHSHSPTLCRAVCQLSEALLELGEDAKLPSTLTGLYVGLLGRAALDSPPGALAELAKLAWELGRRHQSTLQEDQFPSADVRTWAMAKGLVQHPPRAAESELAFPSFLLQCFLGALWLALSGEIKDKELPQYLALTPRKKRPYDNWLEGVPRFLAGLIFQPPARCLGALLGPSAAASVDRKQKVLARYLKRLQPGTLRARQLLELLHCAHEAEEAGIWQHVVQELPGRLSFLGTRLTPPDAHVLGKALEAAGQDFSLDLRSTGICPSGLGSLVGLSCVTRFRAALSDTVALWESLQQHGETKLLQAAEEKFTIEPFKAKSLKDVEDLGKLVQTQRTRSSSEDTAGELPAVRDLKKLEFALGPVSGPQAFPKLVRILTAFSSLQHLDLDALSENKIGDEGVSQLSATFPQLKSLETLNLSQNNITDLGAYKLAEALPSLAASLLRLSLYNNCICDVGAESLARVLPDMVSLRVMDVQYNKFTAAGAQQLAASLRRCPHVETLAMWTPTIPFSVQEHLQQQDSRISLR	1130	MHC class II transactivator	Homo sapiens (Human)	P33076	CIITA	None	"EBOV,SARS-CoV-2"	"[Ref.32855215]Ebola virus (EBOV):The p41 isoform of CD74 disrupts cathepsin-mediated Ebola glycoprotein processing, which prevents viral fusion and entry.##SARS-CoV-2: CD74 p41 can stymie the endosomal entry of coronaviruses including SARS-CoV-2."	AF-P33076-F1	"Has antiviral activity against Ebola virus and coronaviruses, including SARS-CoV-2. Induces resistance by up-regulation of the p41 isoform of CD74, which blocks cathepsin-mediated cleavage of viral glycoproteins, thereby preventing viral fusion"	No modifications on the sequence.	32855215	"Bruchez A, Sha K, Johnson J, Chen L, Stefani C, McConnell H, Gaucherand L, Prins R, Matreyek KA, Hume AJ, M¨¹hlberger E, Schmidt EV, Olinger GG, Stuart LM, Lacy-Hulbert A."	MHC class II transactivator CIITA induces cell resistance to Ebola virus and SARS-like coronaviruses.
DRAVPR0007	MPPRSLSNLSFPTEANESELVPEVWEKDFLPDSDGTTAELVIRCVIPSLYLIIISVGLLGNIMLVKIFLTNSAMRNVPNIFISNLAAGDLLLLLTCVPVDASRYFFDEWVFGKLGCKLIPAIQLTSVGVSVFTLTALSADRYRAIVNPMDMQTSGVLLWTSLKAVGIWVVSVLLAVPEAVFSEVARIGSLDNSSFTACIPYPQTDELHPKIHSVLIFLVYFLIPLVIISIYYYHIAKTLIKSAHNLPGEYNEHTKKQMETRKRLAKIVLVFVGCFVFCWFPNHVLYLYRSFNYKEIDPSLGHMIVTLVARVLSFSNSCVNPFALYLLSESFRKHFNSQLCCGRKSYPERSTSYLLSSSAVRMTSLKSNTKNVVTNSVLLNGHSTKQEIAL	390	Neuromedin-B receptor(NMB-R)	Mus musculus (Mouse)	O54799	Nmbr	None	IAV	[Ref.31601264]Influenza virus strain A/Puerto Rico/8/1934 (H1N1):Neuromedin-B receptor plays a role in the innate immune response to influenza A virus infection by enhancing interferon alpha expression and reducing expression of IL6.	AF-O54799-F1	"The NMB/NMBR system appeared to increase IFN-¦Á expression and decrease IL-6 expression after PR8 infection, which may serve to establish an antiviral state in the host."	"¢ÙGlycosylation of Asn at position 8, 16, 192.¢ÚThe Cys at position 341 indicates S-palmitoyl cysteine.¢ÛPhosphorylation of Ser at position 352.¢ÜThere is a disulfide bond between cys116 and Cys198."	31601264	"Yang G, Huang H, Tang M, Cai Z, Huang C, Qi B, Chen JL."	Role of neuromedin B and its receptor in the innate immune responses against influenza A virus infection in vitro and in vivo.
DRAVPR0008	MARRAGGARMFGSLLLFALLAAGVAPLSWDLPEPRSRASKIRVHSRGNLWATGHFMGKKSLEPSSPSPLGTAPHTSLRDQRLQLSHDLLGILLLKKALGVSLSRPAPQIQYRRLLVQILQK	121	Neuromedin-B	Homo sapiens (Human)	P08949	NMB	1C98##1C9A	IAV	[Ref.31601264]Influenza virus strain A/Puerto Rico/8/1934 (H1N1): NMR up-regulated in response to infection with influenza A virus.	AF-P08949-F1	"It is likely that NMB plays an anti-inflammatory role via the regulation of the host type I IFN signalling pathway. The NMB/NMBR system appeared to increase IFN-¦Á expression and decrease IL-6 expression after PR8 infection, which may serve to establish an antiviral state in the host."	The Met at position 56 is amidation.	31601264	"Yang G, Huang H, Tang M, Cai Z, Huang C, Qi B, Chen JL."	Role of neuromedin B and its receptor in the innate immune responses against influenza A virus infection in vitro and in vivo.
DRAVPR0009	MTRQAGSSWLLRGLLLFALFASGVAPFNWDLPEPRSRASKIRVHPRGNLWATGHFMGKKSLEPPSLSLVGTAPPNTPRDQRLQLSHDLLRILLRKKALGMNFSGPAPPIQYRRLLEPLLQK	121	Neuromedin-B	Mus musculus (Mouse)	Q9CR53	Nmb	None	IAV	[Ref.31601264]Influenza virus strain A/Puerto Rico/8/1934 (H1N1): NMR up-regulated in response to infection with influenza A virus.	AF-Q9CR53-F1	"It is likely that NMB plays an anti-inflammatory role via the regulation of the host type I IFN signalling pathway. The NMB/NMBR system appeared to increase IFN-¦Á expression and decrease IL-6 expression after PR8 infection, which may serve to establish an antiviral state in the host."	The Met at position 56 is amidation.	31601264	"Yang G, Huang H, Tang M, Cai Z, Huang C, Qi B, Chen JL."	Role of neuromedin B and its receptor in the innate immune responses against influenza A virus infection in vitro and in vivo.
DRAVPR0010	MPSKSLSNLSVTTGANESGSVPEGWERDFLPASDGTTTELVIRCVIPSLYLLIITVGLLGNIMLVKIFITNSAMRSVPNIFISNLAAGDLLLLLTCVPVDASRYFFDEWMFGKVGCKLIPVIQLTSVGVSVFTLTALSADRYRAIVNPMDMQTSGALLRTCVKAMGIWVVSVLLAVPEAVFSEVARISSLDNSSFTACIPYPQTDELHPKIHSVLIFLVYFLIPLAIISIYYYHIAKTLIKSAHNLPGEYNEHTKKQMETRKRLAKIVLVFVGCFIFCWFPNHILYMYRSFNYNEIDPSLGHMIVTLVARVLSFGNSCVNPFALYLLSESFRRHFNSQLCCGRKSYQERGTSYLLSSSAVRMTSLKSNAKNMVTNSVLLNGHSMKQEMAL	390	Neuromedin-B receptor	Homo sapiens (Human)	P28336	NMBR	None	IAV	[Ref.31601264]Influenza virus strain A/Puerto Rico/8/1934 (H1N1):Neuromedin-B receptor plays a role in the innate immune response to influenza A virus infection by enhancing interferon alpha expression and reducing expression of IL6.	No predicted structure information available for the entry	"The NMB/NMBR system appeared to increase IFN-¦Á expression and decrease IL-6 expression after PR8 infection, which may serve to establish an antiviral state in the host."	"¢ÙGlycosylation of Asn at position 8, 16, 192.¢ÚThe Cys at position 341 indicates S-palmitoyl cysteine.¢ÛPhosphorylation of Ser at position 352.¢ÜThere is a disulfide bond between cys116 and Cys198."	31601264	"Yang G, Huang H, Tang M, Cai Z, Huang C, Qi B, Chen JL."	Role of neuromedin B and its receptor in the innate immune responses against influenza A virus infection in vitro and in vivo.
DRAVPR0011	MGWDLTVKMLAGNEFQVSLSSSMSVSELKAQITQKIGVHAFQQRLAVHPSGVALQDRVPLASQGLGPGSTVLLVVDKCDEPLSILVRNNKGRSSTYEVRLTQTVAHLKQQVSGLEGVQDDLFWLTFEGKPLEDQLPLGEYGLKPLSTVFMNLRLRGGGTEPGGRS	165	Ubiquitin-like protein ISG15(ISG15)	Homo sapiens (Human)	P05161	ISG15	"1Z2M##	2HJ8##3PHX##3PSE##3R66##3RT3##3SDL##5TL6##5W8T##5W8U##6BI8##6FFA##6XA9##7RBS##7S6P"	"HIV-1,EBOV,IAV"	"[Ref.16434471]Human immunodeficiency virus type-1(HIV-1):inhibits the ubiquitination of HIV-1-encoded Gag polypeptide and Tsg101 and the interaction of Tsg101, a central component of ESCRT-1 with the p6 domain of the Gag polyprotein, thereby preventing assembly and release of virions from infected cells.##[Ref.18305167]Ebola virus(EBOV):inhibits Ebola virus budding mediated by the VP40 protein by disrupting ubiquitin ligase activity of NEDD4 and its ability to ubiquitinate VP40.##[Ref.20133869]Influenza A virus(IAV):ISG15 modification of K41 of the NS1A protein inhibits influenza A virus replication and thus contributes to the antiviral action of IFN-¦Â."	AF-P05161-F1	"ISG15 may affect replication not only of HIV-1, but also of a broad group of RNA viruses."	The Cys at position78 indicates S-nitrosocysteine.	16434471##18305167##20133869	"Okumura A, Lu G, Pitha-Rowe I, Pitha PM.##Okumura A, Pitha PM, Harty RN.##Zhao C, Hsiang TY, Kuo RL, Krug RM."	Innate antiviral response targets HIV-1 release by the induction of ubiquitin-like protein ISG15.##ISG15 inhibits Ebola VP40 VLP budding in an L-domain-dependent manner by blocking Nedd4 ligase activity.##ISG15 conjugation system targets the viral NS1 protein in influenza A virus-infected cells.
DRAVPR0012	MAGSREVVAMDCEMVGLGPHRESGLARCSLVNVHGAVLYDKFIRPEGEITDYRTRVSGVTPQHMVGATPFAVARLEILQLLKGKLVVGHDLKHDFQALKEDMSGYTIYDTSTDRLLWREAKLDHCRRVSLRVLSERLLHKSIQNSLLGHSSVEDARATMELYQISQRIRARRGLPRLAVSD	181	Interferon-stimulated gene 20 kDa protein(ISG20)	Homo sapiens (Human)	Q96AZ6	ISG20	1WLJ	"HCV,HAV,YFV"	"[Ref.21036379]Hepatitis C virus (HCV):ISG20 inhibits HCV RNA replication and progeny virus release in Huh7.5 cells that lack both RIG-I and TLR3 viral RNA sensing pathways which recognize HCV replication and trigger IFN antiviral responses.##ISG20 against HCV, HAV(hepatitis A virus), BVDV(bovine viral diarrhea virus) and YFV(yellow fever virus) all require the exonuclease activity of ISG20."	AF-Q96AZ6-F1	ISG20 is an interferon-inducible 3¡ä¨C5¡ä exonuclease that inhibits replication of several human and animal RNA viruses. 	No modifications on the sequence.	21036379##12594219	"Zhou Z, Wang N, Woodson SE, Dong Q, Wang J, Liang Y, Rijnbrand R, Wei L, Nichols JE, Guo JT, Holbrook MR, Lemon SM, Li K.##Espert L, Degols G, Gongora C, Blondel D, Williams BR, Silverman RH, Mechti N."	"Antiviral activities of ISG20 in positive-strand RNA virus infections.##ISG20, a new interferon-induced RNase specific for single-stranded RNA, defines an alternative antiviral pathway against RNA genomic viruses."
DRAVPR0013	MRQKAVSLFLCYLLLFTCSGVEAGKKKCSESSDSGSGFWKALTFMAVGGGLAVAGLPALGFTGAGIAANSVAASLMSWSAILNGGGVPAGGLVATLQSLGAGGSSVVIGNIGALMGYATHKYLDSEEDEE	130	Interferon alpha-inducible protein 6(IFI6)	Homo sapiens (Human)	P09912	IFI6 	None	HCV	[Ref.25757571]Hepatitis C virus (HCV):IFI6 inhibits HCV entry by disrupting EGFR activation and HRas/Raf-1 signaling and downstream CD81-CLDN1 interactions in response to HCV infection or CD81 crosslinking.	AF-P09912-F1	IFI6 was one of a number of ISGs shown to inhibit yellow fever virus (YFV) infection in STAT1-deficient human.IFI6 suggests a block at a subsequent step in DENV replication.	No modifications on the sequence.	25757571	"Meyer K, Kwon YC, Liu S, Hagedorn CH, Ray RB, Ray R. "	Interferon-¦Á inducible protein 6 impairs EGFR activation by CD81 and inhibits hepatitis C virus infection.
DRAVPR0014	MEASALTSSAVTSVAKVVRVASGSAVVLPLARIATVVIGGVVAMAAVPMVLSAMGFTAAGIASSSIAAKMMSAAAIANGGGVASGSLVATLQSLGATGLSGLTKFILGSIGSAIAAVIARFY	122	Interferon alpha-inducible protein 27(ISG12a)	Homo sapiens (Human)	P40305	IFI27	None	HCV	"[Ref.27194766]Hepatitis C virus (HCV):ISG12a mediates NS5A degradation via a ubiquitination-dependent proteasomal pathway, which is a multifunctional protein is indispensable for HCV replication and virus production."	AF-P40305-F1	"ISG12a relies on the E3 ligase domain of SKP2 to restrict viral infection.The antiviral effects of ISG12a/IFI27 on HCV, NDV, WNV, and mouse hepatitis virus (MHV) infection in vitro or in vivo have been determined."	No modifications on the sequence.	27194766##27777077	"Xue B, Yang D, Wang J, Xu Y, Wang X, Qin Y, Tian R, Chen S, Xie Q, Liu N, Zhu H.##Chen Y, Jiao B, Yao M, Shi X, Zheng Z, Li S, Chen L."	ISG12a Restricts Hepatitis C Virus Infection through the Ubiquitination-Dependent Degradation Pathway.##ISG12a inhibits HCV replication and potentiates the anti-HCV activity of IFN-¦Á through activation of the Jak/STAT signaling pathway independent of autophagy and apoptosis.
DRAVPR0015	MELRHTPARDLDKFIEDHLLPNTCFRTQVKEAIDIVCRFLKERCFQGTADPVRVSKVVKGGSSGKGTTLRGRSDADLVVFLTKLTSFEDQLRRRGEFIQEIRRQLEACQREQKFKVTFEVQSPRRENPRALSFVLSSPQLQQEVEFDVLPAFDALGQWTPGYKPNPEIYVQLIKECKSRGKEGEFSTCFTELQRDFLRNRPTKLKSLIRLVKHWYQTCKKTHGNKLPPQYALELLTVYAWEQGSRKTDFSTAQGFQTVLELVLKHQKLCIFWEAYYDFTNPVVGRCMLQQLKKPRPVILDPADPTGNVGGGDTHSWQRLAQEARVWLGYPCCKNLDGSLVGAWTMLQKI	349	2'-5'-oligoadenylate synthase 1(p42 OAS)	Sus scrofa (Pig)	Q29599	OAS1	1PX5##4RWN##4RWO##4RWP##4RWQ	"VSV,HSV-2,EMCV"	[Ref.20844035]encephalomyocarditis virus (EMCV):inhibition of the cytopathic effect in HepG2 cells(EC50=24.5 ¦Ìg/ml);inhibition of the cytopathic effect in Vero cells(EC50=18.5 ¦Ìg/ml).	AF-Q29599-F1	The OAS family of proteins mediates antiviral activity via the synthesis of 2-5A and subsequent activation of RNase L. 	No modifications on the sequence.	20844035	"Kristiansen H, Scherer CA, McVean M, Iadonato SP, Vends S, Thavachelvam K, Steffensen TB, Horan KA, Kuri T, Weber F, Paludan SR, Hartmann R. "	Extracellular 2'-5' oligoadenylate synthetase stimulates RNase L-independent antiviral activity: a novel mechanism of virus-induced innate immunity.
DRAVPR0016	MAWRYSQLLLVPVQLVFLASVCCPGVWGSTVSEELHRMVGQSLSVQCQYKPKEESYVLKTWCRQTAPSKCTRVVTTSEPRKAARELQHTIWDDPEAGFFNITMTQLTEDDSAFYWCGPYYPSLREVTVLRNISLVVSPAPSTLPSQTIAPLPESTATIFMPFPVLTTSPEETTDSSINGTGHRNQSSSSPGWTSPGLLVSVQYGLLLLKALMLSVFCVLLCWRSGQGREYMAETMELSKLPHISKSLDTVSHISGYEKKANWY	263	Trem-like transcript 4 protein(TLT-4)	Mus musculus (Mouse)	Q3LRV9	Treml4	None	IAV	[Ref.25848864]TREML4 plays an important role in the regulation of TLR7 signaling and that its expression in vivo is required for antiviral host defense to influenza and for promotion of TLR7-mediated autoimmune disease.	AF-Q3LRV9-F1	No comments found in the entry	¢ÙGlycosylation of Asn at position 100.¢ÚThere is a disulfide bond between Cys47 and Cys116.	25848864	"Ramirez-Ortiz ZG, Prasad A, Griffith JW, Pendergraft WF 3rd, Cowley GS, Root DE, Tai M, Luster AD, El Khoury J, Hacohen N, Means TK. "	The receptor TREML4 amplifies TLR7-mediated signaling during antiviral responses and autoimmunity.
DRAVPR0017	MKMKVLEVVGLAISIWLMLTPPASSNIVFDVENATPETYSNFLTSLREAVKDKKLTCHGMIMATTLTEQPKYVLVDLKFGSGTFTLAIRRGNLYLEGYSDIYNGKCRYRIFKDSESDAQETVCPGDKSKPGTQNNIPYEKSYKGMESKGGARTKLGLGKITLKSRMGKIYGKDATDQKQYQKNEAEFLLIAVQMVTEASRFKYIENKVKAKFDDANGYQPDPKAISLEKNWDSVSKVIAKVGTSGDSTVTLPGDLKDENNKPWTTATMNDLKNDIMALLTHVTCKVKSSMFPEIMSYYYRTSISNLGEFE	310	Antiviral protein II/III	Phytolacca americana (American pokeweed) (Phytolacca decandra)	Q40772	PAP2	1LLN	"HIV-1,TMV"	[Ref.10403789]Human immunodeficiency virus (HIV)-1:inhibition the replication of HIV-1 in human peripheral blood mononuclear cells(PAP-II:IC50=25 nM;PAP-III:IC50=16 nM);##tobacco mosaic virus(TMV):PAP-II and PAP-III cause concentration-dependent depurination of genomic RNA purified from TMV.	AF-Q40772-F1	"The potent antiviral activity of PAP may in part be due to its unique ability to extensively depurinate viral RNA. The protein has 2 forms, PAP-II and PAP-III, which differ in their seasonal expression."	"There are two disulfide bonds between Cys57 and Cys284, Cys106 and Cys123."	10403789	"Rajamohan F, Venkatachalam TK, Irvin JD, Uckun FM."	"Pokeweed antiviral protein isoforms PAP-I, PAP-II, and PAP-III depurinate RNA of human immunodeficiency virus (HIV)-1. "
DRAVPR0018	MKSMLVVTISIWLILAPTSTWAVNTIIYNVGSTTISKYATFLNDLRNEAKDPSLKCYGIPMLPNTNTNPKYVLVELQGSNKKTITLMLRRNNLYVMGYSDPFETNKCRYHIFNDISGTERQDVETTLCPNANSRVSKNINFDSRYPTLESKAGVKSRSQVQLGIQILDSNIGKISGVMSFTEKTEAEFLLVAIQMVSEAARFKYIENQVKTNFNRAFNPNPKVLNLQETWGKISTAIHDAKNGVLPKPLELVDASGAKWIVLRVDEIKPDVALLNYVGGSCQTTYNQNAMFPQLIMSTYYNYMVNLGDLFEGF	313	Antiviral protein I	Phytolacca americana (American pokeweed) (Phytolacca decandra)	P10297	PAP1	"1D6A##	1PAF##1PAG##1QCG##1QCI##1QCJ"		[Ref.10403789]Human immunodeficiency virus (HIV)-1:inhibition the replication of HIV-1 in human peripheral blood mononuclear cells(IC50=17 nM);##tobacco mosaic virus(TMV):PAP-I  cause concentration-dependent depurination of genomic RNA purified from TMV.	AF-P10297-F1	The potent antiviral activity of PAP may in part be due to its unique ability to extensively depurinate viral RNA.	"There are two disulfide bonds between Cys56 and Cys281, Cys107 and Cys128."	10403789	"Rajamohan F, Venkatachalam TK, Irvin JD, Uckun FM."	"Pokeweed antiviral protein isoforms PAP-I, PAP-II, and PAP-III depurinate RNA of human immunodeficiency virus (HIV)-1. "
DRAVPR0019	MTSPHFSSYDEGPLDVSMAATNLENQLHSAQKNLLFLQREHASTLKGLHSEIRRLQQHCTDLTYELTVKSSEQTGDGTSKSSELKKRCEELEAQLKVKENENAELLKELEQKNAMITVLENTIKEREKKYLEELKAKSHKLTLLSSELEQRASTIAYLTSQLHAAKKKLMSSSGTSDASPSGSPVLASYKPAPPKDKLPETPRRRMKKSLSAPLHPEFEEVYRFGAESRKLLLREPVDAMPDPTPFLLARESAEVHLIKERPLVIPPIASDRSGEQHSPAREKPHKAHVGVAHRIHHATPPQAQPEVKTLAVDQVNGGKVVRKHSGTDRTV	331	Coiled-coil domain-containing protein 92	Homo sapiens (Human)	Q53HC0	CCDC92	None	EBOV	[Ref.32528005]Ebola virus(EBOV):CCDC92 can inhibit viral transcription and the formation of complete virions via an interaction with the viral protein NP.	AF-Q53HC0-F1	"CCDC92 clearly inhibits viral transcription, which is mediated through the C-terminal coiled-coil domain of CCDC92 (aa 81¨C151) that is necessary for the interaction with NP."	Phosphorylation of Ser at position 209.	32528005	"Kuroda M, Halfmann PJ, Hill-Batorski L, Ozawa M, Lopes TJS, Neumann G, Schoggins JW, Rice CM, Kawaoka Y."	Identification of interferon-stimulated genes that attenuate Ebola virus infection.
DRAVPR0020	MEQDLRSIPASKLDKFIENHLPDTSFCADLREVIDALCALLKDRSFRGPVRRMRASKGVKGKGTTLKGRSDADLVVFLNNLTSFEDQLNQQGVLIKEIKKQLCEVQHERRCGVKFEVHSLRSPNSRALSFKLSAPDLLKEVKFDVLPAYDLLDHLNILKKPNQQFYANLISGRTPPGKEGKLSICFMGLRKYFLNCRPTKLKRLIRLVTHWYQLCKEKLGDPLPPQYALELLTVYAWEYGSRVTKFNTAQGFRTVLELVTKYKQLQIYWTVYYDFRHQEVSEYLHQQLKKDRPVILDPADPTRNIAGLNPKDWRRLAGEAAAWLQYPCFKYRDGSSVCSWEVPTEVGVPMKYLLCRIFWLLFWSLFHFIFGKTSSG	376	Inactive 2'-5'-oligoadenylate synthase 1B	Mus musculus (Mouse)	Q60856	Oas1b	None	WNV	[Ref.16371364]West Nile virus(WNV):Oas1b inhibits the replication of WNV by preventing viral RNA accumulation inside infected cells.	AF-Q60856-F1	"Oas1b-dependent antiviral activity is restricted to the early stages of WNV replication,the Oas1b-mediated inhibition of viral protein synthesis and the subsequent suppression of viral growth are due to a lack of accumulation of viral RNA inside cells."	No modifications on the sequence.	16371364	"Kajaste-Rudnitski A, Mashimo T, Frenkiel MP, Gu¨¦net JL, Lucas M, Despr¨¨s P. "	"The 2',5'-oligoadenylate synthetase 1b is a potent inhibitor of West Nile virus replication inside infected cells. "
DRAVPR0021	MARLCAFLMILIVMSYWSTCSLGCDLPHTYNLRNKRALKVLAQMRRLTPLSCLKDRKDFGFPLEKVDAQQIQKAQSIPVLRDLTQQILNLFASKDSSAAWNATLLDSFCNDLHQQLNDLQGCLMQQVGVQESPLTQEDSLLAVRIYFHRITVFLREKKHSPCAWEVVRAEVWRALSSSANVLGRLREEKA	190	Interferon alpha-11(Limitin)	Mus musculus (Mouse)	Q61716	Ifna11	None		[Ref.22912583]IFN-¦Á11-mediated activation of NK cells enabled cytolytic killing of FV-infected target cells via the exocytosis pathway. 	AF-Q61716-F1	IFN-¦Á11 significantly reduced viral loads during Friend retrovirus infection (FV).	"¢ÙGlycosylation of Asn at position 101.¢ÚThere are two disulfide bonds between Cys24 and Cys122, Cys52 and Cys162."	22912583	"Gibbert K, Joedicke JJ, Meryk A, Trilling M, Francois S, Duppach J, Kraft A, Lang KS, Dittmer U. "	Interferon-alpha subtype 11 activates NK cells and enables control of retroviral infection.
DRAVPR0022	MSLFPSLPLLLLSMVAASYSETVTCEDAQKTCPAVIACSSPGINGFPGKDGRDGTKGEKGEPGQGLRGLQGPPGKLGPPGNPGPSGSPGPKGQKGDPGKSPDGDSSLAASERKALQTEMARIKKWLTFSLGKQVGNKFFLTNGEIMTFEKVKALCVKFQASVATPRNAAENGAIQNLIKEEAFLGITDEKTEGQFVDLTGNRLTYTNWNEGEPNNAGSDEDCVLLLKNGQWNDVPCSTSHLAVCEFPI	248	Mannose-binding protein C(MBP-C)	Homo sapiens (Human)	P11226	MBL2 	1HUP	SARS-CoV-2	"[Ref.35102342]SARS-CoV-2:MBL bound trimeric spike protein and then activated the lectin pathway of complement activation, which leads to the inhibition SARS-CoV-2 infection and a reduction of the induced inflammatory response.(Spike-mediated viral entry was inhibited by 90% at the concentration of 10??g/ml(34?nM) in 293T cells, EC50= 0.5??g/ml (1.7?nM))."	AF-P11226-F1	MBL was found to interact with spike protein and have antiviral activity with an EC50 of approximately 0.08?¦Ìg ml¨C1 (0.27?nM) and an affinity of 34?nM.	"¢ÙHydroxylation of Pro at position 47,73,79,82,88.¢ÚThere are two disulfide bonds between Cys155 and Cys244, Cys222 and Cys236."	35102342	"Stravalaci M, Pagani I, Paraboschi EM, Pedotti M, Doni A, Scavello F, Mapelli SN, Sironi M, Perucchini C, Varani L, Matkovic M, Cavalli A, Cesana D, Gallina P, Pedemonte N, Capurro V, Clementi N, Mancini N, Invernizzi P, Bayarri-Olmos R, Garred P, Rappuoli R, Duga S, Bottazzi B, Uguccioni M, Asselta R, Vicenzi E, Mantovani A, Garlanda C."	Recognition and inhibition of SARS-CoV-2 by humoral innate immunity pattern recognition molecules. 
