Genome polyprotein
Details
- Name
- Genome polyprotein
- Synonyms
- 3.4.22.29
- P2A
- Gene Name
- Not Available
- Organism
- HRV-14
- Amino acid sequence
>lcl|BSEQ0017078|Genome polyprotein MGAQVSTQKSGSHENQNILTNGSNQTFTVINYYKDAASTSSAGQSLSMDPSKFTEPVKDL MLKGAPALNSPNVEACGYSDRVQQITLGNSTITTQEAANAVVCYAEWPEYLPDVDASDVN KTSKPDTSVCRFYTLDSKTWTTGSKGWCWKLPDALKDMGVFGQNMFFHSLGRSGYTVHVQ CNATKFHSGCLLVVVIPEHQLASHEGGNVSVKYTFTHPGERGIDLSSANEVGGPVKDVIY NMNGTLLGNLLIFPHQFINLRTNNTATIVIPYINSVPIDSMTRHNNVSLMVIPIAPLTVP TGATPSLPITVTIAPMCTEFSGIRSKSIVPQGLPTTTLPGSGQFLTTDDRQSPSALPNYE PTPRIHIPGKVHNLLEIIQVDTLIPMNNTHTKDEVNSYLIPLNANRQNEQVFGTNLFIGD GVFKTTLLGEIVQYYTHWSGSLRFSLMYTGPALSSAKLILAYTPPGARGPQDRREAMLGT HVVWDIGLQSTIVMTIPWTSGVQFRYTDPDTYTSAGFLSCWYQTSLILPPETTGQVYLLS FISACPDFKLRLMKDTQTISQTVALTEGLGDELEEVIVEKTKQTVASISSGPKHTQKVPI LTANETGATMPVLPSDSIETRTTYMHFNGSETDVECFLGRAACVHVTEIQNKDATGIDNH REAKLFNDWKINLSSLVQLRKKLELFTYVRFDSEYTILATASQPDSANYSSNLVVQAMYV PPGAPNPKEWDDYTWQSASNPSVFFKVGDTSRFSVPYVGLASAYNCFYDGYSHDDAETQY GITVLNHMGSMAFRIVNEHDEHKTLVKIRVYHRAKHVEAWIPRAPRALPYTSIGRTNYPK NTEPVIKKRKGDIKSYGLGPRYGGIYTSNVKIMNYHLMTPEDHHNLIAPYPNRDLAIVST GGHGAETIPHCNCTSGVYYSTYYRKYYPIICEKPTNIWIEGNPYYPSRFQAGVMKGVGPA EPGDCGGILRCIHGPIGLLTAGGSGYVCFADIRQLECIAEEQGLSDYITGLGRAFGVGFT DQISTKVTELQEVAKDFLTTKVLSKVVKMVSALVIICRNHDDLVTVTATLALLGCDGSPW RFLKMYISKHFQVPYIERQANDGWFRKFNDACNAAKGLEWIANKISKLIEWIKNKVLPQA KEKLEFCSKLKQLDILERQITTMHISNPTQEKREQLFNNVLWLEQMSQKFAPLYAVESKR IRELKNKMVNYMQFKSKQRIEPVCVLIHGTPGSGKSLTTSIVGRAIAEHFNSAVYSLPPD PKHFDGYQQQEVVIMDDLNQNPDGQDISMFCQMVSSVDFLPPMASLDNKGMLFTSNFVLA STNSNTLSPPTILNPEALVRRFGFDLDICLHTTYTKNGKLNAGMSTKTCKDCHQPSNFKK CCPLVCGKAISLVDRTTNIRYSVDQLVTAIISDFKSKMQITDSLETLFQGPVYKDLEIDV CNTPPPECINDLLKSVDSEEIREYCKKKKWIIPEIPTNIERAMNQASMIINTILMFVSTL GIVYVIYKLFAQTQGPYSGNPPHNKLKAPTLRPVVVQGPNTEFALSLLRKNIMTITTSKG EFTGLGIHDRVCVIPTHAQPGDDVLVNGQKIRVKDKYKLVDPENINLELTVLTLDRNEKF RDIRGFISEDLEGVDATLVVHSNNFTNTILEVGPVTMAGLINLSSTPTNRMIRYDYATKT GQCGGVLCATGKIFGIHVGGNGRQGFSAQLKKQYFVEKQGQVIARHKVREFNINPVNTPT KSKLHPSVFYDVFPGDKEPAVLSDNDPRLEVKLTESLFSKYKGNVNTEPTENMLVAVDHY AGQLLSLDIPTSELTLKEALYGVDGLEPIDITTSAGFPYVSLGIKKRDILNKETQDTEKM KFYLDKYGIDLPLVTYIKDELRSVDKVRLGKSRLIEASSLNDSVNMRMKLGNLYKAFHQN PGVLTGSAVGCDPDVFWSVIPCLMDGHLMAFDYSNFDASLSPVWFVCLEKVLTKLGFAGS SLIQSICNTHHIFRDEIYVVEGGMPSGCSGTSIFNSMINNIIIRTLILDAYKGIDLDKLK ILAYGDDLIVSYPYELDPQVLATLGKNYGLTITPPDKSETFTKMTWENLTFLKRYFKPDQ QFPFLVHPVMPMKDIHESIRWTKDPKNTQDHVRSLCMLAWHSGEKEYNEFIQKIRTTDIG KCLILPEYSVLRRRWLDLF
- Number of residues
- 2179
- Molecular Weight
- 242989.38
- Theoretical pI
- 7.28
- GO Classification
- FunctionsATP binding / cysteine-type endopeptidase activity / ion channel activity / RNA binding / RNA helicase activity / RNA-directed RNA polymerase activity / structural molecule activityProcessesDNA replication / endocytosis involved in viral entry into host cell / induction by virus of host autophagy / lysis of host organelle involved in viral entry into host cell / pore formation by virus in membrane of host cell / pore-mediated entry of viral genome into host cell / positive stranded viral RNA replication / protein oligomerization / RNA-protein covalent cross-linking / suppression by virus of host gene expression / suppression by virus of host mRNA export from nucleus / suppression by virus of host RIG-I activity by RIG-I proteolysis / suppression by virus of host translation initiation factor activity / transcription, DNA-templated / viral RNA genome replication / virion attachment to host cellComponentshost cell cytoplasmic vesicle membrane / integral to membrane of host cell / membrane / T=pseudo3 icosahedral viral capsid
