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Index > Protein center > HERC5(Gene name) > Human
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  • HERC5 (Gene name),
  • E3 ISG15--protein ligase HERC5 (Protein name ),  HERC5_HUMAN from NCBI database.
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  • General Annotation
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  • Gene name:
    HERC5(CEB1;CEBP1);
    Protein name:
    E3 ISG15--protein ligase HERC5;
    Alternative:
    HECT domain and RCC1-like domain-containing protein 5;Cyclin-E-binding protein 1;
    Organism:
    Human (Homo sapiens). 
    General Annotation
    Sub Unit:
    Binds to CCNA1, CCNB1, CCND1 and CCNE1. Interacts with UBE2L6. Interacts with IRF3, this interaction is marginal in resting cells but enhanced upon viral infection.
    Function:
    Major E3 ligase for ISG15 conjugation. Acts as a positive regulator of innate antiviral response in cells induced by interferon. Makes part of the ISGylation machinery that recognizes target proteins in a broad and relatively non-specific manner. Catalyzes ISGylation of IRF3 which results in sustained activation, it attenuates IRF3-PIN1 interaction, which antagonizes IRF3 ubiquitination and degradation, and boosts the antiviral response. Catalyzes ISGylation of influenza A viral NS1 which attenuates virulence; ISGylated NS1 fails to form homodimers and thus to interact with its RNA targets. Catalyzes ISGylation of papillomavirus type 16 L1 protein which results in dominant-negative effect on virus infectivity. Physically associated with polyribosomes, broadly modifies newly synthesized proteins in a cotranslational manner. In an interferon-stimulated cell, newly translated viral proteins are primary targets of ISG15.
    Subcellular Location:
    Cytoplasm perinuclear region Associated with the polyribosomes, probably via the 60S subunit.
    Protein Attributes:
    Sequence length:
    1024
    Sequence:
    50:
    MERRSRRKSR | RNGRSTAGKA | AATQPAKSPG | AQLWLFPSAA | GLHRALLRRV | 
    100:
    EVTRQLCCSP | GRLAVLERGG | AGVQVHQLLA | GSGGARTPKC | IKLGKNMKIH | 
    150:
    SVDQGAEHML | ILSSDGKPFE | YDNYSMKHLR | FESILQEKKI | IQITCGDYHS | 
    200:
    LALSKGGELF | AWGQNLHGQL | GVGRKFPSTT | TPQIVEHLAG | VPLAQISAGE | 
    250:
    AHSMALSMSG | NIYSWGKNEC | GQLGLGHTES | KDDPSLIEGL | DNQKVEFVAC | 
    300:
    GGSHSALLTQ | DGLLFTFGAG | KHGQLGHNST | QNELRPCLVA | ELVGYRVTQI | 
    350:
    ACGRWHTLAY | VSDLGKVFSF | GSGKDGQLGN | GGTRDQLMPL | PVKVSSSEEL | 
    400:
    KLESHTSEKE | LIMIAGGNQS | ILLWIKKENS | YVNLKRTIPT | LNEGTVKRWI | 
    450:
    ADVETKRWQS | TKREIQEIFS | SPACLTGSFL | RKRRTTEMMP | VYLDLNKARN | 
    500:
    IFKELTQKDW | ITNMITTCLK | DNLLKRLPFH | SPPQEALEIF | FLLPECPMMH | 
    550:
    ISNNWESLVV | PFAKVVCKMS | DQSSLVLEEY | WATLQESTFS | KLVQMFKTAV | 
    600:
    ICQLDYWDES | AEENGNVQAL | LEMLKKLHRV | NQVKCQLPES | IFQVDELLHR | 
    650:
    LNFFVEVCRR | YLWKMTVDAS | ENVQCCVIFS | HFPFIFNNLS | KIKLLHTDTL | 
    700:
    LKIESKKHKA | YLRSAAIEEE | RESEFALRPT | FDLTVRRNHL | IEDVLNQLSQ | 
    750:
    FENEDLRKEL | WVSFSGEIGY | DLGGVKKEFF | YCLFAEMIQP | EYGMFMYPEG | 
    800:
    ASCMWFPVKP | KFEKKRYFFF | GVLCGLSLFN | CNVANLPFPL | ALFKKLLDQM | 
    850:
    PSLEDLKELS | PDLGKNLQTL | LDDEGDNFEE | VFYIHFNVHW | DRNDTNLIPN | 
    900:
    GSSITVNQTN | KRDYVSKYIN | YIFNDSVKAV | YEEFRRGFYK | MCDEDIIKLF | 
    950:
    HPEELKDVIV | GNTDYDWKTF | EKNARYEPGY | NSSHPTIVMF | WKAFHKLTLE | 
    1000:
    EKKKFLVFLT | GTDRLQMKDL | NNMKITFCCP | ESWNERDPIR | ALTCFSVLFL | 
    1024:
    PKYSTMETVE | EALQEAINNN | RGFG
    3D Structure:
    N/A
    Predicted Eptitope:
    Please Sign in.