DRAVPR0023	MHKEEHEVAVLGPPPSTILPRSTVINIHSETSVPDHVVWSLFNTLFLNWCCLGFIAFAYSVKSRDRKMVGDVTGAQAYASTAKCLNIWALILGILMTIGFILLLVFGSVTVYHIMLQIIQEKRGY	125	Interferon-induced transmembrane protein 1(IFITM1)	Homo sapiens (Human)	P13164	IFITM1	None	"HCV,SARS-CoV-2"	[Ref.26354436]Hepatitis C Virus(HCV):IFITM1 to be able to limit HCV infection at the level of HCV entry through an interaction with the essential entry co-receptor CD81.##[Ref.33270927]SARS-CoV-2:IFITM1 likely restrict SARS©\CoV©\2 infection by mechanically disfavoring viral membrane fusion reactions occurring at endosomes.	AF-P13164-F1	"IFITM1, IFITM2, and IFITM3 primarily act on the early stages of HCV infection.Active against multiple viruses, including influenza A virus, SARS coronaviruses (SARS-CoV and SARS-CoV-2), Marburg virus (MARV), Ebola virus (EBOV), Dengue virus (DNV), West Nile virus (WNV), human immunodeficiency virus type 1 (HIV-1) and hepatitis C virus (HCV)."	"¢ÙPhosphorylation of Ser at position 16.¢ÚThe Cys at position 50,51,84 indicates S-palmitoyl cysteine."	26354436##33270927##33051876	"Narayana SK, Helbig KJ, McCartney EM, Eyre NS, Bull RA, Eltahla A, Lloyd AR, Beard MR.##Shi G, Kenney AD, Kudryashova E, Zani A, Zhang L, Lai KK, Hall-Stoodley L, Robinson RT, Kudryashov DS, Compton AA, Yount JS.##Buchrieser J, Dufloo J, Hubert M, Monel B, Planas D, Rajah MM, Planchais C, Porrot F, Guivel-Benhassine F, Van der Werf S, Casartelli N, Mouquet H, Bruel T, Schwartz O."	"The Interferon-induced Transmembrane Proteins, IFITM1, IFITM2, and IFITM3 Inhibit Hepatitis C Virus Entry.?##Opposing activities of IFITM proteins in SARS-CoV-2 infection. ##Syncytia formation by SARS-CoV-2-infected cells. "
DRAVPR0024	MNHIVQTFSPVNSGQPPNYEMLKEEQEVAMLGVPHNPAPPMSTVIHIRSETSVPDHVVWSLFNTLFMNTCCLGFIAFAYSVKSRDRKMVGDVTGAQAYASTAKCLNIWALILGIFMTILLIIIPVLVVQAQR	132	Interferon-induced transmembrane protein 2(IFITM2)	Homo sapiens (Human)	Q01629	IFITM2	None	"HCV,SARS-CoV-2"	"[Ref.26354436]Hepatitis C Virus(HCV):inhibiting the late stages of HCV entry, possibly in a coordinated manner by trapping the virion in the endosomal pathway and targeting it for degradation at the lysosome.##[Ref.33270927]SARS-CoV-2:IFITM2 likely restrict SARS©\CoV©\2 infection by mechanically disfavoring viral membrane fusion reactions occurring at endosomes."	AF-Q01629-F1	"IFITM1, IFITM2, and IFITM3 primarily act on the early stages of HCV infection.Active against multiple viruses, including influenza A virus, SARS coronaviruses (SARS-CoV and SARS-CoV-2), Marburg virus (MARV), Ebola virus (EBOV), Dengue virus (DNV), West Nile virus (WNV), human immunodeficiency virus type 1 (HIV-1), hepatitis C virus (HCV) and vesicular stomatitis virus (VSV)"	"¢ÙPhosphorylation of Ser at position 19.¢ÚThe Cys at position 70,71,104 indicates S-palmitoyl cysteine."	26354436##33270927	"Narayana SK, Helbig KJ, McCartney EM, Eyre NS, Bull RA, Eltahla A, Lloyd AR, Beard MR.##Shi G, Kenney AD, Kudryashova E, Zani A, Zhang L, Lai KK, Hall-Stoodley L, Robinson RT, Kudryashov DS, Compton AA, Yount JS."	"The Interferon-induced Transmembrane Proteins, IFITM1, IFITM2, and IFITM3 Inhibit Hepatitis C Virus Entry.?##Opposing activities of IFITM proteins in SARS-CoV-2 infection. "
DRAVPR0025	MNHTVQTFFSPVNSGQPPNYEMLKEEHEVAVLGAPHNPAPPTSTVIHIRSETSVPDHVVWSLFNTLFMNPCCLGFIAFAYSVKSRDRKMVGDVTGAQAYASTAKCLNIWALILGILMTILLIVIPVLIFQAYG	133	Interferon-induced transmembrane protein 3(IFITM3)	Homo sapiens (Human)	Q01628	IFITM3 	None	"HCV,SARS-CoV-2"	"[Ref.26354436]Hepatitis C Virus(HCV):inhibiting the late stages of HCV entry, possibly in a coordinated manner by trapping the virion in the endosomal pathway and targeting it for degradation at the lysosome.##[Ref.33270927]SARS-CoV-2:IFITM3 likely restrict SARS©\CoV©\2 infection by mechanically disfavoring viral membrane fusion reactions occurring at endosomes."	AF-Q01628-F1	"IFITM1, IFITM2, and IFITM3 primarily act on the early stages of HCV infection.IFITM3 exhibits both anti©\ and pro©\viral effects against SARS-CoV-2, inhibiting endocytic entry of the virus while also enhancing virus fusion at the plasma membrane.Active against multiple viruses, including influenza A virus, SARS coronaviruses (SARS-CoV and SARS-CoV-2), Marburg virus (MARV), Ebola virus (EBOV), Dengue virus (DNV), West Nile virus (WNV), human immunodeficiency virus type 1 (HIV-1), hepatitis C virus (HCV) and vesicular stomatitis virus (VSV) "	"¢ÙPhosphorylation of Ser at position 20.¢ÚThe Cys at position 71,72,105 indicates S-palmitoyl cysteine."	26354436##33270927	"Narayana SK, Helbig KJ, McCartney EM, Eyre NS, Bull RA, Eltahla A, Lloyd AR, Beard MR.##Shi G, Kenney AD, Kudryashova E, Zani A, Zhang L, Lai KK, Hall-Stoodley L, Robinson RT, Kudryashov DS, Compton AA, Yount JS."	"The Interferon-induced Transmembrane Proteins, IFITM1, IFITM2, and IFITM3 Inhibit Hepatitis C Virus Entry.?##Opposing activities of IFITM proteins in SARS-CoV-2 infection. "
DRAVPR0026	MAISKKSSLFLPIFTFITMFLMVVNKVSSSTHETNALHFMFNQFSKDQKDLILQGDATTGTDGNLELTRVSSNGSPQGSSVGRALFYAPVHIWESSAVVASFDATFTFLIKSPDSHPADGIAFFISNIDSSIPSGSTGRLLGLFPDANVIRNSTTIDFNAAYNADTIVAVELDTYPNTDIGDPNYPHIGIDIKSVRSKKTAKWNMQNGKVGTAHIIYNSVGKRLSAVVSYPNGDSATVSYDVDLDNVLPEWVRVGLSASTGLYKETNTILSWSFTSKLKSNEIPDIATVV	290	Concanavalin-A	Canavalia gladiata (Sword bean) (Dolichos gladiatus)	P14894	N/A	1WUV##2D7F##2EF6##2OVU##2P2K	HIV-1	[Ref.15935326]Human immunodeficiency virus type-1(HIV-1):Inhibits HIV-1 reverse transcriptase.(IC50=35 ¦ÌM)	AF-P14894-F1	The mechanism of anti-HIV-1 activity may be protein¨Cprotein interaction.	Glycosylation of Asn at position 152.	15935326	"Wong JH, Ng TB. "	Isolation and characterization of a glucose/mannose/rhamnose-specific lectin from the knife bean Canavalia gladiata.
DRAVPR0027	MEASPASGPRHLMDPHIFTSNFNNGIGRHKTYLCYEVERLDNGTSVKMDQHRGFLHNQAKNLLCGFYGRHAELRFLDLVPSLQLDPAQIYRVTWFISWSPCFSWGCAGEVRAFLQENTHVRLRIFAARIYDYDPLYKEALQMLRDAGAQVSIMTYDEFKHCWDTFVDHQGCPFQPWDGLDEHSQALSGRLRAILQNQGN	199	DNA dC->dU-editing enzyme APOBEC-3A	Homo sapiens (Human)	P31941	APOBEC3A	2M65##4XXO##5KEG##5SWW##7D3V##7D3W##7D3X	"HTLV-1,AAV"	[Ref.22457529]Human T-lymphotropic virus type 1(HTLV-1):APOBEC3A hapII potently decrease HTLV-1 infectivity.##[Ref.16527742]adeno-associated virus(AAV):APOBEC3A is a potent inhibitor of adeno-associated virus and retrotransposons.	AF-P31941-F1	Exhibits antiviral activity against adeno-associated virus (AAV) and human T-cell leukemia virus type 1 (HTLV-1) and may inhibit the mobility of LTR and non-LTR retrotransposons. 	No modifications on the sequence.	22457529##16527742	"Ooms M, Krikoni A, Kress AK, Simon V, M¨¹nk C. ##Chen H, Lilley CE, Yu Q, Lee DV, Chou J, Narvaiza I, Landau NR, Weitzman MD."	"APOBEC3A, APOBEC3B, and APOBEC3H haplotype 2 restrict human T-lymphotropic virus type 1.##APOBEC3A is a potent inhibitor of adeno-associated virus and retrotransposons."
DRAVPR0028	MNPQIRNPMERMYRDTFYDNFENEPILYGRSYTWLCYEVKIKRGRSNLLWDTGVFRGQVYFKPQYHAEMCFLSWFCGNQLPAYKCFQITWFVSWTPCPDCVAKLAEFLSEHPNVTLTISAARLYYYWERDYRRALCRLSQAGARVTIMDYEEFAYCWENFVYNEGQQFMPWYKFDENYAFLHRTLKEILRYLMDPDTFTFNFNNDPLVLRRRQTYLCYEVERLDNGTWVLMDQHMGFLCNEAKNLLCGFYGRHAELRFLDLVPSLQLDPAQIYRVTWFISWSPCFSWGCAGEVRAFLQENTHVRLRIFAARIYDYDPLYKEALQMLRDAGAQVSIMTYDEFEYCWDTFVYRQGCPFQPWDGLEEHSQALSGRLRAILQNQGN	382	DNA dC->dU-editing enzyme APOBEC-3B	Homo sapiens (Human)	Q9UH17	APOBEC3B	2NBQ##5CQD##5CQH##5CQI##5CQK##5SXG##5SXH##5TD5##5TKM##6NFK##6NFL##6NFM	"HTLV-1,SIV"	"[Ref.22457529]Human T-lymphotropic virus type 1(HTLV-1):APOBEC3B hapII potently decrease HTLV-1 infectivity.##[Ref.15466872]simian immunodeficiency virus(SIV):APOBEC3B induced abundant G ¡ú A mutations in both wild-type and SIV reverse transcripts, exert efficient antiretroviral effects in infected target cells. "	AF-Q9UH17-F1	"Exhibits antiviral activity against simian immunodeficiency virus (SIV), hepatitis B virus (HBV) and human T-cell leukemia virus type 1 (HTLV-1)."	No modifications on the sequence.	22457529##15466872	"Ooms M, Krikoni A, Kress AK, Simon V, M¨¹nk C. ##Yu Q, Chen D, K?nig R, Mariani R, Unutmaz D, Landau NR. "	"APOBEC3A, APOBEC3B, and APOBEC3H haplotype 2 restrict human T-lymphotropic virus type 1.##APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication."
DRAVPR0029	MNPQIRNPMKAMYPGTFYFQFKNLWEANDRNETWLCFTVEGIKRRSVVSWKTGVFRNQVDSETHCHAERCFLSWFCDDILSPNTKYQVTWYTSWSPCPDCAGEVAEFLARHSNVNLTIFTARLYYFQYPCYQEGLRSLSQEGVAVEIMDYEDFKYCWENFVYNDNEPFKPWKGLKTNFRLLKRRLRESLQ	190	DNA dC->dU-editing enzyme APOBEC-3C	Homo sapiens (Human)	Q9NRW3	APOBEC3C	3VM8##3VOW	"SIV,HSV-1,EBV"	[Ref.15466872]simian immunodeficiency virus(SIV):APOBEC3C have potent antiviral activity against simian immuno-deficiency virus (SIV).##[Ref.21632763]Herpes simplex virus 1(HSV-1):APOBEC3C restricts the replication of HSV-1;##Epstein-Barr virus (EBV):APOBEC3C restricts the replication of EBV.	AF-Q9NRW3-F1	"Exhibits antiviral activity against simian immunodeficiency virus (SIV), herpes simplex virus 1 (HSV-1) and Epstein-Barr virus (EBV)."	No modifications on the sequence.	15466872##21632763	"Yu Q, Chen D, K?nig R, Mariani R, Unutmaz D, Landau NR. ##Susp¨¨ne R, Aynaud MM, Koch S, Pasdeloup D, Labetoulle M, Gaertner B, Vartanian JP, Meyerhans A, Wain-Hobson S. "	APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication.##Genetic editing of herpes simplex virus 1 and Epstein-Barr herpesvirus genomes by human APOBEC3 cytidine deaminases in culture and in vivo.
DRAVPR0030	MNPQIRNPMERMYRDTFYDNFENEPILYGRSYTWLCYEVKIKRGRSNLLWDTGVFRGPVLPKRQSNHRQEVYFRFENHAEMCFLSWFCGNRLPANRRFQITWFVSWNPCLPCVVKVTKFLAEHPNVTLTISAARLYYYRDRDWRWVLLRLHKAGARVKIMDYEDFAYCWENFVCNEGQPFMPWYKFDDNYASLHRTLKEILRNPMEAMYPHIFYFHFKNLLKACGRNESWLCFTMEVTKHHSAVFRKRGVFRNQVDPETHCHAERCFLSWFCDDILSPNTNYEVTWYTSWSPCPECAGEVAEFLARHSNVNLTIFTARLCYFWDTDYQEGLCSLSQEGASVKIMGYKDFVSCWKNFVYSDDEPFKPWKGLQTNFRLLKRRLREILQ	386	DNA dC->dU-editing enzyme APOBEC-3D	Homo sapiens (Human)	Q96AK3	APOBEC3D 	None	HIV-1	"[Ref.16920826]Human immunodeficiency virus type 1 (HIV-1):after the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA"	AF-Q96AK3-F1	APOBEC3D blocked the replication of both HIV-1 and SIV but not that of MLV.	No modifications on the sequence.	16920826	"Dang Y, Wang X, Esselman WJ, Zheng YH."	Identification of APOBEC3DE as another antiretroviral factor from the human APOBEC family. 
DRAVPR0031	MKPHFRNTVERMYRDTFSYNFYNRPILSRRNTVWLCYEVKTKGPSRPRLDAKIFRGQVYSQPEHHAEMCFLSWFCGNQLPAYKCFQITWFVSWTPCPDCVAKLAEFLAEHPNVTLTISAARLYYYWERDYRRALCRLSQAGARVKIMDDEEFAYCWENFVYSEGQPFMPWYKFDDNYAFLHRTLKEILRNPMEAMYPHIFYFHFKNLRKAYGRNESWLCFTMEVVKHHSPVSWKRGVFRNQVDPETHCHAERCFLSWFCDDILSPNTNYEVTWYTSWSPCPECAGEVAEFLARHSNVNLTIFTARLYYFWDTDYQEGLRSLSQEGASVEIMGYKDFKYCWENFVYNDDEPFKPWKGLKYNFLFLDSKLQEILE	373	DNA dC->dU-editing enzyme APOBEC-3F	Homo sapiens (Human)	Q8IUX4	APOBEC3F	3WUS##4IOU##4J4J##5HX4##5HX5##5W2M##5ZVA##5ZVB##6NIL	"HIV-1,XMRV"	"[Ref.15141007]Human immunodeficiency virus type 1(HIV-1):APOBEC3F induced G to A hypermutations in HIV genomic DNA at the step of reverse transcription in target cells and thus inhibited the replication of HIV-1.##[Ref.20335265]Xenotropic murine leukemia virus-related virus (XMRV):the expression of APOBEC3F in virus-producing cells resulted in their virion incorporation, inhibition of XMRV replication, and G-to-A hypermutation of the viral DNA."	AF-Q8IUX4-F1	"Exhibits antiviral activity also against hepatitis B virus (HBV), equine infectious anemia virus (EIAV), xenotropic MuLV-related virus (XMRV) and simian foamy virus (SFV)."	There is a disulfide bond between Cys280 and Cys283.	15141007##20335265	"Zheng YH, Irwin D, Kurosu T, Tokunaga K, Sata T, Peterlin BM.##Paprotka T, Venkatachari NJ, Chaipan C, Burdick R, Delviks-Frankenberry KA, Hu WS, Pathak VK. "	Human APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replication.##Inhibition of xenotropic murine leukemia virus-related virus by APOBEC3 proteins and antiviral drugs. 
DRAVPR0032	MKPHFRNTVERMYRDTFSYNFYNRPILSRRNTVWLCYEVKTKGPSRPPLDAKIFRGQVYSELKYHPEMRFFHWFSKWRKLHRDQEYEVTWYISWSPCTKCTRDMATFLAEDPKVTLTIFVARLYYFWDPDYQEALRSLCQKRDGPRATMKIMNYDEFQHCWSKFVYSQRELFEPWNNLPKYYILLHIMLGEILRHSMDPPTFTFNFNNEPWVRGRHETYLCYEVERMHNDTWVLLNQRRGFLCNQAPHKHGFLEGRHAELCFLDVIPFWKLDLDQDYRVTCFTSWSPCFSCAQEMAKFISKNKHVSLCIFTARIYDDQGRCQEGLRTLAEAGAKISIMTYSEFKHCWDTFVDHQGCPFQPWDGLDEHSQDLSGRLRAILQNQEN	384	DNA dC->dU-editing enzyme APOBEC-3G	Homo sapiens (Human)	Q9HC16	APOBEC3G	"2JYW##	2KBO##	2KEM##3E1U##3IQS##3IR2##3V4J##3V4K##4ROV##4ROW##5ZVA##5ZVB##6BUX##6BWY##6K3J##6K3K"	"HIV-1,HBV"	[Ref.15031497]Hepatitis B virus(HBV):The block of HBV DNA accumulation by APOBEC3G thus seems to result primarily from an inhibition of viral pregenomic RNA packaging.	AF-Q9HC16-F1	"Exhibits antiviral activity also against simian immunodeficiency viruses (SIVs), hepatitis B virus (HBV), equine infectious anemia virus (EIAV), xenotropic MuLV-related virus (XMRV) and simian foamy virus (SFV)."	"Phosphorylation of Thr at position 32,218"	12808466##15031497	"Mangeat B, Turelli P, Caron G, Friedli M, Perrin L, Trono D.##Turelli P, Mangeat B, Jost S, Vianin S, Trono D."	Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts.##Inhibition of hepatitis B virus replication by APOBEC3G.
DRAVPR0033	MKPHFRNPVERMYQDTFSDNFYNRPILSHRNTVWLCYEVKTKGPSRPPLDAKIFRGQVYSKLKYHPEMRFFHWFSKWRKLHRDQEYEVTWYISWSPCTKCTRDVATFLAEDPKVTLTIFVARLYYFWDPDYQEALRSLCQKRDGPRATMKIMNYDEFQHCWSKFVYSQRELFEPWNNLPKYYILLHIMLGEILRHSMDPPTFTSNFNNELWVRGRHETYLCYEVERLHNDTWVLLNQRRGFLCNQAPHKHGFLEGRHAELCFLDVIPFWKLDLHQDYRVTCFTSWSPCFSCAQEMAKFISNNKHVSLCIFAARIYDDQGRCQEGLRTLAKAGAKISIMTYSEFKHCWDTFVDHQGCPFQPWDGLEEHSQALSGRLRAILQNQGN	384	DNA dC->dU-editing enzyme APOBEC-3G	Pan troglodytes (Chimpanzee)	Q7YR24	APOBEC3G	None	"HIV-1,SFV"	"[Ref.12859895]Human immunodeficiency virus type 1(HIV-1):APOBEC3G can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells.##[Ref.16378963]simian foamy virus (SFV):inhibition of the replication of SFV."	AF-Q7YR24-F1	Exhibits antiviral activity against vif-deficient: HIV-1 and simian immunodeficiency viruses (SIVs) and also against simian foamy virus (SFV). 	"Phosphorylation of Thr at position 32,218."	12859895##16378963	"Mariani R, Chen D, Schr?felbauer B, Navarro F, K?nig R, Bollman B, M¨¹nk C, Nymark-McMahon H, Landau NR. ##Delebecque F, Susp¨¨ne R, Calattini S, Casartelli N, Sa?b A, Froment A, Wain-Hobson S, Gessain A, Vartanian JP, Schwartz O."	Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif.##Restriction of foamy viruses by APOBEC cytidine deaminases.
DRAVPR0034	MNPQIRNMVEQMEPDIFVYYFNNRPILSGRNTVWLCYEVKTKDPSGPPLDANIFQGKLYPEAKDHPEMKFLHWFRKWRQLHRDQEYEVTWYVSWSPCTRCANSVATFLAEDPKVTLTIFVARLYYFWKPDYQQALRILCQERGGPHATMKIMNYNEFQHCWNEFVDGQGKPFKPRKNLPKHYTLLHATLGELLRHVMDPGTFTSNFNNKPWVSGQRETYLCYKVERSHNDTWVLLNQHRGFLRNQAPDRHGFPKGRHAELCFLDLIPFWKLDDQQYRVTCFTSWSPCFSCAQKMAKFISNNKHVSLCIFAARIYDDQGRCQEGLRTLHRDGAKIAVMNYSEFEYCWDTFVDRQGRPFQPWDGLDEHSQALSGRLRAI	377	DNA dC->dU-editing enzyme APOBEC-3G	Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops)	Q7YR25	APOBEC3G	None	"HIV-1,SFV"	"[Ref.12859895]Human immunodeficiency virus type 1(HIV-1):APOBEC3G can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells.##[Ref.16378963]simian foamy virus (SFV):inhibition of the replication of SFV."	No predicted structure information available for the entry	Exhibits antiviral activity against vif-deficient: HIV-1 and simian immunodeficiency viruses (SIVs) and also against simian foamy virus (SFV). 	"Phosphorylation of Thr at position 32,218."	12859895##16378963	"Mariani R, Chen D, Schr?felbauer B, Navarro F, K?nig R, Bollman B, M¨¹nk C, Nymark-McMahon H, Landau NR. ##Delebecque F, Susp¨¨ne R, Calattini S, Casartelli N, Sa?b A, Froment A, Wain-Hobson S, Gessain A, Vartanian JP, Schwartz O."	Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif.##Restriction of foamy viruses by APOBEC cytidine deaminases.
DRAVPR0035	MALLTAETFRLQFNNKRRLRRPYYPRKALLCYQLTPQNGSTPTRGYFENKKKCHAEICFINEIKSMGLDETQCYQVTCYLTWSPCSSCAWELVDFIKAHDHLNLGIFASRLYYHWCKPQQKGLRLLCGSQVPVEVMGFPEFADCWENFVDHEKPLSFNPYKMLEELDKNSRAIKRRLERIKIPGVRAQGRYMDILCDAEV	200	DNA dC->dU-editing enzyme APOBEC-3H	Homo sapiens (Human)	Q6NTF7	APOBEC3H	"5W45##6B0B##	6BBO"	"HTLV-1,HIV-1"	[Ref.22457529]Human T-lymphotropic virus type 1(HTLV-1):APOBEC3H hapII potently decrease HTLV-1 infectivity.##[Ref.18299330]Human immunodeficiency virus type 1 (HIV-1):APOBEC3H inhibits HIV-1 replication potently by a cytidine deamination-independent mechanism.	AF-Q6NTF7-F1	"APOBEC3H blocked replication of both HIV-1 and SIV. Moreover, its antiretroviral activity was not countered by HIV-1 Vif."	No modifications on the sequence.	22457529##18299330	"Ooms M, Krikoni A, Kress AK, Simon V, M¨¹nk C.##Dang Y, Siew LM, Wang X, Han Y, Lampen R, Zheng YH."	"APOBEC3A, APOBEC3B, and APOBEC3H haplotype 2 restrict human T-lymphotropic virus type 1.##Human cytidine deaminase APOBEC3H restricts HIV-1 replication."
DRAVPR0036	MVEPMDPRTFVSNFNNRPILSGLNTVWLCCEVKTKDPSGPPLDAKIFQGKVYSKAKYHPEMRFLRWFHKWRQLHHDQEYKVTWYVSWSPCTRCANSVATFLAKDPKVTLTIFVARLYYFWKPDYQQALRILCQKRGGPHATMKIMNYNEFQDCWNKFVDGRGKPFKPRNNLPKHYTLLQATLGELLRHLMDPGTFTSNFNNKPWVSGQHETYLCYKVERLHNDTWVPLNQHRGFLRNQAPNIHGFPKGRHAELCFLDLIPFWKLDGQQYRVTCFTSWSPCFSCAQEMAKFISNNEHVSLCIFAARIYDDQGRYQEGLRALHRDGAKIAMMNYSEFEYCWDTFVDRQGRPFQPWDGLDEHSQALSGRLRAI	370	DNA dC->dU-editing enzyme APOBEC-3G	Macaca mulatta (Rhesus macaque)	Q7YR23	APOBEC3G	None	HIV-1	"[Ref.21835787]Human immunodeficiency virus type 1 (HIV-1):the protein expressed in CD4 T lymphocytes, are packaged into and restrict Vif-deficient HIV-1 when stably expressed in T cells, mutate proviral DNA, and are counteracted by HIV-1 Vif. "	No predicted structure information available for the entry	Exhibits antiviral activity against vif-deficient: HIV-1 and simian immunodeficiency viruses (SIVs).	"Phosphorylation of Thr at position 25,211"	12859895##21835787	"Mangeat B, Turelli P, Caron G, Friedli M, Perrin L, Trono D.##Hultquist JF, Lengyel JA, Refsland EW, LaRue RS, Lackey L, Brown WL, Harris RS."	"Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts.##Human and rhesus APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H demonstrate a conserved capacity to restrict Vif-deficient HIV-1. "
DRAVPR0037	MALLTAKTFSLQFNNKRRVNKPYYPRKALLCYQLTPQNGSTPTRGHLKNKKKDHAEIRFINKIKSMGLDETQCYQVTCYLTWSPCPSCAGELVDFIKAHRHLNLRIFASRLYYHWRPNYQEGLLLLCGSQVPVEVMGLPEFTDCWENFVDHKEPPSFNPSEKLEELDKNSQAIKRRLERIKSRSVDVLENGLRSLQLGPVTPSSSIRNSR	210	DNA dC->dU-editing enzyme APOBEC-3H	Macaca mulatta (Rhesus macaque)	Q19Q52	APOBEC3H	None	HIV-1	"[Ref.21835787]Human immunodeficiency virus type 1 (HIV-1):the protein expressed in CD4 T lymphocytes, are packaged into and restrict Vif-deficient HIV-1 when stably expressed in T cells, mutate proviral DNA."	AF-Q19Q52-F1	Exhibits antiviral activity against vif-deficient: HIV-1 and simian immunodeficiency viruses (SIV).	No modifications on the sequence.	21835787	"Hultquist JF, Lengyel JA, Refsland EW, LaRue RS, Lackey L, Brown WL, Harris RS."	"Human and rhesus APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H demonstrate a conserved capacity to restrict Vif-deficient HIV-1."
DRAVPR0038	MQPQRLGPRAGMGPFCLGCSHRKCYSPIRNLISQETFKFHFKNLGYAKGRKDTFLCYEVTRKDCDSPVSLHHGVFKNKDNIHAEICFLYWFHDKVLKVLSPREEFKITWYMSWSPCFECAEQIVRFLATHHNLSLDIFSSRLYNVQDPETQQNLCRLVQEGAQVAAMDLYEFKKCWKKFVDNGGRRFRPWKRLLTNFRYQDSKLQEILRPCYISVPSSSSSTLSNICLTKGLPETRFWVEGRRMDPLSEEEFYSQFYNQRVKHLCYYHRMKPYLCYQLEQFNGQAPLKGCLLSEKGKQHAEILFLDKIRSMELSQVTITCYLTWSPCPNCAWQLAAFKRDRPDLILHIYTSRLYFHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTNFVNPKRPFWPWKGLEIISRRTQRRLRRIKESWGLQDLVNDFGNLQLGPPMS	440	DNA dC->dU-editing enzyme APOBEC-3	Mus musculus (Mouse)	Q99J72	Apobec3	None	"MMTV,FrMLV"	[Ref.17259974]mouse mammary tumour virus(MMTV):APOBEC3 inhibits mouse mammary tumour virus replication.##[Ref.18786991]friend leukemia virus(FrMLV):Mouse APOBEC3 restricts friend leukemia virus infection in vivo.	AF-Q99J72-F1	"TRIM52 is a RING-type E3 ligase, the RING domain of TRIM52 is required for TRIM52 to control JEV replication.TRIM22 is endowed with a potent capacity to repress various viral infections, including HIV, HBV, EMCV, and IAV."	No modifications on the sequence.	17259974##18786991	"Okeoma CM, Lovsin N, Peterlin BM, Ross SR.##Takeda E, Tsuji-Kawahara S, Sakamoto M, Langlois MA, Neuberger MS, Rada C, Miyazawa M. "	APOBEC3 inhibits mouse mammary tumour virus replication in vivo.?##Mouse APOBEC3 restricts friend leukemia virus infection and pathogenesis in vivo.
DRAVPR0039	MAGYATTPSPMQTLQEEAVCAICLDYFKDPVSISCGHNFCRGCVTQLWSKEDEEDQNEEEDEWEEEEDEEAVGAMDGWDGSIREVLYRGNADEELFQDQDDDELWLGDSGITNWDNVDYMWDEEEEEEEEDQDYYLGGLRPDLRIDVYREEEILEAYDEDEDEELYPDIHPPPSLPLPGQFTCPQCRKSFTRRSFRPNLQLANMVQIIRQMCPTPYRGNRSNDQGMCFKHQEALKLFCEVDKEAICVVCRESRSHKQHSVLPLEEVVQEYQEIKLETTLVGILQIEQESIHSKAYNQ	297	E3 ubiquitin-protein ligase TRIM52	Homo sapiens (Human)	Q96A61	TRIM52	None	JEV	"[Ref.27667714]Japanese encephalitis virus (JEV):TRIM52 interacted with NS2A and induced NS2A ubiquitination, resulting in NS2A degradation. "	AF-Q96A61-F1	"Active against multiple viruses, including influenza A virus, SARS coronavirus (SARS-CoV), Marburg virus (MARV), Ebola virus (EBOV), Dengue virus (DNV) and West Nile virus (WNV)."	No modifications on the sequence.	27667714	"Fan W, Wu M, Qian S, Zhou Y, Chen H, Li X, Qian P."	TRIM52 inhibits Japanese Encephalitis Virus replication by degrading the viral NS2A.