- General Function
- Structural molecule activity
- Specific Function
- Capsid protein VP1: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 mainly forms the vertices of the capsid. Capsid protein VP1 interacts with host ICAM1 to provide virion attachment to target host cells. This attachment induces virion internalization. Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm. After genome has been released, the channel shrinks (By similarity).Capsid protein VP2: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity).Capsid protein VP3: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity).Capsid protein VP4: Lies on the inner surface of the capsid shell. After binding to the host receptor, the capsid undergoes conformational changes. Capsid protein VP4 is released, Capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm. After genome has been released, the channel shrinks (By similarity).Capsid protein VP0: Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation. Allows the capsid to remain inactive before the maturation step (By similarity).Protein 2A: Cysteine protease that cleaves viral polyprotein and specific host proteins. It is responsible for the cleavage between the P1 and P2 regions, first cleavage occurring in the polyprotein. Cleaves also the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA translation. Inhibits the host nucleus-cytoplasm protein and RNA trafficking by cleaving host members of the nuclear pores (By similarity).Protein 2B: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cyctoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (By similarity).Protein 2C: Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3 (By similarity).Protein 3AB: Localizes the viral replication complex to the surface of membranous vesicles. Together with protein 3CD binds the Cis-Active RNA Element (CRE) which is involved in RNA synthesis initiation. Acts as a cofactor to stimulate the activity of 3D polymerase, maybe through a nucleid acid chaperone activity (By similarity).Protein 3A: Localizes the viral replication complex to the surface of membranous vesicles. It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the dissassembly of the Golgi complex, possibly through GBF1 interaction. This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface (By similarity).Viral protein genome-linked: acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU. The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome. VPg may be removed in the cytoplasm by an unknown enzyme termed "unlinkase". VPg is not cleaved off virion genomes because replicated genomic RNA are encapsidated at the site of replication (By similarity).Protein 3CD: Is involved in the viral replication complex and viral polypeptide maturation. It exhibits protease activity with a specificity and catalytic efficiency that is different from protease 3C. Protein 3CD lacks polymerase activity. The 3C domain in the context of protein 3CD may have an RNA binding activity (By similarity).Protease 3C: cleaves host DDX58/RIG-I and thus contributes to the inhibition of type I interferon production. Cleaves also host PABPC1 (By similarity).RNA-directed RNA polymerase: Replicates the viral genomic RNA on the surface of intracellular membranes. May form linear arrays of subunits that propagate along a strong head-to-tail interaction called interface-I. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss(+)RNA genomes are either translated, replicated or encapsidated (By similarity).