    EIAab Sequence  Vaild Sequence:
    Please Sign in.
    Related Databases
    String:
    KEGG:
    Pfam:
    UniGene:
    SMR:
    MIM:
    Uniprot:
     
    FOR
    ELISA Kit for Human E3 ISG15--protein ligase HERC5
    CLIA Kit for Human E3 ISG15--protein ligase HERC5
    Polyclonal Antibody for Human E3 ISG15--protein ligase HERC5
    Monoclonal Antibody for Human E3 ISG15--protein ligase HERC5
    Protein for Human E3 ISG15--protein ligase HERC5

    R&D Technical Data
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    Precision
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    Recovery
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    Linearity
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    For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.
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    References
    1. 1.
      "A novel human gene encoding HECT domain and RCC1-like repeats interacts with cyclins and is potentially regulated by the tumor suppressor proteins."
      Mitsui K. , Nakanishi M. , Ohtsuka S. , Norwood T.H. , Okabayashi K. , Miyamoto C. , Tanaka K. , Yoshimura A. , Ohtsubo M.
      Biochem. Biophys. Res. Commun.266:115-122(1999) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA];TISSUE SPECIFICITY;INTERACTION WITH CCNA1; CCNB1; CCND1 AND CCNE1
      tissue: Embryonic kidney.
    2. 2.
      "HERC5, a HECT E3 ubiquitin ligase tightly regulated in LPS activated endothelial cells."
      Kroismayr R. , Baranyi U. , Stehlik C. , Dorfleutner A. , Binder B.R. , Lipp J.
      J. Cell Sci.117:4749-4756(2004) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA];MUTAGENESIS OF CYS-994;TISSUE SPECIFICITY;INDUCTION
    3. 3.
      "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W. , Graves T.A. , Fulton R.S. , Fulton L.A. , Pepin K.H. , Minx P. , Wagner-McPherson C. , Layman D. , Wylie K. , Sekhon M. , Becker M.C. , Fewell G.A. , Delehaunty K.D. , Miner T.L. , Nash W.E. , Kremitzki C. , Oddy L. , Du H. , more...
      Nature434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]
    4. 4.
      "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res.14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]
      tissue: Brain.
    5. 5.
      "Identification and Herc5-mediated ISGylation of novel target proteins."
      Takeuchi T. , Inoue S. , Yokosawa H.
      Biochem. Biophys. Res. Commun.348:473-477(2006) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION
    6. 6.
      "Herc5, an interferon-induced HECT E3 enzyme, is required for conjugation of ISG15 in human cells."
      Dastur A. , Beaudenon S. , Kelley M. , Krug R.M. , Huibregtse J.M.
      J. Biol. Chem.281:4334-4338(2006) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION;MUTAGENESIS OF CYS-994
    7. 7.
      "HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates type I IFN-induced ISGylation of protein targets."
      Wong J.J. , Pung Y.F. , Sze N.S. , Chin K.C.
      Proc. Natl. Acad. Sci. U.S.A.103:10735-10740(2006) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION;MUTAGENESIS OF CYS-994;ISGYLATION;INDUCTION BY IFNB1;INTERACTION WITH ISGYLATED HSPA8 AND TXNRD1
    8. 8.
      "Herc5 attenuates influenza A virus by catalyzing ISGylation of viral NS1 protein."
      Tang Y. , Zhong G. , Zhu L. , Liu X. , Shan Y. , Feng H. , Bu Z. , Chen H. , Wang C.
      J. Immunol.184:5777-5790(2010) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION;MUTAGENESIS OF CYS-994
    9. 9.
      "Positive regulation of interferon regulatory factor 3 activation by Herc5 via ISG15 modification."
      Shi H.X. , Yang K. , Liu X. , Liu X.Y. , Wei B. , Shan Y.F. , Zhu L.H. , Wang C.
      Mol. Cell. Biol.30:2424-2436(2010) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION;MUTAGENESIS OF CYS-994;INTERACTION WITH IRF3
    10. 10.
      "The ISG15 conjugation system broadly targets newly synthesized proteins: implications for the antiviral function of ISG15."
      Durfee L.A. , Lyon N. , Seo K. , Huibregtsesend J.M.
      Mol. Cell38:722-732(2010) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION;SUBCELLULAR LOCATION;INTERACTION WITH 60S SUBUNIT;MUTAGENESIS OF CYS-994
    11. 11.
      "ISG15 conjugation system targets the viral NS1 protein in influenza A virus-infected cells."
      Zhao C. , Hsiang T.Y. , Kuo R.L. , Krug R.M.
      Proc. Natl. Acad. Sci. U.S.A.107:2253-2258(2010) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION;INTERACTION WITH INFLUENZA A VIRUS NS1
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