DRAVPR0040	MPKEQQEVVVLGSPHISTSATATTINMPEISTPDHVVWSLFNTLFMNFCCLGFVAYAYSVKSRDRKMVGDTTGAQAFASTAKCLNISSLFFTILTAIVVIVVCAIR	106	Interferon-induced transmembrane protein 1 	Mus musculus (Mouse)	Q9D103	Ifitm1 	None	MERS-CoV	[Ref.25256397]MERS-CoV:Expression of IFITM proteins in target cells inhibited entry driven by the S protein of MERS-CoV	AF-Q9D103-F1	"Active against multiple viruses, including influenza A virus, SARS coronavirus (SARS-CoV), Marburg virus (MARV) and Ebola virus (EBOV), Dengue virus (DNV) and West Nile virus (WNV)."	"The Cys at position 49,50,83 indicates S-palmitoyl cysteine."	25256397	"Wrensch F, Winkler M, P?hlmann S."	 IFITM proteins inhibit entry driven by the MERS-coronavirus spike protein: evidence for cholesterol-independent mechanisms.
DRAVPR0041	MSHNSQAFLSTNAGLPPSYETIKEEYGVTELGEPSNSAVVRTTVINMPREVSVPDHVVWSLFNTLFFNACCLGFVAYAYSVKSRDRKMVGDVVGAQAYASTAKCLNISSLIFSILMVIICIIIFSTTSVVVFQSFAQRTPHSGF	144	Interferon-induced transmembrane protein 2	Mus musculus (Mouse)	Q99J93	Ifitm2	None	"SARS-CoV,IAV,EBOV"	"[Ref.21253575]influenza A virus(IAV):Ifitm2 inhibits infection mediated by the influenza A virus (IAV) hemagglutinin (HA) protein.##SARS-CoV:IFITM proteins can restrict the replication of infectious SARS coronavirus (SARS-CoV) and entry mediated by the SARS-CoV spike (S) protein. ##Ebola virus(EBOV):IFITM proteins restricted infection mediated by the entry glycoproteins (GP1,2) of Ebola filoviruses."	AF-Q99J93-F1	"Active against multiple viruses, including influenza A virus, SARS coronaviruses (SARS-CoV and SARS-CoV-2), Marburg virus (MARV), Ebola virus (EBOV), Dengue virus (DNV), West Nile virus (WNV), human immunodeficiency virus type 1 (HIV-1), hepatitis C virus (HCV) and vesicular stomatitis virus (VSV) "	"¢ÙPhosphorylation of Ser at position 19.¢ÚThe Cys at position 70,71,104 indicates S-palmitoyl cysteine."	21253575	"Huang IC, Bailey CC, Weyer JL, Radoshitzky SR, Becker MM, Chiang JJ, Brass AL, Ahmed AA, Chi X, Dong L, Longobardi LE, Boltz D, Kuhn JH, Elledge SJ, Bavari S, Denison MR, Choe H, Farzan M. "	"Distinct patterns of IFITM-mediated restriction of filoviruses, SARS coronavirus, and influenza A virus."
DRAVPR0042	MNHTSQAFITAASGGQPPNYERIKEEYEVAEMGAPHGSASVRTTVINMPREVSVPDHVVWSLFNTLFMNFCCLGFIAYAYSVKSRDRKMVGDVTGAQAYASTAKCLNISTLVLSILMVVITIVSVIIIVLNAQNLHT	137	Interferon-induced transmembrane protein 3 	Mus musculus (Mouse)	Q9CQW9	Ifitm3	None	"SARS-CoV,IAV,EBOV,SARS-CoV-2"	"[Ref.21253575]influenza A virus(IAV):Ifitm3 inhibits infection mediated by the influenza A virus (IAV) hemagglutinin (HA) protein.##SARS-CoV:IFITM proteins can restrict the replication of infectious SARS coronavirus (SARS-CoV) and entry mediated by the SARS-CoV spike (S) protein. ##Ebola virus(EBOV):IFITM proteins restricted infection mediated by the entry glycoproteins (GP1,2) of Ebola filoviruses.##[Ref.33270927]SARS-CoV-2:IFITM3 likely restrict SARS©\CoV©\2 infection by mechanically disfavoring viral membrane fusion reactions occurring at endosomes."	AF-Q9CQW9-F1	VAMP8 plays an antiviral role in response to Japanese encephalitis virus (JEV).	"¢ÙPhosphorylation of Ser at position 20,27.¢ÚThe Cys at position 71,72,105 indicates S-palmitoyl cysteine."	21253575##33270927	"Huang IC, Bailey CC, Weyer JL, Radoshitzky SR, Becker MM, Chiang JJ, Brass AL, Ahmed AA, Chi X, Dong L, Longobardi LE, Boltz D, Kuhn JH, Elledge SJ, Bavari S, Denison MR, Choe H, Farzan M. ##Shi G, Kenney AD, Kudryashova E, Zani A, Zhang L, Lai KK, Hall-Stoodley L, Robinson RT, Kudryashov DS, Compton AA, Yount JS."	"Distinct patterns of IFITM-mediated restriction of filoviruses, SARS coronavirus, and influenza A virus.##Opposing activities of IFITM proteins in SARS-CoV-2 infection."
DRAVPR0043	MEEASEGGGNDRVRNLQSEVEGVKNIMTQNVERILARGENLEHLRNKTEDLEATSEHFKTTSQKVARKFWWKNVKMIVLICVIVFIIILFIVLFATGAFS	100	Vesicle-associated membrane protein 8	Homo sapiens (Human)	Q9BV40	VAMP8 	4WY4##7BV6	WNV	[Ref.31694946]West Nile virus(WNV):VAMP8 contributes to the TRIM6-mediated type I interferon antiviral response during west nile virus infection.	AF-Q9BV40-F1	"Cyclophilin A regulates the life cycle of several viruses including human immunodeficiency virus type 1, vesicular stomatitis virus, vaccinia virus (VV), hepatitis C virus"	"¢ÙPhosphorylation of Ser at position 5,18,55.¢ÚThe N-terminal is acetylation.¢ÛPhosphorylation of Thr at position 28,48,54."	31694946	"van Tol S, Atkins C, Bharaj P, Johnson KN, Hage A, Freiberg AN, Rajsbaum R. "	VAMP8 Contributes to the TRIM6-Mediated Type I Interferon Antiviral Response during West Nile Virus Infection.
DRAVPR0044	MVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIADCGQLE	165	Peptidyl-prolyl cis-trans isomerase A(Cyclophilin A)	Homo sapiens (Human)	P62937	PPIA	1AWQ##1BCK##1CWF##1M9X##1W8M##2CPL##3K0M##4N1M##4YUO	"IAV,HIV-1"	"[Ref.19207730]influenza A virus(IAV):cyclophilin A interacts with M1 protein and impairs the early stage of the vial replication.##Human immunodeficiency virus type 1(HIV-1):Cyclophilin A interacts with the Gag protein of HIV-1 by the CA domain and then is incorporated into HIV-1 virion, influencing the infectivity of HIV-1 virions."	AF-P62937-F1	No comments found in the entry	"¢ÙPhosphorylation of Ser at position 77.¢ÚThe N-terminal is acetylation.¢ÛPhosphorylation of Thr at position 93.¢ÜThe Lys at position 28,44,76,82,125,131,133 indicates N6-acetyllysine."	19207730	"Liu X, Sun L, Yu M, Wang Z, Xu C, Xue Q, Zhang K, Ye X, Kitamura Y, Liu W."	Cyclophilin A interacts with influenza A virus M1 protein and impairs the early stage of the viral replication.
DRAVPR0045	MSKLRNLLPTIFGGKEAQNPTPVEGRLEKDAAPVDDNEPDNNNSGALALPSTAGTPTASSDLTESVLRELSDPNYNSMDVVHSANIPGTLSNVQTNNTMNVHSAQQQVVMNFSNANNLHFGSVYNFNQNLSACSSRKGSTSTAEESVASPDGKPRASATRKTVSIVAMMQSQEEPDVRLLDVVSTHLGEGWKQVMRDLGMSEGQIDQAIIDHQMHGNIREVIYQLLLQWIRSSADGVATVGRLTTLLWESQHRDCVQRMKLVWKALEKRKTNS	273	Protein immune deficiency 	Drosophila melanogaster (Fruit fly)	Q7K4Z4	imd	None	SV	[Ref.19763182]Sindbis virus(SV):Imd pathway mediates an antiviral response to Sindbis virus replication.	AF-Q7K4Z4-F1	No comments found in the entry	No modifications on the sequence.	19763182	"Avadhanula V, Weasner BP, Hardy GG, Kumar JP, Hardy RW. "	A novel system for the launch of alphavirus RNA synthesis reveals a role for the Imd pathway in arthropod antiviral response.
DRAVPR0046	MVHRQLPETVLLLLVSSTIFSLEPKRIPFQLWMNRESLQLLKPLPSSSVQQCLAHRKNFLLPQQPVSPHQYQEGQVLAVVHEILQQIFTLLQTHGTMGIWEENHIEKVLAALHRQLEYVESLGGLNAAQKSGGSSAQNLRLQIKAYFRRIHDYLENQRYSSCAWIIVQTEIHRCMFFVFRFTTWLSRQDPDP	192	Interferon epsilon	Mus musculus (Mouse)	Q80ZF2	Ifne	None	HSV-2	[Ref.23449591]Herpes simplex virus 2(HSV-2):Interferon-¦Å directly protects  from viral infection.	AF-Q80ZF2-F1	"IL-17A was implicated in priming T cell responses during lymphocytic choriomeningitis virus (LCMV) hepatitis and mediating the immunopathogenicity of viral infections, such as influenza virus, respiratory syncytial virus, murine encephalomyelitis virus, and hepatitis B virus infections."	There is a disulfide bond between Cys52 and Cys162.	23449591	"Fung KY, Mangan NE, Cumming H, Horvat JC, Mayall JR, Stifter SA, De Weerd N, Roisman LC, Rossjohn J, Robertson SA, Schjenken JE, Parker B, Gargett CE, Nguyen HP, Carr DJ, Hansbro PM, Hertzog PJ. "	Interferon-¦Å protects the female reproductive tract from viral and bacterial infection.
DRAVPR0047	MSPGRASSVSLMLLLLLSLAATVKAAAIIPQSSACPNTEAKDFLQNVKVNLKVFNSLGAKVSSRRPSDYLNRSTSPWTLHRNEDPDRYPSVIWEAQCRHQRCVNAEGKLDHHMNSVLIQQEILVLKREPESCPFTFRVEKMLVGVGCTCVASIVRQAA	158	Interleukin-17A(IL-17)	Mus musculus (Mouse)	Q62386	Il17a	None	"H5N1,WNV"	[Ref.21946434]H5N1:IL17A may play a beneficial role in influenza A virus (H5N1) infection by enhancing B cell recruitment and immune response in the lung.##[Ref.27795421]West Nile virus(WNV):IL17A promotes CD8+ T cell cytotoxicity to facilitate west nile virus clearance.	AF-Q62386-F1	"Viperin contains an N-terminal amphipathic ¦Á-helix that localizes to the cytosolic face of the ER and inhibits bulk protein secretion (22), which could impact virus production directly or indirectly. Viperin also inhibits farnesyl diphosphate synthetase, a cholesterol and isoprenoid biosynthesis enzyme, resulting in the inhibition of lipid raft formation and influenza virus budding"	"¢ÙGlycosylation of Asn at position 71.¢ÚThere are two disulfide bonds between Cys97 and Cys147, Cys102 and Cys149."	21946434##27795421	"Wang X, Chan CC, Yang M, Deng J, Poon VK, Leung VH, Ko KH, Zhou J, Yuen KY, Zheng BJ, Lu L.##Acharya D, Wang P, Paul AM, Dai J, Gate D, Lowery JE, Stokic DS, Leis AA, Flavell RA, Town T, Fikrig E, Bai F. "	A critical role of IL-17 in modulating the B-cell response during H5N1 influenza virus infection.##Interleukin-17A Promotes CD8+ T Cell Cytotoxicity To Facilitate West Nile Virus Clearance. 
DRAVPR0048	MGMLVPTALAARLLSLFQQQLGSLWSGLAILFCWLRIALGWLDPGKEQPQVRGEPEDTQETQEDGNSTQPTTPVSVNYHFTRQCNYKCGFCFHTAKTSFVLPLEEAKRGLLLLKQAGLEKINFSGGEPFLQDRGEYLGKLVRFCKEELALPSVSIVSNGSLIRERWFKDYGEYLDILAISCDSFDEQVNALIGRGQGKKNHVENLQKLRRWCRDYKVAFKINSVINRFNVDEDMNEHIKALSPVRWKVFQCLLIEGENSGEDALREAERFLISNEEFETFLERHKEVSCLVPESNQKMKDSYLILDEYMRFLNCTGGRKDPSKSILDVGVEEAIKFSGFDEKMFLKRGGKYVWSKADLKLDW	362	Radical S-adenosyl methionine domain-containing protein 2(Viperin)	Mus musculus (Mouse)	Q8CBB9	Rsad2	5VSL##5VSM##6Q2P##6Q2Q	"WNV,SBV"	"[Ref.21880757]West Nile virus(WNV):viperin contributes to the antiviral responses against WNV in vivo, as the targeted deletion of viperin was associated with increased lethality and selectively enhanced replication in specific tissues.##[Ref.17686841]Sindbis virus (SBV):viperin exhibited modest replication inhibition of sindbis virus in vitro."	AF-Q8CBB9-F1	"Viperin, a member of the radical S-adenosyl-L-methionine (SAM) superfamily of enzymes, implicated in inhibiting the replication of a remarkable range of RNA and DNA viruses, including dengue virus, West Nile virus, hepatitis C virus, influenza A virus, rabies virus2 and HIV.Viperin suppresses the replication of influenza A and HIV-1 by blocking the release of viral particles, interacts with the RC of HCV and DENV to inhibit viral replication by binding with the nonstructural HCV protein NS5A and the DENV NS3 protein"	The Lys at position 198 idnicates N6-acetyllysine.	17686841##21880757	"Zhang Y, Burke CW, Ryman KD, Klimstra WB.##Szretter KJ, Brien JD, Thackray LB, Virgin HW, Cresswell P, Diamond MS."	Identification and characterization of interferon-induced proteins that inhibit alphavirus replication.##The interferon-inducible gene viperin restricts West Nile virus pathogenesis.
DRAVPR0049	MWVLTPAAFAGKLLSVFRQPLSSLWRSLVPLFCWLRATFWLLATKRRKQQLVLRGPDETKEEEEDPPLPTTPTSVNYHFTRQCNYKCGFCFHTAKTSFVLPLEEAKRGLLLLKEAGMEKINFSGGEPFLQDRGEYLGKLVRFCKVELRLPSVSIVSNGSLIRERWFQNYGEYLDILAISCDSFDEEVNVLIGRGQGKKNHVENLQKLRRWCRDYRVAFKINSVINRFNVEEDMTEQIKALNPVRWKVFQCLLIEGENCGEDALREAERFVIGDEEFERFLERHKEVSCLVPESNQKMKDSYLILDEYMRFLNCRKGRKDPSKSILDVGVEEAIKFSGFDEKMFLKRGGKYIWSKADLKLDW	361	Radical S-adenosyl methionine domain-containing protein 2(Viperin)	Homo sapiens (Human)	Q8WXG1	RSAD2	None	"ZIKV,WNV,DENV,HCV,EVA71,HSV-1"	"[Ref.29925952]Zika virus(ZIKV)/west nile virus(WNV)/dengue virus (DENV)/hepatitis C virus(HCV):viperin catalyzes the conversion of cytidine triphosphate (CTP) to 3¡ä-deoxy-3¡ä,4¡ä-didehydro-CTP (ddhCTP),and inhibits in vivo replication of ZIKA virus.##[Ref.30587778]Enterovirus A71 (EVA71):amino acids 50¨C60 in the N-terminal domain of viperin were the key residues responsible for viperin interaction with 2C, the N-terminal domain of viperin was found responsible for inhibiting EVA71 replication.##[Ref.31921110]Herpes Simplex Virus 1(HSV-1):gD(Glycoprotein D) of HSV-1 and viperin interaction inhibits HSV-1 replication."	No predicted structure information available for the entry	The SAM and N-terminal viperin domains were most important for CSFV and PEDV inhibition.	The Lys at position 197 idnicates N6-acetyllysine.	29925952##30587778##31921110	"Gizzi AS, Grove TL, Arnold JJ, Jose J, Jangra RK, Garforth SJ, Du Q, Cahill SM, Dulyaninova NG, Love JD, Chandran K, Bresnick AR, Cameron CE, Almo SC.##Wei C, Zheng C, Sun J, Luo D, Tang Y, Zhang Y, Ke X, Liu Y, Zheng Z, Wang H. ##Li M, Liao Z, Xu Z, Zou X, Wang Y, Peng H, Li Y, Ou X, Deng Y, Guo Y, Gan W, Peng T, Chen D, Cai M. "	A naturally occurring antiviral ribonucleotide encoded by the human genome.?##Viperin Inhibits Enterovirus A71 Replication by Interacting with Viral 2C Protein.##The Interaction Mechanism Between Herpes Simplex Virus 1 Glycoprotein D and Host Antiviral Protein Viperin. 
DRAVPR0050	MWTLVPVTFALRLLSTFVQPLGSLGSSLGPLFLWLWAAFWRAGGDRSRQQLQGKTEAGEPPRAQEDSHLPTTPTSVNYHFTRQCNYKCGFCFHTAKTSFVLPLEEAKRGLWLLKEAGMEKINFSGGEPFIHDRGEYLGKLVRFCKEELQLPSVSIVSNGSLIWERWFKSYGEYLDILAISCDSFDEQVNVLIGRGQGKKNHVENLQKLRTWCRDYKVAFKINSVINRFNVEEDMTEHIKALNPVRWKVFQCLLIEGENVGEDALREAEQFVISDEEFEEFLDRHKDVSCLVPESNRQMRDSYLILDEYMRFLNCRNGRKDPSKSILDVGVEKAIKFSGFDEKMFLKRGGKYVWSKADLKLDW	362	Radical S-adenosyl methionine domain-containing protein 2	Sus scrofa (Pig)	Q9MZU4	RSAD2 	None	"PEDV,CSFV"	[Ref.32719955]Porcine epidemic diarrhea virus(PEDV):The interaction of the viperin S-adenosylmethionine domain with the N protein of PEDV might interfere with viral replication or assembly to reduce virus proliferation.##[Ref.31517388]Classical swine fever virus (CSFV):Viperin inhibits the replication of CSFV by interacting with viral nonstructural 5A protein.	AF-Q9MZU4-F1	No comments found in the entry	The Lys at position 198 idnicates N6-acetyllysine.	32719955##31517388	"Wu J, Chi H, Fu Y, Cao A, Shi J, Zhu M, Zhang L, Hua D, Huang J.##Xu C, Feng L, Chen P, Li A, Guo S, Jiao X, Zhang C, Zhao Y, Jin X, Zhong K, Guo Y, Zhu H, Han L, Yang G, Li H, Wang Y."	The antiviral protein viperin interacts with the viral N protein to inhibit proliferation of porcine epidemic diarrhea virus.##Viperin inhibits classical swine fever virus replication by interacting with viral nonstructural 5A protein.
DRAVPR0051	LGKFSQTCYNSAIQGSVLTSTCERTNGGYNTSSIDLNSVIENVDGSLKWQPSNFIETCRNTQLAGSSELAAECKTRAQQFVSTKINLDDHIANIDGTLKYE	101	Cyanovirin-N	Nostoc ellipsosporum	P81180	N/A	1LOM##2RDK##3CZZ##4J4C##6X7H	HIV	[Ref.20162270]Human immunodeficiency virus(HIV):CVN is effective against most HIV strains with an EC50 of less than 1 nM.	AF-P81180-F1	"Elevated cellular levels of human BST-2 inhibited the release of virus-like particles (VLPs) consisting of the matrix proteins of multiple highly virulent NIAID Priority Pathogens, including arenaviruses (LASV and Machupo virus [MACV]), filoviruses (ZEBOV and MARV), and paramyxoviruses (Nipah virus). However, filoviruses, RVFV, and CPXV are immune to the inhibitory effect of BST-2."	"There are two disulfide bonds between Cys8 and Cys22, Cys58 and Cys73."	20162270	"Xiong S, Fan J, Kitazato K."	The antiviral protein cyanovirin-N: the current state of its production and applications.
DRAVPR0052	MASTSYDYCRVPMEDGDKRCKLLLGIGILVLLIIVILGVPLIIFTIKANSEACRDGLRAVMECRNVTHLLQQELTEAQKGFQDVEAQAATCNHTVMALMASLDAEKAQGQKKVEELEGEITTLNHKLQDASAEVERLRRENQVLSVRIADKKYYPSSQDSSSAAAPQLLIVLLGLSALLQ	180	Bone marrow stromal antigen 2(Tetherin)	Homo sapiens (Human)	Q10589	BST2	2LK9##2X7A##2XG7##3MQ7##3MQ9##4P6Z##6CM9	"SARS-CoV,HCoV©\229E,HIV-1,LASV, MACV, ZEBOV, MARV, NiV"	"[Ref.31199522]SARS-CoV/HCoV©\229E:BST2 is capable of inhibiting SARS©\CoV and HCoV©\229E VLP release.##[Ref.18342597]Human immunodeficiency virus 1(HIV-1):BST-2 inhibits the release of virions from cells.##[Ref.20686043]Zaire ebolavirus (ZEBOV)/Lake Victoria marburgvirus (MARV)/Lassa virus (LASV)/Machupo virus(MACV)/paramyxoviral (NiV):BST-2 inhibits the release of a variety of VLPs, generated by the expression of arenaviral (LASV and MACV), filoviral (ZEBOV and MARV), or paramyxoviral (NiV) matrix proteins."	AF-Q10589-F1	No comments found in the entry	"Glycosylation of Asn at position 65,92."	31199522##18342597##20686043	"Wang SM, Huang KJ, Wang CT.##Van Damme N, Goff D, Katsura C, Jorgenson RL, Mitchell R, Johnson MC, Stephens EB, Guatelli J.##Radoshitzky SR, Dong L, Chi X, Clester JC, Retterer C, Spurgers K, Kuhn JH, Sandwick S, Ruthel G, Kota K, Boltz D, Warren T, Kranzusch PJ, Whelan SP, Bavari S."	"Severe acute respiratory syndrome coronavirus spike protein counteracts BST2-mediated restriction of virus-like particle release.?##The interferon-induced protein BST-2 restricts HIV-1 release and is downregulated from the cell surface by the viral Vpu protein.##Infectious Lassa virus, but not filoviruses, is restricted by BST-2/tetherin."
DRAVPR0053	MRGDRGRGRGGRFGSRGGPGGGFRPFVPHIPFDFYLCEMAFPRVKPAPDETSFSEALLKRNQDLAPNSAEQASILSLVTKINNVIDNLIVAPGTFEVQIEEVRQVGSYKKGTMTTGHNVADLVVILKILPTLEAVAALGNKVVESLRAQDPSEVLTMLTNETGFEISSSDATVKILITTVPPNLRKLDPELHLDIKVLQSALAAIRHARWFEENASQSTVKVLIRLLKDLRIRFPGFEPLTPWILDLLGHYAVMNNPTRQPLALNVAYRRCLQILAAGLFLPGSVGITDPCESGNFRVHTVMTLEQQDMVCYTAQTLVRILSHGGFRKILGQEGDASYLASEISTWDGVIVTPSEKAYEKPPEKKEGEEEEENTEEPPQGEEEESMETQE	390	Interleukin enhancer-binding factor 2	Homo sapiens (Human)	Q12905	ILF2 (NF45)	None	JEV	"[Ref.31212927]Japanese Encephalitis Virus(JEV):ILF2 interacts with JEV NS3, and involved in the JEV life cycle and inhibits JEV replication in 293T cells."	AF-Q12905-F1	"C19orf66 was suggested to be a novel ISG, the products of which can suppress DENV, WNV, hepatitis C virus (HCV) and Kunjin virus, Chikungunya virus, herpes simplex virus type 1, and human adenovirus replication in vitro."	"¢ÙPhosphorylation of Ser at position 52,68.¢ÚThe Arg at position 16,24 indicates Omega-N-methylarginine.¢ÛPhosphorylation of Thr at position 388."	31212927	"Cui X, Qian P, Rao T, Wei Y, Zhao F, Zhang H, Chen H, Li X. "	"Cellular Interleukin Enhancer-Binding Factor 2, ILF2, Inhibits Japanese Encephalitis Virus Replication In Vitro."
DRAVPR0054	MSQEGVELEKSVRRLREKFHGKVSSKKAGALMRKFGSDHTGVGRSIVYGVKQKDGQELSNDLDAQDPPEDMKQDRDIQAVATSLLPLTEANLRMFQRAQDDLIPAVDRQFACSSCDHVWWRRVPQRKEVSRCRKCRKRYEPVPADKMWGLAEFHCPKCRHNFRGWAQMGSPSPCYGCGFPVYPTRILPPRWDRDPDRRSTHTHSCSAADCYNRREPHVPGTSCAHPKSRKQNHLPKVLHPSNPHISSGSTVATCLSQGGLLEDLDNLILEDLKEEEEEEEEVEDEEGGPRE	291	Shiftless antiviral inhibitor of ribosomal frameshifting protein(RyDEN)	Homo sapiens (Human)	Q9NUL5	SHFL(C19orf66)	None	"ZIKV,DENV,HCV"	"[Ref.32150556]Zika virus(ZIKV):C19orf66 interacts and co-localizes with ZIKV nonstructural protein 3 (NS3), thus inducing NS3 degradation via a lysosome-dependent pathway and interrupts the replication of ZIKV.##[Ref.26735137]Dengue Virus(DENV):RyDEN is likely to interfere with the translation of DENV via interaction with viral RNA and cellular mRNA-binding proteins, resulting in the inhibition of virus replication in infected cells.##[Ref.32294532]Hepatitis C Virus(HCV):C19orf66 inhibits the replication of HCV by restricting formation of the viral replication organelle."	AF-Q9NUL5-F1	The expression of MARCH2 to be upregulated upon HIV-1 infection. MARCH2 inhibits the production and infection of HIV-1 through ligase activity-dependent envelope protein degradation and/or intracellular retention.	Acetylation of Ser at position 2(N-acetylserine)	32150556##26735137##32294532	"Wu Y, Yang X, Yao Z, Dong X, Zhang D, Hu Y, Zhang S, Lin J, Chen J, An S, Ye H, Zhang S, Qiu Z, He Z, Huang M, Wei G, Zhu X.##Suzuki Y, Chin WX, Han Q, Ichiyama K, Lee CH, Eyo ZW, Ebina H, Takahashi H, Takahashi C, Tan BH, Hishiki T, Ohba K, Matsuyama T, Koyanagi Y, Tan YJ, Sawasaki T, Chu JJ, Vasudevan SG, Sano K, Yamamoto N.##Kinast V, Plociennikowska A, Anggakusuma, Bracht T, Todt D, Brown RJP, Boldanova T, Zhang Y, Br¨¹ggemann Y, Friesland M, Engelmann M, Vieyres G, Broering R, Vondran FWR, Heim MH, Sitek B, Bartenschlager R, Pietschmann T, Steinmann E."	C19orf66 interrupts Zika virus replication by inducing lysosomal degradation of viral NS3.##Characterization of RyDEN (C19orf66) as an Interferon-Stimulated Cellular Inhibitor against Dengue Virus Replication.##C19orf66 is an interferon-induced inhibitor of HCV replication that restricts formation of the viral replication organelle. 
DRAVPR0055	MTTGDCCHLPGSLCDCSGSPAFSKVVEATGLGPPQYVAQVTSRDGRLLSTVIRALDTPSDGPFCRICHEGANGECLLSPCGCTGTLGAVHKSCLEKWLSSSNTSYCELCHTEFAVEKRPRPLTEWLKDPGPRTEKRTLCCDMVCFLFITPLAAISGWLCLRGAQDHLRLHSQLEAVGLIALTIALFTIYVLWTLVSFRYHCQLYSEWRKTNQKVRLKIREADSPEGPQHSPLAAGLLKKVAEETPV	246	E3 ubiquitin-protein ligase MARCHF2	Homo sapiens (Human)	Q9P0N8	MARCHF2?	None	HIV-1	[Ref.29573664]Human immunodeficiency virus type 1(HIV-1):MARCH2 decreased or increased the HIV-1 production in both the VSV-G- and Env-pseudo-typed HIV-1 production system. And it exerted its function by degrading VSV-G via the lysosome or by reducing the amount of Env on the plasma membrane.	No predicted structure information available for the entry	MARCH8 might display broad-spectrum activity against enveloped viruses.	No modifications on the sequence.	29573664	"Zhang Y, Lu J, Liu X. "	MARCH2 is upregulated in HIV-1 infection and inhibits HIV-1 production through envelope protein translocation or degradation.