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Virion
- Gene sequence
>lcl|BSEQ0017079|Genome polyprotein ATGGGCGCTCAGGTTTCTACACAGAAAAGTGGATCTCACGAAAATCAAAACATTTTGACC AATGGATCAAATCAGACTTTCACAGTTATAAATTACTATAAGGATGCAGCAAGTACATCA TCAGCTGGTCAATCACTGTCAATGGACCCATCTAAGTTTACAGAACCAGTTAAAGATCTC ATGCTTAAGGGTGCACCAGCATTGAATTCACCCAATGTTGAGGCCTGTGGTTATAGTGAT AGAGTACAACAAATCACACTCGGGAATTCAACAATAACAACACAAGAAGCAGCCAACGCT GTTGTGTGTTATGCTGAATGGCCAGAGTACCTTCCAGATGTGGACGCTAGTGATGTCAAT AAAACTTCAAAACCAGACACTTCTGTCTGTAGGTTTTACACATTGGATAGTAAGACATGG ACAACAGGTTCTAAAGGCTGGTGCTGGAAATTACCAGATGCACTCAAGGATATGGGTGTG TTCGGGCAAAACATGTTTTTCCACTCACTAGGAAGATCAGGTTACACAGTACACGTTCAG TGCAATGCCACAAAATTCCATAGCGGTTGTCTACTTGTAGTTGTAATACCAGAACACCAA CTGGCTTCACATGAGGGTGGCAATGTTTCAGTTAAATACACATTCACGCATCCAGGTGAA CGTGGTATAGATTTATCATCTGCAAATGAAGTGGGAGGGCCTGTCAAGGATGTCATATAC AATATGAATGGTACTTTATTAGGAAATCTGCTCATTTTCCCTCACCAGTTCATTAATCTA AGAACCAATAATACAGCCACAATAGTGATACCATACATAAACTCAGTACCCATTGATTCA ATGACACGTCACAACAATGTCTCACTGATGGTCATCCCTATTGCCCCTCTTACAGTACCA ACTGGAGCAACTCCCTCACTCCCTATAACAGTCACAATAGCACCTATGTGCACTGAGTTC TCTGGGATAAGGTCCAAGTCAATTGTGCCACAAGGTTTGCCAACTACAACTTTGCCGGGG TCAGGACAATTCTTGACCACAGATGACAGGCAATCCCCCAGTGCACTGCCAAATTATGAG CCAACTCCAAGAATACACATACTAGGGAAAGTTCATAACTTGCTAGAAATTATACAGGTA GATACACTCATTCCTATGAACAACACGCATACAAAAGATGAGGTTAACAGTTACCTCATA CCACTAAATGCAAACAGGCAAAATGAGCAGGTTTTTGGGACAAACCTGTTTATTGGTGAT GGGGTCTTCAAAACTACTCTTCTGGGTGAAATTGTTCAGTACTATACACATTGGTCTGGA TCACTTAGATTCTCTTCGATGTATACTGGTCCTGCCTTGTCCAGTGCTAAACTCACTCTA GCATACACCCCGCCTGGTGCTCGTGGTCCACAGGACAGGAGAGAAGCAATGCTAGGTACT CATGTTGTCTGGGATATTGGTCTGCAATCCACCATAGTAATGACAATACCATGGACATCA GGGGTGCAGTTTAGATATACTGATCCAGATACATACACCAGTGCTGGCTTTCTATCATGT TGGTATCAAACTTCTCTTATACTTCCCCCAGAAACGACCGGCCAGGTCTACTTATTATCA TTCATAAGTGCATGTCCAGATTTTAAGCTTAGGCTGATGAAAGATACTCAAACTATCTCA CAGACTGTTGCACTCACTGAAGGCTTAGGTGATGAATTAGAAGAAGTCATCGTTGAGAAA ACGAAACAGACGGTGGCCTCAATCTCATCTGGTCCAAAACACACACAAAAAGTCCCCATA CTAACTGCAAACGAAACAGGGGCCACAATGCCTGTTCTTCCATCAGACAGCATAGAAACC AGAACTACCTACATGCACTTTAATGGTTCAGAAACTGATGTAGAATGCTTTTTGGGTCGT