DRAVPR0056	MSMPLHQISAIPSQDAISARVYRSKTKEKEREEQNEKTLGHFMSHSSNISKAGSPPSASAPAPVSSFSRTSITPSSQDICRICHCEGDDESPLITPCHCTGSLHFVHQACLQQWIKSSDTRCCELCKYEFIMETKLKPLRKWEKLQMTSSERRKIMCSVTFHVIAITCVVWSLYVLIDRTAEEIKQGQATGILEWPFWTKLVVVAIGFTGGLLFMYVQCKVYVQLWKRLKAYNRVIYVQNCPETSKKNIFEKSPLTEPNFENKHGYGICHSDTNSSCCTEPEDTGAEIIHV	291	E3 ubiquitin-protein ligase MARCHF8	Homo sapiens (Human)	Q5T0T0	MARCHF8	2D8S	HIV-1	"[Ref.26523972]Human immunodeficiency virus type 1(HIV-1):MARCH8 blocks the incorporation of HIV-1 envelope glycoprotein into virus particles by downregulating it from the cell surface, probably through their interaction, resulting in a substantial reduction in the efficiency of viral entry. "	AF-Q5T0T0-F1	SAMHD1 interferes with HIV infection of macrophages by preventing efficient viral cDNA synthesis.HIV-2 and related simian viruses have evolved the Vpx function to counteract SAMHD1.	Phosphorylation of Ser at position 253.	26523972	"Tada T, Zhang Y, Koyama T, Tobiume M, Tsunetsugu-Yokota Y, Yamaoka S, Fujita H, Tokunaga K."	MARCH8 inhibits HIV-1 infection by reducing virion incorporation of envelope glycoproteins.
DRAVPR0057	MQRADSEQPSKRPRCDDSPRTPSNTPSAEADWSPGLELHPDYKTWGPEQVCSFLRRGGFEEPVLLKNIRENEITGALLPCLDESRFENLGVSSLGERKKLLSYIQRLVQIHVDTMKVINDPIHGHIELHPLLVRIIDTPQFQRLRYIKQLGGGYYVFPGASHNRFEHSLGVGYLAGCLVHALGEKQPELQISERDVLCVQIAGLCHDLGHGPFSHMFDGRFIPLARPEVKWTHEQGSVMMFEHLINSNGIKPVMEQYGLIPEEDICFIKEQIVGPLESPVEDSLWPYKGRPENKSFLYEIVSNKRNGIDVDKWDYFARDCHHLGIQNNFDYKRFIKFARVCEVDNELRICARDKEVGNLYDMFHTRNSLHRRAYQHKVGNIIDTMITDAFLKADDYIEITGAGGKKYRISTAIDDMEAYTKLTDNIFLEILYSTDPKLKDAREILKQIEYRNLFKYVGETQPTGQIKIKREDYESLPKEVASAKPKVLLDVKLKAEDFIVDVINMDYGMQEKNPIDHVSFYCKTAPNRAIRITKNQVSQLLPEKFAEQLIRVYCKKVDRKSLYAARQYFVQWCADRNFTKPQDGDVIAPLITPQKKEWNDSTSVQNPTRLREASKSRVQLFKDDPM	626	Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 	Homo sapiens (Human)	Q9Y3Z3	SAMHD1 	"2E8O##	4BZB##4MZ7##4QFY##4RXQ##4TNP##4TO4##6CM2##6DWD##6TXC##7LTT"	HIV-1	"[Ref.21613998]Human immunodeficiency virus type 1(HIV-1):dNTPase activity reduces cellular dNTP levels to levels too low for retroviral reverse transcription to occur, blocking early-stage virus replication in dendritic and other myeloid cells."	AF-Q9Y3Z3-F1	"MX2 suppresses infection by all HIV-1 strains tested, has equivalent or reduced effects on divergent simian immunodeficiency viruses, and does not inhibit other retroviruses such as murine leukaemia virus."	"¢ÙPhosphorylation of Ser at position 18,33,93.¢ÚThe N-terminal is acetylation.¢ÛPhosphorylation of Thr at position 21,25,592."	21720370##21613998	"Hrecka K, Hao C, Gierszewska M, Swanson SK, Kesik-Brodacka M, Srivastava S, Florens L, Washburn MP, Skowronski J.?##Laguette N, Sobhian B, Casartelli N, Ringeard M, Chable-Bessia C, S¨¦g¨¦ral E, Yatim A, Emiliani S, Schwartz O, Benkirane M."	Vpx relieves inhibition of HIV-1 infection of macrophages mediated by the SAMHD1 protein.##SAMHD1 is the dendritic- and myeloid-cell-specific HIV-1 restriction factor counteracted by Vpx.
DRAVPR0058	MSKAHKPWPYRRRSQFSSRKYLKKEMNSFQQQPPPFGTVPPQMMFPPNWQGAEKDAAFLAKDFNFLTLNNQPPPGNRSQPRAMGPENNLYSQYEQKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLKKQPCEAWAGRISYRNTELELQDPGQVEKEIHKAQNVMAGNGRGISHELISLEITSPEVPDLTIIDLPGITRVAVDNQPRDIGLQIKALIKKYIQRQQTINLVVVPCNVDIATTEALSMAHEVDPEGDRTIGILTKPDLMDRGTEKSVMNVVRNLTYPLKKGYMIVKCRGQQEITNRLSLAEATKKEITFFQTHPYFRVLLEEGSATVPRLAERLTTELIMHIQKSLPLLEGQIRESHQKATEELRRCGADIPSQEADKMFFLIEKIKMFNQDIEKLVEGEEVVRENETRLYNKIREDFKNWVGILATNTQKVKNIIHEEVEKYEKQYRGKELLGFVNYKTFEIIVHQYIQQLVEPALSMLQKAMEIIQQAFINVAKKHFGEFFNLNQTVQSTIEDIKVKHTAKAENMIQLQFRMEQMVFCQDQIYSVVLKKVREEIFNPLGTPSQNMKLNSHFPSNESSVSSFTEIGIHLNAYFLETSKRLANQIPFIIQYFMLRENGDSLQKAMMQILQEKNRYSWLLQEQSETATKRRILKERIYRLTQARHALCQFSSKEIH	715	Interferon-induced GTP-binding protein Mx2	Homo sapiens (Human)	P20592	MX2	4WHJ##4X0R##5UOT	HIV-1	[Ref.24121441]Human immunodeficiency virus type 1(HIV-1): MX2 acts by targeting the viral capsid and affects the nuclear uptake and/or stability of the HIV-1 replication complex and the subsequent chromosomal integration of the proviral DNA.	AF-P20592-F1	"Human MxA protein has a broad antiviral activity against a wide range of RNA and even some DNA viruses, including influenza A/B/C virus, ASFV(African swine fever virus); CCHFV(Crimean-Congo hemorrhagic fever virus); CVB(Coxsackie virus B); HBV(hepatitis B virus); HNTV(Hantaan virus); HPIV-3(human parainfluenza virus type 3); IBDV( infectious bursal disease virus); LACV(LaCrosse virus); MV(measles virus); RVFV(Rift Valley fever virus); SFV(Semliki Forest virus); THOV(Thogoto virus); VSV(vesicular stomatitis virus)."	No modifications on the sequence.	24048477##24121441	"Goujon C, Moncorg¨¦ O, Bauby H, Doyle T, Ward CC, Schaller T, Hu¨¦ S, Barclay WS, Schulz R, Malim MH. ##Kane M, Yadav SS, Bitzegeio J, Kutluay SB, Zang T, Wilson SJ, Schoggins JW, Rice CM, Yamashita M, Hatziioannou T, Bieniasz PD."	Human MX2 is an interferon-induced post-entry inhibitor of HIV-1 infection.##MX2 is an interferon-induced inhibitor of HIV-1 infection. 
DRAVPR0059	MVVSEVDIAKADPAAASHPLLLNGDATVAQKNPGSVAENNLCSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLKKLVNEDKWRGKVSYQDYEIEISDASEVEKEINKAQNAIAGEGMGISHELITLEISSRDVPDLTLIDLPGITRVAVGNQPADIGYKIKTLIKKYIQRQETISLVVVPSNVDIATTEALSMAQEVDPEGDRTIGILTKPDLVDKGTEDKVVDVVRNLVFHLKKGYMIVKCRGQQEIQDQLSLSEALQREKIFFENHPYFRDLLEEGKATVPCLAEKLTSELITHICKSLPLLENQIKETHQRITEELQKYGVDIPEDENEKMFFLIDKVNAFNQDITALMQGEETVGEEDIRLFTRLRHEFHKWSTIIENNFQEGHKILSRKIQKFENQYRGRELPGFVNYRTFETIVKQQIKALEEPAVDMLHTVTDMVRLAFTDVSIKNFEEFFNLHRTAKSKIEDIRAEQEREGEKLIRLHFQMEQIVYCQDQVYRGALQKVREKELEEEKKKKSWDFGAFQSSSATDSSMEEIFQHLMAYHQEASKRISSHIPLIIQFFMLQTYGQQLQKAMLQLLQDKDTYSWLLKERSDTSDKRKFLKERLARLTQARRRLAQFPG	662	Interferon-induced GTP-binding protein Mx1(MxA)	Homo sapiens (Human)	P20591	MX1	3LJB##3SZR##3SZR##4P4S##4P4T##4P4U##5GTM	"IAV,DUGV,VSV"	[Ref.14687945]Dugbe nairovirus(DUGV):MX1 protein inhibits the replication of DUGV.##[Ref.2161946]Influenza virus/vesicular stomatitis virus(VSV):transfected cell lines expressing MxA acquired a high degree of resistance to influenza A virus and vesicular stomatitis virus.	AF-P20591-F1	No comments found in the entry	The N-terminal is acetylation.	21166595##14687945##2161946	"Haller O, Kochs G.##Bridgen A, Dalrymple DA, Weber F, Elliott RM.##Pavlovic J, Z¨¹rcher T, Haller O, Staeheli P."	Human MxA protein: an interferon-induced dynamin-like GTPase with broad antiviral activity.##Inhibition of Dugbe nairovirus replication by human MxA protein. ##Resistance to influenza virus and vesicular stomatitis virus conferred by expression of human MxA protein.
DRAVPR0060	MKERTSACRHGTPQKHPDTSEESQAMESVDNLCSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLKQLKQGEKWSGKVIYKDTEIEISHPSLVEREINKAQNLIAGEGLKISSDLISLEVSSPHVPDLTLIDLPGITRVAVGDQPADIEHKIKRLITEYIQKQETINLVVVPSNVDIATTEALKMAQEVDPQGDRTIGILTKPDLVDRGTEDKVVDVVRNLVCHLKKGYMIVKCRGQQDIQEQLSLAEALQKEQVFFKEHPQFRVLLEDGKATVPCLAKRLTMELTSHICKSLPILENQINVNHQIASEELQKYGADIPEDDSKRLSFLMNKINVFNKDILSLVQAQENISWEESRLFTKLRNEFLAWNDYIEEHFKKTLGSSEKHSQMEKFESHYRGRELPGFVDYKAFENIIKKEVKALEEPALNMLHRVTTMVKNAFTKVSSNNFGDFLNLHSTAKSKIEDIRFNQEKEAEKLIRLHFQMEHIVYCQDQAYKKALQEIREKEAEKEKSTFGAFQHNSPRKELTTTEMTQHLNAYYQECGRNIGRQIPLIIQYSILQTFGQEMEKAMLQLLQDTSKCNWFLTEQSDSREKKKFLKRRLLRLDEAQRKLAKFSN	652	Interferon-induced GTP-binding protein Mx1	Rattus norvegicus (Rat)	P18588	Mx1	None	"IAV,THOV"	[Ref.21166595]influenza A virus(IAV)/Thogoto virus(THOV):exhibits antiviral activity against IAV and THOV.##[Ref.8249287]Influenza A virus(IAV):murine Mx1 protein blocks primary transcription of orthomyxoviruses via molecular interaction with the PB2 subunit of the viral polymerase.	AF-P18588-F1	No comments found in the entry	No modifications on the sequence.	21166595##8249287	"Haller O, Kochs G.##Stranden AM, Staeheli P, Pavlovic J. "	Human MxA protein: an interferon-induced dynamin-like GTPase with broad antiviral activity.?##Function of the mouse Mx1 protein is inhibited by overexpression of the PB2 protein of influenza virus. 
DRAVPR0061	MDSVNNLCRHYEEKVRPCIDLIDTLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLRKLKEGEEWRGKVSYDDIEVELSDPSEVEEAINKGQNFIAGVGLGISDKLISLDVSSPNVPDLTLIDLPGITRVAVGNQPADIGRQIKRLIKTYIQKQETINLVVVPSNVDIATTEALSMAQEVDPEGDRTIGVLTKPDLVDRGAEGKVLDVMRNLVYPLKKGYMIVKCRGQQDIQEQLSLTEAFQKEQVFFKDHSYFSILLEDGKATVPCLAERLTEELTSHICKSLPLLEDQINSSHQSASEELQKYGADIPEDDRTRMSFLVNKISAFNRNIMNLIQAQETVSEGDSRLFTKLRNEFLAWDDHIEEYFKKDSPEVQSKMKEFENQYRGRELPGFVDYKAFESIIKKRVKALEESAVNMLRRVTKMVQTAFVKILSNDFGDFLNLCCTAKSKIKEIRLNQEKEAENLIRLHFQMEQIVYCQDQVYKETLKTIREKEAEKEKTKALINPATFQNNSQFPQKGLTTTEMTQHLKAYYQECRRNIGRQIPLIIQYFILKTFGEEIEKMMLQLLQDTSKCSWFLEEQSDTREKKKFLKRRLLRLDEARQKLAKFSD	631	Interferon-induced GTP-binding protein Mx1	Mus musculus (Mouse)	P09922	Mx1	None	"IAV,IBV,THOV"	"[Ref.21166595]influenza A virus(IAV)/Thogoto virus(THOV)/influenza B virus (IBV)/:exhibits antiviral activity against IAV,IBV and THOV."	AF-P09922-F1	"poMx1 decreases or delays NP synthesis, and inhibits production of progeny viral particles and hampers viral infection at an early stage."	No modifications on the sequence.	21166595	"Haller O, Kochs G."	Human MxA protein: an interferon-induced dynamin-like GTPase with broad antiviral activity.?
DRAVPR0062	MVYSSCESKEPDSVSASNHLLLNGNDELVEKSHKTGPENNLYSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLKKLVNEEDEWKGKVSYRDSEIELSDASQVEKEVSAAQIAIAGEGVGISHELISLEVSSPHVPDLTLIDLPGITRVAVGNQPYDIEYQIKSLIKKYICKQETINLVVVPCNVDIATTEALRMAQEVDPEGDRTIGILTKPDLVDKGTEDKIVDVARNLVFHLKKGYMIVKCRGQQDIQEQLSLAKALQKEQAFFENHAHFRDLLEEGRATIPCLAERLTSELIMHICKTLPLLENQIKESHQKITEELQKYGSDIPEDESGKMFFLIDKIDAFNSDITALIQGEELVVEYECRLFTKMRNEFCRWSAVVEKNFKNGYDAICKQIQLFENQYRGRELPGFVNYKTFETIIKKQVSVLEEPAVDMLHTVTDLVRLAFTDVSETNFNEFFNLHRTAKSKIEDIKLEQEKEAETSIRLHFQMEQIVYCQDQVYRGALQKVREKEAEEEKNRKSNQYFLSSPAPSSDPSIAEIFQHLIAYHQEVGKRISSHIPLIIQFFILRTFGQQLQKSMLQLLQNKDQYDWLLRERSDTSDKRKFLKERLMRLTQARRRLAKFPG	663	Interferon-induced GTP-binding protein Mx1	Sus scrofa (Pig)	P27594	MX1	None	IAV	[Ref.20167191]Influenza A virus(IAV):Inhibits IAV replication by decreasing or delaying NP synthesis and by blocking endocytic traffic of incoming virus particles.	AF-P27594-F1	"BoMx1 inhibits the replication of members of the Rhabdoviridae and Orthomyxoviridae families. Contrary to human MxA, however, Sendai, bovine and human parainfluenza-3, and measles viruses are resistant to boMx1. "	No modifications on the sequence.	20167191	"Palm M, Garigliany MM, Cornet F, Desmecht D."	Interferon-induced Sus scrofa Mx1 blocks endocytic traffic of incoming influenza A virus particles.
DRAVPR0063	MVHSDLGIEELDSPESSLNGSEDMESKSNLYSQYEEKVRPCIDLIDSLRSLGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLRLKKLGNEDEWKGKVSFLDKEIEIPDASQVEKEISEAQIAIAGEGTGISHELISLEVSSPHVPDLTLIDLPGITRVAVGNQPPDIEYQIKSLIRKYILRQETINLVVVPANVDIATTEALRMAQEVDPQGDRTIGILTKPDLVDKGTEDKVVDVVRNLVFHLKKGYMIVKCRGQQDIKHRMSLDKALQRERIFFEDHAHFRDLLEEGKATIPCLAERLTSELIMHICKTLPLLENQIKETHQRITEELQKYGKDIPEEESEKMFCLIEKIDTFNKEIISTIEGEEFVEQYDSRLFTKVRAEFSKWSAVVEKNFEKGYEAIRKEIKQFENRYRGRELPGFVNYKTFETIIKKQVRVLEEPAVDMLHTVTDIIRNTFTDVSGKHFNEFFNLHRTAKSKIEDIRLEQENEAEKSIRLHFQMEQLVYCQDQVYRRALQQVREKEAEEEKNKKSNHYFQSQVSEPSTDEIFQHLTAYQQEVSTRISGHIPLIIQFFVLRTYGEQLKKSMLQLLQDKDQYDWLLKERTDTRDKRKFLKERLERLTRARQRLAKFPG	648	Interferon-induced GTP-binding protein Mx1	Bos taurus (Bovine)	P79135	MX1	None	RABV	[Ref.16202617]rabies virus(RABV):bovine Mx1 can interfere the replication of rabies virus.	AF-P79135-F1	No comments found in the entry	No modifications on the sequence.	16202617##22385204	"Leroy M, Pire G, Baise E, Desmecht D.##Dermine M, Desmecht D."	Expression of the interferon-alpha/beta-inducible bovine Mx1 dynamin interferes with replication of rabies virus.?##In Vivo modulation of the innate response to pneumovirus by type-I and -III interferon-induced Bos taurus Mx1.
DRAVPR0064	MVLSTEENTGVDSVNLPSGETGLGEKDQESVNNLCSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLRKLNEGEEWRGKVSYDDIEVELSDPSEVEEAINKGQNFIAGVGLGISDKLISLDVSSPNVPDLTLIDLPGITRVAVGNQPADIGRQIKRLIKTYIQKQETINLVVVPSNVDIATTEALSMAQEVDPEGDRTIGILTKPDLVDRGTEDKVVDVVRNLVYHLKKGYMIVKCRGQQDIQEQLSLTEALQNEQIFFKEHPHFRVLLEDGKATVPCLAERLTAELISHICKSLPLLENQIKESHQSASEELQKYGMDIPEDDSEKTFFLIEKINAFNQDITALVQGEENVAEGECRLFTRLRKEFLSWSKEIEKNFAKGYAVLYNEVWAFEKQYRGRELPGFVNYKTFENIIRRQIKTLEEPAIEMLHTVTEIVRAAFTSVSEKNFSEFYNLHRTTKSKLEDIRLEQEKEAEMSIRLHFKMEQIIYCQDQIYRGALQKVREEEAEEEKKTKHGTSSSSQSQDLQTSSMAEIFQHLNAYRQEAHNRISSHVPLIIQYFILKMFAERLQKGMLQLLQDKDSCSWLLKEQSDTSEKRKFLKERLARLAQARRRLAKFPG	655	Interferon-induced GTP-binding protein Mx2	Mus musculus (Mouse)	Q9WVP9	Mx2	None	"VSV,HNTV"	"[Ref.21166595]vesicular stomatitis virus(VSV)/Hantaan virus(HNTV):exhibits antiviral activity against VSV and HNTV.##[Ref.11266216]Hantavirus(HNTV):When the Mx2 gene was constitutively expressed in transfected Vero cells, it prvented the accumulation of viral transcripts and proteins of hantaviruses.##[Ref.10233954]vesicular stomatitis virus(VSV):Mx2 inhibits the replication of VAV."	AF-Q9WVP9-F1	No comments found in the entry	No modifications on the sequence.	21166595##11266216##10233954	"Haller O, Kochs G.##Jin HK, Yoshimatsu K, Takada A, Ogino M, Asano A, Arikawa J, Watanabe T. ##Jin HK, Takada A, Kon Y, Haller O, Watanabe T."	Human MxA protein: an interferon-induced dynamin-like GTPase with broad antiviral activity.?##Mouse Mx2 protein inhibits hantavirus but not influenza virus replication.##Identification of the murine Mx2 gene: interferon-induced expression of the Mx2 protein from the feral mouse gene confers resistance to vesicular stomatitis virus. 
DRAVPR0065	MVLSTEENRSVDLVNLPSVPLPDGEAGVGENNKDSLNNLCSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLKKLNQGEEWKGKVTYDDIEVELSDPSEVEEAINTGQNHIAGVGLGISDKLISLDVSSPHVPDLTLIDLPGITRVAVGNQPADIGRQIKRLITNYIQKQETINLVVVPSNVDIATTEALSMAQKVDPDGDRTIGILTKPDLVDRGTEDKVVDVVRNLVCHLKKGYMIVKCRGQQDIQEQLSLAEALQKEQVFFKEHPQFRALLEDGKATVPCLAERLTMELISHICKSLPLLENQIKESHQSTSEELQKYGADIPEDENEKTLFLIEKINAFNQDITAIVEGEEIVREKECRLFTKLRKEFFLWSEEIERNFQKGSDALYKEVYTFEMQYRGRELPGFVNYKTFENIIRRQIKTLEEPAMEMLHKVTEIVRAAFTTVSEKNFSEFFNLHRTTKSKLEDIRLEQETEAEKSIRLHFQMEQIIYCQDQIYRKALQKVREEEAEEEERKHGKSRSSQSKNLQTSSMDEIFQHLNAYRQEAHNRISSHIPLIIQYFILKMFAEKLQKGMLQLLQDKDSCSWLLKEHSDTSEKRRFLKERLARLAQAQRRLAKFPG	659	Interferon-induced GTP-binding protein Mx2	Rattus norvegicus (Rat)	P18589	Mx2	None	VSV	[Ref.2173790]vesicular stomatitis virus(VSV):Mx2 inhibits the replication of VSV.	AF-P18589-F1	bovine Mx1 protein participates in antiviral activity against the rabies virus.	No modifications on the sequence.	2173790	"Meier E, Kunz G, Haller O, Arnheiter H."	Activity of rat Mx proteins against a rhabdovirus.
DRAVPR0066	MSMSFRPLKYKRHTQTSTQHHPKQDIYFHQQPPGPPLGQTMSPPQWQVEESNPDFLPNNFNQLNLDPQQPEAKGGQQMSKGPENNLYRKYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIITRCPLVLKLTKRECEWTGKITYRNITQQLQNPSEVEWEIRRAQNIIAGNGLGISHELINLEITSPEVPDLTLIDLPGITRVAVENQPQDIGLQIKALIKKYIQRQETINLVVVPCNVDIATTEALSMAQEVDPDGDRTIGILTKPDLVDKGTEKGVLKVMQNLTYHLKKGYMIVKCRGQQDITNKLSLAEATRKETMFFETHPYFRILLDEGKATVPLLAERLTTELIWHINKSLPLLENQIKEKHQRATEELQQYGDDIPSDEGDKMFFLIEKIKVFNEDIGKLIEGEEIVMETESRLCNKIREEFTSWILILTTNIEKVKSILNEEVSKYEKKYRGKELLGFVNYKTFETVVKHYLGQLIDPALKMLQKAMEIVWQTFKDTAKKHFAEFCNLHQTVQNKIEDIKTKQMAEAANLIQLQFRMEKLVFCQDQIYGVVLNKVREDIFNSMGKASETPQSKQPFLNDQSSISSIVEIGVHLNAYFMETSKRLANQIPFIIQYFMLQENGDKVQKAMMQLLQDTQHYSWLLQEQSDTATKRKFLKEKIFRLTQAQQALYEFPHFKG	710	Interferon-induced GTP-binding protein Mx2	Bos taurus (Bovine)	Q9BDI7	MX2	None	VSV	[Ref.17119954]vesicular stomatitis virus(VSV):bovine Mx1 protein confers antiviral activity against vesicular stomatitis virus (VSV).	AF-Q9BDI7-F1	No comments found in the entry	No modifications on the sequence.	17119954	"Babiker HA, Nakatsu Y, Yamada K, Yoneda A, Takada A, Ueda J, Hata H, Watanabe T."	Bovine and water buffalo Mx2 genes: polymorphism and antiviral activity. 
DRAVPR0067	MPKPRMSWPYQRHRQASSPPHPHKEMNFFPQQPLPLGAGPGQMTFPLNWQMGGKDLTKGLNMLTLSPQQPGGKSGQQTSKGPENNLYSPFEEKVRPCIDLIDSLRALGVEQDLALPTIAVIGDQSSGKSSVLEALSGVPLPRGSGIITRCPLALRLKKKECPWQGRISYRKVELQLQDPSQVEREIRKAQDAIAGSGVGISHELISLEVTSPEVPDLTLIDLPGITRVAVGNQPQDIGLQIKALIRKYIQEQQTINLVVVPCNVDIATTEALRMAQEVDPEGDRTIGILTKPDLVDTGAEKVVLNVMQNLTYHLKKGYMIVKCRGQQEILNKLSLAEATKREIAFFHSHPHFRILLEEGKATVPRLAERLTVELIGHISKSLPLLFSQIKEIHQSATEELRLCGASVPSNDADKMFFLIEKIKVFNQDIENLAEGEEIVKEKEARLYNKIREEFKSWIVTLDCNSKKVKNIIHEEVSKYDRQYRGKELMGFVSYKTFESIVRQYLEELVDPALGMLQTVVEIVRQTFSDTAQKNFGEFSNLNQTTQNKVDSIAARAAERAEGLIRLQFRMEQLVFCQDDIYRVDLKAVREELFNPVAEHPQSLQLRLPFVNGPSPVSSITEIGVHVNAYFMGTSQRLANQIPFIIQYCVLQESRDHLQKAMMQMLQGREQYSWLLQEESHTSAKRHFLKEKIHRLAEARHTLSKFAQSLQG	711	Interferon-induced GTP-binding protein Mx2	Sus scrofa (Pig)	A7VK00	MX2	None	IAV	[Ref.18977535]Influenza A virus:porcine Mx2 inhibition of multiplication of influenza virus A/WSN/33 and A/Udorn/72.	AF-A7VK00-F1	No comments found in the entry	No modifications on the sequence.	18977535	"Morozumi T, Naito T, Lan PD, Nakajima E, Mitsuhashi T, Mikawa S, Hayashi T, Awata T, Uenishi H, Nagata K, Watanabe T, Hamasima N.?"	Molecular cloning and characterization of porcine Mx2 gene.
DRAVPR0068	MSKAHGSRPYRRHNVVIPRQQPEKEMNFVQQQPPPSDAAARQMMYPPNCQVGVQDPVYLAKEFNLLTLNPQQLEGSRHQQMAKGPEKSLYSQYEQKVRPCIDLVDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLKRDPHKAWRGRISYRKTELQFQDPSQVEKEIRQAQNIIAGQGLGISHELISLEITSPEVPDLTLIDLPGITRVAVGNQPQDIGVQIKALIKNYIQKQETINLVVVPCNVDIATTEALSMAQEVDPNGDRTIGVLTKPDLVDRGTEKTVVNVAQNLTYHLQKGYMIVRCRGQEEITNQLSLAEATEKERMFFQTHPYFRALLEEGKATVPCLAERLTKELILHINKSLPLLEKQIRESHQRATDELHQCGDSIPSNEADKMFFLIEKIKLFNQDIDKLIEGEEIVKKNETRLYNKIREEFEHWALVLTANTQKVKNIVSEEVSVYEKQYRGKELLGFVNYKTFETIVHQYIEQLVEPALTMLRKTIEIVWQAFTDTAKKHFSVFSNLSQTIQNKIEDIKTRQAETAENLIRLQFRMEQLVYCQDQIYSVVLRKVRKEVFNPAGKAAQDLQLKFPFPKDLPSMSSNDEIGVHLNAYFLETSKRLANQIPFIIQYFVLQENGSCLQKAMMQILQEREQYSWLLQEHADTSAKRRFLKEKIYRLAQARRALYMFFS	711	Interferon-induced GTP-binding protein Mx2	Canis lupus familiaris (Dog) (Canis familiaris)	Q9N0Y2	MX2	None	VSV	[Ref.15767791]vesicular stomatitis virus (VSV):Mx2 had an antiviral activity against recombinant vesicular stomatitis virus (VSV).	AF-Q9N0Y2-F1	"The protein target viruses belong to families which include retroviridae: human immunodeficiency virus type 1 (HIV-1) and moloney and murine leukemia virus (MoMLV), filoviridae: ebola virus (EBOV) and marburg virus (MARV), togaviridae: sindbis virus (SINV) and Ross river virus (RRV). "	No modifications on the sequence.	15767791	"Nakamura T, Asano A, Okano S, Ko JH, Kon Y, Watanabe T, Agui T."	Intracellular localization and antiviral property of canine Mx proteins.
DRAVPR0069	MTDPEVFCFITKILCAHGGRMTLEELLGEISLPEAQLYELLKAAGPDRFVLLETGDQAGITRSVVATTRARVCRRKYCQRPCDSLHLCKLNLLGRCHYAQSQRNLCKYSHDVLSEQNFQVLKNHELSGLNQEELAVLLVQSDPFFMPEICKSYKGEGRKQICGQPQPCERLHICEHFTRGNCSYLNCLRSHNLMDRKVLAIMREHGLSSDVVQNIQDICNNKHTRRNPPSMRAPHPHRRGGAHRDRSKSRDRFHHNSLEVLSTVSPLGSGPPSPDVTGCKDPLEDVSADVTQKFKYLGTQDRAQLSSVSSKAAGVRGPSQMRASQEFLEDGDPDGLFSRNRSDSSTSRTSAAGFPLVAAQRNEAGAMKMGMPSGHHVEVKGKNEDIDRVPFLNSYIDGVTMEEATVSGILGKRATDNGLEEMILSSNHQKSVAKTQDPQTAGRITDSGQDTAFLHSKYEENPAWPGTSTHNGPNGFSQIMDETPNVSKSSPTGFGIKSAVTGGKEAVYSGVQSLRSHVLAMPGETTTPVQGSNRLPPSPLSSSTSHRVAASGSPGKSSTHASVSPASEPSRMMMMMSDPAEYSLCYIVNPVSPRMDDHGLKEICLDHLYRGCQQVNCNKNHFHLPYRWQLFILPTWMDFQDMEYIERAYCDPQIEIIVIEKHRINFKKMTCDSYPIRRLSTPSFVEKTLNSVFTTKWLWYWRNELNEYTQYGHESPSHTSSEINSAYLESFFHSCPRGVLQFHAGSQNYELSFQGMIQTNIASKTQRHVVRRPVFVSSKDVEQKRRGPDHQPVMPQADALTLFSSPQRNASTVSSNEYEFIELNNQDEEYAKISEQFKASMKQFKIVTIKRIWNQKLWDTFERKKQKMKNKTEMFLFHAVGRIHMDYICKNNFEWILHGNREIRYGKGLCWRRENCDSSHAHGFLEMPLASLGRTASLDSSGLQRK	946	Zinc finger CCCH-type antiviral protein 1(PARP-13)	Mus musculus (Mouse)	Q3UPF5	Zc3hav1	6L1W		"[Ref.21102435]PARP-13 inhibits the replication of viruses by recruiting the cellular RNA degradation machineries to degrade the viral mRNAs. Binds to a ZAP-responsive element (ZRE) present in the target viral mRNA, recruits cellular poly(A)-specific ribonuclease PARN to remove the poly(A) tail, and the 3'-5' exoribonuclease complex exosome to degrade the RNA body from the 3'-end. It also recruits the decapping complex DCP1-DCP2 through RNA helicase p72 (DDX17) to remove the cap structure of the viral mRNA to initiate its degradation from the 5'-end. "	AF-Q3UPF5-F1	"Rat ZAP exhibits antiviral activity against diverse viruses including, in addition to alphaviruses, Moloney murine leukemia virus (MLV) and Ebola virus."	"¢ÙPhosphorylation of Ser at position 257,262,265,269,273,324,350,425,553,583,680.¢ÚPhosphorylation of Thr at position 277.¢ÛPhosphorylation of Tyr at position 508."	21102435	"Hayakawa S, Shiratori S, Yamato H, Kameyama T, Kitatsuji C, Kashigi F, Goto S, Kameoka S, Fujikura D, Yamada T, Mizutani T, Kazumata M, Sato M, Tanaka J, Asaka M, Ohba Y, Miyazaki T, Imamura M, Takaoka A."	ZAPS is a potent stimulator of signaling mediated by the RNA helicase RIG-I during antiviral responses.?
DRAVPR0070	MADPGVCCFITKILCAHGGRMTLEELLGEIRLPEAQLYELLETAGPDRFVLLETGGQAGITRSVVATTRARVCRRKYCQRPCDSLHLCKLNLLGRCHYAQSQRNLCKYSHDVLSEQNFQILKNHELSGLNQEELACLLVQSDPFFLPEICKSYKGEGRKQTCGQPQPCERLHICEHFTRGNCSYLNCLRSHNLMDRKVLTIMREHGLSPDVVQNIQDICNNKHARRNPPGTRAAHPHRRGGAHRDRSKSRDRFLHNSLEFLSPVVSPLGSGPPSPDVTSCKDSLEDVSVDVTQKFKYLGTHDRAQLSPVSSKAAGVQGPSQMRASQEFSEDGNLDDIFSRNRSDSSSSRASAAKVAQRNEAVAMKMGMEVKGKKEAPDIDRVPFLNSYIDGVTMEKASVSGIPGKKFTANDLENLLLLNDTWKNVAKPQDLQTTGRITDSGQDKAFLQNKYGGNPVWASASTHNAPNGSSQIMDETPNVSKSSTSGFAIKPAIAGGKEAVYSGVQSPRSQVLAVPGEATTPVQSNRLPQSPLSSSSHRAAASGSPGKNSTHTSVSPAIESSRMTSDPDEYLLRYILNPLFRMDNHGPKEICQDHLYKGCQQSHCDRSHFHLPYRWQMFVYTTWRDFQDMESIEQAYCDPHVELILIENHQINFQKMTCDSYPIRRLSTPSYEEKPLSAVFATKWIWYWKNEFNEYIQYGNESPGHTSSDINSAYLESFFQSCPRGVLPFQAGSQKYELSFQGMIQTNIASKTQRHVVRRPVFVSSNDVEQKRRGPE	776	Zinc finger CCCH-type antiviral protein 1(ZAP)	Rattus norvegicus (Rat) 	Q8K3Y6	Zc3hav1	3U9G	"SINV,EBOV,MARV"	[Ref.17928353]sindbis virus (SINV):ZAP inhibited translation of the incoming viral RNA.##[Ref.17182693]Ebola virus (EBOV)/Marburg virus (MARV):ZAP has an antiviral effect against EBOV and MARV in cell culture.	AF-Q8K3Y6-F1	"The zinc-finger antiviral protein (ZAP) is a host factor that specifically inhibits the replication of certain viruses, including Moloney murine leukemia virus (MoMLV), HIV-1, and certain alphaviruses and filoviruses."	"¢ÙPhosphorylation of Ser at position 257,262,266,270,274,283,325,351,398,544,667.¢ÚPhosphorylation of Thr at position 278.¢ÛPhosphorylation of Tyr at position 501."	17928353##17182693	"MacDonald MR, Machlin ES, Albin OR, Levy DE.##M¨¹ller S, M?ller P, Bick MJ, Wurr S, Becker S, G¨¹nther S, K¨¹mmerer BM."	The zinc finger antiviral protein acts synergistically with an interferon-induced factor for maximal activity against alphaviruses.?##Inhibition of filovirus replication by the zinc finger antiviral protein.
DRAVPR0071	MADPEVCCFITKILCAHGGRMALDALLQEIALSEPQLCEVLQVAGPDRFVVLETGGEAGITRSVVATTRARVCRRKYCQRPCDNLHLCKLNLLGRCNYSQSERNLCKYSHEVLSEENFKVLKNHELSGLNKEELAVLLLQSDPFFMPEICKSYKGEGRQQICNQQPPCSRLHICDHFTRGNCRFPNCLRSHNLMDRKVLAIMREHGLNPDVVQNIQDICNSKHMQKNPPGPRAPSSHRRNMAYRARSKSRDRFFQGSQEFLASASASAERSCTPSPDQISHRASLEDAPVDDLTRKFTYLGSQDRARPPSGSSKATDLGGTSQAGTSQRFLENGSQEDLLHGNPGSTYLASNSTSAPNWKSLTSWTNDQGARRKTVFSPTLPAARSSLGSLQTPEAVTTRKGTGLLSSDYRIINGKSGTQDIQPGPLFNNNADGVATDITSTRSLNYKSTSSGHREISSPRIQDAGPASRDVQATGRIADDADPRVALVNDSLSDVTSTTSSRVDDHDSEEICLDHLCKGCPLNGSCSKVHFHLPYRWQMLIGKTWTDFEHMETIEKGYCNPGIHLCSVGSYTINFRVMSCDSFPIRRLSTPSSVTKPANSVFTTKWIWYWKNESGTWIQYGEEKDKRKNSNVDSSYLESLYQSCPRGVVPFQAGSRNYELSFQGMIQTNIASKTQKDVIRRPTFVPQWYVQQMKRGPDHQPAKTSSVSLTATFRPQEDFCFLSSKKYKLSEIHHLHPEYVRVSEHFKASMKNFKIEKIKKIENSELLDKFTWKKSQMKEEGKLLFYATSRAYVESICSNNFDSFLHETHENKYGKGIYFAKDAIYSHKNCPYDAKNVVMFVAQVLVGKFTEGNITYTSPPPQFDSCVDTRSNPSVFVIFQKDQVYPQYVIEYTEDKACVIS	902	Zinc finger CCCH-type antiviral protein 1	Homo sapiens (Human)	Q7Z2W4	ZC3HAV1	2X5Y##4X52##6UEI##6UEJ##7KZH##7TGQ	"XMRV,HIV-1"	[Ref.22720057]Xenotropic murine leukemia virus-related virus (XMRV):ZAP inhibits XMRV replication by preventing the accumulation of viral mRNA in the cytoplasm.##[Ref.21876179]Human immunodeficiency virus type 1(HIV-1):ZAP inhibits HIV-1 by recruiting both the 5¡ä and 3¡ä mRNA degradation machinery to specifically promote the degradation of multiply spliced HIV-1 mRNAs.	AF-Q7Z2W4-F1	"human OAS3 exhibits antiviral activity against alphaviruses, such as the Chikungunya virus, the Sindbis virus, and the Semliki Forest virus,"	"¢ÙPhosphorylation of Ser at position 257,263,267,271,275,284,302,327,335,355,378,387,407,469,492,494,572,590.¢ÚPhosphorylation of Thr at position 554,393.¢ÛThe N-terminal is Acetylation."	22720057##21876179	"Wang X, Tu F, Zhu Y, Gao G.##Zhu Y, Chen G, Lv F, Wang X, Ji X, Xu Y, Sun J, Wu L, Zheng YT, Gao G. "	Zinc-finger antiviral protein inhibits XMRV infection.?##Zinc-finger antiviral protein inhibits HIV-1 infection by selectively targeting multiply spliced viral mRNAs for degradation.
DRAVPR0072	MDLYSTPAAALDRFVARRLQPRKEFVEKARRALGALAAALRERGGRLGAAAPRVLKTVKGGSSGRGTALKGGCDSELVIFLDCFKSYVDQRARRAEILSEMRASLESWWQNPVPGLRLTFPEQSVPGALQFRLTSVDLEDWMDVSLVPAFNVLGQAGSGVKPKPQVYSTLLNSGCQGGEHAACFTELRRNFVNIRPAKLKNLILLVKHWYHQVCLQGLWKETLPPVYALELLTIFAWEQGCKKDAFSLAEGLRTVLGLIQQHQHLCVFWTVNYGFEDPAVGQFLQRQLKRPRPVILDPADPTWDLGNGAAWHWDLLAQEAASCYDHPCFLRGMGDPVQSWKGPGLPRAGCSGLGHPIQLDPNQKTPENSKSLNAVYPRAGSKPPSCPAPGPTGAASIVPSVPGMALDLSQIPTKELDRFIQDHLKPSPQFQEQVKKAIDIILRCLHENCVHKASRVSKGGSFGRGTDLRDGCDVELIIFLNCFTDYKDQGPRRAEILDEMRAQLESWWQDQVPSLSLQFPEQNVPEALQFQLVSTALKSWTDVSLLPAFDAVGQLSSGTKPNPQVYSRLLTSGCQEGEHKACFAELRRNFMNIRPVKLKNLILLVKHWYRQVAAQNKGKGPAPASLPPAYALELLTIFAWEQGCRQDCFNMAQGFRTVLGLVQQHQQLCVYWTVNYSTEDPAMRMHLLGQLRKPRPLVLDPADPTWNVGHGSWELLAQEAAALGMQACFLSRDGTSVQPWDVMPALLYQTPAGDLDKFISEFLQPNRQFLAQVNKAVDTICSFLKENCFRNSPIKVIKVVKGGSSAKGTALRGRSDADLVVFLSCFSQFTEQGNKRAEIISEIRAQLEACQQERQFEVKFEVSKWENPRVLSFSLTSQTMLDQSVDFDVLPAFDALGQLVSGSRPSSQVYVDLIHSYSNAGEYSTCFTELQRDFIISRPTKLKSLIRLVKHWYQQCTKISKGRGSLPPQHGLELLTVYAWEQGGKDSQFNMAEGFRTVLELVTQYRQLCIYWTINYNAKDKTVGDFLKQQLQKPRPIILDPADPTGNLGHNARWDLLAKEAAACTSALCCMGRNGIPIQPWPVKAAV	1087	2'-5'-oligoadenylate synthase 3	Homo sapiens (Human)	Q9Y6K5	OAS3	4S3N	"DENV,CHIKV"	[Ref.19923450]dengue virus(DENV):The antiviral effects of human OAS3 p100 correlate with their abilities to trigger RNase L activation in DEN-2-infected cells.##[Ref.19056102]Chikungunya virus(CHIKV):OAS3 exhibits antiviral effect by blocking the early stage of virus replication.	AF-Q9Y6K5-F1	"OASL possesses two domains with HCV inhibitory activity. The OAS-homology domain without OAS activity is inhibitory for cell growth as well as HCV replication, whereas C-terminal Ub is inhibitory only for HCV replication."	Phosphorylation of Thr at position 365.	19923450##19056102	"Lin RJ, Yu HP, Chang BL, Tang WC, Liao CL, Lin YL.?##Br¨¦hin AC, Casad¨¦mont I, Frenkiel MP, Julier C, Sakuntabhai A, Despr¨¨s P."	"Distinct antiviral roles for human 2',5'-oligoadenylate synthetase family members against dengue virus infection.##The large form of human 2',5'-Oligoadenylate Synthetase (OAS3) exerts antiviral effect against Chikungunya virus. "
DRAVPR0073	MALMQELYSTPASRLDSFVAQWLQPHREWKEEVLDAVRTVEEFLRQEHFQGKRGLDQDVRVLKVVKVGSFGNGTVLRSTREVELVAFLSCFHSFQEAAKHHKDVLRLIWKTMWQSQDLLDLGLEDLRMEQRVPDALVFTIQTRGTAEPITVTIVPAYRALGPSLPNSQPPPEVYVSLIKACGGPGNFCPSFSELQRNFVKHRPTKLKSLLRLVKHWYQQYVKARSPRANLPPLYALELLTIYAWEMGTEEDENFMLDEGFTTVMDLLLEYEVICIYWTKYYTLHNAIIEDCVRKQLKKERPIILDPADPTLNVAEGYRWDIVAQRASQCLKQDCCYDNRENPISSWNVKRARDIHLTVEQRGYPDFNLIVNPYEPIRKVKEKIRRTRGYSGLQRLSFQVPGSERQLLSSRCSLAKYGIFSHTHIYLLETIPSEIQVFVKNPDGGSYAYAINPNSFILGLKQQIEDQQGLPKKQQQLEFQGQVLQDWLGLGIYGIQDSDTLILSKKKGEALFPAS	514	2'-5'-oligoadenylate synthase-like protein	Homo sapiens (Human)	Q15646	OASL	1WH3##4XQ7	HCV	[Ref.20074559]Hepatitis C virus(HCV):OASL is inhibitory to HCV repllication in HCV replicon cells.	AF-Q15646-F1	No comments found in the entry	Acetylation of Ala at position 2(N-acetylalanine).	20074559	"Ishibashi M, Wakita T, Esumi M."	"2',5'-Oligoadenylate synthetase-like gene highly induced by hepatitis C virus infection in human liver is inhibitory to viral replication in vitro. "
DRAVPR0074	MNATHCILALQLFLMAVSGCYCHGTVIESLESLNNYFNSSGIDVEEKSLFLDIWRNWQKDGDMKILQSQIISFYLRLFEVLKDNQAISNNISVIESHLITTFFSNSKAKKDAFMSIAKFEVNNPQVQRQAFNELIRVVHQLLPESSLRKRKRSRC	155	Interferon gamma(IFN-gamma)	Mus musculus (Mouse)	P01580	Ifng	None		[Ref.8456301]Type II interferon produced by immune cells such as T-cells and NK cells that plays crucial roles in antiviral responses by activating effector immune cells and enhancing antigen presentation.	AF-P01580-F1	"TRIM56 exhibits a broad antiviral activity against bovine viral diarrhea virus (BVDV), yellow fever virus (YFV), dengue virus serotype 2 (DENV2), human coronavirus virus (HCoV), and influenza A and B viruses.TRIM56 had no effect on the replication of vesicular stomatitis virus (VSV) and HCV."	"Glycosylation of Asn at position 38,90."	8456301	"Huang S, Hendriks W, Althage A, Hemmi S, Bluethmann H, Kamijo R, Vilcek J, Zinkernagel RM, Aguet M."	Immune response in mice that lack the interferon-gamma receptor.?
DRAVPR0075	MVSQGSSPSLLEALSSDFLACKICLEQLRVPKTLPCLHTYCQDCLAQLAEGSRLRCPECRESVPVPPAGVAAFKTNFFVNGLLDLVKARAGGDLRAGKPACALCPLMGGASAGGPATARCLDCADDLCQACADGHRCTRQTHSHRVVDLVGYRAGWYDEEARERQAAQCPQHPGEALRFLCQPCSQLLCRECRLDPHLDHPCLPLAEAVRARRPGLEELLAGVDNNLAELEATRLAEKEALARLREQAAKVVTQVEEASERVLRALLAQKQEVLGQLRAHVEAAEEGARERLGELEGQEQVAREAAAFARRVLSLGREAEILSLEGAIAQRLRQLQGCPWVPGPAPCQLPQLELYPGLLDKNCHLLRLSFEEQLPQKDSGKDGARSQGGDATQPQSRDGVQTPNQEDGAKTPKESRAQTPQEDGGTQARVGSRSNKKRKFKGRLKSVSREPSPAPGPNLEGSGLLPRPIFFCSFPTRMPGDKRAPRITGLCPFGSREILVADEQNRALKRFSLNGDYRGAVPVPEGCSPCSVAALQDTVAFSAAARLYLINHNGEVQWRRALSLCQASHAVAAMPSGDRVAVSVSGHVEVYNMEGSLATRFIPGGKANRGLRALVFLTTSPQGHFVGSDWQQNSLVVCDGLGQVVGEYRGPGLHGCQPGSVSVDKKGYIFLTLREVNKVVILDPKGSLLGDFLTAYHGLEKPRVTTMVDGRYLVVSLSNGTIHVFRVRPLDS	732	E3 ubiquitin-protein ligase TRIM56	Bos taurus (Bovine)	E1BD59	TRIM56	None	BVDV	[Ref.21289118]bovine viral diarrhea virus (BVDV):TRIM56 inhibits BVDV propagation by acting on intracellular viral RNA replication. 	AF-E1BD59-F1	No comments found in the entry	¢ÙPhosphorylation of Ser at position 452.¢ÚPhosphorylation of Thr at position 402 and 419.	21289118##27667714	"Wang J, Liu B, Wang N, Lee YM, Liu C, Li K.##Fan W, Wu M, Qian S, Zhou Y, Chen H, Li X, Qian P."	TRIM56 is a virus- and interferon-inducible E3 ubiquitin ligase that restricts pestivirus infection.?##TRIM52 inhibits Japanese Encephalitis Virus replication by degrading the viral NS2A.
DRAVPR0076	MGNWLTGNWSSDRSSGYSSGWSPGGSSGVPSGPVHKLEKSIQANLTPNENCLKQIAVSSVPSQKLEGYIQENLKPNRESLKQIDQAVDAIWDLLRSQIPVKEVAKGGSYGRETALRGCSDGTLVLFMDCFQQFQDQIKYQDAYLDVIELWLKIHEKKSVKHEHALVVQVSVPGQRILLQLLPVFNPLRSNENPSSCVYVDLKKSMDQVRASPGEFSDCFTTLQQRFFKKYPQRLKDLILLVKHWYEQCQEKWKTPPPQPLLYALELLTVYAWEQGCQAEDFDMAQGVRTVLRLIQRPTELCVYWTVNYNFEDETVRNILLHQLRSQRPVILDPTDPTNNVGKDDGFWELLTEEAMAWLYSPSLNTESPAPYWDVLPMPLFVTPSHLLNKFIKDFLQPNKLFLKQIKEAVDIICSFLKNVCFLNSDTKVLKTVKGGSTAKGTALKRGSDADIVVFLSSLESYDSLKTNRSQFVQEIQKQLEEFVQAQEWEVTFEISKWKAPRVLSFTLKSKTLNESVEFDVLPAYDALGQLRSDFTLRPEAYKDLIELCASQDIKEGEFSICFTELQRNFIQTRPTKLKSLLRLIKHWYKQYERKMKPKASLPPKYALELLTVYAWEQGSGTDDFDIAEGFRTVLDLVIKYRQLCIFWTVNYNFEEEYMRKFLLTQIQKKRPVILDPADPTGDVGGGDRWCWHLLAEEAKEWLSSPCFQVEQKGLVQPWKVPVMQTPGSCGGQIYPTVGGVTK	742	2'-5'-oligoadenylate synthase 2	Mus musculus (Mouse)	E9Q9A9	Oas2	None		"[Ref.12396720]2',5'-Oligoadenylate synthetase (2-5OAS) is one of the interferon (IFN)-induced proteins and mediates the antiviral action of IFN.##[Ref.21142819]The 2'-5' oligoadenylate synthetases (OAS) are interferon-induced antiviral enzymes that recognize virally produced dsRNA and initiate RNA destabilization through activation of RNase L within infected cells. "	AF-E9Q9A9-F1	No comments found in the entry	¢ÙThe Gly at position 2 indicates N-myristoyl glycine.¢ÚAcetylation of Lys at position 417.	12396720##21142819	"Kakuta S, Shibata S, Iwakura Y.##Kristiansen H, Gad HH, Eskildsen-Larsen S, Despres P, Hartmann R."	"Genomic structure of the mouse 2',5'-oligoadenylate synthetase gene family.?##The oligoadenylate synthetase family: an ancient protein family with multiple antiviral activities. "
DRAVPR0077	MGNGESQLSSVPAQKLGWFIQEYLKPYEECQTLIDEMVNTICDVLQEPEQFPLVQGVAIGGSYGRKTVLRGNSDGTLVLFFSDLKQFQDQKRSQRDILDKTGDKLKFCLFTKWLKNNFEIQKSLDGFTIQVFTKNQRISFEVLAAFNALSLNDNPSPWIYRELKRSLDKTNASPGEFAVCFTELQQKFFDNRPGKLKDLILLIKHWHQQCQKKIKDLPSLSPYALELLTVYAWEQGCRKDNFDIAEGVRTVLELIKCQEKLCIYWMVNYNFEDETIRNILLHQLQSARPVILDPVDPTNNVSGDKICWQWLKKEAQTWLTSPNLDNELPAPSWNVLPAPLFTTPGHLLDKFIKEFLQPNKCFLEQIDSAVNIIRTFLKENCFRQSTAKIQIVRGGSTAKGTALKTGSDADLVVFHNSLKSYTSQKNERHKIVKEIHEQLKAFWREKEEELEVSFEPPKWKAPRVLSFSLKSKVLNESVSFDVLPAFNALGQLSSGSTPSPEVYAGLIDLYKSSDLPGGEFSTCFTVLQRNFIRSRPTKLKDLIRLVKHWYKECERKLKPKGSLPPKYALELLTIYAWEQGSGVPDFDTAEGFRTVLELVTQYQQLCIFWKVNYNFEDETVRKFLLSQLQKTRPVILDPAEPTGDVGGGDRWCWHLLAKEAKEWLSSPCFKDGTGNPIPPWKVPTMQTPGSCGARIHPIVNEMFSSRSHRILNNNSKRNF	719	2'-5'-oligoadenylate synthase 2	Homo sapiens (Human)	P29728	OAS2	None		[Ref.21142819]The 2'-5' oligoadenylate synthetases (OAS) can mediate the antiviral effect via the classical RNASEL-dependent pathway or an alternative antiviral pathway independent of RNASEL.	No predicted structure information available for the entry	No comments found in the entry	¢ÙThe Gly at position 2 indicates N-myristoyl glycine.¢ÚAcetylation of Lys at position 378.	21142819	"Kristiansen H, Gad HH, Eskildsen-Larsen S, Despres P, Hartmann R."	The oligoadenylate synthetase family: an ancient protein family with multiple antiviral activities. 
DRAVPR0078	MGCNVMMELDYGGRAAWLAFHITNFDRSDLETILRGARVCNTWQDQRLSVYLVGRDCNLLRPFVQAAKFIHNTRRGQTLTHWFTKNIVFSSTGQETEPPIDPTCELLVELISG	113	Non-structural protein 1	Murine pneumonia virus (strain 15) (MPV)	P28888	1C(NS1)	None		[Ref.19052095]NS1 may serve some inhibitory role in viral transcription and RNA replication.	No predicted structure information available for the entry		No modifications on the sequence.	19052095	"Buchholz UJ, Ward JM, Lamirande EW, Heinze B, Krempl CD, Collins PL. "	Deletion of nonstructural proteins NS1 and NS2 from pneumonia virus of mice attenuates viral replication and reduces pulmonary cytokine expression and disease.
DRAVPR0079	MDTLVEDDICILNHEKAHRREAVTPLSAYPGDESVASHFALVTAYEDIKKRLKDSEKENSFLKKRIRALEERLVGARADEETSSVGREQVNKAYHAYREVCIDRDNLKNQLEKINKDNSESLKMLNEQLQSKEVELLQLRTEVETQQVMRNLNPPSSSWEVEKLSCDLKIHGLEQELGLLRKECSDLRTELQKARQTGPPQEDILQGRDVIRPSLSREEHVPHQGLHHSDNMQHAYWELKREMSNLHLVTQVQAELLRKLKTSAAVKKACTPVGCVEDLGRDSTKLHLTNFTATYKRHPSLSPNGKAPCYAPSSPLPGDRKVFSDKAVLQSWTDNERLVPNDGADFPEHSSYGRNSLEDNSWVFPSPPKSSETAFGENKSKILPLSNLPPLHYLDQQNQNCLYKS	405	5-azacytidine-induced protein 2(Nap1)	Mus musculus (Mouse)	Q9QYP6	Azi2	None		[Ref.17568778]Nap1 binds TBK1 and IKBKE playing a role in antiviral innate immunity.	AF-Q9QYP6-F1		"Phosphorylation of Ser at position 331,366."	17568778	"Ryzhakov G, Randow F.?"	"SINTBAD, a novel component of innate antiviral immunity, shares a TBK1-binding domain with NAP1 and TANK."
DRAVPR0080	MNRHLWKSQLCEMVQPSGGPAADQDVLGEESPLGKPAMLHLPSEQGAPETLQRCLEENQELRDAIRQSNQILRERCEELLHFQASQREEKEFLMCKFQEARKLVERLGLEKLDLKRQKEQALREVEHLKRCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQVDQLRMQGQSVEAALRMERQAASEEKRKLAQLQVAYHQLFQEYDNHIKSSVVGSERKRGMQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQREYSKLKASCQESARIEDMRKRHVEVSQAPLPPAPAYLSSPLALPSQRRSPPEEPPDFCCPKCQYQAPDMDTLQIHVMECIE	419	NF-kappa-B essential modulator(NEMO)	Homo sapiens (Human)	Q9Y6K9	IKBKG	2JVX##3BRV##4BWN##6MI3		[Ref.20724660]TRIM23-mediated ubiquitin conjugation to NEMO is essential for TLR3- and RIG-I/MDA5-mediated antiviral innate and inflammatory responses.	AF-Q9Y6K9-F1		"Phosphorylation of Ser at position 31,43,68,85,376,387."	20724660	"Arimoto K, Funami K, Saeki Y, Tanaka K, Okawa K, Takeuchi O, Akira S, Murakami Y, Shimotohno K.?"	Polyubiquitin conjugation to NEMO by triparite motif protein 23 (TRIM23) is critical in antiviral defense.
DRAVPR0081	MAPEIHMTGPMCLIENTNGELVANPEALKILSAITQPVVVVAIVGLYRTGKSYLMNKLAGKNKGFSLGSTVKSHTKGIWMWCVPHPKKPEHTLVLLDTEGLGDVKKGDNQNDSWIFTLAVLLSSTLVYNSMGTINQQAMDQLYYVTELTHRIRSKSSPDENENEDSADFVSFFPDFVWTLRDFSLDLEADGQPLTPDEYLEYSLKLTQGTSQKDKNFNLPRLCIRKFFPKKKCFVFDLPIHRRKLAQLEKLQDEELDPEFVQQVADFCSYIFSNSKTKTLSGGIKVNGPRLESLVLTYINAISRGDLPCMENAVLALAQIENSAAVQKAIAHYDQQMGQKVQLPAETLQELLDLHRVSEREATEVYMKNSFKDVDHLFQKKLAAQLDKKRDDFCKQNQEASSDRCSALLQVIFSPLEEEVKAGIYSKPGGYCLFIQKLQDLEKKYYEEPRKGIQAEEILQTYLKSKESVTDAILQTDQILTEKEKEIEVECVKAESAQASAKMVEEMQIKYQQMMEEKEKSYQEHVKQLTEKMERERAQLLEEQEKTLTSKLQEQARVLKERCQGESTQLQNEIQKLQKTLKKKTKRYMSHKLKI	595	Guanylate-binding protein 3(GBP-3)	Homo sapiens (Human)	Q9H0R5	GBP3	None	influenza virus	[Ref.22106366]influenza virus:GBP-3 mediates anti-influenza activity through inhibition of viral transcription and replication.	AF-Q9H0R5-F1		No modifications on the sequence.	22106366	"Nordmann A, Wixler L, Boergeling Y, Wixler V, Ludwig S."	A new splice variant of the human guanylate-binding protein 3 mediates anti-influenza activity through inhibition of viral transcription and replication.