GCAGCTTGTGTGCATGTAACTGAAATACAAAACAAAGATGCTACTGGAATAGATAATCAC AGAGAAGCAAAATTGTTCAATGATTGGAAAATCAACCTGTCCAGCCTTGTCCAACTTAGA AAGAAACTGGAACTCTTCACTTATGTTAGGTTTGATTCTGAGTATACCATACTGGCCACT GCATCTCAACCTGATTCAGCAAACTATTCAAGCAATTTGGTGGTCCAAGCCATGTATGTT CCACATGGTGCCCCGAAATCCAAAAGAGTGGGCGATTACACATGGCAAAGTGCTTCAAAC CCCAGTGTATTCTTCAAGGTGGGGGATACATCAAGGTTTAGTGTGCCTTATGTAGGATTG GCATCAGCATATAATTGTTTTTATGATGGTTACTCACATGATGATGCAGAAACTCAGTAT GGCATAACTGTTCTAAACCATATGGGTAGTATGGCATTCAGAATAGTAAATGAACATGAT GAACACAAAACTCTTGTCAAGATCAGAGTTTATCACAGGGCAAAGCTCGTTGAAGCATGG ATTCCAAGAGCACCCAGAGCACTACCCTACACATCAATAGGGCGCACAAATTATCCTAAG AATACAGAACCAGTAATTAAGAAGAGGAAAGGTGACATTAAATCCTATGGTTTAGGACCT AGGTACGGTGGGATTTATACATCAAATGTTAAAATAATGAATTACCACTTGATGACACCA GAAGACCACCATAATCTGATAGCACCCTATCCAAATAGAGATTTAGCAATAGTCTCAACA GGAGGACATGGTGCAGAAACAATACCACACTGTAACCGTACATCAGGTGTTTACTATTCC ACATATTACAGAAAGTATTACCCCATAATTTGCGAAAAGCCCACCAACATCTGGATTGAA GGAAGCCCTTATTACCCAAGTAGATTTCAAGCAGGAGTGATGAAAGGGGTTGGGCCGGCA GAGCTAGGAGACTGCGGTGGGATTTTGAGATGCATACATGGTCCCATTGGATTGTTAACA GCTGAAGGTAGTGGATATGTTTGTTTTGCTGACATACGACAGTTGGAGTGTATCGCAGAG GAACAGGGGCTGAGTGATTACATCACAGGTTTGGGTAGAGCTTTTGGTGTCGGGTTCACT GACCAAATCTCAACAAAAGTCACAGAACTACAAGAAGTGGCGAAAGATTTCCTCACCACA AAAGTTTTGTCCAAAGTGGTCAAAATGGTTTCAGCTTTAGTGATCATTTGCAGAAATCAT GATGACTTGGTCACTGTTACGGCCACTCTAGCACTACTTGGATGTGATGGATCTCCTTGG AGATTTCTGAAGATGTACATTTCCAAACACTTTCAGGTGCCTTACATTGAAAGACAAGCA AATGATGGATGGTTCAGAAAGTTTAATGATGCATGTAATGCTGCAAAGGGATTGGAATGG ATTGCTAATAAGATTTCCAAACTGATTGAATGGATAAAAAACAAAGTACTTCCCCAAGCC AAAGAAAAACTAGAATTTTGTAGTAAACTCAAACAACTTGATATACTAGAGAGACAAATA ACCACCATGCATATCTCGAATCCAACACAGGAAAAACGAGAGCAGTTGTTCAATAACGTA TTGTGGTTGGAACAAATGTCGCAAAAGTTTGCCCCATTTTATGCCGTTGAATCAAAAAGA ATCAGGGAACTCAAGAACAAAATGGTAAATTATATGCAATTTAAAAGTAAACAAAGAACT GAACCAGTGTGTGTATTAATCCATGGTACACCCGGTTCTGGTAAATCATTAACAACATCC ATTGTGGGACGTGCAATTGCAGAACACTTCAATTCAGCAGTATATTCACTTCCACCAGAT CCCAAGCACTTTGATGGTTATCAGCAACAGGAAGTTGTGATTATGGATGATCTGAACCAA AATCCAGATGGACAGGATATAAGCATGTTTTGTCAAATGGTTTCTTCAGTGGATTTCTTG CCTCCAATGGCTAGTTTAGATAACAAGGGCATGTTATTCACCAGTAATTTTGTTCTAGCC