DRAVPR0082	MASEIHMTGPMCLIENTNGRLMANPEALKILSAITQPMVVVAIVGLYRTGKSYLMNKLAGKKKGFSLGSTVQSHTKGIWMWCVPHPKKPGHILVLLDTEGLGDVEKGDNQNDSWIFALAVLLSSTFVYNSIGTINQQAMDQLYYVTELTHRIRSKSSPDENENEVEDSADFVSFFPDFVWTLRDFSLDLEADGQPLTPDEYLTYSLKLKKGTSQKDETFNLPRLCIRKFFPKKKCFVFDRPVHRRKLAQLEKLQDEELDPEFVQQVADFCSYIFSNSKTKTLSGGIQVNGPRLESLVLTYVNAISSGDLPCMENAVLALAQIENSAAVQKAIAHYEQQMGQKVQLPTETLQELLDLHRDSEREAIEVFIRSSFKDVDHLFQKELAAQLEKKRDDFCKQNQEASSDRCSALLQVIFSPLEEEVKAGIYSKPGGYRLFVQKLQDLKKKYYEEPRKGIQAEEILQTYLKSKESMTDAILQTDQTLTEKEKEIEVERVKAESAQASAKMLQEMQRKNEQMMEQKERSYQEHLKQLTEKMENDRVQLLKEQERTLALKLQEQEQLLKEGFQKESRIMKNEIQDLQTKMRRRKACTIS	592	Guanylate-binding protein 1	Homo sapiens (Human)	P32455	GBP1	1DG3##1F5N##2B8W##6K1Z	influenza virus	[Ref.22106366]influenza virus:GBP-1 mediates anti-influenza activity through inhibition of viral transcription and replication.	AF-P32455-F1		The Cys at position 589 indicates S-farnesyl cysteine.	22106366	"Nordmann A, Wixler L, Boergeling Y, Wixler V, Ludwig S."	A new splice variant of the human guanylate-binding protein 3 mediates anti-influenza activity through inhibition of viral transcription and replication.
DRAVPR0083	MSGPCGEKPVLEASPTMSLWEFEDSHSRQGTPRPGQELAAEEASALELQMKVDFFRKLGYSSTEIHSVLQKLGVQADTNTVLGELVKHGTATERERQTSPDPCPQLPLVPRGGGTPKAPNLEPPLPEEEKEGSDLRPVVIDGSNVAMSHGNKEVFSCRGILLAVNWFLERGHTDITVFVPSWRKEQPRPDVPITDQHILRELEKKKILVFTPSRRVGGKRVVCYDDRFIVKLAYESDGIVVSNDTYRDLQGERQEWKRFIEERLLMYSFVNDKFMPPDDPLGRHGPSLDNFLRKKPLTLEHRKQPCPYGRKCTYGIKCRFFHPERPSCPQRSVADELRANALLSPPRAPSKDKNGRRPSPSSQSSSLLTESEQCSLDGKKLGAQASPGSRQEGLTQTYAPSGRSLAPSGGSGSSFGPTDWLPQTLDSLPYVSQDCLDSGIGSLESQMSELWGVRGGGPGEPGPPRAPYTGYSPYGSELPATAAFSAFGRAMGAGHFSVPADYPPAPPAFPPREYWSEPYPLPPPTSVLQEPPVQSPGAGRSPWGRAGSLAKEQASVYTKLCGVFPPHLVEAVMGRFPQLLDPQQLAAEILSYKSQHPSE	599	Endoribonuclease ZC3H12A(MCPIP1)	Homo sapiens (Human)	Q5D1E8	ZC3H12A?	3V32##3V33##3V34	"HIV,JEV,DENV"	[Ref.24191027]Human immunodeficiency virus type 1(HIV-1):MCPIP1 exhibits antiviral activity against HIV-1 in lymphocytes by decreasing the abundance of HIV-1 viral RNA species.##[Ref.23355615]Japanese encephalitis virus (JEV)/dengue virus (DENV):MCPIP1 inhibits virus replication by binding to viral RNA.	AF-Q5D1E8-F1		"Phosphorylation of Ser at position 99,344,438,442."	24191027##23355615	"Liu S, Qiu C, Miao R, Zhou J, Lee A, Liu B, Lester SN, Fu W, Zhu L, Zhang L, Xu J, Fan D, Li K, Fu M, Wang T.?##Lin RJ, Chien HL, Lin SY, Chang BL, Yu HP, Tang WC, Lin YL. "	MCPIP1 restricts HIV infection and is rapidly degraded in activated CD4+ T cells.##MCPIP1 ribonuclease exhibits broad-spectrum antiviral effects through viral RNA binding and degradation.
DRAVPR0084	MMDLELPPPGLPSQQDMDLIDILWRQDIDLGVSREVFDFSQRRKEYELEKQKKLEKERQEQLQKEQEKAFFAQLQLDEETGEFLPIQPAQHIQSETSGSANYSQVAHIPKSDALYFDDCMQLLAQTFPFVDDNEVSSATFQSLVPDIPGHIESPVFIATNQAQSPETSVAQVAPVDLDGMQQDIEQVWEELLSIPELQCLNIENDKLVETTMVPSPEAKLTEVDNYHFYSSIPSMEKEVGNCSPHFLNAFEDSFSSILSTEDPNQLTVNSLNSDATVNTDFGDEFYSAFIAEPSISNSMPSPATLSHSLSELLNGPIDVSDLSLCKAFNQNHPESTAEFNDSDSGISLNTSPSVASPEHSVESSSYGDTLLGLSDSEVEELDSAPGSVKQNGPKTPVHSSGDMVQPLSPSQGQSTHVHDAQCENTPEKELPVSPGHRKTPFTKDKHSSRLEAHLTRDELRAKALHIPFPVEKIINLPVVDFNEMMSKEQFNEAQLALIRDIRRRGKNKVAAQNCRKRKLENIVELEQDLDHLKDEKEKLLKEKGENDKSLHLLKKQLSTLYLEVFSMLRDEDGKPYSPSEYSLQQTRDGNVFLVPKSKKPDVKKN	605	"Nuclear factor erythroid 2-related factor 2(HEBP1,Nrf-2)"	Homo sapiens (Human)	Q16236	NFE2L2(NRF2)	2FLU##2LZ1##4IFL##5WFV##7K2A##7K2E##7O7B	SARS-CoV-2	"[Ref.33009401]SARS-CoV2:when NRF2 was activated,  it limits the release of pro-inflammatory cytokines in response to SARS-CoV-2 infection inhibits SARS-CoV-2 replication."	AF-Q16236-F1		"¢ÙPhosphorylation of Ser at position 40,215.¢ÚGlycosylation of Lys at position 462,472,487,574.¢ÛGlycosylation of Arg at position 499,569.¢ÜThe Lys at position 596 and 599 indicates N6-acetyllysine."	33009401	"Olagnier D, Farahani E, Thyrsted J, Blay-Cadanet J, Herengt A, Idorn M, Hait A, Hernaez B, Knudsen A, Iversen MB, Schilling M, J?rgensen SE, Thomsen M, Reinert LS, Lappe M, Hoang HD, Gilchrist VH, Hansen AL, Ottosen R, Nielsen CG, M?ller C, van der Horst D, Peri S, Balachandran S, Huang J, Jakobsen M, Svenningsen EB, Poulsen TB, Bartsch L, Thielke AL, Luo Y, Alain T, Rehwinkel J, Alcam¨ª A, Hiscott J, Mogensen TH, Paludan SR, Holm CK."	SARS-CoV2-mediated suppression of NRF2-signaling reveals potent antiviral and anti-inflammatory activity of 4-octyl-itaconate and dimethyl fumarate.?
DRAVPR0085	MALSFSLLMAVLVLSYKSICSLGCDLPQTHSLGNRRALILLAQMGRISHFSCLKDRHDFGFPEEEFDGHQFQKAQAISVLHEMIQQTFNLFSTEDSSAAWEQSLLEKFSTELYQQLNDLEACVIQEVGVEETPLMNEDSILAVRKYFQRITLYLTEKKYSPCAWEVVRAEIMRSLSFSTNLQKRLRRKD	189	Interferon alpha-4	Homo sapiens (Human)	P05014	IFNA4	None		[Ref.9334213]IFN-alpha have antiviral activities.	AF-P05014-F1		"There are two disulfide bonds between Cys24 and Cys122, Cys52 and Cys162."	9334213	"Domanski P, Fish E, Nadeau OW, Witte M, Platanias LC, Yan H, Krolewski J, Pitha P, Colamonici OR."	A region of the beta subunit of the interferon alpha receptor different from box 1 interacts with Jak1 and is sufficient to activate the Jak-Stat pathway and induce an antiviral state.
DRAVPR0086	MALTFALLVALLVLSCKSSCSVGCDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE	188	Interferon alpha-2	Homo sapiens (Human)	P01563	"IFNA2(IFNA2A, IFNA2B, IFNA2C)"	1ITF##2HYM##2LAG##3S9D##4Z5R		[Ref.9822609]IFN-alpha have antiviral activities.	AF-P01563-F1		"¢ÙThere are two disulfide bonds between Cys24 and Cys121, Cys52 and Cys161.¢ÚGlycosylation of Thr at position 129."	9822609	"Mari¨¦ I, Durbin JE, Levy DE.?"	Differential viral induction of distinct interferon-alpha genes by positive feedback through interferon regulatory factor-7.
DRAVPR0087	MTNKCLLQIALLLCFSTTALSMSYNLLGFLQRSSNFQCQKLLWQLNGRLEYCLKDRMNFDIPEEIKQLQQFQKEDAALTIYEMLQNIFAIFRQDSSSTGWNETIVENLLANVYHQINHLKTVLEEKLEKEDFTRGKLMSSLHLKRYYGRILHYLKAKEYSHCAWTIVRVEILRNFYFINRLTGYLRN	187	Interferon beta	Homo sapiens (Human)	P01574	IFNB1	1AU1		[Ref.6171735]IFN-beta have antiviral activities.	AF-P01574-F1		¢ÙThere is a disulfide bond between Cys52 and Cys162.¢ÚPhosphorylation of Thr at position 24.¢ÛGlycosylation of Asn at position 101.	6171735	"Shepard HM, Leung D, Stebbing N, Goeddel DV."	A single amino acid change in IFN-beta1 abolishes its antiviral activity.
DRAVPR0088	MAASKPVEAAVVAAAVPSSGSGVGGGGTAGPGTGGLPRWQLALAVGAPLLLGAGAIYLWSRQQRRREARGRGDASGLKRNSERKTPEGRASPAPGSGHPEGPGAHLDMNSLDRAQAAKNKGNKYFKAGKYEQAIQCYTEAISLCPTEKNVDLSTFYQNRAAAFEQLQKWKEVAQDCTKAVELNPKYVKALFRRAKAHEKLDNKKECLEDVTAVCILEGFQNQQSMLLADKVLKLLGKEKAKEKYKNREPLMPSPQFIKSYFSSFTDDIISQPMLKGEKSDEDKDKEGEALEVKENSGYLKAKQYMEEENYDKIISECSKEIDAEGKYMAEALLLRATFYLLIGNANAAKPDLDKVISLKEANVKLRANALIKRGSMYMQQQQPLLSTQDFNMAADIDPQNADVYHHRGQLKILLDQVEEAVADFDECIRLRPESALAQAQKCFALYRQAYTGNNSSQIQAAMKGFEEVIKKFPRCAEGYALYAQALTDQQQFGKADEMYDKCIDLEPDNATTYVHKGLLQLQWKQDLDRGLELISKAIEIDNKCDFAYETMGTIEVQRGNMEKAIDMFNKAINLAKSEMEMAHLYSLCDAAHAQTEVAKKYGLKPPTL	608	Mitochondrial import receptor subunit TOM70 	Homo sapiens (Human)	O94826	TOMM70 	7DHG##7KDT	SeV	"[Ref.20628368]Tom70 is found to interact specifically with MAVS during RNA virus infection and plays an essential role in the antiviral response.##[Ref.25609812]Sendai virus:Tom70 recruits IRF3/Bax complex to the mitochondrial outer membrane through Hsp90, which thus induces the release of cytochrome c into the cytosol, initiating virus-induced apoptosis."	AF-O94826-F1		"¢ÙPhosphorylation of Ser at position 91,96,434.¢ÚThe N-terminal is acetylation.¢ÛThe Arg at position 71 indicates Omega-N-methylarginine.¢ÜThe Lys at position 185 indicates N6-acetyllysine."	20628368##25609812	"Liu XY, Wei B, Shi HX, Shan YF, Wang C.?##Wei B, Cui Y, Huang Y, Liu H, Li L, Li M, Ruan KC, Zhou Q, Wang C. "	Tom70 mediates activation of interferon regulatory factor 3 on mitochondria.##Tom70 mediates Sendai virus-induced apoptosis on mitochondria. 
DRAVPR0089	MAGDLSAGFFMEELNTYRQKQGVVLKYQELPNSGPPHDRRFTFQVIIDGREFPEGEGRSKKEAKNAAAKLAVEILNKEKKAVSPLLLTTTNSSEGLSMGNYIGLINRIAQKKRLTVNYEQCASGVHGPEGFHYKCKMGQKEYSIGTGSTKQEAKQLAAKLAYLQILSEETSVKSDYLSSGSFATTCESQSNSLVTSTLASESSSEGDFSADTSEINSNSDSLNSSSLLMNGLRNNQRKAKRSLAPRFDLPDMKETKYTVDKRFGMDFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAEREVKALAKLDHVNIVHYNGCWDGFDYDPETSDDSLESSDYDPENSKNSSRSKTKCLFIQMEFCDKGTLEQWIEKRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFETSKFFTDLRDGIISDIFDKKEKTLLQKLLSKKPEDRPNTSEILRTLTVWKKSPEKNERHTC	551	"Interferon-induced, double-stranded RNA-activated protein kinase(PKA)"	Homo sapiens (Human)	P19525	EIF2AK2	1QU6##2A19##2A1A##3UIU##6D3K##6D3L	"HCV,MeV"	[Ref.23399035]Hepatitis C virus(HCV):PKA inhibits the replication od HCV in Huh7.5.1 cells.##[Ref.23115276]Measles virus(MeV):PKA exhibits antiviral activity against MeV.	AF-P19525-F1		"¢ÙPhosphorylation of Ser at position 83,242,456,542.¢ÚThe N-terminal is acetylation.¢ÛPhosphorylation of Thr at position 88,89,90,255,258,446,451.¢ÜPhosphorylation of Tyr at position 101,162,293."	23399035##23115276	"Zhang L, Alter HJ, Wang H, Jia S, Wang E, Marincola FM, Shih JW, Wang RY.?##Okonski KM, Samuel CE."	The modulation of hepatitis C virus 1a replication by PKR is dependent on NF-kB mediated interferon beta response in Huh7.5.1 cells.##Stress granule formation induced by measles virus is protein kinase PKR dependent and impaired by RNA adenosine deaminase ADAR1.
DRAVPR0090	MGIVEPGCGDMLTGTEPMPSDEGRGPGADQQHRFFYPEPGAQDPTDRRAGSSLGTPYSGGALVPAAPGRFLGSFAYPPRAQVAGFPGPGEFFPPPAGAEGYPPVDGYPAPDPRAGLYPGPREDYALPAGLEVSGKLRVALSNHLLWSKFNQHQTEMIITKQGRRMFPFLSFTVAGLEPTSHYRMFVDVVLVDQHHWRYQSGKWVQCGKAEGSMPGNRLYVHPDSPNTGAHWMRQEVSFGKLKLTNNKGASNNVTQMIVLQSLHKYQPRLHIVEVNDGEPEAACSASNTHVFTFQETQFIAVTAYQNAEITQLKIDNNPFAKGFRENFESMYASVDTSVPSPPGPNCQLLGGDPFSPLLSNQYPVPSRFYPDLPGQPKDMISQPYWLGTPREHSYEAEFRAVSMKPTLLPSAPGPTVPYYRGQDVLAPGAGWPVAPQYPPKMSPAGWFRPMRTLPMDPGLGSSEEQGSSPSLWPEVTSLQPEPSDSGLGEGDTKRRRISPYPSSGDSSSPAGAPSPFDKETEGQFYNYFPN	530	T-box transcription factor TBX21	Mus musculus (Mouse)	Q9JKD8	Tbx21(Tbet)	5T1J		[Ref.27430722]B cell specific loss of T-bet prevents control of persisting viral infection.T-bet is a universal controller of antiviral immunity across multiple immune lineages.	AF-Q9JKD8-F1		"¢ÙPhosphorylation of Ser at position 52,224,508.¢ÚPhosphorylation of Tyr at position 76,117,219,265,304,525.¢ÛPhosphorylation of Thr at position 55,302."	27430722	"Barnett BE, Staupe RP, Odorizzi PM, Palko O, Tomov VT, Mahan AE, Gunn B, Chen D, Paley MA, Alter G, Reiner SL, Lauer GM, Teijaro JR, Wherry EJ.?"	Cutting Edge: B Cell-Intrinsic T-bet Expression Is Required To Control Chronic Viral Infection.?
DRAVPR0091	MSSGLRAADFPRWKRHIAEELRRRDRLQRQAFEEIILQYTKLLEKSDLHSVLTQKLQAEKHDMPNRHEISPGHDGAWNDSQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAVSRAATKRLSQPAGGLLDSITNIFGRRSVSSIPVPQDIMDTHPASGKDVRVPTTASYVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCEFKGSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTVFAGSSCNDIVCTEQCVMSGHFDKKIRFWDIRSESVVREMELLGKITALDLNPERTELLSCSRDDLLKVIDLRTNAVKQTFSAPGFKCGSDWTRVVFSPDGSYVAAGSAEGSLYVWSVLTGKVEKVLSKQHSSSINAVAWAPSGLHVVSVDKGSRAVLWAQP	607	Autophagy-related protein 16-1	Mus musculus (Mouse)	Q8C0J2	Atg16l1 	"6SUR##	6Y09##6ZAY"	IAV	[Ref.33586810]Influenza A virus(IAV):Non©\canonical autophagy limits IAV infection independently of phagocytic cells.	AF-Q8C0J2-F1		"Phosphorylation of Ser at position 139,269,287."	33586810	"Wang Y, Sharma P, Jefferson M, Zhang W, Bone B, Kipar A, Bitto D, Coombes JL, Pearson T, Man A, Zhekova A, Bao Y, Tripp RA, Carding SR, Yamauchi Y, Mayer U, Powell PP, Stewart JP, Wileman T.?"	Non-canonical autophagy functions of ATG16L1 in epithelial cells limit lethal infection by influenza A virus.
DRAVPR0092	MEGSKTSNNSTMQVSFVCQRCSQPLKLDTSFKILDRVTIQELTAPLLTTAQAKPGETQEEETNSGEEPFIETPRQDGVSRRFIPPARMMSTESANSFTLIGEASDGGTMENLSRRLKVTGDLFDIMSGQTDVDHPLCEECTDTLLDQLDTQLNVTENECQNYKRCLEILEQMNEDDSEQLQMELKELALEEERLIQELEDVEKNRKIVAENLEKVQAEAERLDQEEAQYQREYSEFKRQQLELDDELKSVENQMRYAQTQLDKLKKTNVFNATFHIWHSGQFGTINNFRLGRLPSVPVEWNEINAAWGQTVLLLHALANKMGLKFQRYRLVPYGNHSYLESLTDKSKELPLYCSGGLRFFWDNKFDHAMVAFLDCVQQFKEEVEKGETRFCLPYRMDVEKGKIEDTGGSGGSYSIKTQFNSEEQWTKALKFMLTNLKWGLAWVSSQFYNK	450	Beclin-1	Homo sapiens (Human)	Q14457	BECN1	2P1L##4DDP##5HHE##5VAY##6HOI##7BL1	SBV	[Ref.9765397]Sindbis virus:Beclin protects against infection of SBV.	AF-Q14457-F1		"¢ÙPhosphorylation of Ser at position 15,30,90,93,96,.¢ÚThe N-terminal is acetylation.¢ÛPhosphorylation of Thr at position 119."	9765397	"Liang XH, Kleeman LK, Jiang HH, Gordon G, Goldman JE, Berry G, Herman B, Levine B."	"Protection against fatal Sindbis virus encephalitis by beclin, a novel Bcl-2-interacting protein."
DRAVPR0093	MGENADGDQVMENLLQLRCHFTWKLLFENNDIPDLEVRISEQVQFLDIKNPLGMHNLLAYVRHLKGQQDEALQSLKEAEALIQSEQLSKRSLATWGNCAWLHYHRGSLAEAQIYLDKVEKVCKEFSSPFRYRLECAEMDCEEGWALLKCGGGNYKQAMACFAKALKVEPENPEYNTGYAVVAYRQDLDDNFISLEPLRKAVRLNPEDPYLKVLLALKLQDLGEHVEAEAHIEEALSSTSCQSYVIRYAAKYFRRKHRVDKALHLLNRALQASPSSGYLHYQKGLCYKQQISQLRTSRNRQPRRQDNVQELAQQAIHEFQETLKLRPTFEMAYVCMAEVQAEIHQYEEAERNFQKALNNKTLVAHIEQDIHLRYGRFLQFHKQSEDKAITLYLKGLKVEEKSFAWRKLLTALEKVAERRVCQNVHLVESTSLLGLVYKLKGQEKNALFYYEKALRLTGEMNPAF	463	Interferon-induced protein with tetratricopeptide repeats 1	Mus musculus (Mouse)	Q64282	Ifit1	None	WNV	[Ref.22589727]West Nile virus(WNV):Ifit1 restricts replication of WNV lacking 2¡ä-O methylation in subsets of primary cells.	AF-Q64282-F1		No modifications on the sequence.	22589727	"Szretter KJ, Daniels BP, Cho H, Gainey MD, Yokoyama WM, Gale M Jr, Virgin HW, Klein RS, Sen GC, Diamond MS."	2'-O methylation of the viral mRNA cap by West Nile virus evades ifit1-dependent and -independent mechanisms of host restriction in vivo.?
DRAVPR0094	MSTNGDDHQVKDSLEQLRCHFTWELSIDDDEMPDLENRVLDQIEFLDTKYSVGIHNLLAYVKHLKGQNEEALKSLKEAENLMQEEHDNQANVRSLVTWGNFAWMYYHMGRLAEAQTYLDKVENICKKLSNPFRYRMECPEIDCEEGWALLKCGGKNYERAKACFEKVLEVDPENPESSAGYAISAYRLDGFKLATKNHKPFSLLPLRQAVRLNPDNGYIKVLLALKLQDEGQEAEGEKYIEEALANMSSQTYVFRYAAKFYRRKGSVDKALELLKKALQETPTSVLLHHQIGLCYKAQMIQIKEATKGQPRGQNREKLDKMIRSAIFHFESAVEKKPTFEVAHLDLARMYIEAGNHRKAEENFQKLLCMKPVVEETMQDIHFHYGRFQEFQKKSDVNAIIHYLKAIKIEQASLTRDKSINSLKKLVLRKLRRKALDLESLSLLGFVYKLEGNMNEALEYYERALRLAADFENSVRQGP	478	Interferon-induced protein with tetratricopeptide repeats 1(P56)	Homo sapiens (Human)	P09914	IFIT1	4HOU##5UDI##6C6K	"HPV,HCV"	[Ref.19008854]human papillomaviruses(HPV):P56 inhibits the DNA helicase activity of E1 and E1-mediated HPV DNA replication. ##[Ref.21976647]Hepatitis C virus(HCV):IFITM1 inhibits HCV replication in IHH or Huh7 cells	AF-P09914-F1		No modifications on the sequence.	19008854##21976647	"Terenzi F, Saikia P, Sen GC.##Raychoudhuri A, Shrivastava S, Steele R, Kim H, Ray R, Ray RB. "	"Interferon-inducible protein, P56, inhibits HPV DNA replication by binding to the viral protein E1.##ISG56 and IFITM1 proteins inhibit hepatitis C virus replication. "
DRAVPR0095	MAWDLKVKMLGGNDFLVSVTNSMTVSELKKQIAQKIGVPAFQQRLAHQTAVLQDGLTLSSLGLGPSSTVMLVVQNCSEPLSILVRNERGHSNIYEVFLTQTVDTLKKKVSQREQVHEDQFWLSFEGRPMEDKELLGEYGLKPQCTVIKHLRLRGGGGDQCA	161	Ubiquitin-like protein ISG15	Mus musculus (Mouse)	Q64339	Isg15	5CHF##5TL7##6YVA	"SBV,HSV-1"	[Ref.17227866]Sindbs virus(SBV)/herpes virus type 1 (HSV-1):ISG15 inhibits the infection of SBV and HSV-1.	AF-Q64339-F1		The Cys at position 144 and 155 indicates S-nitrosocysteine.	16254333##17227866	"Lenschow DJ, Giannakopoulos NV, Gunn LJ, Johnston C, O'Guin AK, Schmidt RE, Levine B, Virgin HW 4th.##Lenschow DJ, Lai C, Frias-Staheli N, Giannakopoulos NV, Lutz A, Wolff T, Osiak A, Levine B, Schmidt RE, Garc¨ªa-Sastre A, Leib DA, Pekosz A, Knobeloch KP, Horak I, Virgin HW 4th. "	"Identification of interferon-stimulated gene 15 as an antiviral molecule during Sindbis virus infection in vivo.##IFN-stimulated gene 15 functions as a critical antiviral molecule against influenza, herpes, and Sindbis viruses. "
DRAVPR0096	MHRKHLQEIPDLSSNVATSFTWGWDSSKTSELLSGMGVSALEKEEPDSENIPQELLSNLGHPESPPRKRLKSKGSDKDFVIVRRPKLNRENFPGVSWDSLPDELLLGIFSCLCLPELLKVSGVCKRWYRLASDESLWQTLDLTGKNLHPDVTGRLLSQGVIAFRCPRSFMDQPLAEHFSPFRVQHMDLSNSVIEVSTLHGILSQCSKLQNLSLEGLRLSDPIVNTLAKNSNLVRLNLSGCSGFSEFALQTLLSSCSRLDELNLSWCFDFTEKHVQVAVAHVSETITQLNLSGYRKNLQKSDLSTLVRRCPNLVHLDLSDSVMLKNDCFQEFFQLNYLQHLSLSRCYDIIPETLLELGEIPTLKTLQVFGIVPDGTLQLLKEALPHLQINCSHFTTIARPTIGNKKNQEIWGIKCRLTLQKPSCL	424	S-phase kinase-associated protein 2	Homo sapiens (Human)	Q13309	SKP2	1FQV##1FS2##2AST##7B5R	HCV	[Ref.27194766]Hepatitis C virus (HCV):SKP2 has an antiviral activity towards HCV through the ubiquitin-mediated proteasomal degradation of hepatitis C virus non-structural protein 5A.	AF-Q13309-F1		"¢ÙPhosphorylation of Ser at position 64,72,75,179.¢ÚThe Lys at position 68 and 71 indicates N6-acetyllysine."	27194766	"Xue B, Yang D, Wang J, Xu Y, Wang X, Qin Y, Tian R, Chen S, Xie Q, Liu N, Zhu H."	?ISG12a Restricts Hepatitis C Virus Infection through the Ubiquitination-Dependent Degradation Pathway.
DRAVPR0097	MGAVLGVFSLASWVPCLCSGASCLLCSCCPNSKNSTVTRLIYAFILLLSTVVSYIMQRKEMETYLKKIPGFCEGGFKIHEADINADKDCDVLVGYKAVYRISFAMAIFFFVFSLLMFKVKTSKDLRAAVHNGFWFFKIAALIGIMVGSFYIPGGYFSSVWFVVGMIGAALFILIQLVLLVDFAHSWNESWVNRMEEGNPRLWYAALLSFTSAFYILSIICVGLLYTYYTKPDGCTENKFFISINLILCVVASIISIHPKIQEHQPRSGLLQSSLITLYTMYLTWSAMSNEPDRSCNPNLMSFITRITAPTLAPGNSTAVVPTPTPPSKSGSLLDSDNFIGLFVFVLCLLYSSIRTSTNSQVDKLTLSGSDSVILGDTTTSGASDEEDGQPRRAVDNEKEGVQYSYSLFHLMLCLASLYIMMTLTSWYSPDAKFQSMTSKWPAVWVKISSSWVCLLLYVWTLVAPLVLTSRDFS	473	Serine incorporator 3	Homo sapiens (Human)	Q13530	SERINC3	None	HIV-1	[Ref.26416733]Human immunodeficiency virus type 1(HIV-1):SERINC3 restricts HIV-1 infectivity and replication.	AF-Q13530-F1		¢ÙPhosphorylation of Ser at position 371.¢ÚGlycosylation of Asn at position 34.	26416733	"Usami Y, Wu Y, G?ttlinger HG.?"	SERINC3 and SERINC5 restrict HIV-1 infectivity and are counteracted by Nef.
DRAVPR0098	MSAQCCAGQLACCCGSAGCSLCCDCCPRIRQSLSTRFMYALYFILVVVLCCIMMSTTVAHKMKEHIPFFEDMCKGIKAGDTCEKLVGYSAVYRVCFGMACFFFIFCLLTLKINNSKSCRAHIHNGFWFFKLLLLGAMCSGAFFIPDQDTFLNAWRYVGAVGGFLFIGIQLLLLVEFAHKWNKNWTAGTASNKLWYASLALVTLIMYSIATGGLVLMAVFYTQKDSCMENKILLGVNGGLCLLISLVAISPWVQNRQPHSGLLQSGVISCYVTYLTFSALSSKPAEVVLDEHGKNVTICVPDFGQDLYRDENLVTILGTSLLIGCILYSCLTSTTRSSSDALQGRYAAPELEIARCCFCFSPGGEDTEEQQPGKEGPRVIYDEKKGTVYIYSYFHFVFFLASLYVMMTVTNWFNHVRSAFHLLP	423	Serine incorporator 5 	Homo sapiens (Human)	Q86VE9	SERINC5	None	HIV-1	[Ref.26416733]Human immunodeficiency virus type 1(HIV-1):SERINC5 restricts HIV-1 infectivity and replication.	AF-Q86VE9-F1		Glycosylation of Asn at position 113 and 183.	26416733	"Usami Y, Wu Y, G?ttlinger HG.?"	SERINC3 and SERINC5 restrict HIV-1 infectivity and are counteracted by Nef.
DRAVPR0099	MAWASSFDAFFKNFKRESKIISEYDITLIMTYIEENKLQKAVSVIEKVLRDIESAPLHIAVTGETGAGKSTFINTLRGVGHEEKGAAPTGAIETTMKRTPYPHPKLPNVTIWDLPGIGTTNFTPQNYLTEMKFGEYDFFIIISATRFKENDAQLAKAIAQMGMNFYFVRTKIDSDLDNEQKFKPKSFNKEEVLKNIKDYCSNHLQESLDSEPPVFLVSNVDISKYDFPKLETKLLQDLPAHKRHVFSLSLQSLTEATINYKRDSLKQKVFLEAMKAGALATIPLGGMISDILENLDETFNLYRSYFGLDDASLENIAQDLNMSVDDFKVHLRFPHLFAEHNDESLEDKLFKYIKHISSVTGGPVAAVTYYRMAYYLQNLFLDTAANDAIALLNSKALFEKKVGPYISEPPEYWEA	415	T-cell-specific guanine nucleotide triphosphate-binding protein 2	Mus musculus (Mouse)	Q3T9E4	Tgtp2	7VES##7VEX	VSV	"[Ref.9725230]vesicular stomatitis virus (VSV):TGTP conferred an antiviral state for the negative strand RNA virus, VSV."	AF-Q3T9E4-F1		No modifications on the sequence.	9725230	"Carlow DA, Teh SJ, Teh HS.?"	"Specific antiviral activity demonstrated by TGTP, a member of a new family of interferon-induced GTPases."
DRAVPR0100	MAWASSFDAFFKNFKRESKIISEYDITLIMTYIEENKLQKAVSVIEKVLRDIESAPLHIAVTGETGAGKSTFINTLRGVGHEEKGAAPTGAIETTMKRTPYPHPKLPNVTIWDLPGIGTTNFTPQNYLTEMKFGEYDFFIIISATRFKENDAQLAKAIAQMGMNFYFVRTKIDSDLDNEQKFKPKSFNKEEVLKNIKDYCSNHLQESLDSEPPVFLVSNVDISKYDFPKLETKLLQDLPAHKRHVFSLSLQSLTEATINYKRDSLKQKVFLEAMKAGALATIPLGGMISDILENLDETFNLYRSYFGLDDASLENIAQDLNMSVDDFKVHLRFPHLFAEHNDESLEDKLFKYIKHISSVTGGPVAAVTYYRMAYYLQNLFLDTAANDAIALLNSKALFEKKVGPYISEPPEYWEA	415	T-cell-specific guanine nucleotide triphosphate-binding protein 1	Mus musculus (Mouse)	Q62293	Tgtp1	None	VSV	"[Ref.9725230]vesicular stomatitis virus (VSV):TGTP conferred an antiviral state for the negative strand RNA virus, VSV."	AF-Q62293-F1		No modifications on the sequence.	9725230	"Carlow DA, Teh SJ, Teh HS.?"	"Specific antiviral activity demonstrated by TGTP, a member of a new family of interferon-induced GTPases."
DRAVPR0101	MAAPDLSTNLQEEATCAICLDYFTDPVMTDCGHNFCRECIRRCWGQPEGPYACPECRELSAQRNLRPNRPLAKMAEMARRLHPPSPVPQGVCAAHREPLTTFCGDDLSLLCPICERSEHWTHRVRPLQEAADDLKGRLEKSLEHLRKQMEDAMLFQAQAEETCALWQKMVESQRQNVLGEFERLRRLLAEEEQQLLQKLEEEELEVLPRLREGAARLGQQSTQLAALISELESRCQLPALGLLQDIKDALCRVQDVKLQPPAVVPMELRTVCRVPGLVETLRRFRGDITLDPDTANPELVLSEDRRSVQRGEQRQALPDNPERFDPGPCVLGQERITSGRHYWEVEVGDQTSWALGVCKETANRKEKGELSAGNGFWILVFLGSFYNSNEPAFSPLRDPPKRVGIFLDYEAGHLSFYSATDGSLLFIFPETLFSGTLRPLFSPLSSSPTPMTICRLIGVSGDTLGPQ	467	E3 ubiquitin-protein ligase TRIM11	Mus musculus (Mouse)	Q99PQ2	Trim11	None	HIV-1	[Ref.18248090]Human immunodeficiency virus type 1(HIV-1):TRIM11 inhibits the virus entry of HIV	AF-Q99PQ2-F1		Phosphorylation of Ser at position 85.	18248090	"Uchil PD, Quinlan BD, Chan WT, Luna JM, Mothes W."	TRIM E3 ligases interfere with early and late stages of the retroviral life cycle.?
DRAVPR0102	MAELCPLAEELSCSICLEPFKEPVTTPCGHNFCGSCLNETWAVQGSPYLCPQCRAVYQARPQLHKNTVLCNVVEQFLQADLAREPPADVWTPPARASAPSPNAQVACDHCLKEAAVKTCLVCMASFCQEHLQPHFDSPAFQDHPLQPPVRDLLRRKCSQHNRLREFFCPEHSECICHICLVEHKTCSPASLSQASADLEATLRHKLTVMYSQINGASRALDDVRNRQQDVRMTANRKVEQLQQEYTEMKALLDASETTSTRKIKEEEKRVNSKFDTIYQILLKKKSEIQTLKEEIEQSLTKRDEFEFLEKASKLRGISTKPVYIPEVELNHKLIKGIHQSTIDLKNELKQCIGRLQEPTPSSGDPGEHDPASTHKSTRPVKKVSKEEKKSKKPPPVPALPSKLPTFGAPEQLVDLKQAGLEAAAKATSSHPNSTSLKAKVLETFLAKSRPELLEYYIKVILDYNTAHNKVALSECYTVASVAEMPQNYRPHPQRFTYCSQVLGLHCYKKGIHYWEVELQKNNFCGVGICYGSMNRQGPESRLGRNSASWCVEWFNTKISAWHNNVEKTLPSTKATRVGVLLNCDHGFVIFFAVADKVHLMYKFRVDFTEALYPAFWVFSAGATLSICSPK	630	E3 ubiquitin/ISG15 ligase TRIM25	Homo sapiens (Human)	Q14258	TRIM25	4CFG##5EYA##5NT1##6FLN		[Ref.18248090]TRIM25 inhibits viral release.	AF-Q14258-F1		¢ÙThe Lys at position 273 and 567 indicates N6-acetyllysine.¢ÚPhosphorylation of Tyr at position 278.¢ÛPhosphorylation of Thr at position 91.¢ÜPhosphorylation of Ser at position 100.	18248090	"Uchil PD, Quinlan BD, Chan WT, Luna JM, Mothes W."	TRIM E3 ligases interfere with early and late stages of the retroviral life cycle.?
DRAVPR0103	MAASAAAASAAAASAASGSPGPGEGSAGGEKRSTAPSAAASASASAAASSPAGGGAEALELLEHCGVCRERLRPEREPRLLPCLHSACSACLGPAAPAAANSSGDGGAAGDGTVVDCPVCKQQCFSKDIVENYFMRDSGSKAATDAQDANQCCTSCEDNAPATSYCVECSEPLCETCVEAHQRVKYTKDHTVRSTGPAKSRDGERTVYCNVHKHEPLVLFCESCDTLTCRDCQLNAHKDHQYQFLEDAVRNQRKLLASLVKRLGDKHATLQKSTKEVRSSIRQVSDVQKRVQVDVKMAILQIMKELNKRGRVLVNDAQKVTEGQQERLERQHWTMTKIQKHQEHILRFASWALESDNNTALLLSKKLIYFQLHRALKMIVDPVEPHGEMKFQWDLNAWTKSAEAFGKIVAERPGTNSTGPAPMAPPRAPGPLSKQGSGSSQPMEVQEGYGFGSGDDPYSSAEPHVSGVKRSRSGEGEVSGLMRKVPRVSLERLDLDLTADSQPPVFKVFPGSTTEDYNLIVIERGAAAAATGQPGTAPAGTPGAPPLAGMAIVKEEETEAAIGAPPTATEGPETKPVLMALAEGPGAEGPRLASPSGSTSSGLEVVAPEGTSAPGGGPGTLDDSATICRVCQKPGDLVMCNQCEFCFHLDCHLPALQDVPGEEWSCSLCHVLPDLKEEDGSLSLDGADSTGVVAKLSPANQRKCERVLLALFCHEPCRPLHQLATDSTFSLDQPGGTLDLTLIRARLQEKLSPPYSSPQEFAQDVGRMFKQFNKLTEDKADVQSIIGLQRFFETRMNEAFGDTKFSAVLVEPPPMSLPGAGLSSQELSGGPGDGP	835	Transcription intermediary factor 1-beta	Homo sapiens (Human)	Q13263	TRIM28	1FP0##2RO1##6H3A##6QU1	MLV	[Ref.18248090]murine leukemia virus (MLV):TRIM28 restricts MLV in cells of germline origin by inhibiting LTR-driven transcription.	AF-Q13263-F1		"¢ÙThe Lys at position 266,304,340,377,770,779 indicates N6-acetyllysine.¢ÚPhosphorylation of Tyr at position 755.¢ÛPhosphorylation of Thr at position 498,541.¢ÜPhosphorylation of Ser at position 19,26,50,138,417,437,439,453,471,473,479,489,501,594,683,689,697,752,757,784,824.¢ÝThe N-terminal is acetylation."	18248090##18389079	"Uchil PD, Quinlan BD, Chan WT, Luna JM, Mothes W.##Barr SD, Smiley JR, Bushman FD."	TRIM E3 ligases interfere with early and late stages of the retroviral life cycle.?##The interferon response inhibits HIV particle production by induction of TRIM22. 
DRAVPR0104	MAAAAASHLNLDALREVLECPICMESFTEEQLRPKLLHCGHTICRQCLEKLLASSINGVRCPFCSKITRITSLTQLTDNLTVLKIIDTAGLSEAVGLLMCRSCGRRLPRQFCRSCGLVLCEPCREADHQPPGHCTLPVKEAAEERRRDFGEKLTRLRELMGELQRRKAALEGVSKDLQARYKAVLQEYGHEERRVQDELARSRKFFTGSLAEVEKSNSQVVEEQSYLLNIAEVQAVSRCDYFLAKIKQADVALLEETADEEEPELTASLPRELTLQDVELLKVGHVGPLQIGQAVKKPRTVNVEDSWAMEATASAASTSVTFREMDMSPEEVVASPRASPAKQRGPEAASNIQQCLFLKKMGAKGSTPGMFNLPVSLYVTSQGEVLVADRGNYRIQVFTRKGFLKEIRRSPSGIDSFVLSFLGADLPNLTPLSVAMNCQGLIGVTDSYDNSLKVYTLDGHCVACHRSQLSKPWGITALPSGQFVVTDVEGGKLWCFTVDRGSGVVKYSCLCSAVRPKFVTCDAEGTVYFTQGLGLNLENRQNEHHLEGGFSIGSVGPDGQLGRQISHFFSENEDFRCIAGMCVDARGDLIVADSSRKEILHFPKGGGYSVLIREGLTCPVGIALTPKGQLLVLDCWDHCIKIYSYHLRRYSTP	653	E3 ubiquitin-protein ligase TRIM32	Homo sapiens (Human)	Q13049	TRIM32	2CT2##5FEY		[Ref.18248090]TRIM22 was reported to attenuate transcription of the HIV LTR.	AF-Q13049-F1		"¢ÙThe N-terminal is acetylation.¢ÚPhosphorylation of Ser at position 328,335,339."	18248090	"Uchil PD, Quinlan BD, Chan WT, Luna JM, Mothes W."	TRIM E3 ligases interfere with early and late stages of the retroviral life cycle.?
DRAVPR0105	MEPAPARSPRPQQDPARPQEPTMPPPETPSEGRQPSPSPSPTERAPASEEEFQFLRCQQCQAEAKCPKLLPCLHTLCSGCLEASGMQCPICQAPWPLGADTPALDNVFFESLQRRLSVYRQIVDAQAVCTRCKESADFWCFECEQLLCAKCFEAHQWFLKHEARPLAELRNQSVREFLDGTRKTNNIFCSNPNHRTPTLTSIYCRGCSKPLCCSCALLDSSHSELKCDISAEIQQRQEELDAMTQALQEQDSAFGAVHAQMHAAVGQLGRARAETEELIRERVRQVVAHVRAQERELLEAVDARYQRDYEEMASRLGRLDAVLQRIRTGSALVQRMKCYASDQEVLDMHGFLRQALCRLRQEEPQSLQAAVRTDGFDEFKVRLQDLSSCITQGKDAAVSKKASPEAASTPRDPIDVDLPEEAERVKAQVQALGLAEAQPMAVVQSVPGAHPVPVYAFSIKGPSYGEDVSNTTTAQKRKCSQTQCPRKVIKMESEEGKEARLARSSPEQPRPSTSKAVSPPHLDGPPSPRSPVIGSEVFLPNSNHVASGAGEAEERVVVISSSEDSDAENSSSRELDDSSSESSDLQLEGPSTLRVLDENLADPQAEDRPLVFFDLKIDNETQKISQLAAVNRESKFRVVIQPEAFFSIYSKAVSLEVGLQHFLSFLSSMRRPILACYKLWGPGLPNFFRALEDINRLWEFQEAISGFLAALPLIRERVPGASSFKLKNLAQTYLARNMSERSAMAAVLAMRDLCRLLEVSPGPQLAQHVYPFSSLQCFASLQPLVQAAVLPRAEARLLALHNVSFMELLSAHRRDRQGGLKKYSRYLSLQTTTLPPAQPAFNLQALGTYFEGLLEGPALARAEGVSTPLAGRGLAERASQQS	882	Protein PML	Homo sapiens (Human)	P29590	PML(TRIM19)	1BOR##2MVW##4WJO##5YUF##6UYP		"[Ref.18248090]The list of viruses inhibited by TRIM19 includes vesicular stomatitis virus, influenza A virus, human cytomegalovirus, herpes simplex type 1, Ebola virus, Lassa fever virus, lymphocytic choriomeningitis virus, human foamy virus and HIV."	AF-P29590-F1		"¢ÙThe Lys at posistion 487,515 indicates N6-acetyllysine.¢ÚPhosphorylation of Ser at position 8,36,38,48,117,403,493,504,505,512,518,527,530,565.¢ÛPhosphorylation of Thr at position 867."	18248090	"Uchil PD, Quinlan BD, Chan WT, Luna JM, Mothes W."	TRIM E3 ligases interfere with early and late stages of the retroviral life cycle.?
DRAVPR0106	MDFSVKVDIEKEVTCPICLELLTEPLSLDCGHSFCQACITAKIKESVIISRGESSCPVCQTRFQPGNLRPNRHLANIVERVKEVKMSPQEGQKRDVCEHHGKKLQIFCKEDGKVICWVCELSQEHQGHQTFRINEVVKECQEKLQVALQRLIKEDQEAEKLEDDIRQERTAWKNYIQIERQKILKGFNEMRVILDNEEQRELQKLEEGEVNVLDNLAAATDQLVQQRQDASTLISDLQRRLRGSSVEMLQDVIDVMKRSESWTLKKPKSVSKKLKSVFRVPDLSGMLQVLKELTDVQYYWVDVMLNPGSATSNVAISVDQRQVKTVRTCTFKNSNPCDFSAFGVFGCQYFSSGKYYWEVDVSGKIAWILGVHSKISSLNKRKSSGFAFDPSVNYSKVYSRYRPQYGYWVIGLQNTCEYNAFEDSSSSDPKVLTLFMAVPPCRIGVFLDYEAGIVSFFNVTNHGALIYKFSGCRFSRPAYPYFNPWNCLVPMTVCPPSS	498	E3 ubiquitin-protein ligase TRIM22	Homo sapiens (Human)	Q8IYM9	TRIM22	None	"HIV,EMCV,HBV"	[Ref.18389079]Human immunodeficiency virus(HIV):TRIM22 inhibits the replication of HIV.##[Ref.19218198]encephalomyocarditis virus(EMCV):Trim22 inhibits the infection of EMCV.##[Ref.19585648]Hepatitic B virus(HBV):TRIM22 exhibits anti-HBV activity by acting as a transcriptional suppressor	AF-Q8IYM9-F1		No modifications on the sequence.	18389079##19218198##19585648	"Barr SD, Smiley JR, Bushman FD.##Eldin P, Papon L, Oteiza A, Brocchi E, Lawson TG, Mechti N.##Gao B, Duan Z, Xu W, Xiong S."	"The interferon response inhibits HIV particle production by induction of TRIM22.##TRIM22 E3 ubiquitin ligase activity is required to mediate antiviral activity against encephalomyocarditis virus. ##Tripartite motif-containing 22 inhibits the activity of hepatitis B virus core promoter, which is dependent on nuclear-located RING domain. "
DRAVPR0107	MASKILLNVQEEVTCPICLELLTEPLSLDCGHSLCRACITVSNKEAVTSMGGKSSCPVCGISYSFEHLQANQHLANIVERLKEVKLSPDNGKKRDLCDHHGEKLLLFCKEDRKVICWLCERSQEHRGHHTVLTEEVFKECQEKLQAVLKRLKKEEEEAEKLEADIREEKTSWKYQVQTERQRIQTEFDQLRSILNNEEQRELQRLEEEEKKTLDKFAEAEDELVQQKQLVRELISDVECRSQWSTMELLQDMSGIMKWSEIWRLKKPKMVSKKLKTVFHAPDLSRMLQMFRELTAVRCYWVDVTLNSVNLNLNLVLSEDQRQVISVPIWPFQCYNYGVLGSQYFSSGKHYWEVDVSKKTAWILGVYCRTYSRHMKYVVRRCANRQNLYTKYRPLFGYWVIGLQNKCKYGVFEESLSSDPEVLTLSMAVPPCRVGVFLDYEAGIVSFFNVTSHGSLIYKFSKCCFSQPVYPYFNPWNCPAPMTLCPPSS	488	Tripartite motif-containing protein 34	Homo sapiens (Human)	Q9BYJ4	TRIM34	2EGP	SIV	[Ref.17156811]simian immunodeficiency virus(SIV):TRIM34 inhibits simian immunodeficiency virus.	AF-Q9BYJ4-F1		No modifications on the sequence.	17156811	"Li X, Gold B, O'hUigin C, Diaz-Griffero F, Song B, Si Z, Li Y, Yuan W, Stremlau M, Mische C, Javanbakht H, Scally M, Winkler C, Dean M, Sodroski J."	Unique features of TRIM5alpha among closely related human TRIM family members.?
DRAVPR0108	MASGILVNVKEEVTCPICLELLTQPLSLDCGHSFCQACLTANHKKSMLDKGESSCPVCRISYQPENIRPNRHVANIVEKLREVKLSPEGQKVDHCARHGEKLLLFCQEDGKVICWLCERSQEHRGHHTFLTEEVAREYQVKLQAALEMLRQKQQEAEELEADIREEKASWKTQIQYDKTNVLADFEQLRDILDWEESNELQNLEKEEEDILKSLTNSETEMVQQTQSLRELISDLEHRLQGSVMELLQGVDGVIKRTENVTLKKPETFPKNQRRVFRAPDLKGMLEVFRELTDVRRYWVDVTVAPNNISCAVISEDKRQVSSPKPQIIYGARGTRYQTFVNFNYCTGILGSQSITSGKHYWEVDVSKKTAWILGVCAGFQPDAMCNIEKNENYQPKYGYWVIGLEEGVKCSAFQDSSFHTPSVPFIVPLSVIICPDRVGVFLDYEACTVSFFNITNHGFLIYKFSHCSFSQPVFPYLNPRKCGVPMTLCSPSS	493	Tripartite motif-containing protein 5	Homo sapiens (Human)	Q9C035	TRIM5	2ECV##2YRG		[Ref.17156811]TRIM5 exhibited potent antiretroviral activity.	AF-Q9C035-F1		¢ÙThe N-terminal is acetylation.¢ÚPhosphorylation of Ser at position 86.	25127057##17156811	"Mandell MA, Jain A, Arko-Mensah J, Chauhan S, Kimura T, Dinkins C, Silvestri G, M¨¹nch J, Kirchhoff F, Simonsen A, Wei Y, Levine B, Johansen T, Deretic V.?##Li X, Gold B, O'hUigin C, Diaz-Griffero F, Song B, Si Z, Li Y, Yuan W, Stremlau M, Mische C, Javanbakht H, Scally M, Winkler C, Dean M, Sodroski J. "	TRIM proteins regulate autophagy and can target autophagic substrates by direct recognition.?##Unique features of TRIM5alpha among closely related human TRIM family members. 
DRAVPR0109	MASGILLNVKEEVTCPICLELLTEPLSLHCGHSFCQACITANHKKSMLYKEGERSCPVCRISYQPENIQPNRHVANIVEKLREVKLSPEEGQKVDHCARHGEKLLLFCQEDSKVICWLCERSQEHRGHHTFLMEEVAQEYHVKLQTALEMLRQKQQEAEKLEADIREEKASWKIQIDYDKTNVSADFEQLREILDWEESNELQNLEKEEEDILKSLTKSETEMVQQTQYMRELISELEHRLQGSMMDLLQGVDGIIKRIENMTLKKPKTFHKNQRRVFRAPDLKGMLDMFRELTDARRYWVDVTLAPNNISHAVIAEDKRQVSSRNPQIMYQAPGTLFTFPSLTNFNYCTGVLGSQSITSGKHYWEVDVSKKSAWILGVCAGFQSDAMYNIEQNENYQPKYGYWVIGLQEGVKYSVFQDGSSHTPFAPFIVPLSVIICPDRVGVFVDYEACTVSFFNITNHGFLIYKFSQCSFSKPVFPYLNPRKCTVPMTLCSPSS	497	Tripartite motif-containing protein 5(TRIM5alpha)	Macaca mulatta (Rhesus macaque)	Q0PF16	TRIM5	2LM3##3UV9##4TKP##5K3Q	HIV-1	[Ref.18389079]Human immunodeficiency virus type 1(HIV-1):RhTRIM5¦Á blocks early replication steps of HIV-1 and inhibits the replication.	AF-Q0PF16-F1		¢ÙThe N-terminal is acetylation.¢ÚPhosphorylation of Ser at position 87.	18389079	"Barr SD, Smiley JR, Bushman FD."	The interferon response inhibits HIV particle production by induction of TRIM22.
DRAVPR0110	MATSAPLRSLEEEVTCSICLDYLRDPVTIDCGHVFCRSCTTDVRPISGSRPVCPLCKKPFKKENIRPVWQLASLVENIERLKVDKGRQPGEVTREQQDAKLCERHREKLHYYCEDDGKLLCVMCRESREHRPHTAVLMEKAAQPHREKILNHLSTLRRDRDKIQGFQAKGEADILAALKKLQDQRQYIVAEFEQGHQFLREREEHLLEQLAKLEQELTEGREKFKSRGVGELARLALVISELEGKAQQPAAELMQDTRDFLNRYPRKKFWVGKPIARVVKKKTGEFSDKLLSLQRGLREFQGKLLRDLEYKTVSVTLDPQSASGYLQLSEDWKCVTYTSLYKSAYLHPQQFDCEPGVLGSKGFTWGKVYWEVEVEREGWSEDEEEGDEEEEGEEEEEEEEAGYGDGYDDWETDEDEESLGDEEEEEEEEEEEVLESCMVGVARDSVKRKGDLSLRPEDGVWALRLSSSGIWANTSPEAELFPALRPRRVGIALDYEGGTVTFTNAESQELIYTFTATFTRRLVPFLWLKWPGTRLLLRP	539	Tripartite motif-containing protein 26	Homo sapiens (Human)	Q12899	TRIM26	None		[Ref.18248090]TRIM26 inhibits both HIV(human immunodeficiency virus) and MLV(murine leukemia virus).	AF-Q12899-F1		No modifications on the sequence.	18248090	"Uchil PD, Quinlan BD, Chan WT, Luna JM, Mothes W."	TRIM E3 ligases interfere with early and late stages of the retroviral life cycle.?
DRAVPR0111	MGESPASVVLNASGGLFSLKMETLESELTCPICLELFEDPLLLPCAHSLCFSCAHRILVSSCSSGESIEPITAFQCPTCRYVISLNHRGLDGLKRNVTLQNIIDRFQKASVSGPNSPSESRRERTYRPTTAMSSERIACQFCEQDPPRDAVKTCITCEVSYCDRCLRATHPNKKPFTSHRLVEPVPDTHLRGITCLDHENEKVNMYCVSDDQLICALCKLVGRHRDHQVASLNDRFEKLKQTLEMNLTNLVKRNSELENQMAKLIQICQQVEVNTAMHEAKLMEECDELVEIIQQRKQMIAVKIKETKVMKLRKLAQQVANCRQCLERSTVLINQAEHILKENDQARFLQSAKNIAERVAMATASSQVLIPDINFNDAFENFALDFSREKKLLEGLDYLTAPNPPSIREELCTASHDTITVHWISDDEFSISSYELQYTIFTGQANFISKSWCSWGLWPEIRKCKEAVSCSRLAGAPRGLYNSVDSWMIVPNIKQNHYTVHGLQSGTRYIFIVKAINQAGSRNSEPTRLKTNSQPFKLDPKMTHKKLKISNDGLQMEKDESSLKKSHTPERFSGTGCYGAAGNIFIDSGCHYWEVVMGSSTWYAIGIAYKSAPKNEWIGKNASSWVFSRCNSNFVVRHNNKEMLVDVPPHLKRLGVLLDYDNNMLSFYDPANSLHLHTFDVTFILPVCPTFTIWNKSLMILSGLPAPDFIDYPERQECNCRPQESPYVSGMKTCH	735	Probable E3 ubiquitin-protein ligase MID2	Homo sapiens (Human)	Q9UJV3	MID2(TRIM1)	2DJA##2DMK		"[Ref.18389079]TRIM1 has been shown to target the capsid protein at an early stage pre-reverse transcription,which forms the protein shell of the viral core."	AF-Q9UJV3-F1		No modifications on the sequence.	18389079	"Barr SD, Smiley JR, Bushman FD."	The interferon response inhibits HIV particle production by induction of TRIM22.