TCCACAAATTCTAACACACTAAGCCCCCCAACAATCTTGAATCCTGAAGCTTTAGTCAGG AGATTTGGTTTTGACCTAGATATATGTTTGCATACTACCTACACAAAGAATGGAAAACTC AATGCAGGCATGTCAACCAAGACATGCAAAGATTGCCATCAACCATCTAATTTCAAGAAA TGTTGCCCCCTAGTCTGTGGAAAAGCTATTAGCTTGGTAGACAGAACTACCAACGTTAGG TATAGTGTGGATCAACTGGTCACGGCTATTATAAGTGATTTCAAGAGCAAAATGCAAATT ACAGATTCCCTAGAAACACTGTTTCAAGGACCAGTGTATAAAGATTTAGAGATTGATGTT TGCAACACACCACCTTCAGAATGTATCAACGATTTACTGAAATCTGTAGATTCAGAAGAG ATTAGGGAATATTGTAAGAAGAAGAAATGGATTATACCTGAAATTCCTACCAACATAGAA AGGGCTATGAATCAAGCCAGCATGATTATTAATACTATTCTGATGTTTGTCAGTACATTA GGTATTGTTTATGTCATTTATAAATTGTTTGCTCAAACTCAAGGACCATATTCTGGTAAC CCGCCTCACAATAAACTAAAAGCCCCAACTTTACGCCCAGTTGTTGTGCAAGGACCAAAC ACAGAATTTGCACTATCCCTGTTAAGGAAAAACATAATGACTATAACAACCTCAAAGGGA GAGTTCACAGGGTTAGGCATACATGATCGTGTCTGTGTGATACCCACACACGCACAGCCT GGTGATGATGTACTAGTGAATGGTCAGAAAATTAGAGTTAAGGATAAGTACAAATTAGTA GATCCAGAGAACATTAATCTAGAGCTTACAGTGTTGACTTTAGATAGAAATGAAAAATTC AGAGATATCAGGGGATTTATATCAGAAGATCTAGAAGGTGTGGATGCCACTTTGGTAGTA CATTCAAATAACTTTACCAACACTATCTTAGAAGTTGGCCCTGTAACAATGGCAGGACTT ATTAATTTGAGTAGCACCCCCACTAACAGAATGATTCGTTATGATTATGCAACAAAAACT GGGCAGTGTGGAGGTGTGCTGTGTGCTACTGGTAAGATCTTTGGTATTCATGTTGGCGGT AATGGAAGACAAGGATTTTCAGCTCAACTTAAAAAACAATATTTTGTAGAGAAACAAGGC CAAGTAATAGCTAGACATAAGGTTAGGGAGTTTAACATAAATCCAGTCAACACGGCAACT AAGTCAAAATTACATCCCAGTGTATTTTATGATGTTTTTCCAGGTGACAAGGAACCTGCT GTATTGAGTGACAATGATCCCAGACTGGAAGTTAAATTGACTGAATCATTATTCTCTAAG TACAAGGGGAATGTAAATACGGAACCCACTGAAAATATGCTTGTGGCTGTAGACCATTAT GCAGGGCAACTATTATCACTAGATATCCCCACTTCTGAACTTACACTAAAAGAAGCATTA TATGGAGTAGATGGACTAGAACCTATAGATATTACAACCAGTGCAGGATTTCCCTATGTG AGTCTTGGGATCAAAAAGAGAGACATTCTGAATAAAGAGACCCAGGACACAGAAAAGATG AAGTTTTATCTAGACAAGTATGGCATTGACTTGCCTCTAGTTACATATATTAAGGATGAA TTAAGAAGTGTTGACAAAGTCCGATTAGGGAAAAGTAGATTAATTGAAGCCTCCAGTTTG AATGATTCTGTTAACATGAGAATGAAACTAGGCAACCTTTACAAAGCATTCCATCAAAAT CCCGGTGTTCTGACTGGATCAGCAGTGGGTTGTGATCCTGATGTGTTTTGGTCTGTCATC CCTTGCTTAATGGATGGGCACCTGATGGCATTTGATTACTCTAATTTTGATGCCTCTTTG TCACCAGTTTGGTTTGTCTGTCTAGAGAAGGTTTTGACCAAGTTAGGCTTTGCAGGCTCT TCATTAATTCAATCAATTTGTAATACCCATCATATCTTTAGGGATGAAATATATGTGGTT