DRAVPR0112	MCKDYVYDIDIEQIAKEEQGEALKLQASTSTEVSQQQCSVPGLGEKYPTWETTKPELELLGHNPRRRRIASSFTIGLRGLINLGNTCFMNCIVQALTHTPILRDFFLSDRHRCEMPSPELCLVCEMSSLFRELYSGNPSPHVPYKLLHLVWIHARHLAGYRQQDAHEFLIAALDVLHRHCKGDDVGKVASNPNHCNCIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISLDLPGSCTSFWPMSPGRESSLNGESHIPGITTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMKKLPVVACFHFKRFEHSAKQRRKITTYISFPLELDMTPFMASSKETRVNGQLQLPTNSANNENKYSLFAVVNHQGTLESGHYTSFIRHHRDQWFKCDDAVITKASIKDVLDSEGYLLFYHKQVLEPEPEKVKEMTPQAY	438		Mus musculus (Mouse)	Q8CEG8								31534008		
DRAVPR0113	MASETTEARAPFQPDGAYGWRCPEHSERPAELFCRRCGRCVCALCPVLGAHRGHPVGLAEEEAVRVQKLIQDCLECLATKKRQHADNIAHLEDAGERLKVYADSSKAWLTQKFTELRLLLDEEEVLAKKFIDKSTQLTLQVYREQAETCGKQIEVMDDFSTRVWGIGQEPNPVQLLQAYIATKTEMGQQMSPSELSHPVPLSFEPVKNFFKEFVEAIGNTLQTPMDTRLKENINCQLSNSSSTKPGALLKTSPSPERALFLKYARTPTLDPDTMHARLRLSPDGLTVRCSLLGRLGPRPAPRFDALRQVLGRDGFAAGRHYWEVDVQEAGVGWWVGAAYPSLRRRGASAAARLGCNRESWCVKRYDLEYWAFHDGQRSRLRPRRDPHRLGVFLDYEAGILAFYDVAGGMSHLHTFHAAFQEPLYPALRLWEGPISIPRLP	440		Mus musculus (Mouse)	Q8BVW3								27666593		
DRAVPR0114	MGTPKPRILPWLVSQLDLGQLEGVAWVNKSRTRFRIPWKHGLRQDAQQEDFGIFQAWAEATGAYVPGRDKPDLPTWKRNFRSALNRKEGLRLAEDRSKDPHDPHKIYEFVNSGVGDFSQPDTSPDTNGGGSTSDTQEDILDELLGNMVLAPLPDPGPPSLAVAPEPCPQPLRSPSLDNPTPFPNLGPSENPLKRLLVPGEEWEFEVTAFYRGRQVFQQTISCPEGLRLVGSEVGDRTLPGWPVTLPDPGMSLTDRGVMSYVRHVLSCLGGGLALWRAGQWLWAQRLGHCHTYWAVSEELLPNSGHGPDGEVPKDKEGGVFDLGPFIVDLITFTEGSGRSPRYALWFCVGESWPQDQPWTKRLVMVKVVPTCLRALVEMARVGGASSLENTVDLHISNSHPLSLTSDQYKAYLQDLVEGMDFQGPGES	427		Homo sapiens (Human)	Q14653								33440148		
DRAVPR0115	MKESRNLENFVEKKLYECKKKYVDIPKDEGQRYGGKHYEALTSKIFEILRKENPELDIIIAEFSLEGSVGMLKIAKPNEFDLVFKLKFPYYKSIAVTRDPKIPGNVLLDMTRVLELLKDDPREDFQRIRELIQGRLVDAQNFFVVDRLRSWLQSLFSQALNRISYRVELVAGVVSHLKYRTCGPAHTIYVYGDYEYSVDYVPAICLAAEQNVLPTKQLECFKRANTSYWEAIPKPLKPLTETSMISFRSSFYAVEKILLQDVHENCRNAIRFMKKFRDVKTNLGNCKSYYIKTLFLWKIIQEPESYWLNPLSFILADMFDDLAENLRRGVITFFWDPELNMIDALTRDQVWEMYLCVQRIPRDLRGAEISRNKWSFFVLREFSHKKERNVNLKCSSRRKRNVIKGLKTTSICKLRNARTNGTWTAGLWTRPGHAYRGPSETVSTWDTVKDAAWSEGIVE	459		Drosophila melanogaster (Fruit fly)	A8DYP7								34261128		
DRAVPR0116	MAAPDLSTNLQEEATCAICLDYFTDPVMTDCGHNFCRECIRRCWGQPEGPYACPECRELSPQRNLRPNRPLAKMAEMARRLHPPSPVPQGVCPAHREPLAAFCGDELRLLCAACERSGEHWAHRVRPLQDAAEDLKAKLEKSLEHLRKQMQDALLFQAQADETCVLWQKMVESQRQNVLGEFERLRRLLAEEEQQLLQRLEEEELEVLPRLREGAAHLGQQSAHLAELIAELEGRCQLPALGLLQDIKDALRRVQDVKLQPPEVVPMELRTVCRVPGLVETLRRFRGDVTLDPDTANPELILSEDRRSVQRGDLRQALPDSPERFDPGPCVLGQERFTSGRHYWEVEVGDRTSWALGVCRENVNRKEKGELSAGNGFWILVFLGSYYNSSERALAPLRDPPRRVGIFLDYEAGHLSFYSATDGSLLFIFPEIPFSGTLRPLFSPLSSSPTPMTICRPKGGSGDTLAPQ	468		Homo sapiens (Human)	Q96F44								18248090		
DRAVPR0117	MDPFPDLYATPGDSLDHFLEHSLQPQRDWKEEGQDAWERIERFFREQCFRDELLLDQEVRVIKVVKGGSSGKGTTLNHRSDQDMILFLSCFSSFEEQARNREVVISFIKKRLIHCSRSLAYNIIVLTHREGKRAPRSLTLKVQSRKTDDIIWMDILPAYDALGPISRDSKPAPAIYETLIRSKGYPGDFSPSFTELQRHFVKTRPVKLKNLLRLVKFWYLQCLRRKYGRGAVLPSKYALELLTIYAWEMGTESSDSFNLDEGFVAVMELLVNYRDICIYWTKYYNFQNEVVRNFLKKQLKGDRPIILDPADPTNNLGRRKGWEQVAAEAAFCLLQVCCTTVGPSERWNVQRARDVQVRVKQTGTVDWTLWTNPYSPIRKMKAEIRREKNFGGELRISFQEPGGERQLLSSRKTLADYGIFSKVNIQVLETFPPEILVFVKYPGGQSKPFTIDPDDTILDLKEKIEDAGGPCAEDQVLLLDDEELEDDESLKELEIKDCDTIILIRVID	508		Mus musculus (Mouse)	Q9Z2F2								12396720##12799444		
DRAVPR0118	MASDTPGFYMDKLNKYRQMHGVAITYKELSTSGPPHDRRFTFQVLIDEKEFPEAKGRSKQEARNAAAKLAVDILDNENKVDCHTSASEQGLFVGNYIGLVNSFAQKKKLSVNYEQCEPNSELPQRFICKCKIGQTMYGTGSGVTKQEAKQLAAKEAYQKLLKSPPKTAGTSSSVVTSTFSGFSSSSSMTSNGVSQSAPGSFSSENVFTNGLGENKRKSGVKVSPDDVQRNKYTLDARFNSDFEDIEEIGLGGFGQVFKAKHRIDGKRYAIKRVKYNTEKAEHEVQALAELNHVNIVQYHSCWEGVDYDPEHSMSDTSRYKTRCLFIQMEFCDKGTLEQWMRNRNQSKVDKALILDLYEQIVTGVEYIHSKGLIHRDLKPGNIFLVDERHIKIGDFGLATALENDGKSRTRRTGTLQYMSPEQLFLKHYGKEVDIFALGLILAELLHTCFTESEKIKFFESLRKGDFSNDIFDNKEKSLLKKLLSEKPKDRPETSEILKTLAEWRNISEKKKRNTC	515		Mus musculus (Mouse)	Q03963								19264662##20585572##20631127##21994357		
DRAVPR0119	MAVPGEAEEEATVYLVVSGIPSVLRSAHLRSYFSQFREERGGGFLCFHYRHRPERAPPQAAPNSALIPTDPAAEGQLLSQTSATDVRPLSTRDSTPIQTRTCCCVISVRGLAQAQRLIRMYSGRRWLDSHGTWLPGRCLIRRLRLPTEASGLGSFPFKTRKELQSWKAENEAFTLADLKQLPELNPPVLMPRGNVGTPLRVFLELIRACRLPPRIITQLQLQFPKTGSSRRYGNVPFEYEDSETVEQEELVYTAEGEEIPQGTYLADIPASPCGEPEEEVGKEEEEESHSDEDDDRGEEWERHEALHEDVTGQERTTEQLFEEEIELKWEKGGSGLVFYTDAQFWQEEEGDFDEQTADDWDVDMSVYYDRDGGDKDARDSVQMRLEQRLRDGQEDGSVIERQVGTFERHTKGIGRKVMERQGWAEGQGLGCRCSGVPEALDSDGQHPRCKRGLGYHGEKLQPFGQLKRPRRNGLGLISTIYDEPLPQDQTESLLRRQPPTSMKFRTDMAFVRGSSCASDSPSLPD	525		Homo sapiens (Human)	Q96I76								28414768		
DRAVPR0120	MSTTSKESLVCNLRQLKCHFTWNLIAEDESLDEFEDRVFNKDEFQNSEFKATMCNILAYVKHCRGLNEAALQCLGEAEGFIQQQHPDQVEIRSLVTWGNYAWVYYHMGQFSKAQAYLDKVKQVCKKFSSPYRIENPALDCEEGWARLKCTKNQNERVKVCFQKALEKDPKNPEFTSGWAIAFYRLDDWPARNYCIDSLEQAIQLSPDNTYVKVLLALKLDAVHVHKNQAMALVEEALKKDPSAIDTLLRAARFYCKVYDTDRAIQLLRKALEKLPNNAYVHYYMGCCYRSKVHHMLNRREMVFSGDRKKLEELIQLAVNHLRKAEEIKEMLEYSCSFLADLYIIAKKYDEADYYFQKELSKDLPPGPKQLLHLRYGNFQFFQMKRQDKAIYHYMEGVKIKKKTIPQKKMREKLQRIALRRLHEDESDSEALHILAFLQENGGGQQADKDSERGVDSANQVPSASLDEDGAEY	472		Mus musculus (Mouse)	Q64112								21085181		
DRAVPR0121	MGSDFSTVKIRKVTSCSICKAMMSHPVSINCGHSYCKSCIQSYYCNVSPKTGWKMLGCPLCSSPFSLENLRPNKELETIIDMIKGMEEQDQDMVCEEHEEKFNRFCEDDGQLLCWRCYWEDRHKGHTLAHVKDVYQNYKEKLQNTMTKLRELQENHEVQIHFITHQINAWKDAVEDRRQTIKSNFKNLQSFLQEEEKFYLWRLENEEKEMLVQLEGSEANLQQTFERAQCQIQELEAKCQGSAQKLLQDVKNTLSRCEAMKRNPLKADPLKVHTKCNVSELYFDVKTILRRHQVSVILDPSTAHLDLALTKGGRLVTYKRCPRDLQARSSAKRFYGLPCVLGCEGFTSGRYYFEVSVENATSWDLGVCVENVHRGFNMKKEPESGFWTIKMSEEDGLEALTSTPTPPLHLIEKPQILGVFLDYEAGAVSFYSVTTGSHIFTFPKASFQDTLRPFFQVYQYSPLFLPAINNQ	471		Mus musculus (Mouse)	Q5SZ99								27637147		
DRAVPR0122	MPIRALCTICSDFFDHSRDVAAIHCGHTFHLQCLIQWFETAPSRTCPQCRIQVGKRTIINKLFFDLAQEEENVLDAEFLKNELDNVRAQLSQKDKEKRDSQVIIDTLRDTLEERNATVVSLQQALGKAEMLCSTLKKQMKYLEQQQDETKQAQEEARRLRSKMKTMEQIELLLQSQRPEVEEMIRDMGVGQSAVEQLAVYCVSLKKEYENLKEARKASGEVADKLRKDLFSSRSKLQTVYSELDQAKLELKSAQKDLQSADKEIMSLKKKLTMLQETLNLPPVASETVDRLVLESPAPVEVNLKLRRPSFRDDIDLNATFDVDTPPARPSSSQHGYYEKLCLEKSHSPIQDVPKKICKGPRKESQLSLGGQSCAGEPDEELVGAFPIFVRNAILGQKQPKRPRSESSCSKDVVRTGFDGLGGRTKFIQPTDTVMIRPLPVKPKTKVKQRVRVKTVPSLFQAKLDTFLWS	469		Homo sapiens (Human)	Q9BWF2								22945920		
DRAVPR0123	MTSTVLVDIRDEVTCPICLELLTEPLSIDCGHSFCQVCIIGNSNNSVFGQGGRSSCPVCRTSYQPGNLRPNRHLAAIVKRLREVALCPGKQLEVIFCALHGEKLQLFCKEDGKLICWLCERSQEHRGHHTFLMEEVAQEYQDMFQESLKKLRREQQEAEKLKALIQEKRESWKSQVEPEKRRIQTEFKQLRSILDREEQRELKKLEVEERKGLSIIEKAEGDLIHQSQSLKDLISDLEHRCQGSTVELLQDVGDVTKRSEFWTLRKPQALPTKLKSLFRAPDLRKMLKVFRELTDVQSYWVDVTLNPQTANLNLVLSKNRRQVRFVGAQLSEPSSLEEHYDCSVLGSQHFSSGKYYWEVDVSKKTAWILGVCSTPVDPMFSFSQYSSKQGAYSRYQPQCGYWVIGLQCKHEYRAYEDSSPSLLLSMTVPPRRIGIFLDCEAGTVSFYNVTNHGLPIYTFSKYYFPSALCPYFNPCSCIVPMTLRRPTS	488		Mus musculus (Mouse)	Q8BGE7								24882218		
DRAVPR0124	MTSPVLVDIREEVTCPICLELLTEPLSIDCGHSFCQACITPNGRESVIGQEGERSCPVCQTSYQPGNLRPNRHLANIVRRLREVVLGPGKQLKAVLCADHGEKLQLFCQEDGKVICWLCERSQEHRGHHTFLVEEVAQEYQEKFQESLKKLKNEEQEAEKLTAFIREKKTSWKNQMEPERCRIQTEFNQLRNILDRVEQRELKKLEQEEKKGLRIIEEAENDLVHQTQSLRELISDLERRCQGSTMELLQDVSDVTERSEFWTLRKPEALPTKLRSMFRAPDLKRMLRVCRELTDVQSYWVDVTLNPHTANLNLVLAKNRRQVRFVGAKVSGPSCLEKHYDCSVLGSQHFSSGKHYWEVDVAKKTAWILGVCSNSLGPTFSFNHFAQNHSAYSRYQPQSGYWVIGLQHNHEYRAYEDSSPSLLLSMTVPPRRVGVFLDYEAGTVSFYNVTNHGFPIYTFSKYYFPTTLCPYFNPCNCVIPMTLRRPSS	488		Homo sapiens (Human)	Q9C030								24882218		
DRAVPR0125	MSEVTKNSLEKILPQLKCHFTWNLFKEDSVSRDLEDRVCNQIEFLNTEFKATMYNLLAYIKHLDGNNEAALECLRQAEELIQQEHADQAEIRSLVTWGNYAWVYYHLGRLSDAQIYVDKVKQTCKKFSNPYSIEYSELDCEEGWTQLKCGRNERAKVCFEKALEEKPNNPEFSSGLAIAMYHLDNHPEKQFSTDVLKQAIELSPDNQYVKVLLGLKLQKMNKEAEGEQFVEEALEKSPCQTDVLRSAAKFYRRKGDLDKAIELFQRVLESTPNNGYLYHQIGCCYKAKVRQMQNTGESEASGNKEMIEALKQYAMDYSNKALEKGLNPLNAYSDLAEFLETECYQTPFNKEVPDAEKQQSHQRYCNLQKYNGKSEDTAVQHGLEGLSISKKSTDKEEIKDQPQNVSENLLPQNAPNYWYLQGLIHKQNGDLLQAAKCYEKELGRLLRDAPSGIGSIFLSASELEDGSEEMGQGAVSSSPRELLSNSEQLN	490		Homo sapiens (Human)	O14879								20686046##21642987##21813773		
DRAVPR0126	MTQAEIKLCSLLLQEHFGEIVEKIGVHLIRTGSQPLRVIAHDTGTSLDQVKKALCVLVQHNLVSYQVHKRGVVEYEAQCSRVLRMLRYPRYIYTTKTLYSDTGELIVEELLLNGKLTMSAVVKKVADRLTETMEDGKTMDYAEVSNTFVRLADTHFVQRCPSVPTTENSDPGPPPPAPTLVINEKDMYLVPKLSLIGKGKRRRSSDEDAAGEPKAKRPKYTTDNKEPIPDDGIYWQANLDRFHQHFRDQAIVSAVANRMDQTSSEIVRTMLRMSEITTSSSAPFTQPLSSNEIFRSLPVGYNISKQVLDQYLTLLADDPLEFVGKSGDSGGGMYVINLHKALASLATATLESVVQERFGSRCARIFRLVLQKKHIEQKQVEDFAMIPAKEAKDMLYKMLSENFMSLQEIPKTPDHAPSRTFYLYTVNILSAARMLLHRCYKSIANLIERRQFETKENKRLLEKSQRVEAIIASMQATGAEEAQLQEIEEMITAPERQQLETLKRNVNKLDASEIQVDETIFLLESYIECTMKRQ	534		Homo sapiens (Human)	Q9BUI4								19631370		
DRAVPR0127	MDELFPLIFPAEPAQASGPYVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTDTTKTHPTIKINGYTGPGTVRISLVTKDPPHRPHPHELVGKDCRDGFYEAELCPDRCIHSFQNLGIQCVKKRDLEQAISQRIQTNNNPFQVPIEEQRGDYDLNAVRLCFQVTVRDPSGRPLRLPPVLSHPIFDNRAPNTAELKICRVNRNSGSCLGGDEIFLLCDKVQKEDIEVYFTGPGWEARGSFSQADVHRQVAIVFRTPPYADPSLQAPVRVSMQLRRPSDRELSEPMEFQYLPDTDDRHRIEEKRKRTYETFKSIMKKSPFSGPTDPRPPPRRIAVPSRSSASVPKPAPQPYPFTSSLSTINYDEFPTMVFPSGQISQASALAPAPPQVLPQAPAPAPAPAMVSALAQAPAPVPVLAPGPPQAVAPPAPKPTQAGEGTLSEALLQLQFDDEDLGALLGNSTDPAVFTDLASVDNSEFQQLLNQGIPVAPHTTEPMLMEYPEAITRLVTGAQRPPDPAPAPLGAPGLPNGLLSGDEDFSSIADMDFSALLSQISS	551		Homo sapiens (Human)	Q04206								33440148		
DRAVPR0128	MSATSVDQRPKGQGNKVSVQNGSIHQKDAVNDDDFEPYLSSQTNQSNSYPPMSDPYMPSYYAPSIGFPYSLGEAAWSTAGDQPMPYLTTYGQMSNGEHHYIPDGVFSQPGALGNTPPFLGQHGFNFFPGNADFSTWGTSGSQGQSTQSSAYSSSYGYPPSSLGRAITDGQAGFGNDTLSKVPGISSIEQGMTGLKIGGDLTAAVTKTVGTALSSSGMTSIATNSVPPVSSAAPKPTSWAAIARKPAKPQPKLKPKGNVGIGGSAVPPPPIKHNMNIGTWDEKGSVVKAPPTQPVLPPQTIIQQPQPLIQPPPLVQSQLPQQQPQPPQPQQQQGPQPQAQPHQVQPQQQQLQNRWVAPRNRGAGFNQNNGAGSENFGLGVVPVSASPSSVEVHPVLEKLKAINNYNPKDFDWNLKNGRVFIIKSYSEDDIHRSIKYSIWCSTEHGNKRLDAAYRSLNGKGPLYLLFSVNGSGHFCGVAEMKSVVDYNAYAGVWSQDKWKGKFEVKWIFVKDVPNNQLRHIRLENNDNKPVTNSRDTQEVPLEKAKQVLKIIATFKHTTSIFDDFAHYEKRQEEEEAMRRERNRNKQ	585		Homo sapiens (Human)	Q7Z739								32053707		
DRAVPR0129	MSSGLRAADFPRWKRHISEQLRRRDRLQRQAFEEIILQYNKLLEKSDLHSVLAQKLQAEKHDVPNRHEISPGHDGTWNDNQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAATKRLSQPAGGLLDSITNIFGRRSVSSFPVPQDNVDTHPGSGKEVRVPATALCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEVFGEKCEFKGSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTVFAGSSCNDIVCTEQCVMSGHFDKKIRFWDIRSESIVREMELLGKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQTFSAPGFKCGSDWTRVVFSPDGSYVAAGSAEGSLYIWSVLTGKVEKVLSKQHSSSINAVAWSPSGSHVVSVDKGCKAVLWAQY	607		Homo sapiens (Human)	Q676U5								22749352##25645662		
DRAVPR0130	MSTLQELQENITAHEQQLVTARQKLKDAEKAVEVDPDDVNKSTLQSRRAAVSTLETKLGELKRQLADLVAAQKLATKPVDPTGLEPDDHLKEKSSLRYGNVLDVNSIDLEEPSGQTADWKAIGAYILGFAIPIILKALYMLSTRGRQTVKDNKGTRIRFKDDSSFEEVNGIRKPKHLYVSMPTAQSTMKAEEITPGRFRTIACGLFPAQVKARNIISPVMGVIGFGFFVKDWMDRIEEFLAAECPFLPKPKVASEAFMSTNKMYFLNRQRQVNESKVQDIIDLIDHAETESATLFTEIATPHSVWVFACAPDRCPPTALYVAGVPELGAFFSILQDMRNTIMASKSVGTAEEKLKKKSAFYQSYLRRTQSMGIQLDQKIIILYMLSWGKEAVNHFHLGDDMDPELRQLAQSLIDTKVKEISNQEPLKL	428		Andes orthohantavirus (ANDV) (Andes virus)	O36307								25410857		
DRAVPR0131	MTFAEDKTYKYIRDNHSKFCCVDVLEILPYLSCLTASDQDRLRASYRQIGNRDTLWGLFNNLQRRPGWVEVFIRALQICELPGLADQVTRVYQSYLPPGTSLRSLEPLQLPDFPAAVSGPSAFAPGHNIPDHGLRETPSCPKPVQDTQPPESPVENSEQLLQTNSGAVARMSGGSLIPSPNQQALSPQPSREHQEQEPELGGAHAANVASVPIATYGPVSPTVSFQPLPRTALRTNLLSGVTVSALSADTSLSSSSTGSAFAKGAGDQAKAATCFSTTLTNSVTTSSVPSPRLVPVKTMSSKLPLSSKSTAAMTSTVLTNTAPSKLPSNSVYAGTVPSRVPASVAKAPANTIPPERNSKQAKETPEGPATKVTTGGNQTGPNSSIRSLHSGPEMSKPGVLVSQLDEPFSACSVDLAISPSSSLVSEPNHGPEENEYSSFRIQVDESPSADLLGSPEPLATQQPQEEEEHCASSMPWAKWLGATSALLAVFLAVMLYRSRRLAQ	503		Mus musculus (Mouse)	Q8VCF0								24037184		
DRAVPR0132	MAGPERWGPLLLCLLQAAPGRPRLAPPQNVTLLSQNFSVYLTWLPGLGNPQDVTYFVAYQSSPTRRRWREVEECAGTKELLCSMMCLKKQDLYNKFKGRVRTVSPSSKSPWVESEYLDYLFEVEPAPPVLVLTQTEEILSANATYQLPPCMPPLDLKYEVAFWKEGAGNKTLFPVTPHGQPVQITLQPAASEHHCLSARTIYTFSVPKYSKFSKPTCFLLEVPEANWAFLVLPSLLILLLVIAAGGVIWKTLMGNPWFQRAKMPRALDFSGHTHPVATFQPSRPESVNDLFLCPQKELTRGVRPTPRVRAPATQQTRWKKDLAEDEEEEDEEDTEDGVSFQPYIEPPSFLGQEHQAPGHSEAGGVDSGRPRAPLVPSEGSSAWDSSDRSWASTVDSSWDRAGSSGYLAEKGPGQGPGGDGHQESLPPPEFSKDSGFLEELPEDNLSSWATWGTLPPEPNLVPGGPPVSLQTLTFCWESSPEEEEEARESEIEDSDAGSWGAESTQRTEDRGRTLGHYMAR	520		Homo sapiens (Human)	Q8IU57								12483210		
DRAVPR0133	MPFAEDKTYKYICRNFSNFCNVDVVEILPYLPCLTARDQDRLRATCTLSGNRDTLWHLFNTLQRRPGWVEYFIAALRGCELVDLADEVASVYQSYQPRTSDRPPDPLEPPSLPAERPGPPTPAAAHSIPYNSCREKEPSYPMPVQETQAPESPGENSEQALQTLSPRAIPRNPDGGPLESSSDLAALSPLTSSGHQEQDTELGSTHTAGATSSLTPSRGPVSPSVSFQPLARSTPRASRLPGPTGSVVSTGTSFSSSSPGLASAGAAEGKQGAESDQAEPIICSSGAEAPANSLPSKVPTTLMPVNTVALKVPANPASVSTVPSKLPTSSKPPGAVPSNALTNPAPSKLPINSTRAGMVPSKVPTSMVLTKVSASTVPTDGSSRNEETPAAPTPAGATGGSSAWLDSSSENRGLGSELSKPGVLASQVDSPFSGCFEDLAISASTSLGMGPCHGPEENEYKSEGTFGIHVAENPSIQLLEGNPGPPADPDGGPRPQADRKFQEREVPCHRPSPGALWLQVAVTGVLVVTLLVVLYRRRLH	540		Homo sapiens (Human)	Q7Z434								20451243		
DRAVPR0134	MDLVGVASPEPGTAAAWGPSKCPWAIPQNTISCSLADVMSEQLAKELQLEEEAAVFPEVAVAEGPFITGENIDTSSDLMLAQMLQMEYDREYDAQLRREEKKFNGDSKVSISFENYRKVHPYEDSDSSEDEVDWQDTRDDPYRPAKPVPTPKKGFIGKGKDITTKHDEVVCGRKNTARMENFAPEFQVGDGIGMDLKLSNHVFNALKQHAYSEERRSARLHEKKEHSTAEKAVDPKTRLLMYKMVNSGMLETITGCISTGKESVVFHAYGGSMEDEKEDSKVIPTECAIKVFKTTLNEFKNRDKYIKDDFRFKDRFSKLNPRKIIRMWAEKEMHNLARMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLNSEEMKEAYYQTLHLMRQLYHECTLVHADLSEYNMLWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQKGGVKEALSERELFNAVSGLNITADNEADFLAEIEALEKMNEDHVQKNGRKAASFLKDDGDPPLLYDE	519		Homo sapiens (Human)	O14730								24807708		
DRAVPR0135	METPKPRILPWLVSQLDLGQLEGVAWLDESRTRFRIPWKHGLRQDAQMADFGIFQAWAEASGAYTPGKDKPDVSTWKRNFRSALNRKEVLRLAADNSKDPYDPHKVYEFVTPGARDFVHLGASPDTNGKSSLPHSQENLPKLFDGLILGPLKDEGSSDLAIVSDPSQQLPSPNVNNFLNPAPQENPLKQLLAEEQWEFEVTAFYRGRQVFQQTLFCPGGLRLVGSTADMTLPWQPVTLPDPEGFLTDKLVKEYVGQVLKGLGNGLALWQAGQCLWAQRLGHSHAFWALGEELLPDSGRGPDGEVHKDKDGAVFDLRPFVADLIAFMEGSGHSPRYTLWFCMGEMWPQDQPWVKRLVMVKVVPTCLKELLEMAREGGASSLKTVDLHISNSQPISLTSDQYKAYLQDLVEDMDFQATGNI	419		Mus musculus (Mouse)	P70671								15800576		
DRAVPR0136	MSENNKNSLESSLRQLKCHFTWNLMEGENSLDDFEDKVFYRTEFQNREFKATMCNLLAYLKHLKGQNEAALECLRKAEELIQQEHADQAEIRSLVTWGNYAWVYYHMGRLSDVQIYVDKVKHVCEKFSSPYRIESPELDCEEGWTRLKCGGNQNERAKVCFEKALEKKPKNPEFTSGLAIASYRLDNWPPSQNAIDPLRQAIRLNPDNQYLKVLLALKLHKMREEGEEEGEGEKLVEEALEKAPGVTDVLRSAAKFYRRKDEPDKAIELLKKALEYIPNNAYLHCQIGCCYRAKVFQVMNLRENGMYGKRKLLELIGHAVAHLKKADEANDNLFRVCSILASLHALADQYEDAEYYFQKEFSKELTPVAKQLLHLRYGNFQLYQMKCEDKAIHHFIEGVKINQKSREKEKMKDKLQKIAKMRLSKNGADSEALHVLAFLQELNEKMQQADEDSERGLESGSLIPSASSWNGE	472		Homo sapiens (Human)	P09913								21190939		
DRAVPR0137	MMLKSVTESFAGMIHGLKVNHLTDGIIRRSKRMILDSLGVGFLGTGTEVFHKVTQYSKIYSSNTSSTVWGRPDFRLPPTYAAFVNGVAVHSMDFDDTWHPATHPSGAVLPVLTALSEALPQIPKFSGLDLLLAFNVGIEVQGRLMHFSKEAKDIPKRFHPPSVVGTLGSAAAASKFLGLSLTKCREALAIAVSHAGAPIANAATQTKPLHIGNAAKHGMEATFLAMLGLQGNKQILDLGSGFGAFYANYSPEDLPSLDSHIWLLDQQDVAFKSFPAHLATHWVADAAAAVRKHLVTPERALFPADHIERIVLRIPDVQYVNRPFPDSEHEARHSFQYVACASLLDGSITVPSFHSQQVNRPQVRELLKKVKLEHPPDNPPSFDTLYCEISITLKDGTTFTERSDTFYGHWRKPLSQEDLRNKFRANASKMLCRDTVESLITVVEKLEDLEDCSVLTRLLKGPSVQDEASKLSSMSSFDHTTLPRFTNI	488		Mus musculus (Mouse)	P54987								30635240		
DRAVPR0138	MGPQAAAGRMILLVVLMLSAKVGSGALTSTEDPEPPSVPVPTNVLIKSYNLNPVVCWEYQNMSQTPIFTVQVKVYSGSWTDSCTNISDHCCNIYEQIMYPDVSAWARVKAKVGQKESDYARSKEFLMCLKGKVGPPGLEIRRKKEEQLSVLVFHPEVVVNGESQGTMFGDGSTCYTFDYTVYVEHNRSGEILHTKHTVEKEECNETLCELNISVSTLDSRYCISVDGISSFWQVRTEKSKDVCIPPFHDDRKDSIWILVVAPLTVFTVVILVFAYWYTKKNSFKRKSIMLPKSLLSVVKSATLETKPESKYSLVTPHQPAVLESETVICEEPLSTVTAPDSPEAAEQEELSKETKALEAGGSTSAMTPDSPPTPTQRRSFSLLSSNQSGPCSLTAYHSRNGSDSGLVGSGSSISDLESLPNNNSETKMAEHDPPPVRKAPMASGYDKPHMLVDVLVDVGGKESLMGYRLTGEAQELS	477		Mus musculus (Mouse)	P15261								20926559##27286456