GAAGGTGGCATGCCCTCAGGGTGTTCAGGAACCAGCATATTCAATTCCATGATCAACAAC ATAATCATTAGGACTTTGATATTAGATGCATATAAAGGAATAGATTTAGACAAACTTAAA ATCTTAGCTTACGGTGATGATTTGATTGTTTCTTATCCTTATGAACTGGATCCACAAGTG TTGGCAACTCTTGGTAAAAATTATGGACTAACCATCACACCCCCAGACAAATCTGAAACT TTTACAAAAATGACATGGGAAAACTTGACATTTTTAAAGAGATACTTCAAGCCTGATCAA CAATTTCCCTTTTTGGTTCACCCAGTTATGCCCATGAAAGATATACATGAGTCAATCAGA TGGACAAAGGATCCTAAAAACACACAGGATCACGTCCGATCATTATGCATGTTAGCATGG CACTCAGGAGAAAAAGAGTACAATGAATTCATTCAGAAGATCAGAACTACTGACATTGGA AAATGTCTAATTCTCCCAGAATACAGCGTACTTAGGAGGCGCTGGTTGGACCTCTTTTAG
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P03303 UniProtKB Entry Name POLG_HRV14 GenBank Gene ID K02121 - General References
- Stanway G, Hughes PJ, Mountford RC, Minor PD, Almond JW: The complete nucleotide sequence of a common cold virus: human rhinovirus 14. Nucleic Acids Res. 1984 Oct 25;12(20):7859-75. [Article]
- Lee WM, Monroe SS, Rueckert RR: Role of maturation cleavage in infectivity of picornaviruses: activation of an infectosome. J Virol. 1993 Apr;67(4):2110-22. [Article]
- Callahan PL, Mizutani S, Colonno RJ: Molecular cloning and complete sequence determination of RNA genome of human rhinovirus type 14. Proc Natl Acad Sci U S A. 1985 Feb;82(3):732-6. [Article]
- Gustin KE, Sarnow P: Inhibition of nuclear import and alteration of nuclear pore complex composition by rhinovirus. J Virol. 2002 Sep;76(17):8787-96. [Article]
- Fuchs R, Blaas D: Uncoating of human rhinoviruses. Rev Med Virol. 2010 Sep;20(5):281-97. doi: 10.1002/rmv.654. [Article]
- Fuchs R, Blaas D: Productive entry pathways of human rhinoviruses. Adv Virol. 2012;2012:826301. doi: 10.1155/2012/826301. Epub 2012 Nov 26. [Article]
- Rossmann MG, Arnold E, Erickson JW, Frankenberger EA, Griffith JP, Hecht HJ, Johnson JE, Kamer G, Luo M, Mosser AG, et al.: Structure of a human common cold virus and functional relationship to other picornaviruses. Nature. 1985 Sep 12-18;317(6033):145-53. [Article]
- Arnold E, Rossmann MG: The use of molecular-replacement phases for the refinement of the human rhinovirus 14 structure. Acta Crystallogr A. 1988 May 1;44 ( Pt 3):270-82. [Article]
- Kolatkar PR, Bella J, Olson NH, Bator CM, Baker TS, Rossmann MG: Structural studies of two rhinovirus serotypes complexed with fragments of their cellular receptor. EMBO J. 1999 Nov 15;18(22):6249-59. [Article]
- Arnold E, Rossmann MG: Analysis of the structure of a common cold virus, human rhinovirus 14, refined at a resolution of 3.0 A. J Mol Biol. 1990 Feb 20;211(4):763-801. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB05102 Rupintrivir investigational unknown Details DB08017 3-METHOXY-6-[4-(3-METHYLPHENYL)-1-PIPERAZINYL]PYRIDAZINE experimental unknown Details DB08509 1-[6-(2-CHLORO-4-METHYXYPHENOXY)-HEXYL]-IMIDAZOLE experimental unknown Details DB08540 2-[4-(2H-1,4-BENZOTHIAZINE-3-YL)-PIPERAZINE-1-LY]-1,3-THIAZOLE-4-CARBOXYLIC ACID ETHYLESTER experimental unknown Details DB08543 1-[2-HYDROXY-3-(4-CYCLOHEXYL-PHENOXY)-PROPYL]-4-(2-PYRIDYL)-PIPERAZINE experimental unknown Details DB03203 Sphingosine experimental unknown Details DB08719 5-(5-(6-CHLORO-4-(4,5-DIHYDRO-2-OXAZOLYL)PHENOXY)PENTYL)-3-METHYL ISOXAZOLE experimental unknown Details DB08720 5-(5-(4-(4,5-dihydro-2-oxazoly)phenoxy)pentyl)-3-methyl osoxazole experimental unknown Details DB08721 5-(5-(2,6-dichloro-4-(4,5-dihydro-2-oxazolyl)phenoxy)pentyl)-3-(hydroxyethyl oxymethyleneoxymethyl) isoxazole experimental unknown Details DB08722 5-(7-(6-chloro-4-(5-hydro-4-methyl-2-oxazolyl)phenoxy)heptyl)-3-methyl isoxazole experimental unknown Details DB08723 WIN-54954 experimental unknown Details DB08724 5-(5-(4-(5-hydro-4-methyl-2-oxazolyl)phenoxy)pentyl)-3-methyl isoxazole experimental unknown Details DB08725 (S)-5-(7-(4-(4-Ethyl-4,5-dihydro-2-oxazolyl)phenoxy)heptyl)-3-methylisoxazole experimental unknown Details DB08726 5-(7-(4-(4,5-dihydro-2-oxazolyl)phenoxy)heptyl)-3-methyl isoxazole experimental unknown Details DB08727 3-Methyl-5-(7-{4-[(4R)-4-methyl-4,5-dihydro-1,3-oxazol-2-yl]phenoxy}heptyl)-1,2-oxazole experimental unknown Details DB08728 5-(3-(2,6-dichloro-4-(4,5-dihydro-2-oxazolyl)phenoxy)propyl)-3-methyl isoxazole experimental unknown Details